Cloning and molecular analysis of the human citrate synthase gene
A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP kinase-3 and their activation by cytokines and cellular stress
A tandemly repeated sequence at the termini of the extrachromosomal ribosomal RNA genes in Tetrahymena
Casein kinase I phosphorylates and destabilizes the beta-catenin degradation complex
Constitutive activation of fibroblast growth factor receptor 3 by mutations responsible for the lethal skeletal dysplasia thanatophoric dysplasia type I
Enzyme-substrate intermediate formation at lysine 329 of human deoxyhypusine synthase
Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2
Cloning and expression of a human ATP-citrate lyase cDNA
Cyclic nucleotide phosphodiesterase PDE1C1 in human cardiac myocytes
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Rho-kinase/ROCK: A key regulator of the cytoskeleton and cell polarity
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This event has been computationally inferred from an event that has been demonstrated in another species. The inference is based on the homology mapping in Ensembl Compara. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation. More details and caveats of the event inference in Reactome. For details on the Ensembl Compara system see also: Gene orthology/paralogy prediction method.
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GABA(A) receptor trafficking and its role in the dynamic modulation of neuronal inhibition
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Comparison of messenger RNA distribution for 60 proteins in fat cells vs the nonfat cells of human omental adipose tissue
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Procollagen peptidase: an enzyme excising the coordination peptides of procollagen
Cyclin A- and cyclin E-Cdk complexes shuttle between the nucleus and the cytoplasm
Receptor-mediated endocytosis of cobalamin (vitamin B12)
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The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone
Human Na+ -coupled citrate transporter: primary structure, genomic organization, and transport function
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The first CH domain of affixin activates Cdc42 and Rac1 through alphaPIX, a Cdc42/Rac1-specific guanine nucleotide exchanging factor
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A novel secretory pathway for interleukin-1 beta, a protein lacking a signal sequence
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Protein interactions in the human methionine synthase-methionine synthase reductase complex and implications for the mechanism of enzyme reactivation
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Mutations in COX15 produce a defect in the mitochondrial heme biosynthetic pathway, causing early-onset fatal hypertrophic cardiomyopathy
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Isolation and characterization of the gene and cDNA encoding human mitochondrial creatine kinase
Oncogene-induced senescence relayed by an interleukin-dependent inflammatory network
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Chemokine signaling via the CXCR2 receptor reinforces senescence
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TRESK background K(+) channel is inhibited by phosphorylation via two distinct pathways
Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes
Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2
Redox-dependent regulation of the conformation and function of human heat shock factor 1
Wnt family proteins are secreted and associated with the cell surface
PMP70, the 70-kDa peroxisomal membrane protein: a member of the ATP-binding cassette transporters
Aflatoxin metabolism in humans: detection of metabolites and nucleic acid adducts in urine by affinity chromatography
Aggregation states of mitochondrial malate dehydrogenase
p21ras activation via hemopoietin receptors and c-kit requires tyrosine kinase activity but not tyrosine phosphorylation of p21ras GTPase-activating protein
The functional human dihydrofolate reductase gene
TGF-beta induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradation
Adherens and tight junctions: structure, function and connections to the actin cytoskeleton
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HDAC6 controls major cell response pathways to cytotoxic accumulation of protein aggregates
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Transient receptor potential channelopathies
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Saccharomyces cerevisiae Ybr004c and its human homologue are required for addition of the second mannose during glycosylphosphatidylinositol precursor assembly
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p130 and p107 use a conserved domain to inhibit cellular cyclin-dependent kinase activity
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Crystal structures of human glutaryl-CoA dehydrogenase with and without an alternate substrate: structural bases of dehydrogenation and decarboxylation reactions
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Nuclear accumulation of beta-catenin protein in Wilms' tumours
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Characterization of the human mitochondrial methionyl-tRNA synthetase
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Distribution of osteonectin mRNA and protein during human embryonic and fetal development
Defect in synaptic vesicle precursor transport and neuronal cell death in KIF1A motor protein-deficient mice
Crystal structure of human protein tyrosine phosphatase 1B
Cytochrome P450 and arachidonic acid bioactivation. Molecular and functional properties of the arachidonate monooxygenase
Bioinformatics and type II G-protein-coupled receptors
The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci
Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region
Extracellular matrix and cell signalling: the dynamic cooperation of integrin, proteoglycan and growth factor receptor
Structural requirements of SLP-76 in signaling via the high-affinity immunoglobulin E receptor (Fc epsilon RI) in mast cells
Isolation and characterization of the human pyruvate kinase M gene
MST, a physiological caspase substrate, highly sensitizes apoptosis both upstream and downstream of caspase activation
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Regulation of PKC-? function by phosphorylation in T cell receptor signaling
Formation of molecular species of mitochondrial cardiolipin. 1. A novel transacylation mechanism to shuttle fatty acids between sn-1 and sn-2 positions of multiple phospholipid species
NGF signalling via TRKA from the plasma membrane
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Von Willebrand factor: looking back and looking forward
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Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation
Repulsive axon guidance: Abelson and Enabled play opposing roles downstream of the roundabout receptor
The PTEN-regulating microRNA miR-26a is amplified in high-grade glioma and facilitates gliomagenesis in vivo
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The product of the MLD gene is a member of the membrane fatty acid desaturase family: overexpression of MLD inhibits EGF receptor biosynthesis
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Beta-cell CaV channel regulation in physiology and pathophysiology
Am J Physiol Endocrinol Metab 288:E16-28
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International Union of Pharmacology classification of receptors for 5-hydroxytryptamine (Serotonin)
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International Union of Pharmacology nomenclature of adrenoceptors
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Purification and characterization of human Syk produced using a baculovirus expression system
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Antigen processing and presentation: TAPping into ABC transporters
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Tendon hypertrophy is associated with increased hydroxylation of nonhelical lysine residues at two specific cross-linking sites in type I collagen
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Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design
Characterization of the human gene (TBXAS1) encoding thromboxane synthase
Beta-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors
Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p
Gene amplification profiling of esophageal squamous cell carcinomas by DNA array CGH
EVH1/WH1 domains of VASP and WASP proteins belong to a large family including Ran-binding domains of the RanBP1 family
SLC11 family of H+-coupled metal-ion transporters NRAMP1 and DMT1
Vertebrates have conserved capping protein alpha isoforms with specific expression patterns
Protein kinase C phosphorylates G12 alpha and inhibits its interaction with G beta gamma
Gene amplifications associated with the development of hormone-resistant prostate cancer
Purification and partial characterization of aldehyde dehydrogenase from human erythrocytes.
The unfolded protein response: a pathway that links insulin demand with beta-cell failure and diabetes
A direct role for sterol regulatory element binding protein in activation of 3-hydroxy-3-methylglutaryl coenzyme A reductase gene
Structure and formation of a stable histidine-based trifunctional cross-link in skin collagen
Crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site
Accurate cleavage and polyadenylation of exogenous RNA substrate.
Specific armadillo repeat sequences facilitate ?-catenin nuclear transport in live cells via direct binding to nucleoporins Nup62, Nup153, and RanBP2/Nup358
Alcohol dehydrogenases, aldehyde dehydrogenases, and related enzymes
ISG15 Arg151 and the ISG15-conjugating enzyme UbE1L are important for innate immune control of Sindbis virus
Purification and properties of human cytosolic folylpoly-gamma-glutamate synthetase and organization, localization, and differential splicing of its gene
SUMO is transferred from E1 to E2 (UBE2I, UBC9)
TIRAP/Mal, TRIF and TRAM. Differential utilization of these TIR
Toll-like receptor 3: a link between toll-like receptor, interferon and viruses
Regulation of the cyclin E gene by transcription factor E2F1
Smurf1 regulates the inhibitory activity of Smad7 by targeting Smad7 to the plasma membrane
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Netrin stimulates tyrosine phosphorylation of the UNC-5 family of netrin receptors and induces Shp2 binding to the RCM cytodomain
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Passenger-strand cleavage facilitates assembly of siRNA into Ago2-containing RNAi enzyme complexes
The shed ectodomain of type XIII collagen affects cell behaviour in a matrix-dependent manner
Coenzyme Q biosynthesis: Coq6 is required for the C5-hydroxylation reaction and substrate analogs rescue Coq6 deficiency
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Identification and expression of a cDNA for human hydroxypyruvate/glyoxylate reductase
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Homo sapiens dullard protein phosphatase shows a preference for the insulin-dependent phosphorylation site of lipin1
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The discoidin domain receptor tyrosine kinases are activated by collagen
Execution of nonsense-mediated mRNA decay: what defines a substrate?
Contributions of proteomics to understanding phagosome maturation
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Purification of deoxyribonucleic acid polymerase delta from calf thymus: partial characterization of physical properties.
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Functional expression of the human hZIP2 zinc transporter
Identification of TTP mRNA targets in human dendritic cells reveals TTP as a critical regulator of dendritic cell maturation
Evolution, structure, and activation mechanism of family 3/C G-protein-coupled receptors
Structures, enzymatic properties, and expression of novel human and mouse secretory phospholipase A(2)s
Structural analysis of the interaction between Dishevelled2 and clathrin AP-2 adaptor, a critical step in noncanonical Wnt signaling
H2S biogenesis by human cystathionine gamma-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia
Interchain disulfide bonds in procollagen are located in a large nontriple-helical COOH-terminal domain
Human Myt1 is a cell cycle-regulated kinase that inhibits Cdc2 but not Cdk2 activity
Lipid digestion, mobilization, and transport
PPIB mutations cause severe osteogenesis imperfecta
Molecular cloning and functional characterization of human vesicular glutamate transporter 3
The role of aminoacyl-tRNA synthetases in genetic diseases
Binding of DCC by netrin-1 to mediate axon guidance independent of adenosine A2B receptor activation
Dock180 and ELMO1 proteins cooperate to promote evolutionarily conserved Rac-dependent cell migration
Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
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Mapping of the properdin-binding site in the third component of complement
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Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop
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The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity
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Role of the vascular endothelial growth factor pathway in tumor growth and angiogenesis
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Cellular regulation of endothelial nitric oxide synthase
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Plexin-B1 directly interacts with PDZ-RhoGEF/LARG to regulate RhoA and growth cone morphology
Raf and akt mediate distinct aspects of sensory axon growth
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Molecular mechanisms and regulation of insulin exocytosis as a paradigm of endocrine secretion
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Abnormal spine morphology and enhanced LTP in LIMK-1 knockout mice
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The gap junction cellular internet: connexin hemichannels enter the signalling limelight
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Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits
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The role of voltage-gated calcium channels in pancreatic beta-cell physiology and pathophysiology
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Homologous DNA pairing by human recombination factors Rad51 and Rad54
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Morquio's syndrome: deficiency of a chondroitin sulfate N-acetylhexosamine sulfate sulfatase
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Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica
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Tandem of pore domain in a weak inwardly rectifying K+ channels (TWIK)
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GEF what? Dock180 and related proteins help Rac to polarize cells in new ways
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Phosphorylase kinase: the complexity of its regulation is reflected in the complexity of its structure
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Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages
The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
Galpha 12 activates Rho GTPase through tyrosine-phosphorylated leukemia-associated RhoGEF
A partial deficiency of interleukin-7R alpha is sufficient to abrogate T-cell development and cause severe combined immunodeficiency
Coordinating TLR-activated signaling pathways in cells of the immune system
Upf1 senses 3'UTR length to potentiate mRNA decay
Structure of human thymidylate synthase suggests advantages of chemotherapy with noncompetitive inhibitors
Expression cloning of a Na+-independent aromatic amino acid transporter with structural similarity to H+/monocarboxylate transporters
The human REV1 gene codes for a DNA template-dependent dCMP transferase.
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Enzymic synthesis and breakdown of a pyrimidine, orotic acid. I. Dihydro-orotic dehydrogenase
Enzymic conversion of phosphorylase a to phosphorylase b
Transforming growth factor beta type I receptor kinase mutant associated with metastatic breast cancer
Enzymes of fatty acid metabolism. II. Properties of crystalline crotonase.
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Glycogenin-1 deficiency and inactivated priming of glycogen synthesis
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Cold Spring Harb Perspect Biol 4:a007864
Co-crystal structure of sterol regulatory element binding protein 1a at 2.3 A resolution
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Tyrosine 766 in the fibroblast growth factor receptor-1 is required for FGF-stimulation of phospholipase C, phospholipase D, phospholipase A(2), phosphoinositide 3-kinase and cytoskeletal reorganisation in porcine aortic endothelial cells
Localization of p21-activated kinase 1 (PAK1) to pseudopodia, membrane ruffles, and phagocytic cups in activated human neutrophils
The roles of anabolic and catabolic reactions in the synthesis and recycling of polyunsaturated fatty acids
Prostaglandins Leukot Essent Fatty Acids 67:79-83
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Translational silencing of ceruloplasmin requires the essential elements of mRNA circularization: poly(A) tail, poly(A)-binding protein, and eukaryotic translation initiation factor 4G
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Covalent cross-linking of the NC1 domain of collagen type IX to collagen type II in cartilage
Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate
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Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey disease
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On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. II. The electron-transferring flavoprotein.
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_218145.2
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Human gamma-aminobutyric acid type B receptors are differentially expressed and regulate inwardly rectifying K+ channels
Nuclear import of sterol regulatory element-binding protein-2, a basic helix-loop-helix-leucine zipper (bHLH-Zip)-containing transcription factor, occurs through the direct interaction of importin beta with HLH-Zip
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Interaction between citrate synthase and malate dehydrogenase. Substrate channeling of oxaloacetate
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Chromosomal localization and genomic organization of the human retinal rod Na-Ca+K exchanger
Anion exchanger 1 in human kidney and oncocytoma differs from erythroid AE1 in its NH2 terminus
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_259937.1
TC II deficiency: avoidance of false-negative molecular genetics by RNA-based investigations
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_229457.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_242654.1
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632005
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_259429.1
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632002
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653190
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Activation of the small GTPases, rac and cdc42, after ligation of the platelet PAR-1 receptor
The role of transient receptor potential cation channels in Ca2+ signaling
Cold Spring Harb Perspect Biol 2:a003962
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A novel fluor in insoluble collagen: a crosslinking moiety in collagen molecule
Affinity column purification of protocollagen proline hydroxylase from chick embryos and further characterization of the enzyme
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JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
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High-throughput tissue microarray analysis of 3p25 (RAF1) and 8p12 (FGFR1) copy number alterations in urinary bladder cancer
Biotin-responsive basal ganglia disease-linked mutations inhibit thiamine transport via hTHTR2: biotin is not a substrate for hTHTR2
The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes.
Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase
Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats
Molecular cloning and functional expression of cDNAs encoding a human Na+-nucleoside cotransporter (hCNT1)
Control of mRNA decay by phosphorylation of tristetraprolin
Megakaryocyte development and platelet production
NMD: multitasking between mRNA surveillance and modulation of gene expression
Isolation and characterization of a digoxin transporter and its rat homologue expressed in the kidney
Evaluation of the "scanning model" for initiation of protein synthesis in eucaryotes.
Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue monophosphates.
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Plasminogen-activator inhibitor type 1 and coronary artery disease
Chaperonins: The hunt for the Group II mechanism
Processing of Capped Intron-Containing Pre-mRNA
Calcium/calmodulin kinase IV pathway is involved in the transcriptional regulation of the corticotropin-releasing hormone gene promoter in neuronal cells
BMP-1/Tolloid-like metalloproteases process endorepellin, the angiostatic C-terminal fragment of perlecan
SLC26A7 is a Cl- channel regulated by intracellular pH
Cbl-mediated ubiquitinylation and negative regulation of Vav
Leading-edge research: PtdIns(3,4,5)P3 and directed migration
Regulation of nitric oxide-sensitive guanylyl cyclase
Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol
Genetic analysis of chromosome pairing, recombination, and cell cycle control during first meiotic prophase in mammals
The yeast ALG11 gene specifies addition of the terminal alpha 1,2-Man to the Man5GlcNAc2-PP-dolichol N-glycosylation intermediate formed on the cytosolic side of the endoplasmic reticulum
Metabolism of highly unsaturated n-3 and n-6 fatty acids
3'-End processing of pre-mRNA in eukaryotes.
Glutamate Neurotransmitter Release Cycle
Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains
Gap-filling DNA repair synthesis and ligation in GG-NER
COQ6 mutations in human patients produce nephrotic syndrome with sensorineural deafness
Role of adaptor TRIF in the MyD88-independent toll-like receptor signaling pathway
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Acyl-CoA:dihydroxyacetonephosphate acyltransferase: cloning of the human cDNA and resolution of the molecular basis in rhizomelic chondrodysplasia punctata type 2
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Molecular basis for genistein-induced inhibition of Kir2.3 currents
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The SIRT1 modulators AROS and DBC1 regulate HSF1 activity and the heat shock response
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FGFR4 Gly388Arg polymorphism and prognosis of breast and colorectal cancer
Atg9a controls dsDNA-driven dynamic translocation of STING and the innate immune response
Proc. Natl. Acad. Sci. U.S.A. 106:20842-6
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Quantitating protein synthesis, degradation, and endogenous antigen processing
Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase: the importance of potassium and chloride ions for its structure and function
Osteogenesis imperfecta, normal collagen folding, and lack of cyclophilin B
N Engl J Med 362:1940-1; author reply 1941-2
Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA
Purification and properties of beta-hydroxyisobutyric dehydrogenase
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Site-specific casein kinase 1epsilon-dependent phosphorylation of Dishevelled modulates beta-catenin signaling
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The discoidin domain receptor DDR2 is a receptor for type X collagen
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Synaptotagmin activates membrane fusion through a Ca2+-dependent trans interaction with phospholipids
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TWIK-releated acid-sensitive K+ channel (TASK)
The NLRP3 inflammasome: a sensor of immune danger signals
Molecular basis of hereditary fructose intolerance: mutations and polymorphisms in the human aldolase B gene
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Platelet activation, signaling and aggregation
Association of Dishevelled with the clathrin AP-2 adaptor is required for Frizzled endocytosis and planar cell polarity signaling
All three IkappaB isoforms and most Rel family members are stably associated with the IkappaB kinase 1/2 complex
A novel positive feedback loop mediated by the docking protein Gab1 and phosphatidylinositol 3-kinase in epidermal growth factor receptor signaling
Identification of the gene responsible for the cblA complementation group of vitamin B12-responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements
Proc. Natl. Acad. Sci. U.S.A. 99:15554-9
Hydroxylation of (X-Pro-Gly)n by protocollagen proline hydroxylase. Effect of chain length, helical conformation and amino acid sequence in the substrate
Neurotrophins and their receptors: a convergence point for many signalling pathways
L1 and NCAM adhesion molecules as signaling coreceptors in neuronal migration and process outgrowth
Acetylated spermidine is oxidized by the flavoenzyme polyamine oxidase (PAO) to produce putrescine. PAO is involved in the back-conversion of polyamines and thus the regulation of their intracellular concentrations.
Spermidine/spermine N1-acetyltransferase (Spd/Spm acetyltransferase) is the rate-limiting enzyme in the catabolism of polyamines. Defects in SAT1 may be the cause of keratosis follicularis spinulosa decalvans (KFSD).
Acetylated spermine is oxidized by the flavoenzyme polyamine oxidase (PAO) to produce spermidine. PAO is involved in the back-conversion of polyamines and thus the regulation of their intracellular concentrations.
Spermine oxidase (SMOX/PAOh1/SMO) is a polyamine oxidase flavoenzyme which catalyzes the oxidation of spermine to spermidine. It plays an important role in the regulation of endogenous polyamine intracellular concentration. Five different isozymes are produced by alternative splicing with isozyme 3 being the major isoform and possessing the highest affinity for spermine. It is highly inducible by specific antitumor polyamine analogues (Wang et al., 2001).
The reactions catalyzed by aminopropyl-transferases annotated above are generally irreversible. But spermine and spermidine can be recycled respectively into spermidine and putrescine. These events require the formation of N-acetylated intermediates, N1-acetylspermine and N1-acetylspermidine catalyzed by a cytosolic acetyl-CoA:spermidine/spermine N1-acetyl-tranferase (SSAT) enzyme. Subsequently, polyamine-oxidase (PAO), a FAD enzyme present in the peroxysomes, yields a polyamine with release of an aldehyde (3-acetamindopropanal) and H2O2. In addition, SMOX, a FAD-dependent, polyamine oxidase (PAOh1/SMO) that can efficiently use spermine as a substrate and is involved in interconversion reactions.
MTA phosphorylase catalyzes the cleavage of adenine from S-methylthioadenosine (MTA) and subsequent phosphorylation of the product, yielding 5'-methylthio ribose-1-phosphate (Kamatani et al. 1981). The active form of the enzyme is a homotrimer (Della Ragione et al. 1985). Mutations in the gene are associated with a rare bone dysplasia and cancer syndrome, DMS-MFH (Camacho-Vanegas et al. 2012).
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S-Adenosylmethionine decarboxylase belongs to a small class of amino acid decarboxylases that use a covalently bound pyruvate as a prosthetic group. It is an essential enzyme for polyamine biosynthesis and provides an important target for the design of anti-parasitic and cancer chemotherapeutic agents. It catalyzes the formation of the aminopropyl group donor in the biosynthesis of the polyamines spermidine and spermine. These pyruvoyl-dependent decarboxylases also form amines such as histamine, decarboxylated S-adenosylmethionine, phosphatidylethanolamine (a component of membrane phospholipids), and -alanine (a precursor of coenzyme A), which are all of critical importance in cellular physiology and provide important targets for drug design.
L-ornithine is converted into putrescine by ODC holoenzyme complex.Putrescine is subsequent used for polyamine synthesis.
Spermidine synthase is one of four enzymes in the polyamine-biosynthetic pathway and carries out the final step of spermidine biosynthesis. This enzyme catalyzes the conversion of putrescine to spermidine using decarboxylated S-adenosylmethionine as the cofactor.
Polyamines is a family of molecules (i.e. putrescine, spermine, spermidine) derived from ornithine according to a decarboxylation/condensative process. More recently, it has been demonstrated that arginine can be metabolised according to the same pathway leading to agmatine formation. Polyamines are essential for the growth, the maintenance and the function of normal cells. The complexity of their metabolism and the fact that polyamines homeostasis is tightly regulated support the idea that polyamines are essential to cell survival. Multiple abnormalities in the control of polyamines metabolism might be implicated in several pathological processes (Moinard et al., 2005). Legend for the following figure:
Tyrosine hydroxylase (TH) is the first enzyme in catecholamine biosynthesis, as well as being the rate-limiting enzyme in that process. TH requires tetrahydrobiopterin and uses iron as a cofactor in the 3,4-hydroxylation of tyrosine to produce dopa. Four isoforms of TH are expressed in the human brain and all have enzymatic activity (Nagatsu, T, 1989; Lewis, DA et al, 1993).
In the last step MOB gets transaminated to methionine. The reaction was confirmed in yeast, where several transaminases catalyze it, which appears to be also the case in rat. At the moment, the human enzymes involved are unknown but due to homology to the respective enzyme in the parasite Crithidia fasciculata we feel supported to state that human GOT is probably one of the involved transaminases. (Berger et al, 2001)
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Methionine salvage is a sequential pathway of six reactions that create methionine from 5'-methylthioadenosine (MTA) which is a byproduct of polyamine biosynthesis in nearly all organisms. The process happens completely in the cytosol. It is important in humans for recycling of sulphur that has to be assimilated using energy. (Pirkov et al, 2008; Albers, 2009)
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Aromatic L-amino acid decarboxylase (AADC, dopa decarboxylase) decarboxylates dopa to form dopamine.
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A critical review of the origin and control of adrenal androgens
Baillieres Clin Obstet Gynaecol 11:229-48
Equilibrium between 5'-methylthio ribose-1-phosphate and 5'-methylthio ribulose-1-phosphate is catalyzed by 5'-methylthio ribose-1-phosphate isomerase. (Kabuyama et al, 2009)
Acireducone (1,2-Dihydroxy-3-oxo-5'-methylthiopentene) is oxidized using acireductone dioxygenase and dioxygen. There are two reactions possible, dependent on the metal cofactor: the alternative product 3-methylthiopropionate using nickel was confirmed in Klebsiella. In eukaryotes using iron(II) the result is 4-methylthio-2-oxobutanoate (MOB). (Ju et al, 2006)
Acireductone synthase (also: enolase-phosphatase E1) catalyzes the dephosphorylation and conversion to enolate of 2,3-dioxo-5'-methylthiopentane-1-phosphate, yielding acireductone. (Wang et al, 2005)
The human enzyme with 5'-methylthio ribulose-1-phosphate isomerase activity is probably produced from the APIP gene, according to its orthology with the yeast Mde1p enzyme.
Tryptophan is catabolized in seven steps to yield aminomuconate. Intermedistes in this process are used as well for the synthesis of serotonin and kynurenine (Peters 1991).
Note: the coordinates are copied over from Homo sapiens.
DNA repair protein RAD51 homolog 1 (hRAD51) (HsRAD51)
The mitochondrial ornithine transporters SLC25A15 and SLC25A2 mediate the exchange of cytosolic ornithine for citrulline from the mitochondrial matrix. SLC25A15 was the first protein shown to have this function, identified because mutations in the protein are associated with elevated levels of ammonia, ornithine, and citrulline in affected individuals (Camacho et al. 1999). The second transporter, SLC25A2, identified later, is also expressed in normal cells and their apparently partly redundant function may explain the relatively mild symptoms associated with SLC25A15 deficiency compared to other defects of the urea cycle (Fiermonte et al. 2003).
The urea cycle yields urea, the major form in which excess nitrogen is excreted from the human body, and the amino acid arginine (Brusilow and Horwich 2001). It consists of four reactions: that of ornithine and carbamoyl phosphate to form citrulline, of citrulline and aspartate to form argininosuccinate, the cleavage of argininosuccinate to yield fumarate and arginine, and the cleavage of arginine to yield urea and re-form ornithine. The carbamoyl phosphate consumed in this cycle is synthesized in the mitochondria from bicarbonate and ammonia, and this synthesis in turn is dependent on the presence of N-acetylglutamate, which allosterically activates carbamoyl synthetase I enzyme. The synthesis of N-acetylglutamate is stimulated by high levels of arginine. Increased levels of free amino acids, indicated by elevated arginine levels, thus stimulate urea synthesis. Two enzymes catalyze the hydrolysis of arginine to yield ornithine and urea. Cytosolic ARG1 is the canonical urea cycle enzyme. Mitochondrial ARG2 likewise catalyzes urea production from arginine and may have a substantial sparing effect in patients lacking ARG1 enzyme, so its reaction is annotated here although the role of ARG2 under normal physiological conditions remains unclear.
Trimethyllysine dioxygenase dimer (TMLHE) in the mitochondrial matrix catalyzes the reaction of oxygen, 2-oxoglutarate, and 'N6,N6,N6-Trimethyl-L-lysine to form CO2, 3-Hydroxy-N6,N6,N6-trimethyl-L-lysine, and succinate (Vaz et al. 2001).
Cytosolic kynurenine 3-monooxygenase catalyzes the reaction of L-kynurenine, NADPH + H+, and O2 to form 3-hydroxy-L-kynurenine, NADP+, and H2O.
Cytosolic kynureninase catalyzes the hydrolysis of 3-hydroxy-L-kynurenine to form L-alanine and 3-hydroxyanthranilate.
Cytosolic 3-hydroxyanthranilate oxygenase catalyzes the reaction of 3-hydroxyanthranilate and O2 to form 2-amino-3-carboxymuconate semialdehyde.
At the beginning of this reaction, 1 molecule of '2-Amino-3-carboxymuconate semialdehyde' is present. At the end of this reaction, 1 molecule of 'CO2', and 1 molecule of '2-Aminomuconate semialdehyde' are present. This reaction takes place in the 'cytoplasm' and is mediated by the 'carboxy-lyase activity' of '2-amino-3-carboxymuconate-6-semialdehyde decarboxylase homodimer'.
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6-O- methylguanine-DNA methyltransferase
Methylated-DNA--protein-cysteine methyltransferase
Type III cGMP-inhibited cyclic nucleotide phosphodiesterases (PDE3 gene family)
Serine-protein kinase ATM (EC 2.7.1.37) (Ataxia telangiectasia mutated) (A-T, mutated)
Double-strand break repair protein MRE11A
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CCBL2 (KAT 3) catalyzes the reaction of kynurenine and pyruvate to form 4-(2-aminophenyl)-2,4-dioxobutanoate and alanine. CCBL2 is known only as the predicted protein product of a cloned human gene closely homologous to CCBL1 (Yu et al. 2006) and all of the structural and catalytic properties annotated here are inferred from those of CCBL1.
Cytosolic arylformamidase (AFMID) catalyzes the hydrolysis of formylkynurenine to yield formate and L-kynurenine. Human AFMID has been identified only as an open reading frame; its activity is inferred from that of its well-characterized mouse homologue (Pabarcus and Casida 2002).
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Agmatine is an amine that is formed by decarboxylation of L-arginine by the enzyme arginine decarboxylase (ADC) and hydrolyzed by the enzyme agmatinase to putrescine. Agmatine binds to several target receptors in the brain and has been proposed as a novel neuromodulator (Reghunathan 2006). Agmatine has the potential to serve in the coordination of the early and repair phase pathways of arginine in inflammation (Satriano, 2003).
Agmatine is polyamine formed by decarboxylation of L-arginine by arginine decarboxylase (ADC). Human ADC is a 460-amino acid protein that shows about 48% identity to mammalian ornithine decarboxylase (ODC) but has no ODC activity.
As it hydrolyzes a guanidino group within agmatine and also contains signature amino acid residues that act as ligand binding sites for the potential Mn(++) cofactor, agmatinase is classified as a member of the arginase superfamily (Morris, 2003).
Creatine kinase octamers associated with the inner mitochondrial membrane catalyze the reaction of creatine and ATP to form phosphocreatine and ADP. Two mitochondrial creatine kinase proteins have been identified, one encoded by CKMT1A and B that is found in many tissues and one encoded by CKMT2 that is found in sarcomeres (Haas et al. 1988; Haas and Straus 1990). Studies of sarcomeric creatine kinase octamers suggest that their organization and association with phospholipids in the inner mitochondrial membrane may facilitate energy transfer from ATP generated in the mitochondrial matrix to cytosolic phosphocreatine (Khuchua et al. 1998; Schlattner et al. 2004).
In humans, creatine is synthesized primarily in the liver and kidney, from glycine, arginine, and S-adenosylmethionine, in a sequence of two reactions. From the liver, creatine is exported to tissues such as skeletal muscle and brain, where it undergoes phosphorylation and serves as a short-term energy store. The mechanism by which creatine leaves producer tissues is unclear, but its uptake by consumer tissues is mediated by the SLC6A8 transporter. Once formed, phosphocreatine undergoes a slow spontaneous reaction to form creatinine, which is excreted from the body.
Carnitine is synthesized in four steps from trimethyllysine (generated in turn by the S-adenosyl-methionine-mediated methylation of lysine residues in proteins, followed by protein hydrolysis). The enzymes that catalyze the first three steps of carnitine synthesis, converting trimethyllysine to gamma-butyrobetaine, are widely distributed in human tissues. The enzyme that catalyzes the last reaction, converting gamma-butyrobetaine to carnitine, is found only in liver and kidney cells, and at very low levels in brain tissues. Other tissues that require carnitine, such as muscle, are dependent on transport systems that mediate its export from the liver and uptake by other tissues (Kerner and Hoppel 1998).
Cytosolic creatine kinase catalyzes the reaction of creatine and ATP to form phosphocreatine and ADP. The active form of the enzyme is a dimer. Monomers of the cytosolic enzyme occur in two isoforms, B and M, so called because of their abundance in brain and muscle respectively. The enzyme is widely expressed in the body and many tissues express both isoforms. Both homo- (BB, MM) and heterodimers (BM) are catalytically active.
DNA-repair protein complementing XP-A cells
xeroderma pigmentosum, complementation group A
Xeroderma pigmentosum group A complementing protein
DNA-repair protein complementing XP-A cells (Xeroderma pigmentosum group A complementing protein)
Xeroderma pigmentosum group E complementing protein
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DNA-repair protein complementing XP-G cells (Xeroderma pigmentosum group G complementing protein) (DNA excision repair protein ERCC-5)
Xeroderma pigmentosum group G complementing protein
DNA-repair protein complementing XP-G cells
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UV excision repair protein RAD23 homolog B
XP-C repair complementing complex 58 kDa protein
UV excision repair protein RAD23 homolog B (HHR23B) (XP-C repair complementing complex 58 kDa protein) (P58)
DNA-repair protein complementing XP-F cell
DNA-repair protein complementing XP-F cell (Xeroderma pigmentosum group F complementing protein) (DNA excision repair protein ERCC-4)
Xeroderma pigmentosum group F complementing protein
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xeroderma pigmentosum, complementation group C
Xeroderma pigmentosum group C complementing protein
DNA-repair protein complementing XP-C cells (Xeroderma pigmentosum group C complementing protein) (P125)
DNA-repair protein complementing XP-C cells
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Cytosolic gamma-butyrobetaine hydroxylase dimer (BBOX1) catalyzes the reaction of oxygen, 4-trimethylammoniobutanoate, and 2-oxoglutarate to form C)2, succinate, and carnitine (Lindstedt and Nordin 1984; Vaz et al. 1998).
Cytosolic 4-trimethylaminobutyraldehyde dehydrogenase tetramer (ALDH9A1) catalyzes the reaction of NAD+', and 4-trimethylammoniobutanal to form 4-Trimethylammoniobutanoate and NADH + H+ (Kurys et al. 1989; Vaz et al. 2000).
Cytosolic serine hydroxymethyltransferase tetramer (SHMT1) catalyzes the reaction of 3-Hydroxy-N6,N6,N6-trimethyl-L-lysine to form glycine and 4-trimethylammoniobutanal (Hulse et al. 1978).
Cytosolic tyrosine aminotransferase (TAT) catalyzes the reversible reaction of tyrosine and alpha-keto (2-oxo) glutarate to form 3-(4-hydroxyphenyl)pyruvate and glutamate (Mitchell et al. 2001). The enzymatic activity of the protein encoded by the cloned human TAT cDNA is inferred from the biochemical properties of its rat homologue. Unpublished crystallographic studies (PDB 3DYD) have shown TAT to be a homodimer with a pyridoxal phosphate moity attached to lysine-280 in each monomer.
Cytosolic dihydropteridine reductase (QDPR) catalyzes the reaction of q-dihydrobiopterin with NADH + H+to form tetrahydrobiopterin and NAD+. The enzyme is a homodimer (Lockyer et al. 1987; Su et al. 1993).
Alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) catalyzes the reaction of alpha-aminoadipic semialdehyde and NAD+ to form alpha-aminoadipate and NADH + H+ (Mills et al. 2006). Unpublished crystallographic data (PDB 2J6L) indicate that the enzyme is a homodimer. Recent immunofluorescence studies of both endogenous and GFP-tagged ALDH7A1 proteins in cultured human embryonic kidney cells indicate that the protein is present in both mitochondria and the cytosol (Wong et al. 2010).
The saccharopine dehydrogenase activity of lysine-ketoglutarate reductase / saccharopine dehydrogenase homotetramer in the mitochondrial matrix catalyzes the reaction of saccharopine (N6-(L-1,3-Dicarboxypropyl)-L-lysine), H2O, and NAD+ to form 'L-2-Aminoadipate 6-semialdehyde, glutamate, and NADH + H+ (Markovitz et al. 1984; Sacksteder et al. 2001).
The mitochondrial alpha-ketoglutarate dehydrogenase complex catalyzes the reaction of alpha-ketoadipate, CoASH, and NAD+ to form glutaryl-CoA, CO2, and NADH. The enzyme complex contains multiple copies of three different proteins, E1 (OGDH), E2 (DLST), and E3 (DLD), each with distinct catalytic activities (Reed and Hackert 1990; Zhou et al 2001). The reaction starts with the oxidative decarboxylation of alpha-ketoadipate catalyzed by E1alpha and beta (alpha ketoglutarate dehydrogenase). Lipoamide cofactor associated with E1 is reduced at the same time. Next, the glutaryl group derived from alpha ketoglutarate is transferred to coenzyme A in two steps catalyzed E2 (dihydrolipolyl transacetylase). Finally, the oxidized form of lipoamide is regenerated and electrons are transferred to NAD+ in two steps catalyzed by E3 (dihydrolipoyl dehydrogenase). The biochemical details of this reaction have been worked out with alpha ketoglutarate dehydrogenase complex and subunits purified from bovine tissue (McCartney et al. 1998). While all of the human proteins are known as predicted protein products of cloned genes, direct experimental evidence for their functions is available only for E3 (DLD) (Brautigam et al. 2005).
SLC25A21, the mitochondrial 2-oxodicarboxylate carrier, mediates the exchange of 2-oxoadipate and 2-oxoglutarate across the inner mitochondrial membrane. While the exchange is reversible, under physiological conditions it proceeds in the direction of 2-oxoadipate import into the mitochondrial matrix and 2-oxoglutarate export (Fiermonte et al. 2001).
In humans, most catabolism of L-lysine normally proceeds via a sequence of seven reactions which feeds into the pathway for fatty acid catabolism. In the first two reactions, catalyzed by a single enzyme complex, lysine is combined with alpha-ketoglutarate to form saccharopine, which in turn is cleaved and oxidized to yield glutamate and alpha-ketoadipic semialdehyde. The latter molecule is further oxidized to alpha-ketoadipate. Alpha-ketoadipate is oxidatively decarboxylated by the alpha-ketoglutarate dehydrogenase complex (the same enzyme complex responsible for the conversion of alpha-ketoglutarate to succinyl-CoA in the citric acid cycle), yielding glutaryl-CoA. Glutaryl-CoA is converted to crotonyl-CoA, crotonyl-CoA is converted to beta-hydroxybutyryl-CoA, and beta-hydroxybutyryl-CoA is converted to acetoacetyl-CoA. The products of lysine catabolism are thus exclusively ketogenic; i.e., under starvation conditions they can be used for the synthesis of ketone bodies, beta-hydroxybutyrate and acetoacetate, but not for the net synthesis of glucose (Cox 2001; Goodman and Freeman 2001).
Mitochondrial glutaryl-CoA dehydrogenase (GCDH) catalyzes the reaction of glutaryl-CoA and FAD to form crotonyl-CoA, FADH2, and CO2. The active enzyme is a tetramer of GCDH polypeptides lacking a 44-residue aminoterminal mitochondrial targeting sequence. Mutations in GCDH cause glutaric aciduria type 1 in vivo (Fu et al. 2004; Keyser et al. 2008).
Cytosolic pterin-4-alpha-carbinolamine dehydratase (PCDB1) catalyzes the reaction of 4a-hydroxytetrahydrobiopterin to form q-dihydrobiopterin and water (Hauer et al. 1993. The active enzyme is a homotetramer (Ficner et al. 1995); mutations in the PCDB1 gene are associated with mild hyperphenylalanemia in vivo (Citron et al. 1993).
CCBL1 (KAT 1) catalyzes the reaction of phenylalanine and pyruvate to form 3-(indol-3-yl)pyruvate and alanine. The active form of CCBL1 is a homodimer with one molecule of pyridoxal phosphate bound to each monomer (Baran et al. 1994; Han et al. 2009; Rossi et al. 2004). The enzyme's cytosolic localization is inferred from that of recombinant protein overexpressed in transfected cells (Perry et al. 1995).
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MTH1 inhibition eradicates cancer by preventing sanitation of the dNTP pool
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Stereospecific targeting of MTH1 by (S)-crizotinib as an anticancer strategy
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Iron-sulfur proteins in health and disease
Cytosolic tryptophan 2,3-dioxygenase (TDO) tetramer catalyzes the conversion of L-tryptophan and oxygen to formylkynurenine. The structure and catalytic properties of the human enzyme are inferred from the close similarity of its predicted amino acid sequence (Comings et al. 1995) to that of the well-studied rat enzyme (Dick et al. 2001). In the body, TDO is found predominantly in the liver and is induced by metabolites such as tryptophan and histidine, and by glucocorticoids. These properties, together with TDO's narrow substrate specificity, are consistent with the hypothesis that the enzyme functions functions primarily in tryptophan catabolism and NAD biosynthesis (Taylor and Feng 1991).
Accumulation of cyclin B1 requires E2F and cyclin-A-dependent rearrangement of the anaphase-promoting complex
Cytosolic fumarylacetoacetase catalyzes the hydrolysis of 4-fumarylacetoacetate to form fumarate and acetoacetate (Labelle et al. 1993).
Cytosolic maleylacetoacetic acid isomerase (GSTZ1) catalyzes the conversion of 4-maleylacetoacetate to 4-fumarylacetoacetate. The enzyme is a homodimer (Polekhina et al. 2001).
Cytosolic homogentisate 1,2-dioxygenase (HGD) catalyzes the reaction of homogentisate and molecular oxygen to form 4-maleylacetoacetate. The activity of human HGD is inferred from the phenotype of alkaptonuria patients, in whom HGD activity is defective (Fernandez-Canon et al. 1996). HGD is a homohexamer (Titus et al. 2000).
Cytosolic 4-hydroxyphenylpyruvate dioxygenase (HPD) catalyzes the reaction of 3-(4-Hydroxyphenyl)pyruvate with molecular oxygen to form homogentisate and CO2 (Ruetschi et al. 2000). Unpublished crystallographic data indicate that the enzyme is a homodimer (PDB 3ISQ).
Proline is catabolized in two steps to yield L-glutamate gamma-semialdehyde, which can react further with glutamate to yield ornithine and alpha-ketoglutarate (annotated as a reaction of amino acid synthesis and interconversion) or with NAD+ to yield glutamate and NADH + H+ (Phang et al. 2001).
Mitochondrial delta-1-pyrroline-5-carboxylate dehydrogenase (ALDH4A1) catalyzes the reaction of L-glutamate gamma-semialdehyde and NAD+ to form glutamate and NADH + H+ (Hu et al. 1996). The enzyme is a dimer (Forte-McRobbie and Pietruszko 1986). ALDH4A1 mutations cause type II hyperprolinemia in vivo (Geraghty et al. 1998).
The dehydrogenation of proline to L-1-pyrroline-5-carboxylate coupled to the conversion of FAD to FADH2 is the first step in proline breakdown (Bender et al. 2005). Proline dehydrogenase (PRODH), the enzyme that catalyzes this reaction, is found in liver, kidney, and brain cells, where it is tightly bound to the inner mitochondrial membrane.
The first reaction in this pathway converts phenylalanine to tyrosine, coupled to the conversion of tetrahydrobiopterin to 4a-hydroxytetrahydrobiopterin, catalyzed by phenylalanine hydroxylase. (Deficiencies in this enzyme are responsible for the commonest form of phenylketonuria (PKU) in humans.) This reaction functions both as the first step in the pathway by which the body disposes of excess phenylalanine, and as a source of the amino acid tyrosine. The next two reactions are responsible for the regeneration of tetrahydrobiopterin from 4a-hydroxytetrahydrobiopterin. The following five reactions convert tyrosine to fumarate, an intermediate in the citric acid cycle, and acetoacetate, a ketone body.
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Cytosolic tyrosine aminotransferase (TAT) catalyzes the reversible reaction of 3-(4-hydroxyphenyl)pyruvate and glutamate to form tyrosine and alpha-keto (2-oxo) glutarate (Mitchell et al. 2001). The enzymatic activity of the protein encoded by the cloned human TAT cDNA is inferred from the biochemical properties of its rat homologue. Unpublished crystallographic studies (PDB 3DYD) have shown TAT to be a homodimer with a pyridoxal phosphate moity attached to lysine-280 in each monomer.
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Mitochondrial acetyl-CoA acetyltransferase (ACAT1) catalyzes the reaction of alpha-methyl-acetoacetyl-CoA and CoA to form propionyl-CoA and acetyl-CoA. Structural studies have shown the active enzyme to be a tetramer of ACAT1 polypeptides whose aminoterminal 34 residues, a mitochondrial targeting sequence, have been removed (Haapalainen et al. 2007).
Mitochondrial 3-hydroxyacyl-CoA dehydrogenase type-2 (HSD17B10; HADH2) catalyzes the reversible reaction of alpha-methylacetoacetyl-CoA and NADH + H+ to form alpha-methyl-beta-hydroxybutyryl-CoA and NAD+ (Ofman et al. 2003). Crystallographic data indicate that the enzyme is a homotetramer (Kissinger et al. 2004).
Mitochondrial 3-hydroxyisobutyryl-CoA hydrolase (HIBCH) catalyzes the hydrolysis of beta-hydroxyisobutyryl-CoA to form beta-hydroxyisobutyrate (3-hydroxy-2-methylpropanoate) and CoA (Hawes et al. 1996).
Mitochondrial isobutyryl-CoA dehydrogenase (ACAD8) catalyzes the reaction of isobutyryl-CoA and FAD to form methacrylyl-CoA and FADH2 (Roe et al. 1999; Nguyen et al. 2002). Crystallographic studies have shown the active enzyme to be a tetramer of ACAD8 polypeptides whose aminoterminal 23 residues, a mitochondrial targeting sequence, have been removed (Bataille et al. 2004).
Methylcrotonyl CoA carboxylase (MCCA) catalyzes the reversible reaction of beta-methylglutaconyl-CoA, ADP, orthophosphate, and H2O to form beta-methylcrotonyl-CoA, ATP, and CO2. Active MCCA is composed of two polypeptides, MCCA1 and MCCA2 (Baumgartner et al. 2001; Holzinger et al. 2001). The enzyme has been purified from fibroblast mitochondria. By analogy to the more thoroughly studied bovine homologue, MCCA is thought to be a hexamer of six MCCA1:MCCA2 dimers, and the MCCA1 polypeptides are thought to have biotin moieties covalently bound to a lysine residue at position 681 in the polypeptide chain. Mitochondrial import of MCCA1 and 2 is associated with removal of aminoterminal mitochondrial targeting sequences but the exact lengths of these sequences have not been determined.
Methylcrotonyl CoA carboxylase (MCCA) catalyzes the reversible reaction of beta-methylcrotonyl-CoA, ATP, and CO2 to form beta-methylglutaconyl-CoA, ADP, orthophosphate, and H2O. Active MCCA is composed of two polypeptides, MCCA1 and MCCA2 (Baumgartner et al. 2001; Holzinger et al. 2001). The enzyme has been purified from fibroblast mitochondria. By analogy to the more thoroughly studied bovine homologue, MCCA is thought to be a hexamer of six MCCA1:MCCA2 dimers, and the MCCA1 polypeptide is thought to have a biotin moiety covalently bound to lysine residue 681. Localization of the complex to the mitochondrial inner membrane is inferred from studies of the bovine homologue (Hector et al. 1980). Mitochondrial import of MCCA1 and 2 is associated with removal of aminoterminal mitochondrial targeting sequences (Stadler et al. 2005).
Mitochondrial 3-hydroxyacyl-CoA dehydrogenase type-2 (HSD17B10; HADH2) catalyzes the reversible reaction of alpha-methyl-beta-hydroxybutyryl-CoA and NAD+ to form alpha-methylacetoacetyl-CoA and NADH + H+ (Ofman et al. 2003). Crystallographic data indicate that the enzyme is a homotetramer (Kissinger et al. 2004).
Mitochondrial 2-methyl branched chain acyl-CoA dehydrogenase (ACADSB) catalyzes the reaction of alpha-methylbutyryl-CoA and FAD to form 'tiglyl-CoA and FADH2 (Andresen et al. 2000; Gibson et al. 2000). Unpublished crystallographic data (PDB 2JIF) indicate that the enzyme is a tetramer of ACADSB polypeptides whose aminoterminal 51 residues, a mitochondrial targeting sequence, have been removed.
Mitochondrial isovaleryl dehydrogenase (IVD) catalyzes the reaction of isovaleryl-CoA and FAD to form beta-methylcrotonyl-CoA and FADH2 (Finocchiaro et al. 1978; Rhead and Tanaka 1980). Crystallographic studies demonstrated the existene of a tetramer of IVD polypeptides lacking an aminoterminal mitochondrial targeting sequence (Tiffany et al. 1997).
The mitochondrial nranched-chain alpha-ketoacid dehydrogenase (BKCD) complex catalyzes the reactions of alpha-ketoisocaproate, alpha-keto beta-methylvalerate, or aalpha-ketoisovalerate with CoA and NAD+ to form isovaleryl-CoA, a-methylbutyryl-CoA, or isobuyryl-CoA, respectively, and CO2 and NADH (Chuang and Shih 2001). While bovine and microbial BCKD complexes have been characterized most extensively (Reed and Hackert 1990), structural studies of individual components and subcomplexes of human BKCD have confirmed their structures and roles in the overall oxidative carboxylation process, and have related these features to the disruptive effects of mutations on branched-chain amino acid metabolism in vivo: E1a and E1b components - AEvarsson et al. 2000; E2 - Chang et al. 2002; E3- Brautigam et al. 2005. In addition, structural studies have confirmed the lipoylation of lysine residue 44 in E2 protein (Chang et al. 2002) and the loss of an aminoterminal mitochondrial transport sequence from mature E3 protein (Bruatigam et al. 2005). Loss of mitochondrial transport sequences from proteins E1a, E1b, and E2 has been domstrated by sequence analysis (Wynn et al. 1999).
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A dual-kinase mechanism for Wnt co-receptor phosphorylation and activation
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Isozymes of glyceraldehyde-3-phosphate dehydrogenase in man and other mammals.
The saccharopine dehydrogenase activity of lysine-ketoglutarate reductase / saccharopine dehydrogenase homotetramer in the mitochondrial matrix catalyzes the reaction of lysine, alpha-ketoglutarate, and NADPH + H+ to form saccharopine, NADP+, and H2O (Markovitz et al. 1984; Sacksteder et al. 2001).
The major pathway of histidine catabolism, annotated here, proceeds in four steps to yield glutamate and, in the process, convert one molecule of tetrahydrofolate to 5-formiminotetrahydrofolate (Morris et al. 1972). Histidine can also be decarboxylated to form histamine.
Decarboxylation of L-Histidine happens analogously to other decarboxylations of amino acids. It uses the cofactor pyridoxal phosphate and is catalyzed by histidine decarboxylase (Mamune-Sato et al, 1992).
Cytosolic imidazolonepropionase catalyzes the hydrolysis of 4-imidazolone-5-propanoate to form N-Formimino-L-glutamate. While evidence from many experimental systems indicates that this reaction occurs, existence of the human enzyme is inferred only from high-throughput screening studies (e.g., Yamada et al. 2004).
Cytosolic urocanate hydratase (UROC1) catalyzes the hydrolysis of urocanate to form 4-imidazolone-5-propanoate. Human UROC1 was first identified in surveys of genes differentially expressed in hepatoblastoma (Yamamda et al. 2004). Recent biochemical and molecular studies of UROC1 protein and cDNA from a patient with urocanic aciduria has confirmed the function of UROC1 in vivo (Espinos et al. 2009).
Cytosolic histidine ammonia lyase (HAL) catalyzes the reaction of histidine to form urocanate and NH4+ (Kawai et al. 2005).
The branched-chain amino acids, leucine, isoleucine, and valine, are all essential amino acids (i.e., ones required in the diet). They are major constituents of muscle protein. The breakdown of these amino acids starts with two common steps catalyzed by enzymes that act on all three amino acids: reversible transamination by branched-chain amino acid aminotransferase, and irreversible oxidative decarboxylation by the branched-chain ketoacid dehydrogenase complex. Isovaleryl-CoA is produced from leucine by these two reactions, alpha-methylbutyryl-CoA from isoleucine, and isobutyryl-CoA from valine. These acyl-CoA's undergo dehydrogenation, catalyzed by three different but related enzymes, and the breakdown pathways then diverge. Leucine is ultimately converted to acetyl-CoA and acetoacetate; isoleucine to acetyl-CoA and succinyl-CoA; and valine to succinyl-CoA. Under fasting conditions, substantial amounts of all three amino acids are generated by protein breakdown. In muscle, the final products of leucine, isoleucine, and valine catabolism can be fully oxidized via the citric acid cycle; in liver they can be directed toward the synthesis of ketone bodies (acetoacetate and acetyl-CoA) and glucose (succinyl-CoA) (Chuang & Shih 2001, Sweetman & Williams 2001).
Mitochondrial methylmalonate semialdehyde dehydrogenase (ALDH6A1) catalyzes the reaction of methylmalonate semialdehyde, NAD+, and CoA to form propionyl-CoA, CO2, and NADH + H+. A human ALDH6A1 gene has been cloned. Its sequence is closely homologous to that of the better-characterized rat enzyme (Kedishvili et al. 1992) and a missense mutation in a normally well-conserved codon has been found in the allele of the gene from a patient with a defect in methylmalonic semialdehyde dehydrogenase activity (Chambliss et al. 2000).
The control of glycogen metabolism in the liver
Mitochondrial 3-hydroxyisobutyrate dehydrogenase (HIBADH) catalyzes the reversible reaction of methylmalonyl semialdehyde and NADH + H+ to form beta-hydroxyisobutyrate and NAD+. The biochemical properties of human HIBADH are inferred from those of its better-studied porcine homologue (Robinson and Coon 1957). Unpublished crystallographic studies (PDB 2GF2) have shown the active enzyme to be a tetramer of HIBADH polypeptides whose aminoterminal 40 residues, a mitochondrial targeting sequence, have been removed.
Mitochondrial 3-hydroxyisobutyrate dehydrogenase (HIBADH) catalyzes the reversible reaction of beta-hydroxyisobutyrate and NAD+ to form methylmalonyl semialdehyde and NADH + H+. The biochemical properties of human HIBADH are inferred from those of its better-studied porcine homologue (Robinson and Coon 1957). Unpublished crystallographic studies (PDB 2GF2) have shown the active enzyme to be a tetramer of HIBADH polypeptides whose aminoterminal 40 residues, a mitochondrial targeting sequence, have been removed.
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5'-AMP-activated protein kinase catalytic subunit alpha-1
5'-AMP-activated protein kinase subunit beta-1
5'-AMP-activated protein kinase subunit gamma-1
5'-AMP-activated protein kinase subunit gamma-3
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VEGF activates protein kinase C-dependent, but Ras-independent Raf-MEK-MAP kinase pathway for DNA synthesis in primary endothelial cells
Mismatch repair endonuclease PMS2 ecNumber3.1.-.-/ecNumber
Characterization of the omega class of glutathione transferases
The first step in the biogenesis of thyroid hormones is the oxidation of iodide (I-) by H2O2/peroxidase after being taken up by the thyroid gland. This event is known as organification.
Tyrosines can be iodinated in thyroglobulin to produce precursors for thyroid hormone synthesis.
The catecholamine neurotransmitters dopamine, noradrenaline and adrenaline are found in nervous tissue of animals. They are synthesized in catecholaminergic neurons by four enzymes from tyrosine to adrenaline: tyrosine hydroxylase (TH); aromatic L-amino acid decarboxylase (AADC); dopamine beta-hydroxylase (DBH); and phenylethanolamine N-methyltransferase (PNMT).
Iodide (I-) is transported from blood serum into the thyroid cell by the Na+/I- symporter (sodium/iodide). This intrinsic membrane protein uses energy from the inward movement of Na+ to drive the process and accumulate I- in the cell, maintaining a cellular concentration 30-40 times that of the serum concentration. This process, also called the iodide trap, is stimulated by TSH (thyroid stimulating hormone) and is saturable by large amounts of I-.
Dopamine beta-hydroxylase (DBH; dopamine beta-monooxygenase) is a copper-containing glycoprotein consisting of four identical subunits and catalyzes the oxidation of dopamine to norepinephrine. It requires ascorbic acid as an electron donor. DBH is localized in the norepinephrinergic and epinephrinergic neurons in the central nervous system. The enzyme exists in the secretory vesicles as both soluble and membrane-bound forms. The soluble form is secreted with catecholamines by exocytosis whereas the membrane-bound form is recycled into the vesicles.
Phenylethanolamine N-methyltransferase (PNMT) is the terminal enzyme in catecholamine biosynthesis. It performs transmethylation of noradrenaline to adrenaline using S-adenosyl L-methionine (SAM) as the methyl donor.
RAC-beta serine/threonine protein kinase
Mono- and di-iodinated tyrosine can combine to form tri-iodothyronine (T3). The hormone thyrotropin can stimulate the production of T3 and T4.
The human iodotyrosine dehalogenase 1 (DEHAL1) gene is composed of six exons. Two isoforms (DEHAL1 and DEHAL1B) have been published, both of which have a nitroreductase domain and arise from differential splicing in exon 5. The DEHAL1 isoform is a transmembrane protein that catalyzes the NADPH-dependent deiodination of monoiodotyrosine (MIT) and diiodotyrosine (DIT).
Homologues of p-S1108,S1148,S1192-EIF4G1
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Folding of carboxyl domain and assembly of procollagen I
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Selective regulation of Galpha(q/11) by an RGS domain in the G protein-coupled receptor kinase, GRK2
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Interleukin-7 signaling in human B cell precursor acute lymphoblastic leukemia cells and murine BAF3 cells involves activation of STAT1 and STAT5 mediated via the interleukin-7 receptor alpha chain
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Endonuclease III-like protein 1 (EC 4.2.99.18)
DNA repair protein REV1 ecNumber2.7.7.-/ecNumber
Methylated-DNA--protein-cysteine methyltransferase (EC 2.1.1.63) (6-O- methylguanine-DNA methyltransferase)
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Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein
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WD repeat domain phosphoinositide-interacting protein 1
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Zinc finger and BTB domain-containing protein 17
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Sensorineural deafness and seizures in mice lacking vesicular glutamate transporter 3
Oxygen and carbon dioxide transport in vertebrate erythrocytes: an evolutionary change in the role of membrane transport
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A proposed nomenclature system for the cytosolic sulfotransferase (SULT) superfamily
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Serine biosynthesis starts from 3-phosphoglycerate, a glycolysis intermediate. Its dehydrogenation is catalysed by tetrameric phosphoglycerate dehydrogenase PHGDH. (Tabatabaie et al. 2009).
The amino group needed for serine biosynthesis comes from glutamate. Its transfer onto 3-phosphonooxpyruvate is catalysed by the PSAT1 dimer which needs pyridoxal phosphate as cofactor. (Baek et al. 2003)
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Dephosphorylation of O-phospho-L-serine to L-serine proceeds through a phospho-enzyme intermediate of the catalysing phosphatase PSP (Collet et al. 1997).
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L-Serine is needed in human brain in large amounts as precursor to important biomolecules such as nucleotides, phospholipids and the neurotransmitters glycine and D-serine. The pathway for its synthesis starts with 3-phosphoglycerate and it later needs glutamate as an amination agent. Deficiencies in the participating enzymes lead to severe neurological symptoms that are treatable with serine if treatment starts early (de Koning & Klomp 2004).
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CCBL1 (KAT 1) catalyzes the reaction of glutamine and pyruvate to form 2-oxoglutaramate and alanine. The active form of CCBL1 is a homodimer with one molecule of pyridoxal phosphate bound to each monomer (Baran et al. 1994; Han et al. 2009; Rossi et al. 2004). The enzyme's cytosolic localization is inferred from that of recombinant protein overexpressed in transfected cells (Perry et al. 1995).
Mitochondrial branched-chain-amino-acid aminotransferase (BCAT2) catalyzes the reversible reactions of alpha-ketoisocaproate, alpha-keto-beta-methylvalerate, or a-ketoisovalerate with glutamate to form leucine, isoleucine, or valine, respectively, and alpha-ketoglutarate (Bledsoe et al. 1997). The active enzyme is a homodimer (Yennawar et al. 2001, 2002). In the body, this enzyme is widely expressed but is especially abundant in muscle tissue.
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These reactions mediate the synthesis of aspartate, asparagine, glutamate, and glutamine from ammonia and intermediates of glycolysis, and allow the utilization of the carbon atoms from these four amino acids for glucose synthesis under fasting conditions. These reactions also provide a means to collect nitrogen, both as ammonia and as amino groups, and direct it towards urea synthesis. Transamination, the conversion of an amino acid to the corresponding alpha-keto acid coupled to the conversion of a molecule of alpha-ketoglutarate to glutamate, is the first step in the catabolism of most amino acids. Transamination reactions are freely reversible so they also provide a means to balance concentrations of various amino acids and alpha-keto (2-oxo) acids in the cytosol.
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Cytosolic branched-chain-amino-acid aminotransferase (BCAT1) catalyzes the reversible reactions of leucine, isoleucine, or valine with alpha-ketoglutarate (2-oxoglutarate) to form alpha-ketoisocaproate, alpha-keto-beta-methylvalerate, or a-ketoisovalerate, respectively, and glutamate. The active enzyme is a homodimer. Hutson and colleagues have argues that cytosolic BCAT1 plays a major role in the generation of glutamate involved in synaptic transmission in neural tissue (Goto et al. 2005).
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Cytosolic branched-chain-amino-acid aminotransferase (BCAT1) catalyzes the reversible reactions of alpha-ketoisocaproate, alpha-keto-beta-methylvalerate, or a-ketoisovalerate with glutamate to form leucine, isoleucine, or valine, respectively, and alpha-ketoglutarate (2-oxoglutarate). The active enzyme is a homodimer (Goto et al. 2005).
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Mitochondrial branched-chain-amino-acid aminotransferase (BCAT2) catalyzes the reversible reactions of leucine, isoleucine, or valine with alpha-ketoglutarate (2-oxoglutarate) to form alpha-ketoisocaproate, alpha-keto-beta-methylvalerate, or a-ketoisovalerate, respectively, and glutamate (Bledsoe et al. 1997). The active enzyme is a homodimer (Yennawar et al. 2001, 2002). In the body, this enzyme is widely expressed but is especially abundant in muscle tissue.
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The role for endoplasmic reticulum stress in diabetes mellitus
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Signaling through PI3Kgamma: a common platform for leukocyte, platelet and cardiovascular stress sensing
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Molecular cloning and expression of mouse and human cDNA encoding AES and ESG proteins with strong similarity to Drosophila enhancer of split groucho protein
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Topological journey of parasite-derived antigens for presentation by MHC class I molecules
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PAP is generated as a byproduct of sulfonation reactions in vivo; its hydrolysis to AMP and orthophosphate returns its constituents to the pool of molecules available for cytosolic nucleotide metabolism. Bisphosphate 3'-nucleotidase 1catalyzes this reaction efficiently in vitro; whether other nucleotidases also play a role in PAP breakdown in vivo is unknown.
Two groups of sulfotransferease (SULT) enzymes catalyze the transfer of a sulfate group from 3-phosphoadenosine 5-phosphosulfate (PAPS) to a hydroxyl group on an acceptor molecule, yielding a sulfonated acceptor and 3-phosphoadenosine 5-phosphate (PAP). One is localized to the Golgi apparatus and mediates the sulfonation of proteoglycans. The second, annotated here, is cytosolic and mediates the sulfonation of a diverse array of small molecules, increasing their solubilities in water and modifying their physiological functions. There are probably thirteen or more human cytosolic SULT enzymes; eleven of these have been purified and characterized enzymatically, and are annotated here (Blanchard et al. 2004; Gamage et al. 2005). These enzymes appear to be active as dimers. Their substrate specificities are typically broad, and not related in an obvious way to their structures; indeed, apparently orthologous human and rodent SULT enzymes can have different substrate specificities (Glatt 2000), and none has been exhaustively characterized. The substrates listed in the table and annotated here are a sample of the known ones, chosen to indicate the range of activity of these enzymes and to capture some of their known physiologically important targets. Absence of a small molecule - enzyme pair from the table, however, may only mean that it has not yet been studied.
Formation of a pool of free 40S subunits
At the beginning of this reaction, 1 molecule of 'H+', 1 molecule of '6-Methylmercaptopurine', 1 molecule of 'Oxygen', and 1 molecule of 'NADPH' are present. At the end of this reaction, 1 molecule of 'NADP+', 1 molecule of '6-Mercaptopurine', 1 molecule of 'Formaldehyde', and 1 molecule of 'H2O' are present. This reaction takes place in the 'smooth endoplasmic reticulum' and is mediated by the 'oxygen binding activity' of 'Cytochrome P450 1A2 '.
Sulfonation of estrone is catalyzed by SULT1E1 (Aksoy et al. 1994; Falany et al. 1995), and also by SULT2A1 (Comer et al. 1993), although the efficiency of SULT2A1 catalysis is unknown.
Sulfonation of dehydroepiandrosterone (DHEA) is catalyzed by SULT1E1 (Aksoy et al. 1994), SULT2A1 (Radominska et al. 1990) and the a and b isoforms of SULT2B1 (Meloche and Falany 2001).
Sulfonation of lithocholate is catalyzed by SULT2A1 (Radominska et al. 1990).
Sulfonation of taurolithocholate is catalyzed by SULT2A1 (Radominska et al. 1990).
The 3-hydroxyl groups of a number of sterols can undergo sulfonation. Cholesterol sulfate is particularly abundant in the body, and may have both regulatory and biosynthetic functions (Strott and Higashi 2003). Its synthesis is catalyzed by the b isoform of SULT2B1 (Fuda et al. 2002; Javitt et al. 2001).
The sulfonation of pregnenolone (PREG) is catalyzed by both the a and b isoforms of SULT2B1, although the a isoform is more active in assays in vitro (Fuda et al. 2002; Meloche and Falany 2001).
The sulfonation of 27-hydroxycholesterol (27HCHOL) is catalyzed by both the a and b isoforms of SULT2B1 (Javitt et al. 2001).
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The glutathione S-transferases (GSTs) catalyze the nucleophilic attack by reduced glutathione (GSH) on nonpolar compounds that contain an electrophilic carbon, nitrogen, or sulphur atom. Their substrates include halogenonitrobenzenes, arene oxides, quinones, and alpha, beta-unsaturated carbonyls. Three major families of proteins are widely distributed in nature. Two of these, the cytosolic and mitochondrial GST, comprise soluble enzymes that are only distantly related whilst the third family comprises microsomal GST, referred to as membrane-associated proteins in eicosanoid and glutathione (MAPEG) metabolism. At least 16 cytosolic GST subunits exist in human which are all in a dimeric form. Based on amino acid sequence similarities, seven classes of cytosolic GST are recognized in mammalian species; Alpha, Mu, Pi, Sigma, Theta, Omega, and Zeta (25). As well as being homodimers, the Alpha and Mu classes are also able to form heterodimers so a large number of isozymes are possible from all cytosolic GST subunits (Sinning et al. 1993, LeTrong et al. 2002, Ahmad et al. 1993, Pastore et al. 1998, Tars et al. 2010, Bruns et al. 1999, Balogh et al. 2010, Morel et al. 2002, Li et al. 2005, Patskovsky et al. 2006, Raghunathan et al. 1994, Patskovsky et al. 1999, Comstock et al. 1994, Board et al. 2000, Zhou et al. 2011, Zhou et al. 2012, Sun et al. 2011, Tars et al. 2006, Rossjohn et al. 1998, Polekhina et al. 2001, Inoue et al. 2003). Typical electrophilic substrates are chosen as examples for which the majority of the cytosolic GST isozymes act on.
Glutathione S-Transferases (GSTs; EC 2.5.1.18) are another major set of phase II conjugation enzymes. They can be found in the cytosol as well as being microsomal membrane-bound. Cytosolic GSTs are encoded by at least 5 gene families (alpha, mu, pi, theta and zeta GST) whereas membrane-bound enzymes are encoded by single genes. Soluble GSTs are homo- or hetero-dimeric enzymes (approximately 25KDa subunits) which can act on a wide range of endogenous and exogenous electrophiles. GSTs mediate conjugation using glutathione (GSH), a tripeptide synthesized from its precursor amino acids gamma-glutamate, cysteine and glycine. A generalized reaction is RX + GSH -> HX + GSR Glutathione conjugates are excreted in bile and converted to cysteine and mercapturic acid conjugates in the intestine and kidneys. GSH is the major, low molecular weight, non-protein thiol synthesized de novo in mammalian cells. As well as taking part in conjugation reactions, GSH also has antioxidant ability and can metabolize endogenous and exogenous compounds. The nucleophilic GSH attacks the electrophilic substrate forming a thioether bond between the cysteine residue of GSH and the electrophile. The result is generally a less reactive and more water-soluble conjugate that can be easily excreted. In some cases, GSTs can activate compounds to reactive species such as certain haloalkanes and haloalkenes. Substrates for GSTs include epoxides, alkenes and compounds with electrophilic carbon, sulfur or nitrogen centres. There are two types of conjugation reaction with glutathione: displacement reactions where glutathione displaces an electron-withdrawing group and addition reactions where glutathione is added to activated double bond structures or strained ring systems.
Gamma-glutamylcyclotransferase (GGCT) homodimer (Bae et al, 2008) can catalyzes the formation of 5-oxoproline from gamma-glutamyl-amino acid products and thus can play a role in glutathione homeostasis (Oakley et al, 2008).
The combination of glutamate, cysteine and ATP is required to form glutathione. The steps involved in the synthesis and recycling of glutathione are outlined (Meister, 1988).
In the second step in the formation of glutathione, gamma-glutamylcysteine ligates with glycine to form glutathione (Gali and Board, 1995; ).
Extracellular glutathione can be hydrolyzed to give cysteinylglycine (Cys-Gly) and gamma glutamate, which, in the presence of amino acids, can form a gamma-glutamate:AA product (Heisterkamp et al, 2008). This hydrolysis provides cells with a cysteine supply and contributes to the maintainance of intracellular glutathione levels (Tate and Ross, 1977; Pawlak et al, 1989).
Gamma-glutamylcyclotransferase (GGCT) homodimer (Bae et al, 2008) catalyzes the formation of 5-oxoproline from gamma-glutamylcysteine and thus, may play a role in glutathione homeostasis (Oakley et al, 2008).
5-oxoprolinase catalyzes the cleavage of 5-oxoproline to form L-glutamate, coupled to the hydrolysis of ATP to ADP and inorganic phosphate (Chen et al, 1998).
Methylation is a common but minor pathway of Phase II conjugation compared to glucuronidation or sulfonation. The cofactor used in methylation conjugation is S-adenosylmethionine (SAM). SAM is the second most widely used enzyme substrate after ATP and is involved in a wide range of important biological processes. SAM is sythesized from methionine's reaction with ATP, catalyzed by methionine adenosyltransferase (MAT). There are two genes, MAT1A and MAT2A, which encode for two homologous MAT catalytic subunits, 1 and 2. During conjugation with nucleophilic substrates, the methyl group attached to the sulfonium ion of SAM is transferred to the substrate forming the conjugate. SAM, having lost the methyl moiety, is converted to S-adenosylhomocysteine (SAH). SAH can be hydrolyzed to form adenosine and homocysteine. Homocysteine can either be converted to glutathione or methylated to form methionine, thus forming the starting point for SAM synthesis and completing the cycle. Fuctional groups attacked are phenols, catechols, aliphatic and aromatic amines and sulfhydryl-containing groups. The enzymes that catalyze the transfer of the methyl group to these functional groups are the methyltransferases (MT). MTs are small, cytosolic, monomeric enzymes that utilize SAM as a methyl donor. There are many MTs but the best studied ones are named on the basis of their prototypical substrates: COMT (catechol O-methyltransferase), TPMT (thiopurine methyltransferase), TMT (thiol methyltransferase), HNMT (histamine N-methyltransferase) and NNMT (nicotinamide N-methyltransferase). An example of each enzyme mentioned is given. In each case, a typical substrate for the enzyme is shown.
Early signaling pathways activated by c-Kit in hematopoietic cells
Pyridine is a typical substrate for Nicotinamide N-methyltransferase
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Human skeletal-muscle aldolase: N-terminal sequence analysis of CNBr- and o-iodosobenzoic acid-cleavage fragments
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SRP-dependent cotranslational protein targeting to membrane
To be excreted in urine, glutathione conjugates undergo several hydrolysis steps to form mercapturic acids which are readily excreted. The first step is the hydrolysis of a gamma-glutamyl residue from the conjugate catalysed by gamma-glutamyltransferases (GGTs). These are membrane-bound, heterodimeric enzymes composed of light and heavy peptide chains. GGT1 and 2 are well characterised while GGT3P, 5, 6 and 7 are putative transferases. Extracellular glutathione or its conjugates can be hydrolysed to give cysteinylglycine (CG, or CG conjugates) and free glutamate (L-Glu) (Heisterkamp et al. 2008, Tate & Ross 1977, Pawlak et al. 1989).
Aminocyclases 1 and 3 (ACY1,3) can hydrolyse N-acetylated amino acids and N-acetylcysteine-S-conjugates (Lindner et al. 2003). They are functional as dimers and utilise zinc as a cofactor.
The cell biology of cross-presentation and the role of dendritic cell subsets
Aflatoxins are among the principal mycotoxins produced as secondary metabolites by the molds Aspergillus flavus and Aspergillus parasiticus that contaminate economically important food and feed crops (Wild & Turner 2002). Aflatoxin B1 (AFB1) is the most potent naturally occurring carcinogen known and is also an immunosuppressant. It is a potent hepatocarcinogenic agent in many species, and has been implicated in the etiology of human hepatocellular carcinoma. Poultry, especially turkeys, are extremely sensitive to the toxic and carcinogenic action of AFB1 present in animal feed, resulting in multi-million dollar losses to the industry. Discerning the biochemical and molecular mechanisms of this extreme sensitivity of poultry to AFB1 will help with the development of new strategies to increase aflatoxin resistance (Rawal et al. 2010, Diaz & Murcia 2011). AFB1 has one major genotoxic metabolic fate, conversion to AFXBO, and several others that are less mutagenic but that can still be quite toxic, causing [X, Y, and Z]. AFB1 can be oxidised to the toxic AFB1 exo 8,9 epoxide (AFXBO) product by several cytochrome P450 enzymes, especially P450 3A4 in the liver. This 8,9 epoxide can react with the N7 atom of a guanyl base of DNA to produce adducts by intercalating between DNA base pairs. The exo epoxide is unstable in solution, however, and can react spontaneously to form a diol that is no longer reactive with DNA. The diol product in turn undergoes base-catalysed rearrangement to a dialdehyde that can react with protein lysine residues. AFB1 can also be metabolised to products (AFQ1, AFM1, AFM1E) which have far less genotoxic consequences than AFB1. The main route of detoxification of AFB1 is conjugation of its reactive 8,9-epoxide form with glutathione (GSH). This reaction is carried out by trimeric glutathione transferases (GSTs), providing a chemoprotective mechanism against toxicity. Glutathione conjugates are usually excreted as mercapturic acids in urine (Guengerich et al. 1998, Hamid et al. 2013). The main metabolic routes of aflatoxin in humans are described here.
All organisms are constantly exposed to foreign chemicals every day. These can be man-made (drugs, industrial chemicals) or natural (alkaloids, toxins from plants and animals). Uptake is usually via ingestion but inhalation and transdermal routes are also common. The very nature of many chemicals that make them suitable for uptake by these routes, in other words their lipophilicty (favours fat solubility) is also the main reason organisms have developed mechanisms that convert them to hydrophilic (favours water solubility) compounds which are readily excreted via bile and urine. Otherwise, lipophilic chemicals would accumulate in the body and overwhelm defense mechanisms. This process is called biotransformation and is catalyzed by enzymes mainly in the liver of higher organisms but a number of other organs have considerable ability to process xenobiotica such as kidneys, gut and lungs. As well as xenobiotics, many endogenous compounds are commonly eliminated by this process. This mechanism is of ancient origin and a major factor for its development in animals is plants. Most animals are plant eaters and thus are subject to a huge variety of chemical compounds which plants produce to stop themselves being eaten. This complex set of enzymes have several features which make them ideal for biotransformation; (1) metabolites of the parent chemical are usually made more water soluble so it favours rapid excretion via bile and urine (2) the enzymes possess broad and overlapping specificity to be able to deal with newly exposed chemicals (3) metabolites of the parent generally don't have adverse biological effects. In the real world however, all these criteria have exceptions. Many chemicals are transformed into reactive metabolites. In pharmacology, the metabolites of some parent drugs exert the desired pharmacological effect but in the case of polycyclic aromatic hydrocarbons (PAHs), which can undergo epoxidation, it results in the formation of an electrophile which can attack proteins and DNA. Metabolism of xenobiotica occurs in several steps called Phase 1 (functionalization) and Phase 2 (conjugation). To improve water solubility, a functional group is added to or exposed on the chemical in one or more steps (Phase 1) to which hydrophilic conjugating species can be added (Phase 2). Functional groups can either be electrophilic (epoxides, carbonyl groups) or nucleophilic (hydroxyls, amino and sulfhydryl groups, carboxylic groups) (see picture). Once chemicals undergo functionalization, the electrophilic or nucleophilic species can be detrimental to biological systems. Electrophiles can react with electron-rich macromolecules such as proteins, DNA and RNA by covalent interaction whilst nucleophiles have the potential to interact with biological receptors. That's why conjugation is so important as it mops up these potentially reactive species. Many chemicals, when exposed to certain metabolizing enzymes can induce those enzymes, a process called enzyme induction. The effect of this is that these chemicals accelerate their own biotransformation and excretion. The reverse is also true where some chemicals cause enzyme inhibition. Some other factors that alter enzyme levels are sex, age and genetic predisposition. Between species, there can be considerable differences in biotransformation ability which is a problem faced by drug researchers interpreting toxicological results to humans.
As inferred from biochemical studies in yeast and phenotypic studies in mouse, Mitoferrin-1 (SLC25A37) and Mitoferrin-2 (SLC25A28) transport ferrous iron across the inner mitochondrial membrane. Mitoferrin-1 is essential for maintaining mitochondrial iron uptake in developing erythroid cells; mitoferrin-2 is ubiquitously expressed. Defects in Mitoferrin-1 and Mitoferrin-2 cause a reduction in mitochondrial iron acquisition and biogenesis of iron-sulfur clusters and heme.
Phase II of biotransformation is concerned with conjugation, that is using groups from cofactors to react with functional groups present or introduced from phase I on the compound. The enzymes involved are a set of transferases which perform the transfer of the cofactor group to the substrate. The resultant conjugation results in greatly increasing the excretory potential of compounds. Although most conjugations result in pharmacological inactivation or detoxification, some can result in bioactivation. Most of the phase II enzymes are located in the cytosol except UDP-glucuronosyltransferases (UGT), which are microsomal. Phase II reactions are typically much faster than phase I reactions therefore the rate-limiting step for biotransformation of a compound is usually the phase I reaction. Phase II metabolism can deal with all the products of phase I metabolism, be they reactive (Type I substrate) or unreactive/poorly active (Type II substrate) compounds. With the exception of glutathione, the conjugating species needs to be made chemically reactive after synthesis. The availability of the cofactor in the synthesis may be a rate-limiting factor in some phase II pathways as it may prevent the formation of enough conjugating species to deal with the substrate or it's metabolite. As many substrates and/or their metabolites are chemically reactive, their continued presence may lead to toxicity.
Aflatoxin B1 (AFB1) undergoes extensive oxidation, which is catalysed by cytochrome P450s. In addition to formation of the 8,9-oxide, oxidation by CYP1A2 yields a stable metabolite, aflatoxin M1 (AFM1), that is excreted in milk and urine (Ueng et al. 1995). AFM1 is less carcinogenic or mutagenic than AFB1, but is equally toxic.
Metabolites that are formed from aflatoxin B1 (AFB1) include AFQ1, AFM1 and AFP1 (Gallagher et al. 1996). These metabolites and other naturally occurring aflatoxins (G1, B2 and G2) are poorer substrates for epoxidation and, consequently, are less mutagenic, carcinogenic and toxic than AFB1. AFB1 metabolites can be useful biomarkers of human exposure to aflatoxins and AFM1, AFQ1 and AFP1 have all been detected in human urine samples (Groopman et al. 1985). Cytochrome P450 3A4 and 3A5 are the predominant enzymes involved in AFQ1 (3-hydroxy aflatoxin) production (Raney et al. 1992).
Aflatoxin B1 (AFB1) requires microsomal oxidation to produce epoxides which cause the toxic and carcinogenic effects. In humans, cytochrome P450 enzymes produce epoxide stereoisomers of AFB1, the most potent being aflatoxin exo-8,9-oxide (AFNBO). CYP3A4 and CYP1A2 can also produce aflatoxin B1-endo-8,9-epoxide (Raney et al. 1992, Ueng et al. 1995).
Aflatoxin B1 (AFB1) requires microsomal oxidation to produce epoxides which cause the toxic and carcinogenic effects. In humans, cytochrome P450 enzymes produce epoxide stereoisomers of AFB1, the most potent being aflatoxin exo-8,9-oxide (AFXBO). This conversion is carried out by at least four P450s; 1A2, 3A4, 3A5 and 2A13. CYP3A4 mainly produces the exo form whereas CYP1A2 produces a racemic mixture of exo and endo forms (Gallagher et al. 1996, He et al. 2006).
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Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs
Crystal structures of human GAR Tfase at low and high pH and with substrate beta-GAR
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This group of reactions is responsible for: 1) the breakdown of amino acids; 2) the synthesis of urea from ammonia and amino groups generated by amino acid breakdown; 3) the synthesis of the ten amino acids that are not essential components of the human diet; and 4) the synthesis of related nitrogen-containing molecules including carnitine and creatine. Transport of these molecuels across lipid bilayer membranes is annotated separately as part of the module on "transmembrane transport of small molecules".
The main sulfur amino acids are methionine, cysteine, homocysteine and taurine. Of these, the first two are proteinogenic. This group of reactions contains all processes that 1) break down sulfur amino acids, 2) interconvert between them, and 3) synthesize them from solved sulfide which comes from sulfate assimilation and reduction. Only plants and microorganisms employ all processes. Humans cannot de novo synthesize any sulfur amino acid, nor convert cysteine to methionine (Brosnan & Brosnan, 2006).
Heme A is the prosthetic group of cytochrome c oxidase, the terminal enzyme in the respiratory chain. It is formed by the action of cytochrome c oxidase assembly protein COX15 homolog (COX15) on heme O (Petruzzella et al. 1998, Antonicka et al. 2003). Defects in COX15 cause of mitochondrial complex IV deficiency (MT-C4D; MIM:220110), also called cytochrome c oxidase deficiency resulting in a disorder of the mitochondrial respiratory chain seen as heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs (Antonicka et al. 2003). Defects in COX15 also cause Leigh syndrome (LS; MIM:256000), an early-onset progressive neurodegenerative disorder characterised by the presence of focal, bilateral lesions in one or more areas of the central nervous system (Oquendo et al. 2004, Bugiani et al. 2005).
Heme O and heme A are specifically synthesised for the heme-copper respiratory oxidases. Mitochondrial protoheme IX farnesyltransferase (COX10) mediates the transformation of protoheme IX (heme) and farnesyl diphosphate (FAPP) to heme O (Glerum & Tzagoloff 1994). COX10 is highly expressed in muscle, heart and brain (Murakami et al. 1997).
Sulfate leaves the mitochondrion with the help of the dicarboxylate carrier, via antiport with malate (Crompton et al. 1974, Fiemont et al. 1999)
While in humans excess methionine is converted to homocysteine, homocysteine and its transsulfuration product cysteine can be degraded to several end products, two of which, taurine and hydrogen sulfide, have uses in other biological processes (Stipanuk & Ueki 2011).
While the human body is very economical with sulfur amino acids (SAA), superfluous SAA are degraded via cysteine to toxic hydrogen sulfide which must be dealt with. The pathway to oxidize this gas is localized to mitochondria and is highly conserved, pointing back to a time when life was immersed in sulfide-rich waters. The pathway for sulfide oxidation consists of five reactions, one of which, the sulfur transfer from thiosulfate to glutathione, is still to be characterized fully. A mutation in one enzyme has been identified that is associated with ethylmalonyl encephalopathy and where tissue sulfide is elevated (Stipanuk & Ueki 2011).
Porphyrins are heterocyclic macrocycles, consisting of four pyrrole subunits (tetrapyrrole) linked by four methine (=CH-) bridges. The extensive conjugated porphyrin macrocycle is chromatic and the name itself, porphyrin, is derived from the Greek word for purple. The aromatic character of porphyrins can be seen by NMR spectroscopy. Porphyrins readily combine with metals by coordinating them in the central cavity. Iron (heme) and magnesium (chlorophyll) are two well known examples although zinc, copper, nickel and cobalt form other known metal-containing phorphyrins. A porphyrin which has no metal in the cavity is called a free base. Some iron-containing porphyrins are called hemes (heme-containing proteins or hemoproteins) and these are found extensively in nature ie. hemoglobin. Hemoglobin is quantitatively the most important hemoprotein. The hemoglobin iron is the transfer site of oxygen and carries it in the blood all round the body for cell respiration. Other examples are cytochromes present in mitochondria and endoplasmic reticulum which takes part in electron transfer events, catalase and peroxidase whic protect the body against the oxidant hydrogen peroxide and tryptophan oxygenase which is present in intermediary metabolism. Hemoproteins are synthesized in all mammalian cells and the major sites are erythropoietic tissue and the liver. The processes by which heme is synthesized, transported, and metabolized are a critical part of human iron metabolism (Severance and Hamze 2009); here the core processes of heme biosynthesis and catabolism have been annotated.
Eight enzymes are involved in heme biosynthesis, four each in the mitochondria and the cytosol. The process starts in the mitochondria with the condensation of succinyl CoA (from the TCA cycle) and glycine to form 5-aminolevulinate (ALA). The next four steps take place in the cytosol. Two molecules of ALA are condensed to form the monopyrrole porphobilinogen (PBG). The next two steps convert four molecules of PBG into the cyclic tetrapyrrole uroporphyringen III, which is then decarboxylated into coproporphyrinogen III. The last three steps occur in the mitochondria and involve modifications to the tetrapyrrole side chains and finally, insertion of iron. In addition to these synthetic steps, a spontaneous cytosolic reaction allows the formation of uroporphyringen I which is then enzymatically decarboxylated to coproporphyrinogen I, which cannot be metabolized further in humans. Also, lead can inactivate ALAD, the enzyme that catalyzes PBG synthesis, and ferrochelatase, the enzyme that catalyzes heme synthesis. The porphyrias are disorders that arise from defects in the enzymes of heme biosynthesis. Defective pathway enzymes after ALA synthase result in accumulated substrates which can cause either skin problems, neurological complications, or both due to their toxicity in higher concentrations. They are broadly classified as hepatic porphyrias or erythropoietic porphyrias, based on the site of the overproduction of the substrate. Each defect is described together with the reaction it affects.
Cytochrome P450 1B1 (CYP1B1) can oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. CYP1B1 can also activate a range of procarcinogens. A specific substrate is the female sex hormone estradiol-17beta which is hydroxylated at position 4.
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PIKKing on PKB: regulation of PKB activity by phosphorylation
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Aflatoxins are produced by the fungal molds Aspergillus flavus and Aspergillus parasiticus. Dietary contamination accounts for adverse health problems including liver cancer therby classifying aflatoxins as Group 1 carcinogens in humans. The B1 form of aflatoxin (AFB1) is especially carcinogenic in a number of species including humans. AFB1 requires microsomal oxidation to produce epoxides which are the cause of their toxic and carcinogenic effects. In humans, both CYP3A4 and CYP3A5 are able to produce epoxide stereoisomers of AFB1, the most potent being aflatoxin B1 exo-8,9-oxide (AFXBO) (Gallagher et al. 1996).
The CYP3A family are the most abundantly expressed P450s in human liver, accounting for around 50% of xenobiotic drug metabolism. CYP3A4 is the most abundant member of the family and possesses broad specificity to a range of xenobiotics. Loperamide (LOP), an antidiarrheal, is mainly metabolized to desmethylloperamide (DLOP) through the N-demethylation pathway. This initial N-demethylation is carried out by CYP3A4.
CYP1A2 oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. It is most active in catalyzing N-hydroxylation or N-dealkylation reactions.
Heterocyclic and aromatic amines require metabolic activation to convert them to genotoxic metabolites.The initial step is N-hydroxylation and cytochrome P450 1A2 can carry out the catalysis.
Caffeine is one of the world's most frequently consumed xenobiotic. The major source of caffeine comes from tea and coffee. Caffeine is extensively metabolized in humans with at least 17 metabolites formed in its biotransformation. CYP1A2 is a prominent enzyme in the formation of an important metabolite of caffeine (paraxanthine) by N3-demethylation.
A simple example of epoxidation is the oxidation of an alkene (olefin) to the epoxide (oxirane), catalysed by CYP1A1. Even the simplest of epoxides (ethylene oxide) can react with DNA and amino groups in a protein.
A number of CYPs take part in cholesterol biosynthesis and elimination, thus playing an important role in maintaining cholesterol homeostasis. Under normal physiological conditions, cholesterol intake (diet or synthesized de novo from acetyl CoA) equals cholesterol elimination (degraded to bile salts, secreted in bile and used in steroid hormone synthesis). These processes are under tight regulatory control and any disruption leads to increased cholesterol levels resulting in cardiovacular disease. The CYPs involved in cholesterol homeostasis could serve as potential targets for cholesterol-lowering drugs.
P450 11B2 (steroid 11 beta-hydroxylase) is a mitochondrial cytochrome P-450 enzyme necessary for cortisol biosynthesis.The synthesis of the most important glucocorticoid and mineralocorticoid hormones in humans (cortisol and aldosterone, respectively), take place in the adrenal gland. The 11?- and 18-hydroxylation of the substrate 11-deoxycorticosterone (DOC) leads to corticosterone (B)band 18-hydroxycorticosterone (18-OH-B), whose 18-oxidation yields aldosterone. CYP11B1 is also able to produce corticosterone from 11-deoxycorticosterone but it cannot convert corticosterone into aldosterone.
Cloning, in vitro expression, and tissue distribution of a human prostaglandin transporter cDNA(hPGT)
Of the 50 microsomal CYPs, 15 act on xenobiotics. They all possess wide substrate specificity to cater for most foreign compounds that find their way into the body.
CYP3A7 is only expressed in fetal liver and not in adults. It has lower biotransformation capability than other members of the CYP3A family such as 3A4 or 3A5 but possesses a similar broad specificity. CYP3A7 plays a major role in fetal steroid hydroxylation, an example being the 6beta-hydroxylation of testosterone.
Identification of a novel aquaporin, AQP12, expressed in pancreatic acinar cells
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Approximately a quarter of the 57 human CYPs still remain "orphans" in the sense that their function, expression sites, and regulation are largely not elucidated. While there is enough experimental evidence to know that all these proteins get made and can catalyze CYP-like reactions in vitro, evidence of in vivo function and substrate specificity is insufficient to allow them to be placed in any of the classes in the functional scheme.
CYP3A43 belongs to the CYP3A family, of which CYP3A4 is the most active member in the biotransformation of xenobiotics. Testosterone metabolites are a major determinant of prostate growth and differentiation. CYP3A43, which is expressed in the prostate, exhibits minor 6-beta-hydroxylation activity towards testosterone. Thus, CYP3A43 may be involved in the etiology of prostate cancer.
Tamoxifen (TAM) is an antiestrogen and currently used extensively for breast cancer therapy. FMOs, especially FMO1 can N-oxidze TAM to tamoxifen N-oxide (TNO). TNO can be reduced back to TAM by the P450 system. TNO appears to be just as potent as TAM but with fewer side-effects so this metabolic cycling could play a part in the use of TNO in the treatment of breast cancer.
The P450 isozyme system is the major phase 1 biotransforming system in man, accounting for more than 90% of drug biotransformations. This system has huge catalytic versatility and a broad substrate specificity, acting upon xenobiotica and endogenous compounds. It is also called the mixed-function oxidase system, the P450 monooxygenases and the heme-thiolate protein system. All P450 enzymes are a group of heme-containing isozymes which are located on the membrane of the smooth endoplasmic reticulum. They can be found in all tissues of the human body but are most concentrated in the liver. The name "cytochrome P450" (CYP) is derived from the spectral absorbance maximum at 450nm when carbon monoxide binds to CYP in its reduced (ferrous, Fe2+) state. The basic reaction catalyzed by CYP is mono-oxygenation, that is the transfer of one oxygen atom from molecular oxygen to a substrate. The other oxygen atom is reduced to water during the reaction with the equivalents coming from the cofactor NADPH. The basic reaction is; RH (substrate) + O2 + NADPH + H+ = ROH (product) + H2O + NADP+ The end results of this reaction can be (N-)hydroxylation, epoxidation, heteroatom (N-, S-) oxygenation, heteroatom (N-, S-, O-) dealkylation, ester cleavage, isomerization, dehydrogenation, replacement by oxygen or even reduction under anaerobic conditions. The metabolites produced from these reactions can either be mere intermediates which have relatively little reactivity towards cellular sysytems and are readily conjugated, or, they can be disruptive to cellular systems. Indeed, inert compounds need to be prepared for conjugation and thus the formation of potentially reactive metabolites is in most cases unavoidable. There are 57 human CYPs (in 18 families and 42 subfamilies), mostly concentrated in the endoplasmic reticulum of liver cells although many tissues have them to some extent (Nelson DR et al, 2004). CYPs are grouped into 14 families according to their sequence similarity. Generally, enzymes in the same family share 40% sequence similarity and 55% within a subfamily. Nomenclature of P450s is as follows. CYP (to represent cytochrome P450 superfamily), followed by an arabic number for the family, a capital letter for the subfamily and finally a second arabic number to denote the isoenzyme. An example is CYP1A1 which is the first enzyme in subfamily A of cytochrome P450 family 1. The majority of the enzymes are present in the CYP1-4 families. CYP1-3 are primarily concerned with xenobiotic biotransformation whereas the other CYPs deal primarily with endogenous compounds. The CYP section is structured by the typical substrate they act upon. Of the 57 human CYPs, 7 encode mitochondrial enzymes, all involved in sterol biosynthesis. Of the remaining 50 microsomal enzymes, 20 act upon endogenous compounds, 15 on xenobiotics and 15 are the so-called "orphan enzymes" with no substrate identified. The P450 catalytic cycle (picture) shows the steps involved when a substrate binds to the enzyme. (1) The normal state of a P450 with the iron in its ferric [Fe3+] state. (2) The substrate binds to the enzyme. (3) The enzyme is reduced to the ferrous [Fe2+] state by the addition of an electron from NADPH cytochrome P450 reductase. The bound substrate facilitates this process. (4,5) Molecular oxygen binds and forms an Fe2+OOH complex with the addition of a proton and a second donation of an electron from either NADPH cytochrome P450 reductase or cytochrome b5. A second proton cleaves the Fe2+OOH complex to form water. (6) An unstable [FeO]3+ complex donates its oxygen to the substrate (7). The oxidised substrate is released and the enzyme returns to its initial state (1).
Trimethylamine (TMA) is present in the diet (in fish) but primarily formed in vivo from the breakdown of choline. It is N-oxidized by FMO3 in the liver, the major isoform active towards TMA Trimethylaminuria (âfish-odour syndromeâ) is a human genetic disorder characterized by an impaired ability to convert the malodourous TMA to its odourless N-oxide.
Methimazole is a drug used to treat hyperthyroidism, a condition arising when the thyroid gland is producing too much thyroid hormone. FMO2 is able to the S-oxidized form of methimazole.
Polyamine oxidases (PAOs), like MAOs, are also FAD-dependant and form aldehydes and hydrogen peroxide. PAOs are approximately 60KDa in size, are monomers and are located in peroxisomes. They act on endogenous polyamines as well as some xenobiotics. The polyamines of the spermine and spermidine families are important physiologically as they mediate cell function and growth and also play a role in programmed cell death. The balance between biosynthesis, degradation and uptake of these polyamines is strictly controlled in cells and the PAO system is one of a set of enzymes that maintains this regulation.
Flavin-containing monooxygenases (FMOs) are the second family of microsomal oxidative enzymes with broad and overlapping specificity. The major reactions FMOs catalyze are nucleophilic hetero-atom compounds such as nitrogen, sulfur or phosphorus as the hetero-atom to form N-oxides, S-oxides or P-oxides respectively. Despite the functional overlap with cytochrome P450s, the mechanism of action differs. FMOs bind and activate molecular oxygen before the substrate binds to the enzyme (picture). They also require flavin adenosine dinucleotide (FAD) as a cofactor. Unlike cytochrome P450 enzymes, FMOs are heat-labile, a useful way to distinguish which enzyme system is at work for researchers studying metabolism. Also, FMOs are not inducible by substrates, unlike the P450 enzymes.\n(1) NADPH binds to the enzyme and reduces the prosthetic group FAD to FADH2. NADP+ remains bound to the enzyme.\n(2) Incorporation of molecular oxygen to form a hydroperoxide.\n(3) A peroxide oxygen is transferred to the substrate.\n(4) Water is released.\n(5) NADP+ dissociates returning the enzyme to its initial state.\n\nTo date, there are 6 isozymes of FMO (FMO1-6) in humans, the most prominent and active one being FMO3. The FMO6 gene does not encode for a functional enzyme although it has the greatest sequence similarity with FMO3 (71%), whilst the others range from 50-58% sequence similarity with FMO3. FMO1-3 are the ones that exhibit activity towards nucleophiles, the others are insignificant in this respect.
Molecular chaperones as HSF1-specific transcriptional repressors
Human amine oxidases (AO) catalyze the oxidative deamination of biogenic amines (neurotransmitters such as serotonin, noradrenaline, the hormone adrenaline and polyamines such as the spermines) and xenobiotic amines (exogenous dietary tyramine and phenylethylamine). The basic reaction is the oxidative cleavage of the alpha-H to form an imine product with the concomitant reduction of a FAD cofactor. The imine product then hydrolyses to an aldehyde and ammonia (or amine for secondary and tertiary amine substrates). Reduced FAD is reoxidized to form hydrogen peroxide to complete the catalytic cycle. The reaction can be summarized as RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 The resultant hydrogen peroxide is the source of the most toxic free radical, the hydroxyl radical (.OH). This free radical is produced in the Fenton reaction with the use of ferrous (Fe2+) iron.
Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses
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Presentation of antigens by MHC class II molecules: getting the most out of them
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Arachidonic acid is metabolized via three major enzymatic pathways: cyclooxygenase, lipoxygenase, and cytochrome P450. The cytochrome P450 pathway metabolites are oxygenated metabolites of arachidonic acid.
The human gene SLC35D1 encodes the UDP-glucuronic acid transporter which transports both UDP-glucuronic acid (UDP-GlcA) and UDP-N-acetylgalactosamine (UDP-GalNAc) from the cytoplasm into the endoplasmic reticulum lumen (Muraoka et al. 2001).
UDP-glucose dehydrogenase (UGDH) catalyzes the conversion of UDP-glucose to UDP-glucuronic acid. The cytosolic enzyme is active as a hexamer and performs two successive oxidations to convert the 6'-hydroxyl of UDP-glucose to a carboxylate with concurrent reduction of 2 mol of NAD+ to NADH.
Phase 1 of metabolism is concerned with functionalization, that is the introduction or exposure of functional groups on the chemical structure of a compound. This provides a 'handle' for phase 2 conjugating species with which to react with. Many xenobiotics are lipophilic and almost chemically inert (e.g. PAHs) so would not necessarily undergo a phase 2 reaction. Making them more chemically reactive would facilitate their excretion but also increases their chance of reacting with cellular macromolecules (e.g. proteins, DNA). There is a fine balance between producing a more reactive metabolite and conjugation reactions. There are two groups of enzymes in phase 1 - oxidoreductases and hydrolases. Oxidoreductases introduce an oxygen atom into or remove electrons from their substrates. The major oxidoreductase enzyme system is called the P450 monooxygenases. Other systems include flavin-containing monooxygenases (FMO), cyclooxygenases (COX) and monoamine oxidases (MAO). Hydrolases hydrolyse esters, amides, epoxides and glucuronides.
Ethanol and related alcohols can be ingested as part of the diet and are formed by microorganisms in the intestinal tract. Ethanol oxidation to acetate occurs primarily in liver cells in a multistep process first described by Racker (1949). First, in the cytosol, ethanol is oxidized to acetaldehyde, with the formation of NADH. Second, in the mitochondrion, acetaldehyde is oxidized to acetate with the formation of NADH. Finally, acetate in the mitochondrion can be condensed with coenzyme A to form acetyl CoA. Polymorphisms in the enzymes catalyzing the first two steps are associated with variation in the efficiency of alcohol catabolism in human populations (Chen et al. 1999; Lange et al. 1976; Jornvall 1985). The molecular mechanism by which cytosolic acetaldehyde enters the mitochondrial matrix is not known (Lemasters 2007). Cytosolic enzymes capable of oxidizing acetaldehyde to acetate have also been identified and characterized in vitro (Inoue et al. 1979) so a purely cytosolic pathway for ethanol oxidation to acetate and conversion to acetyl-CoA can be annotated. The role of this pathway in vivo is unclear, though limited attempts to correlate deficiencies in the cytosolic enzyme with alcohol intolerance have yielded suggestive data (Yoshida et al. 1989). Additional peroxisomal and microsomal pathways for the oxidation of ethanol to acetaldehyde have been described; their physiological significance is unclear and they are not annotated here.
3,5,3'-Triiodothyronine (T3) 4-sulfate is a major metabolite of T3 in humans (LoPresti and Nicoloff 1994), and seven SULT enzymes, SULT1A1 (Li et al. 2001), 1A3 (Kester, Kaptein et al. 1999), 1B1 (Wang et al. 1998), 1C1 (Li et al. 2000), 1E1 (Li and Anderson 1999; Kester, van Dijk et al. 1999), 2A1 (Li and Anderson 1999), and 4A1 (Sakakibara et al. 2002) can catalyze this reaction in vitro or in tissue culture model systems. All of these enzymes except SULT4A1 also catalyze the sulfonation of 3,3'-diiodothyronine (T2).
Six SULT enzymes, SULT1A1 (Li et al. 2001), 1A3 (Kester, Kaptein et al. 1999), 1B1 (Wang et al. 1998), 1C1 (Li et al. 2000), 1E1 (Li and Anderson 1999; Kester, van Dijk et al. 1999), and 2A1 (Li and Anderson 1999), can catalyze the sulfonation of 3,3'-diiodothyronine (T2) in vitro or in tissue culture model systems. These six enzymes also catalyze the sulfonation of 3,5,3'-triiodothyronine (T3).
Glucuronidation conjugation utilizes UDP-glucuronosyltransferases (UGTs; EC 2.4.1.17) to catalyze a wide range of diverse endogenous and xenobiotic compounds. Glucuronidation is the major pathway in phase II metabolism and accounts for approximately 35% of drug conjugation. UGTs are microsomal membrane-bound and catalyze the transfer of a glucuronate group of uridine diphosphoglucuronate (UDPGA, a co-substrate) to the functional group of specific substrates. UDPGA is synthesized from glucose-1-phosphate (G1P). G1P is required for glycolysis and is present in high concentrations in the cell, making it is unlikely to be a limiting factor in UDPGA synthesis. UDP is added to G1P to form UDP-glucose which is then dehydrogenated to form UDPGA. The basic reaction is UDP-Glucuronate + acceptor -> UDP + acceptor-beta-D-glucuronide The effect of this conjugation is to confer polarity to the substrate which can then be easily excreted in urine or bile. Functional groups acted on include hydroxyl, carboxylate, amino and sulfate groups. There are 2 families of UGTs, UGT1 and UGT2 which are further sub-divided into 3 subfamilies, UGT1A, UGT2A and UGT2B. There are more than 26 different isozymes in humans, of which 18 are functional proteins. They are composed of 527-530 residues and have a molecular weight of 50-57KDa. The UGT1 family comprises of 9 proteins (UGT1A1, 1A3-1A10) but only 5 have been isolated in humans. Example substrates which are glucuronidated are acetaminophen by UGT1A6 and bilirubin by UGT1A1. Members of the UGT2 subfamily are each encoded by their own genes, in contrast to UGT1As which are encoded at the UGT1 locus. Example substrates are morphine conjugation by UGT2B7 and androgenic steroid conjugation by UGT2B17. Xenobiotics conjugated with glucuronic acid can be substrates for beta-glucuronidase, an enzyme common in gut microflora. This enzyme can release the parent or phase I metabolite which can be reabsorbed. It can then either re-exert it's original effects or be conjugated by glucuronic acid again. This cycle is called enterohepatic circulation and can delay the elimination of the xenobiotic.
Glucose 1-phosphate and UTP are the precursors to UDP-glucuronate formation. After oxidation of the resultant complex, UDP-glucuronate is transported to the ER lumen.
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ALDH2 (aldehyde dehydrogenase) in the mitochondrial matrix catalyzes the reaction of acetaldehyde and NAD+ to form acetate and NADH + H+ (Greenfield and Pietruszko 1977; Hempel et al. 1985). The active form of the enzyme is a tetramer (Ni et al. 1999).
Cytosolic ACSS2 (acetyl-coenzyme A synthetase) catalyzes the reaction of acetate, coenzyme A, and ATP to form acetyl-CoA, AMP, and pyrophosphate (Luong et al. 2000).
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Interactions between plexin-A2, plexin-A4, and semaphorin 6A control lamina-restricted projection of hippocampal mossy fibers
Physiological functions of the pentose phosphate pathway
Cytoplasmic domain mutations of the L1 cell adhesion molecule reduce L1-ankyrin interactions
Compartmentalization of aquaporins in the human intestine
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Activation of the FGF receptor underlies neurite outgrowth stimulated by L1, N-CAM, and N-cadherin
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Activation of the Ras signalling pathway in human breast cancer cells overexpressing erbB-2
PKC-beta controls I kappa B kinase lipid raft recruitment and activation in response to BCR signaling
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Structure-function relationships in dihydrolipoamide acyltransferases.
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Metabolic activation of carcinogenic heterocyclic aromatic amines by human liver and colon
Serotonin (5-HT) is a hormone and neurotransmitter used for regulatory purposes in animal CNS. In the human brain, serotonin is involved in many physiological functions such as sleep, pain, mood and is the precursor to melatonin, a hormone produced in the pineal gland.
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Catecholamines and thyroxine are synthesized from tyrosine, and serotonin and melatonin from tryptophan.
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Peroxisomal D-amino-acid oxidase catalyzes the reaction of glycine, water, and O2 to form glyoxylate, H2O2, and NH4+. The active form of the enzyme is a homodimer and has FAD as a cofactor (Kawazoe et al. 2006; Molla et al. 2006).
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Alanine-glyoxylate transaminase (AGXT) catalyzes the irreversible reaction of glyoxylate and alanine to form glycine and pyruvate (Danpure and Jennings 1988). The active form of the enzyme is a homodimer (Zhang et al. 2003) with one molecule of pyridoxal phosphate bound to each subunit (Coulter-Mackie et al. 2005). Mutations in this enzyme are associated with primary hyperoxaluria type I. Mutant alleles encode both catalytically inactive proteins and active ones that are mis-localized to mitochondria (Purdue et al. 1990; Takada et al. 1990).
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Mitochondrial AGXT2 (alanine-glyoxylate transaminase 2) catalyzes the irreversible reaction of glyoxylate and alanine to form glycine and pyruvate (Rodionov et al. 2010). The active form of the enzyme is inferred to be a homotetramer from the properties of the homologous rat protein, which has been purified and characterized in vitro (Tamaki et al.990). Most conversion of glyoxylate to glycine in vivo appears to occur in the peroxisome, catalyzed by AGXT, and the physiological role of the AGXT2 reaction is unclear.
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Peroxisomal GRHPR catalyzes the reaction of glyoxylate and NADPH + H+ to form glycolate and NADP+. The active form of the enzyme is a monomer (Rumsby and Cregeen 1999); mutations in it are associated with primary hyperoxaluria type II (Cramer et al. 1999).
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Thyroxine (T4) can be formed by the combination of two diiodotyrosines. The hormone thyrotropin can stimulate the production of T3 and T4.
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Thyroxine (3,5,3',5'-tetraiodothyronine, T4) promotes normal growth and development. It also regulates heat and energy production. T4 is released from the thyroid gland, the largest endocrine organ in the human body. The primary hormone released is T4 although T3 (3,5,3'-triiodothyronine) is also released in small quantities. Tyrosine residues in thyroglobulin (a glycoprotein scaffold containing many tyrosine residues) are iodinated to form mono- or diiodo-tyrosine which can then couple to form either T3 or T4.
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The first and rate limiting step in serotonin (5-HT) biosynthesis is catalyzed by tryptophan hydroxylase. The enzyme requires iron(II), tetrahydrobiopterin, and dioxygen cofactors for the hydroxylation of L-tryptophan to 5-hydroxytryptophan. Tryptophan hydroxylase belongs to a small family of monooxygenases that utilize tetrahydrobiopterins. Other members are phenylalanine hydroxylase and tyrosine hydroxylase (Fitzpatrick, PF, 1999; Walther et al, 2003).
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Aromatic L-amino acid decarboxylase (AADC) catalyzes the decarboxylation of both dopa and 5-hydroxytryptophan to dopamine and serotonin, respectively. AADC functions as a homodimer, utilizing pyridoxal phosphate as a cofactor.
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When SQR is in the oxidized state, it can bind hydrogen sulfide as persulfide to one of its own cysteine residue, the electrons being transferred to ubiquinone. After that the additional sulfur is dioxygenated by another enzyme (ETHE1). The activity of human SQR was deduced from the orthologue in Arenicola marina (Theissen et al. 2003, Hildebrandt & Grieshaber 2008).
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The sulfur dioxygenase ETHE1 converts persulfides to sulfite. Loss of this activity leads to the rare ethylmalonyl encephalopathy where the body can no longer detoxify H2S (Tiranti et al, 2009).
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The main reaction catalyzed by rhodanase is not the name-giving detoxification of cyanide to thiocyanate, but the transfer of a sulfur atom from SQR-S-SH onto sulfite yielding thiosulfate during sulfide oxidation. The activity of human rhodanase was inferred from the rat orthologue by Hildebrandt & Grieshaber, 2008.
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Sulfite oxidase oxidizes sulfite to sulfate which is among the most important macronutrients in cells and the fourth most abundant anion in human plasma (300 micromolar). The enzyme has a molybdenum-molybdopterin cofactor (MoCo) bound (Wilson et al. 2006, Feng et al. 2007).
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Oxidation of the thiol moiety of cysteine yields sulfinoalanine, which itself is processed to hypotaurine by an as of yet uncharacterized enzyme in humans . Whether further oxidation of hypotaurine to taurine needs an enzyme is unknown at present (Ye et al. 2007).
Cysteine sulfinic acid decarboxylase (CSAD) mediates the decarboxylase of 3-sulfinoalanine to produce hypotuarine. CSAD functions as a homodimer and requires pyridoxal phosphate as a cofactor. Purification, characterisation and activity of CSAD has been determined from rat liver (Guion-Rain et al. 1975).
Excess homocysteine will change the enzymatic activity of CBS such that other reactions than transsulfuration take place. In these reactions, oxobutanoate, lanthionine, and homolanthionine are produced by cystathionine gamma-lyase (CTH) (Chiku et al. 2009, Steegborn et al. 1999)
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alpha,beta-elimination activity of cystathionine-gamma-lyase (CTH) replaces the sulfur in cysteine with oxygen from water, resulting in serine and toxic hydrogen sulfide, which is further oxidized in mitochondria (Chiku et al. 2009, Steegborn et al. 1999).
Involvement of Rac/Cdc42/PAK pathway in cytoskeletal rearrangements
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A cytosolic, non-specific peptidase can hydrolyze cysteinylglycine to release cysteine and glycine (Tuefel et al, 2003).
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Transsulfuration is the interconversion of homocysteine and cysteine, and it fully takes place in bacteria and some plants and fungi. Animals however have only one direction of this bidirectional path, the synthesis of cysteine from homocysteine via cystathionine. Because excess cysteine is degraded to hydrogen sulfide, which is now known as a neuromodulator and smooth muscle relaxant, this pathway is also the main source of its production, which takes place in the cytosol, as well as in extracellular space (Dominy & Stipanuk 2004, Bearden et al. 2010).
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The first step in the formation of glutathione is the ligation of glutamate with cysteine, catalyzed by the dimeric protein glutamate-cysteine ligase (Gipp et al, 1995; Misra and Griffith, 1998).
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The first step of homocysteine conversion to cysteine is catalyzed by cystathionine beta-lyase, which adds a serine molecule to the substrate. The enzyme is a tetramer with two heme molecules as cofactor (Janosik et al. 2001).
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Cystathionine is cleaved to cysteine, oxobutanoate, and ammonia by the alpha,gamma-elimination activity of cystathionine gamma-lyase (CTH) (Chiku et al. 2009, Steegborn et al. 1999).
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S-adenosylmethionine (SAM) is an essential metabolite in all cells. SAM is a precursor in the synthesis of polyamines. Methionine adenosyltransferase (MAT; EC 2.5.1.6) catalyzes the only known SAM biosynthetic reaction from methionine and ATP. In mammalian tissues, three different forms of MAT (MAT I, MAT III and MAT II) have been identified that are the product of two different genes (MAT1A and MAT2A). A third gene MAT2B has been identified and is known to be a part of MAT II heterotetramer complex.
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At the beginning of this reaction, 1 molecule of 'S-adenosylhomocysteine', and 1 molecule of 'H2O' are present. At the end of this reaction, 1 molecule of 'adenosine', and 1 molecule of 'Homocysteine' are present. This reaction takes place in the 'cytosol' and is mediated by the 'adenosylhomocysteinase activity' of 'SAH hydrolase homotetramer'.
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Peroxisomal hydroxyacid oxidase 1 catalyzes the reaction of glyoxylate to form oxalate. The active form of the enzyme is associated with FMN and is a tetramer (Jones et al. 2000; Murray et al. 2008; Vignaud et al. 2007; Williams et al. 2000).
Glyoxylate is generated in the course of glycine and hydroxyproline catabolism and can be converted to oxalate. In humans, this process takes place in the liver. Defects in two enzymes of glyoxylate metabolism, alanine:glyoxylate aminotransferase (AGXT) and glycerate dehydrogenase/glyoxylate reductase (GRHPR), are associated with pathogenic overproduction of oxalate (Danpure 2005). The reactions that interconvert glycine, glycolate, and glyoxylate and convert glyoxylate to oxalate have been characterized in molecular detail in humans. A reaction sequence for the conversion of hydroxyproline to glyoxylate has been inferred from studies of partially purified extracts of rat and bovine liver but the enzymes involved in the corresponding human reactions have not been identified.
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Peroxisomal hydroxyacid oxidase 1 catalyzes the reaction of glycolate and O2 to form glyoxylate and H2O2. The active form of the enzyme is associated with FMN and is a tetramer (Jones et al. 2000; Murray et al. 2008; Vignaud et al. 2007; Williams et al. 2000).
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CD46 plays a key role in tailoring innate immune recognition of apoptotic and necrotic cells
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Complementation analysis in PtdInsP kinase-deficient yeast mutants demonstrates that Schizosaccharomyces pombe and murine Fab1p homologues are phosphatidylinositol 3-phosphate 5-kinases
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Glutathione metabolism and its selective modification
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An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing
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Association of alternative complement pathway components with human blood platelets: secretion and localization of factor D and beta 1H Globulin
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Four transporters mediate GABA uptake in the brain, GAT1-3 and BGT1. They terminates the action of GABA by high affinity sodium-dependent reuptake into presynaptic terminals. Transport of GABA by GAT1-3 is proposed to be accompanied by 2Na+ ions and 1 Cl- ion (Loo DD et al, 2000). SLC6A1 encodes a sodium- and chloride-dependent GABA transporter 1, GAT1, which is the predominant GABA transporter in brain. It is widely distributed in the brain and co-localized to GABAergic neurons (Nelson H et al, 1990). SLC6A13 encodes a sodium- and chloride-dependent GABA transporter 2, GAT2, which is localized to GABAergic neurons in the brain. It is also found in retina, liver and kidney (Christiansen B et al, 2007). SLC6A11 encodes a sodium- and chloride-dependent GABA transporter 3, GAT3. It is expressed in the brain and localizes to GABAergic neurons (Borden LA et al, 1994).
Reuptake of GABA from the synapse terminates the action of GABA thus regulating GABA action. GABA taken up from the synapse into the neurons is reused for synaptic loading. GABA taken up by astrocytes is degraded into C02 and glutamine. Glutamine is transported into the neurons for glutamate and GABA synthesis.
Succinate semialdehyde dehydrogenase (SSADH) converts succinate semialdehyde, in a final step of GABA degradation, into succinate. SSADH uses one water molecule and one molecule of NAD+ per molecule of succinyate semialdehyde.
GABA is converted to succinate semialdehyde by 4-aminobutyrate aminotransferase
GABA is a major inhibitory neurotransmitter in the mammalian central nervous system. GABA modulates neuronal excitability throughout the nervous system. Disruption of GABA neurotransmission leads to many neurological diseases including epilepsy and a general anxiety disorder. GABA is synthesized by two distinct enzymes GAD67 and GAD65 that differ in their cellular localization, functional properties and co-factor requirements. GABA synthesized by GAD65 is used for neurotransmission whereas GABA synthesized by GAD67 is used for processes other than neurotransmission such as synaptogenesis and protection against neuronal injury. GABA is loaded into synaptic vesicle with the help of vesicular inhibitory amino acid transporter or VGAT. GAD65 and VGAT are functionally linked at the synaptic vesicle membrane and GABA synthesized by GAD65 is preferentially loaded into the synaptic vesicle over GABA synthesized in cytoplasm by GAD67.The GABA loaded synaptic vesicles are docked at the plasma membrane with the help of the SNARE complexes and primed by interplay between various proteins including Munc18, complexin etc. Release of GABA loaded synaptic vesicle is initiated by the arrival of action potential at the presynaptic bouton and opening of N or P/Q voltage gated Ca2+ channels. Ca2+ influx results in Ca2+ binding by synaptobrevin, which is a part of the SNARE complex that also includes SNAP25 and syntaxin, leading to synaptic vesicle fusion. Release of GABA in the synaptic cleft leads to binding of GABA by the GABA receptors and post ligand binding events.
GABA is metabolized to succinated by the serial action of two enzymes, 4-aminobutyrate aminotransferase and suucinate semialdehyde dehydrogenase.
5-hydroxyindole acetaldehyde is then catalyzed by aldehyde dehydrogenase to form 5-hydroxyindole acetic acid
Neurotransmitter is stored in the synaptic vesicle in the pre-synaptic terminal prior to its release in the synaptic cleft upon depolarization of the pre-synaptic membrane. The release of the neurotransmitter is a multi-step process that is controlled by electrical signals passing through the axons in form of action potential. Neurotransmitters include glutamate, acetylcholine, nor-epinephrine, dopamine and seratonin. Each of the neurotransmitter cycle is independently described.
Serotonergic neurotransmission affects a wide range of behaviors, from food intake and reproductive activity, to sensory processing and motor activity, to cognition and emotion. One such key regulator is the serotonin transporter (5-HTT), which is observed to remove serotonin released into the synaptic cleft.
Serotonin is first metabolized to 5-hydroxyindole acetaldehyde by monoamine oxidase. 5-hydroxyindole acetaldehyde is then catalyzed by aldehyde dehydrogenase to form 5-hydroxyindole acetic acid.
Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration
Excess L-Glutamate released by the pre-synaptic neuron in the synaptic cleft is cleared by high affinity transporters called the excitatory amino acid transporters (EAATs) to terminate synaptic actions of the neurotransmitter and to recycle these molecules. Five types of EAATs have been identified EAAT1-EAAT5 in the mammalian CNS. EAAT1 and EAAT2 are mainly expressed by astrocytes whereas EAAT3 and EAAT4 are predominantly neuronal. EAAT3 are expressed throughout the CNS however, EAAT4 is predominantly localized to purkinje cells. EAAT5 are expressed rod photoreceptor and bipolar cells of retina. Astrocytic EAATs are expressed in astrocytes in close apposition to the synapses and neuronal EAATs are expressed in the extra-synaptic or peri-synaptic locations on the neurons. Astrocytic EAATs are responsible for majority of the glutamate uptake, neuronal transporters are responsible for glutamate clearance in specialized synapses in cerebellum where the spatial relationship between the glutamate receptors and EAATs is altered and glutamate receptors are expressed in the peri-synaptic region.
In astrocytic glutamate-glutamine cycle, the excess glutamate released by the pre-synaptic neuron in the synaptic cleft is transported into the astrocyte by a family glutamate transporters called the excitatory amino acid transporters 1 and 2, EAAT1 and EAAT2. Astrocytes carrying these transporters exist in close apposition to the synapse to clear excess glutamate to prevent excessive activation of neurons and hence neuronal death. Glutamate in astrocytes is converted to glutamine by glutamine synthetase. Glutamine is then transported into the extracellular space by system N transporters. The glutamate in the extracellular space is available for neuronal uptake.
Neurotransmitter released in the synaptic cleft binds to specific receptors on the post-synaptic cell and the excess of the neurotransmitter is cleared to prevent over activation of the post-synaptic cell. The neurotransmitter is cleared by either re-uptake by the pre-synaptic neuron, diffusion in the perisynaptic area, uptake by astrocytes surrounding the synaptic cleft or enzymatic degradation of the neurotransmitter. This topic will be annotated in a future release.
Deciphering the role of malin in the lafora progressive myoclonus epilepsy
Nicotinic acetylcholine receptors exhibit high influx of Ca2+, the degree of Ca2+ permeability is dependent on the subunit composition; homomeric acetylcholine receptors containing aplha 7 subunits allow maximum Ca2+ influx followed by receptors containing alpha3 beta2 alpha5 or alpha3 beta4 alpha5.
Nicotinic acetylcholine receptors are activated upon ligand binding which opens the acetylcholine channels and permits Ca2+ and Na+ ion influx depending on the subunit composition and stoichiometry of the subunits. The ratio of Ca2+ to Na+ ion influx varies making the receptors either highly Na+ permeable or Ca2+ permeable.
Nicotinic acetylcholine receptors bind two molecules of ligand, acetylcholine, in the alpha beta interface in receptors containing heteromeric subunits or in the interface of 2 aplha subunits in receptors containing homomeric subunits.
Neuotransmitter uptake by astrocytes is mediated by specific transporter located on the astrocytic membrane. The imported neurotransmitter in the astrocytes is metabolized and transported back to the neuron via specialized transporters.
Nicotinic acetylcholne receptors that have low Ca2+ permeability allow the influx of Na+ which causes depolarization of the membrane initiating voltage dependent responses such as activation of voltage dependent opening of Ca2+ channels and thus eliciting an increase in Ca2+ and downstream signaling. These receptors could be found in both presynaptic and postsynaptic terminals.
Nicotinic acetylcholine receptors containing aplha4(2) beta2 (3) and alpha3(2) beta4(3) are selectively highly Na+ permeable upon activation of these receptors by acetylcholine.
Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase.
STIM1 carboxyl-terminus activates native SOC, I(crac) and TRPC1 channels
The cAMP signalling pathway activates CREB through PKA, p38 and MSK1 in NIH 3T3 cells
Serotonin is synthesized in the serotonergic neurons in the central nervous system and the enterochrommaffin cells of the gastroinetstinal system. Serotonin is loaded into the clathrin sculpted monoamine transport vesicles. The vesicles are docked, primed and release after the change in the membrane potential that activates voltage gated calcium channels and the reponse by several proetins to the changes in intracellular Ca2+ increase leads to fusion of the vesicle and release of serotonin into the synapse.
Serotonin is loaded into the clathrin sculpted monoamine transport vesicle by vesicular monoamine transporter.
Noradrenaline is cleared from the synaptic cleft by Noaradrenaline uptake transporter. This reaction is carried out by neurons as well as astrocytes.
Dopamine is transported from the cytosol into the reacidified clathrin sculpted monoamine transport vesicle by membranous vesicular monoamine transporter
Noradrenalin release cycle consists of reacidification of the empty clathrin sculpted monoamine transport vesicle, loading of dopamine into reacidified clathrin coated monamine transport vesicle, conversion of dopamine into Noradrenalin, docking and priming of the noradrenalin synaptic veiscle and then release of noradrenalin synaptic vesicle. In the peripheral nervous system in the peripheral nervous system noradrenalin is stored in large and small dense vesicles and is realesed from large vesicles.
Arginine methylation is a common post-translational modification; around 2% of arginine residues are methylated in rat liver nuclei (Boffa et al. 1977). Arginine can be methylated in 3 different ways: monomethylarginine (MMA); NG,NG-asymmetric dimethylarginine (ADMA) and NG,N'G-symmetric dimethylarginine (SDMA). The formation of MMA, ADMA and SDMA in mammalian cells is carried out by members of a family of nine protein arginine methyltransferases (PRMTs) (Bedford & Clarke 2009). Type I, II and III PRMTs generate MMA on one of the two terminal guanidino nitrogen atoms. Subsequent generation of asymmetric dimethylarginine (ADMA) is catalysed by the type I enzymes PRMT1, PRMT2, PRMT3, co-activator-associated arginine methyltransferase 1 (CARM1), PRMT6 and PRMT8. Production of symmetric dimethylarginine (SDMA) is catalysed by the type II enzymes PRMT5 and PRMT7. On certain substrates, PRMT7 also functions as a type III enzyme, generating MMA only. PRMT9 activity has not been characterized. No known enzyme is capable of both ADMA and SDMA modifications. Arginine methylation is regarded as highly stable; no arginine demethylases are known (Yang & Bedford 2013). Most PRMTs methylate glycine- and arginine-rich (GAR) motifs in their substrates (Boffa et al. 1977). CARM1 methylates a proline-, glycine- and methionine-rich (PGM) motif (Cheng et al. 2007). PRMT5 can dimethylate arginine residues in GAR and PGM motifs (Cheng et al. 2007, Branscombe et al. 2001). PRMTs are widely expressed and are constitutively active as purified recombinant proteins. However, PRMT activity can be regulated through PTMs, association with regulatory proteins, subcellular compartmentalization and factors that affect enzyme-substrate interactions. The target sites of PRMTs are influenced by the presence of other PTMs on their substrates. The best characterized examples of this are for histones. Histone H3 lysine-18 acetylation (H3K18ac) primes the histone tail for asymmetric dimethylation at arginine-17 (H3R17me2a) by CARM1 (An et al. 2003, Daujat et al. 2002, Yue et al. 2007). H3K9ac blocks H3R8 symmetric dimethylation (H3R8me2s) by PRMT5 (Pal et al. 2004). H4R3me2a catalyzed by PRMT1 favours subsequent acetylation of the histone H4tail (Huang et al. 2005). At the same time histone H4 lysine-5 acetylation (H4K5ac) makes the H4R3 motif a better substrate for PRMT5 compared with PRMT1, thereby moving the balance from an activating ADMA mark to a suppressive SDMA mark at the H4R3 motif26 (Feng et al. 2011). Finally methylation of Histone H3 on arginine-2 (H3R2me2a) by PRMT6 blocks methylation by the MLL complex (H3K4me3), and vice versa, methylation of H3K4me3 prevents H3R2me2a methylation (Guccione et al. 2007, Kirmizis et al. 2007, Hyllus et al. 2007).
Symmetric dimethylation of histone H3 arginine-3 (H3R2) enhances binding of WDR5, a component of the coactivator complexes MLL, SET1A, SET1B, NLS1 and ATAC (Migliori et al. 2012).
Chromatin organization refers to the composition and conformation of complexes between DNA, protein and RNA. It is determined by processes that result in the specification, formation or maintenance of the physical structure of eukaryotic chromatin. These processes include histone modification, DNA modification, and transcription. The modifications are bound by specific proteins that alter the conformation of chromatin.
Eukaryotic DNA is associated with histone proteins and organized into a complex nucleoprotein structure called chromatin. This structure decreases the accessibility of DNA but also helps to protect it from damage. Access to DNA is achieved by highly regulated local chromatin decondensation. The 'building block' of chromatin is the nucleosome. This contains ~150 bp of DNA wrapped around a histone octamer which consists of two each of the core histones H2A, H2B, H3 and H4 in a 1.65 left-handed superhelical turn (Luger et al. 1997, Andrews & Luger 2011). Most organisms have multiple genes encoding the major histone proteins. The replication-dependent genes for the five histone proteins are clustered together in the genome in all metazoans. Human replication-dependent histones occur in a large cluster on chromosome 6 termed HIST1, a smaller cluster HIST2 on chromosome 1q21, and a third small cluster HIST3 on chromosome 1q42 (Marzluff et al. 2002). Histone genes are named systematically according to their cluster and location within the cluster. The 'major' histone genes are expressed primarily during the S phase of the cell cycle and code for the bulk of cellular histones. Histone variants are usually present as single-copy genes that are not restricted in their expression to S phase, contain introns and are often polyadenylated (Old & Woodland 1984 ). Some variants have significant differences in primary sequence and distinct biophysical characteristics that are thought to alter the properties of nucleosomes. Others localize to specific regions of the genome. Some variants can exchange with pre-existing major histones during development and differentiation, referred to as replacement histones (Kamakaka & Biggins 2005). These variants can become the predominant species in differentiated cells (Pina & Suau 1987, Wunsch et al. 1991). Histone variants may have specialized functions in regulating chromatin dynamics. The H2A histone family has the highest sequence divergence and largest number of variants. H2A.Z and H2A.XH2A are considered 'universal variants', found in almost all organisms (Talbert & Henikoff 2010). Variants differ mostly in the C-terminus, including the docking domain, implicated in interactions with the (H3-H4)x2 tetramer within the nucleosome, and in the L1 loop, which is the interaction interface of H2A-H2B dimers (Bonisch & Hake 2012). Canonical H2A proteins are expresssed almost exclusively during S-phase. There are several nearly identical variants (Marzluff et al. 2002). No functional specialization of these canonical H2A isoforms has been demonstrated (Bonisch & Hake 2012). Reversible histone modifications such as acetylation and methylation regulate transcription from genomic DNA, defining the 'readability' of genes in specific tissues (Kouzarides 2007, Marmorstein & Trievel 2009, Butler et al. 2012).
Nascent synaptic vesicles are loaded with glutamate by VGLUT1 to form glutamate containing synaptic vesicles. This process occurs while the synaptic vesicle is in the cytosol.
Beta-catenin directly displaces Groucho/TLE repressors from Tcf/Lef in Wnt-mediated transcription activation
GABA is loaded into the synaptic vesicle by inihibitory amino acid transport, VIAAT or VGAT.
GABA synthesized uniquely by two forms of glutamate decarboxylases, GAD65 and GAD67, that are functionally distinct and have different co-factor requirements. GAD65 is functionally linked to VGAT, the GABA transporter and selectively GABA synthesized by GAD65 is preferably loaded into the synaptic vesicles. GABA synthesized by GAD67 may be used for functions other than nuerotransmission.
GAD65 or GAD2 is concentrated in the nerve terminal region in the neurons and is involved in the synthesis of GABA which is used as a neurotransmitter.
GAD1 or GAD67 is evenly spread throghout the neuronal cytoplasm and is invoved in GABA synthesis that is used for synaptogenesis, in protection against neural injury and as energy source through GABA shunt.
Acetylcholine neurotransmitter release cycle involves syntheis of choline, loading of clathrin scultpted synaptic vesicles, docking and priming of the acetyl choline loaded synaptic vesicles and then release of acetylcholine. This cycle occurs in neurons of central nervous system (CNS), peripheral, autonomic and somatic nervous system. In the CNS, the acetylcholine is released by the presynaptic neurons into the synaptic cleft where the released acetylcholine is accessible to acetylcholine receptors located on the postsynaptic neurons.
Choline transporter symports Na ion and Choline from the extracellular region into the cytosol. The choline transporters are located in the nerve terminals of cholinergic neurons.
Dopamine neurotransmitter cycle occurs in dopaminergic neurons. Dopamine is synthesized and loaded into the clathrin sculpted monoamine transport vesicles. The vesicles are docked, primed and fused with the plasmamembrane in the synapse to release dopamine into the synaptic cleft.
Communication at the synapse involves the release of glutamate from the presynaptic neuron and its binding to glutamate receptors on the postsynaptic cell to generate a series of events that lead to propagation of the synaptic transmission. This process begins with the formation of synaptic vesicles in the presynaptic neuron, proceeds to the loading of glutamate into the vesicles, and concludes with the release of glutamate into the synaptic cleft. The glutamate life cycle in the neuron begins with the loading of the nascent synaptic vesicles with cytosolic glutamate with the help the transporter protein, VGLUT1, located in the synaptic vesicular membrane. Glutamate loaded vesicles are formed in the cytoplasm and then transported to a site close to the plasma membrane where the vesicle is docked with the help of several proteins. One of the key players in the docking process in Munc 18, which interacts with syntaxin (in the plasma membrane), MINT (Munc18 interacting molecule), and DOC2. These interactions along with the secondary interactions are needed for docking the synaptic vesicle to the plasma membrane. The docked synaptic vesicle is not ready for release until it undergoes molecular changes to prime it for fusion with the plasma membrane. Munc13 is one of the main players in the priming process. Munc 13 interacts with RIM (Rab3A interacting molecule) located in the synaptic vesicle. Munc 13 also interacts with DOC2. The precise molecular mechanisms of the interactions that result in docking versus priming are not clear and the docking and priming process have been combined in this annotation of this pathway. Once primed the synaptic vesicle is ready for release. Synaptic transmission involves an action potential that is generated in the presynaptic cell which induces the opening of voltage gated Ca2+ channels (VGCC) located in the plasma membrane of the presynaptic neuron. Typically N, P/Q and R type of VGCCs are involved in the neurotransmitter release. Ca2+ influx through these channels results in the rise of intracellular Ca2+ concentration. In the microdomain of glutamatergic synapses, the Ca2+ concentration could rise between 10-25 micro molar. Synaptotagmin, a Ca2+-binding protein located in the synaptic vesicular membrane, responds to the rise in the Ca2+ levels in the microdomain and induces a synaptic vesicle membrane curvature that favors vesicle fusion. Fusion of the synaptic vesicle with the plasma membrane is characterized by the formation of a trimeric trans-SNARE complex that involves VAMP2 from the synaptic vesicle membrane, and syntaxin and SNAP-25 from plasma membrane. Vesicle fusion incorporates the synaptic vesicle membrane into the plasma membrane, releasing the vesicle contents (glutamate) into the synaptic cleft. Postfusion the synaptic vesicle membrane proteins (VAMP2, Rab3A, VGLUT1, and synaptotagmin) are also found in the plasma membrane.
Prolactin-derived amyloid in the aging pituitary gland
Protease-activated receptors in hemostasis, thrombosis and vascular biology
Presynaptic terminal acetylcholine receptors are located at or near nerve terminal and modulate the release of neurotransmitter such as glutamate, noradrenaline and dopamine. Activation of presynaptic acetylcholine receptors leads to influx of Ca2+ and sufficient increase in local Ca2+ concentrations which could be due to either direct or indirect Ca2+ entry. Direct Ca2+ entry through acetylcholine receptors containing alpha3 beta4 receptors is sufficient for the release of noradrenaline in hippocampus. Indirect Ca2+ increase could be due to Na+ dependent depolarization and activation of voltage dependent calcium channels (VDCC) as in the case of dopamine release. Local Ca2+ increase could also be due to an initial Ca2+ influx through acetlycholine homomeric receptors containing alpha7 subunits and further increase in Ca2+ is elicited due to Ca2+ induced Ca2+ release (CICR) that involves the ryanodine receptors in the ER and the IP3 receptors. This mechanism is used in hippocampal mossyfibre pathway. Nicotinic acetylcholine receptors may permit both sodium and calcium ions, however, the ratio of sodium and calcium influx makes these receptors either highly sodium permeable or highly calcium permeable.
Postsynaptic acetylcholine receptors mediate Ca2+ currents that may be involved in the facilitation of long term potentiation (LTP).
Acetylcholine binding activates postsynaptic acetylchloine receptors that show Ca2+ currents which facilitate the process of long term potentiation (LTP).
Each AMPA receptor subunit binds one glutamate molecule in the ligand binding site in the N terminus. Each receptor is capable of binding four glutamate molecule, however, channel opens when two sites are occupied by the ligand and the current increases with increased ligand binding. Ca permeable AMPA receptors containing homomers of GluR1 or heteromers containing GluR1, GluR3 and GluR4 conduct Ca upon glutamate or agonist namely AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) binding. Calcium permeable AMPA receptors conduct Ca and other cations such as Na. The inonic flux leads to Ca or Na currents that leads to either increase in the intracellular Ca concentration leading to further Ca-dependent signaling or increase in depolarization that opens voltage gated channels such as NMDA receptors that require both membrane depolarization and glutamate binding for activation.
Nicotinic acetylcholine receptors are found in the postsynaptic terminals and these receptors are responsible in mediating postsynaptic currents. Most common types of postsynaptic nicotinic acetylcholine receptors are homomeric alpha 7 containing acetylcholine receptors. The densities of acetylcholine receptors are found to be similar to NMDA and AMPA receptors at these sites. Nicotinic acetylcholine receptors may permit both sodium and calcium ions, however, the ratio of sodium and calcium influx makes the receptors either highly sodium permeable or highly calcium permeable.
Nicotinic acetylcholine receptors (nAchR) are a subtype of acetylcholine receptors that are activated by nicotine and allow the influx of monovalent (sodium) and divalent cations(calcium), however, the permeability of sodium and/or calcium maybe high or low depending on the subunit composition of the receptor. Nicotinic acetylcholine receptors are expressed widely in the central and peripheral nervous system in the presynaptic terminal, terminal bouton and post-synaptic neuron. Functionally nicotinic acetylcholine receptors in the pre-synaptic and postsynaptic terminals behave similarly. Nicotinic AChR are a family of acetylcholine gated pentameric receptors that are formed by the association of various combinations of mostly alpha, beta subunits and sometimes gamma delta, episilon subunits. In addition, receptors may be more diverse due the fact that some receptor have same subunits but the stoichiometry of the subunits is different.
Nucleotide sequence for a cDNA encoding the alpha subunit of retinal transducin (GNAT1) isolated from the human eye
AMPA receptors bind glutamate, released in the synaptic cleft by the presynaptic cell, in the ligand binding region in the N terminal domain.
GPVI and integrin alphaIIb beta3 signaling in platelets
Assembly of high order G alpha q-effector complexes with RGS proteins
Use of chromatin immunoprecipitation to clone novel E2F target promoters
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Step-size analyses of the mitochondrial Hsp70 import motor reveal the Brownian ratchet in operation
Biosynthesis of thyroid hormone: basic and clinical aspects
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LDL-receptor-related protein 6 is a receptor for Dickkopf proteins
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Temporal and spatial distribution of activated Pak1 in fibroblasts
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Hyaluronan: from extracellular glue to pericellular cue
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Insulin degradation: mechanisms, products, and significance.
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Cytochrome P450s and cholesterol homeostasis
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The band 3 anion exchange protein (AE1, SLC4A1) exchanges chloride (Cl-) for bicarbonate (HCO3-) across the plasma membrane according to the concentration gradients of the anions (Knauf et al. 1996, Dahl et al. 2003). SLC4A1 may be part of a complex ("metabolon") with carbonic anhydrase II (CA2) which would facilitate the transport of HCO3- (Sterling et al. 2001).
Carbonic anhydrase I (CA1, Khalifah 1971, Pesando 1975, Simonsson et al. 1982, Ren & Lindskog 1992) and carbonic anhydrase II (CA2, Tibell et al. 1984, Jones & Shaw 1983, Ghannam et al. 1986) hydrate carbon dioxide (CO2) to yield bicarbonate (HCO3-) and a proton (H+). During the reaction a hydroxyl group bound by the zinc ion (Zn2+) attacks the CO2 molecule in the active site to directly form HCO3- (reviewed in Lindskog 1997). The HCO3- is displaced by water, which is then deprotonated by a histidine residue to recreate the Zn2+:hydroxyl group. Depending on the concentrations of reactants the reaction is reversible.
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Carbon dioxide (CO2) in plasma is hydrated to yield protons (H+) and bicarbonate (HCO3-) by carbonic anhydrase IV (CA4) located on the apical plasma membranes of endothelial cells. Plasma CO2 is also taken up by erythrocytes via AQP1 and RhAG. Within erythrocytes CA1 and, predominantly, CA2 hydrate CO2 to HCO3- and protons (reviewed in Geers & Gros 2000, Jensen 2004, Boron 2010). The HCO3- is transferred out of the erythrocyte by the band 3 anion exchange protein (AE1, SLC4A1) which cotransports a chloride ion (Cl-) into the erythrocyte. Also within the erythrocyte, CO2 combines with the N-terminal alpha amino groups of HbA to form carbamates while protons bind histidine residues in HbA. The net result is the Bohr effect, a conformational change in HbA that reduces its affinity for O2 and hence assists the delivery of O2 to tissues.
Iron-sulfur clusters are assembled on the scaffold, ISCU. Based on homology with bacterial IscU:IscS complexes (reviewed in Johnson et al. 2005), one molecule of ISCU is bound to each subunit of a NFS1 dimer (Marinoni et al. 2012). A single complex may thus be capable of assembling two 2Fe-2S clusters. Sulfide is provided by desulfuration of cysteine by NFS1:ISD11 (Biederbick et al. 2006, Shi et al. 2009, Tsai and Barondeau 2010). It has been proposed that ferrous iron is delivered by FXN (Gerber et al. 2003, Yoon and Cowan 2003, Schmucker et al. 2011) bound to ISCU (inferred from yeast, Wang and Craig 2008), although more recent studies suggested that FXN functions as an allosteric effector to stimulate sulfide transfer (Tsai et al. 2010). Holo-ISCU (ISCU bound to a newly synthesized 2Fe-2S cluster) transiently interacts with a dedicated HSP70 chaperone system including Mortalin (GRP75) and HSP20 and GLRX5 (GRX5). Electrons supplied by FDXL1 (FDX2) are required and may reduce the sulfur from S0 to S2-. NFU1 binds an Fe-S cluster (Tong et al. 2003, inferred from bacteria Yuvaniyama et al. 2000) and, from biochemical studies of bacterial NFU1 homologues, is proposed to be an intermediate Fe-S cluster carrier (Bandyopadhy et al. 2008). Mutations in human NFU1 affect only a subset of Fe-S proteins (Navarro-Sastre et al. 2011).
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NADPH, ferredoxin reductase (FDXR, Adrenodoxin reductase), and ferredoxins (FDX1, FDX1L) comprise a short electron transport chain that provides electrons for biosynthesis of iron-sulfur clusters and steroid hormones (Sheftel et al. 2010, Shi et al. 2012, reviewed in Grinberg et al. 2000, Lambeth et al. 1982).
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Carbonic anhydrase IV (CA4) anchored to extracellular face of the plasma membrane (Wistrand et al. 1999) hydrates carbon dioxide (CO2) to yield bicarbonate (HCO3-) and a proton (H+) (Zhu & Sly 1990, Okayuma et al. 1992, Baird et al. 1997, Innocenti et al. 2004). During the reaction a hydroxyl group bound by the zinc ion (Zn2+) of CA4 attacks the CO2 molecule to directly form HCO3- (reviewed in Lindskog 1997). The HCO3- is displaced by water, which is then deprotonated by a histidine residue to recreate the Zn2+:hydroxyl group. Depending on the concentrations of reactants the reaction is reversible.
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Iron-sulfur (Fe-S) proteins are localized in the cytosol, nucleus, and mitochondria of mammalian cells (reviewed in Stemmler et al. 2010, Rouault 2012, Bandyopadhyay et al. 2008, Lill 2009, Lill et al. 2012). Fe-S protein biogenesis in the mitochondrial matrix involves the iron-sulfur cluster (ISC) assembly machinery. Ferrous iron is transported across the inner mitochondrial membrane into the mitochondrial matrix by Mitoferrin-1 (SLC25A37) and Mitoferrin-2 (SLC25A28). (Mitoferrin-1 is enriched in erythroid cells while Mitoferrin-2 is ubiquitous.) Frataxin binds ferrous iron in the mitochondrial matrix. The cysteine desulfurase NFS1 in a subcomplex with ISD11 provides the sulfur by converting cyteine into alanine and forming a persulfide which is used for cluster formation on ISCU, the scaffold protein. Interaction between NFS1 and ISD11 is necessary for desulfurase activity. Frataxin binds to a complex containing NFS1, ISD11, and ISCU and is proposed to function as an iron donor to ISCU or as an allosteric switch that activates sulfur transfer and Fe-S cluster assembly (Tsai and Barondeau 2010). Cluster formation also involves the electron transfer chain ferredoxin reductase and ferredoxin. ISCU initially forms clusters containing 2 iron atoms and 2 sulfur atoms ([2Fe-2S] clusters). They are released by the function of HSP70-HSC20 chaperones and the monothiol glutaredoxin GLRX5 and used for assembly of [2Fe-2S] proteins. Assembly of larger clusters such as [4Fe-4S] clusters may involve the function of ISCA1, ISCA2, and IBA57. The clusters are transferred to apo-enzymes such as the respiratory complexes, aconitase, and lipoate synthase through dedicated targeting factors such as IND1, NFU1, and BOLA3.
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Frataxin (FXN) specifically binds 2 atoms of ferrous iron per monomer (reviewed in Stemmler et al. 2010). Iron bound to Frataxin may (Yoon and Cowan 2003, Gerber et al. 2003) or may not (Schmucker et al. 2011) enhance the interaction of Frataxin with NFS1, ICSU, and ISD11. Frataxin was shown to stimulate the cysteine desulfurase activity of NFS1 and was proposed to be a regulator of sulfur production (Tsai et al. 2010). The formation of sulfide by NFS1 is most efficiently observed when NFS1 is in complex with ISD11, ISCU, and FXN in the presence of cysteine and iron. This means that only the complete system of NFS1, ISD11, ISCU, FXN, cysteine, and iron is fully active as a desulfurase. FXN therefore seems to be a regulator of the cysteine desulfurase permitting sulfide production only when all components needed for Fe-S cluster synthesis are present and the ISCU-bound Fe-S cluster can be formed.
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Two electrons are transferred from reduced ferredoxin reductase (FDXR, adrenodoxin reductase) to two ferredoxin-1 or ferredoxin-1L (FDX1, FDX1L) molecules, each of which binds one electron. Two protons are released during the reaction.
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Two electrons and one proton are transferred from NADPH to the FAD moiety of ferredoxin reductase. A proton from the medium is also taken up by ferredoxin reductase.
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Evolutionary conservation and adaptation in the mechanism that regulates SREBP action: what a long, strange tRIP it's been
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Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas
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LKB1 is the upstream kinase in the AMP-activated protein kinase cascade
All characterized lysine demethylases other than KDM1A belong to the jumonjiC domain (JmjC) containing family.The JmjC KDMs are members of the Cupin superfamily of mononuclear Fe (II) dependent oxygenases, which are characterized by the presence of a double-stranded beta-helix core fold. The JmjC KDMs require 2 oxoglutarate (2 OG) and molecular oxygen as co substrates, producing, along with formaldehyde, succinate and carbon dioxide. This hydroxylation based mechanism does not require a protonatable lysine epsilon-amine group and consequently JmjC containing demethylases are able to demethylate tri , di and monomethylated lysines. KDM5A-D (JARID1A-D) catalyse the demethylation of di- or tri-methylated lysine-5 of histone H3 (H3K4Me2/3) (Christensen et al. 2007, Klose et al. 2007, Lee et al. 2007, Secombe et al. 2007, Seward et al. 2007, Iwase et al. 2007).
All characterized lysine demethylases other than KDM1A belong to the jumonjiC domain (JmjC) containing family.The JmjC KDMs are members of the Cupin superfamily of mononuclear Fe (II) dependent oxygenases, which are characterized by the presence of a double-stranded beta-helix core fold. The JmjC KDMs require 2 oxoglutarate (2 OG) and molecular oxygen as co substrates, producing, along with formaldehyde, succinate and carbon dioxide. This hydroxylation based mechanism does not require a protonatable lysine e amine group and consequently JmjC containing demethylases are able to demethylate tri , di and monomethylated lysines. KDM6A (UTX), KDM6B (JMJD3) and KDM7A (JHDM1D) catalyse the demethylation of di or tri-methylated lysine-28 of histone H3 (H3K27Me2/3) (Agger et al. 2007, Cho et al. 2007, De Santra et al. 2007, Hong et al. 2007, Lan et al. 2007, Lee et al. 2007, Horton et al. 2010, Huang et al. 2010).
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Histone lysine demethylases (KDMs) are able to reverse N-methylations of histones and probably other proteins. To date KDMs have been demonstrated to catalyse demethylation of N-epsilon methylated lysine residues. Biochemically there are two distinct groups of N-epsilon methylated lysine demethylases with different catalytic mechanisms, both of which result in methyl group oxidation to produce formaldhyde. KDM1A, formerly known as Lysine Specific Demethylase 1 (LSD1), belongs to the flavin adenine dinucleotide (FAD)-dependent amino oxidase family. The KDM1A reaction mechanism requires a protonatable lysine epsilon-amine group, not available in trimethylated lysines, which consequently are not KDM1 substrates. Other KDMs belong to the Jumonji C (JmjC) -domain containing family. These are members of the Cupin superfamily of mononuclear Fe (II)-dependent oxygenases, which are characterised by the presence of a double-stranded beta-helix core fold. They require 2-oxoglutarate (2OG) and molecular oxygen as co-substrates, producing, in addition to formaldehyde, succinate and carbon dioxide. This hydroxylation-based mechanism does not require a protonatable lysine epsilon-amine group and consequently JmjC-containing demethylases are able to demethylate tri-, di- and monomethylated lysines. The coordinates of post-translational modifications represented and described here follow UniProt standard practice whereby coordinates refer to the translated protein before any further processing. Histone literature typically refers to coordinates of the protein after the initiating methionine has been removed. Therefore the coordinates of post-translated residues in the Reactome database and described here are frequently +1 when compared with the literature. In general, methylation at histone H3 lysine-5 (H3K4) and lysine-37 (H3K36), including di- and trimethylation at these sites, has been linked to actively transcribed genes (reviewed in Martin & Zhang 2005). In contrast, lysine-10 (H3K9) promoter methylation is considered a repressive mark for euchromatic genes and is also one of the landmark modifications associated with heterochromatin (Peters et al. 2002). The first reported JmjC-containing demethylases were KDM2A/B (JHDM1A/B, FBXL11/10). These catalyse demethylation of histone H3 lysine-37 when mono- or di-methylated (H3K36Me1/2) (Tsukada et al. 2006). They were found to contain a JmjC catalytic domain, previously implicated in chromatin-dependent functions (Clissold & Ponting 2001). Subsequently, many other JmjC enzymes have been identified and discovered to have lysine demethylase activities with distinct methylation site and state specificities. KDM3A/B (JHDM2A/B) are specific for mono or di-methylated lysine-10 on histone H3 (H3K9Me1/2) (Yamane et al. 2006, Kim et al. 2012). KDM4A-C (JMJD2A-C/JHDM3A-C) catalyse demethylation of di- or tri-methylated histone H3 at lysine-10 (H3K9Me2/3) (Cloos et al. 2006, Fodor et al. 2006), with a strong preference for Me3 (Whetstine et al. 2007). KDM4D (JMJD2D) also catalyses demethylation of H3K9Me2/3 (Whetstine et al. 2007). KDM4A-C (JHDM3A-C) can also catalyse demethylation of lysine-37 of histone H3 (H3K36Me2/3) (Klose et al. 2006). KDM5A-D (JARID1A-D) catalyses demethylation of di- or tri-methylated lysine-5 of histone H3 (H3K4Me2/3) (Christensen et al. 2007, Klose et al. 2007, Lee et al. 2007, Secombe et al. 2007, Seward et al. 2007, Iwase et al. 2007). KDM6A and KDM6B (UTX/JMJD3) catalyse demethylation of di- or tri-methylated lysine-28 of histone H3 (H3K27Me2/3) (Agger et al. 2007, Cho et al. 2007, De Santra et al. 2007, Lan et al. 2007, Lee et al. 2007). KDM7A (KIAA1718/JHDM1D) catalyses demethylation of mono- or di-methylated lysine-10 of histone H3 (H3K9Me1/2) and mono- and di-methylated lysine-28 of histone H3 (H3K27Me1/2) (Horton et al. 2010, Huang et al. 2010). PHF8 (JHDM1E) catalyses demethylation of mono- or di-methylated lysine-10 of histone H3 (H3K9Me1/2) and mono-methylated lysine-21 of histone H4 (H4K20Me1) (Loenarz et al. 2010, Horton et al. 2010, Feng et al. 2010, Kleine-Kohlbrecher et al. 2010, Fortschegger et al. 2010, Qi et al. 2010, Liu et al. 2010). PHF2 (JHDM1E) catalyses demethylation of mono- or di-methylated lysine-10 of histone H3 (H3K9Me1/2) (Wen et al, 2010, Baba et al. 2011). JMJD6 was initially characterized as an arginine demethylase that catalyses demethylation of mono or di methylated arginine 3 of histone H3 (H3R2Me1/2) and arginine 4 of histone H4 (H4R3Me1/2) (Chang et al. 2007) although it was subsequently also characterized as a lysine hydroxylase (Webby et al. 2009).
Phosphorylation of WDR77 (MEP50) on threonine-5 by cyclin-dependent kinase 4 (CDK4), as part of the complex cyclin D1: CDK4:PRMT5:WDR77 enhances PRMT5:WDR77 methyltransferase activity, which triggers events associated with cyclin D1-dependent neoplastic growth (Aggarwal et al. 2011). Cyclin D1 is an allosteric regulator of CDK4 and CDK6, mediating growth factor-dependent G1-phase progression. Growth factor stimulation induces cyclin D1 expression, its association with CDK4 and nuclear accumulation during mid-G1. Active cyclin D1:CDK4 catalyzes the phosphorylation-dependent inactivation of retinoblastoma (RB) family proteins (Diehl 2002, Gladden & Diehl 2005). Following the G1/S transition, cyclin D1 accumulation is opposed by pro-287 directed phosphorylation of threonine-286 (T286) by glycogen synthase kinase 3 beta (GSK3beta), which promotes cyclin D1 nuclear export (Alt et al. 2000).
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Histone demethylases (HDMs) belong to two groups with distinct catalytic mechanisms. KDM1A and KDM1B (formerly known as Lysine Specific Demethylases 1 and 2), belong to the flavin adenine dinucleotide (FAD)-dependent amino oxidase family, releasing formaldehyde. The reaction mechanism requires a protonatable lysine epsilon-amino group, not available in trimethylated lysines (Shi et al. 2004). KDM1A and subsequently KDM1B were shown to catalyse demethylation of monomethyl and dimethyl, but not trimethyl, histone H3 at lysine 5 (H3K4) in vitro (Shi et al. 2004, Ciccone et al. 2009). Subsequently KDM1A was found to be much more proficient at catalysing demethylation of H3K4 when part of a multiprotein complex (Lee et al. 2005) and shown to catalyse demethylation of histone H3 at lysine 10 (H3K9) in vivo when associated with the androgen receptor (Metzger et al. 2007), suggesting that its substrate specificity is modulated by interacting proteins. KDM1A is a subunit of several complexes, including CtBP, Co-REST, NRD and BRAF35 (Lan et al. 2008). It is also able to catalyse demethylation of a number of non-histone proteins (Nicholson & Chen 2009).
All characterised lysine demethylases other than KDM1A belong to the jumonji C-domain (JmjC) containing family, members of the Cupin superfamily of mononuclear Fe (II)-dependent oxygenases. They require 2-oxoglutarate (2-OG) and molecular oxygen as co-substrates, producing succinate and carbon dioxide. This hydroxylation-based mechanism does not require a protonatable lysine epsilon-amine group and consequently JmjC-containing demethylases are able to demethylate tri-, di- and monomethylated lyines. The first reported JmjC-containing demethylases were KDM2A and KDM2B (JHDM1A/B, FBXL11/10). These demethylate lysine-37 of histone H3 when mono- or di-methylated (H3K36Me1/2) (Tsukada et al. 2006). KDM4A (JHDM3A) can demethylate mono-, di and trimethylated lysine-37 of histone H3 (Klose et al. 2006).
All characterized lysine demethylases other than KDM1A belong to the jumonjiC domain (JmjC) containing family.The JmjC KDMs are members of the Cupin superfamily of mononuclear Fe (II) dependent oxygenases, which are characterized by the presence of a double-stranded beta-helix core fold. The JmjC KDMs require 2 oxoglutarate (2 OG) and molecular oxygen as co substrates, producing, along with formaldehyde, succinate and carbon dioxide. This hydroxylation based mechanism does not require a protonatable lysine e amine group and consequently JmjC containing demethylases are able to demethylate tri , di and monomethylated lysines. KDM4A-D (JMJD2A-D/JHDM3A-D) catalyse the demethylation of di- or tri-methylated histone H3 at lysine-10 (H3K9Me2/3) (Cloos et al. 2006, Fodor et al. 2006, Whetstine et al. 2007), with a strong preference for Me3 (Whetstine et al. 2007). KDM4A (JHDM3A) can also demethylate lysine-37 of histone H3 (H3K36Me2/3) (Klose et al. 2006).
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Histone H3 arginine-9 (H3R8) dimethylation is a PRMT5-specific mark (Pal et al. 2004) associated with gene silencing (Chen et al. 1999, Pal et al. 2004, 2007).
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Histone H3 is symmetrically dimethylated on arginine-3 by PRMT5 and PRMT7 (Migliori et al. 2012, Tsai et al. 2013). This excludes binding of RBBP7, a central component of the co-repressor complexes Sin3a, NURD and PRC2. Conversely Me2sR3-histone H3 enhances binding of WDR5, a common component of the coactivator complexes MLL, SET1A, SET1B, NLS1 and ATAC. The interaction of histone H3 with WDR5 distinguishes symmetric dimethylation of arginine-3 from asymmetric dimethylation, which inhibits the recruitment of WDR5 to chromatin (Guccione et al. 2007, Hyllus et al. 2007, Migliori et al. 2012).
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RBBP7, a central component of the co-repressor complexes Sin3a, NURD and PRC2, can bind histone H3 arginine-3 (H3R2). Symmetrical dimethylation of this residue excludes RBBP7 binding but enhances binding of WDR5, a common component of the coactivator complexes MLL, SET1A, SET1B, NLS1 and ATAC (Migliori et al. 2012).
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Determination and comparison of specific activity of the HIF-prolyl hydroxylases
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Superoxide dismutase in extracellular fluids
Cloning and characterization of mouse lung-type acyl-CoA:lysophosphatidylcholine acyltransferase 1 (LPCAT1). Expression in alveolar type II cells and possible involvement in surfactant production
Iron-sulfur clusters containing 4 atoms of iron and 4 atoms of sulfur (4Fe-4S clusters) are assembled in the cytosol on a heterotetrameric scaffold composed of NUBP2 and NUBP1 subunits (reviewed in Lill et al. 2012, Rouault et al. 2012, Sharma et al. 2010, Lill and Muhlenhoff 2006). The sources of iron and sulfur are uncertain but the process requires a sulfur-containing compound exported from mitochondria via ABCB7 (ABC7). Newly synthesized 4Fe-4S are transferred to apoproteins such as XPD and POLD1 via the CIA targeting complex, composed of NARFL, CIAO1, FAM96B, and MMS19.
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Metabolic processes in human cells generate energy through the oxidation of molecules consumed in the diet and mediate the synthesis of diverse essential molecules not taken in the diet as well as the inactivation and elimination of toxic ones generated endogenously or present in the extracellular environment. The processes of energy metabolism can be classified into two groups according to whether they involve carbohydrate-derived or lipid-derived molecules, and within each group it is useful to distinguish processes that mediate the breakdown and oxidation of these molecules to yield energy from ones that mediate their synthesis and storage as internal energy reserves. Synthetic reactions are conveniently grouped by the chemical nature of the end products, such as nucleotides, amino acids and related molecules, and porphyrins. Detoxification reactions (biological oxidations) are likewise conveniently classified by the chemical nature of the toxin. At the same time, all of these processes are tightly integrated. Intermediates in reactions of energy generation are starting materials for biosyntheses of amino acids and other compounds, broad-specificity oxidoreductase enzymes can be involved in both detoxification reactions and biosyntheses, and hormone-mediated signaling processes function to coordinate the operation of energy-generating and energy-storing reactions and to couple these to other biosynthetic processes.
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Carbonic anhydrases reversibly catalyze the hydration of carbon dioxide and directly produce bicarbonate and protons, bypassing the formation of carbonic acid (reviewed in Lindskog 1997, Breton 2001, Esbaugh and Tufts 2006, Boron 2010, Gilmour 2010). Carbonic anhydrase deprotonates water to yield a zinc-hydroxyl group and a proton which is transferred to external buffer molecules via histidine or glutamate residues in carbonic anhydrase. The hydroxyl group reacts with carbon dioxide in the active site to yield bicarbonate. A water molecule displaces the bicarbonate and the reaction cycle begins again. There are currently 12 known active carbonic anhydrases in humans.
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Cytosolic Fe/S protein biogenesis depends on the electron transfer chain from NAD(P)H to the Fe/S protein (CIAPIN1 in humans, DRE2 in yeast) via the flavoprotein NDOR1 (TAH18 in yeast). The precise role of electrons in the assembly process is unclear but in the absence of the electron chain the stable [4Fe-4S] cluster of NUBP1 is not assembled. CIAPIN1 binds two Fe/S clusters of the [2Fe-2S] and the [4Fe-4S] type. The [2Fe-2S] cluster is reduced by NDOR1-NADPH.
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Carbonic anhydrase VI (CA6) hydrates carbon dioxide to yield bicarbonate and a proton (Thatcher et al. 1998, Nishimori et al. 2007).Carbonic anhydrase deprotonates water to yield a zinc-hydroxyl group and a proton which is transferred to external buffer molecules via histidine or glutamate residues in carbonic anhydrase. The hydroxyl group reacts with carbon dioxide in the active site to yield bicarbonate. A water molecule displaces the bicarbonate and the reaction cycle begins again (reviewed in Lindskog 1997). Depending on the concentrations of reactants the reaction is reversible. CA6 is a major protein of saliva and is also known as gustin.
Carbonic anhydrase VI (CA6) dehydrates bicarbonate to yield water and carbon dioxide (Thatcher et al. 1998, Nishimori et al. 2007). Depending on the concentrations of reactants the reaction is reversible. CA6 is a major protein of saliva and is also known as gustin.
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Structure-function analysis of liver-type (GLUT2) and brain-type (GLUT3) glucose transporters: expression of chimeric transporters in Xenopus oocytes suggests an important role for putative transmembrane helix 7 in determining substrate selectivity
KAT6A (Monocytic leukemia zinc finger protein, MOZ) and KAT6B (Monocytic leukemia zinc finger protein-related factor, MORF) are member of the MYST family of histone acetyltransferases, named after the founding members MOZ, Ybf2/Sas3, Sas2 and TIP60 (Borrow et al. 1996, Reifsnyder et al. 1996). The presence of a MYST domain is the only common structural motif in this family. MOZ and MORF are highly homologous (overall amino-acid sequence identity, 60%; similarity, 66%) but distinct from other family members (Yang & Ullah 2007). KAT6A and KAT6B have intrinsic histone acetyltransferase activity (Champagne et al. 1999, 2001). Both can form tetrameric 'ING5' complexes with BRPF1 (possibly BRPF2 and 3), EAF6 and ING5. BRPF1 and EAF6 drastically stimulate the acetyltransferase activities of KAT6A/B against nucleosomal histone H3 (Doyon et al. 2006, Ullah et al. 2008). ING5-MOZ/MORF complexes acetylate only histone H3 at lysine-14. KAT6A homozygous mice die at birth, with reduced hematopoiesis and profound defects in the stem cell compartment. These mice have no long-term repopulating stem cells and display substantial reduction in the number of multipotent cells able to form spleen colonies (Thomas et al. 2006). Chromosomal rearrangements of the KAT6A gene are associated with acute myeloid leukemia (AML), uterine leiomyomata and therapy-related myelodysplastic syndromes (Yang & Ullah, 2007). Mutations in KAT6B are the cause of the Say-Barber-Biesecker variant of Ohdo syndrome and Genitopatellar syndrome (Campeau et al. 2012, Szakszon et al. 2013).
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Histone acetyltransferases (HATs) involved in histone modifications are referred to as A-type or nuclear HATs. They can be grouped into at least four families based on sequence conservation within the HAT domain: Gcn5/PCAF, MYST, p300/CBP and Rtt109. The p300/CBP and Rtt109 families are specific to metazoans and fungi respectively (Marmorstein & Trievel 2009). Gcn5/PCAF and MYST family members have no significant sequence homology but share a globular alpha/beta fold with a common structure involved in acetyl-Coenzyme A (ACA) binding. Both use a conserved glutamate residue for the acetyl transfer reaction but may not share a common catalytic mechanism (Trievel et al. 1999, Tanner et al. 1999, Yan et al. 2002, Berndsen et al. 2007). The p300/CBP HAT domain has no homology with the other families but some structural conservation within theACA-binding core (Liu et al. 2008). In addition to histone acetylation, members of all 3 human HAT families have been shown to acetylate non-histones (Glozak et al. 2005). HATs and histone deacetylase (HDAC) enzymes generally act not alone but as part of multiprotein complexes. There are numerous examples in which subunits of HAT or HDAC complexes influence their substrate specificity and lysine preference, which in turn, affect the broader functions of these enzymes (Shahbazian & Grunstein 2007). N.B. The coordinates of post-translational modifications represented and described here follow UniProt standard practice whereby coordinates refer to the translated protein before any further processing. Histone literature typically refers to coordinates of the protein after the initiating methionine has been removed. Therefore the coordinates of post-translated residues in the Reactome database and described here are frequently +1 when compared with the literature.
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Studies in the past decade have suggested that the basic mechanism of DNA replication initiation is conserved in all kingdoms of life. Initiation in unicellular eukaryotes, in particular Saccharomyces cerevisiae (budding yeast), is well understood, and has served as a model for studies of DNA replication initiation in multicellular eukaryotes, including humans. In general terms, the first step of initiation is the binding of the replication initiator to the origin of replication. The replicative helicase is then assembled onto the origin, usually by a helicase assembly factor. Either shortly before or shortly after helicase assembly, some local unwinding of the origin of replication occurs in a region rich in adenine and thymine bases (often termed a DNA unwinding element, DUE). The unwound region provides the substrate for primer synthesis and initiation of DNA replication. The best-defined eukaryotic origins are those of S. cerevisiae, which have well-conserved sequence elements for initiator binding, DNA unwinding and binding of accessory proteins. In multicellular eukaryotes, unlike S. cerevisiae, these loci appear not to be defined by the presence of a DNA sequence motif. Indeed, choice of replication origins in a multicellular eukaryote may vary with developmental stage and tissue type. In cell-free models of metazoan DNA replication, such as the one provided by Xenopus egg extracts, there are only limited DNA sequence specificity requirements for replication initiation (Kelly & Brown 2000; Bell & Dutta 2002; Marahrens & Stillman 1992; Cimbora & Groudine 2001; Mahbubani et al 1992, Hyrien & Mechali 1993).
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Cytosolic GUK1 (guanylate kinase 1) catalyzes the reaction of carbovir monophosphate and ATP to form carbovir diphosphate and ADP. The activity of human GUK1 is inferred from that of the corresponding pig protein (Miller et al. 1992).
Cytosolic PCK1 (phosphoenolpyruvate carboxykinase 1) catalyzes the reaction of carbovir diphosphate and ATP to form carbovir triphosphate and ADP. The activity of human PCK1 and relative inactivity of human nucleoside diphosphate kinase are inferred from the properties of the purified rat and bovine enzymes in vitro (Miller et al. 1992).
Abacavir activation proceeds steps of phosphorylation, deamination to yield carbovir monophosphate, and phosphorylation of the latter compound to yield the triphosphate. In addition, abacavir can be conjugated with glucuronide or oxidized to its 5'-carboxylate derivative, the two major forms in which it is excreted from the body (Yuen et al. 2008).
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Abacavir is a nucleoside analogue reverse transcriptase inhibitor with antiretroviral activity, widely used in combination with other drugs to treat HIV-1 infection (Yuen et al. 2008). Its uptake across the plasma membrane is mediated by organic cation transporters SLC22A1, 2, and 3; the transport proteins ABCB1 and ABCG2 mediate its efflux. Abacavir itself is a prodrug. Activation requires phosphorylation by a cytosolic adenosine phosphotransferase and deamination by ADAL deaminase to yield carbovir monophosphate. Cytosolic nucleotide kinases convert carbovir monophosphate to carbovir triphosphate, the active HIV reverse transcriptase inhibitor. Abacavir can be glucuronidated or oxidized to a 5'-carboxylate; these are the major forms in which it is excreted from the body.
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Carbonic anhydrase I (CA1, Khalifah 1971, Simonsson et al. 1982, Ren and Lindskog 1992), carbonic anyhydrase II (CA2, Tibell et al. 1984, Jones and Shaw 1983, Pesando 1975, Ghannam et al. 1986), carbonic anhydrase III (CA3, Carter et al. 1979, Tu et al. 1990, Tu et al. 1994, Tu et al. 1998, Silverman et al. 1993), carbonic anhydrase VII (CA7, Bootorabi et al. 2010, Gitto et al. 2010) hydrate carbon dioxide to yield bicarbonate and a proton. Carbonic anhydrase deprotonates water to yield a zinc-hydroxyl group and a proton which is transferred to external buffer molecules via histidine or glutamate residues in carbonic anhydrase. The hydroxyl group reacts with carbon dioxide in the active site to yield bicarbonate. A water molecule displaces the bicarbonate and the reaction cycle begins again (reviewed in Lindskog 1997). Depending on the concentrations of reactants the reaction is reversible. CA2 and CA7 have high catalytic activity, CA1 has low activity (10% of the activity of CA2), and CA3 has very low activity (1% of the activity of CA2). CA1 and CA2 are found in erythrocytes. CA2 is also found in kidney, lung, and white muscle where it facilitates diffusion of carbon dioxide. CA3 is found in red muscle where it participates in resistance against oxidative stress.
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Carbonic anhydrase I (CA1, Khalifah 1971, Simonsson et al. 1982, Ren and Lindskog 1992), carbonic anyhydrase II (CA2, Tibell et al. 1984, Jones and Shaw 1983, Pesando 1975, Ghannam et al. 1986), carbonic anhydrase III (CA3, Carter et al. 1979, Tu et al. 1990, Tu et al. 1994, Tu et al. 1998, Silverman et al. 1993), carbonic anhydrase VII (CA7, Bootorabi et al. 2010, Gitto et al. 2010) dehydrate cytosolic bicarbonate to yield water and carbon dioxide (reviewed in Lindskog 1997). Depending on the concentrations of reactants the reaction is reversible. CA2 and CA7 have high catalytic activity, CA1 has low activity (10% of the activity of CA2), and CA3 has very low activity (1% of the activity of CA2). CA1 and CA2 are found in erythrocytes. CA2 is also found in kidney, lung, and white muscle where it facilitates diffusion of carbon dioxide. CA3 is found in red muscle where it participates in resistance against oxidative stress.
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Carbonic anhydrase IV (CA4, Zhu and Sly 1990, Okuyama et al. 1992, Baird et al. 1997, Innocenti et al. 2004), carbonic anhydrase IX (CA9, Wingo et al. 2001, Hilvo et al. 2008), carbonic anhydrase XII (CA12, Ulmasov et al. 2000, Pastorekova et al. 2008), and carbonic anhydrase XIV (CA14Ozensoy et al. 2005, Temperini et al. 2008) are membrane-bound enzymes that hydrate extracellular carbon dioxide to yield bicarbonate and a proton.Carbonic anhydrase deprotonates water to yield a zinc-hydroxyl group and a proton which is transferred to external buffer molecules via histidine or glutamate residues in carbonic anhydrase. The hydroxyl group reacts with carbon dioxide in the active site to yield bicarbonate. A water molecule displaces the bicarbonate and the reaction cycle begins again (reviewed in Lindskog 1997). Depending on the concentrations of reactants the reaction is reversible. CA4 has high catalytic activity. CA9, CA12, and CA14 have moderate activity. CA4 is anchored to the extracellular face of the plasma membrane by glycosylphosphatidylinositol. CA9, CA12, and CA14 are single-pass transmembrane proteins. CA4 is found on the extracellular face of capillaries in kidney, lung, and muscle where it maintains the gradient of carbon dioxide between tissue and blood. CA9 and CA12 are found on basolateral membranes of epithelia. CA9 is inducible by Hypoxia-inducible factor 1 alpha (HIF1alpha) and acidifies the extracellular environment of tumors. In rodents CA15 is membrane anchored and has low activity; in primates CA15 is a pseudogene.
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Carbonic anhydrase IV (CA4, Zhu and Sly 1990, Okuyama et al. 1992, Baird et al. 1997, Innocenti et al. 2004), carbonic anhydrase IX (CA9, Wingo et al. 2001, Hilvo et al. 2008), carbonic anhydrase XII (CA12, Ulmasov et al. 2000, Pastorekova et al. 2008), and carbonic anhydrase XIV (CA14, Ozensoy et al. 2005, Temperini et al. 2008) are membrane-bound enzymes that dehydrate bicarbonate to yield water and carbon dioxide. Depending on the concentrations of reactants the reaction is reversible. CA4 has high catalytic activity. CA9, CA12, and CA14 have moderate activity. CA4 is anchored to the extracellular face of the plasma membrane by glycosylphosphatidylinositol. CA9, CA12, and CA14 are single-pass transmembrane proteins. CA4 is found on the extracellular face of capillaries in kidney, lung, and muscle where it maintains the gradient of carbon dioxide between tissue and blood. CA9 and CA12 are found on basolateral membranes of epithelia. CA9 is inducible by Hypoxia-inducible factor 1 alpha (HIF1alpha) and acidifies the extracellular environment of tumors. In rodents CA15 is membrane anchored and has low activity; in primates CA15 is a pseudogene.
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Carbonic anhydrase VA (CA5A, Nagao et al. 1993, Franchi et al. 2003, Nishimori et al. 2007) and carbonic anhydrase VB (CA5B, Fujikawa-Adachi et al. 1999, Nishimori et al. 2005, Nishimori et al. 2007) hydrate carbon dioxide in mitochondria to yield bicarbonate and a proton. Carbonic anhydrase deprotonates water to yield a zinc-hydroxyl group and a proton which is transferred to external buffer molecules via histidine or glutamate residues in carbonic anhydrase. The hydroxyl group reacts with carbon dioxide in the active site to yield bicarbonate. A water molecule displaces the bicarbonate and the reaction cycle begins again (reviewed in Lindskog 1997). Depending on the concentrations of reactants the reaction is reversible.
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Carbonic anhydrase VA (CA5A, Nagao et al. 1993, Franchi et al. 2003, Nishimori et al. 2007) and carbonic anhydrase VB (CA5B, Fujikawa-Adachi et al. 1999, Nishimori et al. 2005, Nishimori et al. 2007) dehydrate bicarbonate in mitochondria to yield water and carbon dioxide (reviewed in Lindskog 1997). Depending on the concentrations of reactants the reaction is reversible.
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Type II phosphoinositide 5-phosphatases have unique sensitivities towards fatty acid composition and head group phosphorylation
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Carbonic anhydrase IV (CA4) located on the extracellular face of the plasma membrane (Wistrand et al. 1999) dehydrates bicarbonate (HCO3--) to yield water and carbon dioxide (CO2) (Zhu & Sly 1990, Okayuma et al. 1992, Baird et al. 1997, Innocenti et al. 2004, reviewed in Lindskog 1997). Depending on the concentrations of reactants the reaction is reversible.
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Erythrocytes circulating through the capillaries of the lung must exchange carbon dioxide (CO2) for oxygen (O2) during their short (0.5-1 sec.) transit time in pulmonary tissue (Reviewed in Jensen 2004, Esbaugh and Tufts 2006, Boron 2010). CO2 bound as carbamate to the N-terminus of hemoglobin and protons (H+) bound to histidine residues in hemoglobin are released as hemoglobin (HbA) binds O2. Bicarbonate (HCO3-) present in plasma is taken up by erythrocytes via the band3 anion exchanger (AE1, SLC4A1) and combined with H+ by carbonic anhydrases I and II (CA1/CA2) to yield water and CO2 (Reviewed by Esbaugh and Tufts 2006). CO2 is passively transported out of the erythrocyte by AQP1 and RhAG. HCO3- in plasma is also directly dehydrated by extracellular carbonic anhydrase IV (CA4) present on endothelial cells lining the capillaries in the lung.
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Binding to Rab3A-interacting molecule RIM regulates the presynaptic recruitment of Munc13-1 and ubMunc13-2
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The ABCB1 transporter associated with the plasma membrane mediates the ATP-dependent efflux of a variety of xenobiotic molecules. Its ability to transport abacavir is inferred from studies of the corresponding mouse protein (Shaik et al. 2007).
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Cytosolic levels of abacavir are determined by the balance of its facilitated diffusion into the cell mediated by organic cation transporters SLC22A1, 2, and 3, and its ATP-dependent efflux from cells mediated by ABCG2 and ABCB1 (Klaasen and Aleksunes 2010; Pan et al. 2007; Shaik et al. 2007).
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In capillaries of the lungs erythrocytes release carbon dioxide (CO2) and acquire oxygen (O2). In other tissues of the body the reverse reaction occurs (reviewed in Nikinmaa 1997, Jensen 2004). In the lungs, CO2 bound as carbamate to the N-terminus of hemoglobin (HbA) and protons bound to histidine residues in HbA are released as HbA binds oxygen. Bicarbonate (HCO3-) present in plasma is taken up by erythrocytes via the band3 anion exchanger (AE1, SLC4A1) and combined with protons by carbonic anhydrases I and II (CA1, CA2) to yield water and CO2 (reviewed by Esbaugh & Tufts 2006, De Rosa et al. 2007). The CO2 is passively transported out of the erythrocyte by AQP1 and RhAG. HCO3- in plasma is also directly dehydrated by extracellular carbonic anhydrase IV (CA4) present on endothelial cells lining the capillaries in the lung. In non-pulmonary tissues CO2 in plasma is hydrated to yield protons and HCO3- by CA4 located on the apical plasma membranes of endothelial cells. Plasma CO2 is also taken up by erythrocytes via AQP1 and RhAG. Within erythrocytes CA1 and, predominantly, CA2 hydrate CO2 to yield HCO3- and protons (reviewed in Geers & Gros 2000, Jensen 2004, Boron 2010). HCO3- is transferred out of the erythrocyte by the band 3 anion exchange protein (AE1, SLC4A1) which cotransports a chloride ion into the erythrocyte. Also within the erythrocyte, CO2 combines with the N-terminal alpha amino groups of HbA to form carbamates while protons bind histidine residues in HbA. The net result is the Bohr effect, a conformational change in HbA that reduces its affinity for O2 and hence assists the delivery of O2 to tissues.
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Organic cation transporters 1 (OCT1, SLC22A1), 2 (OCT2, SLC22A2) and 3 (OCT3, SLC22A3) associated with the plasma membrane all mediate the influx of abacavir. The three transporters have similar affinities for abacavir (Minuesa et al. 2009) but differ in the tissues in which they are expressed and in their distributions on the surfaces of polarized cells (reviewed by Klaasen and Aleksunes 2010).
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Cytosolic ADAL (Adenosine DeAminase-Like) catalyzes the reaction of abacavir monophosphate and water to form carbovir monophosphate and cyclopropylamine. The active form of the enzyme is a protein monomer complexed with a zinc ion (Murakami et al. 2011).
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NT5C2 catalyzes the reaction of carbovir and IMP to form carbovir monophosphate and inosine (Johnson and Fridland 1989; Miller et al. 1992). The enzyme was originally identified as a high-Km soluble 5'-nucleotidase most active on IMP and GMP (Spychala et al. 1988). Its active form is a tetramer (Wallden et al. 2007).
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Assignment of the gene for human arylsulfatase B, ARSB, to chromosome region 5p11----5qter
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The collagen substrate specificity of human skin fibroblast collagenase
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Structure of Rev-erbalpha bound to N-CoR reveals a unique mechanism of nuclear receptor-co-repressor interaction
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Dissecting activation of the PAK1 kinase at protrusions in living cells
Temporal and spatial regulation of the phosphatidate phosphatases lipin 1 and 2
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Mutations in the human sterol delta7-reductase gene at 11q12-13 cause Smith-Lemli-Opitz syndrome
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Chaperonin-mediated folding of vertebrate actin-related protein and gamma-tubulin
Kynurenine formamidase: determination of primary structure and modeling-based prediction of tertiary structure and catalytic triad.
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Human mitochondrial carbonic anhydrase VB. cDNA cloning, mRNA expression, subcellular localization, and mapping to chromosome x
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Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositide-dependent protein kinase-1
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Phosphatidylinositol- and phosphatidylcholine-transfer activity of PITPbeta is essential for COPI-mediated retrograde transport from the Golgi to the endoplasmic reticulum
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Structural and functional evolution of the L1 family: are four adhesion molecules better than one?
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Bile salt and organic anion SLC transporters
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Beta glucuronidase deficiency: report of clinical, radiologic, and biochemical features of a new mucopolysaccharidosis
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Cutting edge: Role of Toll-like receptor 9 in CpG DNA-induced activation of human cells
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626158
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29468
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626169
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626163
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626174
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626127
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_262527.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639319
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628860
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628859
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628858
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639775
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_256592.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641552
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628861
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627982
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_234227.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627990
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627917
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624846
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627696
The precise sequence of FGF receptor autophosphorylation is kinetically driven and is disrupted by oncogenic mutations
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_179586.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627654
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624828
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_252193.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652877
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_242098.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624767
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_254966.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626078
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625960
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624802
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625971
Human plasma epidermal growth factor/beta-urogastrone is associated with blood platelets
Nuclear accumulation of mutated beta-catenin in hepatocellular carcinoma is associated with increased cell proliferation
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625987
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628853
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_261439.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652804
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_258470.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652875
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_255201.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627744
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624839
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_241813.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624838
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624837
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626011
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5647976
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626001
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_256456.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29708
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652796
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4026.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623653
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619487
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623654
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_183240.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619494
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619489
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619490
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619491
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619492
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639240
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_255425.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639255
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639263
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637786
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_257025.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623658
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633390
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623657
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623652
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641553
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641555
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623614
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641011
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=109939
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_227108.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_183241.3
Mutations in the 4-hydroxyphenylpyruvate dioxygenase gene (HPD) in patients with tyrosinemia type III
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653073
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_183242.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653072
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_221674.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653393
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632780
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632994
Glutathione peroxidase 3 mediates the antioxidant effect of peroxisome proliferator-activated receptor gamma in human skeletal muscle cells
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633330
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_231992.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631103
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633354
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_236467.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632809
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652797
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_238831.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634398
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652795
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637216
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_258176.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630987
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652786
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645639
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_214089.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1474179
Identification of cell cycle-regulated phosphorylation sites on nuclear lamin C
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_111417.1
In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1475054
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_111639.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641019
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_212975.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641557
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_250236.1
Human alpha4beta2 neuronal nicotinic acetylcholine receptor in HEK 293 cells: A patch-clamp study
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633032
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633434
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5643341
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5643526
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645633
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635650
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633276
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649087
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633280
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633278
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633283
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641145
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633282
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645643
Cloning, tissue distribution, and functional analysis of the human Na+/N+ exchanger isoform, NHE3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649138
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649109
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649095
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649081
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648227
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648251
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648229
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641142
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641016
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641143
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641006
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641005
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641010
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641009
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641004
Biochemical analysis of the intrinsic Mcm4-Mcm6-mcm7 DNA helicase activity.
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641017
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_216013.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641007
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640999
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640998
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640997
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_111890.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1474124
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638069
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639768
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641008
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_111446.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1497857
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641556
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_111511.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_258520.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641559
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Xenobiotic, bile acid, and cholesterol transporters: function and regulation
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Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis
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Specificity of the deoxyhypusine hydroxylase-eukaryotic translation initiation factor (eIF5A) interaction: identification of amino acid residues of the enzyme required for binding of its substrate, deoxyhypusine-containing eIF5A
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The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency.
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Blocking of FGFR signaling inhibits breast cancer cell proliferation through downregulation of D-type cyclins
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Synthesis of IP2, IP, and Ins in the cytosol
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Heat shock factor 2 (HSF2) contributes to inducible expression of hsp genes through interplay with HSF1
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The Hippo-YAP pathway in organ size control and tumorigenesis: an updated version
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Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_241094.1
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Aminoacyl tRNA synthetases and their connections to disease
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Mechanism of biotin responsiveness in biotin-responsive multiple carboxylase deficiency
Human phosphoglycerate kinase. I. Crystallization and characterization of normal enzyme
Biochemistry of Lipids, Lipoproteins and Membranes, 5th Edition (Book): 213-244
Cell surface-bound IL-1alpha is an upstream regulator of the senescence-associated IL-6/IL-8 cytokine network
Proc. Natl. Acad. Sci. U.S.A. 106:17031-6
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=112478
translation initiation factor 2B delta subunit
eIF-2B GDP-GTP exchange factor, delta subunit
Translation initiation factor eIF-2B delta subunit
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Characterization of human carbonic anhydrase III from skeletal muscle
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translation initiation factor 2B beta subunit
eIF-2B GDP-GTP exchange factor, beta subunit
Translation initiation factor eIF-2B beta subunit
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Translation initiation factor eIF-2B gamma subunit
eIF-2B GDP-GTP exchange factor, gamma subunit
translation initiation factor 2B gamma subunit
eIF-2B GDP-GTP exchange factor, epsilon subunit
Translation initiation factor eIF-2B epsilon subunit
translation initiation factor 2B epsilon subunit
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Signal recognition particle 68 kDa protein
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624129
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624115
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624119
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624120
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624117
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eukaryotic translation initiation factor 5
Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate
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translation initiation factor 2B alpha subunit
Translation initiation factor eIF-2B alpha subunit
eIF-2B GDP-GTP exchange factor, alpha subunit
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624103
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624130
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624112
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624122
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624121
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624108
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624107
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A 13C nuclear magnetic resonance study of CO2/HCO-3 exchange catalyzed by human carbonic anhydrase I
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Identification of chondroitin sulfate glucuronyltransferase as chondroitin synthase-3 involved in chondroitin polymerization: chondroitin polymerization is achieved by multiple enzyme complexes consisting of chondroitin synthase family members
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Identification of c-erbB-3 binding sites for phosphatidylinositol 3'-kinase and SHC using an EGF receptor/c-erbB-3 chimera
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_240144.1
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Mismatch repair deficiency associated with overexpression of the MSH3 gene
Proc. Natl. Acad. Sci. U.S.A. 95:8568-73
Updated biological roles for matrix metalloproteinases and new "intracellular" substrates revealed by degradomics
Purification, molecular cloning, and sequencing of phospholipase C-beta 4
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The 40-kDa subunit of DNA fragmentation factor induces DNA fragmentation and chromatin condensation during apoptosis
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An orphan receptor tyrosine kinase family whose members serve as nonintegrin collagen receptors
Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs
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Implications of the structure of human uridine phosphorylase 1 on the development of novel inhibitors for improving the therapeutic window of fluoropyrimidine chemotherapy
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Sulfation of iodothyronines by human sulfotransferase 1C1 (SULT1C1)*
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Mutations and polymorphisms in GUSB gene in mucopolysaccharidosis VII (Sly Syndrome)
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Groucho-mediated transcriptional repression establishes progenitor cell pattern and neuronal fate in the ventral neural tube
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Interleukin-7 can induce the activation of Jak 1, Jak 3 and STAT 5 proteins in murine T cells
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Integrins and proximal signaling mechanisms in cardiovascular disease
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Mismatch recognition and DNA-dependent stimulation of the ATPase activity of hMutSalpha is abolished by a single mutation in the hMSH6 subunit
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Distinct domains in the SHP-2 phosphatase differentially regulate epidermal growth factor receptor/NF-kappaB activation through Gab1 in glioblastoma cells
eukaryotic translation initiation factor 3 subunit 7
Determinants for activation of the atypical AGC kinase Greatwall during M phase entry
eukaryotic translation initiation factor 3 subunit 10
Eukaryotic translation initiation factor 3 subunit 3
Eukaryotic translation initiation factor 3 subunit 2
eukaryotic translation initiation factor 3 subunit 6
eukaryotic translation initiation factor 3 subunit 9
eukaryotic translation initiation factor 3 subunit 5
Mechanisms involved in the regulation of histone lysine demethylases
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Eukaryotic translation initiation factor 3 subunit 4
eukaryotic translation initiation factor 3 subunit 8
Eukaryotic translation initiation factor 2 gamma subunit
eukaryotic translation initiation factor 2, subunit 3
Eukaryotic translation initiation factor 2 subunit 3
translation initiation factor 2 alpha subunit
Eukaryotic translation initiation factor 2 subunit 1
translation initiation factor 2, subunit 1
Eukaryotic translation initiation factor 2 alpha subunit
eukaryotic translation initiation factor 2, subunit 2
Eukaryotic translation initiation factor 2 subunit 2
eukaryotic translation initiation factor 2 beta subunit
Eukaryotic translation initiation factor 4E
The repertoire of solute carriers of family 6: identification of new human and rodent genes
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CHIP mediates degradation of Smad proteins and potentially regulates Smad-induced transcription
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Cleavage of the star strand facilitates assembly of some microRNAs into Ago2-containing silencing complexes in mammals
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Telomeres shorten during ageing of human fibroblasts
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ABCA3 gene mutations in newborns with fatal surfactant deficiency
Salt wasting and deafness resulting from mutations in two chloride channels
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Secretion of Wnt ligands requires Evi, a conserved transmembrane protein
Wntless, a conserved membrane protein dedicated to the secretion of Wnt proteins from signaling cells
Two novel rat liver membrane proteins that bind advanced glycosylation endproducts: relationship to macrophage receptor for glucose-modified proteins
eukaryotic translation initiation factor 3 subunit 11
Eukaryotic translation initiation factor 1A, X-chromosomal
eukaryotic translation initiation factor 1A
Sequence of the human iduronate 2-sulfatase (IDS) gene
Long-chain n-3 polyunsaturated fatty acids: new insights into mechanisms relating to inflammation and coronary heart disease
Regulation of Hsp90 client proteins by a Cullin5-RING E3 ubiquitin ligase
AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase
Heterogeneous nuclear ribonucleoprotein D0
Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex
RNA Polymerase I, RNA Polymerase III, and Mitochondrial Transcription
Tethering KSRP, a decay-promoting AU-rich element-binding protein, to mRNAs elicits mRNA decay
Mannose-1-phosphate guanyltransferase alpha
Identification of mammalian microRNA host genes and transcription units
Mannose-1-phosphate guanyltransferase beta
Dolichyl-phosphate beta-glucosyltransferase
Crystal structure of human kynurenine aminotransferase I
UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
Characterization of phospholipase D activity in bovine photoreceptor membranes
Glucosamine 6-phosphate N-acetyltransferase
UDP-N-acetylhexosamine pyrophosphorylase
Functional characterization of human sphingosine kinase-1
Interactions between extracellular signal-regulated protein kinase 1, 14-3-3epsilon, and heat shock factor 1 during stress
Glucosamine--fructose-6-phosphate aminotransferase (isomerizing) 1
Glucosamine--fructose-6-phosphate aminotransferase (isomerizing) 2
Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities
Elongation factor 1 beta gamma from Artemia. Purification and properties of its subunits.
N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
The eicosanoids: cyclooxygenase, lipoxygenase, and epoxygenase pathways
Biochemistry of Lipids, Lipoproteins and Membranes, 5th Edition (Book): 331-362
The binding of a transcription factor to deletion mutants of a 5S ribosomal RNA gene
Poly(I-C)-induced Toll-like receptor 3 (TLR3)-mediated activation of NFkappa B and MAP kinase is through an interleukin-1 receptor-associated kinase (IRAK)-independent pathway employing the signaling components TLR3-TRAF6-TAK1-TAB2-PKR
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Phospholipases D1 and D2 coordinately regulate macrophage phagocytosis
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Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes
The intracellular proteolytic processing of extracellular superoxide dismutase (EC-SOD) is a two-step event
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C-terminal lysines determine phospholipid interaction of sarcomeric mitochondrial creatine kinase
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A frequent kinase domain mutation that changes the interaction between PI3Kalpha and the membrane
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guanylyl-(3'->5')-3'-guanylic acid, cyclic 3'->5'''-nucleotide
cyclic-bis(3',5')diguanylic acid
cyclic-bis(3'->5') dimeric GMP
bis-(3'-5')-cyclic dimeric guanosine monophosphate
Guanosine 3',5'-cyclic monophosphate
bis(3',5')-cyclic diguanylic acid
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Characterization of human UDP-glucose dehydrogenase. CYS-276 is required for the second of two successive oxidations
The LZT proteins; the LIV-1 subfamily of zinc transporters
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Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1
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X-linked Cornelia de Lange syndrome owing to SMC1L1 mutations
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Molecular cloning and pharmacology of functionally distinct isoforms of the human histamine H(3) receptor
Mechanisms of maturation and ageing of collagen
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Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase
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Molecular and Biochemical Characterization of Rat epsilon -N-Trimethyllysine Hydroxylase, the First Enzyme of Carnitine Biosynthesis.
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StAR protein and the regulation of steroid hormone biosynthesis
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Fructose transporter in human spermatozoa and small intestine is GLUT5
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The characterization of gene mutations for human glucose phosphate isomerase deficiency associated with chronic hemolytic anemia
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Tumor necrosis factor alpha-induced phosphorylation of I kappa B alpha is a signal for its degradation but not dissociation from NF-kappa B
ChEBI:16618 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
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From structure to disease: the evolving tale of aquaporin biology
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Tristetraprolin recruits functional mRNA decay complexes to ARE sequences
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Differential signal transduction of alternatively spliced FGFR2 variants expressed in human mammary epithelial cells
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Signal transduction by immunoglobulin is mediated through Ig alpha and Ig beta
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Eukaryotic translation initiation factor 5A-1
hNTH1 glycosylase mediated recognition and binding of thymine glycol
Cleavage of thymine glycol by hNTH1 glycosylase
hNTH1 glycosylase mediated recognition and binding of dihydrouracil
hNTH1 glycosylase mediated recognition and binding of formamidopyrimidine
hNTH1 glycosylase mediated recognition and binding of cytosine glycol
Eukaryotic tranlation initiation factor 5A2
Cleavage of cytosine glycol by hNTH1 glycosylase
Loss of signaling through the G protein, Gz, results in abnormal platelet activation and altered responses to psychoactive drugs
Cleavage of formamidopyrimidine by hNTH1 glycosylase
Cleavage of dihydrouracil by hNTH1 glycosylase
Binding of REV1 to lesioned DNA template
Misinsertion of bases opposite to the lesion by HREV1
Displacement of hNTH1 glycosylase by APE1 at the AP site
APE1 mediated endonucleolytic cleavage at the 5' side of the base-free deoxyribose residue
Eukaryotic translation initiation factor 5A
Insertion of correct bases opposite to the lesion by Pol eta
Binding of Pol eta to lesioned DNA template
Dissociation of dimeric phospho-ATM complexes
Intermolecular autophosphorylation of ATM within dimeric ATM complexes
XPC binds to HR23B forming a heterodimeric complex
Association of RAD51 with the resected ends of the DNA double-strand break
Ligation of DNA and formation of Holliday structures following repair synthesis
T-complex protein 1 subunit eta (TCP-1-eta)
T-complex protein 1 subunit alpha (TCP-1-alpha)
T-complex protein 1 subunit theta (TCP-1-theta)
T-complex protein 1 subunit gamma (TCP-1-gamma)
T-complex protein 1 subunit epsilon (TCP-1-epsilon)
Aquaporin-1, nothing but a water channel
Ror2 modulates the canonical Wnt signaling in lung epithelial cells through cooperation with Fzd2
Formation of open bubble structure in DNA by helicases
XPC:HR23B complex binds to damaged DNA site with lesion
Binding of ERCC1-XPF to preincision complex
Formation of ERCC1-XPF heterodimeric complex
Ligation of newly synthesized repair patch to incised DNA in GG-NER
Formation of active Pol II complex with lesioned DNA template
RNA Pol II is blocked by the lesion leading to reduced transcription
T-complex protein 1 subunit beta (TCP-1-beta)
Displacement of stalled Pol II from the lesion site
A novel disorder caused by defective biosynthesis of N-linked oligosaccharides due to glucosidase I deficiency
T-complex protein 1 subunit zeta (TCP-1-zeta)
3' incision of the lesioned strand of DNA in TC-NER
T-complex protein 1 subunit delta (TCP-1-delta)
Regulation of cell growth-dependent expression of mammalian CDC6 gene by the cell cycle transcription factor E2F.
Differential expression of aquaporin 7 in adipose tissue of lean and obese high fat consumers
Identification and characterization of human cardiolipin synthase
Binding of calnexin/calreticulin to the unfolded protein
Removal of the second glucose by glucosidase II
Trimming of the first glucose by glucosidase I
Addition of a third glucose to the N-glycan precursor by an ALG10 homologue
Addition of a second glucose to the N-glycan precursor by ALG8
Addition of the first glucose to the N-glycan precursor by ALG6
Addition of the last mannose to the N-glycan precursor by ALG9
Addition of the eighth mannose to the N-glycan precursor by ALG12
Purification of human platelet-derived growth factor
Transport of glycoproteins with Man8 (or Man9) N-glycans to the Golgi
Glycoproteins with major folding defects are sent to degradation by EDEMs
Progressive trimming of alpha-1,2-linked mannose residues from Man8GlcNAc2 to produce Man5GlcNAc2
Progressive trimming of alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2
Trimming of the first mannose on the A branch
Trimming of the terminal mannose on the C branch
Re-addition of a glucose on the alpha 1,3 branch
Trimming of the second mannose on the A branch
Trimming of the terminal mannose on the B branch
Removal of the third glucose by glucosidase II and release from the chaperone
Protein transport protein Sec61 subunit alpha isoform 1
B3GALTL transfers glucose to O-fucosyl-proteins
POFUT2 transfers fucose to TSR domain-containing proteins
Trimming of mannoses on the alpha1,6 arm by MAN2A1
Addition of GlcNAc to the glycan on the A arm
Progressive trimming of alpha-1,2-linked mannose residues from Man7GlcNAc2 to produce Man5GlcNAc2
IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
Addition of galactose by beta 4-galactosyltransferases
Addition of GlcNAc to position 5 by MGAT5
Addition of alpha 1,6 fucose to the first GlcNAc of the N-glycan
Addition of a GlcNAc on the alpha 1,4 branch by MGAT2
TIMM23 PAM translocates proteins from the mitochndrial intermebrane space to the mitochondrial matrix
MPP hydrolyzes presequence of matrix precursors
Translocon-associated protein subunit alpha
Transfer of SUMO1 from E1 to UBE2I (UBC9)
SAM50 complex inserts proteins into mitochondrial outer membrane
MPP hydrolyzes presequence of inner membrane precursors
TIMM23 SORT inserts proteins into inner membrane
The protein tyrosine kinase Tec regulates mast cell function
The mannose receptor is a pattern recognition receptor involved in host defense
A disintegrin and metalloproteinase with thrombospondin motifs 13
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Aquaporins: translating bench research to human disease
Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
A disintegrin and metalloproteinase with thrombospondin motifs 7
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Multiple isozymes of heparan sulfate/heparin GlcNAc N-deacetylase/GlcN N-sulfotransferase. Structure and activity of the fourth member, NDST4
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Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol 3-kinase for ubiquitination in T cells
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Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
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Sentrin-specific protease 2 ecNumber3.4.22.68/ecNumber
Sentrin-specific protease 1 ecNumber3.4.22.68/ecNumber
Netrin-1/neogenin interaction stabilizes multipotent progenitor cap cells during mammary gland morphogenesis
GDP-fucose protein O-fucosyltransferase 2 ecNumber2.4.1.221/ecNumber
Glycosylation-induced conformational modification positively regulates receptor-receptor association: a study with an aberrant epidermal growth factor receptor (EGFRvIII/DeltaEGFR) expressed in cancer cells
Mitochondrial import inner membrane translocase subunit TIM44
Mitochondrial import inner membrane translocase subunit TIM16
Proteins Inserted into Mitochondrial Outer Membrane by SAM50 Complex
Voltage-dependent anion-selective channel protein 1
Mitochondrial import receptor subunit TOM40 homolog
Mitochondrial import inner membrane translocase subunit TIM50
Sorting and assembly machinery component 50 homolog
Heterodimerization is required for the formation of a functional GABA(B) receptor
G protein-coupled receptor kinase-5 regulates thrombin-activated signaling in endothelial cells
Mitochondrial import inner membrane translocase subunit Tim9
Mitochondrial import inner membrane translocase subunit Tim10
ADP,ATP carrier protein, liver isoform T2
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The mitochondrial electron transport and oxidative phosphorylation system
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Molecular cloning and functional expression of the potassium-dependent sodium-calcium exchanger from human and chicken retinal cone photoreceptors
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The RGD integrin binding site in human L1-CAM is important for nuclear signaling
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Model for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide: a kinetic and computational study
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Functional characterization of human 1-acylglycerol-3-phosphate acyltransferase isoform 8: cloning, tissue distribution, gene structure, and enzymatic activity
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649855
Hyaluronan export by the ABC transporter MRP5 and its modulation by intracellular cGMP
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649853
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649851
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649849
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649847
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640412
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640362
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640361
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640357
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640414
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640413
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_248816.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640467
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640416
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640415
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649869
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649863
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649865
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649867
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649868
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649857
Highly calcium permeable nicotinic acetylcholine receptors
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_232906.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649859
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649861
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649856
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640418
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653373
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_192063.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630098
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_183227.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653109
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_220608.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653110
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_202776.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_223550.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627853
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627860
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627845
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627846
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649871
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_249354.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627843
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627844
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652888
Signalling via integrins: implications for cell survival and anticancer strategies
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_184347.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642841
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630417
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630416
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630412
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_177986.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642733
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642842
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_186165.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627804
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627805
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627867
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627868
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627802
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627803
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642905
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642904
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_186362.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642906
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642902
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642677
The inhibitory anti-FGFR3 antibody, PRO-001, is cytotoxic to t(4;14) multiple myeloma cells
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_186368.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642898
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642896
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642897
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642895
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642893
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=30064
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3957.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642891
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622185
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622202
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622204
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_231246.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622181
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_236747.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_237128.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642885
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642887
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642807
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642883
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622205
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_194822.3
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_256259.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622188
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622186
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5528.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=70986
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3681.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=30034
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_194810.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642889
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642751
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642749
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642752
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642753
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622821
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642747
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_232265.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642701
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622815
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622820
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622819
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4475.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622811
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113569
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642694
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642696
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642698
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642699
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642700
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642692
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2904.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111647
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_240412.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652596
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_239433.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652612
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_233069.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622824
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622822
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622142
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622141
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_244954.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622144
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622146
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622145
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=83951
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2585.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636772
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636771
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636770
Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636774
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636773
Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622153
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_248907.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622150
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622151
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2753.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2561.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=109327
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=109330
Regulation of actin filament assembly by Arp2/3 complex and formins
Annu Rev Biophys Biomol Struct 36:451-77
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_225570.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652611
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_239599.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636776
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622200
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622199
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622198
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622196
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622194
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622189
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622190
UDP-N-acetylglucosamine transferase subunit ALG14 homolog
GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase
Chitobiosyldiphosphodolichol beta-mannosyltransferase
Asparagine-linked glycosylation protein 11 homolog
Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
Mannose-P-dolichol utilization defect 1 protein
Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
Ubiquitin-dependent degradation of Cyclin D
Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
Fat and beyond: the diverse biology of PPARgamma
FGFR1 emerges as a potential therapeutic target for lobular breast carcinomas
UDP-glucose:glycoprotein glucosyltransferase 1
ER degradation-enhancing alpha-mannosidase-like 2
ER degradation-enhancing alpha-mannosidase-like 3
UDP-glucose:glycoprotein glucosyltransferase 2
Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621650
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621651
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111628
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621657
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_227800.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_205985.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3042.1
Multiple coagulation factor deficiency protein 2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621655
Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC
Kiz-1, a protein with LIM zinc finger and kinase domains, is expressed mainly in neurons
Ether lipid biosynthesis: alkyl-dihydroxyacetonephosphate synthase protein deficiency leads to reduced dihydroxyacetonephosphate acyltransferase activities
Asymmetric localization of Vangl2 and Fz3 indicate novel mechanisms for planar cell polarity in mammals
Absorption of chlorophyll phytol in normal man and in patients with Refsum's disease
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622848
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622870
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622874
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622878
Vav3 mediates receptor protein tyrosine kinase signaling, regulates GTPase activity, modulates cell morphology, and induces cell transformation
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622885
Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622861
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622856
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622860
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622886
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622881
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622880
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622879
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652591
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621826
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621825
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_253954.1
60 kDa heat shock protein, mitochondrial
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621827
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620557
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621821
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620573
Iron-sulfur cluster co-chaperone protein HscB, mitochondrial
Proteins Imported to the Matrix by TIMM23 PAM
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622866
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622865
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622852
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_242690.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652593
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_238809.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652592
PTG depletion removes Lafora bodies and rescues the fatal epilepsy of Lafora disease
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_248884.1
Testis-specific Y-encoded-like protein 2
Frequent activating mutations of FGFR3 in human bladder and cervix carcinomas
TRIP: a novel double stranded RNA binding protein which interacts with the leucine rich repeat of flightless I
From cell-ECM interactions to tissue engineering
Identification of the alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase gene, the human ortholog of the yeast LYS5 gene
Probable ATP-dependent RNA helicase DDX11
Hot-spot mutations in p110alpha of phosphatidylinositol 3-kinase (pI3K): differential interactions with the regulatory subunit p85 and with RAS
Catalytic pathway of manganese superoxide dismutase by direct observation of superoxide
Molecular characterization of heat shock-like factor encoded on the human Y chromosome, and implications for male infertility
Molecular cloning and characterization of a human multisubstrate specific nucleotide-sugar transporter homologous to Drosophila fringe connection
Calcium signalling in lymphocyte activation and disease
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=30181
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_258340.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623981
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623980
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623979
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623978
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2515.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=83747
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2277.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=112475
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623983
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_238139.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113448
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_248528.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624095
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2667.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623982
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_258154.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5104.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623976
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=112134
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111987
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3498.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623977
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_234377.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624094
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113443
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3117.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629139
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629156
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113704
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4233.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624149
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_253374.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=76050
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4215.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622843
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622844
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622887
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622889
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_236227.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622074
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622828
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622832
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622841
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622837
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622833
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5643062
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626330
Inositol hexakisphosphate kinase products contain diphosphate and triphosphate groups
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636206
Human and Drosophila UDP-galactose transporters transport UDP-N-acetylgalactosamine in addition to UDP-galactose
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621341
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621610
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4674.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622888
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111980
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4709.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622842
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=112051
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111984
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2689.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623975
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_256673.1
Cloning and functional characterization of the human 5-HT2B serotonin receptor
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624576
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624548
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624566
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624562
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638050
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622987
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638047
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640471
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640462
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628971
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640470
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628992
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640465
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633999
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640466
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636175
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640463
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640464
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640353
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640472
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_193744.3
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_256609.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622985
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623277
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623280
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623278
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631804
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631838
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634726
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622999
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635996
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640458
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640459
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640461
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634672
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_242016.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634679
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640496
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_193756.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640468
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640469
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622989
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622997
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Failure of highly purified lysyl hydroxylase to hydroxylate lysyl residues in the non-helical regions of collagen
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Movement through Slits: cellular migration via the Slit family
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A cytoplasmic chaperonin that catalyzes beta-actin folding
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Probable D-lactate dehydrogenase, mitochondrial
ATP synthase subunit beta, mitochondrial
Para-hydroxybenzoate--polyprenyltransferase, mitochondrial
ATP synthase lipid-binding protein precursor
Transforming growth factor beta receptor type II inactivation induces the malignant transformation of intestinal neoplasms initiated by Apc mutation
Precursors Imported to the Matrix by TIMM23 PAM
Mitochondrial-processing peptidase subunit alpha
Mitochondrial-processing peptidase subunit beta
Mitochondrial import inner membrane translocase subunit TIM14
Mitochondrial import inner membrane translocase subunit Tim17-A
Mitochondrial import inner membrane translocase subunit Tim17-B
Functional analysis of alternatively spliced transcripts of the human histidine decarboxylase gene and its expression in human tissues and basophilic leukemia cells
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Purification of superoxide dismutases from human placenta using immunoadsorbent columns
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Modulation of Kit/stem cell factor receptor-induced signaling by protein kinase C
Endoplasmic reticulum stress induction of insulin-like growth factor-binding protein-1 involves ATF4
Comparative analysis of gene regulation by the transcription factor PPARalpha between mouse and human
Conversion of Phosphatidylcholine to Phosphatidylglycerol with Phospholipase D and glycerol
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Accumulation of nonphosphorylated beta-catenin and c-myc in primary and uremic secondary hyperparathyroid tumors
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Transcriptional and post-transcriptional regulation of iNOS expression in human chondrocytes
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Expression of isoforms of the human receptor tyrosine kinase c-kit in leukemic cell lines and acute myeloid leukemia
Crystallization and properties of human liver ornithine aminotransferase
High mobility group proteins stimulate DNA cleavage by apoptotic endonuclease DFF40/CAD due to HMG-box interactions with DNA
The H+/Cl- exchange transporters CLCN4 (Kawasaki et al. 1999, Zdebik et al. 2008), CLCN5 (Zdebik et al. 2008) and CLCN6 (Neagoe et al. 2010) mediate the exchange of endosomal Cl- for cytosolic H+ across endosomal membranes, contributing to the acidification of endosomes.
Bestrophins 1-4 (BEST1-4, aka vitelliform macular dystrophy proteins) mediate cytosolic Cl- efflux across plasma membranes. This transport is sensitive to intracellular Ca2+ concentrations (Sun et al. 2002, Tsunenari et al. 2003). Mutations in bestrophins that impair their function are implicated in macular degeneration in the eye. Defects in BEST1 cause vitelliform macular dystrophy (BVMD, Best's disease, MIM:153700), an autosomal dominant form of macular degeneration that usually begins in childhood and is characterized lesions due to abnormal accumulation of lipofuscin within and beneath retinal pigment epithelium (RPE) cells (Marquardt et al. 1998, Petrukhin et al. 1998).
Many Cl- channels such as CFTR, ClC, CaCC, and ligand-gated anion channels are permeable to bicarbonate (HCO3-) which is an important anion in the regulation of pH. Many tissues, including retinal pigment epithelium (RPE), utilize HCO3- transporters to mediate transport of HCO3-. Bestrophns 1-4 (BEST1-4, aka vitelliform macular dystrophy proteins) have high permeability to HCO3- (Hu & Hartzell 2008). Defective BEST1 may play a role in macular degeneration in the eye due to impaired HCO3- and Cl- conductance (Hu & Hartzell 2008).
The microsomal Na+/(PO4)3- transporter isoform 1 (SLC17A3, NPT4 isoform 1) is a member of the anion-cation symporter family. It is expressed in liver, kidney and intestine and may function as a cotransporter of sodium (Na+) and phosphate ((PO4)3- or Pi) across the ER membrane (Melis et al. 2004).
Human serum urate levels are largely maintained by its reabsorption and secretion in the kidney. Loss of this maintenance can elevate urate levels leading to gout, hypertension, and various cardiovascular diseases. Renal urate reabsorption is controlled via two proximal tubular urate transporters; apical SLC22A12 (URAT1) and basolateral SLC2A9 (URATv1, GLUT9). On the other hand, urate secretion is mediated by the orphan sodium phosphate transporter 4 isoform 2 (SLC17A3, NPT4 isoform 2). It is mainly expressed at the apical side of renal tubules and functions as a voltage-driven urate transporter (Jutabha et al. 2010). Genetic variations in SLC17A3 influence the variance in serum uric acid concentrations and define the serum uric acid concentration quantitative trait locus 4 (UAQTL4; MIM:612671). Excess serum urate (hyperuricemia) can lead to the development of gout, characterized by tissue deposition of monosodium urate crystals.
The sodium/hydrogen exchanger 9B1 (SLC9B1 aka Na+/H+ exchanger like domain containing 1, NHEDC1) is specifically expressed on the plasma membrane of the testis and may be implicated in infertility (Ye et al. 2006). Sodium/hydrogen exchanger 9C2 (SLC9C2), also localized to the plasma membrane, may be involved in pH regulation although this protein has not been fully characterized.
Mitochondrial sodium/hydrogen exchanger 9B2 (SLC9B2, aka NHA2) is ubiquitously expressed and mediates the electrogenic exchange of 1 Na+ (or 1 Li+) for 2 H+ across the inner mitochondrial membrane (Xiang et al. 2007, Taglicht et al. 1993). This transport is thought to play a role in salt homeostasis and pH regulation in humans.
All functionally characterized TRP channels are permeable to the divalent cation Ca2+ except TRPM4 and 5 (Latorre et al. 2009, Wu et al. 2010).
Most members of the TRP channel family are permeable to Ca2+. Although TRPM4 and 5 can be activated by increased levels of intracellular Ca2+, they are impermeable to it. Instead, they are monovalent-selective with highest affinity for Na+ transport, of which leads to depolarization of the membrane (Launay et al. 2002, Prawitt et al. 2003). They play a central role in cardiomyocytes, neurons, endocrine pancreas cells, kidney epithelial cells and cochlea hair cells.
Transient receptor potential (TRP) channel proteins were first discovered in Drosophila melanogaster and have many homologues in other species including humans. TRPs form cationic channels that can detect sensory stimuli such as temperature, pH or oxidative stress and transduce that into either electrical (change in membrane potential) or chemical signals (change in intracellular Ca2+ concentration). In humans, there are 28 TRP genes arranged into 6 subfamilies; TRPA, TRPC, TRPM, TRPML, TRPP, and TRPV (Wu et al. 2010). Each TRP channel subunit consists of six putative transmembrane-spanning segments (S1-S6) with a pore-forming loop between S5 and S6. These subunits assemble into tetramers to form functional channels. All functionally characterized TRP channels are permeable to Ca2+ except TRMP4 and 5 which are only permeable to monovalent cations such as Na+ (Latorre et al. 2009). Most TRPs can cause channelopathies which are risk factors for many disease states (Nilius & Owsianik 2010).
Together, the complex of coatomer, Arf1, and ArfGAP assembles into a lattice that concentrates cargo proteins and deforms the membrane. Eventually this membrane pocket forms into a bud that pinches off the membrane, and is released into the cytoplasm (Lippincott-Schwartz and Liu 2006).
All of the key components and regulators of the COPI coat (GBF1, Arf1, ArfGAP1 and coatomer) cycle on and off the Golgi membrane. This cycle is required for vesicle formation, but is uncoupled from the actual vesicle release. Continuous membrane binding and release of these molecules enables the COPI lattice to be dynamically modulated. Once the vesicle is released from the Golgi apparatus, this lattice is completely disassociated from the vesicle.
In models of COPI coat assembly and disassembly, after GBF1 activates Arf1 on membranes, the active form of Arf1 recruits coatomer complexes from the cytoplasm.
Once both coatomer and the active form of Arf1 have been recruited to the Golgi membrane surface, ArfGAP joins the complex.
The H+/Cl- exchange transporter CLCN3 (Borsani et al. 1995) mediates the exchange of endosomal Cl- for cytosolic H+ across late endosomal membranes, contributing to the acidification of endosomes. The activity of CLCN3 is inferred from experiments in mice (Stobrawa et al. 2001, Hara-Chikuma et al. 2005).
The 5-hydroxytryptamine receptor (HTR3) family are members of the superfamily of ligand-gated ion channels (LGICs). Five receptors (HTR3A-E) form a heteropentamer. Binding of the neurotransmitter 5-hydroxytryptamine (5HT, serotonin) to the HTR3 complex opens the channel, which in turn, leads to an excitatory response in neurons and is permeable to sodium, potassium, and calcium ions (Miyake et al. 1995, Davies et al. 1999, Niesler et al. 2007).
Nephrin strands contribute to a porous slit diaphragm scaffold as revealed by electron tomography
Acid-sensing ion channels 1, 2, 3 and 5 (ASIC1, 2, 3 and 5, aka amiloride-sensitive cation channels) are homotrimeric, multi-pass membrane proteins which can transport sodium (Na+) when activated by extracellular protons. Members of the ASIC family are sensitive to amiloride and function in neurotransmission. The encoded proteins function in learning, pain transduction, touch sensation, and development of memory and fear. Many neuronal diseases cause acidosis, accompanied by pain and neuronal damage; ASICs can mediate the pathophysiological effects seen in acidiosis (Wang & Xu 2011, Qadri et al. 2012). The diuretic drug amiloride inhibits these channels, resulting in analgesic effects. NSAIDs (Nonsteroidal anti-inflammatory drugs) can also inhibit ASICs to produce analgesia (Voilley et al. 2001). ASICs are also partially permeable to Ca2+, Li+ and K+ (not shown here). ASIC1 and 2 are expressed mostly in brain (Garcia-Anoveros et al. 1997, Price et al. 1996), ASIC3 is strongly expressed in testis (de Weille et al. 1998, Ishibashi & Marumo 1998) and ASIC5 is found mainly in intestine (Schaefer et al. 2000). ASIC4 subunits do not form functional channels and it's activity is unknown. It could play a part in regulating other ASIC activity (Donier et al. 2008).
Amiloride-sensitive sodium channels (SCNNs, aka ENaCs, epithelial Na+ channels, non voltage-gated sodium channels) belong to the epithelial Na+ channel/degenerin (ENaC/DEG) protein family and mediate the transport of Na+ (and associated water) through the apical membrane of epithelial cells in kidney, colon and lungs. This makes SCNNs important determinants of systemic blood pressure. The physiological activator for SCNNs is unknown but as they belong in the same family as acid-sensitive ion channels (ASICs, which are mediated by protons), these may also be the activating ligands for SCNNs. SCNNs are probable heterotrimers comprising an alpha (or interchangeable delta subunit), beta and gamma subunit (Horisberger 1998).
ARF1 helps to recruit AP-1 to Golgi membrane. AP-1 is not alone in this process of establishing a docking complex at the trans-Golgi Network. This section of the Golgi membrane will be where the new vesicle will be built and loaded.
The glycine receptor (GLR) is a ligand-gated ion channel. It is functional as a heteropentamer, consisting of alpha (GLRA) and beta (GLRB) subunits. With no ligand bound, the receptor complex is closed to chloride ions. Binding of the inhibitory neurotransmitter glycine (Gly) to this receptor complex increases chloride conductance into neurons and thus produces hyperpolarization (inhibition of neuronal firing) (Grenningloh et al. 1990, Nikolic et al. 1998, Handford et al. 1996).
The anterograde membrane flow from the ER to the Golgi is compensated for by a retrograde pathway. This pathway's functions include the recycling of membrane and proteins to the ER.
Ligand-gated ion channels (LGICs) are a group of transmembrane ion channels that are opened or closed in response to the binding of a chemical messenger (Purves, 2001).
Secretory transport depends on membrane-bounded carriers to move protein and lipid between intracellular compartments. The COPI coat has a central role in this process, creating a sorting domain on the membrane into which cargo proteins, destined to return to the endoplasmic reticulum (ER), concentrate. The membrane domain deforms into a coated bud, pinches off the membrane as a coated carrier, and then uncoats. Successful operation of the COPI coat system is necessary for selective retrieval of protein and lipid components back to the ER.
The sodium leak channel non-selective protein NALCN, a nonselective cation channel, forms the background Na+ leak conductance and controls neuronal excitability (Lu et al. 2007). Mice with mutant NALCN have a severely disrupted respiratory rhythm and die within 24 hours of birth. Calcium (Ca2+) influences neuronal excitability via the NALCN:UNC79:UNC80 complex, with high Ca2+ concentrations inhibiting transport of Na+ (Lu et al. 2010).
Ultimately the hydrolysis of Arf1-bound GTP, induced by the recruited ArfGAP, allows the inactive Arf1-GDP to diffuse away from the membrane, initiating disassembly of the lattice from the vesicle (Lippincott-Schwartz and Liu 2006).
Chloride channel proteins 1, 2, Ka and Kb (CLCN1, 2, KA, KB) can mediate Cl- influx across the plasma membrane of almost all cells. CLCN1 is expressed mainly on skeletal muscle where it is involved in the electrical stability of the muscle. CLCN1 is thought to function in a homotetrameric form (Steimeyer et al. 1994). CLCN2 is ubiquitously expressed, playing a role in the regulation of cell volume (Cid et al. 1995, Niemeyer et al. 2009). Defects in CLCN1 cause myotonia congenita, an autosomal dominant disease (MCD aka Thomsen disease, MIM:160800). It is characterized by muscle stiffness due to delayed relaxation, resulting from membrane hyperexcitability (Meyer-Kleine et al. 1995, Steimeyer et al. 1994). Defects in CLCN1 also cause autosomal recessive myotonia congenita (MCR aka Becker disease, MIM:255700) (Koch et al. 1992, Meyer-Kleine et al. 1995), a nondystrophic skeletal muscle disorder characterized by muscle stiffness and an inability of the muscle to relax after voluntary contraction. Becker disease is more common and more severe than Thomsen disease. CLCNKA and B (Kieferle et al. 1994) are predominantly expressed in distal nephron segments of the kidney (Takeuchi et al. 1995) and the inner ear (Estevez et al. 2001, Schlingmann et al. 2004). They are tightly associated with their essential beta subunit barttin (BSND), requiring it to be fully functional channels (Fischer et al. 2010, Scholl et al. 2006). These channels bound to BSND are essential for renal Cl- reabsorption (Waldegger & Jentsch 2000) and K+ recycling in the inner ear (Estevez et al. 2001). Defects in CLCNKA and B cause Bartter syndrome type 4B (BS4B; MIM:613090) characterized by impaired salt reabsorption and sensorineural deafness (Schlingmann et al. 2004, Nozu et al. 2008). Defects in BSND cause Bartter syndrome type 4A (BS4A aka infantile Bartter syndrome with sensorineural deafness; MIM:602522) characterized by impaired salt reabsorption in the thick ascending loop of Henle and sensorineural deafness (Birkenhager et al. 2001, Nozu et al. 2008).
Inactive Arf1-GDP then diffuses away from the membrane, initiating the disassembly of the lattice.
Amiloride-sensitive sodium channels (SCNNs, aka ENaCs, epithelial Na+ channels, non voltage-gated sodium channels) comprises three subunits (alpha, beta and gamma) and plays an essential role in Na+ and fluid absorption in the kidney, colon and lung. The number of channels at the cell's surface (consequently its function) can be regulated. This is achieved by ubiquitination of SCNN via E3 ubiquitin-protein ligases (NED4L and WPP1) (Staub et al. 2000, Farr et al. 2000). NED4L/WPP1 is found in a signaling complex including Raf1 (RAF proto-oncogene serine/threonine-protein kinase), SGK (serum/glucocorticoid-regulated kinase) and GILZ (glucocorticoid-induced leucine zipper protein, TSC22D3) (Soundararajan et al. 2009). Ubiquitinated SCNN (Ub-SCNN) is targeted for degradation so a lesser number of channels are present at the cell surface, reducing the amount of Na+ absorption. Proline-rich sequences at the C-terminus of SCNNs include the PY motif containing a PPxY sequence. PY motifs bind WW domains of NED4L/WPP1. Protein kinases with no lysine K (WNKs) can activate SCNN activity by interacting non-enzymatically with the signaling complex, specifically SGK although the mechanism is unknown (Heise et al. 2010).
The hydrolysis of Arf1-bound GTP is induced by the recruited ArfGAP.
Calcium-activated chloride channels (CaCCs) are ubiquitously expressed and implicated in physiological processes such as sensory transduction, fertilization, epithelial secretion, and smooth muscle contraction. The anoctamin family of transmembrane proteins (ANO, TMEM16) belong to CaCCs and have been shown to transport Cl- ions when activated by intracellular Ca2+ (Galietta 2009, Huang et al. 2012). There are currently 10 members, ANO1-10, all having a similar structure, with eight putative transmembrane domains and cytosolic amino- and carboxy-termini. ANO1 and 2 possess Ca2+ activated Cl- transport activity (Yang et al. 2008, Scudieri et al. 2012) while the remaining members also show some demonstrable activity (Tian et al. 2012).
Dynamin is recruited to the growing vesicle and, under conditions that interfere with its GTPase activity, dynamin forms a collar or ring around the neck of the budding vesicle. It is unclear whether dynamin acts as a mechanochemical transducer to generate fission or as a recruiter to attach other proteins that are directly responsible for the fission step. Lipid-modifying enzymes such as endophilin are also involved in vesicle formation. Endophilin is an acyltransferase that interacts with dynamin and that generates lysophosphatidic acid. The current view is that this reaction produces a negative curvature at the neck of the vesicle.
Proteins that have been synthesized, processed and sorted eventually reach the final steps of the secretory pathway. This pathway is responsible not only for proteins that are secreted from the cell but also enzymes and other resident proteins in the lumen of the ER, Golgi, and lysosomes as well as integral proteins transported in the vesicle membranes.
The P-type ATPases (E1-E2 ATPases) are a large group of evolutionarily related ion pumps that are found in bacteria, archaea and eukaryotes. They are referred to as P-type ATPases because they catalyze auto-phosphorylation of a key conserved aspartate residue within the pump. They all appear to interconvert between at least two different conformations, E1 and E2. Most members of this transporter family pump a large variety of cations (Kuhlbrandt W, 2004).
Dynamin is recruited to the growing lysosome destined vesicle and, under conditions that interfere with its GTPase activity, dynamin forms a collar or ring around the neck of the budding vesicle. It is unclear whether dynamin acts as a mechanochemical transducer to generate fission or as a recruiter to attach other proteins that are directly responsible for the fission step. Lipid-modifying enzymes such as endophilin are also involved in vesicle formation. Endophilin is an acyltransferase that interacts with dynamin and that generates lysophosphatidic acid. The current view is that this reaction produces a negative curvature at the neck of the vesicle.
The plasma membrane contains a broad range of lipids making up the bilayer. Aminophospholipids (APLs) such as phosphatidylserine (PS) and phosphatidylethanolamine (PE) are distributed in this bilayer and their arrangement is mediated by the P-type ATPases type IV family (Paulusma and Oude Elferink, 2005).
Proteins that have been synthesized, processed and sorted eventually reach the final steps of the secretory pathway. This pathway is responsible not only for proteins that are secreted from the cell but also enzymes and other resident proteins in the lumen of the ER, Golgi, and lysosomes as well as integral proteins transported in the vesicle membranes. Here the proteins in this secretory pathway are ultimately found in lysososmes.
The vamp2 associated vesicle docks and fuses with the plasma membrane.
Structural and biochemical properties of cloned and expressed human and rat steroid 5 alpha-reductases
T-cell activation Rho GTPase-activating protein
There at least two classes of clathrin coated vesicles in cells, one predominantly Golgi-associated, involved in budding from the trans-Golgi network and the other at the plasma membrane. Here the clathrin-coated vesicles emerging from the Golgi apparatus are triggered by the heterotetrameric adaptor protein complex, AP-1 at the trans-Golgi network membrane. The cargo can be transmembrane, membrane associated or golgi luminal proteins. Each step in the vesicle sculpting pathway, gathers cargo and clathrin triskeletons, until a complete vesicular sphere is formed. With the scission of the membrane the vesicle is released and eventually losses its clathrin coat.
Intracellular pools of Ca2+ serve as the source for inositol 1,4,5-trisphosphate (IP3) -induced alterations in cytoplasmic free Ca2+. In most human cells Ca2+ is stored in the lumen of the sarco/endoplastic reticulum by ATPases known as SERCAs (ATP2As). In platelets, ATP2As transport Ca2+ into the platelet dense tubular network. ATP2As are P-type ATPases, similar to the plasma membrane Na+ and Ca+-ATPases. Humans have three genes for SERCA pumps; ATP2A1-3. Studies on ATP2A1 suggest that it binds two Ca2+ ions from the cytoplasm and is subsequently phosphorylated at Asp351 before translocating Ca2+ into the SR lumen. There is a counter transport of two or possibly three protons ensuring partial charge balancing.
The vamp8 associated vesicle docks and fuses with the plasma membrane.
Accumulation of calcium into the Golgi apparatus is mediated by sarco(endo)plasmic reticulum calcium-ATPases (SERCAs) and by secretory pathway calcium-ATPases (SPCAs). There are two human genes which encode SPCAs; ATP2C1 and ATP2C2 which encode magnesium-dependent calcium-transporting ATPase type 2C members 1 and 2 (ATP2C1 and 2) respectively (Sudbrak et al, 2000; Vanoevelen et al, 2005). Defects in ATP2C1 are the cause of Hailey-Hailey disease (HHD), an autosomal dominant disease characterized by persistent blisters and erosions of the skin (Hu et al, 2000).
Dab2 is recruited to Cx43-based GJs possibly through a direct interaction between its N-terminal phosphotyrosine binding (PTB) domain and a putative XPXY internalization motif found in the C-terminal tail of Cx43 as well as a number of other connexin family members (Piehl et al., 2007).The distal portion of Dab2 on its opposite end binds the globular N-terminal domain of clathrin heavy chains (Piehl et al., 2007).
The potassium-transporting ATPase heterodimer (ATP4A/12A:ATP4B) catalyzes the hydrolysis of ATP coupled with the exchange of H+ and K+ ions across the plasma membrane. It is composed of alpha and beta chains. Two human genes encode the catalytic alpha subunit, ATP4A and ATP12A (Maeda et al, 1990; Grishin et al, 1994). ATP4A is responsible for acid production in the stomach. ATP12A is responsible for potassium absorption in various tissues. One human gene encodes the beta subunit, ATP4B (Ma et al, 1991).
After passing through the Golgi complex, secretory cargo is packaged into post-Golgi transport intermediates (post-Golgi), which translocate plus-end directed along microtubules to the plasma membrane.
The plasma membrane contains a broad range of lipids making up the bilayer. Aminophospholipids such as phosphatidylserine (PS) and phosphatidylethanolamine (PE) are distributed in this bilayer and their arrangement is mediated by the P-type ATPases type IV family (Paulusma and Oude Elferink, 2005).
The transport of iron between cells is mediated by transferrin. However, iron can also enter and leave cells not only by itself, but also in the form of heme and siderophores. When entering the cell via the main path (by transferrin endocytosis), its goal is not the (still elusive) chelated iron pool in the cytosol nor the lysosomes but the mitochondria, where heme is synthesized and iron-sulfur clusters are assembled (Kurz et al,2008, Hower et al 2009, Richardson et al 2010).
The GTPase dynamin, which functions in the completion of vesicle budding localizes in Cx43-based GJs and especially invaginating plaques and AGJ vesicles (Piehl et al., 2007).
The human gene ATP7B encodes the copper-transporting ATPase 2 (ATP7B, ATPase2, Wilson's protein) which is expressed mainly in the liver, brain and kidneys (Bull et al, 1993). ATP7B resides on the trans-Golgi membrane where it it thought to sequester copper from the cytosol into the golgi (Yang et al, 1997). Defects in ATP7B are the cause of Wilson disease (WD), an autosomal recessive disorder of copper metabolism characterized by the toxic accumulation of copper in a number of organs, particularly the liver and brain (Thomas et al, 1995).
The plasma membrane Ca-ATPases 1-4 (ATP2B1-4, PMCAs) are P-type Ca2+-ATPases regulated by calmodulin. The PMCA also counter-transports a proton. PMCA is important for Ca2+ homeostasis and function.
Gap junction plaque internalization and the disruption cell communication requires a reorganization of Cx molecular interactions. Proteins including Dab-2, AP-2, Dynamin and Myosin VI associate with gap junction plaques permitting the internalisation of plaques after clathrin association (Piehl et al., 2007).
The half-life of Cx is very short (1 to 5h) compared to other junctional proteins (Laird et al., 1995 ; Fallon and Goudenough, 1981). Connexins are targeted for degradation by the proteasome and the lysosome. Degradation appears to involve the phosphorylation of Connexins as well as their interactions with other proteins (Piehl et al., 2007).
Initiation/Cargo Recognition is mediated by ESCRT-0, a heterodimer consisting of Vps27 and Hse1. ESCRT-0 binds Phosphatidyl inositol 3- phosphate (PI3P) on endosomes via a FVYE domain and ubiquitinated cargo via two UIM domains.
ESCRT-0 recruits ESCRT-I and thereby initiates the MVB pathway. Cargo Sorting ESCRT-I is a heterotetramer consisting of Vps23, Vps28, Vps37, and Mvb12. The UEV domain of Vps23 binds ubiquitinated membrane proteins. Vps28 interacts with the GLUE domain of Vps36 in ESCRT-II. Cargo Sorting ESCRT-II is a heterotetramer formed of Vps36, Vps22, and two Vps25 molecules. The GLUE domain of Vps36 binds PI3P, Vps28, and ubiquitinated membrane proteins. Vps25 interacts with Vps20 of ESCRT-III.
Ferritin oxidises Fe(II) ions to Fe(III), migrates them to its centre, and collects thousands of them as FeO(OH) in the central mineral core from which they can be later remobilised (Harrison & Arrosio 1996).
Gap junctions are intercellular communication channels formed from Cx (connexin) protein subunits (see Segretain and Falk 2004 and Evans et al. 2006 for comprehensive reviews). Connexins are transported to the plasma membrane after oligomerizing into hexameric assemblies called hemichannels (CxHcs) or connexons. Connexons dock head-to-head in the extracellular space with opposing hexameric channels located in the plasma membranes of neighbouring cells. The double membrane channel or gap junction generated directly links the cytoplasms of interacting cells and facilitates the integration and co-ordination of cellular signalling, metabolism, secretion and contraction. In addition to their role in intercellular communication, connexon hemichannels coordinate the release of ATP, glutamate, NAD+ and prostaglandin E2 from the cells. CxHcs open in response to various types of external changes, including mechanical, shear, ionic and ischaemic stress. The trafficking of gap junctions involves (1) synthesis of connexin polypeptides at endoplasmic reticulum membranes, (2) oligomerization into homomeric- and heteromeric gap junction connexons (hemi-channels), (3) passage through the Golgi stacks, (4) intracellular storage within Trans Golgi membranes, (5) trafficking along microtubules, (6) insertion of connexons into the plasma membrane, (7) lateral diffusion of connexons in the plasma membrane, (8) aggregation of individual gap junction channels into plaques, (9) stabilization of peripheral microtubule plus-ends by binding to Cx43-based gap junctions, (10) internalization of the channel plaque leading to cytoplasmic annular junctions, and (11) complete degradation via lysosomal and proteasomal pathways (see Segretain and Falk 2004). Aspects of gap assembly are described here. Additional details of assembly, regulation and degradation will be covered in the next release.
Endocytosis of iron loaded transferrin/receptor complex leads, after acidification of the endosome, to the separation of iron and its diffusion out of the vesicle. The endosome is not fused with a lysosome but recycles its content back to the cell surface where soon transferrin dissociates from its receptor (Dautry-Varsat, 1986).
Gap junctions are clusters of intercellular channels connecting adjacent cells and permitting the direct exchange of ions and small molecules between cells. These channels are composed of two hemichannels, or connexons, one located on each of the two neighboring cells. Each connexon is composed of 6 trans-membrane protein subunits of the connexin (Cx) family. A gap of approximately 3 nm remains between the adjacent cell membranes, but two connexons interact and dock head-to-head in the extra-cellular space forming a tightly sealed, double-membrane intercellular channel (see Segretain and Falk, 2004). The activity of these intercellular channels is regulated, particularly by intramolecular modifications such as phosphorylation which appears to regulate connexin turnover, gap junction assembly and the opening and closure (gating) of gap junction channels.
Mucolipin-1 is an iron ion channel specifically expressed in endosome and lysosome membranes. It catalyzes the diffusion of Fe2+ ions into the cytosol (Dong et al, 2008).
RAB8A/10/13/14 release GDP and bind GTP to yield the active complex. Guanine nucleotide exchange factors (GEFs) stimulate the reaction. GTPase-activating proteins (GAPs) oppose the reaction by stimulating the intrinsic GTPase activity of the RAB proteins.
The heme transporter FLVCR is expressed in intestine and liver tissue, but also in developing erythroid cells where it is required to protect them from heme toxicity (Quigley et al, 2004; Rey et al, 2008).
Many plasma membrane proteins are in a constant flux throughout the internal trafficking pathways of the cell. Some receptors are continuously internalized into recycling endosomes and returned to the cell surface. Others are sorted into intralumenal vesicles of morphologically distinctive endosomes that are known as multivesicular bodies (MVBs). These MVBs fuse with lysosomes, resulting in degradation of their cargo by lysosomal acidic hydrolases. Endosomes can be operationally defined as being either early or late, referring to the relative time it takes for endocytosed material to reach either stage. Ultrastructural studies indicate that early endosomes are predominantly tubulovesicular structures, which constitute a major sorting platform in the cell, whereas late endosomes show the characteristics of typical MVBs and are capable of fusing with lysosomes. A well characterized signal for shunting membrane proteins into the degradative MVB pathway is the ubiquitylation of these cargoes. At the center of a vast protein:protein and protein:lipid interaction network that underpins ubiquitin mediated sorting to the lysosome are the endosomal sorting complexes required for transport (ESCRTs), which are conserved throughout all major eukaryotic taxa.
The function of V-type proton pumping ATPases is basically the same as that of F-type ATPases, except that V-ATPases cannot synthesize ATP from the proton motive force, the reverse reaction of pumping. When pumping, ATP hydrolysis drives a 120 degree rotation of the rotor which leads to movement of three protons into the phagosome (Adachi et al. 2007).
Disassembly Phase The AAA-ATPase, Vps4 disassembles ESCRT-III and catalyzes the final step of the MVB pathway. The microtubule interacting and trafficking (MIT) domain of Vps4 interacts directly with the C-terminal region of Vps2 (MIM1) and Vps20 (MIM2). The association of Vta1, which contains two MIT domains, greatly enhances the activity of Vps4. Please note that the recomended names of the Vacuolar protein sorting-associated proteins (Vps) are Charged multivesicular body proteins or CHMPs.
Aquaporins (AQP's) are six-pass transmembrane proteins that form channels in membranes. Each monomer contains a central channel formed in part by two asparagine-proline-alanine motifs (NPA boxes) that confer selectivity for water and/or solutes. The monomers assemble into tetramers. Most aquaporins (i.e. AQP0/MIP, AQP1, AQP2, AQP3, AQP4, AQP5, AQP7, AQP8, AQP9, AQP10) passively transport water into and out of cells according to the osmotic gradient across the membrane. Four aquaporins (the aquaglyceroporins AQP3, AQP7, AQP9, AQP10) conduct glycerol, three aquaporins (AQP7, AQP9, AQP10) conduct urea, and one aquaporin (AQP6) conducts anions, especially nitrate. AQP8 also conducts ammonia in addition to water. AQP11 and AQP12, classified as group III aquaporins, were identified as a result of the genome sequencing project and are characterized by having variations in the first NPA box when compared to more traditional aquaporins. Additionally, a conserved cysteine residue is present about 9 amino acids downstream from the second NPA box and this cysteine is considered indicative of group III aquaporins. Purified AQP11 incorporated into liposomes showed water transport. Knockout mice lacking AQP11 had fatal cyst formation in the proximal tubule of the kidney. Exogenously expressed AQP12 showed intracellular localization. AQP12 is expressed exclusively in pancreatic acinar cells. Aquaporins are important in fluid and solute transport in various tissues. In adipocytes, glycerol generated by triglyceride hydrolysis is exported by AQP7 and is imported by liver cells via AQP9. AQP1 plays a role in forming cerebrospinal fluid and AQP1, AQP4, and AQP9 appear to be important in maintaining fluid balance in the brain. AQP0, AQP1, AQP3, AQP4, AQP8, AQP9, and AQP11 play roles in the physiology of the hepatobiliary tract. In the kidney, water and solutes are passed out of the bloodstream and into the proximal tubule via the slit-like structure formed by nephrin in the glomerulus. Water is reabsorbed from the filtrate during its transit through the proximal tubule, the descending loop of Henle, the distal convoluted tubule, and the collecting duct. Aquaporin-1 (AQP1) in the proximal tubule and the descending thin limb of Henle is responsible for about 90% of reabsorption (as estimated from mouse knockouts of AQP1). AQP1 is located on both the apical and basolateral surface of epithelial cells and thus transports water through the epithelium and back into the bloodstream. In the collecting duct epithelial cells have AQP2 on their apical surfaces and AQP3 and AQP4 on their basolateral surfaces to transport water across the epithelium. The permeability of the epithelium is regulated by vasopressin, which activates a signaling cascade leading to the phosphorylation of AQP2 and its translocation from intracellular vesicles to the apical membrane of collecting duct cells. Here, three views of aquaporin-mediated transport have been annotated: a generic view of transport mediated by the various families of aquaporins independent of tissue type, a view of the role of specific aquaporins in maintenance of renal water balance, and a view of the role of specific aquaporins in glycerol transport from adipocytes to the liver.
ESCRT-III assembles into a highly ordered filament-like hetero-oligomer. Vps20 nucleates the homo-oligomerization of Snf7 that is capped by Vps24. Vps24 recruits Vps2 and initiates Vps4-dependent ESCRT-III disassembly. ESCRT-III is required for the last steps of MVB sorting, cargo sequestration, and MVB vesicle formation.
Cytochrome b reductase 1 not only reduces ferrous iron in the brush-border membrane but also in the airways. It is upregulated on iron starvation. However, its electron donor molecule is still unknown (Oakhill et al, 2007; Turi et al, 2006).
Aquaporin-9 (AQP9) passively transports water, glycerol, urea, and some other small neutral solutes across the plasma membrane according to the osmotic gradient. AQP9 is expressed in the sinusoidal plasma membrane in the liver facing the portal vein where it is believed to be responsible for glycerol uptake as part of gluconeogenesis. AQP9 is also expressed in glia, neurons, and peripheral leukocytes.
Triglycerides stored in adipocytes are hydrolyzed to yield fatty acids and glycerol. The glycerol is passively transported out of the adipocyte and into the bloodstream by Aquaporin-7 (AQP7) located in the plasma membrane of adipocytes. Glycerol in the bloodstream is passively transported into liver cells by AQP9 located in the plasma membrane of hepatocytes. Once inside the liver cell the glycerol is a substrate for gluconeogenesis.
Aquaporin-7 (AQP7) passively transports glycerol and water across the plasma membrane according to the osmotic gradient. AQP7 is expressed in adipocytes under the direct control of the PPARG and RXRA nuclear receptors. Expression of AQP7 correlates with release of glycerol from adipocytes. AQP7 is seen to translocate from the nuclear periphery to the plasma membrane during adrenaline-stimulated lipolysis. In rat AQP7 also transports urea.
Interferons: signaling, antiviral and viral evasion
SLC1A4-mediated exchange of extracellular cysteine for cytosolic alanine, serine, or threonine
SLC1A4-mediated exchange of extracellular alanine for cytosolic serine, threonine, or cysteine
SLC16A10-mediated uptake of aromatic amino acids
SLC1A4-mediated exchange of extracellular threonine for cytosolic alanine, serine, or cysteine
SLC1A4-mediated exchange of extracellular serine for cytosolic alanine, threonine, or cysteine
Na+/H+ exchanger transport (at late endosome membrane)
Na+/H+ exchanger transport (at cell membrane)
Na+/H+ exchanger transport (at trans-golgi membrane)
Na+/H+ exchanger transport (at early endosome membrane)
The docking protein Gab1 is the primary mediator of EGF-stimulated activation of the PI-3K/Akt cell survival pathway
The gene encoding carbonic anhydrase IX (CA9) is transcribed to yield mRNA and the mRNA is translated to yield protein. Hypoxia-inducible factor binds the promoter of CA9 and enhances expression of CA9.
HIF (heterodimer of HIF-alpha and HIF-beta) recruits p300 and CBP to the promoters of target genes (Kallio et al. 1998, Ebert and Bunn 1998, Ema et al. 1999, Gu et al. 2001, Dames et al. 2002, Freedman et al. 2002).
HIF-alpha subunits, comprising HIF1A (Bruick and McKnight 2001, Ivan et al. 2001, Jaakkola et al. 2001), HIF2A (Percy et al. 2008, Furlow et al. 2009), and HIF3A (Maynard et al. 2003), are hydroxylated at proline residues by the prolyl hydroxylases PHD1 (EGLN2), PHD2 (EGLN1), and PHD3 (EGLN3) (Bruick and McKnight 2001, Berra et al. 2003, Hirsila et al. 2003, Metzen et al. 2003, Tuckerman et al. 2004, Appelhoff et al. 2004, Fedulova et al. 2007, Tian et al. 2011). The reaction requires molecular oxygen as a substrate and so it is inhibited by hypoxia. PHD2 (EGLN1) is predominantly cytosolic (Metzen et al. 2003) and is the key determinant in the regulation of HIF-alpha subunits by oxygen (Berra et al. 2003). HIF-alpha subunits hydroxylated at proline residues are bound by VHL, an E3 ubiquitin ligase in a complex containing ElonginB, Elongin C, CUL2, and RBX1. VHL ubiquitinates HIF-alpha, resulting in destruction of HIF-alpha by proteolysis. Hypoxia inhibits proline hydroxylation and interaction with VHL, stabilizing HIF-alpha, which transits to the nucleus and activates gene expression.
Destruction of ubiquitinated HIF-alpha can occur in both the cytosol and nucleus (Berra et al. 2001). Upon reoxygenation of hypoxic cells HIF-alpha is ubiquitinated in the nucleus and transported to the cytosol in a complex with VHL:ElonginB:ElonginC:CUL2:RBX1 where it is destroyed (Groulx and Lee 2002, Jaakkola et al. 2001, Ivan et al. 2001)
HIF-alpha (HIF1A, HIF2A (EPAS1), HIF3A) forms a heterodimer with ARNT (HIF1-beta) (Wang et al. 1995, Jiang et al. 1996, Tian et al. 1997, Gu et al. 1998, Erbel et al. 2003).
HIF-alpha is translocated into the nucleus (Kallio et al. 1998, Depping et al. 2008, Chachami et al. 2009). Importin 4 and importin 7 (Chachami et al. 2009) as well as the importin alpha/beta pathway (Depping et al. 2008) appear to be capable of interacting with HIF-alpha. During hypoxia HIF-alpha accumulates in the nucleus where it associates with CBP and p300 (Kallio et al. 1998).
VHL is an E3 ubiquitin ligase that conjugates ubiquitin to hydroxylated HIF-alpha (Iwai et al. 1999, Kamura et al. 2000, Ohh et al. 2000, Groulx and Lee 2002, Maynard et al. 2003). VHL is predominantly cytosolic and shuttles between the cytosol and the nucleus (Lee et al. 1999, Groulx and Lee 2002). Ubiquitination and degradation of HIF-alpha can occur in both the cytosol and the nucleus (Berra et al. 2001).
The VHL component of the VHL:ElonginB:ElonginC:CUL2:RBX1 binds HIF-alpha that have hydroxylated proline residues (Cockman et al. 2000, Ohh et al. 2000, Tanimoto et al. 2000, Jaakkola et al. 2001, Ivan et al. 2001, Yu et al. 2001, Bonicalzi et al. 2001). The VHL:HIF-alpha complex is predominantly nuclear (Lewis and Roberts 2003) however binding and degradation of HIF-alpha can also occur in the cytosol (Berra et al. 2001).
When hypoxic cells return to normoxia, HIF-alpha is ubiquitinated in the nucleus and exported to the cytosol (Groulx and Lee 2002). The shuttling of VHL between the nucleus and cytosol is required (Groulx and Lee 2002, Lee et al. 1999).
VHL is an E3 ubiquitin ligase that conjugates ubiquitin to hydroxylated HIF-alpha (Iwai et al. 1999, Kamura et al. 2000, Ohh et al. 2000, Groulx and Lee 2002, Maynard et al. 2003). VHL is predominantly cytosolic and shuttles between the cytosol and the nucleus (Lee et al. 1999, Groulx and Lee 2002). Ubiquitination and degradation of HIF-alpha can occur in both the cytosol and the nucleus (Berra et al. 2001). Upon return to normoxia from hypoxia most ubiquitinated HIF-alpha is nuclear (Groulx and Lee 2002).
VHL within the VHL:ElonginB:ElonginC:CUL2:RBX1 Complex binds HIF-alpha subunits that have hydroxylated proline residues (Cockman et al. 2000, Ohh et al. 2000, Tanimoto et al. 2000, Jaakkola et al. 2001, Ivan et al. 2001, Yu et al. 2001). VHL constitutively shuttles between the cytosol and nucleoplasm (Lewis and Roberts 2003) and though the VHL:HIF-alpha complex is predominantly nuclear, binding and degradation can occur in both the cytosol and the nucleus (Berra et al. 2001).
Proline hydroxylases PHD1 (EGLN2) and PHD3 (EGLN3) located in the nucleus (Metzen et al. 2003) hydroxylate HIF3A at proline-492 (Hirsila et al. 2003, Maynard et al. 2003). Note that proline-492 of the reference isoform is proline-490 in isoform 2, the protein cited by Maynard et al. 2003. The amount of hydroxylation occurring in the nucleus is controversial. Most hydroxylation is believed to occur in the cytosol.
Proline hydroxylases PHD1 (EGLN2) and PHD3 (EGLN3) located in the nucleus (Metzen et al. 2003) hydroxylate HIF1A at proline-402 and proline-564 (Buick and McKnight 2001, Jaakkola et al. 2001, Ivan et al. 2001, Ivan et al. 2002, Berra et al. 2003, Hirsila et al. 2003, Appelhoff et al. 2004, Tuckerman et al. 2004, Fedulova et al. 2007, Tian et al. 2011). The amount of hydroxylation occurring in the nucleus is controversial. Most hydroxylation is believed to occur in the cytosol.
Proline hydroxylases PHD1 (EGLN2) and PHD3 (EGLN3) located in the nucleus hydroxylate HIF2A (EPAS1) at proline-405 and proline-531 (Hirsila et al. 2003, Percy et al. 2008, Furlow et al. 2009). The amount of hydroxylation occurring in the nucleus is controversial. Most hydroxylation is believed to be cytosolic.
Proline hydroxylases PHD2 (EGLN1) and PHD3 (EGLN3) located in the cytosol (Metzen et al. 2003) hydroxylate HIF3A at proline-492 (Hirsila et al. 2003, Maynard et al. 2003). A portion of PHD3 (EGLN3) is also located in the nucleus (Rantanen et al. 2008).
Proline hydroxylases PHD2 (EGLN1) and PHD3 (EGLN3) located in the cytosol (Metzen et al. 2003) hydroxylate HIF1A at proline-402 and proline-564 (Bruick and McKnight 2001, Jaakkola et al. 2001, Ivan et al. 2001, Ivan et al. 2002, Berra et al. 2003, Hirsila et al. 2003, Appelhoff et al. 2004, Tuckerman et al. 2004, Fedulova et al. 2007, Tian et al. 2011). A portion of PHD3 (EGLN3) is also located in the nucleus (Rantanen et al. 2008).
Proline hydroxylases PHD2 (EGLN1) and PHD3 (EGLN3) located in the cytosol (Metzen et al. 2003) hydroxylate EPAS1 (HIF2A) at proline-405 and proline-531 (Hirsila et al. 2003, Percy et al. 2008, Furlow et al. 2009). A portion of PHD3 (EGLN3) is also located in the nucleus (Rantanen et al. 2008).
Ion channels mediate the flow of ions across the plasma membrane of cells. They are integral membrane proteins, typically a multimer of proteins, which, when arranged in the membrane, create a pore for the flow of ions. There are different types of ion channels. P-type ATPases undergo conformational changes to translocate ions. Ligand-gated ion channels operate like a gate, opened or closed by a chemical signal. Voltage-gated ion channels are activated by changes in electrical potential difference at the membrane (Purves, 2001; Kuhlbrandt, 2004).
beta-Ureidopropionase deficiency: an inborn error of pyrimidine degradation associated with neurological abnormalities
Ion channels that mediate sensations such as pain, warmth, cold, taste pressure and vision. Channels that mediate these sensations include acid-sensing ion channels (ASICs) (Wang & Xu 2011, Qadri et al. 2012, Deval et al. 2010) and the transient receptor potential channels (TRPCs) (Takahashi et al. 2012, Numata et al. 2011 in "TRP Channels" Zhu, MX editor, CRC Press, 2011, Ramsey et al. 2006, Montell 2005). Many channels are sensitive to changes in calcium (Ca2+) levels, both inside and outside the cell. Examples are protein tweety homologs 2 and 3 (TTYH2, 3) (Suzuki 2006), bestrophins 1-4 (BEST1-4) (Sun et al. 2002, Tsunenari et al. 2003, Kunzelmann et al. 2009, Hartzell et al. 2008) and ryanodine receptor tetramers (RYRs) (Beard et al. 2009).
L-2-Hydroxyglutaric aciduria: identification of a mutant gene C14orf160, localized on chromosome 14q22.1
MagT transporters mediate magnesium uptake into cells
ZIP7 mediates zinc efflux from the endoplasmic reticulum
Cellular copper transport is mediated by human copper transporter 1 hCTR1
The accessory protein, Cks1 promotes efficient interaction between phosphorylated p27 and the SCF (Skp2) complex (Ganoth et al., 2001; Spruck et al., 2001). Cks1 binds to Skp2 in the leucine-rich repeat (LRR) domain and C-terminal tail (Hao et al., 2005). The phosphorylated Thr187 side chain of p27 associates with a phosphate binding site on Cks1, and the side chain containing Glu185 is positioned in the interface between Skp2 and Cks1 where it interacts with both (Hao et al., 2005).
ZnT8 transports zinc into the secretory vesicles of pancreatic beta cells specifically
SLC30A8 transports Zn2+ from cytosol to secretory granule
The E-type cyclins and Cyclin Dependent Kinase 2 control the transition from G1 to S phase. Cdk2 is competent to carry out the necessary reactions only when complexed with Cyclin E.
ZIP6 and ZIP14 mediate zinc influx into cells
Follow their formation, the Cyclin E:Cdk2 complexes are translocated to the nucleus.
Three D-type cyclins are essential for progression from G1 to S-phase. These D cyclins bind to and activate both CDK4 and CDK6. The formation of all possible complexes between the D-type cyclins and CDK4/6 is promoted by the proteins, p21(CIP1/WAF1) and p27(KIP1). The cyclin-dependent kinases are then activated due to phosphorylation by CAK. The cyclin dependent kinases phosphorylate the RB1 protein and RB1-related proteins p107 (RBL1) and p130 (RBL2). Phosphorylation of RB1 leads to release of activating E2F transcription factors (E2F1, E2F2 and E2F3). After repressor E2Fs (E2F4 and E2F5) dissociate from phosphorylated RBL1 and RBL2, activating E2Fs bind to E2F promoter sites, stimulating transcription of cell cycle genes, which then results in proper G1/S transition. The binding and sequestration of p27Kip may also contribute to the activation of CDK2 cyclin E/CDK2 cyclin A complexes at the G1/S transition (Yew et al., 2001).
Early cell cycle progression in G1 is under the control of the D-type cyclins together with Cdk4 and Cdk6. An important target for these CDKs is the Retinoblastoma (Rb) protein, which when phosphorylated promotes cell cycle progression by releasing E2F transcription factors that transactivate several important genes for later cell cycle events. The formation of Cyclin D - Cdk4/6 complexes is promoted by two proteins, p21Cip1/Waf1 and p27kip1, and their activity can be inhibited by the binding of several small CDK-inhibitory proteins (CKIs): p15INK4B, p16INK4A, p18INK4C and p19INK4D.
Phosphorylated p130 (RBL2) binds SCF (Skp2) ubiquitin ligase in complex with Cks1. Phosphorylation of p130 (RBL2) serine residue S672 by CDK4/6 is critical for this interaction.
As quiescent G0 cells reenter the cell cycle, p130 (RBL2) is phosphorylated by CDK4/6. This phosphorylated p130 (RBL2) binds ubiquitin ligase SCF (Skp2) in complex with Cks1, and is subsequently ubiquitinated and degraded similarly to p27, which is another target of SCF (Skp2).
Dephosphorylation of p107 (RBL1) by PP2A complex containing either PPP2R3B (B" beta) or PPP2R2A (B alpha) regulatory subunit plays a role in maintaining the equilibrium of hyperphosphorylated and hypophosphorylated p107 (RBL1), through counteracting action of cyclin dependent kinases (CDKs) throughout the cell cycle. It is assumed that PP2A dephosphorylates p107 (RBL1) on all four phosphorylation sites, but further experiments are needed to confirm this.
Dephosphorylation of p130 (RBL2) by PP2A complex containing either PPP2R3B (B" beta) or PPP2R2A (B alpha) regulatory subunit plays a role in maintaining the equilibrium of hyperphosphorylated and hypophosphorylated p130 (RBL2), through counteracting action of cyclin dependent kinases (CDKs). It is assumed that PP2A dephosphorylates p130 (RBL2) on all three phosphorylation sites, but further experiments are needed to confirm this.
In G0 and early G1 in quiescent cells, p130 (RBL2) bound to E2F4 or E2F5 and either DP1 or DP2, associates with the MuvB complex, forming an evolutionarily conserved DREAM complex, that represses transcription of cell cycle genes. During early G1 phase in actively cycling cells, p107 (RBL1) forms a complex with E2F4 and DP1 or DP2 and represses transcription of E2F target genes. Both p130 (RBL2) and p107 (RBL1) repress transcription of E2F targets through recruiting histone deacetylase HDAC1, possibly in complex with other chromatin modifying enzymes, to E2F-regulated promoters. Expression of p107 (RBL1) is cell cycle regulated, with its levels peaking in late G1 and S phase. Although p107 (RBL1) is phosphorylated by cyclin D assocaited kinases during late G1 phase, a small pool of p107 (RBL1) is thought to be present throughout G1 and S phase, and could be involved in fine tuning the transcription of S-phase genes. This is supported by studies showing that unlike RB1 and p130 (RBL2), which are able to induce G1 arrest when over-expressed, p107 (RBL1) over-expression can arrest the cell cycle in both G1 and S phase. For recent reviews on the function of p107, p130 and pocket proteins in general, please refer to Wirt and Sage, 2010, MacPherson 2008 and Cobrinik 2005.
Maple syrup urine disease (branched-chain ketoaciduria)
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1971-2005
Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1
ZnT6 transports zinc into the golgi apparatus
ZnT3 transports zinc into synaptic vesicles
ZnT5 transports zinc into secretory granules in pancreatic beta cells
DCT1 (NRAMP2) mediates divalent iron uptake across the apical membrane of enterocytes
ZnT2 facilitates zinc vesicular sequestration
NaDC3 co-transports the dicarboxylic acid succinate and three sodium ion
NACT co-transports trivalent citrate and a sodium ion
The transition from the G1 to S phase is controlled by the Cyclin E:Cdk2 complexes. As the Cyclin E:Cdk2 complexes are formed, the Cdk2 is phosphorylated by the Wee1 and Myt1 kinases. This phosphorylation keeps the Cdk2 inactive. In yeast this control is called the cell size checkpoint control. The dephosphorylation of the Cdk2 by Cdc25A activates the Cdk2, and is coordinated with the cells reaching the proper size, and with the DNA synthesis machinery being ready. The Cdk2 then phosphorylates G1/S specific proteins, including proteins required for DNA replication initiation. The beginning of S-phase is marked by the first nucleotide being laid down on the primer during DNA replication at the early-firing origins.Failure to appropriately regulate cyclin E accumulation can lead to accelerated S phase entry, genetic instability, and tumorigenesis. The amount of cyclin E protein in the cell is controlled by ubiquitin-mediated proteolysis (see Woo, 2003).This pathway has not yet been annotated in Reactome.
NaDC1 co-transports dicarboxylic acids and a sodium ion
E2F1 binds to E2F binding sites on the genome activating the synthesis of the target proteins. For annotation purposes, the reactions regulated by E2F1 are grouped under this pathway and information about the target genes alone are displayed for annotation purposes. Cellular targets for activation by E2F1 include thymidylate synthetase, Rir2, Dihydrofolate reductase, Cdc2, Cyclin A1, Cdc6 (DeGregori et al., 1995), Cdt1 (Yoshida and Inoue, 2004), CDC45 (Arata et al., 2000), CDC6 (Yan et al., 1998; Ohtani et al., 1998), Cyclin E (Ohtani et al., 1996), Emi1 (Hsu et al., 2002), and Orc1 (Ohtani et al., 1997). The activation of TK2 (Dnk1) and Cdc25A by E2F1 have been inferred from similar events in Drosophila (Duronio and O'Farrell, 1994;Reis and Edgar, 2004). Rir2 protein is involved in dNTP level regulation and activation of this enzyme results in higher levels of dNTPs in anticipation of S-phase. E2F activation of Rir2 has been shown also in Drosophila by Duronio and O'Farrell (1994). E2F1 activation of CDC45 is shown in mouse cells by using human E2F1 construct (Arata et al., 2000). Cyclin E is also transcriptionally regulated by E2F1. Cyclin E protein plays important role in the transition of G1 in S-phase by associating with Cdk2 (Ohtani et al., 1996). E2F activation of PCNA has been demonstrated in Drosophila (DeGregori et al., 1995) and in some human cells by using recombinant adenovirus constructs. E2F activation of Polymerase A (Pol A) has been demonstrated in some human cells. It has also been demonstrated in Drosophila by Ohtani and Nevins (1994). It has been observed in Drosophila that E2F1 regulated expression of Orc1 stimulates ORC1-6 complex formation and binding to the origin of replication (Asano and Wharton, 1999). Orc1-6 recruit Cdc6 and Cdt1 that are required to recruit the MCM2-7 replication helicases. E2F1 regulation incorporates a feedback mechanism where in Geminin can inhibit MCM2-7 recruitment of ORC1-6 complex by interacting with Cdc6/Cdt1. The activation of Cdc25A and TK2 (Dnk1) by E2F1 has been inferred from similar events in Drosophila (Duronio RJ, O'Farrell 1994; Reis and Edgar, 2004). E2F1 activates string (Cdc25) that in turn activates Cyclin B/Cdk1. A similar phenomenon has been observed in mouse NIH 3T3 cells and in Rat1 cells.
NaS2 co-transports sulphate and two sodium ions
NaS1 co-transports sulphate and a sodium ion
At the beginning of this reaction, 1 molecule of 'Cyclin E2:Cdk2 complex', and 1 molecule of 'ATP' are present. At the end of this reaction, 1 molecule of 'Cyclin E2:phospho-Cdk2 complex', and 1 molecule of 'ADP' are present. This reaction takes place in the 'nucleoplasm' and is mediated by the 'kinase activity' of 'Myt1 kinase'.
The Myc/Max heterodimer binds to elements in the cdc25A gene and activates transcription in mid to late G1.
Cdc25A dephosphorylates Cdk2 and activates cyclin E-Cdk2 and cyclin A-Cdk2 kinases (Blomberg and Hoffmann, 1999).
Phosphorylation of cyclin-dependent kinases (CDKs) by the CDK-activating kinase (CAK) is required for the activation of the CDK kinase activity. The association of p21/p27 with the Cyclin A/E:Cdk2 complex prevents CAK mediated phosphorylation of Cdk2 (Aprelikova et al., 1995).
Once in tight contact with the SCF (Skp2):Cks1 complex, phosphorylated p27/p21 is ubiquitinated.
Following ubiquitination by the SCF(Skp2):Cks1 complex, phospho-p27/p21 is degraded by the 26S proteasome.
During G1, the activity of cyclin-dependent kinases (CDKs) is kept in check by the CDK inhibitors (CKIs) p27 and p21, thereby preventing premature entry into S phase (see Guardavaccaro and Pagano, 2006). These two CKIs are degraded in late G1 phase by the ubiquitin pathway (Pagano et al., 1995; Bloom et al., 2003) involving the ubiquitin ligase SCF(Skp2) (Tsvetkov et al., 1999; Carrano et al., 1999; Sutterluty et al., 1999, Bornstein et al., 2003) and the cell-cycle regulatory protein Cks1 (Ganoth et al., 2001; Spruck et al 2001; Bornstein et al., 2003). Recognition of p27 by SCF(Skp2) and its subsequent ubiquitination is dependent upon Cyclin E/A:Cdk2- mediated phosphorylation at Thr 187 of p27 (Montagnoli et al., 1999). There is evidence that Cyclin A/B:Cdk1 complexes can also bind and phosphorylate p27 on Th187 (Nakayama et al., 2004). Degradation of polyubiquitinated p27 by the 26S proteasome promotes the activity of CDKs in driving cells into S phase. (Montagnoli et al., 1999; Tsvetkov et al., 1999, Carrano et al 1999). The mechanism of SCF(Skp2)-mediated degradation of p21 is similar to that of p27 in terms of its requirements for the presence of Cks1 and of Cdk2/cyclin E/A (Bornstein et al.,2003; Wang et al., 2005). In addition, as observed for p27, p21 phosphorylation at a specific site (Ser130) stimulates its ubiquitination. In contrast to p27, however, ubiquitination of p21 can take place in the absence of phosphorylation, although with less efficiency (Bornstein et al.,2003). SCF(Skp2)-mediated degradation of p27/p21 continues from late G1 through M-phase. During G0 and from early G1 to G1/S, Skp2 is degraded by the anaphase promoting complex/Cyclosome and its activator Cdh1 [APC/C(Cdh1)] (Bashir et al, 2004; Wei et al, 2004). The tight regulation of APC/C(Cdh1) activity ensures the timely elimination Skp2 and, thus, plays a critical role in controlling the G1/S transition. APC/C(Cdh1) becomes active in late M-phase by the association of unphosphorylated Cdh1 with the APC/C. APC/C(Cdh1) remains active until the G1/S phase at which time it interacts with the inhibitory protein, Emi1 (Hsu et al., 2002). Inhibition of APC/C(Cdh1) activity results in an accumulation of cyclins, which leads to the phosphorylation and consequently to a further inactivation of Cdh1 at G1/S (Lukas et al., 1999). Finally, to make the inactivation of APC/C(Cdh1) permanent, Cdh1 and its E2, namely Ubc10, are eliminated in an auto-ubiquitination event (Listovsky et al., 2004; Rape and Kirschner, 2004). At G1/S, Skp2 reaccumulates as Cdh1 is inactivated, thus allowing the ubiquitination of p21 and p27 and resulting in a further increase in CDK activity.
At the beginning of this reaction, 1 molecule of 'ATP', and 1 molecule of 'Cyclin E1:Cdk2 complex' are present. At the end of this reaction, 1 molecule of 'Cyclin E1:phospho-Cdk2 complex', and 1 molecule of 'ADP' are present. This reaction takes place in the 'nucleoplasm' and is mediated by the 'kinase activity' of 'Myt1 kinase'.
Bone morphogenetic protein receptor type IA
Na+-dependent monocarboxylate transport by SMCT
Proton-coupled di- and tri-peptide cotransport
Vesicular inhibitory amino acid transport
Retrovirally mediated complementation of the glyB phenotype. Cloning of a human gene encoding the carrier for entry of folates into mitochondria.
GLUT7 and GLUT11 transport glucose and fructose
GLUT9 transports glucose, fructose and urate
HMIT co-transports myo-inositol with a proton
Na+/I- cotransport (influx) by the Na+/I- symporter
Type I Na+-coupled phosphate co-transport
Wnts need a p(assport)24 to leave the ER
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 2125-2163
SLC17A5 cotransports lysosomal Neu5Ac and H+ to cytosol
SLC36A2-mediated uptake of glycine and proline
SLC6A14-mediated uptake of basic and neutral amino acids and of beta-alanine
SLC1A5-mediated exchange of glutamine and alanine across the plasma membrane
SLC36A1-mediated uptake of glycine, proline, and alanine
SLC6A19-mediated uptake of neutral amino acids
SLC7A9-mediated exchange of extracellular arginine, lysine, or cystine for cytosolic leucine
SLC1A5-mediated exchange of alanine and glutamine across the plasma membrane
Organic acidemias due to defects in lysine oxidation: 2-ketoadipic acidemia and glutaric acidemia
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 2195-2204
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1965-1970
Chk1 directly phosphorylates Cdc25A at Ser-123. Chk1 phosphorylation is required for cells to delay cell cycle progression in response to double-strand DNA breaks (Zhao et al., 2002).
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Aquaporins passively transport water out of cells
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Aquaporins passively transport water into cells
In adipocytes and myocytes insulin signaling causes intracellular vesicles carrying the GLUT4 (SLC2A4) glucose transporter to translocate to the plasma membrane, allowing the cells to take up glucose from the bloodstream (reviewed in Zaid et al. 2008, Leney and Tavare 2009, Bogan and Kandror 2010, Foley et al. 2011, Hoffman and Elmendorf 2011, Kandror and Pilch 2011). In myocytes muscle contraction alone can also cause translocation of GLUT4. Though the entire pathway leading to GLUT4 translocation has not been elucidated, several steps are known. Insulin activates the kinases AKT1 and AKT2. Muscle contraction activates the kinase AMPK-alpha2 and possibly also AKT. AKT2 and, to a lesser extent, AKT1 phosphorylate the RAB GTPase activators TBC1D1 and TBC1D4, causing them to bind 14-3-3 proteins and lose GTPase activation activity. As a result RAB proteins (probably RAB8A, RAB10, RAB14 and possibly RAB13) accumulate GTP. The connection between RAB:GTP and vesicle translocation is unknown but may involve recruitment and activation of myosins. Myosins 1C, 2A, 2B, 5A, 5B have all been shown to play a role in translocating GLUT4 vesicles near the periphery of the cell. Following docking at the plasma membrane the vesicles fuse with the plasma membrane in a process that depends on interaction between VAMP2 on the vesicle and SNAP23 and SYNTAXIN-4 at the plasma membrane.
The secretory membrane system allows a cell to regulate delivery of newly synthesized proteins, carbohydrates, and lipids to the cell surface, a necessity for growth and homeostasis. The system is made up of distinct organelles, including the endoplasmic reticulum (ER), Golgi complex, plasma membrane, and tubulovesicular transport intermediates. These organelles mediate intracellular membrane transport between themselves and the cell surface. Membrane traffic within this system flows along highly organized directional routes. Secretory cargo is synthesized and assembled in the ER and then transported to the Golgi complex for further processing and maturation. Upon arrival at the trans Golgi network (TGN), the cargo is sorted and packaged into post-Golgi carriers that move through the cytoplasm to fuse with the cell surface. This directional membrane flow is balanced by retrieval pathways that bring membrane and selected proteins back to the compartment of origin.
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After docking at the membrane VAMP2 on the vesicle interacts with SYNTAXIN-4 and SNAP23 on the plasma membrane to catalyze fusion of the vesicle with the plasma membrane. STXBP3 (MUNC18C) bound to STX4 prevents fusion until STXBP3 is phosphorylated.
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SLCO1B1, SLCO4A1 and SLCO1C1 mediate the transport of thyroid hormones
As inferred from mouse, GLUT4 (SLC2A4) initially translocates from endosomes to insulin-responsive vesicles (IRVs, GSVs). RAB11 appears to play a role in this process. IRVs bearing GLUT4 are then translocated across the cortical actin network to the plasma membrane. Myosins 2A, 2B, 5A, and 5B contribute to translocation and are presumed to be involved in this step. Myosin 1C appears to act close to the plasma membrane and may facilitate fusion of the vesicle with the plasma membrane. RAB:GTP complexes coupled to the vesicles may interact with myosins to regulate their activity.
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As inferred from mouse, AKT2 phosphorylates Myosin 5A on serine-1652. The phosphorylation promotes association of Myosin 5A with actin and ATPase activity of Myosin 5A.
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SLCO2B1 has a narrow substrate specificity
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RALA is a guanine nucleotide binding protein that hydrolyzes bound GTP to yield GDP and phosphate. RGC1 and RGC2 are GAPs (GTPase-activating proteins) that activate the GTPase activity of RALA. Insulin activates AKT, which phosphorylates RGC2, inactivating the GAP activity of RGC1:RGC2 and allowing RALA:GTP to accumulate.
SLCO4C1 mediates the transport of digoxin
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RALA releases GDP and binds GTP, producing the active form of RALA. The reaction is accelerated by guanine nucleotide exchange factors (GEFs) and opposed by GTPase-activating proteins (GAPs) which enhance the conversion of RALA:GTP back to RALA:GDP by activating the GTPase activity of RALA.
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SLC35B4 mediates the transport of UDP-N-acetylglucosamine into the Golgi lumen
As inferred from mouse, AKT2 (PKB-beta) phosphorylates RBC2 (RALGAPA2) on serine-486, serine-696, and threonine-715 in response to insulin. The phosphorylation prevents RBC1:RBC2 from activating RALA GTPase and allows RALA:GTP to accumulate.
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SLC35C1 mediates the transport of UDP-fucose into the Golgi lumen
RAB proteins have intrinsic weak GTPase activity that is enhanced by RAB-GTPase activating proteins (RAB-GAPs, Sano et al. 2007). The GTPase activity of RAB13 is inferred from other RAB proteins. AS160 (TBC1D4) and TBC1D1 are GAPs that activate the GTPase activity of RAB8A/10/13. Insulin signaling activates AKT, which phosphorylates and inactivates AS160 and TBC1D1, allowing GTP-bound (active) RABs to accumulate.
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SLC35D2 mediates the antiport of GDP-mannose in exchange for GMP
FATP1, 4 and 6 can mediate the influx of long chain fatty acids into cells
Zinc finger FYVE domain-containing protein 16
At the beginning of this reaction, 1 molecule of 'ATP', and 1 molecule of 'Chk2' are present. At the end of this reaction, 1 molecule of 'phospho-Chk2', and 1 molecule of 'ADP' are present. This reaction takes place in the 'nucleus' and is mediated by the 'kinase activity' of 'phospho-ATM (Ser 1981)'.
Cdc25C is negatively regulated by phosphorylation on Ser 216, the 14-3-3-binding site. This is an important regulatory mechanism used by cells to block mitotic entry under normal conditions and after DNA damage (Bulavin et al., 2003).
SLC35B4 mediates the transport of UDP-xylose into the Golgi lumen
Bone morphogenetic protein receptor type IB
SLC35A3 mediates the antiport of UDP-GlcNAc in exchange for UMP
SLC35A2 mediates the antiport of UDP-Gal and UDP-GalNAc in exchange for UMP
Mothers against decapentaplegic homolog 1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_255237.1
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In response to DNA damage due to exposure to ultraviolet light or to ionizing radiation, Cdc25A is phosphorylated by Chk1 or Chk2. The phosphorylation of Cdc25A at ser-123, in response to DNA damage from ionizing radiation is a signal for ubiquitination and subsequent degradation of Cdc25A. The destruction of Cdc25A prevents the normal G1/S transition. Cdc25A is required for the activation of the Cyclin E:Cdk2 complexes via dephosphorylation. Chk1 is activated in response to DNA damage due to uv light. However, the phosphorylation occurs at a different site.
AT1 transports acetyl-CoA into the Golgi lumen
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cdc25A protein is degraded by the ubiquitin-proteasome machinery in both terminally differentiating and cycling cells (Bernardi et al. 2000).
SLC35A1 mediates the antiport of CMP-sialic acid in exchange for CMP
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In the G1 phase there are two types of DNA damage responses, the p53-dependent and the p53-independent pathways. The p53-dependent responses inhibit CDKs through the up-regulation of genes encoding CKIs mediated by the p53 protein, whereas the p53-independent mechanisms inhibit CDKs through the inhibitory T14Y15 phosphorylation of Cdk2. Failure of DNA damage checkpoints in G1 leads to mutagenic replication of damaged templates and other replication defects.
Equilibrative transport (export) of adenosine and biogenic amines by solute carrier family 29 (nucleoside transporters), member 4
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The G1 arrest induced by DNA damage has been ascribed to the transcription factor and tumor suppressor protein p53. To be effective within minutes after DNA damage, induction of the G1 block should exploit transcription and protein synthesis independent mechanisms. Upon exposure to ultraviolet light (UV) or ionizing radiation (IR), the abundance and activity of a protein, Cdc25A, rapidly decreases; this DNA damage response is not dependent on p53. The rapid destruction of Cdc25A phosphatase prevents entry of a cell into S-phase, by maintaining the CyclinE:Cdk2 complexes in their T14Y15 phosphorylated form.
Equilibrative transport (import) of adenosine and biogenic amines by solute carrier family 29 (nucleoside transporters), member 4
p24 proteins are required for secretion of Wnt ligands
At the beginning of this reaction, 1 molecule of 'Ubiquitinated Phospho-Cdc25A' is present. At the end of this reaction, 1 molecule of 'Amino Acid' is present. This reaction takes place in the 'cytosol' and is mediated by the 'endopeptidase activity' of '26S proteasome'.
Equilibrative transport (export) of nucleosides and adenine by solute carrier family 29 (nucleoside transporters), member 3
Detection of DNA damage caused by ionizing radiation results in the phosphorylation of Cdc25A at Ser-123 by Chk2.
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Equilibrative transport (import) of nucleosides and adenine by solute carrier family 29 (nucleoside transporters), member 3
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Detection of DNA damage caused by ionizing radiation results in the phosphorylation of Cdc25A at Ser-123 by Chk1, inhibiting Cdc25A.
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At the beginning of this reaction, 1 molecule of 'ATP', and 1 molecule of 'Chk1' are present. At the end of this reaction, 1 molecule of 'phospho-Chk1', and 1 molecule of 'ADP' are present. This reaction takes place in the 'nucleus' and is mediated by the 'kinase activity' of 'phospho-ATM (Ser 1981)'.
Equilibrative transport (import) of nucleosides and free bases by solute carrier family 29 (nucleoside transporters), member 2
Equilibrative transport (export) of nucleosides and free bases by solute carrier family 29 (nucleoside transporters), member 1
Concentrative transport (import) of nucleosides plus sodium ions by solute carrier family 28 (sodium-coupled nucleoside transporter), member 2
In the sequestration model, the Mad2 molecules that dissociate from unattached kinetochores are perceived to bind to Cdc20, a protein that recruits specific substrates to the APC/C. Consequently, Mad2 indirectly inhibits the APC/C by sequestering its activator, Cdc20. This requires interaction between Mad1 and Mad2. Cdc20 and Mad1 bind to the same site on Mad2.
Equilibrative transport (import) of nucleosides and free bases by solute carrier family 29 (nucleoside transporters), member 1
Equilibrative transport (export) of nucleosides and free bases by solute carrier family 29 (nucleoside transporters), member 2
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Cdc25C is phosphorylated by Chk1 at ser-216 (Blasina et al.,1999 ) resulting in both inhibition of the Cdc25 phosphatase activity and creation of a 14-3-3 docking site (Peng et al., 1997). Association of 14-3-3 protein is believed to exclude Cdc25C from the nucleus via cytoplasmic retention of the Cdc25C:14-3-3 complex.
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The G2/M DNA replication checkpoint ensures that mitosis is not initiated until DNA replication is complete. If replication is blocked, the DNA replication checkpoint signals to maintain Cyclin B - Cdc2 complexes in their T14Y15 phosphorylated and inactive state. This prevents the phosphorylation of proteins involved in G2/M transition, and prevents mitotic entry. Failure of these checkpoints results in changes of ploidy: in the case of mitosis without completion of DNA replication, aneuploidy of <2C will result, and the opposite is true if DNA replication is completed more than once in a single cell cycle with an overall increase in ploidy. The mechanism by which unreplicated DNA is first detected by the cell is unknown.
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Myt1, which localizes preferentially to the endoplasmic reticulum and Golgi complex, phosphorylates Cdc2 on threonine 14 ( Liu et al., 1997).
Throughout the cell cycle, the genome is constantly monitored for damage, resulting either from errors of replication, by-products of metabolism or through extrinsic sources such as ultra-violet or ionizing radiation. The different DNA damage checkpoints act to inhibit or maintain the inhibition of the relevant CDK that will control the next cell cycle transition. The G2 DNA damage checkpoint prevents mitotic entry solely through T14Y15 phosphorylation of Cdc2 (Cdk1). Failure of the G2 DNA damage checkpoint leads to catastrophic attempts to segregate unrepaired chromosomes.
Carnitine transporters mediates sodium-dependent uptake of carnitine
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DNA damage induced activation of the checkpoint kinases Chk1/Chk2(Cds1) results in the conversion and/or maintenance of CyclinB:Cdc2 complex in its Tyrosine 15 phosphorylated (inactive) state. Cdc2 activity is regulated by a balance between the phosphorylation and dephosphorylation by the Wee1/Myt1 kinase and Cdc25 phosphatase. Inactivation of the Cyclin B:Cdc2 complex likely involves both inactivation of Cdc25 and/or stimulation of Wee1/Myt1 kinase activity.
ORCTL2 mediates the transport of chloroquine and quinidine with efflux of protons
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G2/M checkpoints include the checks for damaged DNA, unreplicated DNA, and checks that ensure that the genome is replicated once and only once per cell cycle. If cells pass these checkpoints, they follow normal transition to the M phase. However, if any of these checkpoints fail, mitotic entry is prevented by specific G2/M checkpoint events. The G2/M checkpoints can fail due to the presence of unreplicated DNA or damaged DNA. In such instances, the cyclin-dependent kinase, Cdc2(Cdk1), is maintained in its inactive, phosphorylated state, and mitotic entry is prevented. Events that ensure that origins of DNA replication fire once and only once per cell cycle are also an example of a G2/M checkpoint. In the event of high levels of DNA damage, the cells may also be directed to undergo apopotosis (not covered).
OAT1-3 transport organic anions with antiport of dicarboxylic acids
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Genotoxic stress caused by DNA damage or stalled replication forks can lead to genomic instability. To guard against such instability, genotoxically-stressed cells activate checkpoint factors that halt or slow cell cycle progression. Among the pathways affected are DNA replication by reduction of replication origin firing, and mitosis by inhibiting activation of cyclin-dependent kinases (Cdks). A key factor involved in the response to stalled replication forks is the ATM- and rad3-related (ATR) kinase, a member of the phosphoinositide-3-kinase-related kinase (PIKK) family. Rather than responding to particular lesions in DNA, ATR and its binding partner ATRIP (ATR-interacting protein) sense replication fork stalling indirectly by associating with persistent ssDNA bound by RPA. These structures would be formed, for example, by dissociation of the replicative helicase from the leading or lagging strand DNA polymerase when the polymerase encounters a DNA lesion that blocks DNA synthesis. Along with phosphorylating the downstream transducer kinase Chk1 and the tumor suppressor p53, activated ATR modifies numerous factors that regulate cell cycle progression or the repair of DNA damage. The persistent ssDNA also stimulates recruitment of the RFC-like Rad17-Rfc2-5 alternative clamp-loading complex, which subsequently loads the Rad9-Hus1-Rad1 complex onto the DNA. The latter '9-1-1' complex serves to facilitate Chk1 binding to the stalled replication fork, where Chk1 is phosphorylated by ATR and thereby activated. Upon activation, Chk1 can phosphorylate additional substrates including the Cdc25 family of phosphatases (Cdc25A, Cdc25B, and Cdc25C). These enzymes catalyze the removal of inhibitory phosphate residues from cyclin-dependent kinases (Cdks), allowing their activation. In particular, Cdc25A primarily functions at the G1/S transition to dephosphorylate Cdk2 at Thr 14 and Tyr 15, thus positively regulating the Cdk2-cyclin E complex for S-phase entry. Cdc25A also has mitotic functions. Phosphorylation of Cdc25A at Ser125 by Chk1 leads to Cdc25A ubiquitination and degradation, thus inhibiting DNA replication origin firing. In contrast, Cdc25B and Cdc25C regulate the onset of mitosis through dephosphorylation and activation of Cdk1-cyclin B complexes. In response to replication stress, Chk1 phosphorylates Cdc25B and Cdc25C leading to Cdc25B/C complex formation with 14-3-3 proteins. As these complexes are sequestered in the cytoplasm, they are unable to activate the nuclear Cdk1-cyclin B complex for mitotic entry. These events are outlined in the figure. Persistent single-stranded DNA associated with RPA binds claspin (A) and ATR:ATRIP (B), leading to claspin phosphorylation (C). In parallel, the same single-stranded DNA:RPA complex binds RAD17:RFC (D), enabling the loading of RAD9:HUS1:RAD1 (9-1-1) complex onto the DNA (E). The resulting complex of proteins can then repeatedly bind (F) and phosphorylate (G) CHK1, activating multiple copies of CHK1.
OAT2 and OAT4 mediate transport of sulphate conjugates
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Phosphorylation of Cdc25C at Ser 216 results in both the inhibition of Cdc25C phosphatase activity and the creation of a 14-3-3 docking site (Peng et al. 1997).
Concentrative transport (import) of a nucleoside and a sodium ions by solute carrier family 28 (sodium-coupled nucleoside transporter), member 1
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The 9-1-1 complex is a heterotrimeric ring-shaped structure that is loaded onto DNA by the Rad17-RFC complex. In vitro studies indicate that loading is preferred onto DNA substrates containing ssDNA gaps that presumably resemble structures found upon replication fork stalling and DNA polymerase/helicase uncoupling. The Rad17-RFC and 9-1-1 complexes are structurally similar to the RFC (replication factor C) clamp loader and PCNA sliding clamp, respectively, and similar mechanisms are thought to be used during loading of the 9-1-1 complex and PCNA. Upon loading, the 9-1-1 complex can recruit Chk1 onto sites of replication fork uncoupling or DNA damage. The purified Rad17 and Rad9-Hus1-Rad1 (9-1-1) complexes can form a stable co-complex in the presence of ATP, using Rad17-Rad9 interactions. From computer modeling studies, the Rad17 subunit of the complex is also proposed to interact with the C-terminus of Rad1, p36 with the C-terminus of Hus1, and p38 with the C-terminus of Rad9. A major known function of the 9-1-1 complex is to recruit Chk1 to stalled replication forks for activation by ATR. However, the presence of the 9-1-1 complex also alters the ability of Rad17 to become phosphorylated, perhaps suggesting that 9-1-1 may regulate the recruiment of additional ATR substrates. The 9-1-1 complex has also been found to interact with base excision repair factors human DNA polymerase beta, flap endonuclease FEN1, and the S. pombe MutY homolog (SpMYH), indicating that 9-1-1 also plays a direct role in DNA repair.
Concentrative transport (import) of a nucleoside and two sodium ions by solute carrier family 28 (sodium-coupled nucleoside transporter), member 3
OCT3 mediates renal uptake of organic cations
OCT3 mediates renal clearance of organic cations
OCT2 mediates tubular secretion of organic cations in the kidney
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OCT2 mediates tubular uptake of organic cations in the kidney
OCT4 mediates transport of ergothioneine
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The mitotic checkpoint or spindle assembly checkpoint is an evolutionarily conserved mechanism that ensures that cells with misaligned chromosomes do not exit mitosis and divide to form aneuploid cells. As chromosome attachment to the spindle microtubules is a stochastic process, not all chromosomes achieve alignment at the spindle equator at the same time. It is therefore essential that even a single unaligned chromosome can prevent the onset of anaphase. The ability of the checkpoint to monitor the status of chromosome alignment is achieved by assigning checkpoint proteins to the kinetochore, a macromolecular complex that resides at centromeres of chromosomes that establishes connections with spindle microtubules. The checkpoint proteins monitor, in an unknown way, the mechanical activities between kinetochore-associated proteins and microtubules. Defects in mechanical activities at kinetochores activate the resident checkpoint proteins to initiate a signal that is amplified throughout the cell that ultimately prevents the activation of the proteolytic process that is required for sister chromatid separation and the onset of anaphase. Kinetochores of unaligned chromosomes differ from those of aligned chromosomes in two ways. Kinetochores of aligned chromosomes are saturated with between 20 to 30 microtubules. In addition, poleward directed forces exerted at each sister kinetochore generates tension between them. Unaligned kinetochores on the other hand, are not saturated with microtubules and are not under tension. The mitotic checkpoint detects the presence of unattached kinetochores rather than monitoring for the presence of attached kinetochores. Consequently, unattached kinetochores emit an inhibitory signal that inhibits the biochemical events that are required to initiate the onset of anaphase. The mechanism by which this inhibitory signal is generated at unattached kinetochores has not precisely been determined but the signal is generated as a result of the lack of microtubule occupancy and kinetochore tension. A single unattached kinetochore is capable of preventing cells from exiting mitosis. The mitotic checkpoint provides a way for a localized defect to affect the global biochemical status of the cell. In principle, the signal that is generated at an unattached kinetochore diffuses throughout the cell to affect its target. There are currently two models for how this is achieved. One model is based on the observation that the Mad2 checkpoint protein binds and is rapidly released from unattached kinetochores. The kinetochore is believed to act as a catalyst that converts Mad2 into an inhibitory state that diffuses throughout the cell upon its release from the kinetochore. A second model proposes that the signal is amplified by a kinase cascade much like a conventional signal transduction pathway. This kinase cascade is believed to be comprised of the checkpoint kinases, hBUBR1, hBUB1, hMPS1.
The target of the mitotic checkpoint is the Anaphase Promoting Complex/Cyclosome (APC/C) an E3 ubiquitin ligase that targets proteins whose destruction is essential for mitotic exit. Currently, there are two proposed mechanism by which inhibition of the APC/C is achieved. These mechanisms differ depending on the mechanism of signal transduction. The APC/C may be inhibited directly by association with the Mitotic Checkpoint Complex (MCC) or through the sequestration of its activator, Cdc20.
DREAM complex is evolutionarily conserved and is reponsible for transcriptional repressession of cell cycle-regulated genes in G0 and early G1.
Physiology and pathophysiology of vascular signaling controlled by guanosine 3',5'-cyclic monophosphate-dependent protein kinase [corrected]
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A hallmark of the human cell cycle in normal somatic cells is its precision. This remarkable fidelity is achieved by a number of signal transduction pathways, known as checkpoints, which monitor cell cycle progression ensuring an interdependency of S-phase and mitosis, the integrity of the genome and the fidelity of chromosome segregation. Checkpoints are layers of control that act to delay CDK activation when defects in the division program occur. As the CDKs functioning at different points in the cell cycle are regulated by different means, the various checkpoints differ in the biochemical mechanisms by which they elicit their effect. However, all checkpoints share a common hierarchy of a sensor, signal transducers, and effectors that interact with the CDKs. The stability of the genome in somatic cells contrasts to the almost universal genomic instability of tumor cells. There are a number of documented genetic lesions in checkpoint genes, or in cell cycle genes themselves, which result either directly in cancer or in a predisposition to certain cancer types. Indeed, restraint over cell cycle progression and failure to monitor genome integrity are likely prerequisites for the molecular evolution required for the development of a tumor. Perhaps most notable amongst these is the p53 tumor suppressor gene, which is mutated in >50% of human tumors. Thus, the importance of the checkpoint pathways to human biology is clear.
p130 (RBL2) in complex with E2F4 or E2F5 and DP1 or DP2 recruits histone deacetylase HDAC1, probably in complex with other chromatin modification factors, and represses transcription of E2F target promoters during G0 in quiescent cells.
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p107 (RBL1) in complex with E2F4 and DP1 or DP2 recruits histone deacetylase HDAC1 (possibly in complex with other chromatin modification proteins) through LXCXE-like motif, shared by pocket proteins, to repress transcription of E2F target genes in early G1.
p107 (RBL1) in complex with E2F4 and DP1/2 binds to cyclin A or cyclin E in complex with CDK2 through its conserved LFG pocket domain motif and amino terminus, leading to inhibition of CDK2 kinase activity and suppression of cellular growth.
OCT1 transports organic cations into hepatic cells
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p107 (RBL1) is able to bind complexes of CDK2 with either cyclin A or cyclin E, through cyclin-binding LFG motif in the pocket domain, which is conserved in p130 (RBL2) and p21/WAF1/Cip1 family of cyclin-dependent kinase inhibitors. In addition to the LFG motif, the amino terminal sequence conserved in the p107 (RBL1) and p130 (RBL2) is needed for inhibition of CDK2 kinase activity. Presence of E2F is not required for this interaction.
OCT1 transports organic cations out of hepatic cells
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p130 (RBL2) in complex with E2F4/5 and DP1/2 binds to cyclin A or cyclin E in complex with CDK2 through its conserved LFG pocket domain motif and amino terminus, leading to inhibition of CDK2 kinase activity and suppression of cellular growth.
VMAT1/2 can mediate the transport of biogenic amines
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p130 (RBL2) is able to bind complexes of CDK2 with either cyclin A or cyclin E through the cyclin-binding LFG motif within the pocket domain, which is conserved in p107 (RBL1) and p21/WAF1/Cip1 family of cyclin-dependent kinases. In addition to LFG motif, amino terminal region of p130 (RBL2), conserved in p107 (RBL1), is necessary for inhibition of CDK2 kinase activity. Presence of E2F is not required for this interaction.
Sodium- and chloride-dependent choline transport by CHT
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The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1857-1895
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The renal plumbing system: aquaporin water channels
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The solution structure of the guanine nucleotide exchange domain of human elongation factor 1beta reveals a striking resemblance to that of EF-Ts from Escherichia coli
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Important role of cathepsin S in generating peptides for TAP-independent MHC class I crosspresentation in vivo
Muscle glycogenosis with low phosphorylase kinase activity: mutations in PHKA1, PHKG1 or six other candidate genes explain only a minority of cases
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Disorders of proline and hydroxyproline metabolism
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1821-1838
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Mammalian Orc1 protein is selectively released from chromatin and ubiquitinated during the S-to-M transition in the cell division cycle.
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Essential role for IKK? in production of type 1 interferons by plasmacytoid dendritic cells
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BNaC1 and BNaC2 constitute a new family of human neuronal sodium channels related to degenerins and epithelial sodium channels
Proc. Natl. Acad. Sci. U.S.A. 94:1459-64
Molecular cloning of genomic DNA and chromosomal assignment of the gene for human aromatic L-amino acid decarboxylase, the enzyme for catecholamine and serotonin biosynthesis
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HIF-alpha (HIF1A, HIF2A (EPAS1), HIF3A) is translocated to the nucleus, possibly by two pathways: importin 4/7 (Chachami et al. 2009) and importin alpha/beta (Depping et al. 2008). Once in the nucleus HIF-alpha heterodimerizes with HIF-beta (ARNT) (Wang et al. 1995, Jiang et al. 1996, Tian et al. 1997, Gu et al. 1998, Erbel et al. 2003) and recruits CBP and p300 to promoters of target genes (Ebert and Bunn 1998, Kallio et al. 1998, Ema et al. 1999, Gu et al. 2001, Dames et al. 2002, Freedman et al. 2002).
In the presence of oxygen members of the transcription factor family HIF-alpha, comprising HIF1A, HIF2A (EPAS1), and HIF3A, are hydroxylated on proline residues by PHD1 (EGLN2), PHD2 (EGLN1), and PHD3 (EGLN3) and on asparagine residues by HIF1AN (FIH) (reviewed in Pouyssegur et al. 2006, Semenza 2007, Kaelin and Ratcliffe 2008, Nizet and Johnson 2009, Brahimi-Horn and Pouyssegur 2009, Majmundar et al. 2010, Loenarz and Schofield 2011). Both types of reaction require molecular oxygen as a substrate and it is probable that at least some HIF-alpha molecules carry both hydroxylated asparagine and hydroxylated proline (Tian et al. 2011). Hydroxylated asparagine interferes with the ability of HIF-alpha to interact with p300 and CBP while hydroxylated proline facilitates the interaction of HIF-alpha with the E3 ubiquitin ligase VHL, causing ubiquitination and proteolysis of HIF-alpha. Hypoxia inhibits both types of hydroxylation, resulting in the stabilization of HIF-alpha, which then enters the nucleus, binds HIF-beta, and recruits p300 and CBP to activate target genes such as EPO and VEGF.
SOD3 is secreted from cells into the extracellular region. Before secretion a portion of SOD3 molecules are cleaved near the C-terminus at glutamate-227 (glutamate-209 in the mature protein) (Olsen et al. 2004, Karlsson et al. 1993). Removal of the C-terminus prevents interaction with the extracellular matrix so cleaved molecules are soluble. Cleaved and uncleaved molecules are believed to be capable of forming mixed tetramers (Sandstrom et al. 1993).
As inferred from the cytosolic reaction and from the mitochondrial reaction in mouse, Copper chaperone of superoxide dismutase (CCS) transfers a copper(I) atom to a SOD1 monomer that already contains a Zn atom. After initial heterodimerization between SOD1 and CCS, the copper atom is transferred, intramolecular cysteine disulfide bonds are formed in SOD1, and SOD1 dimerizes.
A portion of SOD1 is located in the mitochondrial intermembrane space (IMS) where it catalyzes the formation of oxygen (O2) and hydrogen peroxide (H2O2) from superoxide (O2.-) (He et al. 2011, Higgins et al. 2002, inferred from rat in Okado-Matsumoto and Fridovich 2001).
Cu-Zn superoxide dismutase (SOD1), originally known as erythrocuprein, catalyzes the reaction of two molecules of superoxide (O2.-) to yield one molecule of hydrogen peroxide (H2O2) and one molecule of oxygen (O2) (McCord and Fridovich 1969 assayed both bovine and human Cu-Zn superoxide dismutase, the human sample provided by Carrico and Deutsch). Diffusion of hydrogen peroxide, the product of SOD1, across the cytosol is limited (Mishina et al. 2011)
Copper chaperone of superoxide dismutase (CCS) transfers a copper(I) atom to a SOD1 monomer that already contains a Zn atom (Culotta et al. 1997, Casareno et al. 1998, Rae et al. 2001, Brown et al. 2004, Banci et al. 2012). The reaction proceeds by a two step mechanism in which SOD1 first forms heterodimers with CCS (Rae et al. 2001, Banci et al. 2012).
Oxygen plays a central role in the functioning of human cells: it is both essential for normal metabolism and toxic. To begin the annotation of stress responses in Reactome, we have annotated one aspect of cellular responses to oxygen (Semenza 2004), the role of hypoxia-inducible factor in regulating cellular transcriptional responses to changes in oxygen availability.
As inferred from the cytosolic reaction and from the mouse mitochondrial reaction, Copper chaperone of superoxide dismutase (CCS) transfers a copper(I) atom to a SOD1 monomer that already contains a Zn atom. The reaction proceeds by a two step mechanism in which SOD1 first forms heterodimers with CCS. The amounts of CCS and SOD1 in the intermembrane space appear to be regulated by the concentration of oxygen. Mutations in SOD1 are responsible for familial amyotrophic lateral sclerosis (fALS) and cause unregulated localization and aggregation of SOD1 in the intermembrane space (reviewed in Kawamata and Manfredi 2010).
Copper chaperone of superoxide dismutase (CCS) transfers a copper(I) atom to a SOD1 monomer that already contains a Zn atom. After initial heterodimerization between SOD1 and CCS, the copper atom is transferred, intramolecular cysteine disulfide bonds are formed in SOD1, and SOD1 dimerizes (Banci et al. 2012, Casareno et al. 1998, Culotta et al. 1997, Rae et al. 2001, Brown et al. 2004, Carroll et al. 2006, Kawamata and Manfredi 2008). The transfer of copper to SOD1 requires oxygen but it is unknown at which step the oxygen acts (Brown et al. 2004). There is also a CCS-independent, oxygen-independent pathway of maturation of SOD1 (Leitch et al. 2009) whose molecular details and physiological role are not well characterized.
Extracellular Cu-Zn superoxide dismutase (SOD3) catalyzes the reaction of two molecules of superoxide (O2.-) to form one molecule of oxygen (O2) and one molecule of hydrogen peroxide (H2O2) (Marklund et al. 1982, Marklund 1982)
As inferred from rat heart mitochondria, hydrogen peroxide is released from mitochondria at a rate that is dependent on the membrane potential. Knockdown of Aquaporin-8 (AQP8) in human cells indicates that hydrogen peroxide is able to transit through the water channel of AQP8 located in the inner mitochodrial membrane (Marchissio et al. 2012). The resulting level of cytosolic hydrogen peroxide is hypothesized to signal the state of the mitochondria to regulatory molecules in the cytosol and nucleus (reviewed in Antico Arciuch et al. 2012).
Mn superoxide dismutase (SOD2) is located in the mitochondrial matrix where it catalyzes the reaction of two molecules of superoxide (O2-.) to form one molecule of oxygen (O2) and one molecule of hydrogen peroxide (H2O2). Data from mouse liver indicate that respiratory complex I leaks superoxide into the matrix and respiratory complex III leaks superoxide into both the matrix and the intermembrane space (Muller et al. 2004). Because of its negative charge superoxide is unable to cross membranes, however hydrogen peroxide, a product of SOD2, is released from mitochondria to the cytosol in proportion to the proton potential (inferred from rat heart mitochondria in Boveris et al. 2006, Korshunov et al. 1997).
Glutathione peroxidase 7 (GPX7) and GPX8 are atypical glutathione peroxidases that catalyze the peroxidation of protein disulfide isomerases, such as PDI (P4HB) (Nguyen et al. 2011 and inferred from mouse in Bosello-Travain et al. 2013). GPX7 and GPX8 are each able to form heterodimers with the sulfhydryl oxidase ERO1alpha (ERO1L) in the endoplasmic reticulum lumen. It is hypothesized that GPX7 and GPX8 use hydrogen peroxide produced by ERO1L.
Peroxiredoxin 1 (PRDX1), PRDX2, and PRDX5 in the cytosol reduce hydrogen peroxide (H2O2) with thioredoxin yielding oxidized thioredoxin and water (Yamashita et al. 1999, Lee et al. 2007, Nagy et al. 2011).
Superoxide can reduce cytochrome c in the intermembrane space (Wegerich et al. 2013, and inferred from other mammals in Butler et al. 1975, Koppenol et al. 1976, Butler et al. 1982). Superoxide has been shown in rat and mouse mitochondria to be released into the intermembrane space by the complex III of the respiratory chain (Han et al. 2001, Muller et al. 2004).
Thioredoxin reductase 2 (TXNRD2) in the mitochondrial matrix regenerates reduced thioredoxin (TXN) by reacting oxidized thioredoxin with NADPH (Gasdaska et al. 1999, Cao et al. 2007).
Peroxiredoxin 3 (PRDX3) and PRDX5 in the mitochondrial matrix reduce hydrogen peroxide (H2O2) with thioredoxin to yield oxidized thioredoxin and water (Yamashita et al. 1999, Knoops et al. 1999, Cao et al. 2007, Nagy et al. 2011). Reduced PRDX5 is a monomer (Declercq et al. 2001) and oxidized PRDX5 is a dimer (Evrard et al. 2004) therefore the enzyme may cycle between states.
Glutathione peroxidase 3 (GPX3) in plasma reduces hydrogen peroxide (H2O2) with glutathione to yield oxidized glutathione and water (Maddipati and Marnett 1987, Takahashi et al. 1987, Chung et al. 2009, Ottaviano et al. 2009). Glutathione is synthesized in the liver and exported into the plasma.
Glutathione reductase (GSR) in the mitochondrial matrix regenerates reduced glutathione from oxidized glutathione and NADPH (Berkholz et al. 2008).
Two distinct disulfide bonds formed in human heat shock transcription factor 1 act in opposition to regulate its DNA binding activity
The ability of HSF1 to respond to cellular stresses is under negative regulation by chaperones, modulation of nucleocytoplasmic shuttling, post-translational modifications and transition from monomeric to trimeric state.
Sirtuin 1 (SIRT1) functions as a NAD(+)-dependent deacetylase, which regulates the heat shock response through deacetylation of HSF1 at Lys80. The acetylation at Lys80, which is located within DNA binding domain of HSF1 disrupts HSF1 DNA-binding ability. SIRT1-mediated stress-inducible regulation of HSF1 results in prolonged HSF1 binding to the heat shock promoter of hsp70 gene. The mechanism of the enzymatic reaction which couples NAD(+) hydrolysis with lysine deacetylation in the presence of acetylated peptide is described by several groups (Landry J et al. 2000; Sauve AA et al. 2001)
When in reduced form, TXN (thioredoxin) binds the amino terminus of MAP3K5 (ASK1) and inhibits its kinase activity. Once reactive oxygen species (ROS) oxidize TXN, TXN dissociates from MAP3K5, enabling MAP3K5 to phosphorylate downstream targets (Saitoh et al. 1998). Increased expression and activity of MINK1 (MINK) (and possibly other Ste20 family kinases TNIK and MAP4K), which is induced by ROS generated as a consequence of oncogenic RAS signaling, may contribute to MAP3K5 activation (Nicke et al. 2005).
In response to exposure to elevated temperature and certain other proteotoxic stimuli (e.g., hypoxia, free radicals) cells activate a number of cytoprotective mechanisms known collectively as "heat shock response". Major aspects of the heat shock response (HSR) are evolutionarily conserved events that allow cells to recover from protein damage induced by stress (Liu XD et al. 1997; Voellmy R & Boellmann F 2007; Shamovsky I & Nudler E 2008; Anckar J & Sistonen L 2011). The main hallmark of HSR is the dramatic alteration of the gene expression pattern. A diverse group of protein genes is induced by the exposure to temperatures 3-5 degrees higher than physiological. Functionally, most of these genes are molecular chaperones that ensure proper protein folding and quality control to maintain cell proteostasis. At the same time, heat shock-induced phosphorylation of translation initiation factor eIF2alpha leads to the shutdown of the nascent polypeptide synthesis reducing the burden on the chaperone system that has to deal with the increased amount of misfolded and thermally denatured proteins (Duncan RF & Hershey JWB 1989; Sarkar A et al. 2002; Spriggs KA et al. 2010). The induction of HS gene expression primarily occurs at the level of transcription and is mediated by heat shock transcription factor HSF1(Sarge KD et al. 1993; Baler R et al. 1993). Human cells express five members of HSF protein family: HSF1, HSF2, HSF4, HSFX and HSFY. HSF1 is the master regulator of the heat inducible gene expression (Zuo J et al. 1995; Akerfelt M et al. 2010). HSF2 is activated in response to certain developmental stimuli in addition to being co-activated with HSF1 to provide promoter-specific fine-tuning of the HS response by forming heterotrimers with HSF1 (Ostling P et al. 2007; Sandqvist A et al. 2009). HSF4 lacks the transcription activation domain and acts as a repressor of certain genes during HS (Nakai A et al. 1997; Tanabe M et al. 1999; Kim SA et al. 2012). Two additional family members HSFX and HSFY, which are located on the X and Y chromosomes respectively, remain to be characterized (Bhowmick BK et al. 2006; Shinka T et al. 2004; Kichine E et al. 2012). Under normal conditions HSF1 is present in both cytoplasm and nucleus in the form of an inactive monomer. The monomeric state of HSF1 is maintained by an intricate network of protein-protein interactions that include the association with HSP90 multichaperone complex, HSP70/HSP40 chaperone machinery, as well as intramolecular interaction of two conserved hydrophobic repeat regions. Monomeric HSF1 is constitutively phosphorylated on Ser303 and Ser 307 by (Zou J et al. 1998; Knauf U et al. 1996; Kline MP & Moromoto RI 1997; Guettouche T et al. 2005). This phosphorylation plays an essential role in ensuring cytoplasmic localization of at least a subpopulation of HSF1 molecules under normal conditions (Wang X et al. 2004). Exposure to heat and other proteotoxic stimuli results in the release of HSF1 from the inhibitory complex with chaperones and its subsequent trimerization, which is promoted by its interaction with translation elongation factor eEF1A1 (Baler R et al. 1993; Shamovsky I et al. 2006; Herbomel G et al 2013). The trimerization is believed to involve intermolecular interaction between hydrophobic repeats 1-3 leading to the formation of a triple coil structure. Additional stabilization of the HSF1 trimer is provided by the formation of intermolecular S-S bonds between Cys residues in the DNA binding domain (Lu M et al.2008). Trimeric HSF1 is predominantly localized in the nucleus where it binds the specific sequence in the promoter of hsp genes (Sarge KD et al. 1993; Wang Y and Morgan WD 1994). The binding sequence for HSF1 (HSE, heat shock element) contains series of inverted repeats nGAAn in head-to-tail orientation, with at least three elements being required for the high affinity binding. Binding of the HSF1 trimer to the promoter is not sufficient to induce transcription of the gene (Cotto J et al. 1996). In order to do so, HSF1 needs to undergo inducible phosphorylation on specific Ser residues such as Ser230, Ser326. This phosphorylated form of HSF1 trimer is capable of increasing the promoter initiation rate. HSF1 bound to DNA promotes recruiting components of the transcription mediator complex and relieving promoter-proximal pause of RNA polymerase II through its interaction with TFIIH transcription factor (Yuan CX & Gurley WB 2000). HSF1 activation is regulated in a precise and tight manner at multiple levels (Zuo J et al. 1995; Cotto J et al. 1996). This allows fast and robust activation of HS response to minimize proteotoxic effects of the stress. The exact set of HSF1 inducible genes is probably cell type specific. Moreover, cells in different pathophysiological states will display different but overlapping profile of HS inducible genes.
Surtuin 1 (SIRT1) has been shown to bind HSF1 and to function as a regulator of HSF1 DNA binding activity by controling the acetylation status of HSF1 (Westerheide SD et al 2009). SIRT1 mediates NAD(+)-dependent protein deacetylation.
Phosphorylation on Ser-121 inhibits transactivation and promotes HSP90 binding
Nuclear factor 1 (NF1) affects accurate termination and multiple-round transcription by human RNA polymerase III.
Reactive oxygen species (ROS) generated as a consequence of oncogenic RAS signaling induce expression and activation of Ste20 family kinases MINK1 (MINK), TNIK and, possibly, MAP4K4, which contributes to growth arrest and cellular senescence (Nicke et al. 2005).
MAP3K5 (ASK1) phosphorylates and activates MAP2K3 (MKK3) and MAP2K6 (MKK6) (Ichijo et al. 1997). A conserved docking site, DVD, at the C-terminus of MAP2K3 and MAP2K6 is needed for the interaction with MAP3K5 and MAP3K5-mediated activation (Takekawa et al. 2005).
The p38 activators MKK3 and MKK6 were present in both the nucleus and the cytoplasm, consistent with a role in activating p38 in the nucleus.
The MAPK level components of this cascade are p38MAPK-alpha, -beta, -gamma and -sigma. All of those isoforms are activated by phosphorylation of the Thr and Tyr in the Thr-Gly-Tyr motif in their activation loops.
MAPK14 (p38 alpha) and MAPK11 (p38 beta) phosphorylate MAPKAPK5 (PRAK) on threonine residue 182, located in the conserved LMTP site in the T-loop of the kinase domain. Phosphorylation of T182 is necessary for the MAPKAPK5 catalytic activity (New et al. 1998).
MAPKAPK5 (PRAK) forms a complex with MAPK14 (p38 alpha) or MAPK11 (p38 beta) irrespective of the phosphorylation status and kinase activity of MAPKAPK5, MAPK14 and MAPK11 (New et al. 2003). Phosphorylation of p38 alpha and p38 beta by MKK3 or MKK6 (Raingeaud et al. 1996), however, is required for the subsequent activation of MAPKAPK5 by p38 MAPK (New et al. 1998, Sun et al. 2007).
JNK (c-Jun N-terminal Kinase) phosphorylates several transcription factors including c-Jun after translocation to the nucleus.
c-Jun NH2 terminal kinase (JNK) plays a role in conveying signals from the cytosol to the nucleus, where they associate and activate their target transcription factors.
Activated human JNK kinases (MKK4 and MKK7) phosphorylate Thr183 and Tyr185 residues in the characteristic Thr-Pro-Tyr phosphoacceptor loop of each JNK. JNK is differentially regulated by MKK4 and MKK7 depending on the stimulus. MKK7 is the primary activator of JNK in TNF, LPS, and PGN responses. However, TLR3 cascade requires both MKK4 and MKK7. Some studies reported that in three JNK isoforms tested MKK4 shows a striking preference for the tyrosine residue (Tyr-185), and MKK7 a striking preference for the threonine residue (Thr-183).
MAP3K5 (ASK1) phosphorylates and activates MAP2K4 (SEK1) (Ichijo et al. 1997). MAP3K5-mediated phosphorylation of MAP2K4 may be facilitated by MAPK8IP3 (JSAP1) (Matsuura et al. 2002).
Human p38 MAPK alpha forms a complex with MK2 even when the signaling pathway is not activated. This heterodimer is found mainly in the nucleus. The crystal structure of the unphosphorylated p38alpha-MK2 heterodimer was determined. The C-terminal regulatory domain of MK2 binds in the docking groove of p38 MAPK alpha, and the ATP-binding sites of both kinases are at the heterodimer interface (ter Haar et al. 2007). Upon activation, p38 MAPK alpha activates MK2 by phosphorylating Thr-222, Ser-272, and Thr-334 (Ben-Levy et al. 1995). The phosphorylation of MK2 at Thr-334 attenuates the affinity of the binary complex MK2:p38 alpha by an order of magnitude and leads to a large conformational change of an autoinhibitory domain in MK2. This conformational change unmasks not only the MK2 substrate-binding site but also the MK2 nuclear export signal (NES) thus leading to the MK2:p38 alpha translocation from the nucleus to the cytoplasm. Cytoplasmic active MK2 then phosphorylates downstream targets such as the heat-shock protein HSP27 and tristetraprolin (TTP) (Meng et al. 2002, Lukas et al. 2004, White et al. 2007). MAPKAPK (MAPK-activated protein) kinase 3 (MK3, also known as 3pK) has been identified as the second p38 MAPK-activated kinase that is stimulated by different stresses (McLaughlin et al. 1996; Sithanandam et al. 1996; reviewed in Gaestel 2006). MK3 shows 75% sequence identity to MK2 and, like MK2, is activated by p38 MAPK alpha and p38 MAPK beta. MK3 phosphorylates peptide substrates with kinetic constants similar to MK2 and phosphorylates the same serine residues in HSP27 at the same relative rates as MK2 (Clifton et al. 1996) indicating an identical phosphorylation-site consensus sequence. Hence, it is assumed that its substrate spectrum is either identical to or at least overlapping with MK2.
Phosphate bond hydrolysis by NUDT proteins
The culture medium of senescent cells in enriched in secreted proteins when compared with the culture medium of quiescent i.e. presenescent cells and these secreted proteins constitute the so-called senescence-associated secretory phenotype (SASP), also known as the senescence messaging secretome (SMS). SASP components include inflammatory and immune-modulatory cytokines (e.g. IL6 and IL8), growth factors (e.g. IGFBPs), shed cell surface molecules (e.g. TNF receptors) and survival factors. While the SASP exhibits a wide ranging profile, it is not significantly affected by the type of senescence trigger (oncogenic signalling, oxidative stress or DNA damage) or the cell type (epithelial vs. mesenchymal) (Coppe et al. 2008). However, as both oxidative stress and oncogenic signaling induce DNA damage, the persistent DNA damage may be a deciding SASP initiator (Rodier et al. 2009). SASP components function in an autocrine manner, reinforcing the senescent phenotype (Kuilman et al. 2008, Acosta et al. 2008), and in the paracrine manner, where they may promote epithelial-to-mesenchymal transition (EMT) and malignancy in the nearby premalignant or malignant cells (Coppe et al. 2008). Interleukin-1-alpha (IL1A), a minor SASP component whose transcription is stimulated by the AP-1 (FOS:JUN) complex (Bailly et al. 1996), can cause paracrine senescence through IL1 and inflammasome signaling (Acosta et al. 2013). Here, transcriptional regulatory processes that mediate the SASP are annotated. DNA damage triggers ATM-mediated activation of TP53, resulting in the increased level of CDKN1A (p21). CDKN1A-mediated inhibition of CDK2 prevents phosphorylation and inactivation of the Cdh1:APC/C complex, allowing it to ubiquitinate and target for degradation EHMT1 and EHMT2 histone methyltransferases. As EHMT1 and EHMT2 methylate and silence the promoters of IL6 and IL8 genes, degradation of these methyltransferases relieves the inhibition of IL6 and IL8 transcription (Takahashi et al. 2012). In addition, oncogenic RAS signaling activates the CEBPB (C/EBP-beta) transcription factor (Nakajima et al. 1993, Lee et al. 2010), which binds promoters of IL6 and IL8 genes and stimulates their transcription (Kuilman et al. 2008, Lee et al. 2010). CEBPB also stimulates the transcription of CDKN2B (p15-INK4B), reinforcing the cell cycle arrest (Kuilman et al. 2008). CEBPB transcription factor has three isoforms, due to three alternative translation start sites. The CEBPB-1 isoform (C/EBP-beta-1) seems to be exclusively involved in growth arrest and senescence, while the CEBPB-2 (C/EBP-beta-2) isoform may promote cellular proliferation (Atwood and Sealy 2010 and 2011). IL6 signaling stimulates the transcription of CEBPB (Niehof et al. 2001), creating a positive feedback loop (Kuilman et al. 2009, Lee et al. 2010). NF-kappa-B transcription factor is also activated in senescence (Chien et al. 2011) through IL1 signaling (Jimi et al. 1996, Hartupee et al. 2008, Orjalo et al. 2009). NF-kappa-B binds IL6 and IL8 promoters and cooperates with CEBPB transcription factor in the induction of IL6 and IL8 transcription (Matsusaka et al. 1993, Acosta et al. 2008). Besides IL6 and IL8, their receptors are also upregulated in senescence (Kuilman et al. 2008, Acosta et al. 2008) and IL6 and IL8 may be master regulators of the SASP. IGFBP7 is also an SASP component that is upregulated in response to oncogenic RAS-RAF-MAPK signaling and oxidative stress, as its transcription is directly stimulated by the AP-1 (JUN:FOS) transcription factor. IGFBP7 negatively regulates RAS-RAF (BRAF)-MAPK signaling and is important for the establishment of senescence in melanocytes (Wajapeyee et al. 2008). Please refer to Young and Narita 2009 for a recent review.
Oxidative stress, caused by increased concentration of reactive oxygen species (ROS) in the cell, can happen as a consequence of mitochondrial dysfunction induced by the oncogenic RAS (Moiseeva et al. 2009) or independent of oncogenic signaling. Prolonged exposure to interferon-beta (IFNB, IFN-beta) also results in ROS increase (Moiseeva et al. 2006). ROS oxidize thioredoxin (TXN), which causes TXN to dissociate from the N-terminus of MAP3K5 (ASK1), enabling MAP3K5 to become catalytically active (Saitoh et al. 1998). ROS also stimulate expression of Ste20 family kinases MINK1 (MINK) and TNIK through an unknown mechanism, and MINK1 and TNIK positively regulate MAP3K5 activation (Nicke et al. 2005). MAP3K5 phosphorylates and activates MAP2K3 (MKK3) and MAP2K6 (MKK6) (Ichijo et al. 1997, Takekawa et al. 2005), which act as p38 MAPK kinases, as well as MAP2K4 (SEK1) (Ichijo et al. 1997, Matsuura et al. 2002), which, together with MAP2K7 (MKK7), acts as a JNK kinase. MKK3 and MKK6 phosphorylate and activate p38 MAPK alpha (MAPK14) and beta (MAPK11) (Raingeaud et al. 1996), enabling p38 MAPKs to phosphorylate and activate MAPKAPK2 (MK2) and MAPKAPK3 (MK3) (Ben-Levy et al. 1995, Clifton et al. 1996, McLaughlin et al. 1996, Sithanandam et al. 1996, Meng et al. 2002, Lukas et al. 2004, White et al. 2007), as well as MAPKAPK5 (PRAK) (New et al. 1998 and 2003, Sun et al. 2007). Phosphorylation of JNKs (MAPK8, MAPK9 and MAPK10) by MAP3K5-activated MAP2K4 (Deacon and Blank 1997, Fleming et al. 2000) allows JNKs to migrate to the nucleus (Mizukami et al. 1997) where they phosphorylate JUN. Phosphorylated JUN binds FOS phosphorylated by ERK1 or ERK2, downstream of activated RAS (Okazaki and Sagata 1995, Murphy et al. 2002), forming the activated protein 1 (AP-1) complex (FOS:JUN heterodimer) (Glover and Harrison 1995, Ainbinder et al. 1997). Activation of p38 MAPKs and JNKs downstream of MAP3K5 (ASK1) ultimately converges on transcriptional regulation of CDKN2A locus. In dividing cells, nucleosomes bound to the CDKN2A locus are trimethylated on lysine residue 28 of histone H3 (HIST1H3A) by the Polycomb repressor complex 2 (PRC2), creating the H3K27Me3 (Me3K-28-HIST1H3A) mark (Bracken et al. 2007, Kotake et al. 2007). The expression of Polycomb constituents of PRC2 (Kuzmichev et al. 2002) - EZH2, EED and SUZ12 - and thereby formation of the PRC2, is positively regulated in growing cells by E2F1, E2F2 and E2F3 (Weinmann et al. 2001, Bracken et al. 2003). H3K27Me3 mark serves as a docking site for the Polycomb repressor complex 1 (PRC1) that contains BMI1 (PCGF4) and is therefore named PRC1.4, leading to the repression of transcription of p16-INK4A and p14-ARF from the CDKN2A locus, where PCR1.4 mediated repression of p14-ARF transcription in humans may be context dependent (Voncken et al. 2005, Dietrich et al. 2007, Agherbi et al. 2009, Gao et al. 2012). MAPKAPK2 and MAPKAPK3, activated downstream of the MAP3K5-p38 MAPK cascade, phosphorylate BMI1 of the PRC1.4 complex, leading to dissociation of PRC1.4 complex from the CDKN2A locus and upregulation of p14-ARF transcription (Voncken et al. 2005). AP-1 transcription factor, formed as a result of MAP3K5-JNK signaling, as well as RAS signaling, binds the promoter of KDM6B (JMJD3) gene and stimulates KDM6B expression. KDM6B is a histone demethylase that removes H3K27Me3 mark i.e. demethylates lysine K28 of HIST1H3A, thereby preventing PRC1.4 binding to the CDKN2A locus and allowing transcription of p16-INK4A (Agger et al. 2009, Barradas et al. 2009, Lin et al. 2012). p16-INK4A inhibits phosphorylation-mediated inactivation of RB family members by CDK4 and CDK6, leading to cell cycle arrest (Serrano et al. 1993). p14-ARF inhibits MDM2-mediated degradation of TP53 (p53) (Zhang et al. 1998), which also contributes to cell cycle arrest in cells undergoing oxidative stress. In addition, phosphorylation of TP53 by MAPKAPK5 (PRAK) activated downstream of MAP3K5-p38 MAPK signaling, activates TP53 and contributes to cellular senescence (Sun et al. 2007).
The p90 ribosomal S6 kinases (RSK1-4) comprise a family of serine/threonine kinases that lie at the terminus of the ERK pathway. RSK family members are unusual among serine/threonine kinases in that they contain two distinct kinase domains, both of which are catalytically functional . The C-terminal kinase domain is believed to be involved in autophosphorylation, a critical step in RSK activation, whereas the N-terminal kinase domain, which is homologous to members of the AGC superfamily of kinases, is responsible for the phosphorylation of all known exogenous substrates of RSK. RSKs can be activated by the ERKs (ERK1, 2, 5) in the cytoplasm as well as in the nucleus, they both have cytoplasmic and nuclear substrates, and they are able to move from nucleus to cytoplasm. Efficient RSK activation by ERKs requires its interaction through a docking site located near the RSK C terminus. The mechanism of RSK activation has been studied mainly with regard to ERK1 and ERK2. RSK activation leads to the phosphorylation of four essential residues Ser239, Ser381, Ser398, and Thr590, and two additional sites, Thr377 and Ser749 (the amino acid numbering refers to RSK1). ERK is thought to play at least two roles in RSK1 activation. First, activated ERK phosphorylates RSK1 on Thr590, and possibly on Thr377 and Ser381, and second, ERK brings RSK1 into close proximity to membrane-associated kinases that may phosphorylate RSK1 on Ser381 and Ser398. Moreover, RSKs and ERK1/2 form a complex that transiently dissociates upon growth factor signalling. Complex dissociation requires phosphorylation of RSK1 serine 749, a growth factor regulated phosphorylation site located near the ERK docking site. Serine 749 is phosphorylated by the N-terminal kinase domain of RSK1 itself. ERK1/2 docking to RSK2 and RSK3 is also regulated in a similar way. The length of RSK activation following growth factor stimulation depends on the duration of the RSK/ERK complex, which, in turn, differs among the different RSK isoforms. RSK1 and RSK2 readily dissociate from ERK1/2 following growth factor stimulation stimulation, but RSK3 remains associated with active ERK1/2 longer, and also remains active longer than RSK1 and RSK2.
Reactive oxygen species such as superoxide (O2.-), peroxides (ROOR), singlet oxygen, peroxynitrite (ONOO-), and hydroxyl radical (OH.) are generated by cellular processes such as respiration (reviewed in Murphy 2009, Brand 2010) and redox enzymes and are required for signaling yet they are damaging due to their high reactivity (reviewed in Imlay 2008, Buettner 2011, Kavdia 2011, Birben et al. 2012, Ray et al. 2012). Aerobic cells have defenses that detoxify reactive oxygen species by converting them to less reactive products. Superoxide dismutases convert superoxide to hydrogen peroxide and oxygen (reviewed in Fukai and Ushio-Fukai 2011). Catalase and peroxidases then convert hydrogen peroxide to water. Humans contain 3 superoxide dismutases: SOD1 is located in the cytosol and mitochondrial intermembrane space, SOD2 is located in the mitochondrial matrix, and SOD3 is located in the extracellular region. Superoxide, a negative ion, is unable to easily cross membranes and tends to remain in the compartment where it was produced. Hydrogen peroxide, one of the products of superoxide dismutase, is able to diffuse across membranes and pass through aquaporin channels. In most cells the primary source of hydrogen peroxide is mitochondria and, once in the cytosol, hydrogen peroxide serves as a signaling molecule to regulate redox-sensitive proteins such as transcription factors, kinases, phosphatases, ion channels, and others (reviewed in Veal and Day 2011, Ray et al. 2012). Hydrogen peroxide is decomposed to water by catalase, decomposed to water plus oxidized thioredoxin by peroxiredoxins, and decomposed to water plus oxidized glutathione by glutathione peroxidases (Presnell et al. 2013).
Peroxiredoxin 6 (PRDX6) forms a heterodimer with GSTP1 (Pi Glutathione transferase) and catalyzes the reduction of hydrogen peroxide (H2O2) by glutathione to yield oxidized glutathione and water (Ralat et al. 2006, Ralat et al. 2008, Zhou et al. 2013).
Proteotoxic stress results in an accumulation of misfolded proteins which tend to form insoluble protein aggregates. Histone deacetylase 6 (HDAC6) binds to ubiquitinated protein aggregates to regulate their degradation (Boyault C et al. 2006). HDAC6 was also found to interact with HSP90 and to regulate HSP90 chaperone complex activity via deacetylation of HSP90 (Kovacs JJ et al. 2005; Boyault C et al. 2007). Binding of HDAC6 to polyubiquitinted proteins triggers the dissociation of the HDAC6:HSP90:HSF1 complex resulting in the activation of HSF1 (Boyault C et al. 2007). In the absence of stress HSF1 is predominantly monomeric and is thought to be repressed in its inactive monomeric state by the following mechanisms: interaction with chaperone proteins such as HSP90 (Zou J et al.1998; Guo Y et al. 2001) intramolecular coiled-coil interactions between a hydrophobic leucine zipper domain in the carboxyl-terminus of the protein and three amino-terminal leucine zippers, which are required for homotrimerization and transcriptional activation (Rabindran SK et al. 1993; Zuo J et al. 1995) post-translation modifications that include protein acetylation, sumoylation and phosphorylation may also contribute to HSF1 repression (Knauf U et al. 1996; Hietakangas V et al. 2003; Batista-Nascimento L et al. 2011)
In the absence of stress HSF1 is predominantly monomeric and is thought to be repressed in its inactive monomeric state by the following mechanisms: interaction with chaperone proteins such as HSP90 (Zou J et al.1998; Guo Y et al. 2001) intramolecular coiled-coil interactions between a hydrophobic leucine zipper domain in the carboxyl-terminus of the protein and three amino-terminal leucine zippers, which are required for homotrimerization and transcriptional activation (Rabindran SK et al. 1993; Zuo J et al. 1995) post-translation modifications that include protein acetylation, sumoylation and phosphorylation may also contribute to HSF1 repression (Knauf U et al. 1996; Hietakangas V et al. 2003; Batista-Nascimento L et al. 2011) The accumulation of misfolded proteins upon proteotoxic stresses leads to the release of HSF1 from the HSP90-containing multichaperone complex and results in HSF1 self-association to form homotrimers (Baler R et al. 1993). There is also evidence showing that HDAC6 senses the accumulation of misfolded, ubiquitinated protein aggregates in cells and induces dissociation of a repressive HDAC6:HSF1:HSP90 complex and subsequent HSF1 activation (Boyault C et al. 2007).
Accumulation of non-native or misfolded proteins upon cellular stress is believed to release monomeric HSF1 from chaperon regulatory proteins (Guo Y et al. 2001). The released HSF1 monomer is rapidly converted to a homotrimer (Baler R et al. 1993; Herbomel G et al 2013). Upon trimerization HSF1 undergoes significant conformational changes resulting in an assembly of a stable triple-stranded alpha-helical coiled-coil structure with the amino-terminal hydrophobic domains from individual monomeric units (Rabindran SK et al. 1993; Zuo J et al. 1994, 1995; Neef DW et al. 2013). Biochemical and structural analysis strongly suggest that the monomer-to-trimer transition is tightly regulated at several interdependent levels. Thus, HSPs and cofactors bind HSF1 monomers preventing trimerization (Zou J et al.1998; Guo Y et al. 2001). In addition, leucine zippers (LZ) in the trimerization domain (LZ1-LZ3) are thought to retain HSF1 in its inactive monomeric form by intramolecular coiled-coil interactions with LZ4 in the carboxyl-terminus of HSF1, while LZ interactions between trimerization domains of individual monomeric units facilitate homotrimerization (Rabindran SK et al. 1993; Zuo J et al. 1994, 1995; Neef DW et al. 2013). HSF1 flexible linker region between DNA binding domain and first LZ of the trimerization domain was also found to modulate the monomer-trimer equilibrium (Liu PCC and Thiele DJ 1999). Furthermore, intermolecular disulfide bonds between cysteine residues 36 and 103 were reported to stabilize HSF1 trimer, while intramolecular disulfide crosslink inhibited HSF1 oligomerization (Lu M et al. 2008, 2009). Moreover, redox regulatory mechanisms were shown to regulate thiol-disulfide exchange and the conformation and activity of mammalian HSF1 in response to stress (Manalo DJ et al. 2002; Ahn SG and Thiele DJ 2003). A ribonucleoprotein complex containing translation elongation factor EEF1A1 (eEF1A) and a long non-coding RNA, HSR1 (heat shock RNA-1) was shown to mediate trimerization of HSF1 (Shamovsky I et al. 2006).
There is no consensus on whether inactive HSF1 monomers localize in the nucleus or in the cytosol (Sarge KD et al. 1993; Zuo J et al. 1995; Mercier PA et al. 1999; Vujanac M et al. 2005). Moreover, inactive HSF1 was reported to constitutively shuttle between the nucleus and the cytoplasm in mammalian cells (Vujanac M et al. 2005). However, active HSF1 trimers were shown to rapidly accumulate in the nucleus where they bind to heat shock elements (HSE) present within promoters of hsp genes (Wang Y and Morgan WD 1994; Herbomel G et al. 2013). Heat shock response in human and monkey cells (but not rodent cells) is also associated with the stress-induced relocalization of HSF1 within the nucleus not only on hsp gene promoters but also into specific subnuclear organelles termed nuclear stress bodies (nSBs, also known as HSF1 granules) (Sarge KD et a. 1993; Cotto JJ et al. 1997; Jolly C et al. 1999). nSBs are rarely detectable in unstressed cells but their number drastically increases after heat shock. Formation of nSBs is initiated by the interaction between HSF1 and pericentric tandem repeats of satellite III sequences on chromosome 9, where sat III repeats are transcribed by RNA polymerase II in an HSF1-dependent manner. (Jolly C et al. 2002, 2004). HSF1 can also bind to DNA regions enriched in sat II and sat III repeated sequences detected on other human chromosomes (Eymery A et al. 2010). The functional relevance of HSF1 granules and their transcripts remains an open question.
The inactive HSF1 was reported to constitutively shuttle between the nucleus and the cytoplasm in mammalian cells (Vujanac M et al. 2005). There is no consensus on whether inactive HSF1 monomers localize in the nucleus or in the cytosol (Sarge KD et al. 1993; Zuo J et al. 1995; Mercier PA et al. 1999; Vujanac M et al. 2005). This event shows stress-induced activation of HSF1 in the nucleus. In the absence of stress HSF1 is predominantly monomeric and is thought to be repressed in its inactive monomeric state by the following mechanisms: interaction with chaperone proteins such as HSP90 (Zou J et al.1998; Guo Y et al. 2001) intramolecular coiled-coil interactions between a hydrophobic leucine zipper domain in the carboxyl-terminus of the protein and three amino-terminal leucine zippers, which are required for homotrimerization and transcriptional activation (Rabindran SK et al. 1993; Zuo J et al. 1995) post-translation modifications that include protein acetylation, sumoylation and phosphorylation may also contribute to HSF1 repression (Knauf U et al. 1996; Hietakangas V et al. 2003; Batista-Nascimento L et al. 2011) The accumulation of misfolded proteins upon proteotoxic stresses leads to the release of HSF1 from the HSP90-containing multichaperone complex and results in HSF1 self-association to form homotrimers (Baler R et al. 1993).
Proteoglycans and Sulfated Glycosaminoglycans
Heat shock factor 1 (HSF1) is a transcription factor that activates gene expression in response to a variety of stresses, including heat shock, oxidative stress, as well as inflammation and infection (Shamovsky I and Nudler E 2008; Akerfelt et al. 2010; Bjork and Sistonen 2010; Anckar and Sistonen 2011). HSF1 is constitutively present in the cell. In the absence of stress HSF1 is found in both the cytoplasm and the nucleus as an inactive monomer (Sarge KD et al. 1993; Mercier PA et al. 1999; Vujanac M et al. 2005). A physical or chemical proteotoxic stress rapidly induces HSF1 activation, which occurs through a multi?step process, involving HSF1 monomer-to-homotrimer transition, nuclear accumulation, and binding to a promoter element, called the heat shock element (HSE), which leads to the increase in the stress-inducible gene expression (Sarge KD et al. 1993; Baler R et al. 1998; Sonna LA et al. 2002; Shamovsky I and Nudler E 2008; Sakurai H and Enoki Y 2010; Herbomel G et al. 2013). Depending on the type of stress stimulus, the multiple events associated with HSF1 activation might be affected differently (Holmberg CI et al 2000; Bjork and Sistonen 2010).
Mutagenesis experiments and functional studies suggest that phosphorylation of HSF1 residue Ser326 promotes induction of the HSF1 transcriptional competence in response to heat and other cell stressors including proteasome inhibitors and sodium arsenite (Guettouche T et al. 2005; Chou SD et al. 2012). The mammalian target of rapamycin complex 1 (mTORC1) has been implicated in sensing intracellular protein misfolding (Qian SB et al. 2010; Chou SD et al. 2012). RNA interference?mediated repression of mTOR kinase activity in human HeLa cells was found to increase sensitivity to heat shock. Moreover, inhibition of HSF1 phosphorylation on Ser326 by rapamycin suggests that this site in HSF1 is a target for the mTORC1complex (Chou SD et al. 2012).
The transcriptional activity of HSF1 has been shown to be controlled by the regulatory domain composed of amino acids 221-310 (Green M et al. 1995; Zuo J et al. 1995; Newton EM et al., 1996). Ser230 is located in this regulatory domain of HSF1 and is constitutively and stress-inducibly phosphorylated (Holmberg CI et al. 2001). Analyses with phosphopeptide-specific antibody and site-directed mutagenesis revealed that phosphorylation at Ser230 enhanced the inducible HSF1 transcriptional activity in heat-shocked human K562 erythroleukemia and HeLa cells (Holmberg CI et al 2001). Active calcium/calmodulin-dependent protein kinase II (CaMKII) was shown to phosphorylate HSF1 at Ser230 in vitro. Moreover, CaMKII enhanced heat-induced tranactivating capacity of HSF1 and the level of endogenous Ser230 phosphorylation in K562 cells transfected with active CaMKII together with a CAT reporter plasmid containing the proximal HSE of human hsp70 promoter. Thus, CaMKII signaling may be involved in the positive regulation of HSF1-mediated transactivation. However, the possibility that other protein kinases might also phosphorylate Ser230 in vivo should not be excluded (Holmberg CI et al 2001).
Characteristics of human types 1, 2 and 3 17 beta-hydroxysteroid dehydrogenase activities: oxidation/reduction and inhibition
Heat shock factor binding protein 1 (HSBP1) is a nuclear localized hydrophobic repeat-containing protein, which interacts with trimerization domain of HSF1 and negatively regulates DNA-binding activity of HSF1. Overexpression of HSBP1 in mammalian cells represses the transactivation activity of HSF1 (Satyal SH et al. 1998).
Acetylated HSF1 was detected in lysates of human embryonic kidney 293T cells which were transfected with vectors encoding a Flag-HSF1 fusion and p300 proteins and exposed to various stress conditions (Westerheide SD et al. 2012). No acetylation was found in lysates of unstressed cells. Acetylation of HSF1 may occurs on multiple lysines, such as Lys80 within the DNA binding domain. Mutation of Lys80 disrupted the DNA-binding ability of recombinant HSF1, indicating that the acetylation at Lys80 caused the regulated release of the HSF1 trimers from DNA and thus represents a regulatory step in the attenuation of the heat shock responce (Westerheide SD et al. 2009; Herbomel G et al 2013).
During attenuation and recovery from heat shock, increased levels of HSP70 and HDJ1 (HSP40) were found to associate with the HSF1 activation domain, repressing its transcriptional activity (Shi Y et al. 1998)
Combination of chromatin immunoprecipitation (ChIP) microarray analysis and time course gene expression microarray analysis with and without siRNA-mediated inhibition of HSF1 showed that human HSF1 can induce the expression of different sets of target genes to maintain a wide range of biological processes (e.g., anti-apoptosis, RNA splicing, ubiquitination)(Page TG et al. 2006; Vihervaara A. et al. 2013). However, HSF1 is best known for rapid stress-induced upregulation of certain genes related to protein folding, such as HSPA1A/HSP70, HSPC/HSP90, HSPB1/HSP27, and DNAJB1/HSP40 (Mosser DD et al. 1988; Trinklein ND et al. 2004a,b; Page TG et al. 2006; Vihervaara A. et al. 2013).
The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions
Acquisition of DNA binding activity by HSF1 is necessary but insufficient for transcriptional activation (Cotto JJ et al. 1996; Trinklein ND et al. 2004). In addition to having a sequence-specific DNA binding domain, HSF1 contains a C-terminal region which is involved in activating the transcription of the target genes (Green M et al. 1995). However, the transactivating ability of the transactivation domain itself is not stress sensitive. Rather, it's controled by a regulatory domain of HSF1 (amino acids 221-310), which represses the transactivating ability under normal physiological conditions (Green M et al. 1995; Zuo J et al. 1995; Newton EM et al. 1996). The HSF1 transactivation domain can be divided into two distinct regions, activation domain 1 (AD1) and activation domain 2 (AD2) (Brown SA et al. 1998). AD1 and AD2 each contain residues that are important for both transcriptional initiation and elongation. Mutations in acidic residues in both AD1 and AD2 preferentially affect the ability of HSF1 to stimulate transcriptional initiation, while mutations in phenylalanine residues preferentially affect stimulation of elongation (Brown SA et al. 1998). Activation of the DNA-bound but transcriptionally incompetent HSF1 is thought to occur upon stress induced HSF1 phosphorylation at several serine residues (Ding XZ et al. 1997; Holmberg CI et al. 2001; Guettouche T et al. 2005). In cells exposed to heat, acquisition of HSE DNA-binding activity was observed to precede phosphorylation of HSF1 (Cotto JJ et al. 1996; Kline MP & Morimoto RI 1997). While there is a sufficient evidence to suggest that phosphorylation of HSF1 is essential to modulate HSF1 transactiviting capacity, mechanisms behind stress stimuli and kinases/phosphatases involved have not been clearly established.
Constitutive phosphorylation at Ser307 was shown to inhibit HSF1 transcriptional activity under normal temperatures. Substitution of Ser307 with alanine derepresses the transactivation domain such that the S307A mutant showed increased transcriptional activity in human and mouse cells (Knauf U et al. 1996; Kline MP & Morimoto RI 1997). HSF1-ERK association was shown to promote ERK activity in human HeLa, acute monocytic leukemia THP1 and metastatic cutaneous SCC7 cells resulting in phosphorylation of HSF1 on Ser307 (Chu B et al. 1996; Wang X et al. 2004). This phosphorylation in turn promoted HSF1 association with YWHAE (14-3-3 epsilon), which may be involved in the attenuation of HSF1 activity during recovery and leads to accelerated cytoplasmic localization of HSF1 (Wang X et al. 2003, 2004).
Under non-stress conditions monomeric HSF1 is sequestered in a HSP90-containing heterocomplex. FKBP4 (immunophilin) is one of the components of HSP90-chaperone machinery which was found to associate with trimeric, but not monomeric form of HSF1 (Guo Y et al. 2001). Multichaperone complex of HSP90:FKBP4:PKGES3 has been shown to associate with HSF1 trimer through its regulatory domain, and this is thought to repress HSF1 transcriptional activity (Guo Y et al. 2001).
Attenuation of the heat shock transcriptional response occurs during continuous exposure to intermediate heat shock conditions or upon recovery from stress (Abravaya et al. 1991). The attenuation phase of HSF1 cycle involves the transcriptional silencing of HSF1 bound to HSE, the release of HSF1 trimers from HSE and dissociation of HSF1 trimers to monomers. HSF1-driven heat stress associated transcription was shown to depend on inducible and reversible acetylation of HSF1 at Lys80, which negatively regulates DNA binding activity of HSF1 (Westerheide SD et al. 2009). In addition, the attenuation of HSF1 activation takes place when enough HSP70/HSP40 is produced to saturate exposed hydrophobic regions of proteins damaged as a result of heat exposure. The excess HSP70/HSP40 binds to HSF1 trimer, which leads to its dissociation from the promoter and conversion to the inactive monomeric form (Abravaya et al. 1991; Shi Y et al. 1998). Interaction of HSP70 with the transcriptional corepressor repressor element 1-silencing transcription factor corepressor (CoREST) assists in terminating heat-shock response (Gomez AV et al. 2008). HSF1 DNA-binding and transactivation activity were also inhibited upon interaction of HSF1-binding protein (HSBP1) with active trimeric HSF1(Satyal SH et al. 1998).
Constitutive phosphorylation at Ser303 within the regulatory domain of HSF1 was shown to inhibit its transcriptional activity under normal temperatures. Substitution of Ser303 with alanine derepresses the transactivation domain such that the S303A mutant showed increased transcriptional activity in human and mouse cells (Knauf U et al. 1996; Kline MP & Morimoto RI 1997). Phosphorylation of HSF1 at Ser303 was mediated by glycogen synthase kinase 3 (GSK3) activity in human acute monocytic leukemia THP1 cells and mouse embryonic fibroblast NIH 3T3 cells (Chu B et al. 1996, 1998). However, the other group showed that GSK3 inhibits HSF1 activity in HeLa cells through a mechanism that is independent of Ser303 phosphorylation, thus suggesting that Ser303 may be phosphorylated by multiple MAPKs (Batista?Nascimento L et al. 2011). The phosphorylation at Ser303 in turn promoted HSF1 association with YWHAE (14-3-3 epsilon), which may be involved in the attenuation of HSF1 activity during recovery leading to accelerated cytoplasmic localization of HSF1 (Wang X et al. 2003, 2004).In addition, stress stimulated human K562 erythroleukemia cells showed enhanced level of sumoylation in the HSF1 regulatory domain at Lys298, which was positively regulated by Ser303 phosphorylation (Hietakangas V et al. 2003).
Point mutations in the aromatic/arginine region in aquaporin 1 allow passage of urea, glycerol, ammonia, and protons
There are two classes of glutamate transporters; the excitatory amino acid transporters (EAATs) which depend on an electrochemical gradient of Na+ ions and vesicular glutamate transporters (VGLUTs) which don't. Together, these transporters uptake and release glutamate to mediate this neurotransmitter's excitatory signal and are part of the glutamate-gluatamine cycle. Three members of the SLC17A gene family (7, 6 and 8) encode VGLUTs 1-3 respectively (Ni B et al, 1996; Takamori S et al, 2001; Takamori S et al, 2002 respectively). VGLUT1 (brain-specific Na+-dependent phopshate transporter, BNPI) and VGLUT2 (differentiation-associated Na+-dependent phosphate transporter, DNPI) were identified first and originally characterized as phosphate transporters. However, they are localized to synaptic vesicles, not the plasma membrane (like EAATs) and transport the organic anion glutamate into synaptic vesicles. This uptake is thought to be coupled to the proton electrochemical gradient generated by a vacuolar type H+-ATPase. They are all expressed in the CNS in neuron-rich areas but VGLUT3 is also expressed on astrocytes and in liver and kidney.
There are two classes of glutamate transporters; the excitatory amino acid transporters (EAATs) which depend on an electrochemical gradient of Na+ ions and vesicular glutamate transporters (VGLUTs) which don't. Together, these transporters uptake and release glutamate to mediate this neurotransmitter's excitatory signal and are part of the glutamate-gluatamine cycle. The SLC1 gene family includes five high-affinity glutamate transporters encoded by SLC1, 2, 3, 6 and 7. These transporters can mediate transport of L-Glutamate, L-Aspartate and D-Aspartate with cotransport of 3 Na+ ions and H+ and antiport of a K+ ion. This mechanism allows glutamate into cells against a concentration gradient. This is a crucial factor in the protection of neurons against glutamate excitotoxicity in the CNS. SLC1A1 encodes an excitatory amino-acid carrier 1 (EAAC1, also called EAAT3) (Shashidharan P et al, 1994; Arriza JL et al, 1994) and is abundant particularly in brain but also in liver, muscle, ovary, testis and in retinoblastoma cell lines. In the kidney, EAAC1 is present at apical membranes of proximal tubes. Defects in SLC1A1 may be a cause of dicarboxylicamino aciduria (glutamate-aspartate transport defect in the kidney and intestine). SLC1A2 encodes the glial-type high affinity glutamate transporter (GLT1, EAAT2) (Arriza JL et al, 1994). GLT1 is expressed mainly in the brain and is essential for terminating the postsynaptic action of glutamate by rapidly removing released glutamate from the synaptic cleft. SLC1A3 encodes a sodium-dependent glutamate/aspartate transporter 1 (GLAST1, EAAT1). It is particularly abundant in the cerebellum and, like GLT1, plays a role in terminating the postsynaptic action of glutamate (Arriza JL et al, 1994). Defects in SLC1A3 are the cause of episodic ataxia type 6 (EA6), characterized by episodic ataxia, seizures, migraine and alternating hemiplegia (Jen JC et al, 2005). SLC1A6 encodes an excitatory amino-acid transporter 4 (EAAT4) (Fairman WA et al, 1995) and is predominantly expressed in cerebellar Purkinje cells. SLC1A7 encodes an excitatory amino acid transporter 5 (EAAT5, retinal glutamate transporter) (Arriza JL et al, 1997) which is highly expressed in the retina.
SLC17A5 encodes a lysosomal sialic acid transporter, Sialin (AST, membrane glycoprotein HP59) (Verheijen et al. 1999, Fu et al. 2001). SLC17A5 exports sialic acid (N-acetylneuraminic acid, Neu5Ac) which is derived from the degradation of glycoconjugates. This export is dependent on the proton electrochemical gradient across the lysosomal membrane. SLC17A5 is present in the pathological tumor vasculature of the lung, breast, colon, and ovary, but not in the normal vasculature, suggesting that the protein may be critical to pathological angiogenesis. Sialin is not expressed in a variety of normal tissues, but is significantly expressed in human fetal lung. Defects in SLC17A5 cause Salla disease (Sialic acid storage disease, SD) and infantile sialic acid storage disorder (ISSD aka N-acetylneuraminic acid storage disease, NSD). These are autosomal recessive neurodegenerative disorders characterized by hypotonia, cerebellar ataxia and mental retardation in very young infants (Verheijen et al. 1999, Aula et al. 2000).
SLC6A14, associated with the plasma membrane, mediates the uptake of multiple basic and nonpolar amino acids as well as beta-alanine. Uptake of one amino acid molecule is accompanied by uptake of two sodium ions and a chloride ion. As assessed by Northern blotting, SLC6A14 is expressed at high levels in lung but only at low levels, if at all, in intestine or kidney (Sloan and Mager 1999; Anderson et al. 2008).
SLC6A19, associated with the plasma membrane, mediates the uptake of neutral amino acids. Uptake of an amino acid molecule is accompanied by uptake of a sodium ion. The protein is abundant in cells in the small intestine and kidney. Its deficiency is associated with Hartnup disorder, the failure to take up neutral amino acids efficiently from the gut lumen and to reabsorb them in the proximal kidney tubule (Kleta et al. 2004; Seow et al, 2004).
SLC7A9 as a heterodimer with SLC3A1 in the plasma membrane mediates the exchange of arginine, lysine, or cystine for leucine. The physiological concentrations of these amino acids favor leucine export and arginine / lysine / cystine import. Defects in SLC7A9 and SLC3A1 are associated with cystinuria. In the body, this transport process is prominent in the kidney (Mizoguchi et al. 2001).
Amino acid transport across plasma membranes is critical to the uptake of these molecules from the gut, to their reabsortion in the kidney proximal tubulues, and to their distribution to cells in which they are required for the synthesis of proteins and of amino acid derived small molecules such as neurotransmitters. Physiological studies have defined 18 "systems" that mediate amino acid transport, each characterized by its amino acid substrates, as well as its pH sensitivity and its association (or not) with ion transport. More recently, molecular cloning studies have allowed the identification of the plasma membrane transport proteins that mediate these reactions. Amino acid uptake mediated by 17 of these transporters is annotated here (Broer 2008).
SLC1A5, associated with the plasma membrane, mediates the exchange of extracellular glutamine for cytosolic alanine (Broer et al. 2000).
SLC36A1 (PAT1), associated with the plasma membrane, mediates the uptake of glycine, alanine, and proline coupled to the uptake of a proton. Northern blotting experiments indicate gene expression principally in the intestine (Chen et al. 2003).
SLC36A2 (PAT2), associated with the plasma membrane, has been shown in a limited set of tests in vitro to mediate the uptake of glycine and proline coupled to the uptake of a proton (Boll et al. 2003). PAT2 is most abundantly expressed in kidney and muscle.
Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3----p36.2
Feedback upregulation of HER3 (ErbB3) expression and activity attenuates antitumor effect of PI3K inhibitors
Proc. Natl. Acad. Sci. U.S.A. 109:2718-23
SLC1A5, associated with the plasma membrane, mediates the exchange of extracellular alanine for cytosolic glutamine (Broer et al. 2000).
SLC1A4, associated with the plasma membrane, mediates the exchange of threonine and an extracellular sodium ion for a cytosolic sodium ion and any one of the four amino acids alanine, serine, threonine, or cysteine (Zerangue and Kavanaugh 1996).
SLC1A4, associated with the plasma membrane, mediates the exchange of serine and an extracellular sodium ion for a cytosolic sodium ion and any one of the four amino acids alanine, serine, threonine, or cysteine (Zerangue and Kavanaugh 1996).
SLC1A4, associated with the plasma membrane, mediates the exchange of cysteine and an extracellular sodium ion for a cytosolic sodium ion and any one of the four amino acids alanine, serine, threonine, or cysteine (Zerangue and Kavanaugh 1996).
SLC6A20, associated with the plasma membrane, mediates the uptake of proline plus a sodium ion. The human protein is expressed in the intestine and kidney (Takanaga et al. 2005).
SLC1A4, associated with the plasma membrane, mediates the exchange of alanine and an extracellular sodium ion for a cytosolic sodium ion and any one of the four amino acids alanine, serine, threonine, or cysteine (Zerangue and Kavanaugh 1996).
SLC6A15, associated with the plasma membrane, mediates the uptake of a broad range of amino acids plus a sodium ion, transporting branched-chain amiono acids and methionine most efficiently. The human protein is expressed in the brain (Takanaga et al. 2005).
The protein SLC6A18 was first identified as an amino acid transporter based on sequence similarity to other members of the SLC6 protein family (Hoglund et al. 2005). It is annotated here as mediating glycine uptake based on the phenotype of mice homozygous for a null mutation in the homologous gene (Quan et al. 2004).
Phosphorus is an essential element that is critical for structural and metabolic roles in all living organisms. Cells obtain phosphorus in the form of negatively-charged inorganic phosphate (Pi). Two SLC families transport phosphate in mammals; SLC34 (Murer H et al, 2004) and SLC20 (Collins JF et al, 2004). Both are secondary-active, Na+-coupled transporter systems which use the inward Na+ gradient (from the Na+-K+-ATPase) to drive phosphate influx into cells (Virkki LV et al, 2007).
SLC16A10 mediates the reversible facilitated diffusion of phenylalanine, tyrosine, and tryptophan across the plasma membrane. The process is Na+-independent and not coupled to H+ transport. As measured by Northern blotting SLC16A10 is widely expressed in the body but especially abundant in kidney. In situ hybridization studies indicate that the gene product is abundant in kidney proximal tubules (Kim et al. 2001; Kim et al. 2002; Park et al. 2005).
Mammalian sodium/dicarboxylate cotransporters (transport succinate and other Krebs cycle intermediates) fall into two categories based on their substrate affinity. The human gene SLC13A2 encodes a low-affinity sodium/dicarboxlate co-transporter, NaDC1. NaDC1 is highly expressed in the brush-border membranes of kidney and intestinal cells and reabsorbs Krebs cycle intermediates, such as succinate and citrate, from the glomerular filtrate (Pajor AM, 1996).
SLC2A7 encodes GLUT7, a class II facilitative glucose transporter which was cloned from a human intestinal cDNA library (Li Q et al, 2004). It has a high affinity for glucose and fructose uptake. GLUT7 is found predominantly in the small intestine, colon, testis and prostate. SLC2A11 encodes GLUT11 (Doege H et al, 2001), another member of the class II facilitative glucose transporters. It has the highest similarity with GLUT5 and in humans, three isoforms are expressed (GLUT11A-C) (Sasaki T et al, 2001). Human GLUT11 has been shown to transport glucose and fructose but not galactose when expressed in Xenopus oocytes ( Scheepers A et al, 2005).
The human SLC2A9 gene encodes two isoforms of class II facilitative glucose transporter 9; GLUT9 (Phay JE et al, 2000) and GLUT9DeltaN (Augustin R et al, 2004). GLUT9 is expressed mainly in kidney (proximal tubules of epithelial cells) and liver while GLUT9DeltaN is expressed mainly in kidney and placenta. As well as mediating the uptake of fructose and glucose (at a low rate), GLUT9 can also mediate the tranpsort of urate (uric acid), the end product of purine metabolism in humans and great apes (Vitart V et al, 2008). Mutations in SLC2A9 influence serum urate concentrations with excess serum accumulation of urate leading to the development of gout (Vitart V et al, 2008).
Class II facilitative transporters consist of GLUT5, 7, 9 and 11 (Zhao FQ and Keating AF, 2007; Wood IS and Trayhurn P, 2003).
Two gene families are responsible for glucose transport in humans. SLC2 (encoding GLUTs) and SLC5 (encoding SGLTs) families mediate glucose absorption in the small intestine, glucose reabsorption in the kidney, glucose uptake by the brain across the blood-brain barrier and glucose release by all cells in the body. Glucose is the main energy source used by cells to make energy. Im mammals, blood glucose levels are tightly controlled and glucose is taken up from interstitial fluid by a passive, facilitative transport driven by the diffusion gradient of glucose (and other sugars) across the plasma membrane. This process is mediated by a family of Na+-independent, facilitative glucose transporters (GLUTs) encoded by the SLC2A gene family (Zhao FQ and Keating AF, 2007; Wood IS and Trayhurn P, 2003). There are 14 members belonging to this family (GLUT1-12, 14 and HMIT (H+/myo-inositol symporter)). The GLUT family can be subdivided into three subclasses (I-III) based on sequence similarity and characteristic sequence motifs (Joost HG and Thorens B, 2001).
SLC2A13 encodes a H+/myo-inositol co-transporter, HMIT (Uldry M et al, 2001) which is abundantly expressed in the brain. A proton is co-transported with myo-inositol uptake into cells. No glucose transport function has been detected to date.
Myo-Inositol is a neutral cyclic polyol, abundant in mammalian tissues. It plays important roles; it is a precursor to phosphatidylinositols (PtdIns) and to the inositol phosphates (IP), which serve as second messengers and as key regulators of many cell functions. It can also serve as a compatible osmolyte during volume regulation in many tissues where cells are exposed to hyperosmotic conditions. Three members of the glucose transporter families are inositol transporters. Two (SMIT1 and SMIT2) couple myo-inositol transport with two Na+ ions. Unlike SMIT1, SMIT2 also transports D-chiro_inositol. The third transporter (HMIT), couples myo-inositol transport with a proton.
The human gene SLC13A1 encodes a sodium/sulphate co-transporter NaS1 (Lee A et al, 2000). NaS1 is almost exclusively expressed in the kidney and mediates sulphate reabsorption there.
The human gene SLC13A4 encodes a sodium/sulphate co-transporter NaS2 (Girard JP et al, 1999). NaS2 is highly expressed in placenta and testis, mainly in high endothelial venules. Kinetic experiments suggest two sodium ions co-transported for every sulphate ion (Markovich D et al, 2005).
The class I facilitative glucose transporters contain GLUT1-4. As well as glucose, these proteins can transport other hexoses such as fructose, galactose and glucosamine. GLUT2 is expressed by SLC2A2 and is a low affinity glucose transporter (Fukumoto H et al, 1988). It is expressed mainly in the kidney, liver and pancreatic beta-cells. In beta-cells, it functions as a glucose-sensor for insulin secretion and in the liver, it allows for bi-directional glucose transport. In this reaction, it is shown to mediate the influx of glucose. In the next reaction, it is shown to be mediating efflux of glucose. Defects in SLC2A2 are the cause of Fanconi-Bickel syndrome (FBS). It is characterized by hepatorenal glycogen accumulation, proximal renal tubular dysfunction, and impaired utilization of glucose and galactose (Burwinkel B et al, 1999). SLC2A3 encodes GLUT3 which is mainly expressed in the brain but also in a wide range of tissues. If has a high affinity for glucose and can also transport other sugars (Kayano T et al, 1988). GLUT4, encoded by SLC2A4, is an insulin-responsive glucose transporter found in heart, skeletal muscle, brain and adipose tissue. Due to its sensitivity to insulin, it may play a role in diabetes. In a non-insulin condition, GLUT4 is localized in intracellular GLUT4-containing vesicles. On insulin stimulation, GLUT4 translocates to the plasma membrane where it can increase glucose transport 10-20-fold (Fukumoto H et al, 1989). Defects in SLC2A4 may be a cause of non-insulin-dependent diabetes mellitus (NIDDM) (Kusari J et al, 1991; Choi WH et al, 1991). GLUT1 is curated in its own reaction in this section.
Teleologically, one might argue that inorganic cation and anion transport would be evolutionarily among the oldest transport functions. Eight families comprise the group that transports exclusively inorganic cations and anions across membranes : SLC4 plays a pivotal role in mediating Na+ - and/or Cl- -dependent transport of basic anions [e.g. HCO3-, (CO3)2-] in various tissues and cell types (in addition to pH regulation, specific members of this family also contribute to vectorial trans-epithelial base transport in several organ systems including the kidney, pancreas, and eye) (Pushkin A and Kurtz I, 2006); SLC8 is a group of Na+/Ca2+ exchangers (SLC8A1 is involved in cardiac contractility) (Quednau BD et al, 2004); SLC24 is a group of Na+/Ca2+ or Na+/K+ exchangers (Altimimi HF and Schnetkamp PP, 2007); SLC9 comprises Na+/H+ exchanger proteins involved in the electroneutral exchange of sodium ion and protons (Orlowski J and Grinstein S, 2004); SLC12 functions as Na+, K+ and Cl- ion electroneutral symporters (Hebert SC et al, 2004); SLC26 is the trans-epithelial multifunctional anion (e.g. sulfate, oxalate, HCO-, Cl-) exchanger family, important in cartilage development, production of thyroid hormone, sound amplification in the cochlea etc (Sindic A et al, 2007; Dorwart MR et al, 2008; Ashmore J, 2008). SLC34 is an important Type II Na+/(HPO4)2- symporter (Forster IC et al, 2006; Virkki LV et al, 2007); SLC20 was originally identified as a viral receptor, and functions as a Type III Na+/(H2PO4)- symporter (Collins JF et al, 2004; Virkki LV et al, 2007). Eight SLC gene families are involved in the transport of amino acids and oligopeptides.
Gamma-Aminobutyric acid (GABA) is the major inhibitory transmitter of the vertebrate retina. The gene SLC32A1 encodes the vesicular inhibitory amino acid transporter (VIAAT, also called vesicular GABA transporter VGAT) (Jellali A et al, 2002). VIAAT is a proton-coupled amino acid antiporter, uptaking the inhibitory neurotransmitters GABA and glycine into synaptic vesicles in exchange for protons. This process is driven by the H+-ATPase, providing the driving force for uptake of these neurotransmitters. The protein is expressed throughout the terminal ends of horizontal cells of the retina.
SLC5A8 encodes for the apical iodide transporter, AIT (also known as SMCT1). As well as functioning as a Na+-dependent monocarboxylate co-transporter, AIT also mediates iodide transport from the thyrocyte into the colloid lumen through the apical membrane (Rodriguez AM et al, 2002). AIT, together with NIS (see previous reaction), mediates iodide transfer from blood to the colloid lumen of thyrocytes.
The human tumour suppressor gene SLC5A8 encodes for a sodium-coupled monocarboxylate transporter 1, SMCT1 (also called AIT) and is abundantly expressed in the colon (Coady MJ et al, 2004; Myauchi S et al, 2004). When the human protein is expressed in Xenopus oocytes, it was found to transport small monocarboxylates, co-transporting Na+ ions electrogenically (3 Na+ ions co-transported with 1 carboxylate).
Four SLC17 genes are thought to encode type I Na+-dependent phosphate co-transporters in humans. SLC17A1 (NPT1) encodes Na+-dependent phosphate co-transporter 1 (Na/Pi-4). It is abundant in human kidney cortex, liver and brain and is important for the resorption of phosphate by the kidney. It does this by actively transporting phosphate into cells via Na+ cotransport in the renal brush border membrane (Chong SS et al, 1993). Three close relatives of NPT1 have been identified through genomic analysis and designated NPT3 (SLC17A2), NPT4 (SLC17A3) and a putative small intestine sodium-dependent phosphate co-transporter (SLC17A4). None of these three proteins have been functionally characterized yet.
Human SLC5A5 encodes a Na+/I- symporter, NIS (Smanik PA et al, 1996). NIS is localized in the basolateral membrane facing the bloodstream and mediates iodide accumulation into thyrocytes.Defects in SLC5A5 cause congenital hypothyroidism due to dyshormonogenesis type 1 (CHDH1) (Fujiwara H et al, 1997). NIS, together with AIT (see next reaction), mediates iodide transfer from blood to the colloid lumen of thyrocytes.
The prototypical transporters of the SLC15 gene family are PEPT1 and PEPT2, which mediate the uptake of every possible di- and tri-peptide. PEPT1 (PTR1) is expressed mainly in the intestine (Liang R et al, 1995; Saito H et al, 1997) while PEPT2 (PTR2) is expressed in the kidney (Liu W et al, 1995).
The human SLC15 gene family encode four proton-coupled oligopeptide transporters; PEPT1 (SLC15A1), PEPT2 (SLC15A2), PHT2 (SLC15A3) and PHT1 (SLC15A4). These cotransporters are part of the Proton-coupled Oligopeptide Transporter (POT) superfamily (also called Peptide Transporter (PTR) family) (Daniel H and Kottra G, 2004).
The SLC17 gene family encode proteins which are organic anion transporters. There are three distinct subfamilies within SLC17; vesicular glutamate transporters (VGLUT1-3 encoded by SLC17A7,6 and 8), type I Na+-coupled phosphate co-transporters (encoded by SLC17A1-4) and a proton-coupled sialic acid co-transporter (encoded by SLC17A5) (Reimer RJ and Edwards RH, 2004). Two members of the SLC5 gene family encode carboxylate transporters, SMCT1 and SMCT2 (Ganapathy V et al, 2008).
The human SLC36A gene family encodes four proton-coupled neutral amino acid transporters, PAT1-4. PAT1 and 2 mediate electroneutral symport of protons and small neutral amino acids like glycine, alanine and proline. PAT3 and 4 are orphans with unknown function (Boll M et al, 2004).
The human gene SLC39A1 encodes the zinc transporter hZIP1. It is ubiquitously expressed (Lioumi M et al, 1999) and mediates the influx of zinc into cells (Gaither LA and Eide DJ, 2001). The human gene SLC39A2 encodes the zinc transporter hZIP2. It is expressed exclusively in prostate and uterine epithelial cells and mediates zinc transport into cells (Gaither LA and Eide DJ, 2000). Normal prostate cells have the ability to accumulate high levels of zinc. In prostate cancer, hZIP1-3 transporters are down-regulated and the cells lose the ability to accumulate zinc. Zinc plays a role as a tumour-suppressing agent thus prostate cells can become cancerous. Silencing of the genes that express hZIP1-3 transporters is a required event for malignancy (Costello LC et al, 1999; Desouki MM et al, 2007). The human gene SLC39A4 encodes the zinc transporter hZIP4 (Kury S et al, 2002). The role of zinc in tumour progression is complicated and, subsequently, so are the role of ZIP transporters. For example, ZIP4 can actually enhance cancer progression (Li M et al, 2007; Li M et al, 2009). Defects in SLC39A4 result in the inherited condition acrodermatitis enteropathica (AE) results from defective absorption of dietary zinc from the duodenum and jejunum. Clinical features include growth retardation, immune system dysfunction, severe dermatitis and mental disorders (Wang K et al, 2002).
E3 ubiquitin-protein ligase Itchy homolog
Aminophospholipids are transported from in the internal to the external side of the plasma membrane
P-type ATPases type IV transport internal-facing APLs to external side of the plasma membrane
The human gene SLC39A6 encodes the zinc transporter ZIP6 (LIV-1). The gene is oestrogen-regulated and has been implicated in metastatic breast cancer. ZIP6 mediates the transport of zinc into cells, is localized to the plasma membrane and is expressed mainly in hormonal tissues such as breast, prostate and brain (Taylor KM et al, 2003). The human gene SLC39A14 encodes the zinc transporter ZIP14. This protein is ubiquitously expressed with higher expression seen in heart, liver and pancreas. ZIP14 is localized to the plasma membrane and mediates zinc influx into cells (Taylor KM et al, 2005).
P-type ATPases type IV transport external-facing APLs to internal side of the plasma membrane
P-type ATPase type IV subfamily transporters may mediate phospholipid transfer
The human gene SLC39A5 encodes the zinc transporter hZIP5 (Wang F et al, 2004). Highest expressions are seen in liver, kidney, pancreas and throughout the small intestine and colon with little expression detected in other tissues. hZIP5 is localized to the basolateral membrane of cells in these tissues. The functionality of ZIP5 as a zinc transporter was determined using mouse protein (mZIP5) (Wang F et al, 2004).
The K+-transporting ATPase mediates the exchange of potassium and hydrogen ions
Amyloid beta-protein: monomer structure and early aggregation states of Abeta42 and its Pro19 alloform
Copper (Cu2+) is essential for many important biological processes such as mitochondrial oxidative phosphorylation, detoxification of free radicals, iron metabolism and neurotransmiter synthesis. Too much influx results in cell poisoning. In humans, there are two member of the SLC31 gene family that are implicated in copper transport. The human gene SLC31A1 encodes human copper transporter 1, hCTR1 and is ubiquitiously expressed, with highest levels seen in the liver.. It was first identified by functional complementation in ctr1-deficient yeast (Zhou B and Gitschier J, 1997). hCTR1 exists as a homotrimer at the plasma membrane of cells (De Feo CJ et al, 2007) and is responsible for high-affinity copper uptake (Lee J et al, 2002). The second gene product, hCTR2, has not be characterized yet.
Copper sequestration by copper-transporting ATPase 2
ATP7B transports cytosolic Cu2+ to Golgi lumen
Zinc is an essential element for all organisms because it serves as a catalytic or structural cofactor for many different proteins. Cellular zinc homoeostasis is co-ordinated through Zn2+-specific transporters which are members of two distinct gene families. Members of the SLC39 gene family (ZRTL-like import proteins1-14, ZIP1-14) are responsible for Zn2+ import into the cytoplasm, either across the plasma membrane or out of intracellular organelles. In contrast, members of the SLC30 gene family (zinc transporters 1-10, ZnT1-10) export Zn2+ from the cytoplasm, either across the plasma membrane into the extracellular space or into intracellular organelles (Murakami M and Hirano T, 2008; Devirgiliis C et al, 2007; Eide DJ, 2006).
Cloning and expression of a human choline/ethanolaminephosphotransferase: synthesis of phosphatidylcholine and phosphatidylethanolamine
Magnesium (Mg2+) is an abundant cation that is important for many intracellular biochemical functions, especially as a cofactor for ATP. Intracellular Mg2+ concentrations must be finely regulated and recently, transporters for this cation have been elucidated. The human genes SLC41A1 and SLC41A2 encode magnesium transport proteins 1 and 2 respectively (MagT1 and MagT2). They both mediate the uptake of Mg2+ into cells (Goytain A and Quamme GA, 2005; Sahni J et al, 2007). A third human gene, SLC41A3, is also thought to encode a MagT protein but has not been characterized yet.
The human gene SLC39A8 encodes the zinc transporter ZIP8 (BIGM103, BCG-induced integral membrane protein in monocyte clone 103 protein). It is highly expressed in the pancreas and localized to the plasma membrane where it mediates the influx of zinc into the cell (Besecker B et al, 2008). The highly homologous mouse ZIP8 have been shown to play important roles in regulating zinc homeostasis and determining sensitivity to cadmium toxicity in mouse testicular endothelium and kidney tissue. It is expected the human transporter plays a similar role (He L et al, 2009). ZIP8 belongs to the LZT subfamily of ZIP transporters.
Calcium is sequestered to the golgi by secretory pathway calcium-ATPases (SPCAs)
ATP2C1/2:Mg2+ transport cytosolic Ca2+ to Golgi lumen
The human gene SLC39A7 encodes the zinc transporter ZIP7 (HKE4, Histidine-rich membrane protein Ke4). It is expressed in many tissues but especially in liver, kidney and the hormonal tissues apart from brain. Unlike the other members of the LZT subfamily, ZIP7 is localized to intracellular membranes of the ER rather than the plasma membrane and mediates zinc efflux into the cytoplasm (Taylor KM et al, 2004).
Sequestration of Ca2+ to intracellular stores
ATP2A1-3 transport cytosolic Ca2+ to ER lumen
The SLC39 gene family encode zinc transporters belonging to the ZIP (Zrt-, Irt-like proteins) family of metal ion transporters. All ZIPs transport metal ions into the cytoplasm of cells, be it across cellular membranes or from intracellular compartments. To date, there are 14 human SLC39 genes that encode the zinc transporters hZIP1-14. There are 9 members which belong to a subfamily of the ZIPs called the LZTs (LIV-1 subfamily of ZIP zinc transporters) (Taylor KM and Nicholson RI, 2003). Of these 14 proteins, four (hZIP9, 11, 12 and 13) have no function determined yet (Eide DJ, 2004).
ATP2A1-3 transport cytosolic Ca2+ to dense tubular network lumen
Sequestration of Ca2+ to dense tubular network lumen
The human gene SLC39A10 encodes the zinc transporter hZIP10. It is thought to be involved in the invasive behaviour of breast cancer cells where depletion of hZIP10 and intracellular zinc levels inhibit the migratory effects these cells (Kagara N et al, 2007). Functional characterization of this transporter was elucidated in the rat orthologue rZip10.
ATP2B1-4 transport cytosolic Ca2+ to extracellular region
GluR3 flip and flop: differences in channel opening kinetics
The human SLC13A5 gene encodes a sodium-coupled citrate transporter, NACT. This gene is expressed mainly in the liver, with lower levels in brain and testis. NACT has a preference for trivalent citrate (Inoue K et al, 2002).
Mammalian sodium/dicarboxylate cotransporters (transport succinate and other Krebs cycle intermediates) fall into two categories based on their substrate affinity. The human gene SLC13A3 encodes a high-affinity sodium/dicarboxlate co-transporter, NaDC3. NaDC3 is expressed in the basolateral membrane of renal proximal tubular epithelial cells, sinusoidal membrane of hepatocytes, and brain synaptosomes. Kinetic studies in human retinal pigment epithelial (HRPE) cells suggest three sodium ions co-transported with every divalent succinate (Wang H et al, 2000).
Aquaporin-9 passively transports glycerol into cell
Acidification of Tf:TfR1 containing endosome
The human SLC30 gene family of solute carriers is thought to participate in the homeostasis of zinc ions and facilitate zinc transport into specialized compartments of the cell such as endosomes, golgi network and synaptic vesicles. There are 10 members of this family, named ZnT1-10. ZnT4, ZnT9 and ZnT10 have no function determined as of yet (Palmiter RD and Huang L, 2004).
The human SLC30A8 gene encodes the zinc transporter ZnT8 which is specifically expressed in pancreatic beta cells (Chimienti et al. 2005). Zinc is required for zinc-insulin crystallization within secretory vesicles of these cells. After glucose stimulation, large amounts of zinc are secreted locally in the extracellular matrix together with insulin. It has been suggested that this co-secreted zinc plays a role in islet cell paracrine and/or autocrine communication (Chimienti F et al, 2006). Loss of function mutations in SLC30A8 are strongly protective against type 2 diabetes, suggesting SLC20A8 inhibition as a therapeutic target in T2D prevention. (Flannick et al. 2014).
Two human genes mediate the transport of zinc into the TGN and they are both localized to the TGN. The human gene SLC30A6 encodes the zinc transporter ZnT6. By Western blot studies, ZnT6 is only found in the brain and lung in human (Huang L et al, 2002).
Aquaporins passively transport glycerol out of cells
The human gene SLC30A5 encodes the zinc transporter ZnT5. This protein is widely expressed but is most abundant in pancreatic beta cells (Kambe T et al, 2002). In these cells, ZnT5 mediates the transport of zinc into secretory granules that contain insulin.
Aquaporins passively transport glycerol into cells
The human gene SLC30A3 encodes zinc transporter ZnT3. Through experiments on the mouse homologue Znt3, it is thought this transporter is expressed mainly in brain and testis and mediated the accumulation of zinc into synaptic vesicles (Palmiter et al, 1996).
Aquaporins passively transport urea out of cells
The human gene SLC30A2 encodes zinc transporter ZnT2. Its function is inferred from experiments using rat Znt2 (Palmiter RD et al, 1996).
Aquaporins passively transport urea into cells
The primary site for absorption of dietary iron is the duodenum. Ferrous iron (Fe2+) is taken up from the gut lumen across the apical membranes of enterocytes and released into the portal vein circulation across basolateral membranes. The human gene SLC11A2 encodes the divalent cation transporter DCT1 (NRAMP2, Natural resistance-associated macrophage protein 2). NRAMP2 resides on the apical membrane of enterocytes and mediates the uptake of ferrous iron into these cells (Tandy S et al, 2000). DCT1 can also accept a broad range of transition metal ions.
Aquaporin-7 passively transports glycerol out of cell
Five human SLC13 genes encode sodium-coupled sulphate, di- and tri-carboxylate transporters located on the plasma membrane. Two transporters (NaS1 and NaS2) co-transport sulphate with sodium. The other members (NaDC1, NaDC3, and NaCT) co-transport sodium with di- and tri-carboxylates such as succinate, citrate and alpha-ketoglutarate (Pajor AM, 2006).
Aquaporin-3 passively transports water out of cell
BESTs transport cytosolic Cl- to extracellular region
The human gene SLC22A3 encodes organic cation transporter OCT3. It is mainly expressed in skeletal muscle, liver, placenta, kidney and heart, and to a lesser extent in brain. OCT3 is involved in the biliary excretion of cationic drugs. In CNS, ganglia and heart, OCT3 regulates the interstitial concentrations of monoamine neurotransmitters and cationic drugs. In placenta, OCT3 is responsible for the release of acetylcholine during nonneuronal cholinergic regulation (Grundemann D et al,1998; Wu X et al, 2000).
The human gene SLC22A4 encodes the ergothioneine transporter (ETT). It was originally discovered as a organic cation/carnitine transporter (OCTN1) (Tamai I et al, 1997) but its main substrate is not carnitine. It is widely expressed and transports ergothioneine more than 100 times more efficiently than tetraethylammonium and carnitine (Grundemann D et al, 2005), leading to the name change from OCTN1 to ETT. Defects in SLC22A4 may be a cause of susceptibility to Crohn disease (CD) (Peltekova VD et al, 2004).
The human gene SLC22A18 encodes organic cation transporter-like protein 2 (ORCTL2). It is expressed to high levels in kidney, liver and colon. ORCTL2 can transport chloroquine and quinidine with the antiport of protons (Reece M et al, 1998). Defects in SLC22A18 may play a role in tumorigenesis (Schwienbacher C et al, 1998).
The human gene SLC22A5 encodes the organic cation/carnitine transporter 2 (OCTN2). OCTN2 is strongly expressed in the kidney, skeletal muscle, heart and placenta (Tamai I et al, 1998). Defects in SLC22A5 are the cause of systemic primary carnitine deficiency (CDSP) (Tang NL et al, 1999) and susceptibility to Crohn disease (CD) (Peltekova VD et al, 2004). The human gene SLC22A15 encodes the fly-like putative transporter1 (FLIPT1). FLIPT1 is a novel transporter highly expressed in kidney and brain is shown to be homologous to other carnitine transporters (Eraly SA and Nigan SK, 2002). The human gene SLC22A16 encodes the organic cation/carnitine transporter 6 (also called the fly-like putative transporter 2, FLIPT2) (Enomoto A et al, 2002). FLIPT2 is strongly expressed in the testis and epididymas as well as generally in other tissues and in leukaemia cells ( Enomoto A et al, 2002; Gong S et al, 2002). All of these transporters are sodium-dependent, high affinity carnitine cotransporters.
Cytosolic PHD2,3 hydroxylates proline residues on HIF1A
The mechanism of adenosine to inosine conversion by the double-stranded RNA unwinding/modifying activity: a high-performance liquid chromatography-mass spectrometry analysis.
The human gene SLC22A6 encodes organic anion transporter1 (OAT1). It was originally characterized in mouse as Novel Kidney Transcript (NKT). OAT1 is located on the basolateral membrane of the proximal tubule in human kidney as well as in the brain (Reid G et al, 1998; Lu R et al, 1999; Hosoyamada M et al, 1999). The human gene SLC22A7 encodes organic anion transporter 2 (OAT2) and is highly expressed in the liver and kidney (Sun W et al, 2001; Kobayashi Y et al, 2005). The human gene SLC22A8 encodes organic anion transporter 3 (OAT3) which is expressed mainly in the brain and kidney (Race JE et al, 1999; Bakhiya A et al, 2003). OAT1-3 transport organic anions such as p-aminohippurate and drugs such as cimetidine and acyclovir. This transport is is coupled with an efflux of one molecule of endogenous dicarboxylic acid such as alpha-ketoglutarate (2-oxoglutarate). OAT2 is classified as both a transporter of organic anions and sulphate conjugates.
Cytosolic PHD2,3 hydroxylates proline residues on EPAS1 (HIF2A)
The organic cation transporters comprise three SLC22 members, OCT1-3. They can transport a wide range of organic cations including weak bases. All transport by OCTs is electrogenic, sodium-independent and bidirectional. Two further organic cation transporters mediate transport of ergothioneine and carnitine (Koepsell H and Endou H, 2004).
TRPM4,5 transport extracellular Na+ to cytosol
Organic anion transporters (OATs) mediate the renal absorption and excretion of a broad range of endogenous substrates and anionic drugs such as diuretics and NSAIDs. Five members belong to these polyspecific transporters (OAT1-4 and URAT1) and are predominantly expressed in the kidney (Koepsell H and Endou H, 2004; Rizwan AN and Burckhardt G, 2007; Ahn SY and Bhatnagar V, 2008).
TRPs transport extracellular Ca2+ to cytosol
The human gene SLC22A7 encodes organic anion transporter 2 (OAT2) and is highly expressed in the liver and kidney (Sun W et al, 2001; Kobayashi Y et al, 2005). The human gene SLC22A11 encodes organic anion transporter 4 (OAT4) which is highly expressed in the placenta and kidney (Cha SH et al, 2000; Ekaratanawong S et al, 2004). Both of these transporters mediate the influx of sulfate conjugates with antiport of dicarboxylic acid. OAT2 is classified as both a transporter of organic anions and sulphate conjugates.
The SLC22 gene family of solute carriers function as organic cation transporters (OCTs), cation/zwitterion transporters (OCTNs) and organic anion transporters (OATs). The SLC22 family belongs to the major facilitator superfamily and comprises uniporters, symporters and antiporters.Most of this family are polyspecific transporters. Since many of these transporters are expressed in the liver, kidney and intestine, they play an important role in drug absorption and excretion. Substrates include xenobiotics, drugs, and endogenous amine compounds (Koepsell H and Endou H, 2004).
SLC17A3-2 transports cytosolic urate to extracellular region
SLC17A3-1 cotransports extracellular Na+ and Pi to cytosol
BESTs transport cytosolic HCO3- to extracellular region
The human gene SLC18A1 encodes the vesicular monoamine transporter 1 (VMAT1) (Erickson JD et al, 1996). VMAT1 is mainly expressed in neuroendocrine cells. The human gene SLC18A2 encodes VMAT2 (Erickson JD and Eiden LE, 1993). Both transporters can mediate the transport of biogenic amines into secretory vesicles, which can then discharge their contents into the extracellular space by exocytosis. Predominant biogenic amines these proteins can transport are serotonin, dopamine, adrenaline, noradrenaline and histamine.
The amino acid glycine plays an important role in neurotransmission. Its action is terminated by rapid re-uptake into the pre-synaptic terminal or surrounding glial cells. This re-uptake is mediated by the sodium- and chloride-dependent glycine transporters 1 and 2 (GLYT1 and GLYT2 respectively). GLYT1 is encoded by the human gene SLC5A9 and is expressed in the brain, liver, kidney, pancreas, lung and placenta (Kim KM et al, 1994). GLYT2 is encoded by the human gene SLC6A5 and is predominantly expressed in the medulla (Morrow JA et al, 1998). Defects in SLC6A5 cause startle disease (STHE or hyperekplexia). STHE is is a human neurological disorder characterized by an excessive startle response (Rees MI et al, 2006).
Noradrenaline (norepinephrine) is a neurotransmitter whose action is mediated by the noradrenaline transporter NAT1. NAT1 is a monoamine transporter that transports noradrenaline from the synapse back to its vesicles for storage until later use. NAT1 is encoded by the human gene SLC6A2 and is expressed in the CNS and adrenal gland (Pacholczyk T et al, 1991). Defects in SLC6A2 results in orthostatic intolerance (OI), which is a syndrome characterized by lightheadedness, fatigue and development of symptoms during upright standing, relieved by sitting back down again (Shannon JR et al, 2000).
Six SLC gene families encode proteins which mediate transport of metals. The families are SLC11, SLC30, SLC31, SLC39, SLC40 and SLC41 (He L et al, 2009; Bressler JP et al, 2007).
The human gene SLC22A1 expresses the organic cation transporter 1 (OCT1) mainly in the liver. It can mediate the reversible transport of a broad array of organic cations with various structures and molecular weights including the model compounds 1-methyl-4-phenylpyridinium (MPP), tetraethylammonium (TEA), N-1-methylnicotinamide (NMN) and 4-(4-(dimethylamino)styryl)-N-methylpyridinium (Zhang L et al, 1998; Gorboulev V et al, 1997).
Cytosolic Cl- is transported to extracellular region by ANOs
ANOs transport cytosolic Cl- to extracellular region
RAF1:SGK:TSC22D3:WPP ubiquitinates SCNN channels
The human SLC5A7 gene encodes a sodium- and chloride-dependent, high affinity choline transporter, CHT (Apparsundaram S et al, 2000). CHT transports choline from the extracellular space into neuronal cells and is dependent on Na+ and Cl- ions for transport (Okuda T and Haga T, 2000). Choline uptake is the rate-limiting step in acetylcholine synthesis.
CLCN1/2/KA/KB transport cytosolic Cl- to extracellular region
The SLC6 gene family encodes proteins that mediate neurotransmitter uptake thus terminating a synaptic signal. The proteins mediate transport of GABA (gamma-aminobutyric acid), norepinephrine, dopamine, serotonin, glycine, taurine, L-proline, creatine and betaine. These transporters are mainly present in the CNS and PNS (Chen NH et al, 2004).
UNC79:UNC80:NALCN transports cytosolic Na+ to extracellular region
The glycine receptor complex is permeable to Cl- when glycine binds to it
GLRA:GLRB:Gly transports extracellular Cl- to cytosol
The human gene SLC22A2 encodes the organic cation transporter OCT2. It is expressed in a variety of tissues, especially the kidney and placenta. OCT2 can mediate the reversible transport of a broad array of organic cations with various structures and molecular weights including the model compounds 1-methyl-4-phenylpyridinium (MPP), tetraethylammonium (TEA), N-1-methylnicotinamide (NMN) and 4-(4-(dimethylamino)styryl)-N-methylpyridinium (Gorboulev V et al, 1997). Pharmaceuticals that up-regulate OCT2 in the kidney can increase the renal excretion of cationic drugs.
Extracellular Na+ is transported to cytosol by SCNN channel
SCNN channels transport extracellular Na+ to cytosol
Extracellular Na+ is transported to cytosol by ASICs
ASICs transport extracellular Na+ to cytosol
SOD1 apoenzyme binds CCS:Cu1+ (mitochondrial)
CCS transfers Cu to SOD1 (mitochondrial)
SOD1 catalyzes 2H+ + 2O2.- => O2 + H2O2 (cytosol)
SOD1 catalyzes 2H+ + O2.- => O2 + H2O2 (mitochondrial intermembrane space)
Calmodulin-kinases: modulators of neuronal development and plasticity
Missense mutations of the transforming growth factor beta type II receptor in human head and neck squamous carcinoma cells
HIF-alpha translocates from cytosol to nucleus
Formation of HIF:CBP:p300 complex at promoters
HIF-alpha binds ARNT (HIF1-beta) forming HIF-alpha:ARNT
Cytosolic VHL:EloB,C:CUL2:RBX1 binds hydroxyprolyl-HIF-alpha
Nuclear VHL:EloB,C:CUL2:RBX1 binds hydroxyprolyl-HIF-alpha
Nuclear PHD1,3 hydroxylates proline residues on HIF1A
Nuclear PHD1,3 hydroxylates proline residues on HIF3A
ub-HIF-alpha:VHL:EloB,C:CUL2:RBX1 translocates from the nucleus to the cytosol
SLIT-ROBO Rho GTPase-activating protein 3
Cytosolic VCB complex ubiquitinylates hydroxyprolyl-HIF-alpha
The links between axin and carcinogenesis
Nuclear VCB complex ubiquitinylates HIF-alpha
Genomic structure and promoter analysis of the human alpha1, 6-fucosyltransferase gene (FUT8)
Nuclear PHD1,3 hydroxylates proline residues on EPAS1 (HIF2A)
Cytosolic PHD2,3 hydroxylates proline residues on HIF3A
Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3
Dissociation of HSF1:HSP90 complex in the nucleus
Phosphorylation of HSF1 at Ser326 induces transactivation
Phosphorylation of HSF1 at Ser230 induces transactivation
SLIT-ROBO Rho GTPase-activating protein 1
Dissociation of cytosolic HSF1:HSP90:HDAC6:PTGES3 upon sensing protein aggregates
Dissociation of cytosolic HSF1:HSP90 complex
PRDX6:GSTP1 catalyzes 2 glutathione, reduced + H2O2 => glutathione, oxidized + 2 H2O
PRDX1,2,5 catalyze TXN reduced + H2O2 => TXN oxidized + 2H2O
GPX7,8 catalyze peroxidation of P4HB (PDI)
TXNRD2 catalyzes the reduction of TXN2 by NADPH
GPX3 catalyzes 2 glutathione, reduced + H2O2 => glutathione, oxidized + 2 H2O
PRDX3,5 catalyze TXN2 reduced + H2O2 => TXN2 oxidized + 2H2O
Hereditary orotic aciduria and other disorders of pyrimidine metabolism
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 2663-2704
GSR catalyzes glutathione (oxidized) + NADPH + H+ => 2 glutathione (reduced) + NADP+
H2O2 diffuses from the mitochondrial matrix to the cytosol
SOD3 catalyzes 2H+ + 2O2.- => O2 + H2O2 (extracellular)
SOD2 catalyzes 2H+ + 2O2.- => O2 + H2O2 (mitochondrial matrix)
Activated human MKK3/MKK6 phosphorylates p38 MAPK complexed with MAPKAPK5
Phosphorylated MKK3/MKK6 migrates to nucleus
Activated human MKK3/MKK6 phosphorylates p38 MAPK complexed with MAPKAPK2 or MAPKAPK3
Active p38 MAPK phosphorylates MAPKAPK2 or 3
MAP3K5 (ASK1) phosphorylates MAP2K4 (SEK1)
Phosphorylation of human JNKs by activated MKK4/MKK7
Activated human JNKs migrate to nucleoplasm
Different human TFIIIB activities direct RNA polymerase III transcription from TATA-containing and TATA-less promoters
Mammalian wax biosynthesis. I. Identification of two fatty acyl-Coenzyme A reductases with different substrate specificities and tissue distributions
ROS oxidize thioredoxin and activate MAP3K5
Single eubacterial origin of eukaryotic sulfide:quinone oxidoreductase, a mitochondrial enzyme conserved from the early evolution of eukaryotes during anoxic and sulfidic times
Constitutive and inducible expression and regulation of vascular endothelial growth factor
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Mutations in GLUT2, the gene for the liver-type glucose transporter, in patients with Fanconi-Bickel syndrome
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Nuclear envelope phosphatase 1-regulatory subunit 1 (formerly TMEM188) is the metazoan Spo7p ortholog and functions in the lipin activation pathway
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Three-dimensional structure of the bifunctional protein PCD/DCoH, a cytoplasmic enzyme interacting with transcription factor HNF1.
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Constitutive PI3K/AKT Signaling in Cancer
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GABA synthesis, release, reuptake and degradation
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Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling.
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Biochemical Pathways - An Atlas of Biochemistry and Molecular Biology
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Biochemistry - The Chemical Reactions of Living Cells 2nd Edn.
Lehninger - Principles of Biochemistry 4th Edn.
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Two period homologs: circadian expression and photic regulation in the suprachiasmatic nuclei
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Phosphorylation of 2',3'-dideoxyinosine by cytosolic 5'-nucleotidase of human lymphoid cells
Design and expression of human alpha7 nicotinic acetylcholine receptor extracellular domain mutants with enhanced solubility and ligand-binding properties
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Diabetes-associated sustained activation of the transcription factor nuclear factor-kappaB
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Protein arginine methylation in mammals: who, what, and why
Sanfilippo disease type D: deficiency of N-acetylglucosamine-6-sulfate sulfatase required for heparan sulfate degradation
Hexoses like glucose, galactose and fructose serve as basic fuel molecules for eukaryotic cells. Indeed, glucose is the main energy source for mammalian cells. These sugars are unable to diffuse across cellular membranes, and require transporter proteins for entry into and exit out of cells. Four gene families encode hexose transporter proteins (He et al, 2009). SLC2 family contains 14 genes and encode facilitative glucose transporters (GLUTs) (Uldry M and Thorens B, 2004). SLC5 family contains 12 genes and encode Na+/glucose symporters (Wright EM and Turk E, 2004). SLC37 family contains 4 members and encode sugar-phosphate/phosphate exchangers (Bartoloni L and Antonarakis SE, 2004). SLC45 family has 4 members and encode putative sugar/H+ symporters.
The plasma membrane-associated protein SLC28A3 mediates the transport of one molecule of adenosine, cytidine, guanosine, inosine, thymidine, or uridine, and two sodium ions, from the extracellular space to the cytosol.
The plasma membrane-associated protein SLC28A1 mediates the transport of one molecule of 2'-deoxyadenosine, adenosine, cytidine, thymidine, or uridine, and one sodium ion, from the extracellular space to the cytosol.
The plasma membrane-associated protein SLC28A2 mediates the transport of one molecule of adenosine, guanosine, inosine, or uridine, and one sodium ion, from the extracellular space to the cytosol.
The plasma membrane-associated protein SLC29A1 mediates the reversible transport of one molecule of adenosine, cytosine, guanosine, inosine, thymidine, or uridine from the extracellular space to the cytosol.
The plasma membrane-associated protein SLC29A2 mediates the reversible transport of one molecule of adenine, adenosine, cytidine, cytosine, guanine, guanosine, hypoxanthine, inosine, thymidine, thymine, uracil, or uridine from the cytosol to the extracellular space.
The plasma membrane-associated protein SLC29A1 mediates the reversible transport of one molecule of adenosine, guanosine, inosine, or uridine from the cytosol to the extracellular space.
The plasma membrane-associated protein SLC29A2 mediates the reversible transport of one molecule of adenine, adenosine, cytidine, cytosine, guanine, guanosine, hypoxanthine, inosine, thymidine, thymine, uracil, or uridine from the extracellular space to the cytosol.
The human gene SLC29A3 encodes the equilibrative nucleoside transporter 3 (ENT3). It is abundant in many tissues, especially the placenta and is localized intracellularly on the lysosomal membrane. ENT3 mediates the reversible transport of nucleosides and the nucleobase adenine (Baldwin SA et al, 2005). Defects in SLC29A3 are the cause of H syndrome, an autosomal recessive disorder(Molho-Pessach V et al, 2008).
The human gene SLC33A1 encodes acetyl-CoA transporter AT1 (Kanamori A et al, 1997).Acetyl-CoA is transported to the lumen of the Golgi apparatus, where it serves as the substrate of acetyltransferases that modify the sialyl residues of gangliosides and glycoproteins. Defects in SLC33A1 are the cause of spastic paraplegia autosomal dominant type 42 (SPG42) which is a neurodegenerative disorder (Lin P et al, 2008).
Two families of transport proteins mediate the movement of nucleosides and free purine and pyrimidine bases across the plasma membrane. Equilibrative nucleoside transporters allow the movement of these molecules along concentration gradients into or out of cells (Baldwin et al. 2003); concentrative nucleoside transporters actively transport nucleosides into cells by coupling their transport to the inward movement of sodium ions (Gray et al. 2003). Of the four human equilibrative nucleoside transporters, two are well characterized. SLC29A1 (solute carrier family 29 (nucleoside transporters), member 1) mediates the transport of nucleosides across the plasma membrane. SLC29A2 (solute carrier family 29 (nucleoside transporters), member 2) mediates the transport of both nucleosides and free bases. Transporter specificities were determined by expressing cloned human genes in Xenopus oocytes or in mammalian cultured cell lines whose own nucleotide transporters had been disrupted by mutation. These studies establish that the transport processes are specific and saturable, and that the multiple nucleotides and bases compete for a single binding site on each transporter. Some features of SLC29A2 specificity are complex. For example, in the Xenopus oocyte system, radiolabeled uracil and adenine are taken up, and an excess of either molecule inhibits uptake of radiolabeled hypoxanthine, while in the cultured mammalian cell system, neither adenine nor uracil can inhibit uptake of radiolabeled uridine. If these results reflect ENT2 function in vivo, they indicate that the net movement of a nucleoside or base across the cell membrane is determined not only by its own concentrations in the extracellular space and the cytosol, but also by the concentrations of the other nucleosides and bases competing for access to the transporter. The human genome encodes three concentrative transporters, SLC28A1, 2, and 3 (solute carrier family 28 (sodium-coupled nucleoside transporter), member 1, 2, and 3). All three genes have been cloned, and expression of the human proteins in Xenopus oocytes has allowed their transport properties to be determined. SLC28A1 mediates the uptake of pyrimidine nucleosides and adenosine (Ritzel et al. 1997); SLC28A2 the uptake of purine nucleosides and uridine (Wang et al. 1997); and SLC28A3 the uptake of purine and pyrimidine nucleosides (Ritzel et al. 2001). Amino acid sequence motifs that determine the specificities of these transporters have been identified in studies of chimeric and mutant proteins (Loewen et al. 1999). SLC28A3 protein co-transports two sodium ions per nucleoside; SLC28A1 and 2 transport one sodium per nucleoside (Ritzel et al. 2001). Physiological roles for nucleoside and base transport include provision of nucleosides to cells with little capacity to synthesize these molecules de novo, and regulation of extracellular levels of adenosine, which is released from muscle during intense exercise and has signaling properties. In kidney and intestinal epithelia, the combination of apically localized CNT transporters and basolaterally localized ENT transporters provides a mechanism for net transport of nucleosides (Mangravite et al. 2003). These transporters also mediate the uptake of nucleoside analogs used clinically as anti-viral and anti-tumor drugs. Orthologs of human concentrative and equilibrative transporter proteins have been identified in many eukaryotes, but functional studies of transporters even from organisms closely related to humans (e.g. rat, Gerstin et al. 2002) have revealed differences in substrate specificities. Prediction of drug uptake and other functions of these molecules by human - model organism orthology is thus risky.
The human gene SLC29A4 encodes the equilibrative nucleoside transporter 4 (ENT4). It is ubiquitously expressed and mediates the reversible transport of the nucleoside adenosine at acidic pH (this transport is absent at pH 7.4) (Barnes K et al, 2006). ENT4 has also been shown to mediate the transport of biogenic amines such as serotonin, dopamine, norepinephrine and epinephrine. For this reason, ENT4 is also known as the plasma membrane monoamine transporter (PMAT) (Engel K et al, 2004).
The human gene SLC35A3 encodes the UDP-GlcNAc transporter (Ishida N et al, 1999). It is ubiquitously expressed and resides on the Golgi membrane where it transports UDP- N-acetylglucosamine (GlcNAc) into the Golgi lumen in exchange for UMP.
The human gene SLC35B4 encodes the bifunctional UDP-xylose and UDP-N-acetylglucosamine transporter YEA4. YEA4 resides on the Golgi membrane and mediates the influx of UDP-xylose into the lumen (Ashikov A et al, 2005).
The human gene SLC35A1 encodes the CMP-sialic acid transporter which mediates the antiport of CMP-sialic acid (CMP-Neu5Ac) into the Golgi lumen in exchange for CMP (Ishida et al. 1996). Defects in SLC35A1 are the cause of congenital disorder of glycosylation type 2F (CDG2F; MIM:603585). CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation (Martinez-Duncker et al. 2005).
The human gene SLC35A2 encodes the UDP-galactose transporter (Miura N et al, 1996). It is located on the Golgi membrane and mediates the antiport of UDP-Gal into the Golgi lumen in exchange for UMP. This transporter is also known to transport UDP-N-acetylgalactosamine (UDP-GalNAc) in the same way as UDP-Gal (Segawa H et al, 2002).
PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth
The human gene SLC35B4 encodes the bifunctional UDP-xylose and UDP-N-acetylglucosamine transporter YEA4. YEA4 resides on the Golgi membrane and mediates the influx of UDP-N-acetylglucosamine into the lumen (Ashikov A et al, 2005).
The human gene SLC35C1 encodes the GDP-fucose transporter FUCT1. It resides on the Golgi membrane and mediates the transport of UDP-fucose into the Golgi lumen. Defects in SLC35C1 causes the congenital disorder of glycosylation type 2C, also known as leukocyte adhesion deficiency type II (LAD2) (Lubke T et al, 2001).
Herc5, an interferon-induced HECT E3 enzyme, is required for conjugation of ISG15 in human cells
Of the six fatty acid transporter proteins (FATP) characterized, only three have been shown to mediate the influx into cells of long chain fatty acids (LCFAs); FATP1, 4 and 6. They have been shown to transport the prototypical LCFA oleic acid (OLEA) but are believed to be able to transport LCFAs with chain lengths longer than 10 carbons. FATP1 is highly expressed in adipose tissue and muscle (Hatch GM et al, 2002). FATP4 is the major intestinal LCFA transporter (Fitscher BA et al, 1998; Stahl A et al, 1999). FATP6 is localized to cardiac myocytes (Gimeno RE et al, 2003).
Nucleotide sugars are used as sugar donors by glycosyltransferases to create the sugar chains for glycoconjugates such as glycoproteins, polysaccharides and glycolipids. Glycosyltransferases reside mainly in the lumen of the Golgi apparatus and endoplasmic reticulum (ER) whereas nucleotide sugars are synthesized in the cytosol. The human solute carrier family SLC35 encode nucleotide sugar transporters (NSTs) which can mediate the antiport of nucleotide sugars in exchange for the corresponding nucleoside monophosphates (eg. UMP for UDP-sugars). Owing to their function, NSTs are primarily located on Golgi and ER membranes (He L et al, 2009; Handford M et al, 2006; Ishida N and Kawakita M, 2004).
Three organic anion transporting polypeptides (OATPs; now called solute carrier organic anion transporters, SLCOs) are able to mediate the transport of thryoid hormones, predominantly thyroxine (T4) and triiodothyronine (T3) (Fujiwara K et al, 2001). SLCO1B1 (formerly OATP-C), which can also transport bile salts, is mainly expressed in the liver (Abe T et al, 1999; Hsiang B et al, 1999). SLCO4A1 (formerly OATP-E) is mainly expressed in peripheral tissue and has a broad substrate specificty (Tamai I et al, 2000). SLCO1C1 (formerly OATP-F) is highly expressed in brain and is also a high affinity thyroid hormone transporter (Pizzagalli F et al, 2002).
Long chain fatty acids (LCFAs) are involved in many cellular functions. They can be used as an important source of energy by skeletal muscle and heart tissues. Also, they are used in the production of hormones which can regulate inflammation, blood pressure, the clotting process, blood lipid levels and the immune response. Fatty acid transporter proteins (FATPs) are a family of proteins which mediate fatty acid uptake into cells when overexpressed. FATPs also possess enzymatic activity, the details of which are captured elsewhere. There are 6 human genes of the SLC27A family which encode for FATP1-6 (Stahl A, 2004; Gimeno RE, 2007). To date, only FATP1, 4 and 6 have demonstrable transporter function. Fatty acids with carbon chain lengths of more than 10 are the most likely substrates for these transporters.
The human gene SLC35D2 encodes the UDP-N-acetylglucosamine/UDP-glucose/GDP-mannose transporter (UGTREL8; homolog of Fringe connection protein 1, HFRC1). It resides on the Golgi membrane where it mediates the antiport of GDP-mannose into the Golgi lumen in exchange for GMP (Suda T et al, 2004; Ishida N et al, 2005).
This pathway groups the processes mediated by SLC transporters, by which vitamins and cofactors, as well as nucleosides, nucleotides, nucleobases, and related molecules cross lipid bilayer membranes.
The human gene SLCO2A1 encodes prostaglandin transporter PGT. It is ubiquitously expressed and can transport PGD2, PGE1, PGE2 and PGF2A (Lu R et al, 1996).
SLCO2B1 (formerly OATP-B) is abundantly expressed in human liver, where it is localized at the basolateral membrane of hepatocytes. It has a narrow substrate range, able to transport bromosulphophthalein (BSP), estrone-3-sulphate and dehydroepiandrosterone-sulphate (DHEAS) (Kullak-Ublick GA et al, 2001).
Digoxin is a commonly prescribed drug for the treatment of heart failure. It is mainly eliminated from the body by the kidneys. Human SLCO4C1 (formerly OATP-H) is the first member of the organic anion transporting polypeptide (OATP) family expressed in human kidney. It is found on the baolateral membrane of the nephron and is thought to be the first step of the transport of digoxin into urine (Mikkaichi T et al, 2004).
Organic anion transporting polypeptides (OATPs) are membrane transport proteins that mediate the sodium-independent transport of a wide range of amphipathic organic compounds including bile salts, steroid conjugates, thyroid hormones, anionic oligopeptides and numerous drugs (Hagenbuch B and Meier PJ, 2004).
Correlation between subunit interactions and enzymatic activity of phosphorylase a. Method for determining equilibrium constants from initial rate measurements
Aquaporin-9 (AQP9) and AQP10 are 6-pass transmembrane proteins that passively transport urea across the plasma membrane through a pore in each subunit of a homotetramer.
Aquaporin-3 (AQP3), AQP7, AQP9, and AQP10 are 6-pass transmembrane proteins that passively transport glycerol across the plasma membrane through a pore in each subunit of a homotetramer.
Aquaporin-0 (AQP0, also known as MIP), AQP1, AQP2, AQP3, AQP4, AQP5, AQP7, AQP8, AQP9, and AQP10 are 6-pass transmembrane proteins that passively transport water across the plasma membrane according to the concentration gradient. Each molecule contains a water channel and subunits assemble into homotetramers. In principle water can move in either direction through an aquaporin, however in vivo flow may occur in only one direction. Conductance of water by AQP0 and AQP11 are low relative to other aquaporins.
Proteins with transporting functions can be roughly classified into 3 categories: ATP-powered pumps, ion channels, and transporters. Pumps utilize the energy released by ATP hydrolysis to power the movement of the substrates across the membrane, against their electrochemical gradient. Channels at the open state can transfer the substrates (ions or water) down their electrochemical gradient, at an extremely high efficiency (up to 108 s-1). Transporters facilitate the movement of a specific substrate âeither against or following their concentration gradient, at a lower speed (about 102 -104 s-1); as generally believed, conformational change of the transporter protein is involved in the transfer process. According to the Human Genome Organization (HUGO) Gene Nomenclature Committee, all human transporters can be grouped into the solute-carrier (SLC) superfamily. Currently, there are 55 SLC families in the superfamily, with a total of at least 362 putatively functional protein-coding genes (Hediger et al, 2004; He et al., 2009). At least 20-25% amino-acid sequence identity is shared by members belonging to the same SLC family. No homology is shared between different SLC families. While the HUGO nomenclature system by definition only includes human genes, the nomenclature system has been informally extended to include rodent species through the use of lower cases letters (e.g., Slc1a1 denotes the rodent ortholog of the human SLC1A1 gene). And it's worthwhile to mention that pumps, channels and aquporins are not included in SLC superfamily.
Aquaporin-3 (AQP3) passively transports water and glycerol across the plasma membrane according to the osmotic gradient. AQP3 is expressed in airway epithelia, secretory glands, skin, the collecting ducts of the kidney, and the basolateral surface of intestinal epithelium..
In the kidney water and solutes are passed out of the bloodstream and into the proximal tubule via the slit-like structure formed by nephrin in the glomerulus. Water is reabsorbed from the filtrate during its transit through the proximal tubule, the descending loop of Henle, the distal convoluted tubule, and the collecting duct. Aquaporin-1 (AQP1) in the proximal tubule and the descending thin limb of Henle is responsible for about 90% of reabsorption (as estimated from mouse knockouts of AQP1). AQP1 is located on both the apical and basolateral surface of epithelial cells and thus transports water through the epithelium and back into the bloodstream. In the collecting duct epithelial cells have AQP2 on their apical surface and AQP3 and AQP4 on their basolateral surface to transport water across the epithelium. The permeability of the epithelium is regulated by vasopressin, which activates the phosphorylation and subsequent translocation of AQP2 from intracellular vesicles to the plasma membrane.
Recognition and binding of the mRNA cap by the cap-binding complex
Methylation of GMP-cap by RNA Methyltransferase
Dissociation of transcript with 5'-GMP from GT
Transfer of GMP from the capping enzyme GT site to 5'-end of mRNA
Formation of the CE:GMP intermediate complex
Hydrolysis of the 5'-end of the nascent transcript by the capping enzyme
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Protein Kinase C, unconventional isoforms
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Differential expression of exons 1a and 1c in mRNAs for sterol regulatory element binding protein-1 in human and mouse organs and cultured cells
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Cleavage of Intronless Pre-mRNA at 3'-end
Addition of nucleotides leads to transcript elongation
Hyperphosphorylation (Ser2) of RNA Pol II CTD by P-TEFb complex
cAMP-specific 3',5'-cyclic phosphodiesterase 4A
Separation of elongating transcript from template
Pol II elongation complex moves on the template as transcript elongates
SPT5 subunit of Pol II binds the RNA triphosphatase (RTP)
DSIF complex binds to RNA Pol II (hypophosphorylated)
Hypophosphorylation of RNA Pol II CTD by FCP1P protein
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High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A
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High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B
cAMP-specific 3',5'-cyclic phosphodiesterase 4D
cAMP-specific 3',5'-cyclic phosphodiesterase 4B
cAMP-specific 3',5'-cyclic phosphodiesterase 4C
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RNA Polymerase II CTD (phosphorylated) binds to CE
Newly Formed Phosphodiester Bond Stabilized and PPi Released
Nucleophillic Attack by 3'-hydroxyl Oxygen of nascent transcript on the Alpha Phosphate of NTP
NTP Binds Active Site of RNA Polymerase II
RNA Polymerase II Promoter Opening: First Transition
Addition of nucleotides between position +11 and +30
Addition of nucleotides 10 and 11 on the growing transcript: Third Transition
Addition of the fourth nucleotide on the Nascent Transcript: Second Transition
Addition of the third nucleotide on the nascent transcript
Inositol 1,4,5-trisphosphate receptor type 2
Identification and expression of a cDNA for human glycolate oxidase
Phosphorylation (Ser5) of RNA pol II CTD
Extrusion of 5'-end of 30 nt long transcript through the pore in Pol II complex
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Molecular genetics of mucopolysaccharidosis type IIIA and IIIB: Diagnostic, clinical, and biological implications
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Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing
Resumption of elongation after recovery from pausing
Human xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site: roles of active site residues in binding and activation of purine substrate
TFIIS-mediated recovery of elongation from arrest
2-4 nt.backtracking of Pol II complex on the template leading to elongation pausing
Abortive termination of elongation after arrest
Abortive termination of early transcription elongation by DSIF:NELF
Recognition and Binding of Core Promoter Elements by TFIID
Fall Back to Closed Pre-initiation Complex
Binding of TFIIE to the growing preinitiation complex
Recruitment of RNA Polymerase II Holoenzyme by TFIIF to the pol II promoter:TFIID:TFIIA:TFIIB complex
Formation of the closed pre-initiation complex
Cloning, characterization and chromosomal assignment of NBC4, a new member of the sodium bicarbonate cotransporter family
Glucagon-like peptide-1: regulation of insulin secretion and therapeutic potential
Abortive Initiation After Second Transition
Initiation of RNA Polymerase III Productive Transcription
Resumption of RNA Polymerase III Productive Transcription
RNA Polymerase III Termination and release of transcribed mRNA
RNA Polymerase III Transcriptional Pause at Terminator Sequence
RNA Polymerase III Simple Start Sequence Initiation At Type 2 Promoters
EGF-like module-containing mucin-like hormone receptor-like 2
RNA Polymerase III Promoter Opening at Type 1 Promoters
RNA Polymerase III Promoter Opening at Type 2 Promoters
RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites
RNA Polymerase III Simple Start Sequence Initiation At Type 1 Promoters
RNA Polymerase III Abortive Initiation At Type 1 Open Promoters
RNA Polymerase III Abortive Initiation At Type 2 Open Promoters
RNA Polymerase III Productive Transcription
Group I Metabotropic glutamate receptors
YARS (cytosolic tyrosyl tRNA synthetase) catalyzes the reaction of tyrosine, tRNA(Tyr), and ATP to form Tyr tRNA(Tyr), AMP, and pyrophosphate. The enzyme, a class I tRNA synthetase, is a homodimer (Yang et al. 2003). Mutations in the YARS gene are associated with dominant-intermediate Charcot-Marie-Tooth disease â a form of peripheral neuropathy characterized by axon and Schwann cell dysfunction (Jordanova et al. 2006).
VARS (cytosolic valyl tRNA synthetase) catalyzes the reaction of valine, tRNA(Val), and ATP to form Val-tRNA(Val), AMP, and pyrophosphate. The enzyme is a class I tRNA synthetase (Vilalta et al. 1993).
Phosphodiesterases, dual (cAMP, cGMP) activity
cGMP-inhibited 3',5'-cyclic phosphodiesterase 3A
cGMP-dependent 3',5'-cyclic phosphodiesterase
NARS2 (mitochondrial asparaginyl tRNA synthetase) catalyzes the reaction of asparagine, mitochondrial tRNA(Asn), and ATP to form Asn-tRNA(Asn), AMP, and pyrophosphate. The NARS2 gene has been identified by computational analysis of the human genome sequence; its function has been inferred from those of the biochemically characterized mitochondrial aspartyl and tyrosyl tRNA synthetases (Bonnefond et al. 2005).
DARS2 (mitochondrial aspartyl tRNA synthetase) catalyzes the reaction of aspartate, mitochondrial tRNA(Asp), and ATP to form Asp tRNA(Asp), AMP, and pyrophosphate. The enzyme, a class II tRNA synthetase, is a homodimer (Bonnefond et al. 2005). Homozygosity for DARS2 mutations is associated with leukoencephalopathy with brainstem and spinal cord involvement plus lactate elevation (Scheper et al 2007).
EARS2 (mitochondrial glutamyl tRNA synthetase) catalyzes the reaction of glutamate, mitochondrial tRNA(Glu), and ATP to form Glu-tRNA(Glu), AMP, and pyrophosphate. The EARS2 gene has been identified by computational analysis of the human genome sequence; its function has been inferred from those of the biochemically characterized mitochondrial aspartyl and tyrosyl tRNA synthetases (Bonnefond et al. 2005).
QARS (mitochondrial glutaminyl tRNA synthetase) catalyzes the reaction of glutamine, tRNA(Gln), and ATP to form Gln-tRNA(Gln), AMP, and pyrophosphate. The enzyme is a class I tRNA synthetase. The same gene encodes both the cytosolic and mitochondrial QARS enzymes (Lamour et al. 1994).
Cytosolic PPA1 (pyrophosphatase (inorganic) 1) catalyzes the hydrolysis of pyrophosphate to yield two molecules of orthophosphate. The enzyme, a homodimer, requires Mg++ for activity (Fisher et al. 1974; Pynes and Younathan 1967; Thuiller et al. 1978).
Cytosolic tRNA synthetases catalyze the reactions of tRNAs encoded in the nuclear genome, their cognate amino acids, and ATP to form aminoacyl-tRNAs, AMP, and pyrophosphate. Eight of the tRNA synthetases, those specific for arginine, aspartate, glutamate and proline, glutamine, isoleucine, leucine, lysine, and methionine, associate to form a complex with three accessory proteins. Each of the component synthetases is active in vitro as a purified protein; complex formation is thought to channel aminoacylated tRNAs more efficiently to the site of protein synthesis in mRNA:ribosome complexes (Quevillon et al. 1999; Wolfe et al. 2003, 2005).
AARS2 (mitochondrial alanyl tRNA synthetase) catalyzes the reaction of alanine, mitochondrial tRNA(Ala), and ATP to form Ala-tRNA(Ala), AMP, and pyrophosphate. The AARS2 gene has been identified by computational analysis of the human genome sequence; its function has been inferred from those of the biochemically characterized mitochondrial aspartyl and tyrosyl tRNA synthetases (Bonnefond et al. 2005).
RARS2 (mitochondrial arginyl tRNA synthetase) catalyzes the reaction of arginine, mitochondrial tRNA(Arg), and ATP to form Arg tRNA(Arg), AMP, and pyrophosphate. The enzyme is a class I tRNA synthetase. Homozygosity for RARS2 mutations has been associated with pontocerebellar hypoplasia â a disease characterized by a severe reduction in cerebellum and brainstem size (Edvardson et al. 2007).
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
After transcription, some RNA molecules are altered to contain bases not encoded in the genome. Most often this involves the editing or modification of one base to another, but in some organisms can involve the insertion or deletion of a base. Such editing events alter the coding properties of mRNA. RNA editing can be generally defined as the co- or post transcriptional modification of the primary sequence of RNA from that encoded in the genome through nucleotide deletion, insertion, or base modification mechanisms. There are two pathways of RNA editing: the substitution/conversion pathway and the insertion/deletion pathway. The insertion/deletion editing occurs in protozoans like Trypanosoma, Leishmania; in slime molds like Physarum spp., and in some viral categories like paramyxoviruses, Ebola virus etc. To date, the substitution/conversion pathway has been observed in human along with other mammals, Drosophila, and some plants. The RNA editing processes are known to create diversity in proteins involved in various pathways like lipid transport, metabolism etc. and may act as potential targets for therapeutic intervention (Smith et al., 1997). The reaction mechanisms of cytidine and adenosine deaminases is represented below. In both these reactions, NH3 is presumed to be released:
SARS (cytosolic seryl tRNA synthetase) catalyzes the reaction of serine, tRNA(Ser), and ATP to form Ser-tRNA(Ser), AMP, and pyrophosphate. The enzyme, a class II tRNA synthetase, is a homodimer (Hartlein and Cusack 1995; Vincent et al. 1997).
TARS (cytosolic threonyl tRNA synthetase) catalyzes the reaction of threonine, tRNA(Thr), and ATP to form Thr-tRNA(Thr), AMP, and pyrophosphate. The enzyme, a class II tRNA synthetase, is a homodimer (Pan et al. 1982).
HARS (cytosolic histidyl tRNA synthetase) catalyzes the reaction of histidine, tRNA(His), and ATP to form His-tRNA(His), AMP, and pyrophosphate (Lee et al. 2002).
FARS (cytosolic phenylalanyl tRNA synthetase) catalyzes the reaction of phenylalanine, tRNA(Phe), and ATP to form Phe-tRNA(Phe), AMP, and pyrophosphate. The enzyme, a class II tRNA synthetase, is a heterotetramer of two alpha and two beta subunits (Moor et al. 2002).
CARS (cytosolic cysteinyl tRNA synthetase) catalyzes the reaction of cysteine, tRNA(cys), and ATP to form Cys-tRNA(Cys), AMP, and pyrophosphate. The enzyme, a class I tRNA synthetase, is a homomultimer, probably a dimer (Davidson et al. 2001).
GARS (cytosolic glycyl tRNA synthetase) catalyzes the reaction of glycine, tRNA(Gly), and ATP to form Gly tRNA(Gly), AMP, and pyrophosphate. The enzyme, a class II tRNA synthetase, is a dimer. Cytosolic and mitochondrial glycyl tRNA synthetase enzymes are both encoded by the same gene; the cytosolic protein lacks an aminoterminal 54 residue sequence found in the mitochondrial protein. Mutations in GARS are associated with Charcot Marie Tooth disease and distal spinal muscular atrophy, two diseases characterized by axonal dysfunction (Antonellis et al. 2006)
AARS (cytosolic alanyl tRNA synthetase) catalyzes the reaction of alanine, tRNA(ala), and ATP to form Ala tRNA(Ala), AMP, and pyrophosphate. The enzyme, a class II tRNA synthetase, is a monomer (Shiba et al. 1995). A mutation in the editing domain of the mouse Aars gene results in misincorporation of non-cognate amino acids into cellular proteins. This is associated with protein misfolding in Purkinje cells and a phenotype consistent with human ataxia (Lee et al. 2006).
NARS (cytosolic asparaginyl tRNA synthetase) catalyzes the reaction of asparagine, tRNA(Asn), and ATP to form Asn-tRNA(Asn), AMP, and pyrophosphate. The enzyme is a class I tRNA synthetase (Beaulande et al. 1998).
WARS (cytosolic tryptophanyl tRNA synthetase) catalyzes the reaction of tryptophan, tRNA(Trp), and ATP to form Trp-tRNA(Trp), AMP, and pyrophosphate. The enzyme, a class I tRNA synthetase, is a homodimer (Bange et al. 1992; Rubin et al. 1991; Yu et al. 2004).
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Sustained recruitment of phospholipase C-gamma to Gab1 is required for HGF-induced branching tubulogenesis
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Characterization of type II phosphatidylinositol 4-kinase isoforms reveals association of the enzymes with endosomal vesicular compartments
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arginine + tRNA(Arg) + ATP => Arg-tRNA(Arg) + AMP + pyrophosphate
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alanine + tRNA(Ala) + ATP => Ala-tRNA(Ala) + AMP + pyrophosphate
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aspartate + tRNA(Asp) + ATP => Asp-tRNA(Asp) + AMP + pyrophosphate
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asparagine + tRNA(Asn) + ATP => Asn-tRNA(Asn) + AMP + pyrophosphate
pyrophosphate + H2O => 2 orthophosphate [cytosolic]
valine + tRNA(Val) + ATP => Val-tRNA(Val) + AMP + pyrophosphate
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New insights into the diversity and function of neuronal immunoglobulin superfamily molecules
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glutamate + tRNA(Glu) + ATP => Glu-tRNA(Glu) + AMP + pyrophosphate
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glutamine + tRNA(Glu) + ATP => Glu-tRNA(Glu) + AMP + pyrophosphate
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glycine + tRNA(Gly) + ATP => Gly-tRNA(Gly) + AMP + pyrophosphate
histidine + tRNA(His) + ATP => His-tRNA(His) + AMP + pyrophosphate
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cysteine + tRNA(Cys) + ATP => Cys-tRNA(Cys) + AMP + pyrophosphate
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Inositol 1,4,5-trisphosphate receptor type 1
Inositol 1,4,5-trisphosphate receptor type 3
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tyrosine + tRNA(Tyr) + ATP =>Tyr-tRNA(Tyr) + AMP + pyrophosphate
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threonine + tRNA(Thr) + ATP => Thr-tRNA(Thr) + AMP + pyrophosphate
tryptophan + tRNA(Trp) + ATP => Trp-tRNA(Trp) + AMP + pyrophosphate
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phenylalanine + tRNA(Phe) + ATP => Phe-tRNA(Phe) + AMP + pyrophosphate
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serine + tRNA(Ser) + ATP => Ser-tRNA(Ser) + AMP + pyrophosphate
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Binding of SLBP to Replication-Dependent Histone Pre-mRNA
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Fractionation and properties of glutamic oxalacetic transaminase
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Recruitment of CstF to the CPSF Bound Pre-mRNA
Binding of Cleavage factors and Poly(A)Polymerase to the CstF:CPSF:Pre-mRNA Complex
Cleavage and polyadenylation of Intronless Pre-mRNA
Binding of ADAR2 homodimer to dsRNA duplex
Deamination at C6 position of adenosine in Editosome (ADAR2)
Formation of the active Spliceosomal C complex
Formation of an intermediate Spliceosomal C complex
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Formation of the Cleavage and Polyadenylation Complex
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Lariat Formation and 5'-Splice Site Cleavage
ATAC spliceosome mediated 3' splice site cleavage, exon ligation
ATAC spliceosome mediated Lariat formation,5' splice site cleavage
Lysyl oxidase: from basic science to future cancer treatment
Structural basis for activation of G-protein-coupled receptors
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SARS2 (mitochondrial seryl tRNA synthetase) catalyzes the reaction of serine, mitochondrial tRNA(Ser), and ATP to form Ser-tRNA(Ser), AMP, and pyrophosphate. SARS2 is a class II tRNA synthetase inferred from the biochemical properties of its bovine homologue to function as a dimer (Yokogawa et al. 2000).
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TARS2 (mitochondrial threonyl tRNA synthetase) catalyzes the reaction of threonine, mitochondrial tRNA(Thr), and ATP to form Thr-tRNA(Thr), AMP, and pyrophosphate. The TARS2 gene has been identified by computational analysis of the human genome sequence; its function has been inferred from those of the biochemically characterized mitochondrial aspartyl and tyrosyl tRNA synthetases (Bonnefond et al. 2005).
FARS2 (mitochondrial phenylalanyl tRNA synthetase) catalyzes the reaction of phenylalanine, mitochondrial tRNA(Phe), and ATP to form Phe-tRNA(Phe), AMP, and pyrophosphate. The enzyme, a class II tRNA synthetase, is a monomer (Bullard et al. 1999).
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PARS2 (mitochondrial prolyl tRNA synthetase) catalyzes the reaction of proline, mitochondrial tRNA(Pro), and ATP to form Pro-tRNA(Pro), AMP, and pyrophosphate. The PARS2 gene has been identified by computational analysis of the human genome sequence; its function has been inferred from those of the biochemically characterized mitochondrial aspartyl and tyrosyl tRNA synthetases (Bonnefond et al. 2005).
KARS (mitochondrial lysyl tRNA synthetase) catalyzes the reaction of lysine, tRNA(Lys), and ATP to form Lys-tRNA(Lys), AMP, and pyrophosphate. The enzyme, a class II tRNA synthetase, is a homodimer. The same gene encodes both cytosolic and mitochondrial KARS enzymes (Shiba et al. 1997).
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MARS2 (mitochondrial methionyl tRNA synthetase) catalyzes the reaction of methionine, mitochondrial tRNA(Met), and ATP to form Met-tRNA(Met), AMP, and pyrophosphate. The enzyme, a class I tRNA synthetase, is a monomer (Spencer et al. 2004).
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IARS2 (mitochondrial isoleucyl tRNA synthetase) catalyzes the reaction of isoleucine, mitochondrial tRNA(Ile), and ATP to form Ile-tRNA(Ile), AMP, and pyrophosphate. The enzyme is a class I tRNA synthetase (Degoul et al. 1995).
LARS2 (mitochondrial leucyl tRNA synthetase) catalyzes the reaction of leucine, mitochondrial tRNA(Leu), and ATP to form Leu-tRNA(Leu), AMP, and pyrophosphate. The enzyme, a class I tRNA synthetase, is a monomer (Bullard et al. 2000).
GARS (mitochondrial glycyl tRNA synthetase) catalyzes the reaction of glycine, tRNA(Gly), and ATP to form Gly-tRNA(Gly), AMP, and pyrophosphate. The enzyme, a class II tRNA synthetase, is a dimer. Cytosolic and mitochondrial glycyl tRNA synthetase enzymes are both encoded by the same gene; the cytosolic protein lacks an aminoterminal 54-residue sequence found in the mitochondrial protein. Mutations in GARS are associated with Charcot-Marie-Tooth disease (Antonellis et al. 2007).
HARS2 (mitochondrial histidyl tRNA synthetase) catalyzes the reaction of histidine, mitochondrial tRNA(His), and ATP to form His-tRNA(His), AMP, and pyrophosphate. The enzyme is a class II tRNA synthetase (O'Hanlon et al. 1995).
WARS2 (mitochondrial tryptophanyl tRNA synthetase) catalyzes the reaction of tryptophan, mitochondrial tRNA(Trp), and ATP to form Trp-tRNA(Trp), AMP, and pyrophosphate. The enzyme is a class I tRNA synthetase (Jorgensen et al. 2000).
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The Lsm1-7 complex forms a heptameric ring that binds the 3' oligoadenylated ends of mRNAs that have been deadenylated. The bound Lsm1-7 may prevent access of the exosome (a 3' to 5' exonuclease) to the 3' end and thereby direct the mRNA to the 5' to 3' exonuclease pathway. The yeast Lsm1-7 complex has a preference for oligoadenylated RNA compared to polyadenylated RNA, however other determinants of binding by Lsm1-7 are unknown.
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Leber congenital amaurosis: genes, proteins and disease mechanisms
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tRNA synthetases catalyze the ligation of tRNAs to their cognate amino acids in an ATP-dependent manner. The reaction proceeds in two steps. First, amino acid and ATP form an aminoacyl adenylate molecule, releasing pyrophosphate. The aminoacyl adenylate remains associated with the synthetase enzyme where, in the second step it reacts with tRNA to form aminoacyl tRNA and AMP. The rapid hydrolysis of pyrophosphate makes these reactions essentially irreversible under physiological conditions (Fersht and Kaethner 1976a). Specificity of the tRNA charging reactions is achieved both by specific recognition of amino acid and tRNA substrates by the synthetase, and by an editing process in which incorrect aminoacyl adenylate molecules (e.g., valyl adenylate associated with isoleucyl tRNA synthetase) are hydrolyzed rather than conjugated to tRNAs in the second step of the reaction (Baldwin and Berg 1966a,b; Fersht and Kaethner 1976b). The tRNA synthetases can be divided into two structural classes based on conserved amino acid sequence features (Burnbaum and Schimmel 1991). A single synthetase mediates the charging of all of the tRNA species specific for any one amino acid but, with three exceptions, glycine, lysine, and glutamine, the synthetase that catalyzes aminoacylation of mitochondrial tRNAs is encoded by a different gene than the one that acts on mitochondrial tRNAs. Both mitochondrial and cytosolic tRNA synthetase enzymes are encoded by genes in the nuclear genome. A number of tRNA synthetases are known to have functions distinct from tRNA charging (reviewed by Park et al. 2005). Additionally, mutations in several of the tRNA synthetases, often affecting protein domains that are dispensable in vitro for aminoacyl tRNA synthesis, are associated with a diverse array of neurological and other diseases (Antonellis and Green 2008; Park et al. 2008). These findings raise interest into the role of these enzymes in human development and disease.
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The exosome complex hydrolyzes capped, deadenylated mRNA from 3' to 5' and yields ribonucleotides having 5'-monophosphates. In yeast the Ski2-Ski3-Ski8 complex assists degradation by the exosome complex, however little is known about the function of the homologous Ski complex in mammals. Although many exosomal components contain exonuclease signatures, only two components have been shown to degrade RNA. Rrp6/PMSCL-100 has been shown to be involved in the 3â-5â decay of nuclear mRNAs in yeast. Rrp6 may also function in the absence of the core exosomal components. The Rrp44/dDis3 component of the core exosome has been shown to possess both 3â-5â exonuclease activity along with endonuclease activity via its PIN domain.
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The scavenging nuclease DCPS hydrolyzes the triphosphate bond between the 7-methylguanosine cap and the remaining oligoribonucleotide body of the mRNA. The products are 7-methylguanosine 5'-monophosphate and an oligoribonucleotide with a 5'-diphosphate.
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The degradation of mRNA from 3' to 5' occurs in two steps. First, the exosome exoribonuclease complex binds the 3' end of the oligoadenylated mRNA and hydrolyzes it from 3' to 5', yielding ribonucleotides having 5'-monophosphates, until a capped oligoribonucleotide remains. Second, the scavenging decapping enzyme DCPS hydrolyzes the 7-methylguanosine cap.
YARS2 (mitochondrial tyrosyl tRNA synthetase) catalyzes the reaction of tyrosine, mitochondrial tRNA(Tyr), and ATP to form Tyr-tRNA(Tyr), AMP, and pyrophosphate. The enzyme, a class I tRNA synthetase, is a homodimer (Bonnefond et al. 2005).
VARS2 (mitochondrial valyl tRNA synthetase) catalyzes the reaction of valine, mitochondrial tRNA(val), and ATP to form Val-tRNA(Val), AMP, and pyrophosphate. The VARS2 gene has been identified by computational analysis of the human genome sequence; its function has been inferred from those of the biochemically characterized mitochondrial aspartyl and tyrosyl tRNA synthetases (Bonnefond et al. 2005).
Mitochondrial PPA2 (pyrophosphatase (inorganic) 2) catalyzes the hydrolysis of pyrophosphate to yield two molecules of orthophosphate. The enzyme requires Mg++ for activity (Curbo et al. 2006). The enzyme is inferred to be a homodimer by analogy to its cytosolic isoform.
Mitochondrial tRNA synthetases act in the mitochondrial matrix to catalyze the reactions of tRNAs encoded in the mitochondrial genome, their cognate amino acids, and ATP to form aminoacyl-tRNAs, AMP, and pyrophosphate (Schneider et al. 2000). The synthetase enzymes that catalyze these reactions are all encoded in the nuclear genome. In three cases, glycine, lysine, and glutamine, a single gene encodes two enzyme isoforms, one cytosolic and one mitochondrial. All other mitochondrial tRNA synthetases are encoded by genes different from the ones encoding the corresponding cytosolic enzymes.
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Basic Medical Biochemistry: A Clinical Approach, 2nd ed (Book): 527
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The biochemistry and physiology of nucleotides
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Receptor-dependent RhoA activation in G12/G13-deficient cells: genetic evidence for an involvement of Gq/G11
Role of syndecan-1 in leukocyte-endothelial interactions in the ocular vasculature
Invest. Ophthalmol. Vis. Sci. 43:1135-41
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The L13a subunit of the 60s ribosome is phosphorylated about 16 hours after INF gamma induction by an unknown kinase. At this time, L13a is also released from the 60s subunit (Mazumder et al.,2003). It is unclear, however, whether phosphorylation occurs before or after the release of L13a. Here, phosphorylation is shown as occurring after release.
Although the mechanism through which L13a prevents translation initiation has not been determined, Mazumder et al. (2003) have described four alternatives. L13a could (1) inhibit the function of eIF4F, (2) block the recruitment of the 43S preinitiation complex, (3) prevent scanning of the 43S complex to the initiation codon, or 4) interfere with joining of the 60S ribosomal subunit.
eIF2B is a guanine nucleotide releasing factor that is required to cause GDP release so that a new GTP molecule can bind and activate eIF2, so that it can be reused.
Inactive eIF2:GDP binds eIF2B to form an eIF2:GDP:eIF2B intermediate.
Translation initiation is a complex process in which the Met-tRNAi initiator, 40S, and 60S ribosomal subunits are assembled by eukaryotic initiation factors (eIFs) into an 80S ribosome at the start codon of an mRNA. The basic mechanism for this process can be described as a series of five steps: 1) formation of a pool of free 40S subunits, 2) formation of the ternary complex (Met-tRNAi/eIF2/GTP), and subsequently, the 43S complex (comprising the 40S subunit, Met-tRNAi/eIF2/GTP, eIF3 and eIF1A), 3) activation of the mRNA upon binding of the cap-binding complex eIF4F, and factors eIF4A, eIF4B and eIF4H, with subsequent binding to the 43S complex, 4) ribosomal scanning and start codon recognition, and 5) GTP hydrolysis and joining of the 60S ribosomal subunit.
The active eIF2:GTP complex may be formed by direct binding of GTP to free eIF2 or by GDP-GTP exchange on the eIF2:GDP:eIF2B complex. The eIF2:GDP complex binds eIF2B forming an eIF2:GDP:eIF2B intermediate complex. eIF2B is a guanine nucleotide releasing factor required to cause GDP release so that a new GTP molecule can bind and activate eIF2. Phosphorylated eIF2:GDP sequesters all eIF2B as an inactive complex, and thus, reuse of eIF2 is inhibited as a consequence of the tight bond it forms with eIF2B, which prevents nucleotide exchange. Therefore, in the absence of free eIF2B, excess eIF2 remains in its inactive GDP-bound form and protein synthesis slows dramatically.
Once the 60S subunit joins the translation initiation complex, eIF5B hydrolyzes its GTP and is released from the now 80S monosome. The fully assembled 80s ribosome is now ready to start elongation of the polypeptide chain.
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The 80S ribosome bound to the mRNA moves along the mRNA molecule from its initial site to the initiation codon and forms a 48S complex, in which the initiation codon is base paired to the anticodon of the Met-tRNAi. Proper recognition of the AUG initiation codon depends on base pairing with the anticodon of the Met-tRNAi and requires eIF1, eIF1A, eIF2 and eIF5.
Hydrolysis of eIF2-GTP occurs after the Met-tRNAi has recognized the AUG. This reaction is catalyzed by eIF5 (or eIF5B) and is thought to cause dissociation of all other initiation factors and allow joining of the large 60S ribosomal subunit. The 60S subunit joins - a reaction catalyzed by eIF5 or eIF5B - resulting in a translation-competent 80S ribosome. Following 60S subunit joining, eIF5B hydrolyzes its GTP and is released from the 80S ribosome, which is now ready to start elongating the polypeptide chain.
Joining of the 60S subunit to form the 80S ribosome is catalyzed by the presence of GTP-bound eIF5B.
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Sn1-specific diacylglycerol lipase alpha
The binding of eEF1A:GTP to aminoacyl tRNA (aa-tRNA) results in the formation of a ternary complex (eEF1A:GTP:aa-tRNA). Human eEF1A and rabbit eEF1A are 100% identical, and prokaryotic homologue of eEF1A (EF-Tu) shows 59% identity in the GTP-binding domain.This process is illustrated below with: a GTP molecule in white and eEF1A protein in yellow.
The cycle of elongation starts with an empty ribosomal A-site and the peptidyl-tRNA in the P-site. eEF1A is activated by GTP binding and allows for the subsequent binding of aminoacyl-tRNA (aa-tRNA).This process is illustrated below with a GTP molecule in white and eEF1A protein in yellow.
The process for translation of a protein destined for the endoplasmic reticulum (ER) branches from the canonical cytoslic translation process at the point when a nascent polypeptide containing a hydrophobic signal sequence is exposed on the surface of the cytosolic ribosome:mRNA:peptide complex. The signal sequence mediates the interaction of this complex with a cytosolic signal recognition particle (SRP) to form a complex which in turn docks with an SRP receptor complex on the ER membrane. There the ribosome complex is transferred from the SRP complex to a translocon complex embedded in the ER membrane and reoriented so that the nascent polypeptide protrudes through a pore in the translocon into the ER lumen. Translation, which had been halted by SRP binding, now resumes, the signal peptide is cleaved from the polypeptide, and elongation proceeds, with the growing polypeptide oriented into the ER lumen.
As the signal peptide of the nascent protein enters the lumen of the endoplasmic reticulum (ER), the signal peptide is recognized and cleaved by the ER membrane-associated Signal Peptidase. Translation of the protein then proceeds to completion.
The Signal Recognition Particle (SRP) receptor mediates transfer of the ribosome:mRNA:nascent protein complex to the Translocon Complex. A coupled reaction (not annotated here) in which GTP molecules are hydrolyzed by the alpha subunit of the SRP Receptor and the SRP54 subunit of the SRP is thought to ensure release of the SRP only after the ribosome is properly reoriented. At the end of this process, the ribosome is attached to the endoplasmic reticulum (ER) membrane with its associated nascent polypeptide protruding through the Translocon Complex into the ER lumen.
The SRP receptor in the the endoplasmic reticulum (ER) membrane binds via its alpha subunit to the the SRP54 subunit of the Signal Recognition Particle (SRP), which itself is bound to a ribosome:mRNA:polypeptide complex. This interaction tethers the ribosome to the ER membrane, oriented so that the nacent polypeptide will traverse the ER membrane and enter the ER lumen. This process has been characterized in detail in cultured canine cells; this human event is inferred by homology from its canine counterpart.
CLAC binds to amyloid beta peptides through the positively charged amino acid cluster within the collagenous domain 1 and inhibits formation of amyloid fibrils
The Ribosome Nascent Complex containing the ribosome and protruding signal peptide of preprolactin is bound by the Signal Recognition Particle Complex. Translation is paused during this step.
The synthesis of a protein destined for the endoplasmic reticulum starts with the canonical events of cytosolic translation initiation and proceeds to the point where a nascent polypeptide chain containing a signal sequence protrudes from the mRNA:ribosome complex. Merrick (2010) provides an overview of these events.
The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-alpha/beta-induced ubiquitin-like protein
Initiation of translation in the majority of eukaryotic cellular mRNAs depends on the 5'-cap (m7GpppN) and involves ribosomal scanning of the 5' untranslated region (5'-UTR) for an initiating AUG start codon. Therefore, this mechanism is often called cap-dependent translation initiation. Proximity to the cap, as well as the nucleotides surrounding an AUG codon, influence the efficiency of the start site recognition during the scanning process. However, if the recognition site is poor enough, scanning ribosomal subunits will ignore and skip potential starting AUGs, a phenomenon called leaky scanning. Leaky scanning allows a single mRNA to encode several proteins that differ in their amino-termini. Merrick (2010) provides an overview of this process and hghlights several features of it that remain incompletely understood. Several eukaryotic cell and viral mRNAs initiate translation by an alternative mechanism that involves internal initiation rather than ribosomal scanning. These mRNAs contain complex nucleotide sequences, called internal ribosomal entry sites, where ribosomes bind in a cap-independent manner and start translation at the closest downstream AUG codon. Initiation on several viral and cellular mRNAs is cap-independent and is mediated by binding of the ribosome to internal ribosome entry site (IRES) elements. These elements are often found in characteristically long structured regions on the 5'-UTR of an mRNA that may or may not have regulatory upstream open reading frames (uORFs). Both of these features on the 5'-end of the mRNA hinder ribosomal scanning, and thus promote a cap-independent translation initiation mechanism. IRESs act as specific translational enhancers that allow translation initiation to occur in response to specific stimuli and under the control of different trans-acting factors, as for example when cap-dependent protein synthesis is shut off during viral infection. Such regulatory elements have been identified in the mRNAs of growth factors, protooncogenes, angiogenesis factors, and apoptosis regulators, which are translated under a variety of stress conditions, including hypoxia, serum deprivation, irradiation and apoptosis. Thus, cap-independent translational control might have evolved to regulate cellular responses in acute but transient stress conditions that would otherwise lead to cell death, while the same mechanism is of major importance for viral mRNAs to bypass the shutting-off of host protein synthesis after infection. Encephalomyocarditis virus (EMCV) and hepatitis C virus exemplify two distinct mechanisms of IRES-mediated initiation. In contrast to cap-dependent initiation, the eIF4A and eIF4G subunits of eIF4F bind immediately upstream of the EMCV initiation codon and promote binding of a 43S complex. Accordingly, EMCV initiation does not involve scanning and does not require eIF1, eIF1A, and the eIF4E subunit of eIF4F. Nonetheless, initiation on some EMCV-like IRESs requires additional non-canonical initiation factors, which alter IRES conformation and promote binding of eIF4A/eIF4G. Initiation on the hepatitis C virus IRES is simpler: a 43S complex containing only eIF2 and eIF3 binds directly to the initiation codon as a result of specific interaction of the IRES and the 40S subunit.
While circularization of mRNA during translation initiation is thought to contribute to an increase in the efficiency of translation, it also appears to provide a mechanism for translational silencing. This might be achieved by bringing inhibitory 3' UTR-binding proteins into a position in which they interfere either with the function of the translation initiation complex or with the assembly of the ribosome (Mazumder et al 2001). Translational silencing of Ceruloplasmin (Cp) occurs 16 hrs after its induction by INF-gamma (Mazumder et al., 1997). Although the mechanism by which silencing occurs has not yet been determined, this process is mediated by the L13a subunit of the 60s ribosome and thought to require circularization of the Cp mRNA (Sampath et al., 2003; Mazumder et al., 2001; Mazumder et al., 2003). Between 14 and 16 hrs after INF gamma induction, the L13a subunit of the 60s ribosome is phosphorylated and released from the 60s subunit. Phosphorylated L13a then associates with the GAIT element in the 3' UTR of the Cp mRNA inhibiting its translation.
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HuR (ELAVL1) is a ubiquitous protein that binds AU-rich elements in mRNAs and acts to stabilize the mRNAs. HuR activity is controlled by phosphorylation, with PKC alpha and PCK delta enhancing the ability of HuR to bind and stabilize mRNAs. Binding of mRNAs occurs in the nucleus and HuR then interacts with the CRM1 export pathway to transfer the mRNA to the cytoplasm. The mechanism by which HuR shields the mRNA from degradation is unknown. HuR also regulates translation of some mRNAs, in some cases repressing translation and in some cases enhancing translation of bound mRNAs by recruiting them to polysomes. HuR binds and regulates mRNAs encoding Cyclooxygenase-2 (COX2, PTGS2), Cyclin A (CCNA, CCNA2), Cyclin D1 (CCND1), Cyclin B1 (CCNB1), CD83 antigen (CD83), and proto-oncogene c-Fos (FOS). HuR is a member of a family of proteins that also contains HuD (ELAVL4), HuB (ELAVL2), and HuC (ELAVL3). HuB, HuC, and HuD are specifically expressed in neural tissue. HuR participates in apoptosis. During lethal stress HuR becomes mostly cytoplasmic and is a target of Caspase-3 and Caspase-7. The cleavage products of HuR in turn promote apoptosis.
RNA elements rich in adenine and uracil residues (AU-rich elements) bind specific proteins which either target the RNA for degradation or, more rarely, stabilize the RNA. The activity of the AU-element binding proteins is regulated, usually by phosphorylation but also by subcellular localization.
80S monosomes dissociate into 40S and 60S ribosomal subunits. eIF1A promotes this dissociation.
eIF3 and eIF1A bind to the 40S ribosomal subunit.
Protein kinase C alpha (PKCalpha) phosphorylates HuR (ELAVL1) on serine221 and serine 158.
KSRP binds to AU-rich sequences in the 3' untranslated regions of mRNAs. KSRP causes the bound mRNA to be targeted for hydrolysis by recruiting exonucleases and decapping enzymes. The activity of KSRP is regulated by phosphorylation. Protein kinase B/Akt phosphorylates KSRP at serine193. The phosphorylation inhibits the ability of KSRP to destabilize mRNA. KSRP phosphorylated at serine193 binds 14-3-3zeta (YWHAZ) which causes KSRP to be retained in the nucleus.
HuR (ELAV1) phosphorylated on serine221 and serine158 binds COX-2 mRNA in the nucleus. The phosphorylation of serine 158 appears to affect RNA-binding while phosphorylation on serine 221 affects nucleocytoplasmic shuffling.
Protein kinase C delta (PKCdelta) phosphorylates HuR (ELAVL1) at serine 221 and serine 318.
HuR binds AU-rich elements of mRNAs. Bound HuR can form oligomers on longer AU-rich elements. Phosphorylated HuR binds mRNA more tightly than unphosphorylated HuR does.
HuR phosphorylated on ser221 and ser318 binds AU-rich regions of mRNAs. Phosphorylation on ser318 appears to affect RNA binding and phosphorylation of ser221 affects nucleocytoplasmic shuttling.
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Dynamic binding of PKA regulatory subunit RI alpha
The AUG initiation codon in the mRNA is recognized by base pairing with the anticodon of the Met-tRNAi. This reaction requires eIF1, eIF1A, eIF2 and eIF5.
The cap-binding complex is constituted by the initiation factors eIF4A, eIF4G and eIF4E. First, eIF4E must be released from the inactive eIF4E:4E-BP complex. Then eIF4A interacts with eIF4G, and eIF4E binds to the amino-terminal domain of eIF4G, resulting in the formation of the cap-binding complex eIF4F. eIF4A together with eIF4B or eIF4H is thought to unwind RNA secondary structures near the 5'-end of the mRNA. The translation initiation complex is formed when the 43S complex binds the cap-bound mRNA.
The mRNA-bound ribosomal complex moves along the 5'-untranslated region (5'-UTR) of the mRNA from its initial site to the initiation codon to form a 48S complex, in which the initiation codon (AUG) is base paired to the anticodon of the Met-tRNAi. It is not known whether eIF4A (or another ATPase, such as DED1) facilitates scanning by melting mRNA secondary structures or by actively propelling the ribosome.
The ternary complex forms upon binding of the initiator methionyl-tRNA to the active eIF2:GTP complex.
Activation of eIF2 through direct binding of GTP.
The 80S ribosome dissociates into free 40S (small) and 60S (large) ribosomal subunits. Each ribosomal subunit is constituted by several individual ribosomal proteins and rRNA.
The factor eIF4E within the eIF4F (cap-binding) complex directly binds the 5'-cap on eukaryotic mRNAs. Note that the mRNA is in complex with cytoplasmic proteins constituting an mRNP complex.
eIF4A interacts with eIF4G, and eIF4E interacts with the amino-terminal domain of eIF4G to form the cap-binding complex eIF4F.
Binding of the methionyl-tRNA initiator to the active eIF2:GTP complex results in the formation of the ternary complex. Subsequently, this Met-tRNAi:eIF2:GTP (ternary) complex binds to the complex formed by the 40S subunit, eIF3 and eIF1A, to form the 43S complex.
The ternary complex (Met-tRNAi:eIF2:GTP) binds to the complex formed by the 40S subunit, eIF3 and eIF1A, to form the 43S complex. eIF1A promotes binding of the ternary complex to the 40S subunit within 43S. The initiator methionyl-tRNA from the ternary complex is positioned at the ribosomal P site.
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Phosphorylated BRF1 interacts with 14-3-3, becomes localized to the cytoskeleton, and no longer promotes RNA degradation. Phosphorylated BRF1 is, however, still able to bind RNA.
Butyrate response factor 1 (BRF1) binds AU-rich elements in the 3' untranslated region of mRNAs.
AUF1 (hnRNP D0) dimers bind U-rich regions of AU-rich elements (AREs) in the 3' untranslated regions of mRNAs. The binding causes AUF1 dimers to assemble into higher order tetrameric complexes. Diphosphorylated AUF1 bound to RNA recruits additional proteins, including eIF4G, polyA-binding protein, Hsp, Hsc70, Hsp27, NSEP-1, NSAP-1, and IMP-2 which target the mRNA and AUF1 for degradation. Unphosphorylated AUF1 is thought to be less able to recruit additional proteins. AUF1 also interacts directly or indirectly with HuR and the RNA-induced silencing complex (RISC). AUF1 complexed with RNA and other proteins is ubiquitinated and targeted for destruction by the proteasome while the bound mRNA is degraded. Inhibition of ubiquitin addition to AUF1 blocks mRNA degradation. The mechanism by which ubiquitin-dependent proteolysis is coupled to mRNA degradation is unknown. At least 4 isoforms of AUF1 exist: p45 (45 kDa) contains all exons, p42 lacks exon 2, p40 lacks exon 7, and p37 lacks exons 2 and 7. The presence of exon 7 in p42 and p45 seems to block ubiquitination while the absence of exon 7 (p37 and p40) targets AUF1 for ubiquitination and destabilizes bound RNAs. Lack of exon 2 (p37 and p42) is associated with higher affinity for RNA and 14-3-3sigma (SFN). AUF1 binds and destabilizes mRNAs encoding Interleukin-1 beta (IL1B), Tumor Necrosis Factor alpha (TNFA), Cyclin-dependent kinase inhibitor 1 (CDNK1A, p21), Cyclin-D1 (CCND1), Granulocyte-macrophage colony stimulating factor (GM-CSF, CSF2), inducible Nitric oxide synthase (iNOS, NOS2), Proto-oncogene cFos (FOS), Myc proto-oncogene (MYC), Apoptosis regulator Bcl-2 (BCL2).
MAPK-activated protein kinase 2 (MK2) phosphorylates BRF1 at serine 54, serine 92, serine 203, and an unknown site in the C terminus. Phosphorylation inhibits the ability of BRF1 to cause degradation of RNA. It is unknown if tetraphosphorylated BRF1 binds 14-3-3 in the same way as diphosphorylated BRF1 does.
BRF1 is phosphorylated at Serine92 and Serine203 by Protein kinase B/AKT. Protein kinase B is activated by phosphatidylinositol 3-kinase. Phosphorylation of BRF1 does not interfere with the ability of BRF1 to bind RNA or interact with enzymes that catalyze RNA degradation therefore larger complexes may contain phosphorylated BRF1.
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AUF1 monomers form dimers which bind the U-rich sequences in AU-rich elements of mRNAs. Binding of the mRNA causes the dimers of AUF1 to form tetramers. Nonphosphorylated AUF1 isoform p40 causes the mRNA to form a rigid structure whereas p40 that is phosphorylated at serines 83 and 87 does not. This difference may cause nonphosphorylated p40 to fail to destabilize the bound mRNA.
Tetrameric AUF1 bound to RNA forms a complex with other proteins, including elongation factor eIF4G, polyA-binding protein PABP, Hsp, Hsc70, and Hsp27. AUF1 also directly interacts with polyadenylate.
AUF1 is ubiquitinated at unknown sites. The number of ubiquitin molecules conjugated to AUF1 and their linkage is unknown. Ubiquitination is required for subsequent degradation of both AUF1 and the mRNA bound by AUF1. It is uncertain if AUF1 is in a larger complex when it is ubiquitinated.
Ubiquitin-dependent proteolysis of AUF1 and nuclease-dependent destruction of AUF1-bound mRNA are coupled in an unknown way. It is possible that ubiquitinated AUF1 targets other members of the AUF1 and signal transduction regulated complex (ASTRC), such as polyA-binding protein, for degradation and this renders the mRNA susceptible to nucleases.
Activated MAPK p38 alpha and beta phosphorylate KSRP at threonine692. The phosphorylation interferes with the ability of KSRP to bind and destabilize RNA. Thus RNAs become stabilized.
KSRP phosphorylated at serine193 binds 14-3-3zeta (YWHAZ) which impairs the ability of KSRP to destabilize RNA. Thus the RNAs become stabilized. KSRP is able to shuttle between the nucleus and the cytoplasm. 14-3-3zeta is nucleoplasmic. Binding of KSRP to 14-3-3zeta causes KSRP to be retained in the nucleus.
KSRP is phosphorylated by activated protein kinase B/AKT at serine 193. Phosphorylation does not prevent KSRP from binding RNA.
KSRP (KHSRP) forms a complex with the PARN deadenylase, exosome components (3' to 5' mRNA decay), and the decapping enzyme DCP2. Tethering KSRP to a mRNA is sufficient to target the mRNA for degradation.
KSRP (KHSRP) binds AU-rich regions of target RNAs via its four K-homology (KH) domains.
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Binding and Uptake of Ligands by Scavenger Receptors
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Phosphorylated tristetraproline (TTP) binds 14-3-3, which inhibits the ability of TTP to destabilize RNA. Thus RNAs bound by TTP become stabilized. The binding of 14-3-3 causes TTP to be excluded from stress granules.
Tristetraproline (TTP) binds RNAs that contain AU-rich elements and recruits enzymes that degrade RNA. TTP interacts with the exosome (3' to 5' exonuclease), XRN1 (5' to 3' exonuclease), and the decapping enzymes DCP1 and DCP2a. The activity of TTP is regulated by phosphorylation. MK2 phosphorylates TTP, which then binds 14-3-3.The interaction with 14-3-3 prevents phosphorylated TTP from entering stress granules and stabilizes mRNA bound by phosphorylated TTP. Tristetraproline is known to bind AU-rich elements in the following mRNAs: Tumor necrosis factor alpha (TNFA), Granulocyte-macrophage colony stimulating factor (CSF2, GM-CSF), Interleukin-2 (IL-2), and Proto-oncogene C-FOS (FOS, c-fos). Mice deficient in TTP exhibit arthritis, weight loss, skin lesions, autoimmunity, and myeloid hyperplasia.
Tristetraprolin (TTP) binds UUAUUUAUU motifs in the AU-rich elements of mRNAs. TTP binds Transportin-1 (Importin beta-2) which plays a role in shuttling TTP between P-bodies and stress granules.
TTP is phosphorylated by MK2 at serines 60 and 186.
Butyrate Response Factor 1 (BRF1, ZFP36L1, not to be confused with transcription factor IIIB) binds AU-rich elements in the 3' region of mRNAs. After binding, BRF1 recruits exonucleases (XRN1 and the exosome) and decapping enzymes (DCP1a and DCP2) to hydrolyze the RNA. The ability of BRF1 to direct RNA degradation is controlled by phosphorylation of BRF1. Protein kinase B/AKT1 phosphorylates BRF1 at serines 92 and 203. Phosphorylated BRF1 can still bind RNA but is sequestered by binding 14-3-3 protein, preventing BRF1 from destabilizing RNA. BRF1 is also phosphorylated by MK2 at serines 54, 92, 203, and at an unknown site in the C-terminus. It is unknown if this particular phosphorylated form of BRF1 binds 14-3-3.
The presence of an exon junction complex (EJC) downstream of a termination codon enhances nonsense-mediated decay (NMD) but is not absolutely required for NMD. The EJC is deposited during splicing and remains bound to the mRNA until a ribosome dislodges it during the pioneer round of translation, distinguished by the presence of the cap-binding complex at the 5' end. If translation terminates at least 50-55 nucleotides 5' to an EJC during the pioneer round then termination factors (eRF1 and eRF3) and the EJC recruit UPF1 and other NMD machinery (Lykke-Andersen et al. 2001, Ishigaki et al. 2001, Le Hir et al. 2001, Gehring et al. 2003, Hosoda et al. 2005, Kashima et al. 2006, Singh et al. 2007, Chamieh et al. 2008, Ivanov et al. 2008, Buchwald et al. 2010). A current model for NMD enhanced by the EJC posits recruitment of UPF1, SMG1, SMG8, and SMG9 to eRF3 at the ribosome to form the SURF complex (Kashima et al. 2006, Chang et al. 2007, Isken et al. 2008, Muhlemann et al. 2008, Stalder and Muhlemann 2008, Chamieh et al. 2009, Maquat and Gong 2009, Rebbapragada and Lykke-Andersen 2009, Hwang et al. 2010, Nicholson et al. 2010). UPF1 and SMG1 then interact with components of the EJC, activating phosphorylation of UPF1 by SMG1. The model of the NMD mechanism is inferred from known protein interactions: eRF1 and eRF3 interact with UPF1, the key regulator of NMD which also binds SMG1, UPF2, and UPF3 (UPF3a or UPF3b) to form the SURF complex (Kashima et al.2006, Ivanov et al. 2008, Clerici et al. 2009, Chakrabarti et al. 2011). UPF1 also interacts with CBP80 at the cap of the mRNA (Hwang et al. 2010). SMG8 and SMG9 associate with SMG1 and the SURF complex and modulate the phosphorylation activity of SMG1 (Yamashita et al. 2009). UPF2 and UPF3 are peripheral components of the EJC and thus may link the EJC to the SURF complex (Chamieh et al. 2008). UPF3b binds UPF1 and a composite surface formed by the Y14, MAGOH, and eIF4A3 subunits of the core EJC (Gehring et al. 2003, Kunz et al. 2006, Buchwald et al. 2010). SMG1 also interacts with the EJC (Kashima et al. 2006, Yamashita et al. 2009). UPF3a more weakly activates NMD than does UPF3b (Kunz et al. 2006) and UPF3a levels increase in response to loss of UPF3b (Chan et al. 2009). The binding of UPF1 to translated RNAs may occur in two steps: Binding of the SURF complex to the terminating ribosome followed by transfer of UPF1 and SMG1 to the EJC (Kashima et al. 2006, Hwang et al. 2010). The core EJC (Y14, MAGOH, eIF4A3, and BTZ) can activate NMD without UPF2, however RNPS1, another EJC subunit, requires UPF2 to activate NMD (Gehring et al. 2005). RNAs show differential dependence on RNPS1-activated NMD (Gehring et al. 2005). Also, NMD of some transcripts requires EJC component eIF4A3 but not UPF3b (Chan et al. 2007) therefore there may be more than one route to activating NMD via the EJC.
After undergoing rounds of translation, mRNA is normally destroyed by the deadenylation-dependent pathway. Though the trigger is unclear, deadenylation likely proceeds in two steps: one catalyzed by the PAN2-PAN3 complex that shortens the poly(A) tail from about 200 adenosine residues to about 80 residues and one catalyzed by the CCR4-NOT complex or by the PARN enzyme that shortens the tail to about 10-15 residues. After deadenylation the mRNA is then hydrolyzed by either the 5' to 3' pathway or the 3' to 5' pathway. It is unknown what determinants target a mRNA to one pathway or the other. The 5' to 3' pathway is initiated by binding of the Lsm1-7 complex to the 3' oligoadenylate tail followed by decapping by the DCP1-DCP2 complex. The 5' to 3' exoribonuclease XRN1 then hydrolyzes the remaining RNA. The 3' to 5' pathway is initiated by the exosome complex at the 3' end of the mRNA. The exosome processively hydrolyzes the mRNA from 3' to 5', leaving only a capped oligoribonucleotide. The cap is then removed by the scavenging decapping enzyme DCPS.
SMG6 is an endoribonuclease which cleaves the mRNA bound by UPF1 near the premature termination codon (Glavan et al. 2006, Eberle et al. 2009).
SMG1 phosphorylates UPF1 in vitro and in vivo (Denning et al. 2001, Yamashita et al. 2001, Kashima et al. 2006). Serines 1073, 1078, 1096, and 1116 in isoform 2 (Serines 1084, 1089, 1107, 1127 in isoform 1) are phosphorylated in vitro and phosphorylation at serines 1078 and 1096 has been confirmed in vivo (Yamashita et al. 2001, Ohnishi et al. 2003, Kashima et al. 2006). UPF1 also contains additional serine and threonine residues that could be phosphorylated. SMG8 and SMG9 associate with SMG1 and regulate the kinase activity of SMG1 (Yamashita et al. 2009). The phosphorylation reaction is rate-limiting in nonsense-mediated decay and is therefore regarded as a licensing step (reviewed in Rebbapragada and Lykke-Andersen 2009). Phosphorylation is enhanced by the exon junction complex, which can interact with UPF1 via UPF2 and/or UPF3 (Kashima et al. 2006, Ivanov et al. 2008) or via Y14:Magoh (Ivanov et al. 2008). SMG8 and SMG9 bind SMG1 and regulate its kinase activity (Yamashita et al. 2009, Fernandez et al. 2011).
Nonsense-mediated decay of an mRNA can be triggered even if the termination codon does not precede an exon junction (Buhler et al. 2006, Eberle et al. 2008, Silva et al. 2008, Singh et al. 2008, Ivanov et al. 2008). UPF1 and PABP seem to modulate the efficiency of translation termination and PABP in the proximity of a termination codon prevents NMD likely by outcompeting UPF1 for interaction with eRF3 (Singh et al. 2008, Ivanov et al. 2008, Silva et al. 2008). Factors in the competition may be the length and secondary structure of the 3' UTR (Buhler et al. 2006, Eberle et al. 2008). UPF1 preferentially binds some but not all longer UTRs (Hogg and Goff 2010). Interaction of eRF3 with PABP stimulates ribosome dissociation and initiation of a new round of translation on the mRNA. Interaction of eRF3 with UPF1 appears to promote nonsense-mediated decay. It is possible but not yet demonstrated that all components of the SURF complex (SMG1, UPF1, eRF1, eRF3) are assembled on an mRNA without an exon junction complex and that UPF1 is phosphorylated by SMG1.
During normal translation termination eRF3 associates with the ribosome and then interacts with PABP bound to the polyadenylate tail of the mRNA to release the ribosome and allow a new round of translation to commence. Nonsense-mediated decay (NMD) is triggered if eRF3 at the ribosome interacts with UPF1, which may compete with PABP (reviewed in Isken and Maquat 2007, Chang et al. 2007, Behm-Ansmant et al. 2007, Rebbapragada and Lykke-Andersen 2009, Bhuvanagiri et al. 2010, Nicholson et al. 2010, Durand and Lykke-Andersen 2011). An exon junction located 50-55 nt downstream of a termination codon is observed to enhance NMD. Exon-junction complexes (EJCs) are deposited on the mRNA during splicing in the nucleus, remain on mRNAs after transport to the cytosol, and are dislodged by the ribosome as it progresses along the mRNA during the pioneer round of translation (Gehring et al. 2009). EJCs contain the core factors eIF4A-III, Magoh-Y14, and CASC3 as well as the peripheral factors RNPS1, UPF2, and UPF3. UPF2 and UPF3 recruit UPF1 to eRF3 at the terminating ribosome. Thus an EJC downstream of a termination codon will not have been dislodged during translation and will recruit UPF1, triggering NMD. UPF1 is believed to form a complex containing SMG1, SMG8, and SMG9. In the key regulatory step of NMD SMG1 phosphorylates UPF1. The phosphorylated UPF1 then recruits either SMG6 or SMG5 and SMG7. SMG6 is itself an endoribonuclease that cleaves the mRNA. SMG5 and SMG7 do not have endoribonuclease activty, but are thought to recruit ribonucleases. Nonsense-mediated decay has been observed to involve deadenlyation, decapping, and both 5' to 3' and 3' to 5' exonuclease activities, but the exact degradative pathways taken by a given mRNA are not yet known. UPF1 also plays roles in Staufen-mediated decay, histone mRNA decay, telomere maintenance, genome integrity, and may play a role in normal termination of translation.
The Nonsense-Mediated Decay (NMD) pathway activates the destruction of mRNAs containing premature termination codons (PTCs) (reviewed in Isken and Maquat 2007, Chang et al. 2007, Behm-Ansmant et al. 2007, Neu-Yilik and Kulozik 2008, Rebbapragada and Lykke-Andersen 2009, Bhuvanagiri et al. 2010, Nicholson et al. 2010, Durand and Lykke-Andersen 2011). In mammalian cells a termination codon can be recognized as premature if it precedes an exon-exon junction by at least 50-55 nucleotides or if it is followed by an abnormal 3' untranslated region (UTR). While length of the UTR may play a part, the qualifications for being "abnormal" have not been fully elucidated. Also, some termination codons preceding exon junctions are not degraded by NMD so the criteria for triggering NMD are not yet fully known (reviewed in Rebbapragada and Lykke-Andersen 2009). While about 30% of disease-associated mutations in humans activate NMD, about 10% of normal human transcripts are also degraded by NMD (reviewed in Stalder and Muhlemann 2008, Neu-Yilik and Kulozik 2008, Bhuvanagiri et al. 2010, Nicholson et al. 2010). Thus NMD is a normal physiological process controlling mRNA stability in unmutated cells. Exon junction complexes (EJCs) are deposited on an mRNA during splicing in the nucleus and are displaced by ribosomes during the first round of translation. When a ribosome terminates translation the A site encounters the termination codon and the eRF1 factor enters the empty A site and recruits eRF3. Normally, eRF1 cleaves the translated polypeptide from the tRNA in the P site and eRF3 interacts with Polyadenylate-binding protein (PABP) bound to the polyadenylated tail of the mRNA. During activation of NMD eRF3 interacts with UPF1 which is contained in a complex with SMG1, SMG8, and SMG9. NMD can arbitrarily be divided into EJC-enhanced and EJC-independent pathways. In EJC-enhanced NMD, an exon junction is located downstream of the PTC and the EJC remains on the mRNA after termination of the pioneer round of translation. The core EJC is associated with UPF2 and UPF3, which interact with UPF1 and stimulate NMD. Once bound near the PTC, UPF1 is phosphorylated by SMG1. The phosphorylation is the rate-limiting step in NMD and causes UPF1 to recruit either SMG6, which is an endoribonuclease, or SMG5 and SMG7, which recruit ribonucleases. SMG6 and SMG5:SMG7 recruit phosphatase PP2A to dephosphorylate UPF1 and allow further rounds of degradation. How EJC-independent NMD is activated remains enigmatic but may involve competition between PABP and UPF1 for eRF3.
Nonsense-mediated decay has been observed with mRNAs that do not have an exon junction complex (EJC) downstream of the termination codon (reviewed in Isken and Maquat 2007, Chang et al. 2007, Behm-Ansmant et al. 2007, Rebbapragada and Lykke-Andersen 2009, Nicholson et al. 2010). In these cases the trigger is unknown but a correlation with the length of the 3' UTR has sometimes been seen. The current model posits a competition between PABP and UPF1 for access to eRF3 at the terminating ribosome (Ivanov et al. 2008, Singh et al. 2008, reviewed in Bhuvanagiri et al. 2010). Abnormally long 3' UTRs may prevent PABP from efficiently interacting with eRF3 and allow UPF1 to bind eRF3 instead. Long UTRs with hairpin loops may bring PABP closer to eRF3 and help evade NMD (Eberle et al. 2008). The pathway of degradation taken during EJC-independent NMD has not been elucidated. It is thought that phosphorylation of UPF1 by SMG1 and recruitment of SMG6 or SMG5 and SMG7 are involved, as with EJC-enhanced NMD, but this has not yet been shown.
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The XRN1 exoribonuclease hydrolyzes decapped mRNA from 5' to 3' and yields ribonucleotides having 5'-monophosphates. In yeast Xrn1 associates with the Lsm1-7 complex.
Degradation of mRNA from 5' to 3' occurs in three steps. First, the mRNA is bound at its 3' end by the Lsm1-7 complex. The bound Lsm1-7 may prevent nucleases from accessing the 3' end. Second, the 7-methylguanosine cap of the mRNA is hydrolyzed by the DCP1-DCP2 complex. Third, the 5' end of the decapped mRNA is attacked by the XRN1 exoribonuclease which digests the remainder of the mRNA from 5' to 3'. These processes may be physically connected by PATL1, the homolog of yeast Pat1, which stably binds the Lsm1-7 complex and interacts with the DCP1-DCP2 decapping complex and the Ccr4-NOT deadenylation complex (Ozgur et al. 2010).
Small interfering RNAs (siRNAs) are 21-25 nucleotide single-stranded RNAs produced by cleavage of longer double-stranded RNAs by the enzyme Dicer. Typically the long double-stranded substrates originate from viruses or repetitive elements in the genome and the two strands of the substrate are exactly complementary. After cleavage by Dicer the 21-25 nucleotide double-stranded product is loaded into an Argonuate protein (humans contain 4 Argonautes) and rendered single-stranded.
A short double-stranded RNA is passed from Dicer to an Argonaute and rendered single-stranded by removal and loss of the passenger strand. All Argonautes (AGO1 (EIF2C1), AGO2 (EIF2C2), AGO3 (EIF2C3), AGO4 (EIF2C4)) can remove the passenger strand without cleaving it. AGO2 (EIF2C2) possesses endonucleolytic activity and cleaves the passenger strand of siRNAs, which facilitates but is not required for removal of the passenger strand (Matranga et al. 2005). RNA helicase A associated with the RISC loading complex can facilitate removal of the passenger strand. The mechanism that selects which strand is retained as the guide RNA is not well understood in humans. Overhanging nucleotides and strength of base-pairing at each end of the input duplex are observed to influence strand selection. Argonaute proteins directly or indirectly bind many other proteins and appear to be present in more than one distinct complex.
In the case of AGO2 (EIF2C2), cleavage of one strand (the "passenger" strand) of the 21-25 nucleotide double-stranded RNA facilitates the loss of the passenger strand and the retention of the guide strand (Matranga et al. 2005). RNA helicase A has also been shown to enhance this reaction. AGO2 of humans may contain either miRNAs or siRNAs. The mechanism that selects which strand is retained as the guide RNA is not well understood in humans. Overhanging nucleotides and strength of base-pairing at each end of the input duplex are observed to influence strand selection. Argonaute proteins directly or indirectly bind many other proteins and appear to be present in more than one distinct complex.
Biogenesis of microRNAs (miRNAs) can be summarized in five steps (reviewed in Ketting 2011, Nowotny and Yang 2009, Kim et al. 2009, Chua et al. 2009, Hannon and He 2004): 1. Transcription. miRNA transcripts may come from autonomously transcribed genes, they may be contained in cotranscripts with other genes, or they may be located in introns of host genes. Most miRNAs are transcribed by RNA polymerase II, however a few miRNAs originate as RNA polymerase III cotranscripts with neighboring repetitive elements. The initial transcript, termed a primary microRNA (pri-miRNA), contains an imperfectly double-stranded region within a hairpin loop. Longer sequences extend from the 5' and 3' ends of the hairpin and may also contain double-stranded regions. 2. Cleavage by Drosha. The 5' and 3' ends of the pri-miRNA are removed during endoribonucleolytic cleavage by the Drosha nuclease in a complex with the RNA-binding protein DGCR8 (the Microprocessor complex). The cleavage product is a short hairpin of about 60 to 70 nt called the pre-microRNA (pre-miRNA). 3. Nuclear export by Exportin-5. The resulting pre-miRNA is bound by Exportin-5 in a complex with Ran and GTP. The complex translocates the pre-miRNA through the nuclear pore into the cytoplasm. 4. Cleavage by Dicer. Once in the cytoplasm the pre-miRNA is bound and cleaved by the Dicer ribonuclease in complex with the RNA-binding protein TRBP (TAR binding protein). The product is an imperfectly double-stranded miRNA of about 21 to 23 nucleotides. At this stage the double-stranded miRNA has protruding single-stranded 3' ends of 2-3 nt. 5. Strand selection and incorporation into RNA-Induced Silencing Complex (RISC). At this stage the miRNA has two strands: the passenger strand, which will be removed and degraded, and the guide strand, which will be retained and guides the RISC to target mRNAs. An Argonaute protein is already bound to the Dicer:miRNA complex or subsequently binds the complex (the order is unknown). The human genome encodes 4 Argonaute proteins (AGO1 (EIF2C1), AGO2 (EIF2C2), AGO3 (EIF2C3), AGO4 (EIF2C4)), however only AGO2 (EIF2C2) can cleave target mRNAs with perfect or nearly perfect complementarity to the guide miRNA. In mammalian cells, such endogenous interactions are very rare; most miRNAs only cause translational repression. For complexes that contain AGO2, cleavage of the passenger strand of the double-stranded miRNA accompanies removal of the passenger strand. Complexes containing other Argonautes may use a helicase to remove the passenger strand but this is not fully known. The resulting single-stranded miRNA (the guide strand) remains in a complex containing Argonaute, Dicer, TRBP, and other proteins termed the RNA-induced Silencing Complex (RISC). The full set of proteins composing RISC is not yet known.
In this module, the biology of various types of regulatory non-coding RNAs are described. Currently, biogenesis and functions of small interfering RNAs (siRNAs) and microRNAs are annotated.
Small RNAs act with components of the RNA-induced silencing complex (RISC) to repress expression of mRNAs (reviewed in Nowotny and Yang 2009, Chua et al. 2009). Two mechanisms exist: 1) cleavage of target RNAs by complexes containing Argonaute2 (AGO2, EIF2C2) and a guide RNA that exactly matches the target mRNA and 2) inhibition of translation of target RNAs by complexes containing AGO2 and an inexactly matching guide RNA or by complexes containing a nonendonucleolytic Argonaute (AGO1 (EIF2C1), AGO3 (EIF2C3), or AGO4 (EIF2C4)) and a guide RNA of exact or inexact match. Small interfering RNAs (siRNAs) and microRNAs (miRNAs) can serve as guide RNAs in both types of mechanism. RNAi also appears to direct chromatin modifications that cause transcriptional gene silencing (reviewed in Verdel et al. 2009).
Human Argonaute-2 (AGO2, EIF2C2) possesses ribonucleolytic activity in its PIWI domain and cleaves target RNAs that are exactly complementary to the guide RNA at a location around 10 nucleotides from the 5' end of the match with the guide RNA. The products of cleavage have a 5' phosphate and a 3' hydroxyl group. Both complexes containing siRNAs and miRNAs are capable of cleavage. Although Argonaute proteins interact with many other proteins, the complex of AGO2 and the guide RNA are sufficient to direct cleavage of target RNAs in vitro. In vivo, cleavage requires interaction of AGO2 with a TNRC6 protein and MOV10.
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Post-transcriptional regulation of gene expression by degradation of messenger RNAs
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Nuclear processing by Drosha Microprocessor complex. The primary-microRNA (pri-miRNA) is recognized by the Microprocessor complex (Drosha:DGCR8) and both strands of the pri-miRNA are cleaved by Drosha near the free 5' and 3' ends of the pri-miRNA, that is, at the ends distal from the internal loop. The product is a double-stranded RNA having 2 nucleotides protruding at the 3' end and having an internal loop.
A short double-stranded RNA is passed from Dicer to an Argonaute and rendered single-stranded by removal and loss of the passenger strand. All Argonautes (AGO1 (EIF2C1), AGO2 (EIF2C2), AGO3 (EIF2C3), AGO4 (EIF2C4)) can remove the passenger strand without cleaving it and most miRNAs are processed in this way. AGO2 (EIF2C2) can cleave the passenger strand of a subset of miRNAs that have no mismatches in the central region (Shin 2008). RNA helicase A associated with the RISC loading complex can facilitate removal of the passenger strand. The mechanism that selects which strand is retained as the guide RNA is not well understood in humans. Overhanging nucleotides and strength of base-pairing at each end of the input duplex are observed to influence strand selection. Argonaute proteins directly or indirectly bind many other proteins and appear to be present in more than one distinct complex.
Transcription of miRNA genes. Most miRNAs are transcribed by RNA polymerase II. The miRNAs may be autonomous transcription units or they may be located in other transcripts, including locations within introns and other untranslated regions. Of the polymerase II transcribed miRNAs, about 60% are located in introns of protein coding genes, 12 % are in introns of non-coding RNAs, 18% are in exons of non-coding RNAs, and 10% uncertain. A second class of miRNA genes are associated with Alu and other repetitive elements and are cotranscribed with these elements by RNA polymerase III. There are currently only a few proven examples of polymerase III transcribed miRNAs.
RecName: Full=5-hydroxytryptamine receptor 1A; Short=5-HT-1A; Short=5-HT1A; AltName: Full=Serotonin receptor 1A; AltName: Full=G-21; GN Name=HTR1A; Synonyms=ADRB2RL1, ADRBRL1; OS Homo sapiens
RecName: Full=5-hydroxytryptamine receptor 1B; AltName: Full=5-HT-1D-beta; Short=5-HT-1B; Short=5-HT1B; AltName: Full=Serotonin receptor 1B; AltName: Full=Serotonin 1D beta receptor; AltName: Full=S12; GN Name=HTR1B; Synonyms=HTR1DB; OS Homo sapiens
RecName: Full=5-hydroxytryptamine receptor 1D; Short=5-HT-1D; AltName: Full=5-HT-1D-alpha; AltName: Full=Serotonin receptor 1D; GN Name=HTR1D; Synonyms=HTR1DA, HTRL; OS Homo sapiens
RecName: Full=5-hydroxytryptamine receptor 1E; Short=5-HT-1E; Short=5-HT1E; AltName: Full=Serotonin receptor 1E; AltName: Full=S31; GN Name=HTR1E; OS Homo sapiens
RecName: Full=5-hydroxytryptamine receptor 1F; Short=5-HT-1F; AltName: Full=Serotonin receptor 1F; GN Name=HTR1F; Synonyms=HTR1EL; OS Homo sapiens
Formation of the cap-binding eIF4F complex
Formation of the 43S pre-initiation complex
Formation of eIF2:GDP:eIF2B intermediate
The 60S subunit joins the translation initiation complex
RecName: Full=Histamine H4 receptor; Short=HH4R; AltName: Full=G-protein coupled receptor 105; AltName: Full=GPRv53; AltName: Full=SP9144; AltName: Full=AXOR35; AltName: Full=Pfi-013; GN Name=HRH4; Synonyms=GPCR105; OS Homo sapiens
Cloning and expression of a human metabotropic glutamate receptor 1 alpha: enhanced coupling on co-transfection with a glutamate transporter
Met-tRNAi binds to eIF2:GTP to form the ternary complex
RecName: Full=Histamine H3 receptor; Short=HH3R; AltName: Full=G-protein coupled receptor 97; GN Name=HRH3; Synonyms=GPCR97; OS Homo sapiens
RecName: Full=Histamine H1 receptor; GN Name=HRH1; OS Homo sapiens
p-S193-KSRP binds 14-3-3zeta in the nucleus
Frequent and focal FGFR1 amplification associates with therapeutically tractable FGFR1 dependency in squamous cell lung cancer
Release of 40S and 60S subunits from the 80S ribosome
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unfolded actin/tubulin associates with prefoldin
Polypeptide release from the eRF3-GDP:eRF1:mRNA:80S Ribosome complex
GTP Hydrolysis by eRF3 bound to the eRF1:mRNA:polypeptide:80S Ribosome complex
GTP bound eRF3:eRF1 complex binds the peptidyl tRNA:mRNA:80S Ribosome complex
Regeneration of eEF1A:GTP by eEF1B activity
Peptide transfer from P-site tRNA to the A-site tRNA
Translocation of ribosome by 3 bases in the 3' direction
Molecular characterization and expression of heparan-sulfate 6-sulfotransferase. Complete cDNA cloning in human and partial cloning in Chinese hamster ovary cells
Cloning of the human glycine transporter type 1: molecular and pharmacological characterization of novel isoform variants and chromosomal localization of the gene in the human and mouse genomes
RecName: Full=Alpha-1D adrenergic receptor; AltName: Full=Alpha 1D-adrenoreceptor; AltName: Full=Alpha 1D-adrenoceptor; AltName: Full=Alpha-1A adrenergic receptor; AltName: Full=Alpha-adrenergic receptor 1a; GN Name=ADRA1D; Synonyms=ADRA1A; OS Homo sapiens
Sulfation of iodothyronines by recombinant human liver steroid sulfotransferases
RecName: Full=Alpha-1A adrenergic receptor; AltName: Full=Alpha 1A-adrenoreceptor; AltName: Full=Alpha 1A-adrenoceptor; AltName: Full=Alpha-1C adrenergic receptor; AltName: Full=Alpha-adrenergic receptor 1c; GN Name=ADRA1A; Synonyms=ADRA1C; OS Homo sapiens
RecName: Full=Alpha-1B adrenergic receptor; AltName: Full=Alpha 1B-adrenoreceptor; AltName: Full=Alpha 1B-adrenoceptor; GN Name=ADRA1B; OS Homo sapiens
Signal peptidase hydrolyzes signal peptide from ribosome-associated nascent protein
Aminoacyl-tRNA binds to the ribosome at the A-site
eEF1A:GTP:aminoacyl tRNA ternary complex formation.
Nascent polypeptide:mRNA:ribosome complex binds signal recognition particle (SRP)
Synthesis of nascent polypeptide containing signal sequence
Signal-containing nascent peptide translocates to endoplasmic reticulum
The SRP receptor binds the SRP:nascent peptide:ribosome complex
Dissociation of L13a from the 60s ribosomal subunit
Association of phospho-L13a with GAIT element of Ceruloplasmin mRNA
Efficient transcript production requires efficient release of RNA polymerase at the terminator; slow release at the terminator of a short transcription unit quickly becomes rate limiting for transcription at steady state. Although pol III autonomously recognizes sequence terminators, proteins that help to rapidly detach pol III from the terminator can affect the productivity of transcription if they eliminate termination as the rate-limiting step. La, NF1 family proteins, PC4 and topoisomerase I have been proposed as accessory pol III transcription factors that facilitate multi-cycle transcription by hspol III, and are hence described as positive regulators of termination.
RNA Polymerase III terminates transcription at extremely simple sites, consistent with its role in producing small transcripts. These sites are essentially "Tn" (in the non-transcribed strand).
Abortive initiation, the repetitive formation of short oligonucleotides, is a ubiquitous feature of transcriptional initiation. This Pathway contains events inferred from events in Saccharomyces cerevisiae.
The type 1 promoters recruit TFIIIA, the founding member of the C2H2 zinc finger family of DNA-binding proteins (Engelke et al., 1980; Sakonju et al., 1981). The binding of TFIIIA then allows the binding of TFIIC (Lassar et al., 1983), a complex consisting of five subunits (which differs from the six subunits in S. cerevisiae) in human cells and S. pombe. Once the DNA/TFIIIA/TFIIIC complex is formed, Brf1-TFIIIB joins the complex and this in turn allows the recruitment of RNA polymerase III (Bieker et al., 1985; Setzer and Brown, 1985).
Pol III initiation complexes open the promoter spontaneously. Indeed, this is the general case for DNA-dependent RNA polymerases. Only pol II, with its requirement for TFIIH-directed and ATP-dependent promoter opening is exceptional. TFIIH introduces a layer of mechanism that is not in the repertoire of any other transcriptase. Thus, it is pol III-mediated transcription that is, from a mechanistic perspective, most directly comparable with archaeal and also bacterial transcription. As promoter opening has been analyzed only in the S. cerevisiae this event is Inferred from the homologous pathway in yeast.
DCPS scavenges the 7-methylguanosine cap of mRNA
Rational design of a drug for Alzheimer's disease with cholinesterase inhibitory and neuroprotective activity
Productive transcription is accompanied by retractive RNase activity at U-tract pause sites and at the terminator. The principal cleavage products are dinucleotides, and they are produced in large stoichiometric excess over complete transcripts, despite the rapid overall rate of productive RNA chain elongation. This event is inferred from an event in Saccharomyces cerevisiae.
Transcription by pol III initiates at characteristic, simple start sequences. The universal core of these start sites is a pyrimidine-purine step, transcription initiating most frequently with ATP or GTP. This event is inferred from an event in Saccharomyces cerevisiae.
pyrophosphate + H2O => 2 orthophosphate [mitochondrial]
Exosome Complex hydrolyzes mRNA by 3' to 5' exoribonuclease digestion
SMG1 phosphorylates UPF1 (enhanced by Exon Junction Complex)
Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex
SMG6 hydrolyzes mRNA with premature termination codon
5' to 3' exoribonuclease hydrolyzes decapped mRNA
UPF1 binds an mRNP with a termination codon preceding an Exon Junction Complex
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Formation of UPF1:eRF3 complex on mRNA with a premature termination codon and no Exon Junction Complex
RecName: Full=Muscarinic acetylcholine receptor M2; GN Name=CHRM2; OS Homo sapiens
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RecName: Full=Muscarinic acetylcholine receptor M4; GN Name=CHRM4; OS Homo sapiens
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The type 2 promoters can recruit TFIIIC without the help of TFIIIA because TFIIIC binds directly to the A and B boxes. As for the type 1 promoters, this then allows the binding of Brf1-TFIIIB and RNA polymerase III. Importantly, in the yeast system, once Brf1-TFIIIB has been recruited to type 1 or 2 promoters, TFIIIA and/or TFIIIC can be stripped from the DNA with high salt or heparin treatment. Brf1-TFIIIB remains bound to the DNA and is sufficient to direct multiple rounds of transcription .
The rRNA genes are transcribed by RNA polymerase I, one of three eukaryotic nuclear RNA polymerases. The polymerase is a multisubunit complex, composed of two large subunits (the most conserved portions include the catalytic site that shares similarity with other eukaryotic and bacterial multisubunit RNA polymerases) and a number of smaller subunits. Under a number of experimental conditions the core is competent to mediate ribonucleic acid synthesis, in vivo however, it requires additional factors to select the appropriate template. In humans the RNA transcript (45S) is approximately 13,000 nucleotides long. Before leaving the nucleus as assembled ribosomal particles, the 45S rRNA is cleaved to give one copy each of the 28S rRNA, the 18S rRNA, and the 5.8S rRNA. Equal quantities of the three rRNAs are produced by initially transcribing them as one transcript.
Abortive initiation, the repetitive formation of short oligonucleotides, is a ubiquitous feature of transcriptional initiation. This event is inferred from an event in Saccharomyces cerevisiae.
During initiation the double-stranded DNA must be melted and transcription begins. SL1 forms and interacts with UBF-1 and the rDNA promoter. It is this platform that will recruit active RNA polymerase I to the SL1:phosphorlated UBF-1:rDNA promoter complex. Mammalian rRNA genes are preceded by a terminator element that is recognized by the SL1 complex. This SL1 modulated acetylation of the basal Pol I transcription machinery has functional consequences suggesting that the reversible acetylation may be one way to regulate rDNA transcription.
Promoter clearance is one of the rate-limiting steps in Polymerase I transcription. This step is composed of three phases, promoter opening, transcription initiation and promoter escape.
OVERVIEW OF TRANSCRIPTION REGULATION: Detailed studies of gene transcription regulation in a wide variety of eukaryotic systems has revealed the general principles and mechanisms by which cell- or tissue-specific regulation of differential gene transcription is mediated (reviewed in Naar, 2001. Kadonaga, 2004, Maston, 2006, Barolo, 2002; Roeder, 2005, Rosenfeld, 2006). Of the three major classes of DNA polymerase involved in eukaryotic gene transcription, Polymerase II generally regulates protein-encoding genes. Figure 1 shows a diagram of the various components involved in cell-specific regulation of Pol-II gene transcription. Core Promoter: Pol II-regulated genes typically have a Core Promoter where Pol II and a variety of general factors bind to specific DNA motifs: i: the TATA box (TATA DNA sequence), which is bound by the "TATA-binding protein" (TBP). ii: the Initiator motif (INR), where Pol II and certain other core factors bind, is present in many Pol II-regulated genes. iii: the Downstream Promoter Element (DPE), which is present in a subset of Pol II genes, and where additional core factors bind. The core promoter binding factors are generally ubiquitously expressed, although there are exceptions to this. Proximal Promoter: immediately upstream (5') of the core promoter, Pol II target genes often have a Proximal Promoter region that spans up to 500 base pairs (b.p.), or even to 1000 b.p.. This region contains a number of functional DNA binding sites for a specific set of transcription activator (TA) and transcription repressor (TR) proteins. These TA and TR factors are generally cell- or tissue-specific in expression, rather than ubiquitous, so that the presence of their cognate binding sites in the proximal promoter region programs cell- or tissue-specific expression of the target gene, perhaps in conjunction with TA and TR complexes bound in distal enhancer regions. Distal Enhancer(s): many or most Pol II regulated genes in higher eukaryotes have one or more distal Enhancer regions which are essential for proper regulation of the gene, often in a cell or tissue-specific pattern. Like the proximal promoter region, each of the distal enhancer regions typically contain a cluster of binding sites for specific TA and/or TR DNA-binding factors, rather than just a single site. Enhancers generally have three defining characteristics: i: They can be located very long distances from the promoter of the target gene they regulate, sometimes as far as 100 Kb, or more. ii: They can be either upstream (5') or downstream (3') of the target gene, including within introns of that gene. iii: They can function in either orientation in the DNA. Combinatorial mechanisms of transcription regulation: The specific combination of TA and TR binding sites within the proximal promoter and/or distal enhancer(s) provides a "combinatorial transcription code" that mediates cell- or tissue-specific expression of the associated target gene. Each promoter or enhancer region mediates expression in a specific subset of the overall expression pattern. In at least some cases, each enhancer region functions completely independently of the others, so that the overall expression pattern is a linear combination of the expression patterns of each of the enhancer modules. Co-Activator and Co-Repressor Complexes: DNA-bound TA and TR proteins typically recruit the assembly of specific Co-Activator (Co-A) and Co-Repressor (Co-R) Complexes, respectively, which are essential for regulating target gene transcription. Both Co-A's and Co-R's are multi-protein complexes that contain several specific protein components. Co-Activator complexes generally contain at lease one component protein that has Histone Acetyl Transferase (HAT) enzymatic activity. This functions to acetylate Histones and/or other chromatin-associated factors, which typically increases that transcription activation of the target gene. By contrast, Co-Repressor complexes generally contain at lease one component protein that has Histone De-Acetylase (HDAC) enzymatic activity. This functions to de-acetylate Histones and/or other chromatin-associated factors. This typically increases the transcription repression of the target gene. Adaptor (Mediator) complexes: In addition to the co-activator complexes that assemble on particular cell-specific TA factors, - there are at least two additional transcriptional co-activator complexes common to most cells. One of these is the Mediator complex, which functions as an "adaptor" complex that bridges between the tissue-specific co-activator complexes assembled in the proximal promoter (or distal enhancers). The human Mediator complex has been shown to contain at least 19 protein distinct components. Different combinations of these co-activator proteins are also found to be components of specific transcription Co-Activator complexes, such as the DRIP, TRAP and ARC complexes described below. TBP/TAF complex: Another large Co-A complex is the "TBP-associated factors" (TAFs) that assemble on TBP (TATA-Binding Protein), which is bound to the TATA box present in many promoters. There are at least 23 human TAF proteins that have been identified. Many of these are ubiquitously expressed, but TAFs can also be expressed in a cell or tissue-specific pattern. Specific Coactivator Complexes for DNA-binding Transcription Factors. A number of specific co-activator complexes for DNA-binding transcription factors have been identified, including DRIP, TRAP, and ARC (reviewed in Bourbon, 2004, Blazek, 2005, Conaway, 2005, and Malik, 2005). The DRIP co-activator complex was originally identified and named as a specific complex associated with the Vitamin D Receptor member of the nuclear receptor family of transcription factors (Rachez, 1998). Similarly, the TRAP co-activator complex was originally identified as a complex that associates with the thyroid receptor (Yuan, 1998). It was later determined that all of the components of the DRIP complex are also present in the TRAP complex, and the ARC complex (discussed further below). For example, the DRIP205 and TRAP220 proteins were show to be identical, as were specific pairs of the other components of these complexes (Rachez, 1999). In addition, these various transcription co-activator proteins identified in mammalian cells were found to be the orthologues or homologues of the Mediator ("adaptor") complex proteins (reviewed in Bourbon, 2004). The Mediator proteins were originally identified in yeast by Kornberg and colleagues, as complexes associated with DNA polymerase (Kelleher, 1990). In higher organisms, Adapter complexes bridge between the basal transcription factors (including Pol II) and tissue-specific transcription factors (TFs) bound to sites within upstream Proximal Promoter regions or distal Enhancer regions (Figure 1). However, many of the Mediator homologues can also be found in complexes associated with specific transcription factors in higher organisms. A unified nomenclature system for these adapter / co-activator proteins now labels them Mediator 1 through Mediator 31 (Bourbon, 2004). For example, the DRIP205 / TRAP220 proteins are now identified as Mediator 1 (Rachez, 1999), based on homology with yeast Mediator 1. Example Pathway: Specific Regulation of Target Genes During Notch Signaling: One well-studied example of cell-specific regulation of gene transcription is selective regulation of target genes during Notch signaling. Notch signaling was first identified in Drosophila, where it has been studied in detail at the genetic, molecular, biochemical and cellular levels (reviewed in Justice, 2002; Bray, 2006; Schweisguth, 2004; Louvri, 2006). In Drosophila, Notch signaling to the nucleus is thought always to be mediated by one specific DNA binding transcription factor, Suppressor of Hairless. In mammals, the homologous genes are called CBF1 (or RBPJkappa), while in worms they are called Lag-1, so that the acronym "CSL" has been given to this conserved transcription factor family. There are at least two human CSL homologues, which are now named RBPJ and RBPJL. In Drosophila, Su(H) is known to be bifunctional, in that it represses target gene transcription in the absence of Notch signaling, but activates target genes during Notch signaling. At least some of the mammalian CSL homologues are believed also to be bifunctional, and to mediate target gene repression in the absence of Notch signaling, and activation in the presence of Notch signaling. Notch Co-Activator and Co-Repressor complexes: This repression is mediated by at least one specific co-repressor complexes (Co-R) bound to CSL in the absence of Notch signaling. In Drosophila, this co-repressor complex consists of at least three distinct co-repressor proteins: Hairless, Groucho, and dCtBP (Drosophila C-terminal Binding Protein). Hairless has been show to bind directly to Su(H), and Groucho and dCtBP have been shown to bind directly to Hairless (Barolo, 2002). All three of the co-repressor proteins have been shown to be necessary for proper gene regulation during Notch signaling in vivo (Nagel, 2005). In mammals, the same general pathway and mechanisms are observed, where CSL proteins are bifunctional DNA binding transcription factors (TFs), that bind to Co-Repressor complexes to mediate repression in the absence of Notch signaling, and bind to Co-Activator complexes to mediate activation in the presence of Notch signaling. However, in mammals, there may be multiple co-repressor complexes, rather than the single Hairless co-repressor complex that has been observed in Drosophila. During Notch signaling in all systems, the Notch transmembrane receptor is cleaved and the Notch intracellular domain (NICD) translocates to the nucleus, where it there functions as a specific transcription co-activator for CSL proteins. In the nucleus, NICD replaces the Co-R complex bound to CSL, thus resulting in de-repression of Notch target genes in the nucleus (Figure 2). Once bound to CSL, NICD and CSL proteins recruit an additional co-activator protein, Mastermind, to form a CSL-NICD-Mam ternary co-activator (Co-A) complex. This Co-R complex was initially thought to be sufficient to mediate activation of at least some Notch target genes. However, there now is evidence that still other co-activators and additional DNA-binding transcription factors are required in at least some contexts (reviewed in Barolo, 2002). Thus, CSL is a good example of a bifunctional DNA-binding transcription factor that mediates repression of specific targets genes in one context, but activation of the same targets in another context. This bifunctionality is mediated by the association of specific Co-Repressor complexes vs. specific Co-Activator complexes in different contexts, namely in the absence or presence of Notch signaling.
isoleucine + tRNA(Ile) + ATP => Ile-tRNA(Ile) + AMP + pyrophosphate
After the assembly of the RNA Polymerase I Holoenzyme, Rrn3 binding occurs.
leucine + tRNA(Leu) + ATP => Leu-tRNA(Leu) + AMP + pyrophosphate
Cellular senescence involves irreversible growth arrest accompanied by phenotypic changes such as enlarged morphology, reorganization of chromatin through formation of senescence-associated heterochromatic foci (SAHF), and changes in gene expression that result in secretion of a number of proteins that alter local tissue environment, known as senescence-associated secretory phenotype (SASP). Senescence is considered to be a cancer protective mechanism and is also involved in aging. Senescent cells accumulate in aged tissues (reviewed by Campisi 1997 and Lopez-Otin 2013), which may be due to an increased senescence rate and/or decrease in the rate of clearance of senescent cells. In a mouse model of accelerated aging, clearance of senescent cells delays the onset of age-related phenotypes (Baker et al. 2011). Cellular senescence can be triggered by the aberrant activation of oncogenes or loss-of-function of tumor suppressor genes, and this type of senescence is known as the oncogene-induced senescence, with RAS signaling-induced senescence being the best studied. Oxidative stress, which may or may not be caused by oncogenic RAS signaling, can also trigger senescence. Finally, the cellular senescence program can be initiated by DNA damage, which may be caused by reactive oxygen species (ROS) during oxidative stress, and by telomere shortening caused by replicative exhaustion which may be due to oncogenic signaling. The senescent phenotype was first reported by Hayflick and Moorhead in 1961, when they proposed replicative senescence as a mechanism responsible for the cessation of mitotic activity and morphological changes that occur in human somatic diploid cell strains as a consequence of serial passaging, preventing the continuous culture of untransformed cells-the Hayflick limit (Hayflick and Moorhead 1961). Senescent cells may remain viable for years, such as senescent melanocytes of moles and nevi, or they can be removed by phagocytic cells. The standard marker for immunohistochemical detection of senescent cells is senescence-associated beta-galactosidase (SA-beta-Gal), a lysosomal enzyme that is not required for senescence. For a recent review, please refer to Collado et al. 2007, Adams 2009, Kuilman et al. 2010. For a review of differential gene expression between senescent and immortalized cells, please refer to Fridman and Tainsky 2008.
lysine + tRNA(Lys) + ATP => Lys-tRNA(Lys) + AMP + pyrophosphate
Cells are subject to external molecular and physical stresses such as foreign molecules that perturb metabolic or signaling processes, and changes in temperature or pH. The ability of cells and tissues to modulate molecular processes in response to such external stresses is essential to the maintenance of tissue homeostasis (Kultz 2005).
methionine + tRNA(Met) + ATP => Met-tRNA(Met) + AMP + pyrophosphate
proline + tRNA(Pro) + ATP => Pro-tRNA(Pro) + AMP + pyrophosphate
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tyrosine + tRNA(Tyr) + ATP => Tyr-tRNA(Tyr) + AMP + pyrophosphate
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The principal cleavage products are dinucleotides, and they are produced in large stoichiometric excess over complete transcripts. Overall productive RNA chain elongation proceeds quite rapidly. This event is inferred from an event in Saccharomyces cerevisiae.
Recovery from pausing occurs spontaneously after a variable length of time as the enzyme spontaneously slides forward again. This renders the transcript's 3'-OH terminus realigned with the catalytic Mg2+ site of the enzyme. TFIIS is capable of excising the nascent transcript at 2 or 3 nucleotides upstream of the transcript's 3'-end to reinitiate processive elongation (reviewed by Shilatifard et al., 2003).
MK2 phosphorylates ZFP36 (Tristetraproline, TTP)
Pol II pausing is believed to result from reversible backtracking of the Pol II enzyme complex by ~2 to 4 nucleotides. This leads to misaligned 3'-OH terminus that is unable to be an acceptor for the incoming NTPs in synthesis of next phosphodiester bond (reviewed by Shilatifard et al., 2003).
p-S60,S186-ZFP36 (Tristetraproline, TTP) binds 14-3-3beta
TFIIS reactivates arrested RNA Pol II directly interacting with the enzyme resulting in endonucleolytic excision of nascent transcript ~7-14 nucleotides upstream of the 3' end. This reaction is catalyzed by the catalytic site and results in the generation of a new 3'-OH terminus that could be used for re-extension from the correctly base paired site (reviewed by Shilatifard et al., 2003).
RNA Pol II arrest is believed to be a result of irreversible backsliding of the enzyme by ~7-14 nucleotides. It is suggested that, arrest leads to extrusion of displaced transcripts 3'-end through the small pore near the Mg2+ ion. Pol II arrest may lead to abortive termination of elongation due to irreversible trapping of the 3'-end of the displaced transcript in the pore (reviewed by Shilatifard et al., 2003).
ZFP36 (Tristetraproline, TTP) binds AU-rich elements in 3' UTR of target mRNAs
In the early elongation phase, shorter transcripts typically of ~30 nt in length are generated due to random termination of elongating nascent transcripts. This abortive cessation of elongation has been observed mainly in the presence of DSIF-NELF bound to Pol II complex. (Reviewed in Conaway et al.,2000; Shilatifard et al., 2003 ).
At the beginning of this reaction, 1 molecule of 'Arrested processive elongation complex' is present. At the end of this reaction, 1 molecule of 'Aborted elongation complex after arrest' is present. This reaction takes place in the 'nucleus'.
At the beginning of this reaction, 1 molecule of 'pol II open pre-initiation complex' is present. At the end of this reaction, 1 molecule of 'pol II closed pre-initiation complex' is present. This reaction takes place in the 'nucleus'.
Protein Kinase B/Akt phosphorylates BRF1
Mothers against decapentaplegic homolog 5
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Protein Kinase B/Akt phosphorylates KSRP
At the beginning of this reaction, 1 molecule of 'FACT 140 kDa subunit', and 1 molecule of 'FACT 80 kDa subunit' are present. At the end of this reaction, 1 molecule of 'FACT complex' is present. This reaction takes place in the 'nucleus'.
At the beginning of this reaction, 1 molecule of 'Cdk 9 protein', 1 molecule of 'Cyclin T1', and 1 molecule of 'Cyclin T2' are present. At the end of this reaction, 1 molecule of 'P-TEFb complex' is present. This reaction takes place in the 'nucleus'.
KSRP binds AU-rich element in 3' UTR of mRNA
At the beginning of this reaction, 1 molecule of 'Elongin A1 protein', and 1 molecule of 'Elongin B:C complex' are present. At the end of this reaction, 1 molecule of 'Elongin Complex' is present. This reaction takes place in the 'nucleus'.
KSRP recruits RNA degradation activities
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Mothers against decapentaplegic homolog 9
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Cleavage-based removal of the siRNA passenger strand by AGO2
RNA polymerase III is one of three types of nuclear RNA polymerases present in eucaryotic cells. About 10% of the total transcription in dividing cells can be attributed to its activity. It synthesizes an eclectic collection of catalytic or structural RNA molecules, some of which are involved in protein synthesis, pre-mRNA splicing, tRNA processing, and the control of RNA polymerase II elongation, whereas some others have still unknown functions. Like other RNA polymerases, RNA polymerase III cannot recognize its target promoters directly. Instead it is recruited to specific promoter sequences through the help of transcription factors. There are three basic types of RNA polymerase III promoters, called types 1, 2, and 3(Geiduschek and Kassavetis, 1992). Although in vivo, RNA polymerase III may be recruited to these promoters as part of a large complex (holo RNA polymerase III) containing the polymerase and its initiation factors (Wang et al., 1997), in vitro the reaction can be divided into several steps. First, the promoter elements are recognized by DNA binding factors, which then recruit a factor known as TFIIIB. TFIIIB itself then directly contacts RNA polymerase III. In human cells but not in S. cerevisiae, there are at least two versions of TFIIIB. One contains TBP, Bdp1, and Brf1 (Brf1-TFIIIB), and the other TBP, Bdp1, and Brf2 (Brf2-TFIIIB) (Schramm et al., 2000; Teichmann et al., 2000).
Endonucleolytic RISC hydrolyzes target RNAs
Pol III initiation complexes open the promoter spontaneously similar to the mechanism employed in archaeal and bacterial transcription.
AUF1(hnRNP D0) dimers bind AU-rich element in 3' UTR of mRNA
At the beginning of this reaction, 1 molecule of 'SUPT5H protein', and 1 molecule of 'SPT4H1 protein' are present. At the end of this reaction, 1 molecule of 'DSIF complex' is present. This reaction takes place in the 'nucleus'.
At the beginning of this reaction, 1 molecule of 'Elongin B protein', and 1 molecule of 'Elongin C protein' are present. At the end of this reaction, 1 molecule of 'Elongin B:C complex' is present. This reaction takes place in the 'nucleus'.
Transcription by RNA Polymerase I, RNA Polymerase III and transcription from mitochondrial promoters.
Microprocessor complex cleaves pri-miRNA to pre-miRNA
At the beginning of this reaction, 1 molecule of 'pol II transcription complex containing 4-9 nucleotide long transcript' is present. At the end of this reaction, 1 molecule of 'template DNA:4-9 nucleotide transcript hybrid', 1 molecule of 'TFIIH', 1 molecule of 'TFIIE', and 1 molecule of 'RNA Polymerase II (unphosphorylated):TFIIF complex' are present. This reaction takes place in the 'nucleus'.
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There are three basic types of RNA polymerase III promoters. The three types of RNA polymerase III promoters are known as type 1, type 2, and type 3 promoters. Type 1 promoters are found in the 5S genes and consist of a gene-internal element called the internal control region (ICR), that is subdivided into A block, intermediate element, and C block (Bogenhagen, 1985; Sakonju et al., 1980). Type 2 promoters are found in tRNA genes, Adenovirus 2 VAI gene, and other genes (Galli et al., 1981; Sharp et al., 1981). These promoters consists of two gene-internal elements called the A and the B boxes. Type 3 promoters consist of a distal sequence element (DSE) that serves as an enhancer, a proximal sequence element (PSE), and a TATA box (Baer et al., 1989; Lobo and Hernandez, 1989). Some promoters combine elements from type 2 and 3 promoters. For example, the S. cerevisiae U6 promoter, also shown in the figure, contains the TATA box typical of type 3 promoters and the A and B boxes typical of type 2 promoters. Moreover, in S. pombe, nearly all tRNA and 5S genes contain a TATA box in addition to gene-internal elements, and the TATA box is required for transcription.
AUF1 binds translation and heat shock proteins
The transition from abortive to productive transcription may occur at bp +5. The primary transcripts of pol III-transcribed genes are short, ~90 to 120 nt for tRNA and 5s RNA genes (which constitute the great majority of products) and even the longest transcripts (e.g. the RNA of the signal recognition particles) are only ~500 nt. This event is inferred from an event in Saccharomyces cerevisiae.
Butyrate Response Factor1 (BRF1) binds AU-rich element in 3' UTR of mRNA
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New insights into the mechanism of heat shock response activation
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626560
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631726
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15723.2
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631732
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626569
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=390625
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626573
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649928
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626562
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_174153.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626561
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649929
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625893
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649927
Laminin gamma2 mediates Wnt5a-induced invasion of gastric cancer cells
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649932
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_174171.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626575
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642541
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642601
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642442
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642475
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642579
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642617
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_195180.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646538
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_161274.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2162198
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_258174.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652530
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_197668.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653474
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649905
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649906
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649903
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646562
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649915
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_195183.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642572
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642519
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649892
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642577
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642498
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642615
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Critical role for Ebf1 and Ebf2 in the adipogenic transcriptional cascade
Cell surface interactions at the vascular wall
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646559
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2162212
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=352605
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_160371.1
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649964
Concerted action of two cation filters in the aquaporin water channel
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_195181.3
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649946
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646551
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649961
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642456
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_174178.3
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649911
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649969
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642553
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_174180.3
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_161541.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_161345.1
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A yeast chromosomal origin of DNA replication defined by multiple functional elements.
Beta-tubulin:GTP:Cofactor D+alpha-tubulin:GTP:Cofactor E-> Beta-tubulin:GTP:Cofactor D:alpha-tubulin:GTP:Cofactor E
EIF5A + spermidine <=> EIF5A(Dhp) + 1,3-diaminopropane
Beta-tubulin:GTP:Cofactor D:alpha-tubulin:GTP:Cofactor E+ Cofactor C-> Beta-tubulin:GTP:Cofactor D:alpha-tubulin:GTP:Cofactor E:Cofactor C
EIF5A(Dhp) + 1,3-diaminopropane <=> EIF5A + spermidine
N-acetylglucosaminyl-PI + H2O -> glucosaminyl-PI + acetate
CD44 interaction with Na+-H+ exchanger (NHE1) creates acidic microenvironments leading to hyaluronidase-2 and cathepsin B activation and breast tumor cell invasion
glucosaminyl-PI + fatty acyl-CoA -> glucosaminyl-acyl-PI + CoA-SH
mannose(a1-4)glucosaminyl-acyl-PI + phosphatidylethanolamine -> (ethanolamineP) mannose(al1-4)glucosaminyl-acyl-PI + diacylglycerol
(ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI + dolichol phosphate D-mannose -> mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI + dolichol phosphate
mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI + dolichol phosphate D-mannose -> mannose (a1-2) mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI + dolichol phosphate
Matrix metalloproteinases and the regulation of tissue remodelling
Communication between the synapse and the nucleus in neuronal development, plasticity, and disease
Exchange of ADP for ATP in CCT/TriC:actin complex
Hydrolysis of ATP and release of tubulin folding intermediate from CCT/TriC
ADP is exchanged for ATP in the (ADP:CCT/TriC):tubulin complex
Actin/tubulin:prefoldin complex associates with CCT/TriC
Beta-tubulin:GTP + Cofactor D -> Beta-tubulin:GTP: Cofactor D
alpha-tubulin:GTP + Cofactor B -> alpha-tubulin:GTP: Cofactor B
Hydrolysis of ATP and release of folded actin from CCT/TriC
Association of CCT/TriC with sphingosine kinase 1
alpha-tubulin:GTP + Cofactor E -> alpha-tubulin:GTP:Cofactor E
alpha-tubulin:GTP:Cofactor B +Cofactor E -> alpha-tubulin:GTP: Cofactor E +Cofactor B
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649923
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649922
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649921
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649920
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_174124.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649841
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642555
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649835
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649834
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649832
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649830
RecName: Full=5-hydroxytryptamine receptor 6; Short=5-HT-6; AltName: Full=Serotonin receptor 6; GN Name=HTR6; OS Homo sapiens
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642418
RecName: Full=5-hydroxytryptamine receptor 4; Short=5-HT-4; Short=5-HT4; AltName: Full=Serotonin receptor 4; GN Name=HTR4; OS Homo sapiens
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642500
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642545
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642581
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642619
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642610
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642560
RecName: Full=5-hydroxytryptamine receptor 7; Short=5-HT-7; Short=5HT7; AltName: Full=5-HT-X; AltName: Full=Serotonin receptor 7; GN Name=HTR7; OS Homo sapiens
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642608
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_164849.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3238096
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2982.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=162743
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649828
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649827
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_174131.3
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649825
RecName: Full=5-hydroxytryptamine receptor 2A; Short=5-HT-2A; Short=5-HT-2; AltName: Full=Serotonin receptor 2A; GN Name=HTR2A; Synonyms=HTR2; OS Homo sapiens
RecName: Full=5-hydroxytryptamine receptor 2B; Short=5-HT-2B; AltName: Full=Serotonin receptor 2B; GN Name=HTR2B; OS Homo sapiens
RecName: Full=5-hydroxytryptamine receptor 2C; Short=5-HTR2C; Short=5-HT-2C; Short=5-HT2C; AltName: Full=5HT-1C; AltName: Full=Serotonin receptor 2C; GN Name=HTR2C; Synonyms=HTR1C; OS Homo sapiens
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652315
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652314
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_229047.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5340556
Congenital Disorders of Glycosylation Overview
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649839
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641990
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653067
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_27417.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1660674
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_253116.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=917716
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_116261.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652268
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_260682.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637865
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637864
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642194
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637868
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637867
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637866
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642198
tetra-mu3-sulfido-tetrairon [ChEBI:49883]
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_176022.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649821
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653416
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649823
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642205
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The myeloma-associated oncogene fibroblast growth factor receptor 3 is transforming in hematopoietic cells
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Protein phosphatase 1 regulates assembly and function of the beta-catenin degradation complex
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Genetic Analysis of Coenzyme Q Biosynthesis
Coenzyme Q: Molecular Mechanisms in Health and Disease (Book): 185-208
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The dishevelled protein is modified by wingless signaling in Drosophila
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The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen
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Magnesium transporters: properties, regulation and structure
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Two isoforms of glutamate decarboxylase: why?
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The 5'-ends of all eukaryotic pre-mRNAs studied thus far are converted to cap structures. The cap is thought to influence splicing of the first intron, and is bound by 'cap-binding' proteins, CBP80 and CBP20, in the nucleus. The cap is important for translation initiation, and it also interacts with the poly(A)terminus, via proteins, resulting in circularization of the mRNA to facilitate multiple rounds of translation. The cap is also important for mRNA stability, protecting it from 5' to 3' nucleases, and is required for mRNA export to the cytoplasm. The capping reaction usually occurs very rapidly on nascent transcripts; after the synthesis of only a few nucleotides by RNA polymerase II. The capping reaction involves the conversion of the 5'-end of the nascent transcript from a triphosphate to a diphosphate by a RNA 5'-triphosphatase, followed by the addition of a guanosine monophosphate by the mRNA guanylyltransferase, to form a 5'-5'-triphosphate linkage. This cap is then methylated by 2'-O-methyltransferases.
The formation of the B complex is ATP-dependent, and both the 5' and 3' splice sites are essential for B complex assembly. The U4 and U6 snRNPS are extensively base-paired, and this U4:U6 complex associates with the U5 snRNP to form a tri-snRNP particle. This tri-snRNP particle then binds to the spliceosomal A complex, to form the spliceosomal B complex.
The spliceosomal C complex is a very short-lived intermediate; the splicing intermediates are rapidly converted to splicing products. Also, the spliced products are released very rapidly, and no complex containing both the splicing products has been isolated. Conversion of the spliceosomal B complex to the spliceosomal C complex requires ATP. The extensive base-pairing between the U4 and U6 snRNAs is disrupted during the formation of the C complex, which is thought to require helicase-type activity associated with the DEAD box factors.
The active C complex is formed due to a conformational change in the intermediate C complex. After formation of the active C complex, the splicing reactions occur very rapidly.
The diphosphate 5'-end of the mRNA is joined to the GMP, releasing it from the enzyme. At this time, it is unclear how the RNA diphosphate end is transferred from the active site of the triphosphatase to the guanylyltransferase site. The covalent enzyme-GMP complex can form in the absence of RNA. Guanylyltransferase (GT) catalyzed second reaction can be represented as:ppN(pN)n + GTP -> GpppN(pN)n + PPi
In the final step of the capping reaction, the methyltransferase takes a methyl group from S-adenosyl-methionine to the N7 position of the cap guanine. N7G-methyltransferase (MT) mediated reaction can be represented as: GpppN(pN)n + S-adenosylmethionine (Adomet) ->m7GpppN(pN)n + S-adenosylhomocysteine (Adohcy).
GMP capped mRNA transcript dissociates from GT for further modification.
At the beginning of this reaction, 1 molecule of 'CBP80', and 1 molecule of 'CBP20' are present. At the end of this reaction, 1 molecule of 'Cap Binding Complex (CBC)' is present. This reaction takes place in the 'nucleus'.
The cap binding complex binds to the methylated GMP cap on the nascent mRNA transcript.
The splicing of a subset of pre-mRNA introns occurs by a second pathway, designated the AT-AC or U12-dependent splicing pathway. AT-AC introns have highly conserved, non-canonical splice sites that are removed by the AT-AC spliceosome, which contains distinct snRNAs (U11, U12, U4atac, U6atac) that are structurally and functionally analogous to the major spliceosome. U5 snRNA as well as many of the protein factors appear to be conserved between the two spliceosomes.
The process in which excision of introns from the primary transcript of messenger RNA (mRNA) is followed by ligation of the two exon termini exposed by removal of each intron, is called mRNA splicing. Most of the mRNA is spliced by the major pathway, involving the U1, U2, U4, U5 and U6 snRNPs. A minor fraction, about 1 %, of the mRNAs are spliced via the U12 dependent pathway.
At the beginning of this reaction, 1 molecule of 'ATAC C Complex' is present. At the end of this reaction, 1 molecule of 'ATAC C Complex with lariat containing 5'-end cleaved mRNA' is present. This reaction takes place in the 'nucleus'.
At the beginning of this reaction, 1 molecule of 'ATAC C Complex with lariat containing 5'-end cleaved mRNA' is present. At the end of this reaction, 1 molecule of 'U6 ATAC snRNP', 1 molecule of 'post exon ligation complex', 1 molecule of 'U12 snRNP', 1 molecule of 'U11 snRNP', and 1 molecule of 'U5 snRNP' are present. This reaction takes place in the 'nucleus'.
Electron transport from NADPH to Ferredoxin
Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers
At the beginning of this reaction, 1 molecule of 'Magoh-Y14 complex', and 1 molecule of 'Spliceosomal active C complex with lariat containing, 5'-end cleaved pre-mRNP:CBC complex' are present. At the end of this reaction, 1 molecule of 'Exon Junction Complex' is present. This reaction takes place in the 'nucleoplasm'.
In the first catalytic step of mRNA splicing, the 2' OH group of the bulged A at the branch site performs a nucleophilic attack on the 5' splice site phosphodiester bond, resulting in cleavage of the bond between the 5' exon and the 5' end of the intron, and formation of a new bond between the 5' end of the intron and the branch site A. This results in a lariat-shaped intermediate, with the intron still attached to the 3' exon. The branch site A has a 2'-5' phosphodiester bond with the G at the beginning of the intron, in addition to the usual 5'-3' and 3'-5'phosphodiester bonds.
At the beginning of this reaction, 1 molecule of 'ATAC B Complex' is present. At the end of this reaction, 1 molecule of 'U4 ATAC snRNP', and 1 molecule of 'ATAC C Complex' are present. This reaction takes place in the 'nucleus'.
The U4atac/U6atac enters the spliceosome and U6atac snRNA forms base pairing interactions with the 5' ss and also forms base pairing interactions with U12 and U4atac is partially displaced. U5 snRNP, the only snRNP common to both the major and minor splicing pathways, also joins the spliceosome to form the B complex and interacts with nucleotides within the 3' end of the exon flanking the 5' ss.
U12-type AT-AC introns are distinguished from the major U2-type introns by the consensus sequences of their highly conserved splicing signals. U12 introns have the 5' ss consensus sequence (G/A)TATCCTTT, the branchpoint sequence TTTCCTTAACT and the 3' ss (C/T)AG. Initial recognition of AT-AC introns involves interaction of U12 snRNP with the branch-point sequence and U11 with the 5' ss. Unlike the major splicing pathway, U11 and U12 are in a complex and interact with the pre-mRNA simultaneously, binding in an ATP-dependent manner as a di-snRNP complex and likely bridging the 5' ss and 3' ss region. Twenty proteins have been identified in the U11/U12 di-snRNP complex including the snRNP Sm proteins BÃ¢â¬â¢, B, D3, D2, D1, E, F, and G which are identical to the major splicing pathway Sm proteins. A U2 snRNP core protein complex, SF3b is also found in the U11/U12 di-snRNP, including p14, a protein that interacts with the branchpoint adenosine. SR proteins are required for formation of A complex in AT-AC splicing. The same SR proteins involved in splicing of the major introns are also active in splicing of AT-AC introns, though, as in the major pathway, there is substrate specificity.
The splicing of pre-mRNA occurs within a large, very dynamic complex, designated the 'spliceosome'. The 50-60S spliceosomes are estimated to be 40-60 nm in diameter, and have molecular weights in the range of 3-5 million kDa. Small nuclear RNAs (snRNAs) U1, U2, U4, U5, and U6, are some of the best characterized components of spliceosomes, and are known to play key roles not only in spliceosomal assembly, but also in the two catalytic steps of the splicing reaction. Over 150 proteins have been detected in spliceosomes, and only a subset of these has been characterized. The characterization, and the determination of the functions of the protein components of the spliceosome, is still work in progress. During spliceosome assembly, the snRNAs and the spliceosomal proteins assemble on the pre-mRNA in a stepwise pathway. First the E complex forms, followed by complexes A and B; the C complex forms next and contains the products of the first step of the splicing reaction. Complexes called i and D form as a consequence of the second step of the splicing reaction, which contain the excised intron and the spliced exons, respectively.
There are two well-documented trans-acting factors required for histone pre-mRNA processing. These are: 1 Stem-loop binding protein (SLBP), also termed hairpin binding protein (HBP). This 32 kDa protein is likely the first protein that binds to the histone pre-mRNA as it is being transcribed. The U7 snRNP. This particle contains the U7 snRNA, the smallest of the snRNAs which varies from 57-70 nts long depending on the species. The 5' end of U7 snRNA binds to a sequence 3' of the stemloop, termed the histone downstream element (HDE). There are a number of proteins found in the U7 snRNP. There are 7 Sm proteins, as are present in the spliceosomal snRNP. Five of these proteins are the same as ones found in the spliceosomal snRNPs and there are 2, Lsm10 and Lsm11 that are unique to U7 snRNP. A third protein joins the U7 snRNP, ZFP100, a large zinc finger protein. ZFP100 interacts with SLBP bound to the histone pre-mRNA and with Lsm11 and likely plays a critical role in recruiting U7 snRNP to the histone pre-mRNA. It should be noted that there must be other trans-acting factors, including the factor that catalyzes the cleavage reaction. The cleavage occurs in the presence of EDTA as does the cleavage reaction in polyadenylation, it is likely that this reaction is catalyzed by a protein. There may well be additional proteins associated with U7 snRNP, and since under some conditions in vitro processing occurs in the absence of SLBP, it is possible that all of the other factors required for processing are associated with the active form of U7 snRNP.
Poly(A) polymerase has no specificity for any particular RNA sequence, as well as a very low affinity for the RNA. Under physiological conditions, the activity of poly(A) polymerase depends on two auxiliary factors, both of which bind to specific RNA sequences and recruit the poly(A) polymerase by a direct contact. One of these proteins is the heterotetrameric CPSF, which binds the AAUAAA sequence and is also essential for 3' cleavage.
Endonucleolytic cleavage separates the pre-mRNA into an upstream fragment destined to become the mature mRNA and a downstream fragment that is rapidly degraded. Polyadenylation and cleavage occur concurrently, with complexes co-assembling, cleavage depends on two signals in the RNA, a highly conserved hexanucleotide, AAUAAA, 10 to 30 nucleotides upstream of the cleavage site, and a poorly conserved GU- or U-rich downstream element. Additional sequences, often upstream of AAUAAA, can enhance the efficiency of the reaction. Cleavage occurs most often after a CA dinucleotide. A single gene can have more than one 3' processing site. Cleavage is preceded by the assembly of a large processing complex, the composition of which is poorly defined. ATP, but not its hydrolysis, is required for assembly. Cleavage depends on a number of protein factor. CPSF, a heterotetramer, binds specifically to the AAUAAA sequence. The heterotrimer CstF binds the GU- or U-rich downstream element.
GlcNAc1P is dephosphorylated to UDP-N-acetyl-glucosamine
Acetylation of glucosamine 6-phosphate to GlcNAc6P
Molecular cloning and characterization of a new human histamine receptor, HH4R
Formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine
GFPT1,2 transfer an amino group from L-Gln to F6P to form GlcN6P
Mannose-1-phosphate converted to GDP-Mannose
Mannose 6-phosphate isomerizes to Mannose 1-phosphate
Fructose 6-phosphate isomerizes to Mannose 6-phosphate
Transport of mRNA through the Nuclear Pore Complex (NPC) is a dynamic process involving distinct machinery and receptor subsets. The separation of the two compartments and the regulation of this transport provide spatial and temporal control over mRNA expression and ultimately control over translation. It should be noted that mRNA export does not rely on a specific motif in the mRNA molecule, but rather transport appears to be coupled to processing and regulation. The specific proteins that are bound to the mRNA determine when it will be transported to the cytoplasm. This limitation insures that transport overwhelmingly favors transport of fully processed mRNA molecules.
Lysosomal disorders: from storage to cellular damage
Transport of mRNA from the nucleus to the cytoplasm, where it is translated into protein, is highly selective and closely coupled to correct RNA processing. This coupling is achieved by the nuclear pore complex, which recognizes and transports only completed mRNAs.
The 32 kDa stem-loop binding protein (SLBP), also termed hairpin binding protein (HBP) is likely the first protein that binds to the histone pre-mRNA as it is being transcribed.
Co-transcriptional pre-mRNA splicing is not obligatory. Pre-mRNA splicing begins co-transcriptionally and often continues post-transcriptionally. Human genes contain an average of nine introns per gene, which cannot serve as splicing substrates until both 5' and 3' ends of each intron are synthesized. Thus the time that it takes for pol II to synthesize each intron defines a minimal time and distance along the gene in which splicing factors can be recruited. The time that it takes for pol II to reach the end of the gene defines the maximal time in which splicing could occur co-transcriptionally. Thus, the kinetics of transcription can affect the kinetics of splicing.Any covalent change in a primary (nascent) mRNA transcript is mRNA Processing. For successful gene expression, the primary mRNA transcript needs to be converted to a mature mRNA prior to its translation into polypeptide. Eucaryotic mRNAs undergo a series of complex processing reactions; these begin on nascent transcripts as soon as a few ribonucleotides have been synthesized during transcription by RNA Polymerase II, through the export of the mature mRNA to the cytoplasm, and culminate with mRNA turnover in the cytoplasm.
The upstream fragment generated by 3' cleavage of the pre-mRNA receives a poly(A) tail of approximately 250 AMP residues in a reaction depending on the AAUAAA sequence 10 to 30 nucleotides upstream of the 3' end. Polyadenylation is carried out by three proteins: Poly(A) polymerase carries the catalytic activity. The enzyme has no specificity for any particular RNA sequence, and it also has a very low affinity for the RNA. Under physiological conditions, the activity of poly(A) polymerase thus depends on two auxiliary factors, both of which bind to specific RNA sequences and recruit the enzyme by a direct contact. One of these proteins is the heterotetrameric CPSF, which binds the AAUAAA sequence and is also essential for 3' cleavage. The second is the nuclear poly(A) binding protein (PABPN1), which binds the growing poly(A) tails once this has reached a length of about ten nucleotides. Stimulation of poly(A) polymerase by both proteins is synergistic and results in processive elongation of the RNA, i.e. the polymerase adds AMP residues without dissociating from the RNA. The processive reaction is terminated when the tail has reached a length of about 250 nucleotides.
Aly/Ref recruits TAP to the Exon Junction Complex. This makes the mRNP complex ready for export to the cytoplasm.
DHDDS elongates E,E-FPP with (n)IPPP to form pPPP
The 3' ends of eukaryotic mRNAs are generated by posttranscriptional processing of an extended primary transcript. For almost all RNAs, 3'-end processing consists of two steps: (i) the mRNA is first cleaved at a particular phosphodiester bond downstream of the coding sequence, (ii) the upstream fragment then receives a poly(A) tail of approximately 250 adenylate residues, whereas the downstream fragment is degraded. The two partial reactions are coupled so that reaction intermediates are usually undetectable. While 3' processing can be studied as an isolated event in vitro, it appears to be connected to transcription, splicing, and transcription termination in vivo. The only known exception to the rule of cleavage followed by polyadenylation are the major histone mRNAs, which are cleaved but not polyadenylated.
Hydrolytic deamination of adenosine leads to inosine. Ammonia is presumed to be released during this reaction.
In humans the deamination of adenosines to inosines is the most common editing event. It is particularly prevalent in the brain, where it leads to amino acid changes that affect the conductance of several ion channels. Inosines are recognized by the translation machinery as if they were guanosines. ADARs (Adenosine Deaminases Acting on RNA) modify pre-mRNA, acting as single peptides and recognize structural determinants in the RNA. To date 3 members of this deaminase family are known: ADAR 1, ADAR 2, and ADAR 3 that share a common modular domain structure. ADAR 1 and 2 contain a catalytic deaminase domain, a double-stranded RNA binding domain and exhibit RNA editing activity. ADAR1 activity is found in various mammalian tissues with the highest concentration in brain. An increasing number of mammalian genes have been found to undergo deamination by ADARs. Deamination by editing in pre-mRNAs encoding subunits of ionotropic glutamate receptors (GluRs) is another well studied example. An editing event at the Q/R site of the GluR2 (GluRB) subunit of AMPA receptors converts a Gln codon CAG to an Arg codon CIG rendering the heteromeric receptor impermeable to Ca 2+ ions. Another example is the editing of 5-HT2C subtype serotonin receptor mRNA resulting in receptor isoforms with reduced G-protein coupling efficiency (reviewed by Gerber and Keller, 2001). In mice, the editosomes with ADAR proteins require some cis-acting elements like an intronic 'editing-site complementary sequence (ECS)'. Although evolutionarily conserved, the actual role of ECS is not yet elucidated in humans. The editing complex can be generally represented as:
Addition of a third mannose to the N-glycan precursor by ALG2
Addition of a second mannose to the N-glycan precursor by ALG2
Flipping of the N-glycan precursor to inside the ER
Addition of a fourth and fifth mannose to the N-glycan precursor by ALG11
ALG11 transfers the fourth and fifth Man to the N-glycan precursor
Addition of the seventh mannose to the N-glycan precursor by ALG9
Addition of the sixth mannose to the N-glycan precursor by ALG3.
Bile salt transporters: molecular characterization, function, and regulation
At the beginning of this reaction, 1 molecule of 'H2O', and 1 molecule of 'Editosome (ADAR2) complex' are present. At the end of this reaction, 1 molecule of 'NH3', and 1 molecule of 'A to I edited RNA:Editosome (ADAR2) complex' are present. This reaction takes place in the 'nucleus' and is mediated by the 'double-stranded RNA adenosine deaminase activity' of 'ADAR2 homodimer'.
It is still unclear how ADAR 1 and ADAR 2 proteins form the editosomes with the target RNA. Other components of these editosomes for A to I editing are unknown.
At the beginning of this reaction, 1 molecule of 'dsRNA duplex', and 1 molecule of 'ADAR2 homodimer' are present. At the end of this reaction, 1 molecule of 'Editosome (ADAR2) complex' is present. This reaction takes place in the 'nucleus'.
At the beginning of this reaction, 2 molecules of 'ADAR2 protein' is present. At the end of this reaction, 1 molecule of 'ADAR2 homodimer' is present. This reaction takes place in the 'nucleus'.
Co-transcriptional pre-mRNA splicing is not obligatory. Pre-mRNA splicing begins co-transcriptionally and often continues post-transcriptionally. Human genes contain an average of nine introns per gene, which cannot serve as splicing substrates until both 5' and 3' ends of each intron are synthesized. Thus the time that it takes for pol II to synthesize each intron defines a minimal time and distance along the gene in which splicing factors can be recruited. The time that it takes for pol II to reach the end of the gene defines the maximal time in which splicing could occur co-transcriptionally. Thus, the kinetics of transcription can affect the kinetics of splicing. There are two classes of intronless pre-mRNAs (mRNAs expressed from genes that lack introns). The first class encodes the replication dependent histone mRNAs. These mRNAs have unique 3' ends that do not have a polyA tail. The replication dependent histone mRNAs in all metazoans, as well as Chlamydomonas and Volvox fall into this class. The second class of mRNAs end in polyA tails, which are formed by a mechanism similar to that which poly-adenylate pre-mRNAs containing introns. In the intronless genes there is a different method of replacing the 3' splice site that activates polyadenylation.
Addition of N-acetyl-D-glucosamine to Dolichyl phosphate
The 3' ends of eukaryotic mRNAs are generated by posttranscriptional processing of an extended primary transcript. For almost all RNAs, 3' processing consists of two steps: The mRNA is first cleaved at a particular phosphodiester bond downstream of the coding sequence. The upstream fragment then receives a poly(A) tail of approximately 250 adenylate residues whereas the downstream fragment is degraded. The two partial reactions are coupled so that reaction intermediates are usually undetectable. While 3' processing can be studied as an isolated event in vitro, it appears to be connected to transcription, splicing and transcription termination in vivo.
The nuclear poly(A) binding protein (PABPN1), which binds the growing poly(A) tails once it has reached a length of about ten nucleotides. Stimulation of poly(A) polymerase by both CPSF and PABPN1 is synergistic and results in processive elongation of the RNA (the polymerase adds AMP residues without dissociating from the RNA). The processive reaction is terminated when the tail has reached a length of about 250 nucleotides.
Addition of the first mannose to the N-glycan precursor by ALG1
CF I, which appears to be composed of two subunits, one of several related larger polypeptides and a common smaller one, also binds RNA, but with unknown specificity. RNA recognition by these proteins is cooperative. Cleavage also requires CF II, composed of at least two subunits, and poly(A) polymerase, the enzyme synthesizing the poly(A) tail in the second step of the reaction.
Addition of the second N-acetyl-glucosamine to the N-glycan precursor
At the beginning of this reaction, 1 molecule of 'Pol II Initiation complex with phosphodiester-PPi intermediate' is present. At the end of this reaction, 1 molecule of 'pyrophosphate', and 1 molecule of 'pol II transcription complex' are present. This reaction takes place in the 'nucleus'.
The general transcription factor TFIIF has a high affinity for the RNA Polymerase II holoenzyme. TFIIF stabilizes the preinitiation complex, and suppresses non-specific binding of RNA Pol II to DNA, and is thus critical for start site recognition.
Although TBP (TATA box binding factor) is necessary and sufficient for initiation of basal transcription, the other subunits of the general transcription factor TFIID, the TBP-associated factors, are required for response to transcriptional activators. TBP binds to the TATA box (a core promoter element), and bends the DNA 80 degrees toward the major groove. This conformation of TBP-TATA box provides the proper topology for the binding of the general transcription factor TFIIB. Transcriptional activators function by affecting the kinetics of binding of TBP to the promoter DNA.
The binding of TFIIH completes the assembly of the preinitiation complex (PIC) for RNA Polymerase II transcription. Although RNA polymerase binds the TATA box on the promoter DNA, no initiation of transcription occurs until TFIIH is bound to the PIC. TFIIH is the only factor with known enzymatic activities.
Factor TFIIE enters the preinitiation complex after TFIIF recruits RNA Polymerase II. TFIIE is composed of two subunits of 56 kDA and 34 kDa. TFIIE facilitates the recruitment of factor TFIIH to the preinitiation complex, and it also stimulates the phosphorylation of the RNA Polymerase II CTD by TFIIH.
Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells
Purification and characterization of human plasma glutathione peroxidase: a selenoglycoprotein distinct from the known cellular enzyme
After assembly of the complete RNA polymerase II-preinitiation complex, the next step is separation of the two DNA strands. This isomerization step is known as the closed-to-open complex transition and occurs prior to the initiation of mRNA synthesis. In the RNA polymerase II system this step requires the hydrolysis of ATP or dATP into Pi and ADP or dADP (in contrast to the other RNA polymerase systems) and is catalyzed by the XPB subunit of TFIIH. The region of the promoter, which becomes single-stranded , spans from ââ¬â10 to +2 relative to the transcription start site. Negative supercoiling in the promoter region probably induces transient opening events and can alleviate requirement of TFIIE, TFIIH and ATP-hydrolysis for open complex formation. ATP is also used in this step by the cdk7-subunit of TFIIH to phosphorylate the heptad repeats of the C-terminal domain of the largest subunit of RNA polymerase II (RPB1) on serine-2
At the beginning of this reaction, 1 molecule of 'Pol II initiation complex' is present. At the end of this reaction, 1 molecule of 'Pol II Initiation complex with phosphodiester-PPi intermediate' is present. This reaction takes place in the 'nucleus'.
At the beginning of this reaction, 1 molecule of 'pol II open pre-initiation complex', and 2 molecules of 'NTP' are present. At the end of this reaction, 1 molecule of 'Pol II initiation complex' is present. This reaction takes place in the 'nucleus'.
RNA Polymerase II promoter escape occurs after the first phosphodiester bond has been created.
RNA polymerase II transcription complexes are susceptible to transcriptional stalling and arrest, when extending nascent transcripts to 30-nt. This susceptibility depends on presence on down-stream DNA, the particular DNA-sequence of the template and presence of transcription factors. Transcription factor TFIIH remains associated to the RNA pol II elongation complex until position +30. At this stage transcription elongation factor TFIIS can rescue stalled transcription elongation complexes. The transcription bubble varies between 13- and 22-nt in size.
Formation of phosphodiester bonds nine and ten creates RNA products, which do not dissociate from the RNA pol II initiation complex. The transcription complex has enter the productive elongation phase. TFIIH and ATP-hydrolysis are required for efficient promoter escape. The open region (ââ¬Åtranscription bubbleââ¬Â) expands concomitant with the site of RNA-extension. The region upstream from the transcription start site (-9 to -3) collapses to the double-stranded state. TFIIH remains associated to the RNA pol II initiation complex.
Formation of the third phosphodiester bond creates a 4-nt product. This commits the initiation complex to promoter escape. The short 4-nt transcript is still loosely associated with the RNA polymerase II initiation complex and can dissociate to yield abortive products, which are not further extended. Inhibition of ATP-hydrolysis by TFIIH does not lead to collapse of the open region any longer. The transcription complex has lost the sensitivity to single-stranded oligo-nucleotide inhibition. However, ATP-hydrolysis and TFIIH are required for efficient promoter escape. The open region (ââ¬Åtranscription bubbleââ¬Â) expands concomitant with the site of RNA-extension. In this case this region spans positions -9 to +4.
At the beginning of this reaction, 1 molecule of 'mRNA capping enzyme', and 1 molecule of 'Pol II transcription complex with (ser5) phosphorylated CTD containing extruded transcript to +30' are present. At the end of this reaction, 1 molecule of 'RNA Pol II with phosphorylated CTD: CE complex' is present. This reaction takes place in the 'nucleus'.
Phosphorylation of serine 5 residue at the CTD of pol II largest subunit is an important step signaling the end of initiation and escape into processive elongation processes. Cdk7 protein subunit of TFIIH phosphorylates RNA Pol II CTD serine 5 residues on its heptad repeats.
At the beginning of this reaction, 1 molecule of 'Pol II transcription complex containing transcript to +30' is present. At the end of this reaction, 1 molecule of 'Pol II transcription complex containing extruded transcript to +30' is present. This reaction takes place in the 'nucleus'.
Formation of the open complex exposes the template strand to the catalytic center of the RNA polymerase II enzyme. This facilitates formation of the first phosphodiester bond, which marks transcription initiation. As a result of this, the TFIIB basal transcription factor dissociates from the initiation complex. The open transcription initiation complex is unstable and can revert to the closed state. Initiation at this stage requires continued (d)ATP-hydrolysis by TFIIH. Dinucleotide transcripts are not stably associated with the transcription complex. Upon dissociation they form abortive products. The transcription complex is also sensitive to inhibition by small oligo-nucleotides. Dinucleotides complementary to position -1 and +1 in the template can also direct first phosphodiester bond formation. This reaction is independent on the basal transcription factors TFIIE and TFIIH and does not involve open complex formation. This reaction is sensitive to inhibition by single-stranded oligonucleotides.
Formation of the second phosphodiester bond creates a 3-nt product. This short transcript is still loosely associated with the RNA polymerase II initiation complex and can dissociate to yield abortive products, which are not further extended. The transcription complex still requires continued ATP-hydrolysis by TFIIH and remains sensitive to single-stranded oligo-nucleotide inhibition. The open region (ââ¬Åtranscription bubbleââ¬Â) expands concomitant with the site of RNA-extension. In this case this region spans positions -9 to +3.
Protein sorting receptors in the early secretory pathway
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Functional characterization of ORCTL2--an organic cation transporter expressed in the renal proximal tubules
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High-resolution structures of free, catalytically active yeast Pol II and of an elongating form reveal that Pol II elongation complex includes features like: - RNA-DNA hybrid, an unwound template ahead of 3'-OH terminus of growing transcript and an exit groove at the base of the CTD, possibly for dynamic interaction of processing and transcriptional factors. - a cleft or channel created by Rpb1 and Rpb2 subunits to accommodate DNA template, extending to Mg2+ ion located deep in the enzyme core -a 50 kDa "clamp" with open confirmation in free polymerase, allowing entry of DNA strands but closed in the processive elongation phase. The clamp is composed of portions of Rpb1,Rpb2 and Rpb3 , five loops or "switches" that change from unfolded to well-folded structures stabilizing the elongation complex, and a long "bridging helix" that emanates from Rpb1 subunit, crossing near the Mg2+ ion. The bridging helix is thought to "bend" to push on the base pair at the 3'-end of RNA-DNA hybrid like a ratchet, translocating Pol II along the DNA (Cramer et al.,2001; Gnatt et al.,2001).In addition to its dynamic biochemical potential, Pol II possess a repertoire of functions to serve as a critical platform of recruiting and coordinating the actions of a host of additional enzyme and proteins involved in various pathways.
TFIIS is a transcription factor involved in different phases of transcription, occurring in a major ubiquitous form and other tissue specific forms. TFIIS stimulates RNA Pol II complex out of elongation arrest. Other transcription factors like ELL, Elongin family members and TFIIF interact directly with elongating Pol II and increase its elongation rate. These factors have been observed to act on naked DNA templates by suppressing transient pausing by the enzyme at all or most steps of nucleotide addition. In Drosophila, ELL is found at a large number of transcriptionally active sites on polytene chromosomes. In general, ELL is suspected to have more unidentified functions. Elongin is a heterotrimeric protein complex that stimulates the overall rate of elongation. In addition, Elongin may act as an E3 Ubiquitin ligase. Ubiquitylation of RNA Pol II occurs rapidly after genotoxic assault by UV light or chemicals, and results in degradation by proteasome. The FACT complex appears to promote elongation by facilitating passage of polymerase through chromatin. All these factors contribute to the formation of a processive elongation complex centered around the RNA Pol II complex positioned on the DNA:RNA hybrid. This enables the RNA Pol II elongation complex to function as a platform that coordinates mRNA processing and export (Reviewed by Shilatifard et al., 2003).
Translocation after synthesis of a four-nucleotide RNA commits RNA polymerase II to promoter escape.
At the beginning of this reaction, 1 molecule of 'Processive elongation complex', and 1 molecule of 'NTP' are present. At the end of this reaction, 1 molecule of 'Elongation complex prior to separation', and 1 molecule of 'NTP' are present. This reaction takes place in the 'nucleus'.
DSIF is a heterodimer consisting of hSPT4 (human homolog of yeast Spt4- p14) and hSPT5 (human homolog of yeast Spt5-p160). DSIF association with Pol II may be enabled by Spt5 binding to Pol II creating a scaffold for NELF binding (Wada et al.,1998). Spt5 subunit of DSIF can be phosphorylated by P-TEFb.
FCP1 dephosphorylates RNAP II in ternary elongation complexes as well as in solution and, therefore, is thought to function in the recycling of RNAP II during the transcription cycle. Biochemical experiments suggest that human FCP1 targets CTDs that are phosphorylated at serine 2 (CTD-serine 2) and/or CTD-serine 5. It is also observed to stimulate elongation independent of its catalytic activity. Dephosphorylation of Ser2 - phosphorylated Pol II results in hypophosphorylated form that disengages capping enzymes (CE).
Cdk-9 is the kinase subunit of P-TEFb that phosphorylates Serine 2 on the heptapeptide repeats of Pol II CTD alleviating the negative action of DSIF-NELF complex. This reaction is considered to be a rate limiting step for processive elongation. P-TEFb complex, that has a DRB-sensitive cyclin-dependent kinase activity, is composed of ~43 kDa, Cdk9 kinase (PITALRE), and either Cyclin T1, Cyclin T2a, Cyclin T2b, or Cyclin K. The exact mechanism by which P-TEFb removes the inhibition of elongation by DSIF-NELF is not yet known. P-TEFb is also capable of phosphorylating Spt5 subunit of DSIF complex. A P-TEFb complex (which contains only the Cyclin T1) is implicated in the efficient synthesis of human immunodeficiency virus-1 (HIV-1) transcripts. Cyclin T1 subunit of the P-TEFb(Cyclin T1:Cdk9) complex interacts with HIV-1 encoded Tat protein that binds to the transactivation response (TAR) element in the nascent HIV-1 transcript (reviewed in Price,2000). The mechanism by which DSIF, NELF and P-TEFb or TAK/P-TEFb act together in Pol II-regulated elongation is yet to be fully understood. Various biochemical evidences point to a model in which DSIF and NELF negatively regulate elongation through interactions with polymerase containing a hypophosphorylated CTD. Subsequent phosphorylation of the Pol II CTD by P-TEFb might promote elongation by inhibiting interactions of DSIF and NELF with the elongation complex.
Transcription elongation by RNA polymerase II (RNAPII) is controlled by a number of trans-acting transcription elongation factors as well as by cis-acting elements. Transcription elongation is a rate-limiting step for proper mRNA production in which the phosphorylation of Pol II CTD is a crucial biochemical event. The role of CTD phosphorylation in transcription by Pol II is greatly impaired by protein kinase inhibitors such as 5,6-dichloro-1- ribofuranosylbenzimidazole (DRB), which block CTD phosphorylation and induce arrest of elongating Pol II. DRB-sensitive activation Pol II CTD during elongation has enabled the isolation of two sets of factors -Negative Elongation Factors (NELF) and DRB sensitivity inducing factor (DSIF). P-Tefb is a DRB-sensitive, cyclin-dependent CTD kinase composed of Cdk9 that carries out Serine-2 phosphorylation of Pol II CTD during elongation. The mechanism by which DSIF, NELF and P-TEFb act together in Pol II-regulated elongation is yet to be fully understood. Various biochemical evidences point to a model in which DSIF and NELF negatively regulate elongation through interactions with polymerase containing a hypophosphorylated CTD. Subsequent phosphorylation of the Pol II CTD by P-Tefb might promote elongation by inhibiting interactions of DSIF and NELF with the elongation complex.
At the beginning of this reaction, 1 molecule of 'RNA Pol II with phosphorylated CTD: CE complex' is present. At the end of this reaction, 1 molecule of 'RNA Pol II with phosphorylated CTD: CE complex with activated GT' is present. This reaction takes place in the 'nucleus'.
The capping enzyme interacts with the Spt5 subunit of transcription elongation factor DSIF. This interaction may couple the capping reaction with promoter escape or elongation, thereby acting as a ââ¬Åcheckpointââ¬Â to assure that capping has occurred before the polymerase proceeds to make the rest of the transcript.
Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK-3beta and beta-catenin and promotes GSK-3beta-dependent phosphorylation of beta-catenin
To facilitate co-transcriptional capping, and thereby restrict the cap structure to RNAs made by RNA polymerase II, the capping enzymes bind directly to the RNA polymerase II. The C-terminal domain of the largest Pol II subunit contains several phosphorylation sites on its heptapeptide repeats. The capping enzyme guanylyltransferase and the methyltransferase bind specifically to CTD phosphorylated at Serine 5 within the CTD. Kinase subunit of TFIIH, Cdk7, catalyzes this phosphorylation event that occurs near the promoter. In addition, it has been shown that binding of capping enzyme to the Serine-5 phosphorylated CTD stimulates guanylyltransferase activity in vitro.
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A highly conserved lysine within the guanylyltransferase (GT) site of the mRNA capping enzyme attacks the alpha-phosphate of GTP. An enzyme-GMP covalent intermediate is formed.
The spindle checkpoint: structural insights into dynamic signalling
After the capping complex is formed, the RNA triphosphatase activity of the capping enzyme hydrolyzes the 5'-end phosphate group of the nascent mRNA transcript to a diphosphate. The RNA triphosphatase (RTP) domain of mammalian capping enzyme is a member of a superfamily of phosphatases that include the protein tyrosine phosphatases, some lipid phosphatases, and several nucleic acid phosphatases. This family uses a conserved nucleophilic cysteine residue to attack the target phosphate. A transient phospho-cysteinyl enzyme intermediate is then hydrolyzed to regenerate the enzyme active site. It should be noted that while higher eukaryotic capping enzymes use PTP-like triphosphatase domains, the yeast triphosphatases are a completely different class of enzymes. The yeast RTPs are metal-dependent phosphatases. RNA 5'-triphosphatase (RTP) catalyzed first reaction can be represented as:pppN(pN)n + GTP -> ppN(pN)n + Pi; (n=20-25)
The capping enzyme binds the 5'-end of the nascent transcript soon after it is synthesized on the DNA template, and results in the formation of the capping complex along with the C-terminal domain of RNA polymerase II, and Spt5.
The detailed annotation of this section will be completed in the next release.
This section includes the cleavage of both polyadenylated and non-polyadenylated transcripts. In the former case polyadenylation has to precede transcript cleavage, while in the latter case there is no polyadenylation.
Endonucleolytic cleavage separates the pre-mRNA into an upstream fragment destined to become the mature mRNA, and a downstream fragment that is rapidly degraded. Cleavage depends on two signals in the RNA, a highly conserved hexanucleotide, AAUAAA, 10 to 30 nucleotides upstream of the cleavage site, and a poorly conserved GU- or U-rich downstream element. Additional sequences, often upstream of AAUAAA, can enhance the efficiency of the reaction. Cleavage occurs most often after a CA dinucleotide. A single gene can have more than one 3' processing site. Cleavage is preceded by the assembly of a large processing complex, the composition of which is poorly defined. ATP, but not its hydrolysis, is required for assembly. Cleavage at the 3'-end of mRNAs depends on a number of protein factors. CPSF, a heterotetramer, binds specifically to the AAUAAA sequence. The heterotrimer CstF binds the downstream element. CF I, which appears to be composed of two subunits, one of several related larger polypeptides and a common smaller one, also binds RNA, but with unknown specificity. RNA recognition by these proteins is cooperative. Cleavage also requires CF II, composed of at least two subunits, and poly(A) polymerase, the enzyme synthesizing the poly(A) tail in the second step of the reaction. The polypeptide catalyzing the hydrolysis of the phosphodiester bond remains to be identified. Cleavage produces a 3'-OH on the upstream fragment and a 5'-phosphate on the downstream fragment. At some unknown point after cleavage, the downstream RNA fragment, CstF, CF I and CF II are thought to be released, whereas CPSF and poly(A) polymerase remain to carry out polyadenylation.
The polypeptide catalyzing the hydrolysis of the phosphodiester bond remains to be identified. Cleavage produces a 3'-OH on the upstream fragment and a 5'-phosphate on the downstream fragment. At some unknown point after cleavage, the downstream fragment, CstF, CF I and CF II are thought to be released, whereas CPSF and poly(A) polymerase remain to carry out polyadenylation.
At the beginning of this reaction, 1 molecule of 'Elongation complex prior to separation' is present. At the end of this reaction, 1 molecule of 'Elongation complex with separated and uncleaved transcript' is present. This reaction takes place in the 'nucleus'.
The mechanisms governing the process of elongation during eukaryotic mRNA synthesis are being unraveled by recent studies. These studies have led to the expected discovery of a diverse collection of transcription factors that directly regulate the activities of RNA Polymerase II and unexpected discovery of roles for many elongation factors in other basic processes like DNA repair, recombination, etc. The transcription machinery and structural features of the major RNA polymerases are conserved across species. The genes active during elongation fall under different classes like, housekeeping, cell-cycle regulated, development and differentiation specific genes etc. The list of genes involved in elongation has been growing in recent times, and include: -TFIIS,DSIF, NELF, P-Tefb etc. that are involved in drug induced or sequence-dependent arrest - TFIIF, ELL, elongin, elongator etc. that are involved in increasing the catalytic rate of elongation by altering the Km and/or the Vmax of Pol II -FACT, Paf1 and other factors that are involved chromatin modification - DNA repair proteins, RNA processing and export factors, the 19S proteasome and a host of other factors like Spt5-Spt5, Paf1, and NELF complexes, FCP1P etc. (Arndt and Kane, 2003). Elongation also represents processive phase of transcription in which the activities of several mRNA processing factors are coupled to transcription through their binding to RNA polymerase (Pol II). One of the key events that enables this interaction is the differential phosphorylation of Pol II CTD. Phosphorylation pattern of CTD changes during transcription, most significantly at the beginning and during elongation process. TFIIH-dependent Ser5 phosphorylation is observed primarily at promoter regions while P-Tefb mediated Ser2 phosphorylation is seen mainly in the coding regions, during elongation. Experimental evidence suggests a dynamic association of RNA processing factors with differently modified forms of the polymerase during the transcription cycle. (Komarnitsky et al., 2000). [Komarnitsky et al 2000, Arndt & Kane 2003, Shilatifard et al 2003]
Identification, functional expression and chromosomal localisation of a sustained human proton-gated cation channel
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Mutations in the urocanase gene UROC1 are associated with urocanic aciduria
Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB
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FGFR3-related dwarfism and cell signaling
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PDP-catalyzed dephosphorylation (activation) of phospho E1 alpha subunit
Activation of PDC by dephosphorylation of phospho-E1 alpha component
Acetyl-CoA + H2O + Oxaloacetate => Citrate + CoA
Oxidative decarboxylation of pyruvate to acetyl CoA by pyruvate dehydrogenase
pyruvate + CoASH + NAD+ => acetylCoA + CO2 + NADH + H+
PDK-catalyzed phosphorylation (inactivation) of PDC E1 alpha subunit
Inactivation of PDC by phosphorylation of PDC E1 alpha component
(S)-Lactate + NAD+ <=> Pyruvate + NADH + H+
Cytosolic PYR is transported to the mitochondrial matrix by MPC1:MPC2
PYR + H+ (cytosol) => PYR + H+ (mitochondrial matrix)
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Pyruvate + NADH + H+ <=> (S)-Lactate + NAD+
GCHFR binds to GCH1 and negatively regulates its activity
Triple functional domain protein ecNumber2.7.11.1/ecNumber
Oxidative decarboxylation of alpha-ketoglutarate to succinyl CoA by alpha-ketoglutarate dehydrogenase
alpha-ketoglutarate + CoASH + NAD+ => succinyl-CoA + CO2 + NADH + H+
GDP + Orthophosphate + Succinyl-CoA <=> GTP + Succinate + CoA
ADP + Orthophosphate + Succinyl-CoA <=> ATP + Succinate + CoA
Succinate <=> Fumarate (with FAD redox reaction on enzyme)
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isocitrate + NAD+ => alpha-ketoglutarate + CO2 + NADH + H+ [IDH3]
NADPH + NAD+ + H+ [cytosol] => NADP+ + NADH + H+ [mitochondrial matrix]
isocitrate + NADP+ => alpha-ketoglutarate + CO2 + NADPH + H+ [IDH2]
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Primer on genes encoding enzymes in sialic acid metabolism in mammals
Rho guanine nucleotide exchange factor 12
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Vav family proteins are required for optimal regulation of PLCgamma2 by integrin alphaIIbbeta3
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GEFs and GAPs: critical elements in the control of small G proteins
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Chibby, a nuclear beta-catenin-associated antagonist of the Wnt/Wingless pathway
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Characterization of human PLD2 and the analysis of PLD isoform splice variants
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T cell receptor (TCR) interacting molecule (TRIM), a novel disulfide-linked dimer associated with the TCR-CD3-zeta complex, recruits intracellular signaling proteins to the plasma membrane
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Expression, processing, and glycosaminoglycan binding activity of the recombinant human 315-kDa hyaluronic acid receptor for endocytosis (HARE)
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Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1)
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At the beginning of this reaction, 1 molecule of 'hNTH1', and 1 molecule of 'Double-strand DNA containing a cytosine glycol' are present. At the end of this reaction, 1 molecule of 'hNTH1 glycosylase:cytosine glycol complex' is present. This reaction takes place in the 'nucleus'.
Protein metabolism comprises the pathways of translation, post-translational modification and protein folding.
The Unfolded Protein Response (UPR) is a regulatory system that protects the Endoplasmic Reticulum (ER) from overload. The UPR is provoked by the accumulation of improperly folded protein in the ER during times of unusually high secretion activity. Analysis of mutants with altered UPR, however, shows that the UPR is also required for normal development and function of secretory cells. One level at which the URP operates is transcriptional and translational regulation: mobilization of ATF6 and IRE1 leads to increased transcription of genes encoding chaperones, and mobilization of PERK (pancreatic eIF2alpha kinase, EIF2AK3) leads to phosphorylation of the translation initiation factor eIF2alpha and global down-regulation of protein synthesis. These three regulatory pathways are annotated here.
PERK (EIF2AK3) is a single-pass transmembrane protein located in the endoplasmic reticulum (ER) membrane such that the N-terminus of PERK is luminal and the C-terminus is cytosolic. PERK is maintained in an inactive form by interaction of its luminal domain with BiP, an ER chaperone. BiP also binds unfolded proteins and so BiP dissociates from PERK when unfolded proteins accumulate in the ER. Dissociated PERK monomers spontaneously form homodimers and the homodimeric form of PERK possesses kinase activity in its cytosolic C-terminal domain. The kinase specifically phosphorylates the translation factor eIF2alpha at Ser52, resulting in an arrest of translation. Thus translation of proteins targeted to the ER is downregulated. The translation arrest also causes depletion of Cyclin D1, a rapidly turned over protein. The depletion of Cyclin D1 in turn causes arrest of the cell cycle in G1 phase.
ATF4 is a transcription factor and activates expression of IL-8, MCP1, IGFBP-1, CHOP, HERP1 and ATF3.
The HERPUD gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The Aspariagine Synthetase (ASNS) gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
At the beginning of this reaction, 1 molecule of 'hNTH1', and 1 molecule of 'Double-strand DNA containing a thymine glycol ' are present. At the end of this reaction, 1 molecule of 'hNTH1 glycosylase:thymine glycol' is present. This reaction takes place in the 'nucleus'.
At the beginning of this reaction, 1 molecule of 'hNTH1', and 1 molecule of 'Double-strand DNA containing a dihydrouracil' are present. At the end of this reaction, 1 molecule of 'hNTH1 glycosylase:dihydrouracil complex' is present. This reaction takes place in the 'nucleus'.
At the beginning of this reaction, 1 molecule of 'hNTH1', and 1 molecule of 'Double-strand DNA containing a formamidopyrimidine ' are present. At the end of this reaction, 1 molecule of 'hNTH1 glycosylase: foramidopyrimidine complex' is present. This reaction takes place in the 'nucleus'.
Mitogen-activated protein kinase kinase 1-dependent Golgi unlinking occurs in G2 phase and promotes the G2/M cell cycle transition
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RNA Polymerase II Pre-transcription Events
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The Talin-1 (TLN1) gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The TSPYL2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The YIF1A gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The WIPI1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The TATDN2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The Sec31A gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The ZBTB17 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The p58IPK (DNAJC3) gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Xbp-1 (S) binds the sequence CCACG in ER Stress Responsive Elements (ERSE, consensus sequence CCAAT (N)9 CCACG) located upstream from many genes. The ubiquitous transcription factor NF-Y, a heterotrimer, binds the CCAAT portion of the ERSE and together the IRE1-alpha: NF-Y complex activates transcription of a set of chaperone genes including DNAJB9, EDEM, RAMP4, p58IPK, and others. This results in an increase in protein folding activity in the ER.
IRE1-alpha is a single-pass transmembrane protein that resides in the endoplasmic reticulum (ER) membrane. The C-terminus of IRE1-alpha is located in the cytosol; the N-terminus is located in the ER lumen. In unstressed cells IRE1-alpha exists in an inactive heterodimeric complex with BiP such that BiP in the ER lumen binds the N-terminal region of IRE1-alpha. Upon accumulation of unfolded proteins in the ER, BiP binds the unfolded protein and the IRE1-alpha:BiP complex dissociates. The dissociated IRE1-alpha then forms homodimers. Initially the luminal N-terminal regions pair. This is followed by trans-autophosphorylation of IRE1-alpha at Ser724 in the cytosolic C-terminal region. The phosphorylation causes a conformational change that allows the dimer to bind ADP, causing a further conformational change to yield back-to-back pairing of the cytosolic C-terminal regions of IRE1-alpha. The fully paired IRE1-alpha homodimer has endoribonuclease activity and cleaves the mRNA encoding Xbp-1. A 26 residue polyribonucleotide is released and the 5' and 3' fragments of the original Xbp-1 mRNA are rejoined. The spliced Xbp-1 message encodes Xbp-1 (S), a potent activator of transcription. Xbp-1 (S) together with the ubiquitous transcription factor NF-Y bind the ER Stress Responsive Element (ERSE) in a number of genes encoding chaperones. Recent data suggest that the IRE1-alpha homodimer can also cleave specific subsets of mRNAs, including the insulin (INS) mRNA in pancreatic beta cells.
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The PDIA5 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The SHC1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The RAMP4 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The PPP2R5B gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The PDIA6 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The SSR1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The SYVN1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The SRPR gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The SRPRB gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The Sec12 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
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The EXTL3 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The EDEM gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The GFPT1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The GAP gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The GOSR2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The GSK3A gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The HDGF gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The HYOU1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The KDELR3 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The KLHDC3 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
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Beta-oxidation of long-chain fatty acids by human fibroblasts: evidence for a novel long-chain acyl-coenzyme A dehydrogenase.
GMP + NADPH + H+ => IMP + NADP+ + NH4+ [GMPR,GMPR2]
N-glycans are further modified after the commitment to Complex or Hybrid N-glycans. The exact structure of the network of metabolic reactions involved is complex and not yet validated experimentally. Here we will show a generic reaction for each of the genes known to be involved in N-Glycosylation. For a better annotation of the reactions and genes involved in the synthesis of Complex and Hybrid N-glycans we recommend the GlycoGene Database (Ito H. et al, 2010) (http://riodb.ibase.aist.go.jp/rcmg/ggdb/textsearch.jsp) for annotations of genes, and the Consortium for Functional Genomics (http://riodb.ibase.aist.go.jp/rcmg/ggdb/textsearch.jsp) for annotation of Glycan structures and reactions. Moreover, a computationally inferred prediction for the structure of this network is available through the software GlycoVis (Hossler P. et. al. 2006).
(d)GMP or (d)IMP + H2O => (2'-deoxy)guanosine or (2'-deoxy)inosine + orthophosphate [NT5C2]
In the latter compartments of the distal Golgi the N-Glycan is further modified, leading to the wide range of N-Glycans observed in multicellular organisms. The first step of N-Glycan elongation in the Golgi is the addition of a GlcNAc residue on the alpha 1,3 branch by the enzyme MGAT1 (GlcNAc-TI), which commits the elongation pathway to Complex or Hybrid N-Glycans from Oligomannose N-Glycans. At this point, the pathway bifurcates again to generate Complex or Hybrid N-Glycans. The addition of a GlcNAc in the middle of the two arms of the N-Glycan, catalyzed by MGAT3 (GNT-III), inhibits the removal of the mannoses on the alpha1,3 branches by MAN2 and the addition of a GlcNAc by MGAT2 (GlcNAc-TII), and commits the pathway toward the synthesis of hybrid N-Glycans. Alternatively, the removal of these mannoses and the action of MGAT2 leads to the synthesis of complex N-Glycans (Kornfeld and Kornfeld 1985). The exact structure of the network of reactions leading to Complex or Hybrid N-Glycans is still not completely described and validated experimentally. Here we will annotate only one generic reaction for each of the enzymes known to participate in this process. For a better annotation on the reactions and genes involved in the synthesis of Complex and Hybrid N-Glycans we recommend the GlycoGene Database (Ito H. et al, 2010) (http://riodb.ibase.aist.go.jp/rcmg/ggdb/textsearch.jsp) for annotations on genes, and the Consortium for Functional Genomics (http://riodb.ibase.aist.go.jp/rcmg/ggdb/textsearch.jsp) for annotation of Glycan structures and reactions. Moreover, a computationally inferred prediction on the structure of this network is available through the software GlycoVis (Hossler P. et. al. 2006).
Structure and biological activity of basement membrane proteins
At least two mechanisms of transport of proteins from the ER to the Golgi have been described. One is a general flow requiring no export signals (Wieland et al, 1987; Marti­nez-Menarguez et al, 1999). The other is mediated by LMAN1/MCFD2, mannose-binding lectins that recognize a glycan signal (Zhang B et al, 2003).
guanine or hypoxanthine + PRPP => GMP or IMP + PPi [HPRT1]
N-linked glycosylation is the most important form of post-translational modification for proteins synthesized and folded in the Endoplasmic Reticulum (Stanley et al. 2009). An early study in 1999 revealed that about 50% of the proteins in the Swiss-Prot database at the time were N-glycosylated (Apweiler et al. 1999). It is now established that the majority of the proteins in the secretory pathway require glycosylation in order to achieve proper folding. The addition of an N-glycan to a protein can have several roles (Shental-Bechor & Levy 2009). First, glycans enhance the solubility and stability of the proteins in the ER, the golgi and on the outside of the cell membrane, where the composition of the medium is strongly hydrophilic and where proteins, that are mostly hydrophobic, have difficulty folding properly. Second, N-glycans are used as signal molecules during the folding and transport process of the protein: they have the role of labels to determine when a protein must interact with a chaperon, be transported to the golgi, or targeted for degradation in case of major folding defects. Third, and most importantly, N-glycans on completely folded proteins are involved in a wide range of processes: they help determine the specificity of membrane receptors in innate immunity or in cell-to-cell interactions, they can change the properties of hormones and secreted proteins, or of the proteins in the vesicular system inside the cell. All N-linked glycans are derived from a common 14-sugar oligosaccharide synthesized in the ER, which is attached co-translationally to a protein while this is being translated inside the reticulum. The process of the synthesis of this glycan, known as Synthesis of the N-glycan precursor or LLO, constitutes one of the most conserved pathways in eukaryotes, and has been also observed in some eubacteria. The attachment usually happens on an asparagine residue within the consensus sequence asparagine-X-threonine by an complex called oligosaccharyl transferase (OST). After being attached to an unfolded protein, the glycan is used as a label molecule in the folding process (also known as Calnexin/Calreticulin cycle) (Lederkremer 2009). The majority of the glycoproteins in the ER require at least one glycosylated residue in order to achieve proper folding, even if it has been shown that a smaller portion of the proteins in the ER can be folded without this modification. Once the glycoprotein has achieved proper folding, it is transported via the cis-Golgi through all the Golgi compartments, where the glycan is further modified according to the properties of the glycoprotein. This process involves relatively few enzymes but due to its combinatorial nature, can lead to several millions of different possible modifications. The exact topography of this network of reactions has not been established yet, representing one of the major challenges after the sequencing of the human genome (Hossler et al. 2006). Since N-glycosylation is involved in an great number of different processes, from cell-cell interaction to folding control, mutations in one of the genes involved in glycan assembly and/or modification can lead to severe development problems (often affecting the central nervous system). All the diseases in genes involved in glycosylation are collectively known as Congenital Disorders of Glycosylation (CDG) (Sparks et al. 2003), and classified as CDG type I for the genes in the LLO synthesis pathway, and CDG type II for the others.
Hypoxanthine + H2O + O2 => Xanthine + H2O2
If MAN2 acts before MGAT3, the pathway progresses to complex N-glycans, because MAN2 is not able to operate on bisected oligosaccharides (11421343, page 5). The expression of MAN2 over MGAT3 in a tissue can regulate the synthesis of hybrid or complex N-glycans.
(deoxy)guanosine + orthophosphate <=> guanine + (deoxy)ribose 1-phosphate [NP]
N-acetylglucosaminyltransferase (GnT)-V catalyzes the addition of GlcNAc beta 1,4 on the GlcNAc beta1,2 Man,alpha1,6 arm of complex type N-Glycans (Park C et al, 1999; Granowski M et al, 2000; Wang L et al, 2007). The activity of MGAT5 competes with MGAT3 (Pinho SS et al, 2009) and is associated with gastric cancer (Tian H et al, 2008) and multiple sclerosis (Brynedal B et al, 2010).
Rho guanine nucleotide exchange factor 1
(deoxy)inosine + orthophosphate <=> hypoxanthine + (deoxy)ribose 1-phosphate [NP]
Addition of a galactose residue on N-acetylglucosamine. The family of beta 4-galactosyltransferases is composed by at least six known members with different K(m) and acceptor specifities (Guo S et al, 2001) and probably originated by duplication (Lo NW et al, 1998). B4GALT1 is associated with Congenital Disorder of Glycosylation of type IId (Hansske B et al, 2002), and is expressed as two splicing isoforms of which only one is localizated in the Golgi system (Lopez LC et al, 1991; Schaub BE et al, 2006). B4GALT2 is key in the regulation of proteins involved in neuronal development (Sasaki N et al, 2005).
The O-fucosylation of proteins containing thrombospondin type 1 repeat (TSR1) domains is carried out by protein fucosyltransferase 2 (POFUT2). Only POFUT2 recognises the consensus sequence CSXS/TCG found in TSR1 domains and the fucosyl residue is attached to the hydroxyl group of conserved serine (S) or threonine (T) residues within the consensus sequence (Chen et al. 2012). The modification was first demonstrated on thrombospondin 1 (THBS1, TSP1), found in platelets and the ECM (Hofsteenge et al. 2001, Luo et al. 2006). In humans, there are more than 60 of these TSR1 domain-containing proteins. Only the proteins with similarity to experimentally confirmed ones are listed as candidates.
Sato et al. identified the human beta-1,3-glucosyltransferase-like protein (B3GALTL), localised on the ER membrane, which glucosylates O-fucosylated proteins (Sato et al. 2006). The resultant glc-beta-1,3-fuc disaccharide modification on TSR1 domain-containing proteins is thought assist in the secretion of many of these proteins from the ER lumen.
The O-fucosylation of proteins containing thrombospondin type 1 repeat (TSR) domains is an important PTM, regulating many biological processes such as Notch signalling, inflammation, wound healing, angiogenesis amd neoplasia (Adams & Tucker 2000, Moremen et al. 2012). Fucose addition is carried out by two protein fucosyltransferases, POFUT1 and 2. Only POFUT2 recognises the consensus sequence CSXS/TCG found in TSR1 domains and the fucosyl residue is attached to the hydroxyl group of conserved serine (S) or threonine (T) residues within the consensus sequence. The modification was first demonstrated on thrombospondin 1, found in platelets and the ECM (Hofsteenge et al. 2001, Luo et al. 2006). The resulting O-fucosyl-protein is subsequently a substrate for beta-1,3-glucosyltransferase-like protein (B3GALTL), which adds a glucosyl moiety to form the rare disaccharide modification Glc-beta-1,3-Fuc. More than 60 human proteins contain TSR1 domains, The disaccharide modification has been demonstrated on a small number of these TSR1 domain-containing proteins such as thrombospondin 1 (Hofsteenge et al. 2001, Luo et al. 2006), properdin (Gonzalez de Peredo et al. 2002) and F-spondin (Gonzalez de Peredo et al. 2002). The ADAMTS (a disintegrin-like and metalloprotease domain with thrombospondin type-1 repeats) superfamily consists of 19 secreted metalloproteases (ADAMTS proteases) and at lease five ADAMTS-like proteins in humans. Five members of the ADAMTS superfamily have also had experimental confirmation of the disaccharide modification. Examples are ADAMTS13 (Ricketts et al. 2007) and ADAMTSL1 (Wang et al. 2007). In the two reactions described here, the TSR1 domain-containing proteins with similarity to the experimentally confirmed ones are included as putative substrates.
L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate
bicarbonate and glutamine combine to form carbamoyl phosphate
In the cis-Golgi, Man7, Man8 or Man9 N-glycans are progressively trimmed to Man5 N-glycans. The reaction can be catalyzed by one of three known mannosidases, expressed in different tissues and with slightly different affinity. These enzymes trim the mannoses in a different order (Tremblay and Herscovics, 2000), but produce the same output with 5 mannoses. A small confusion on the nomenclature of these genes coding for these enzymes is present in the literature: the standard HGNC symbols are MAN1A1, MAN1A2, MAN1C1, but MAN1A2 is also referred to as MAN1B in certain publications, while MAN1B1 is the enzyme acting in the ERQC compartment on unfolded glycoproteins. Moreover, the names do not correspond to a preference of these enzymes for which of the three mannose branches these trim first.
inosine 5'-monophosphate (IMP) + NAD+ + H2O => xanthosine 5'-monophosphate (XMP) + NADH + H+
IMP + H2O + NAD+ => XMP + NADH + H+ [IMPDH1,2]
This is the first committed step in the synthesis of complex and hybrid N-glycans and is specific to multicellular organisms (Kumar et al, 1990; Hull et al, 1991). Hybri N-glycans are important for inter-cellular interactions and therefore during embryonic development of multicellular organisms, and it is probable that these pathways have evolved just before the emergence of multicellular organisms. Support for this hypothesis is provided by the phenomena of CDG and by the effects of null mutations in C.elegans.
xanthosine 5'-monophosphate (XMP) + L-glutamine + ATP + H2O => guanosine 5'-monophosphate (GMP) + L-glutamate + adenosine 5'-monophosphate (AMP) + pyrophosphate
XMP + L-Glutamine + ATP + H2O => GMP + L-Glutamate + AMP + pyrophosphate
inosine 5'-monophosphate + L-aspartate + GTP => adenylosuccinate + guanosine 5'-diphosphate + orthophosphate
IMP + L-Aspartate + GTP => Adenylosuccinate + GDP + Pi [ADSS]
adenylosuccinate => adenosine 5'-monophosphate + fumarate
The LMAN1(also known as ERGIC-53)/MCFD2 complex recognizes Man8 and Man9 N-glycans released by the Calnexin/Calreticulin cycle and mediate their transport to the Golgi (Nyefeler B et al, 2003; Zhang B et al, 2003). Man8 glycan transfer is shown here.
(2'-deoxy)adenosine + H2O => (2'-deoxy)inosine + NH3 [ADA]
(2'-deoxy)adenosine + ATP => (d)AMP + ADP [ADK]
The addition of a GlcNAc on the alpha,1,6 mannose on the alpha,1,4 branch is required for the synthesis of complex N-glycans (Tan et al. 1995). Defects in this gene are associated with Congenital Disorder of Glycosylation type IIa (Tan et al. 1996, Wang et al. 2002).
Addition of a fucose moiety as an alpha 1-6 linkage to the first GlcNAc residue of the N-glycan (Clarke JL, Watkins WM 1999; Yamaguchi Y et al, 1999; Yamaguchi Y et al 2000).
After the transport of the glycoprotein to the cis-Golgi, the pathway of N-glycosylation bifurcates. Some N-glycans can be moved to subsequent steps of the secretory pathway without further modifications, or alternatively, with the removal of a few mannoses (Oligo Mannoses pathway). In yeast and other unicellular species, a series of mannose residues are added (High Mannoses pathway). The presence of this modification is a major obstacle to the production of pharmaceutical drugs in yeast, where the HighMannose pathway must be inhibited or modified in order to avoid the presence of high mannose xenoglycans. The first N-glycan modification step is the trimming of up to four mannoses by one of three mannosidase enzymes. Moreover, Glycoproteins that have not entered in the Calnexin/Calreticulin cycle or that have not had their glucose residues trimmed earlier in the ER, can enter the main pathway here due to the existence to an alternative route catalyzed by the enzyme Endomannosidase I (Schachter, 2000; Stanley et al, 2009)
The removal of mannoses on the alpha,1,6 arm by MAN2A1 or MAN2A2 is required for efficient formation of complex-type N-glycans (Misago M et al, 1995; Crispin M et al, 2007). These two enzymes carry out the same function and the disruption of both inhibits the formation of complex N-glycans in vivo (Akama TO et al, 2006).
FYVE, RhoGEF and PH domain-containing protein 4
guanine + (deoxy)ribose 1-phosphate <=> (deoxy)guanosine + orthophosphate [NP]
Deamination of N6-methyl-AMP to form IMP
N6-methyl-AMP + H2O => IMP + methylamine
FYVE, RhoGEF and PH domain-containing protein 2
hypoxanthine + (deoxy)ribose 1-phosphate <=> (deoxy)inosine + orthophosphate [NP]
FYVE, RhoGEF and PH domain-containing protein 3
5'-phosphoribosylformylglycinamidine (FGAM) + ATP => 5'-phosphoribosyl-5-aminoimidazole (AIR) + ADP + orthophosphate
5'-phosphoribosyl-5-aminoimidazole (AIR) + CO2 <=> 5'-phosphoribosyl-5-aminoimidazole-4-carboxylate (CAIR)
5-phosphoribosylglycinamide (GAR) + 10-formyl-tetrahydrofolate => 5'-phosphoribosylformylglycinamide (FGAR) + tetrahydrofolate
5'-phosphoribosylformylglycinamide (FGAR) + L-glutamine + ATP + H2O => 5'-phosphoribosylformylglycinamidine (FGAM) + L-glutamate + adenosine 5'-diphosphate + orthophosphate
FGAR + L-Glutamine + ATP + H2O => FGAM + L-Glutamate + ADP + Pi
5-phospho-alpha-D-ribose 1-diphosphate (PRPP) + H2O + L-glutamine <=> 5-phosphoribosylamine + L-glutamate +pyrophosphate
PRPP + H2O + L-Glutamine => 5-Phosphoribosylamine + L-Glutamate + PPi
5-phosphoribosylamine + glycine + ATP => 5-phosphoribosylglycinamide (GAR) + ADP + orthophosphate
5-Phosphoribosylamine + Glycine + ATP => GAR + ADP + Pi
(IscS-IscU)2 complex structures provide insights into Fe2S2 biogenesis and transfer
5'-phosphoribosyl-5-formaminoimidazole-4-carboxamide (FAICAR) <=> inosine 5'-monophosphate + H2O
5'-phosphoribosyl-5-aminoimidazole-4-carboxamide (AICAR) + 10-formyltetrahydrofolate => 5'-phosphoribosyl-5-formaminoimidazole-4-carboxamide (FAICAR) + tetrahydrofolate
5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide (SAICAR) <=> 5'-phosphoribosyl-5-aminoimidazole-4-carboxamide (AICAR) + fumarate
5'-phosphoribosyl-5-aminoimidazole-4-carboxylate (CAIR) + L-aspartate + ATP => 5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide (SAICAR) + ADP + orthophosphate
CAIR + Aspartate + ATP => SAICAR + ADP + Pi
(S)-2-hydroxyglutarate + FAD => 2-oxoglutarate + FADH2
(R)-2-hydroxyglutarate + FAD => 2-oxoglutarate + FADH2
(R)-2-hydroxyglutarate + succinate semialdehyde <=> 2-oxoglutarate + 4-hydroxybutyrate
2-oxoglutarate + 4-hydroxybutyrate <=> (R)-2-hydroxyglutarate + succinate semialdehyde
(S)-Malate + NAD+ <=> Oxaloacetate + NADH + H+
Molecular cloning, sequencing and expression of cDNA encoding human trehalase
Dissociation of phosphoribosyl pyrophosphate amidotransferase tetramer
Reducing equivalents from beta-oxidation of fatty acids transfer to ETF
High affinity nerve growth factor receptor
Transfer of electrons through the succinate dehydrogenase complex
Formation of phosphoribosyl pyrophosphate amidotransferase tetramer
Transfer of electrons from ETF to ubiquinone by ETF-QO
amination of uridine 5'-triphosphate (UTP) to form cytidine 5'-triphosphate (CTP)
UTP + glutamine + ATP + H2O => CTP + glutamate + ADP + orthophosphate [CTPS]
dUDP or TDP + ADP <=> dUMP or TMP + ATP [DTYMK]
dUMP or TMP + ATP <=> dUDP or TDP + ADP [DTYMK]
phosphorylation of dUMP or TMP to dUDP or TDP
(d)CDP or UDP + ADP <=> (d)CMP or UMP + ATP [CMPK1]
Reduction of nuclear ribonucleoside 5'-diphosphates to deoxyribonucleoside 5'-diphosphates (thioredoxin)
NDP + reduced thioredoxin => dNDP + oxidized thioredoxin + H2O
The DDX11 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Carbonic anhydrase inhibitors. DNA cloning, characterization, and inhibition studies of the human secretory isoform VI, a new target for sulfonamide and sulfamate inhibitors
Reduction of cytosolic ribonucleoside 5'-diphosphates to deoxyribonucleoside 5'-diphosphates (thioredoxin)
The DCTN1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Reduction of cytosolic ribonucleoside 5'-diphosphates to deoxyribonucleoside 5'-diphosphates (glutaredoxin)
NDP + reduced glutaredoxin => dNDP + oxidized glutaredoxin + H2O
UTP + glutamine + ATP + H2O => CTP + glutamate + ADP + orthophosphate [CTPS2]
The DNAJB11 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The CTDSP2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The ATP6VOD1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
glutathione (oxidized) + NADPH + H+ => 2 glutathione (reduced) + NADP+
The Cullin-7 (CUL7) gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
glutaredoxin (oxidized) + glutathione (reduced) => glutaredoxin (reduced) + glutathione (oxidized)
The CXXC1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Phosphorylation of the C-terminal region causes a loop in the C-terminus to change position, enabling access to an ADP-binding pocket. Phosphorylated IRE1-alpha dimers bind ADP in preference to ATP.
The ACADVL gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The ADD1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
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conversion of 5,6-Dihydrothymine to 3-Ureidoisobutyrate
5,6-dihydrothymine + H2O => beta-ureidoisobutyrate
(R)-3-aminoisobutyric acid + pyruvate => 2-methyl-3-oxopropanoate + alanine
beta-ureidoisobutyrate + H2O => 3-aminoisobutyrate + NH4+ + CO2
conversion of 3-Ureidoiosbutyrate to 3-Aminoisobutyrate
Dimerization of the N-terminal luminal regions of IRE1-alpha brings the cytosolic C-terminal regions in proximity. The C-terminal region possesses kinase activity and the homodimer trans-autophosphorylates. From homology with Saccharomyces IRE1-alpha the phosphorylation of human IRE1-alpha is believed to be at Ser724.
The dissociation of the IRE1-alpha:BiP heterodimer liberates IRE1-alpha, which forms homodimers. Dimer formation is initiated by interaction between the N-terminal, luminal domains.
ATF6-alpha is a transmembrane protein that normally resides in the Endoplasmic Reticulum (ER) membrane. Here its luminal C-terminal domain is associated with BiP, shielding 2 Golgi-targeting regions and thus keeping ATF6-alpha in the ER. Upon interaction of BiP with unfolded proteins in the ER, ATF6-alpha dissociates and transits to the Golgi where it is cleaved by the S1P and S2P proteases that reside in the Golgi, releasing the N-terminal domain of ATF6-alpha into the cytosol. After transiting to the nucleus, the N-terminal domain acts as a transcription factor to activate genes encoding chaperones.
The N-terminal fragment of ATF6-alpha contains a bZIP domain and binds the sequence CCACG in ER Stress Response Elements (ERSEs). ATF6-alpha binds ERSEs together with the heterotrimeric transcription factor NF-Y, which binds the sequence CCAAT in the ERSEs, and together the two factors activate transcription of ER stress-responsive genes. Evidence from overexpression and knockdowns indicates that ATF6-alpha is a potent activator but its homolog ATF6-beta is not and ATF6-beta may actually reduce expression of ER stress proteins.
The XBP1 gene is transcribed to yield mRNA, the mRNA is spliced to yield Xbp(s) mRNA, and the mRNA is translated to yield protein.
The Endoplasmin (HSP90B1) gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The Calreticulin gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
(d)CMP or UMP + ATP <=> (d)CDP or UDP + ADP [CMPK1]
The BIP (HSPA5) gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The generation of insulin-containing secretory granules from proinsulin in the lumen of the endoplasmic reticulum (ER) can be described in 4 steps: formation of intramolecular disulfide bonds, formation of proinsulin-zinc-calcium complexes, proteolytic cleavage of proinsulin to yield insulin, translocation of the granules across the cytosol to the plasma membrane. Transcription of the human insulin gene INS is activated by 4 important transcription factors: Pdx-1, MafA, Beta2/NeuroD1, and E47. The transcription factors interact with each other at the promoters of the insulin gene and act synergistically to promote transcription. Expression of the transcription factors is upregulated in response to glucose. The preproinsulin mRNA is translated by ribosomes at the rough endoplasmic reticulum (ER) and the preproinsulin enters the secretion pathway by virtue of its signal peptide, which is cleaved during translation to yield proinsulin. Evidence indicates that the preproinsulin mRNA is stabilized by glucose. In the process annotated in detail here, within the ER, three intramolecular disulfide bonds form between cysteine residues in the proinsulin. Formation of the bonds is the spontaneous result of the conformation of proinsulin and the oxidizing environment of the ER, which is maintained by Ero1-like alpha The cystine bonded proinsulin then moves via vesicles from the ER to the Golgi Complex. High concentrations of zinc are maintained in the Golgi by zinc transporters ZnT5, ZnT6, and ZnT7 and the proinsulin forms complexes with zinc and calcium. Proinsulin-zinc-calcium complexes bud in vesicles from the trans-Golgi to form immature secretory vesicles (secretory granules) in the cytosol. Within the immature granules the endoproteases Prohormone Convertase 1/3 and Prohormone Convertase 2 cleave at two sites of the proinsulin and Carboxypeptidase E removes a further 4 amino acid residues to yield the cystine-bonded A and B chains of mature insulin and the C peptide, which will also be secreted with the insulin. The insulin-zinc-calcium complexes form insoluble crystals within the granule The insulin-containing secretory granules are then translocated across the cytosol to the inner surface of the plasma membrane. Translocation occurs initially by attachment of the granules to Kinesin-1, which motors along microtubules, and then by attachment to Myosin Va, which motors along the microfilaments of the cortical actin network. A pancreatic beta cell contains about 10000 insulin granules of which about 1000 are docked at the plasma membrane and 50 are readily releasable in immediate response to stimulation by glucose or other secretogogues. Docking is due to interaction between the Exocyst proteins EXOC3 on the granule membrane and EXOC4 on the plasma membrane. Exocytosis is accomplished by interaction between SNARE-type proteins Syntaxin 1A and Syntaxin 4 on the plasma membrane and Synaptobrevin-2/VAMP2 on the granule membrane. Exocytosis is a calcium-dependent process due to interaction of the calcium-binding membrane protein Synaptotagmin V/IX with the SNARE-type proteins.
Peptide hormones are cleaved from larger precursors in the secretory system (endoplasmic reticulum, Golgi apparatus, secretory granules) of the cell. After secretion peptide hormones are modified and degraded by extracellular proteases.
Rap guanine nucleotide exchange factor 1
thymidine + ATP => TMP (deoxythymidine 5'-monophosphate) + ADP [TK1]
phosphorylation of 2'-Deoxythymidine to dTMP
cytidine or uridine + ATP => CMP or UMP + ADP [UCK2]
A beta cell contains about 10 000 secretory granules. Of these, about 1000 are docked at the inner surface of the plasma membrane and a subset of about 100 docked granules form the "readily releasable" pool (granules which are released within about 5 minutes of glucose stimulation). As inferred from rat MIN6 cells, docking occurs by interaction between EXOC3/Sec6 located on the membrane of the secretory granule and EXOC4/Sec8 located at the plasma membrane (Tsuboi et al. 2005). Additional components (EXOC1, EXOC2, EXOC5, EXOC6, EXOC7, EXOC8) form the Exocyst Complex. EXOC7 binds the plasma membrane (Matern et al. 2001).
thymine + NADPH + H+ => 5,6-dihydrothymine + NADP+
reduction of thymine to form 5,6-Dihydrothymine
As inferred from the yeast TIM23 complex, the human TIMM23 complex resides in the inner membrane of the mitochondrion and transfers precursor proteins to the inner membrane. The TIMM23 complex appears to adopt different configurations (and perhaps different subunit compositions) depending on whether the substrate is destined for the inner membrane or the matrix. Here we refer to the TIMM23 SORT complex as the configuration that delivers inner membrane proteins. The TIMM21 subunit is required for this activity. In yeast, the N-terminal presequences of precursors first interact with TIM50 and TIM23 (TIMM50 and TIMM23 in human). The TIM17 and TIM23 subunits (TIMM17 and TIMM23 in human) form a channel and are required to initiate translocation of precursors. In yeast experimentally verified substrates of the TIM23 SORT complex targeted to the inner membrane include CYB2, DLD (LDHD in human), ATP9 (ATP5G1 in human), COQ2, TIM54 (TIMM54 in human), COX4, COX5A, and ATP2 (ATP5B in human). Many other inner membrane proteins are believed to be substrates of the TIMM23 complex.
beta-alanine + pyruvate => 3-oxopropanoate + alanine
As inferred from the yeast SAM50 complex, the human SAMM50 Complex (SAM50 complex, TOB55 complex) inserts mainly beta-barrel proteins into the outer membrane after they have passed from the cytosol, through the TOMM40:TOMM70 complex, and into the intermembrane space. In yeast, experimentally verified substrates of the SAM50 complex include TOM40 (TOMM40 in human), MDM10, Porin1 (VDAC1 in human), and TOM22 (TOMM22 in human). In humans, TOMM40 (Humphries et al. 2005) and VDAC1 (Kozjak-Pavlovic et al. 2007, homologous to yeast Porin1) have been shown to be substrates. Many other mitochondrial proteins are anticipated to be substrates of the SAMM50 complex.
beta-ureidopropionate + H2O => beta-alanine + NH4+ + CO2
conversion of 3-ureidopropionate to beta-alanine
As inferred from the yeast TIM23 complex, the human TIMM23 complex resides in the inner membrane of the mitochondrion and transfers precursor proteins to the inner membrane. The presequences of proteins targeted to the inner membrane are transferred to the matrix where they are cleaved. Sequences in the mature regions of the proteins then interact with the TIMM23 complex to halt transfer across the inner membrane and the proteins are released laterally into the inner membrane. TIMM21 is required. In yeast experimentally verified substrates of the TIM23 complex targeted to the inner membrane include CYB2, DLD (LDHD in human), ATP9 (ATP5G1 in human), COQ2, TIM54 (TIMM54 in human), COX4, COX5A, and ATP2 (ATP5B in human). Many other inner membrane proteins are believed to be substrates of the TIMM23 complex.
conversion of 5,6-dihydrouracil to 3-ureidopropionate
5,6-dihydrouracil + H2O => beta-ureidopropionate
As inferred from yeast, the alpha subunit of the mitochondrial processing peptidase (MPP) binds presequences of mitochondrial precursors and the beta subunit cleaves the presequence. After cleavage, proteins destined for the inner membrane are released laterally from TIMM23 SORT into the membrane.
Blockage of Ca(2+)-permeable AMPA receptors suppresses migration and induces apoptosis in human glioblastoma cells
uracil + NADPH + H+ => 5,6-dihydrouracil + NADP+
reduction of uracil to form dihydrouracil
As inferred from yeast, the alpha subunit of the mitochondrial processing peptidase (MPP) binds presequences of mitochondrial precursors and the beta subunit cleaves the presequence. After cleavage, proteins destined for the matrix are drawn into the matrix by ATP-dependent interaction with mtHSP70 (HSPA9, homolog of yeast SSC1) of the PAM complex.
cis-Delta(9,12)-octadecadienoyl-coenzyme A
(deoxy)uridine + orthophosphate <=> uracil + (deoxy)ribose 1-phosphate [UPP]
As inferred from the yeast TIM23 complex, the human TIMM23 complex resides in the inner membrane of the mitochondrion and transfers precursor proteins to the matrix. The TIMM23 complex appears to adopt different configurations (and perhaps different subunit compositions) depending on whether the substrate is destined for the inner membrane or the matrix. Here we refer to the TIMM23 PAM complex as the configuration that delivers inner membrane proteins. The PAM17 subcomplex is required for this activity. The N-terminal presequence of precursors first interacts with TIMM50 and TIMM23. The TIMM17 and TIMM23 subunits form a channel and are required to initiate translocation of precursors. In yeast experimentally verified substrates of TIM23:PAM include Hsp60 (HSP60 in human) and Yfh1 (Frataxin, FXN in human). Many other matrix proteins are believed to be substrates of the TIMM23 complex.
(d)CMP, TMP, or (d)UMP + H2O => (deoxy)cytidine, thymidine, or (deoxy)uridine + orthophosphate [NT5C3]
A human mitochondrion contains about 1500 proteins, more than 99% of which are encoded in the nucleus, synthesized in the cytosol and imported into the mitochondrion. Proteins are targeted to four locations (outer membrane, intermembrane space, inner membrane, and matrix) and must be sorted accordingly (reviewed in Kutik et al. 2007, Milenkovic et al. 2007, Bolender et al. 2008, Endo and Yamano 2009). Newly synthesized proteins are transported from the cytosol across the outer membrane by the TOMM40:TOMM70 complex. Proteins that contain presequences first interact with the TOMM20 subunit of the complex while proteins that contain internal targeting elements first interact with the TOMM70 subunit. After initial interaction the protein is conducted across the outer membrane by TOMM40 subunits. In yeast some proteins such as Aco1, Atp1, Cit1, Idh1, and Atp2 have both presequences that interact with TOM20 and mature regions that interact with TOM70 (Yamamoto et al. 2009). After passage across the outer membrane, proteins may be targeted to the outer membrane via the SAMM50 complex, to the inner membrane via the TIMM22 or TIMM23 complexes (reviewed in van der Laan et al. 2010), to the matrix via the TIMM23 complex (reviewed in van der Laan et al. 2010), or proteins may fold and remain in the intermembrane space (reviewed in Stojanovski et al. 2008, Deponte and Hell 2009, Sideris and Tokatlidis 2010). Presequences on matrix and inner membrane proteins cause interaction with TIMM23 complexes; internal targeting sequences cause outer membrane proteins to interact with the SAMM50 complex and inner membrane proteins to interact with the TIMM22 complex. While in the intermembrane space hydrophobic proteins are chaperoned by the TIMM8:TIMM13 complex and/or the TIMM9:TIMM10:FXC1 complex.
(deoxy)cytidine + H2O => (deoxy)uridine + NH4+ [CDA]
deamination of 2'-Deoxycytidine to 2'-Deoxyuridine
As inferred from the yeast TIM23 complex, the human TIMM23 complex transports precursor proteins across the inner membrane and into the matrix. As in yeast, subunits TIMM50, TIMM17, and TIMM23 are probably necessary for initiating translocation while the PAM complex with mtHSP70 (HSPA9, yeast SSC1) provides the motive force that drives the transport. mtHSP70 binding to the precursor pulls the protein into the matrix in a reaction requiring ATP hydrolysis. The yeast reaction appears to use a Brownian ratchet mechanism (Yamano et al. 2008). In yeast experimentally verified substrates of TIM23 PAM include Hsp60 (HSP60 in human) and Yfh1 (Frataxin, FXN in human). Many other matrix proteins are believed to be substrates of the TIMM23 complex
As inferred from the yeast TIM9:TIM10 complex, the human TIMM9:TIMM10:FXC1 complex chaperones hydrophobic membrane proteins in the intermembrane space until their insertion into the inner or outer membrane. Whereas the yeast TIM9:TIM10 complex is soluble in the intermembrane space, the human TIMM9:TIMM10 complex is associated with the outer surface of the inner membrane (Muhlebein et al. 2004). Experimentally verified substrates of the yeast TIM9:TIM10 complex include AAC (ADP/ATP translocase 1, ANT, SLC25A4 in human), TIM17 (TIMM17 in human), TOM40 (TOMM40 in human), TIM23 (TIMM23 in human), TIM22 (TIMM22 in human), and Tafazzin (Tafazzin, TAZ in human). Many other mitochondrial proteins are anticipated to be chaperoned by the TIMM9:TIMM10 complex.
carbamoyl phosphate + L-aspartate <=> N-carbamoyl L-aspartate + orthophosphate
carbamoyl phosphate and L-aspartate combine to form N-Carbamoyl-L-aspartate
After translation, many newly formed proteins undergo further covalent modifications that alter their functional properties and that are essentially irreversible under physiological conditions in the body. These modifications include the internal peptide bond cleavages that activate proenzymes, the attachment of oligosaccharide moieties to membrane-bound and secreted proteins, the attachment of lipid or glycolipid moieties that serve to anchor proteins to cellular membranes, and the vitamin K-dependent attachment of carboxyl groups to glutamate residues.
Small Ubiquitin-like MOdifiers (SUMOs) are a family of 3 proteins (SUMO1,2,3) that are reversibly conjugated to lysine residues of target proteins via a glycine-lysine isopeptide bond (reviewed in Hay 2013, Hannoun et al. 2010, Gareau and Lima 2010, Wilkinson and Henley 2010, Wang and Dasso 2009). Proteomic methods have yielded estimates of hundreds of target proteins. Targets are mostly located in the nucleus and therefore SUMOylation disproportionately affects gene expression. SUMOs are initially translated as proproteins possessing extra amino acid residues at the C-terminus which are removed by the SUMO processing endoproteases SENP1,2,5 (Hay 2007). Different SENPs have significantly different efficiencies with different SUMOs. The processing exposes a glycine residue at the C-terminus that is activated by ATP-dependent thiolation at cysteine-173 of UBA2 in a complex with SAE1, the E1 complex. The SUMO is transferred from E1 to cysteine-93 of a single E2 enzyme, UBC9 (UBE2I). UBC9 with or, in some cases, without an E3 ligase conjugates the glycine C-terminus of SUMO to an epsilon amino group of a lysine residue on the target protein. SUMO2 and SUMO3 may then be further polymerized, forming chains. SUMO1 is unable to form polymers. Conjugated SUMO can act as a biinding site for proteins possessing SUMO interaction motifs (SIMs) and can also directly affect the formation of complexes between the target protein and other proteins. Conjugated SUMOs are removed by cleavage of the isopeptide bond by processing enzymes SENP1,2,3,5. The processing enzymes SENP6 and SENP7 edit chains of SUMO2 and SUMO3.
Laminin forms an independent network in basement membranes
hydrolysis of 2'-deoxyuridine 5'-triphosphate to form 2'-deoxyuridine 5'-phosphate
The UBA2:SAE1 complex catalyzes the formation of a thioester bond between SUMO1 and cysteine-173 of UBA2 (Desterro et al. 1999, Okuma et al. 1999, Werner et al. 2009, Olsen et al. 2010, Wang and Chen 2010). ATP reacts with the C-terminal glycine residue of SUMO1 to yield pyrophosphate and a transient intermediate, SUMO1 adenylate, which then reacts with the thiol group of the cysteine residue on UBA2.
SUMO1, 2, and 3 are initially expressed as propeptides containing extra residues at the C-terminus. (SUMO1 has 4 residues, SUMO2 has 2 residues, and SUMO3 has 11 residues,) SENP1, 2, and 5 are endoproteases that process the precursors to produce the mature peptides (reviewed in Wang and Dasso 2009, Wilkinson and Henley 2010, Hannoun et al. 2010, Gareau and Lima 2010). SENP1 processes SUMO1 with greater efficiency than SUMO2 or SUMO3. SENP2 and SENP5 process SUMO2 with greater efficiency than SUMO1 or SUMO3 (Gong and Yeh 2006, Mikolajczyk et al. 2007). SENP1 shuttles between the cytosol and nuceoplasm and is predominantly nuclear (Bailey and O'hare 2004, Kim et al. 2005). SENP2 also shuttles (Itahana et al. 2006) and is mainly located on nucleoplasmic filaments of the nuclear pore complex (Hang and Dasso 2002, Zhang et al. 2002). SENP5 is located mostly in the nucleolus (Di Bacco et al. 2006, Gong and Yeh 2006).
uracil + (deoxy)ribose 1-phosphate <=> (deoxy)uridine + orthophosphate [UPP]
The SUMO1 precursor has 4 extra residues at the C-terminus which can be removed endoproteolytically by either SENP1, SENP2, or SENP5 (Zheng and Au, 2005, Mikolajczyk et al. 2007). The order of processing activity is: SENP1 greater than SENP2 greater than SENP5 (Mikolajczyk et al. 2007). Both SENP1 and SENP2 shuttle between the nucleus and cytoplasmic and both are predominantly nucleoplasmic (Bailey and O'Hare 2004, Kim et al. 2005, Zhang et al. 2002, Hang and Dasso 2002, Itahana et al. 2006).
dUMP + N5,N10-methylene tetrahydrofolate => TMP + dihydrofolate
O-glycosylation is an important post-translational modification (PTM) required for correct functioning of many proteins (Van den Steen et al. 1998, Moremen et al. 2012). The O-glycosylation of proteins containing thrombospondin type 1 repeat (TSR) domains and O-glycosylation of mucins are currently described here.
(S)-dihydroorotate + ubiquinone => orotate + ubiquinol
oxidation of (S)-Dihydroorotate to form Orotate
The initial translation products of SUMO1, SUMO2, and SUMO3 are precursors that have extra amino acid residues at the C-terminus (reviewed in Wang and Dasso 2009, Wilkinson and Henley 2010, Hannoun et al. 2010, Gareau and Lima 2010, Hay 2007). SUMO1 has 4 extra residues, SUMO2 has 2 extra residues, and SUMO3 has 11 extra residues. Proteolytic cleavage by SUMO peptidases (SENPs) removes the propeptide and leaves diglycine residues at the C-terminus. Each SENP has distinct preferences for certain SUMOs. SENP1 has highest activity on SUMO1; SENP2 and SENP5 have highest activity on SUMO2 (Shen et al. 2006, Reverter and Lima 2006, Mikolajczyk et al. 2007). SENP1 and SENP2 are predominantly nucleoplasmic (Bailey and O'Hare 2004, Kim et al. 2005, Zhang et al. 2002, Hang and Dasso 2002, Itahana et al. 2006) and SENP5 is predominantly nucleolar (Di Bacco et al. 2006, Gong and Yeh 2006), therefore the processing reactions are believed to occur in the nucleus. The processed SUMO is then activated by formation of a thioester bond with a cysteine residue of an E1 enzyme, UBA2 (SAE2) in a complex with SAE1. SUMO is then transferred from the E1 enzyme to an E2 enzyme, UBC9 (UBE2I).
condensation of N-Carbamoyl-L-aspartate to form (S)-Dihydroorotate (ring closure)
N-carbamoyl L-aspartate + H+ <=> (S)-dihydroorotate + H2O
SUMO is transferred from cysteine-173 of UBA2 to cysteine-93 of UBC9 (UBE2I) in a transthiolation reaction (reviewed in Wang and Dasso 2009, Wilkinson and Henley 2010, Hannoun et al. 2010, Gareau and Lima 2010). UBC9 is the only known E2 enzyme for SUMO and on certain substrates such as RanGAP1 may act without the requirement of an E3 ligase.
decarboxylation of Orotidine 5'-phosphate to form Uridine 5'-phosphate
orotidine 5'-monophosphate => uridine 5'-monophosphate + CO2
SUMO1 is transferred from cysteine-173 of UBA2 to cysteine-93 of UBC9 (UBE2I) in a transthiolation reaction (Desterro et al. 1999, Okuma et al. 1999, Tatham et al. 2003, Lois and Lima 2005, Wang et al. 2007, Werner et al. 2009). The UbL domain of E1 recruits E2 into proximity for the transfer of SUMO (Lois and Lima 2005, Wang et al. 2009),
Cell cycling through Cdc25A: transducer of cytokine proliferative signals
orotate + 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) <=> orotidine 5'-monophosphate (OMP) + pyrophosphate
phosphoribosylation of orotate to form oritidine 5'-phosphate (OMP)
The UBA2:SAE1 complex catalyzes the formation of a thioester linkage between the C-terminal glycine of the mature SUMO and a cysteine residue (cysteine-173) in UBA2 (SAE2) (reviewed in Wang and Dasso 2009, Wilkinson and Henley 2010, Hannoun et al. 2010, Gareau and Lima 2010). During the process the C-terminal glycine residue of SUMO is reacted with ATP to yield pyrophosphate and a transient intermediate, SUMO adenylate. The SUMO adenylate then reacts with the thiol group of the cysteine residue of UBA2 (Olsen et al. 2010).
cytidine or uridine + ATP => CMP or UMP + ADP [UCK1]
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Polyamines: metabolism and implications in human diseases
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(d)NTP + ADP <=> (d)NDP + ATP [NME1,2,3]
thioredoxin, reduced (cytosol) <=> thioredoxin, reduced (nucleus)
(d)NDP + ATP <=> (d)NTP + ADP [NME1,2,3]
thioredoxin, oxidized + NADPH + H+ => thioredoxin, reduced + NADP+
regeneration of active (reduced) Thioredoxin
thioredoxin, oxidized (nucleus) <=> thioredoxin, oxidized (cytosol)
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Translocation of lipid-linked oligosaccharides across the ER membrane requires Rft1 protein
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ADP-ribose + H2O => AMP + D-ribose 5-phosphate (cytosolic)
Cytosolic NUDT5 hydrolyses ADP-ribose to R5P and AMP
ADP-ribose + H2O => AMP + D-ribose 5-phosphate (mitochondrial)
Mitochondrial NUDT9 hydrolyses ADP-ribose to R5P and AMP
alanine + alpha-ketoglutarate <=> pyruvate + glutamate [GPT]
pyruvate + glutamate <=> alanine + alpha-ketoglutarate [GPT]
alanine + alpha-ketoglutarate <=> pyruvate + glutamate [GPT2]
pyruvate + glutamate <=> alanine + alpha-ketoglutarate [GPT2]
oxaloacetate + glutamate <=> aspartate + alpha-ketoglutarate [GOT1]
8-oxo-dGDP + H2O => 8-oxo-dGMP + Pi (NUDT18)
NUDT18 hydrolyses 8-oxo-dGDP to 8-oxo-dGMP
Na+/Cl- dependent neurotransmitter transporters
8-hydroxy-dADP + H2O => 8-hydroxy-dAMP + Pi
NUDT18 hydrolyses 8-OH-dADP to 8-OH-dAMP
NUDT18 hydrolyses 8-oxo-GDP to 8-oxo-GMP
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glutamate + NH4+ + ATP => glutamine + ADP + orthophosphate [GLUL]
glutamine + H2O => glutamate + NH4+ [GLS]
alpha-ketoglutarate + NH4+ + NAD(P)H + H+ <=> glutamate + NAD(P)+ [GLUD1]
glutamate + NAD(P)+ => alpha-ketoglutarate + NH4+ + NAD(P)H + H+ [GLUD1]
L-1-pyrroline-5-carboxylate + NADPH + H+ => proline + NADP+
aspartate + glutamine + ATP <=> asparagine + glutamate + AMP + pyrophosphate [ASNS]
glutamate + ATP + NADPH + H+ => L-glutamate gamma-semialdehyde + NADP+ + ADP + orthophosphate [P5CS]
glutamate + L-glutamate gamma-semialdehyde <=> ornithine + alpha-ketoglutarate [OAT]
ornithine + alpha-ketoglutarate <=> glutamate + L-glutamate gamma-semialdehyde [OAT]
aspartate + alpha-ketoglutarate <=> oxaloacetate + glutamate [GOT2]
MHC II and the endocytic pathway: regulation by invariant chain
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isovaleryl-CoA + FAD => beta-methylcrotonyl-CoA + FADH2
a-ketoisocaproate, a-keto-b-methylvalerate, or a-ketoisovalerate + glutamate <=> leu, ile, or val + alpha-ketoglutarate [BCAT1]
leu, ile, or val + alpha-ketoglutarate <=> a-ketoisocaproate, a-keto-b-methylvalerate, or a-ketoisovalerate + glutamate [BCAT2]
a-ketoisocaproate, a-keto-b-methylvalerate, or a-ketoisovalerate + glutamate <=> leu, ile, or val + alpha-ketoglutarate [BCAT2]
a-ketoisocaproate, a-keto b-methylvalerate, or a-ketoisovalerate + CoA + NAD+ => isovaleryl-CoA, a-methylbutyryl-CoA, or isobuyryl-CoA + CO2 + NADH + H+
Oxidative decarboxylation of branched-chain alpha-keto acids
3-phosphonooxypyruvic acid + L-glutamate = O-phospho-L-serine + 2-oxoglutarate
leu, ile, or val + alpha-ketoglutarate <=> a-ketoisocaproate, a-keto-b-methylvalerate, or a-ketoisovalerate + glutamate [BCAT1]
glutamine + pyruvate => 2-oxoglutaramate + alanine
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The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
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Genetics of childhood disorders: LII. Learning and memory, part 5: human cognitive disorders and the ras/ERK/CREB pathway
J Am Acad Child Adolesc Psychiatry 42:873-6
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Compressed microfibril models of the native collagen fibril
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RNA editing by base deamination: more enzymes, more targets, new mysteries.
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The ER membrane-associated enzyme dehydrodolichyl diphosphate synthase (DHDDS) mediates the sequential head-to-tail cis addition of multiple isopentyl pyrophosphate (IPP) molecules to farnesyl pyrophosphate (E,E-FPP) to produce polyprenol pyrophosphate (pPPP) (Shridas et al. 2003). Dolichol in humans contain homologues ranging from 17-23 isoprene units, the most common homologues contain 19 or 20 isoprene units (Freeman et al. 1980). Defects in DHDDS cause retinitis pigmentosa 59 (RP59; MIM:613861), a pigment retinopathy, characterised by retinal pigment deposits (visible on fundus examination) and primary loss of rod photoreceptors followed by secondary loss of cone photoreceptors. Sufferers typically have night vision blindness and loss of mid to peripheral vision. As the condition progresses, they lose far peripheral vision and eventually central vision (Zuchner et al. 2011).
Glycosylphosphatidyl inositol (GPI) acts as a membrane anchor for many cell surface proteins. GPI is synthesized in the endoplasmic reticulum. In humans, a single pathway consisting of eleven reactions appears to be responsible for the synthesis of the major GPI species involved in membrane protein anchoring. As a nascent protein fated to become GPI-anchored moves into the lumen of the endoplasmic reticulum, it is attacked by a transamidase complex that cleaves it near its carboxy terminus and attaches an acylated GPI moiety. The GPI moiety is deacylated, yielding a protein-GPI conjugate that can be efficiently transported to the Golgi apparatus.
Glycosylphosphatidyl inositol (GPI) acts as a membrane anchor for many cell surface proteins. GPI is synthesized in the endoplasmic reticulum. In humans, a single pathway consisting of nine reactions appears to be responsible for the synthesis of the major GPI species involved in membrane protein anchoring. This pathway is shown in the figure. Two additional reactions, not shown, allow the synthesis of variant forms of GPI, one with an additional mannose residue and one with an additional ethanolamine (Tauron et al. 2004; Shishioh et al. 2005). These variant GPI molecules may be used for tissue-specific protein modifications, or may function independently. The steps of GPI synthesis were first identified by isolating large numbers of mutant cell lines that had lost the ability to express GPI anchored proteins on their surfaces. Somatic cell hybrid analyses of these lines allowed the definition of complementation groups corresponding to distinct mutated genes, and cDNAs corresponding to normal forms of these genes were identified on the basis of their abilities to restore normal cell surface protein expression in mutant cells. Co-precipitation experiments with tagged cloned proteins have allowed the identification of additional proteins involved in GPI anchor biosynthesis.
In the eighth reaction of GPI synthesis, a third mannose residue is added, catalyzed by PIG-B (Takahashi et al. 1996).
Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing
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Downregulation of TGF-beta receptor signaling
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Dolichol is a polyisoprenol lipid comprised of five-carbon isoprene units linked linearly in a head-to-tail fashion. Almost all eukaryotic membranes contain dolichol and its phosphorylated form is used in the N-glycosylation of proteins where it is used as an anchor for the N-glycan sugar to the ER membrane, and as an initiation point for the synthesis. Dolichol biosynthesis occurs on the cytoplasmic face of the ER membrane, which is where N-glycosylation occurs too, so is perfectly placed to serve as a substrate for this process. Dolichyl phosphate can be obtained either from direct phosphorylation of dolichol, formed in a series of reactions from mevalonate 5-pyrophosphate, or a salvage reaction by de-phosphorylation of dolichyl diphosphate, released at the end of N-glycan biosynthesis (Cantagrel & Lefeber 2011).
Glucosamine-fructose 6-phosphate aminotransferases 1 and 2 (GFPT1,2) are the first and rate-limiting enzymes in the hexosamine synthesis pathway, and thus formation of hexosamines like N-acetylglucosamine (GlcNAc). These enzymes probably plays a role in limiting the availability of substrates for the N- and O- linked glycosylation of proteins (McKnight et al. 1992, Oki et al. 1999). GFPT1 and 2 are required for normal functioning of neuromuscular synaptic transmission. Defects in GFPT1 leads to altered muscle fibre morphology and impaired neuromuscular junction development (Senderek et al. 2011).
Polyprenol reductase (SRD5A3), resident on the endoplasmic reticulum membrane, mediates the reduction of the alpha-isoprene unit of polyprenol (pPNOL) to form dolichol (DCHOL) in a NADPH-dependent manner (Cantagrel et al. 2010). Defects in SRD5A3 cause congenital disorder of glycosylation 1q (SRD5A3-CDG, CDG1Q; MIM:612379), a neurodevelopmental disorder characterised by under-glycosylated serum glycoproteins resulting in nervous system development, psychomotor retardation, hypotonia, coagulation disorders and immunodeficiency (Cantagrel et al. 2010, Kasapkara et al. 2012). Defects in SRD5A3 can also cause Kahrizi syndrome (KHRZ; MIM:612713), a neurodevelopmental disorder characterised by mental retardation, cataracts, coloboma, kyphosis, and coarse facial features (Kahrizi et al. 2011).
Dolichol kinase (DOLK, TMEM15) mediates the phosphorylation of dolichol (DCHOL) to form dolichyl phosphate (DOLP) in the ER membrane (Fernandez et al. 2002). Defects in DOLK cause congenital disorder of glycosylation type 1M (CDG1M aka dolichol kinase deficiency; MIM:610768), a severe mutisystem disorder characterised by under-glycosylated serum glycoproteins which results in nervous system under-development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. Death occurs in early life (Kranz et al. 2007).
Cytosolic GNPNAT1 catalyzes the reaction of glucosamine 6-phosphate and acetyl-CoA to form N-acetyl-glucosamine 6-phosphate (GlcNAc6P) and CoA-SH. Structural studies indicate that the active form of the enzyme is a dimer (Wang J et al, 2008).
Cytosolic PGM3 catalyzes the isomerization of N-acetyl-D-glucosamine 6-phosphate (GlcNAc6P) to form N-acetyl-D-glucosamine 1-phosphate (GlcNAc1P) (Pang H et al, 2002).
Due to the crowded envirnoment within the cell, many proteins must interact with molecular chaperones to attain their native conformation (reviewed in Young et al., 2004). Chaperones recognize and associate with proteins in their non-native state and facilitate their folding by stabilizing the conformation of productive folding intermediates. Chaperones that take part broadly in de novo protein folding, such as the Hsp70s and the chaperonins, facilitate the folding process through cycles of substrate binding and release regulated by their ATPase activity (see Young et al., 2004; Spiess et al., 2004; Bigotti and Clarke, 2008).
The reaction of EIF5A, spermidine, and NAD+ to form EIF5A(Dhp), 1,3-diaminopropane, and NADH + H+ is reversible in vitro. Under physiological conditions, the reverse reaction is probably minimized by the rapid, irreversible conversion of FIF5A(Dhp) to EIF5A(Hyp).
Cytosolic deoxyhypusine synthase catalyzes the reaction of EIF5A protein, spermidine, and NAD+ to convert lysine-50 of EIF5A to deoxyhypusine, generating 1,3-diaminopropane and NADH + H+ in the process (Park 2006). Although the reaction is reversible, the reverse reaction is probably minimized under physiological conditions by the rapid, irreversible conversion of EIF5A(Dhp) to EIF5A(Hyp).
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Cytosolic deoxyhypusine hydroxylase catalyzes the irreversible conversion of peptidyl-deoxyhypusine to peptidyl-hypusine. The only known substrate for this enzyme is the modified lysine at residue 50 of eIF5A (Kang et al. 2007; Kim et al. 2006).
Cytosolic eIF5A undergoes a unique two-step post-translational modification at Lys 50 via deoxyhypusine (Dhp) to hypusine (Hyp). In the first step deoxyhypusine synthase transfers the aminobutyl group of spermidine to the epsilon-amino group of lysine 50, using NAD+ as a cofactor. Hydroxylation of the C2 of the newly added moiety in the second step is catalyzed by deoxyhypusine hydroxylase/monooxygenase with molecular oxygen as the source. The molecular function of eIF5A is unknown, but the protein is required for viability in eukaryotic cells and its normal function requires hypusinylation. eIF5A is the only protein known to undergo hypusinylation (Park 2006).
After translation, many newly formed proteins undergo further covalent modifications that alter their functional properties and that are essentially irreversible under physiological conditions in the body. These modifications include the vitamin K-dependent attachment of carboxyl groups to glutamate residues and the conversion of lysine residues to hypusine.
In the second step of GPI synthesis, N-acetylglucosaminyl-PI is hydrolyzed to yield glucosaminyl-PI and acetate. The phosphatidylinositol (PI) derivatives involved in this reaction are located in the endoplasmic reticulum membrane, as is the PIG-L enzyme that catalyzes it (Sharma et al. 1999; Pottekat and Menon 2004).
In the fourth step of GPI synthesis, an acyl group (typically palmitate) is transferred from acyl CoA to glucosaminyl-PI. Mutagenesis and cloning studies suggest that a single protein, PIG-W, catalyzes this reaction (Murakami et al. 2003).
In the sixth step of GPI synthesis, a phosphoethanolamine group is transferred from phosphatidylethanolamine onto the first mannose of the GPI precursor. The human protein that catalyzes this reaction was first identified because it could complement a yeast mutant strain defective for GPI synthesis (Gaynor et al. 1999); its specific function in phosphoethanolamine transfer is inferred from functional studies of the homologous mouse protein (Hong et al. 1999). The reaction is annotated here with phosphatidylethanolamine as the donor of the phosphoethanolamine group on the basis of studies in yeast (Imhof et al. 2000).
In the seventh reaction of GPI synthesis, a second mannose residue is added to the glycolipid on the lumenal face of the endoplasmic reticulum membrane. PIG-V was identified as the catylyst, or a component of the catalyst, of this reaction, on the basis of its ability to correct the metabolic defects of yeast and mammalian mutant cells arrested at this stage of the GPI synthetic process (Fabre et al. 2005; Kang et al. 2005).
A fourth mannose is added to the N-glycan precursor by ALG11. The addition of the fifth mannose, also by ALG11, is the last step occurring on the cytosolic side of the ER membrane (Cipollo JF et al, 2001). Both these reactions are alpha1,2 mannose additions.
A third mannose is added to the N-glycan precursor by ALG2 using its alpha1,6-mannosyltransferase activity. This has been demonstrated experimentally in yeast (O'Reilly MK et al, 2006; Kämpf M et al, 2009); the human reaction is inferred by homology. Defects in ALG2 are the cause for CDG1I (Thiel C et al, 2003).
A second mannose is added to the N-glycan precursor via an alpha-1,3 linkage. The reaction is catalyzed by the mannosyltransferase ALG2. This is a bifunctional enzyme with both alpha 1,3- and alpha 1,6-mannosyltransferase activities. In humans, only the alpha 1,3 activity used in this reaction has been elucidated (Thiel et al. 2003). Defects in ALG2 are the cause of ALG2-CDG (CDG-1i; MIM:607906) (Thiel et al. 2003).
A mannose is added to the N-glycan precursor via a beta-1,4 linkage. The reaction is catalyzed by ALG1 (Takahashi T et al, 2000). Defects in ALG1 lead to congenital disorder of glycosylation type 1K (CDG1K) (Schwarz et al. 2004; Kranz et al. 2004; Grubenmann et al. 2004).
A second N-acetylglucosamine is added to the N-glycan precursor via a beta-1,4 linkage. This reaction is catalyzed by the ALG13:ALG14 complex, in which ALG13 functions as the catalyst and ALG14 functions as a membrane anchor which recruits ALG13 to the cytosolic face of ER (Gao XD et al, 2005).
In the first step of N-glycan precursor (LLO) synthesis, N-acetylglucosamine is added, via an alpha-1,3 linkage, to a molecule of dolichyl phosphate, producing N-acetyl-D-glucosaminyl-diphosphodolichol (Eckert et al. 1998). This reaction is catalyzed by DPAGT1 (ALG7 in yeast), mutations in which are associated with CDG disorder type I-J (Wu et al. 2003). The dolichyl phosphate acts as an anchor for the LLO, so that subsequent sugar-addition reactions take place on a sugar anchored in the ER membrane.
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The seventh mannose is added to the N-glycan precursor. This reaction occurs in the ER lumen and uses dolichyl phosphate D-mannose as the mannose donor with ALG9 mediating the reaction. Defects in ALG9 are the cause of congenital disorder of glycosylation type 1L (CDG1L) (Frank CG et al, 2004; Weinstein M et al, 2005). For many years ALG9 has been thought to be involved in bipolar affective disorder (Baysal BE et al, 2002), but this hypothesis has been proven wrong (Baysal BE et al, 2006).
PP2A-mediated dephosphorylation of key metabolic factors
The eighth mannose is added to the N-glycan precursor. This reaction occurs in the ER lumen and uses dolichyl phosphate D-mannose as a mannose donor. Defects in ALG12 are the cause of congenital disorder of glycosylation type 1G (CDG1G) (Chantret I et al, 2002).
The precursor of the N-glycan sugar, now in the form of (GlcNAc)2 (Man)5 (PP-Dol), is flipped across the ER membrane, moving it from the cytosolic side into the ER lumen. The exact mechanism of this translocation is not well understood: the protein RFT1 is known to be involved (Helenius et al. 2002), along with an unknown flippase, which is distinct from the one that flips the Dol-P linked precursors (Dol-P-Mannose and Dol-P-glucose) (Sanyal et al. 2008). Defects in RFT1 are associated with Congenital Disorder of Glycosylation 1N (CDG1N) (Haeuptle et al. 2008).
The sixth mannose is added to the N-glycan precursor. This reaction occurs in the ER lumen and uses a different mannose donor (dolichyl-phosphate-mannose) than the previous steps. It has been proposed that ALG3, along with all the mannosyl- and glucosyltransferases in the N-glycan biosynthesis pathway that use dolichyl-phosphate-mannose or dolichyl-phosphate-glucose as donor, derive from duplications of a common ancestral enzyme (Oriol et al. 2002). Defects in ALG3 are associated with Congenital Disorder of Glycosylation 1D (CDG1D) (Sun et al. 2005).
Mannose-6-phosphate isomerase (MPI) isomerizes fructose 6-phosphate (Fru6P) to mannose 6-phosphate (Man6P) (Proudfoot et al. 1994). Defects in this gene are associated with congenital disorder of glycosylation type 1B (CDG1B). Oral administration of mannose is an efficient therapy against this defect (Schollen et al. 2000).
UDP-acetylglucosamine acts as a donor for the first two steps of the N-glycan precursor biosynthesis pathway, and is later used as a substrate for further modifications after the precursor has been attached to the protein. It is synthesized from fructose 6-phosphate, glutamine, acetyl-CoA, and UTP in four steps.
A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic
Mannose 1-phosphate is converted to GDP-Mannose by mannose-1-phosphate guanyltransferase alpha and beta forms (GMPPA/B). This enzyme had originally been characterized from rat and bovine sources (Verachtert H et al, 1966) and more recently from pig (Ning B and Elbein AD, 2000).
Phosphomannomutases 1 and 2 (PMM1 and PMM2) catalyze the isomerization of mannose 6-phosphate (Man6P) to mannose 1-phosphate (Man1P) in the cytosol of cells (Wada & Sakamoto 1997, Matthijs et al. 1997). Mutations in the PMM2 gene are one of the causes of Jaeken syndrome. a disease of glycosylation, type CDGIa. (Matthijs et al. 1997b).
Cytosolic UAP1 catalyzes the reaction of N-acetyl-D-glucosamine 1-phosphate (GlcNAc1P) and UTP to UDP-N-acetyl-D-glucosamine and pyrophosphate. Structural studies indicate that the active form of the enzyme is a dimer (Peneff C et al, 2001).
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E2F mediated regulation of DNA replication
Reactions for the synthesis of the small nucleotide-linked sugar substrates that are used in the synthesis of the N-glycan precursor and in the later steps of glycosylation are annotated here. All these nucleotide-linked sugar donors are synthesized in the cytosol; however, to participate in the later reactions of N-glycan precursor biosynthesis (when the glycan is oriented toward the lumen of the endoplasmic reticulum (ER)), these substrates must be attached to a dolichyl-phosphate molecule and then flipped toward the luminal side of the ER, through a mechanism which is still not known but which involves a different protein than the one that mediates the flipping of the LLO itself (Sanyal et al. 2008). Two of the genes encoding enzymes involved in these reactions, MPI and PMM2, are known to be associated with Congenital Disorders of Glycosylation (CDG) diseases of type I. Of these, CDG-Ia, associated with defects in PMM2, is the most frequent CDG disease reported.
GDP-mannose is the mannose donor for the first 5 mannose addition reactions in the N-glycan precursor synthesis, and also for the synthesis of Dolichyl-phosphate-mannose involved in other mannose transfer reactions. It is synthesized from fructose 6-phosphate and GTP in three steps.
Dolichyl-phosphate beta-glucosyltransferase (ALG5) associated with the endoplasmic reticulum (ER) membrane catalyzes the reaction of cytosolic UDP-glucose with dolichyl phosphate exposed on the cytosolic face of the ER membrane to form Dolichyl-P-glucose with its glucose moiety oriented toward the cytosol (Imbach T et al, 1999).
Dolichyl-phosphate-glucose functions as a donor of glucose groups in reactions including three steps of N-glycan precursor biosynthesis. Dolichyl-phosphate-glucose itself is synthesized from UDP-glucose and dolichol phosphate on the cytosolic face of the endoplasmic reticulum membrane, then flipped to the luminal surface of that membrane.
Sialic acids are a family of 9 carbon alpha-keto acids that are usually present in the non reducing terminal of glycoconjuates on the cell surface of eukaryotic cells. These sialylated conjugates play important roles in cell recognition and signaling, neuronal development, cancer metastasis and bacterial or viral infection. More than 50 forms of sialic acid are found in nature, the most abundant being N-acetylneuraminic acid (Neu5Ac, N-acetylneuraminate) (Li & Chen 2012, Wickramasinghe & Medrano 2011). The steps below describe the biosynthesis, transport, utilization and degradation of Neu5Ac in humans.
The enzyme ER Man I can slowly trim up to four of the mannoses on the N-glycan on unfolded proteins accumulated in the ER. This step describes the removal of the mannose in the C position (Hirao et al, 2006).
The enzyme ER Man I can slowly trim up to four of the mannoses on the N-glycan on unfolded proteins accumulated in the ER. This step describes the removal of the mannose in the A position (Hirao et al, 2006; Frenkel et al, 2003).
While the protein is bound to the chaperone complex, the glycan is still accessible to glucosidase II, which eventually removes the last remaining glucose residue. This also results in breaking the interaction between the chaperone and the glycoprotein, independently of whether the latter has achieved proper folding (Pelletier MF et al, 2000). This has been interpreted as a 'timing mechanism', in which a protein has only a limited period of time to achieve correct folding when bound to the chaperone, to avoid the scenario where proteins that take too long to fold would block the availability of CNX or CRT. Proteins with folding defects get transported to the Endoplasmic Reticulum Quality Control Compartment, while proteins with correct folding are transported to the cis-Golgi where the glycan is further modified.
The enzyme ER Man I can slowly trim up to four of the mannoses on the N-glycan on unfolded proteins accumulated in the ER. This step describes the removal of the mannose in the B position (Gonzalez et al, 1999: Hirao et al, 2006).
Proteins with major folding defects are extracted from futile folding cycles in the calnexin chaperone system and the ER Quality Control Compartment, and are translocated back to the citosol for degradation. The N-glycan is used as a signal to distinguish proteins to be degraded, upon recognition by EDEM1, EDEM2 and EDEM3, three ER-stress-induced members of the glycosyl hydrolase 47 family (see Olivari S, Molinari M 2007 for a review) and OS9 (Mikami K, 2010; Hosokawa N, 2009).
Proteins that are released from the CNX or CRT complex with folding defects accumulate in a compartment of the ER called ERQC (Kamhi-Nesher et al. 2001). Here, the enzymes UGGG1 or UGGG2 are able to recognize glycoproteins with minor folding process and re-add the glucose on the alpha,1,3 branch; this is a signal for the transport of these glycoproteins back to the ER, where they can interact again with CNX or CRT in order to achieve a correct folding. At the same time that the glycoprotein is in the ERQC, the enzyme ER mannosidase I progressively removes the mannoses in position 1A, 2A, B, C on N-glycans; when the mannose on 1A is trimmed, UGGG1/UGGG2 is no longer able to re-add the glucose, and therefore the protein is destined for degradation. For years it has been thought that the removal of the mannose in position B of the N-glycan was the signal to direct proteins to degradation. However, this mechanism has been described better by Avezov et al (Avezov et al. 2008) and it has been demonstrated that even glycoproteins with Man8 or Man7 glycans can be re-glucosylated and interact again with CNX or CRT. For a review on this topic, see Lederkremer 2009 and Maattanen P et al, 2010.
Removal of the second mannose on the alpha 1,3 branch (Frenzel Z et al, 2003).
The enzymes UGGT1 and UGGT2 are able to distinguish proteins with minor folding defects in the ERQC and reglucosylate them, by adding a glucose on the alpha 1,3 branch (Arnold SM et al, 2000; Arnold SM et al, 2003). The major affinity of these enzymes for proteins with minor folding defects has been demonstrated, but the exact mechanism that enable them to distinguish proteins with major and minor defects is still unknown (Pearse BR et al, 2008).
After being synthesized in the ER membrane the 14-sugars lipid-linked oligosaccharide is co-translationally transferred to an unfolded protein, as described in the previous steps. After this point the N-glycan is progressively trimmed of the three glucoses and some of the mannoses before the protein is transported to the cis-Golgi. The role of these trimming reactions is that the N-glycan attached to an unfolded glycoprotein in the ER assume the role of 'tags' that direct the interactions of the glycoprotein with different elements that mediate its folding. The removal of the two outer glucoses leads to an N-glycan with only one glucose, which is a signal for the binding of either one of two chaperone proteins, calnexin (CNX) and calreticulin (CRT). These chaperones provide an environment where the protein can fold more easily. The interaction with these proteins is not transient and is terminated by the trimming of the last remaining glucose, after which the glycoprotein is released from CNX or CRT and directed to the ER Quality Control compartment (ERQC) if it still has folding defects, or transported to the Golgi if the folding is correct. The involvement of N-glycans in the folding quality control of proteins in the ER explains why this form of glycosylation is so important, and why defects in the enzymes involved in these reactions are frequently associated with congenital diseases. However, there are many unknown points in this process, as it is known that even proteins without N-glycosylation sites can be folded properly (Caramelo JJ and Parodi AJ, 2008).
The unfolded protein is recognized by a chaperon protein (calnexin or calreticulin) and the folding process starts. The binding of these protein requires a mono-glucosylated glycan (Caramelo JJ and Parodi AJ, 2008), but in certain cases can occur even in the absence of glycosylation (Ireland BS et al, 2008).
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Peroxisome proliferator-activated receptor alpha (PPARalpha) and athero-sclerosis
Curr Drug Targets Cardiovasc Haematol Disord 5:513-23
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The last mannose is added to the N-glycan precursor. This reaction occurs in the ER lumen, uses Dolichyl phosphate D-mannose as the mannose donor, and is catalyzed by ALG9. Defects in ALG9 are the cause of congenital disorder of glycosylation type 1L (CDG1L) (Frank CG et al, 2004; Weinstein M et al, 2005). For many years ALG9 was thought to be involved in bipolar affective disorder (Baysal BE et al, 2002), but this hypothesis has been proven wrong (Baysal BE et al, 2006).
The first glucose is added to the N-glycan precursor, mediated by ALG6. Defects in ALG6 are associated with CDG-Ic disorder (Imbach T et al, 1999; Sun L et al, 2005). The donor is a dolichol-phosphate-glucose (synthesized by ALG5).
The second glucose (supplied from the donor dolichol-phosphate-glucose) is added to the N-glycan precursor, mediated by ALG8 (Schollen E et al, 2004). Defects in ALG8 are the cause of congenital disorder of glycosylation type 1H (CDG1H) (Schollen E et al, 2004; Sun L et al, 2005).
The last glucose is added to the N-glycan precursor. This reaction occurs inside the ER lumen and uses Dol-P-Glc as the glucose donor. In yeast, this reaction is catalyzed by ALG10 (Burda P and Aebi M,1998); however, this gene is duplicated in primates (Ciccarelli FD et al, 2005; Table 1), leading to two homologues, ALG10A and ALG10B, and to date there is no clear evidence to say which of these two paralogues (or both) is responsible for catalyzing this reaction in humans. No Congenital Disorders of Glycosylations are known to be associated with either gene.
N-linked glycosylation commences with the 14-step synthesis of a dolichol lipid-linked oligosaccharide (LLO) consisting of 14 sugars (2 core GlcNAcs, 9 mannoses and 3 terminal GlcNAcs). This pathway is highly conserved in eukaryotes, and a closely related pathway is found in many eubacteria and Archaea. Mutations in the genes associated with N-glycan precursor synthesis lead to a diverse group of disorders collectively known as Congenital Disorders of Glycosylation (type I and II) (Sparks et al. 1993). The phenotypes of these disorders reflect the important role that N-glycosylation has during development, controlling the folding and the properties of proteins in the secretory pathway, and proteins that mediate cell-to-cell interactions or timing of development.
After the glycosylated precursor is attached to the protein, the outer alpha-1,2-linked glucose is removed by glucosidase I (MOGS, GCS1 in yeast). This is a mandatory step for the protein folding control and glycan extension, and defects in MOGS are associated with congenital disorder of glycosylation type IIb (CDGIIb) (De Praeter et al. 2000, Völker et al. 2002).
A recently discovered protein called malectin is known to recognize the Glc(2)Man(9)GlcNAc(2) glycan (Schallus T et al, 2008). The exact role of this interaction is not clear but malectin is thought to regulate the availability of this substrate to glucosidase II, or to act as a chaperone to stabilize the unfolded protein.
Calnexin (membrane protein) and calreticulin (soluble in ER) are two lectins (proteins that can bind a glycan) which recognize the mono-glucosylated form of the N-glycan and mediate the folding of the glycoproteins to which they are attached to (Ou WJ et al, 1993; Nauseef Wm et al, 1995). Calmegin is another chaperone with the same role expressed only in testis (van Lith M et al, 2007). These lectins act as chaperons, providing a protected environment where the unfolded glycoprotein can fold without forming interactions with other proteins or components in the ER. The unfolded protein can loop between these two steps multiple time, therefore this process is called the 'calnexin/calreticulin cycle'. If the protein achieves correct folding, it is modified by Mannosidase I and then moved to the cis-Golgi where the glycan is further processed.
A second glucose is removed from the N-linked glycan. The removal of an alpha1,3 glucose moiety is catalyzed by glucosidase II, a complex composed of an alpha subunit (GANAB) with catalytic activity and a beta subunit (GLU2B; PRKCSH), probably with regulatory and recruitment function (Pelletier MF et al, 2000). GANAB can exist in two different isoforms, but both are able to catalyze both of the reactions catalyzed by glucosidase II (Pelletier MF et al, 2000). Defects in PRKCSH are a cause of polycystic liver disease (PCLD).
ERp57/ERp27 is a thiol-oxidoreductase that interacts with calnexin and mediates the formation of disulfide bonds in the unfolded glycoprotein (Alanen HI et al, 2006).
Role of microtubules and myosins in Fc gamma receptor-mediated phagocytosis
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Enzymatic synthesis and properties of 5-phosphoribosylpyrophosphate
lysine + alpha-ketoglutarate +NADPH + H+ => saccharopine + NADP+ + H2O
saccharopine + NAD+ + H2O => alpha-aminoadipic semialdehyde + glutamate + NADH + H+
4-imidazolone-5-propionate + H2O => N-formiminoglutamate + 2H+
Histidine is decarboxylated to histamine
urocanate + H2O => 4-imidazolone-5-propionate
methylmalonate semialdehyde + NAD+ + CoA => propionyl-CoA + CO2 + NADH + H+
Oxidative decarboxylation of alpha-ketoadipate to glutaryl CoA by alpha-ketoglutarate dehydrogenase
alpha-ketoadipate + CoASH + NAD+ => glutaryl-CoA + CO2 + NADH + H+
2-oxoglutarate [mitochondrial matrix] + 2-oxoadipate [cytosol] <=> 2-oxoglutarate [cytosol] + 2-oxoadipate [mitochondrial matrix]
Exchange of cytosolic 2-oxoadipate for mitochondrial 2-oxoglutarate
alpha-aminoadipic semialdehyde + NAD+ => alpha-aminoadipate + NADH + H+
alpha-methylbutyryl-CoA + FAD => tiglyl-CoA + FADH2
alpha-methyl-beta-hydroxybutyryl-CoA + NAD+ <=> alpha-methylacetoacetyl-CoA + NADH + H+
alpha-methylacetoacetyl-CoA + NADH + H+ <=> alpha-methyl-beta-hydroxybutyryl-CoA + NAD+
alpha-methyl-acetoacetyl-CoA + CoA => propionyl-CoA + acetyl-CoA
beta-methylcrotonyl-CoA + ATP + CO2 <=> beta-methylglutaconyl-CoA + ADP + orthophosphate + H2O [MCCA]
beta-methylglutaconyl-CoA + ADP + orthophosphate + H2O <=> beta-methylcrotonyl-CoA + ATP + CO2 [MCCA]
beta-hydroxyisobutyryl-CoA + H2O => beta-hydroxyisobutyrate + CoA
isobutyryl-CoA + FAD => methacrylyl-CoA + FADH2
methylmalonyl semialdehyde + NADH + H+ <=> beta-hydroxyisobutyrate + NAD+
beta-hydroxyisobutyrate + NAD+ <=> methylmalonyl semialdehyde + NADH + H+
N-formylkynurenine + H2O => kynurenine + formate
kynurenine + pyruvate => 4-(2-aminophenyl)-2,4-dioxobutanoic acid + alanine [CCBL2]
L-glutamate gamma-semialdehyde + NAD+ => glutamate + NADH + H+
tryptophan + O2 => N-formylkynurenine [TDO]
3-hydroxyanthranilate + O2 => 2-amino-3-carboxymuconate semialdehyde
2-amino-3-carboxymuconate semialdehyde => 2-aminomuconate semialdehyde + CO2
kynurenine + O2 + NADPH + H+ => 3-hydroxykynurenine + NADP+ + H2O
3-hydroxykynurenine + H2O => 3-hydroxyanthranilate + alanine
ornithine (cytosolic) + citrulline (mitochondrial) => ornithine (mitochondrial) + citrulline (cytosolic)
glutaryl-CoA + FAD => crotonyl-CoA + FADH2 + CO2
phenylalanine + pyruvate => 3-(indol-3-yl)pyruvate + alanine
4a-hydroxytetrahydrobiopterin => q-dihydrobiopterin + H2O
q-dihydrobiopterin + NADH + H+ => tetrahydrobiopterin + NAD+
tyrosine + alpha-ketoglutarate <=> p-hydroxyphenylpyruvate + glutamate
p-hydroxyphenylpyruvate + glutamate <=> tyrosine + alpha-ketoglutarate
p-hydroxyphenylpyruvate + O2 => homogentisate + CO2
homogentisate + O2 => maleylacetoacetate
fumarylacetoacetate => fumarate + acetoacetate
maleylacetoacetate => fumarylacetoacetate
Please note that this reaction was inferred from experiments performed using Saccharomyces cerevisiae.
Methylthio-ribulose-P = Methylthio-ribose-P
Protein synthesis is accomplished through the process of translation of an mRNA sequence into a polypeptide chain. This process can be divided into three distinct stages: initiation, elongation and termination. During the initiation phase, the two subunits of the ribosome are brought together to the translation start site on the mRNA where the polypeptide chain is to begin. Extension of the polypeptide chain occurs when a specific aminoacyl-tRNA, as determined by the template mRNA, binds an elongating ribosome. The protein chain is released from the ribosome when any one of three stop codons in the relevant reading frame on the mRNA is reached. Individual reactions at each one of these stages are catalyzed by a number of initiation, elongation and release factors, respectively.
Methylthio-ribose-P = Methylthio-ribulose-P
The arrival of any of the three stop codons (UAA, UAG and UGA) into the ribosomal A-site triggers the binding of a release factor (RF) to the ribosome and subsequent polypeptide chain release. In eukaryotes, the RF is composed of two proteins, eRF1 and eRF3. eRF1 is responsible for the hydrolysis of the peptidyl-tRNA, while eRF3 provides a GTP-dependent function. The ribosome releases the mRNA and dissociates into its two complex subunits, which can reassemble on another molecule to begin a new round of protein synthesis. It should be noted that at present, there is no factor identified in eukaryotes that would be the functional equivalent of the bacterial ribosome release (or recycling) factor, RRF, that catalyzes dissociation of the ribosome from the mRNA following release of the polypeptide
Many biosynthetic reactions are coupled to the cleavage of ATP to yield AMP and pyrophosphate. These reactions are typically freely reversible when carried out with purified substrates and enzymes in vitro. In vivo, however, the pyrophosphate is rapdily and essentially irreversibly hydrolyzed by a ubiquitous inorganic pyrophosphatase. This hydrolysis has the effect of pulling the first reaction strongly in the direction of biosynthesis, at the expense of two high-energy phosphate bonds. Studies of human cells have identified two forms of the enzyme, one localized to the cytosol and the other to the mitochondrial matrix (Raja et al. 1981).
Gene Expression covers the pathways by which genomic DNA is transcribed to yield RNA, the regulation of these transcription processes, and the pathways by which newly-made RNA Transcripts are processed. Most annotation is centered on the generation of messenger RNAs (mRNAs) by regulated RNA polymerase II (PolII) transcription, although the activities of PolI and PolIII are also covered briefly, as are some aspects of microRNA generation and function. Aspects of mRNA synthesis annotated here include the assembly of transcription factor complexes and their role in targeting specific genes for transcription, PolII-mediated transcription (RNA synthesis) itself, and the co- and post-translational processing of this RNA, via capping, splicing, and 3'-cleavage and polyadenylation to yield mature mRNA molecules that are exported from the nucleus. mRNA editing and nonsense-mediated decay are also annotated. Processes leading to mRNA breakdown are described: deadenylation-dependent mRNA decay, microRNA-mediated RNA cleavage, and regulation of mRNA stability by proteins that bind AU-rich elements. Other pathways included here are tRNA aminoacylation and snRNP assembly.
N-acetylspermine is oxidised to spermidine
N-acetylspermidine is oxidized to putrescine
Post-transcriptional splicing of introns is affected neither by the elongating properties of RNA polymerase II, nor by the binding of splicing regulatory factors to the enzyme. It is only affected by the relative abundance of constitutive and/or regulatory splicing factors at the sites where splicing takes place. Nevertheless it is important to point out that cytological evidence indicates that unspliced or partially spliced pre-mRNAs do not diffuse in the nucleoplasm far from the transcription sites. Therefore, recruitment of splicing factors to transcription sites would still favor the post-transcriptional splicing of introns.
Putrescine + dc-Adenosyl methionine => Spermidine + 5'-methylthioadenosine
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The A- and P-sites of the ribosome positions the aa-tRNA and peptidyl-tRNA such that a nucleophilic attack can occur between the amine group of the A-site aa-tRNA and the carbonyl group of the growing peptide chain on the P-site tRNA, resulting in the formation of a peptide bond. The carboxyl end of the peptide chain is uncoupled from the tRNA molecule in the P-site and forms a new peptide bond with the amino acid that is in the A-site. This process is illustrated below with: a peptidyl-tRNA with a growing peptide,a deacylated tRNA with an -OH and a ribosome with A,P and E sites to accommodate these three forms of tRNA.
Once the correct codon-anticodon match occurs between the mRNA and aa-tRNA, the decoding event triggers GTP hydrolysis on eEF1A. The resulting conformational change releases the aa-tRNA to the A-site, and GDP bound form of eEF1A is released from the ribosome. This process is illustrated below with: an amino acyl-tRNA with an amino acid,a peptidyl-tRNA with a growing peptide and a ribosome with A,P and E sites to accommodate these two forms of tRNA.
S-Adenosyl methionine <=> Decarboxylated-Adenosyl methionine + CO2
Once the correct codon-anticodon match occurs between the mRNA and aa-tRNA, the decoding event triggers GTP hydrolysis on eEF1A. The resulting conformational change releases the aa-tRNA to the A-site, and GDP bound form eEF1A is released from the ribosome. Insight into the mechanics of this system has been obtained from earlier works with rabbit reticulocytes and the E.coli system. This process is illustrated below with: an amino acyl-tRNA with an amino acid, a peptidyl-tRNA with a growing peptide and a ribosome with A,P and E sites to accommodate these two forms of tRNA.
gamma-butyrobetaine + alpha-ketoglutarate + O2 => carnitine + succinate + CO2
The eEF1B complex binds to eEF1A and regulates its activity by catalyzing the release of GDP. Subsequently, GTP is able to bind eEF1A allowing the formation of the ternary complex (eEF1A-GTP-aa-tRNA).In metazoans eEF1 protein family is composed of four subunits: eEF1A and eEF1B alpha, beta, and gamma (formerly EF-1alpha, EF-1beta, EF-1delta, and EF-1gamma, respectively). Both eEF1B alpha and eEF1B beta function as nucleotide exchange proteins. eEF1B gamma associates with eEF1B alpha and stimulates its exchange activity. This process is illustrated below with a GTP molecule in white and eEF1A protein in yellow.The three subunits of eEF1B are also shown.
gamma-butyrobetaine semialdehyde + NAD+ => gamma-butyrobetaine + NADH + H+
The mechanism of a peptide bond requires the movement of three protons. First the deprotonation of the ammonium ion generates a reactive amine, allowing a nucleophilic attack on the carbonyl group. This is followed by the loss of a proton from the reaction intermediate, only to be taken up by the oxygen on the leaving group (from the end of the amino acid chain bound to the tRNA in the P-site). The peptide bond formation results in the net loss of one water molecule, leaving a deacylated-tRNA in the P-site, and a nascent polypeptide chain one amino acid larger in the A-site. For the purpose of illustration, the figures used in the section show one amino acid being added to a peptidyl-tRNA with a growing peptide chain.
creatine + ATP => phosphocreatine + ADP [CK octamer]
At the beginning of this reaction, 1 molecule of 'eEF2', and 1 molecule of 'GTP' are present. At the end of this reaction, 1 molecule of 'eEF2:GTP' is present. This reaction takes place in the 'cytosol'.
creatine + ATP => phosphocreatine + ADP [CKB,CKM]
Following peptide bond formation, GTP-bound eEF2 catalyzes the translocation of the deacylated tRNA in the P-site and the peptidyl-tRNA in the A-site (the pre-translocation state) into the E- and P- sites (the post-translocation state), respectively. Thus, the mRNA advances by three bases to expose the next codon in the A-site. After translocation, GDP-bound eEF2 leaves the ribosome to allow another round of elongation. eEF2 is reactivated by the release of GDP and binds GTP for subsequent rounds. This process is illustrated below with a peptidyl-tRNA with a growing peptide, a deacylated tRNA with an -OH and a ribosome with A,P and E sites to accommodate these three forms of tRNA is also shown.
beta-hydroxy-trimethyllysine => gamma-butyrobetaine aldehyde + glycine
The translation elongation cycle adds one amino acid at a time to a growing polypeptide according to the sequence of codons found in the mRNA. The next available codon on the mRNA is exposed in the aminoacyl-tRNA (aa-tRNA) binding site (A site) on the 30S subunit. A: Ternary complexes of aa -tRNA:eEF1A:GTP enter the ribosome and enable the anticodon of the tRNA to make a codon/anticodon interaction with the A-site codon of the mRNA. B: Upon cognate recognition, the eEF1A:GTP is brought into the GTPase activating center of the ribosome, GTP is hydrolyzed and eEF1A:GDP leaves the ribosome. C: The peptidyl transferase center of ribosome catalyses the formation of a peptide bond between the incoming amino acid and the peptide found in the peptidyl-tRNA binding site (P site). D: In the pre-translocation state of the ribosome, the eEF2:GTP enters the ribosome, physically translocating the peptidyl-tRNA out of the A site to P site and leaves the ribosome eEF2:GDP. This action of eEF2:GTP accounts for the precise movement of the mRNA by 3 nucleotides.Consequently, deacylated tRNA is shifted to the E site. A ribosome associated ATPase activity is proposed to stimulate the release of deacylated tRNA from the E site subsequent to translocation (Elskaya et al., 1991). In this post-translocation state, the ribosome is now ready to receive a new ternary complex. This process is illustrated below with: an amino acyl-tRNA with an amino acid, a peptidyl-tRNA with a growing peptide, a deacylated tRNA with an -OH, and a ribosome with A,P and E sites to accommodate these three forms of tRNA.
trimethyllysine + alpha-ketoglutarate + O2 => beta-hydroxy-trimethyllysine + succinate + CO2
At the beginning of this reaction, 1 molecule of 'eEF1B alpha', 1 molecule of 'eEF1B gamma', and 1 molecule of 'eEF1B beta' are present. At the end of this reaction, 1 molecule of 'eEF1B complex' is present. This reaction takes place in the 'cytosol'.
Factor E:alpha tubulin and Factor D:beta tubulin interact with each other in a reversible reaction to form the complex (Factor E alpha tubulin:Factor D:beta tubulin) (Tian et al., 1997).
Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress
The factor B:alpha tubulin complex act as a reservoir capable of accepting or delivering alpha tubulin to cofactor E (Tian et al., 1997). In the reverse reaction, cofactor B may displace cofactor E in the cofactor E:alpha tubulin complex.
Alpha and beta tubulin folding intermediates are formed through ATP-dependent interaction with TriC/CCT. In order to form a functional heterodimer, these folding intermediates undergo a series of interactions with five proteins: (cofactors A-E) following release from TriC/CCT (reviewed in Cowan and Lewis et al., 2001). These interactions are described in the reactions below. Ultimately, alpha tubulin, when associated with cofactor E, interacts with cofactor D-bound beta-tubulin. The entry of cofactor C into this complex results in the discharge of native heterodimer triggered by GTP hydrolysis in beta tubulin (Tian et al., 1997).
Entry of cofactor C to the factor E:alpha tubulin: factor D:beta tubulin complex generates the active alpha:beta-supercomplex (Tian et al., 1997).
Mechanisms of type-I- and type-II-interferon-mediated signalling
Beta-tubulin folding intermediates generated via ATP-dependent interaction with TriC/CCT are captured by tubulin-specific chaperones A and D (TBCA and TBCD) (Tian et al. 1996, Tian et al. 1997) in a reversible reaction forming tubulin intermediate/cofactor complexes Factor A:beta tubulin or Factor D:beta tubulin. TBCD is involved in the tubulin-folding pathway, acting as a GTPase activating protein (GAP) for beta-tubulin. The ADP-ribosylation factor-like protein 2 (ARL2) is able to down-regulate TBCD specifically, thus preventing microtuble disruption (Bhamidipati et al. 2000, Tian et al. 2010).
The eukaryotic chaperonin TCP-1 ring complex (TRiC/ CCT) plays an essential role in the folding of a subset of proteins prominent among which are the actins and tubulins (reviewed in Altschuler and Willison, 2008). CCT/TRiC is an example of a type II chaperonin, defined (in contrast to type I) as functioning in the absence of a cochaperonin. TriC/CCT is a multisubunit toroidal complex that forms a cylinder containing two back-to-back stacked rings enclosing a cavity where substrate folding occurs in an ATP dependent process (reviewed in Altschuler and Willison, 2008 ). CCT/TriC contains eight paralogous subunits that are conserved throughout eukaryotic organisms (Leroux and Hartl 2000; Archibald et al. 2001; Valpuesta et al. 2002). CCT-mediated folding of non-native substrate protein involves capture through hydrophobic contacts with multiple chaperonin subunits followed by transfer of the protein into the central ring cavity where it folds. Although folding is initiated within this central cavity, only 5%-20% of proteins that are released have partitioned to the native state. The remaining portion is then recaptured by other chaperonin molecules (Cowan and Lewis 2001). This cycling process may be repeated multiple times before a target protein partitions to the native state. In the cell, binding to CCT occurs via presentation of target protein bound to upstream chaperones. During translation, the emerging polypeptide chain may be transferred from the ribosome to CCT via the chaperone Prefoldin (Vainberg et al., 1998) or the Hsp70 chaperone machinery (Melville et al., 2003). While the majority of CCT substrates ultimately partition to the native state as soluble, monomeric proteins, alpha and beta tubulin are unusual in that they require additional cofactors that are required to assemble the tubulin heterodimer (Cowan and Lewis 2001).
Quasi-native alpha-tubulin folding intermediates generated via ATP-dependent interaction with CCT (Tian et al., 1995) are captured in a reversible reaction by cofactors B and/or E (Tian et al., 1997), forming the tubulin intermediate/cofactor complexes Factor B:alpha tubulin or Factor E:alpha tubulin.
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CCT/TRiC facilitates folding of newly translated SK1 into its mature active form (Zebol et al., 2008)
TRiC has broad recognition specificities, but in the cell it interacts with only a defined set of substrates (Yam et al. 2008). Many of its substrates that are targeted during biosynthesis are conserved between mammals and yeast (Yam et al. 2008).
Nucleotide-independent transfer of beta-actin from prefoldin to CCT occurs when prefoldin binds to CCT (Vainberg et al., 1998). Following ATP- dependent folding within CCT (Gao et al., 1992), beta-actin is released as a soluble, monomeric protein.
TriC/CCT-mediated beta-actin folding involves rapid ATP-independent formation of a binary complex, followed by a slower ATP-dependent release of the native product (Gao et al., 1992). Group II chaperonins enclose substrate proteins following substrate binding through the formation of a "built- in" lid over the central cavity. Upon ATP binding, lid formation is triggered by the transition state of ATP hydrolysis (Meyer, et al., 2003).
The interaction between CCT and unfolded target proteins is thought to occur when CCT is in its ADP-bound state. ADP is then exchanged for ATP in CCT.
TriC/CCT forms a binary complex with unfolded alpha- or beta-tubulin (Frydman et al., 1992; Gao et al., 1993). The tubulin folding intermediates produced by TriC are unstable (Gao et al., 1993). Five additional protein cofactors (cofactor A-E) are required for the generation of properly folded alpha- and beta-tubulin and for the formation of alpha/beta-tubulin heterodimers (Gao et al., 1993) (Tian et al., 1997, Cowan and Lewis 2001).
Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors
Group II chaperonins enclose substrate proteins following substrate binding through the formation of a "built- in" lid over the central cavity. Upon ATP binding, lid formation is triggered by the transition state of ATP hydrolysis (Meyer, et al., 2003). In the case of CCT-mediated tubulin folding, one or more rounds of ATP hydrolysis are likely required before the association of non-exchangeable GTP with chaperonin-bound alpha tubulin.
Unfolded actins and tubulins bound to prefoldin are transferred to CCT via a docking mechanism (McCormack and Willison, 2001).
Unfolded actins and tubulins compete efficiently for binding to TriC/CCT and their chaperonin binding sites appear to be at least in part overlapping (Melki et al., 1993).
In the case of actin and tubulin folding, and perhaps other substrates, the emerging polypeptide chain is transferred from the ribosome to TRiC via Prefoldin (Vainberg et al., 1998).
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The LDL receptor locus in familial hypercholesterolemia: mutational analysis of a membrane protein
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During the synthesis of actin and tubulin, the nascent ribosome-associated chains bind to the heteromeric chaperone protein, prefoldin (PFD) (Hansen et al., 1999).
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LKB1 forms a complex with STRAD and MO25 thereby attaining a higher activity towards its substrates belonging to the subfamily of AMPK like kinases. LKB1:STRAD:MO25 complex phosphorylates AMPK constantly. This phosphorylation is immediately removed in basal conditions by PP2C, but if the cellular AMP:ATP ratio rises, binding of AMP by AMPK inhibits the dephosphorylation, and the maintained phosphorylation results in activation of the AMPK.
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Activated AMPK (phosphorylated on Thr172/Thr174 and AMP bound) phosphorylates Raptor on Ser 722 and Ser 792. These phosphorylations are required for inhibition of mTORC1 activity in response to energy stress (Gwinn DM et al, 2008).
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Upon formation of a trimeric LKB1:STRAD:MO25 complex, LKB1 phosphorylates and activates AMPK. If the AMP:ATP ratio rises, this activation is maintained and AMPK activates the TSC complex by phosphorylating TSC2. Active TSC activates the intrinsic GTPase activity of Rheb, resulting in GDP-loaded Rheb and inhibition of mTOR pathway.
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At the beginning of this reaction, 1 molecule of '3-phosphoinositide dependent protein kinase-1 ', and 1 molecule of 'Phosphatidylinositol-3,4,5-trisphosphate' are present. At the end of this reaction, 1 molecule of 'PIP3:PDK complex [plasma membrane]' is present. This reaction takes place in the 'cell'.
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PKB and PDK1 are activated via membrane-bound PIP3. Activated PDK1 phosphorylates PKB, which in turn phosphorylates PDE3B. The latter hydrolyses cAMP to 5'AMP, depleting cAMP pools.
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Ethylene is oxidized to Ethylene oxide by CYP1A1
11-deoxycorticosterone is oxidised to corticosterone by CYP11B2
The cytosolic AMPK complex is activated by phosphorylation. LKB1 phosphorylates AMPK heterotrimer on Thr174 of the alpha 1 subunit (or Thr172 on alpha 2 subunit) leading to activation of AMPK (if cellular AMP/ATP ratio is high) (Hawley SA et al, 2003; Woods A et al, 2003; Shaw RJ et al, 2004). Signals leading to this phosphorylation event can be mediated by exercise, leptin and adiponectin, the hypothalamic-sympathetic nervous system (SNS), and alpha adrenergic receptors, as demonstrated in studies of rat and human skeletal muscle (Minoksohi et al, 2002, Kahn et al, 2005). The details of AMPK activation in response to these stimuli will be annotated in the future. Nuclear AMPK may well be a substrate for LKB1 but, to date, there is no clear evidence for this.
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Upon complex formation with STRAD and MO25, LKB1 (also known as serine/threonine kinase 11, STK11) is mostly cytosolic. LKB1 attains 20x activity towards the substrates belonging to the subfamily of AMPK-like kinases (5'AMP-activated protein kinases).
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If AMP:ATP ratio rises, AMP (instead of ATP) is bound by the AMPK-gamma subunit, which inhibits the dephosphorylation of the AMPK-alpha subunit resulting in activation of AMPK. It is not clear, as of yet, whether AMP binds to unphosphorylated AMPK.
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Normally under low AMP:ATP conditions, the active AMPK is dephosphorylated (possibly by PP2C), and thus inactivated.
CYP3A7 can 6beta-hydroxylate testosterone
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Now with the complete receptor-ligand dissociation and subsequent degradation of insulin in the endosomal lumen, the endosomally associated protein tyrosine phosphatases (PTPs) complete the receptor dephosphorylation. So too are all the receptor substrates dephosphorylated leading to the collapse of the signalling complexes and signal attenuation.
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At the beginning of this reaction, 1 molecule of 'ATP', and 1 molecule of 'GRB2:SOS:SHC-P' are present. At the end of this reaction, 1 molecule of 'GRB2:SHC-P', 1 molecule of 'phospho-SOS', and 1 molecule of 'ADP' are present. This reaction takes place on the 'internal side of plasma membrane' and is mediated by the 'kinase activity' of 'ERK1'.
IRS is one of the mediators of insulin signalling events. It is activated by phosphorylation and triggers a cascade of events involving PI3K, SOS, RAF and the MAP kinases. The proteins mentioned under IRS are examples of IRS family members acting as indicated. More family members are to be confirmed and added in the future.
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Release of phospho-IRS from the insulin receptor triggers a cascade of signalling events via PI3K, SOS, RAF and the MAP kinases.
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Autophosphorylation of the insulin receptor triggers a series of signalling events, mediated by SHC or IRS, and resulting in activation of the Ras/RAF and MAP kinase cascades. A second effect of the autophosphorylation of the insulin receptor is its internalisation into an endosome, which downregulates its signalling activity.
Trimethylamine N-oxidised to Trimethylamine-N-oxide
FMO3 N-oxidizes the tertiary amine trimethylamine
At the beginning of this reaction, 1 molecule of 'PKB:PKB Regulator', and 1 molecule of 'Phosphatidylinositol-3,4,5-trisphosphate' are present. At the end of this reaction, 1 molecule of 'PKB regulator', and 1 molecule of 'PIP3:PKB complex ' are present. This reaction takes place in the 'cell'.
FMO2 S-oxidizes the antithyroid drug methimazole
acetate + CoA + ATP => acetyl-CoA + AMP + pyrophosphate [cytosolic]
acetaldehyde + NAD+ => acetate + NADH + H+ [mitochondrial]
SOS is recruited to the plasma membrane and mediates activation of Ras.
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FMO1 N-oxidizes the anti-cancer drug tamoxifen
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CYP3A43 catalyzes the 6beta-hydroxylation of testosterone
At the beginning of this reaction, 2 molecules of 'ATP', and 1 molecule of 'PIP3:PKB complex ' are present. At the end of this reaction, 1 molecule of 'PIP3:Phosphorylated PKB complex', and 2 molecules of 'ADP' are present. This reaction takes place on the 'plasma membrane' and is mediated by the 'kinase activity' of 'PIP3:PDK complex [plasma membrane]'.
Mast/stem cell growth factor receptor precursor
UDP-glucose is oxidised to UDP-glucuronate
Ras-related C3 botulinum toxin substrate 1
UDP-glucuronate transport from the cytosol to ER lumen
3,3'-diiodothyronine + PAPS => 3,3'-diiodothyronine 4-sulfate + PAP
3,5,3'-triiodothyronine + PAPS => 3,5,3'-triiodothyronine 4-sulfate + PAP
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glyoxylate + NADPH + H+ => glycolate + NADP+
Cystathionine is formed from homocysteine and serine
SAM is sythesized from methionine's reaction with ATP
Homocysteine is degraded to oxobutanoate and H2S
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Excess homocysteine yields homolanthionine and H2S
The Wnt receptor Ryk plays a role in mammalian planar cell polarity signaling
CSAD decarboxylates 3-sulfinoalanine to hypotaurine
Excess cysteine yields lanthionine and H2S
SQR oxidizes sulfide to bound persulfide
Persulfide sulfur is transferred onto sulfite
Sulfate is exported to the cytosol in exchange for dicarboxylate
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Iodide is taken up by thyroid epithelial cells
Noradrenaline is converted to adrenaline
Monoiodinated tyrosine can be deiodinated
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glycine + O2 => glyoxylate + H2O2 + NH4+
Decarboxylation of 5-hydroxytryptophan forms serotonin
glyoxylate + alanine => glycine + pyruvate [mitochondrial matrix]
glyoxylate + alanine => glycine + pyruvate [peroxisome]
DIT and MIT combine to form triiodothyronine
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Cell division control protein 42 homolog
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Diacylglycerol, when simplicity becomes complex
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Processing of alkylcobalamins in mammalian cells: A role for the MMACHC (cblC) gene product
New insights into the regulation of T cells by gamma(c) family cytokines
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B cell lymphoma 10 is essential for FcepsilonR-mediated degranulation and IL-6 production in mast cells
Transforming growth factor-beta receptor type I gene is frequently mutated in ovarian carcinomas
Isoleucylation properties of native human mitochondrial tRNAIle and tRNAIle transcripts. Implications for cardiomyopathy-related point mutations (4269, 4317) in the tRNAIle gene
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The molecular and fibrillar structure of collagen and its relationship to the mechanical properties of connective tissue
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Structure and physiologic function of the low-density lipoprotein receptor
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Reversible modification of adenomatous polyposis coli (APC) with K63-linked polyubiquitin regulates the assembly and activity of the ?-catenin destruction complex
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Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method
Acta Crystallogr Sect F Struct Biol Cryst Commun 61:346-9
Tankyrase inhibition stabilizes axin and antagonizes Wnt signalling
A single enzyme catalyzes both platelet-activating factor production and membrane biogenesis of inflammatory cells. Cloning and characterization of acetyl-CoA:LYSO-PAF acetyltransferase
Tiam1 regulates the Wnt/Dvl/Rac1 signaling pathway and the differentiation of midbrain dopaminergic neurons
Activation domains from both monomers contribute to transcriptional stimulation by sterol regulatory element-binding protein dimers
The forkhead transcription factor FOXM1 controls cell cycle-dependent gene expression through an atypical chromatin binding mechanism
The free radical nitric oxide (NO), produced by endothelial NO synthase (eNOS), is an important vasoactive substance in normal vascular biology and pathophysiology. It plays an important role in vascular functions such as vascular dilation and angiogenesis (Murohara et al. 1998, Ziche at al. 1997). NO has been reported to be a downstream mediator in the angiogenic response mediated by VEGF, but the mechanism by which NO promotes neovessel formation is not clear (Babaei & Stewart 2002). Persistent vasodilation and increase in vascular permeability in the existing vasculature is observed during the early steps of angiogenesis, suggesting that these hemodynamic changes are indispensable during an angiogenic processes. NO production by VEGF can occur either through the activation of PI3K or through a PLC-gamma dependent manner. Once activated both pathways converge on AKT phosphorylation of eNOS, releasing NO (Lin & Sessa 2006). VEGF also regulates vascular permeability by promoting VE-cadherin endocytosis at the cell surface through a VEGFR-2SrcVav2RacPAK signalling axis.
CDC42 is involved in the formation of filopodia with potential functions in guidance and migration in response to a VEGF gradient. CDC42 is activated downstream of VEGFR2 and involved in the formation of stress fibres by contributing to the activation of the p38 pathway. The activation of CDC42 may rely on FYN activity but the precise mechanism that leads to activation is not known (Lamalice et al. 2004, 2006).
Activated MAP kinase-activated protein kinase (MAPK/MAPKAPK) 2 and 3 in turn phosphorylate heat shock protein beta 1 (HSPB1, HSP27). HSP27 is an actin-capping protein. Its phosphorylation has been proposed to release it from actin filaments, thus allowing addition of actin monomers and elongation of filaments. Phosphorylation-induced conformational changes causes disaggregation of oligomeric complexes of HSP27 and subsequent disassociation from actin filaments, which may result in a higher rate of actin polymerization (Lamalice et al. 2007, Rousseau et al. 2000, Lavoie et al. 1995).
Protein kinase C (PKC) activation enhances angiogenesis by participating in the intracellular signaling of vascular endothelial growth factor (VEGF) in endothelial cells. VEGF can activate several PKC isoforms including alpha, beta, delta and zeta isoforms. Their activation is preceded by the activation of PLC gamma (Suzuma et al. 2002, Xia et al. 1996, Takahashi et al. 1999, Wellner et al. 1999). Before Protein kinase C (PKC) is competent to respond to second messengers it must first be phosphorylated at three conserved positions: the activation loop and two positions at the carboxyl terminus of the protein (Dutil et al. 1998). The phosphorylation of the activation loop appears to occur first and is mediated by phosphoinositide dependent protein kinases (PDKs). PDK1 phosphorylates PKCs at a critical Thr (T) residue in the activation loop, a requirement for PKC to gain catalytic competency (Toker 2003).
Activated PAK then phosphorylates a serene residue (S665) within a conserved motif in the cytoplasmic tail of VE-cadherin. VE-cadherin is also phosphorylated by c-Src in a manner dependent on TSAD (Sun et al. 2012, Lambeng et al. 2005). Serine-phosphorylated VE-cadherin recruits beta-arrestin 2 which promotes the internalization of VE-cadherin into clathrin-coated pits. This process leads to the disassembly of endothelial-cell junctions, resulting in the enhanced permeability of the blood-vessel wall (Gavard & Gutkind 2006).
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Angiogenesis is the formation of new blood vessels from preexisting vasculature. One of the most important proangiogenic factors is vascular endothelial growth factor (VEGF). VEGF exerts its biologic effect through interaction with transmembrane tyrosine kinase receptors VEGFR, selectively expressed on vascular endothelial cells. VEGFA signaling through VEGFR2 is the major pathway that activates angiogenesis by inducing the proliferation, survival, sprouting and migration of endothelial cells (ECs), and also by increasing endothelial permeability (Lohela et al. 2009, Shibuya & Claesson-Welsh 2006, Claesson-Welsh & Welsh, 2013). The critical role of VEGFR2 in vascular development is highlighted by the fact that VEGFR2-/- mice die at E8.5-9.5 due to defective development of blood islands, endothelial cells and haematopoietic cells (Shalaby et al. 1995).
PKC contains a N-terminal C2 like domain, a pseudosubstrate (PS), DAG binding (C1) domain and a C-terminal kinase domain. The PS sequence resembles an ideal substrate with the exception that it contains an alanine residue instead of a substrate serine residue. It is bound to the kinase domain in the resting state. As a result, PKC is maintained in a closed inactive state, inaccessible to cellular substrates. On stimulation of receptors there is an increase in intracellular calcium and diacylglycerol (DAG) levels which leads to the activation of PKC and its translocation from the cytosol to the plasma membrane. PKCs tether to the plasma membrane through DAG binding to the C1 domain. This confers a high-affinity interaction between PKC and the membrane, leading to a massive conformational change that releases the PS domain from the catalytic site, the system becomes both competent and accessible (Colon-Gonzalez & Kazanietz 2006).
After phosphorylation by PDK1, PKC undergoes autophosphorylation at two sites important for PKC activity, one in the turn motif (Thr-642 in PKCB) and the second in the hydrophobic phosphorylation motif (Ser-661 in PKCB). These phosphorylations render the enzyme catalytically competent but still inactive; diacylglycerol (DAG) and calcium are required for full activation.
VEGFR2 stimulates ERK not via GRB2-SOS-RAS, but via pY1175-dependent phosphorylation of PLC gamma and subsequent activation of PKCs. PKC plays an important mediatory role in the proliferative Ras/Raf/MEK/ERK pathway. PKC alpha can intersect the Ras/Raf/MEK/ERK cascade at the level of Ras (Clark et al. 2004) or downstream of Ras through direct phosphorylation of Raf (Kolch et al. 1993). VEGF stimulation leads to Ras activation in a Ras-guanine nucleotide exchange factor (GEF) independent mechanism. It rather relies on modulating the regulation of Ras-GTPase activating protein (GAP) than regulation of Ras-GEFS (Wu et al. 2003).
VEGF mediated activation of ERK1/2 depends on the activity of PKC. Sphingosine kinase 1 (SPHK1) has been identified as the connecting link between PKC and Ras activation. Activated SPHK1 does not activate Ras-GEF directly but rather modulates Ras-GAP activity to favour Ras activation. VEGF-mediated stimulation of SPHK1 results from the direct phosphorylation of SPHK1 by PKC (Shu et al. 2002). S225 in SPHK1 may be the target site of phosphorylation (Piston et al. 2003).
RHOA propagates downstream signals by binding to effector proteins such as Rho-associated, coiled-coil containing protein kinases (ROCKs). ROCKs consist of an amino-terminal kinase domain, followed by a Rho-binding domain (RBD) and a carboxy terminal cysteine-rich domain (CRD) located within the pleckstrin homology (PH) motif. RHOA:GTP interacts with the RBD domain and activates the phosphotransferase activity (Ishizaki et al. 1996, Amano et al. 2000).
The role of autophosphorylation sites on PDGF receptors are to provide docking sites for downstream signal transduction molecules which contain SH2 domains. The SH2 domain is a conserved motif of around 100 amino acids that can bind a phosphorylated tyrosine residue. These downstream molecules are activated upon binding to, or phosphorylated by, the receptor kinases intrinsic to PDGF receptors. Some of the dowstream molecules are themselves enzymes, such as phosphatidylinositol 3'-kinase (PI3K), phospholipase C (PLC-gamma), the Src family of tyrosine kinases, the tyrosine phosphatase SHP2, and a GTPase activating protein (GAP) for Ras. Others such as Grb2 are adaptor molecules which link the receptor with downstream catalytic molecules.
Platelet-derived Growth Factor (PDGF) is a potent stimulator of growth and motility of connective tissue cells such as fibroblasts and smooth muscle cells as well as other cells such as capillary endothelial cells and neurons.The PDGF family of growth factors is composed of four different polypeptide chains encoded by four different genes. The classical PDGF chains, PDGF-A and PDGF-B, and more recently discovered PDGF-C and PDGF-D. The four PDGF chains assemble into disulphide-bonded dimers via homo- or heterodimerization, and five different dimeric isoforms have been described so far; PDGF-AA, PDGF-AB, PDGF-BB, PDGF-CC and PDGF-DD. It is notable that no heterodimers involving PDGF-C and PDGF-D chains have been described. PDGF exerts its effects by binding to, and activating, two protein tyrosine kinase (PTK) receptors, alpha and beta. These receptors dimerize and undergo autophosphorylation. The phosphorylation sites then attract downstream effectors to transduct the signal into the cell.
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Increased PAK1-3 catalytic activity is associated with autophosphorylation of key residues, including one site in the regulatory portion (S144 in PAK1) and another in the so-called activation loop (T423 in PAK1).
Binding of Rac1 increases p21 activated kinases 1-3 (PAK1-3) kinase activity and breaks the PAK dimer into monomers.
Activated Rac1 binds to and stimulates the kinase activity of PAK1-3 (p21 activated kinases 1-3). PAK dimers are arranged in head-to-tail fashion, in which the kinase domain of one molecule is inhibited by the regulatory domain of the other molecule and vice versa. Binding of activated Rac1 breaks the PAK dimer and removes the trans-inhibition (Knaus et al. 1998, Parrini et al. 2002). PAK activated by Rac1 in turn phosphorylates VE-cadherin thereby promoting the beta-arestin-dependent endocytosis of VE-cadherin. This consequently disassemblies intracellular junctions leading to vascular permeability (Gavard & Gutkind 2006).
Tyrosine-phosphorylated VAVs act as guanine nucleotide exchange factors (GEFs) for RAC1, catalysing the exchange of bound GDP for GTP. RAC1 is a key regulator for actin cytoskeleton and cell migration and is also a critical component of endothelial NADPH oxidase (Wittmann et al. 2003, Tan et al. 2008, UshioFukai 2007, UshioFukai et al. 2002). Activated RAC1 then stimulates actin polymerisation to form lamellipodia through a number of proteins such as WASP-family veroprilin homologous protein (WAV). WAVE proteins stimulate the formation of a branched actin network by binding to the p21 subunit of the ARP2/3 nucleating complex, which is located on the sides of the pre-existing filaments.
Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15
Vav interacts directly with PIP2 and PIP3, with a fivefold selectivity for PIP3 over PIP2. PIP3 gives a twofold stimulation of Vav1 GEF activity while PIP2 leads to 90% inhibition. Binding probably occurs through the PH domain, known to bind phosphoinositides.
PI3-kinase (PI3K) catalyzes the phosphorylation of inositol phospholipids at the 3 position to generate phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 3,4-bisphosphate. PIP2 and PIP3 generated serve as lipid substrates where they recruit guanine nucleotide exchange factors (GEFs) like VAV (Proto-oncogene vav) that catalyze the exchange of GDP for GTP on Rac, activating it (Han et al. 1998). VAV2 acts downstream of VEGF to activate Rac1 (Garretta et al. 2007).
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MAP Kinases are inactivated by a family of protein named MAP Kinase Phosphatases (MKPs). They act through dephosphorylation of threonine and/or tyrosine residues within the signature sequence -pTXpY- located in the activation loop of MAP kinases (pT=phosphothreonine and pY=phosphotyrosine). MKPs are divided into three major categories depending on their preference for dephosphorylating; tyrosine, serine/threonine and both the tyrosine and threonine (dual specificity phoshatases or DUSPs). The tyrosine-specific MKPs include PTP-SL, STEP and HePTP, serine/threonine-specific MKPs are PP2A and PP2C, and many DUSPs acting on MAPKs are known. Activated MAP kinases trigger activation of transcription of MKP genes. Therefore, MKPs provide a negative feedback regulatory mechanism on MAPK signaling, by inactivating MAPKs via dephosphorylation, in the cytoplasm and the nucleus. Some MKPs are more specific for ERKs, others for JNK or p38MAPK.
ERK/MAPK kinases have a number of targets within the nucleus, usually transcription factors or other kinases. The best known targets, ELK1, ETS1, ATF2, MITF, MAPKAPK2, MSK1, RSK1/2/3 and MEF2 are annotated here.
MSK1 is required for the mitogen-induced phosphorylation of the transcription factor, cAMP response element-binding protein (CREB).
Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms
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Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
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CREB is phosphorylated at Serine 133 by RSK1/2/3.
Cyclic-AMP-dependent transcription factor 1 (ATF1) can be phosphorylated at Serine 63 by MSK1, thus activating it.
Nerve growth factor (NGF) activates multiple signalling pathways that mediate the phosphorylation of CREB at the critical regulatory site, serine 133. CREB phosphorylation at serine 133 is a crucial event in neurotrophin signalling, being mediated by ERK/RSK, ERK/MSK1 and p38/MAPKAPK2 pathways. Several kinases, such as MSK1, RSK1/2/3 (MAPKAPK1A/B/C), and MAPKAPK2, are able to directly phosphorylate CREB at S133. MSK1 is also able to activate ATF (Cyclic-AMP-dependent transcription factor). However, the NGF-induced CREB phosphorylation appears to correlate better with activation of MSK1 rather than RSK1/2/3, or MAPKAPK2. In retrograde signalling, activation of CREB occurs within 20 minutes after neurotrophin stimulation of distal axons.
p38 MAPK activation leads to CREB Serine 133 phosphorylation through the activation of MAPKAP kinase 2 or the closely related MAPKAP kinase 3.
Trk receptors signal from the plasma membrane and from intracellular membranes, particularly from early endosomes. Signalling from the plasma membrane is fast but transient; signalling from endosomes is slower but long lasting. Signalling from the plasma membrane is annotated here. TRK signalling leads to proliferation in some cell types and neuronal differentiation in others. Proliferation is the likely outcome of short term signalling, as observed following stimulation of EGFR (EGF receptor). Long term signalling via TRK receptors, instead, was clearly shown to be required for neuronal differentiation in response to neurotrophins.
An important function of the kinase cascade triggered by neurotrophins is to induce the phosphorylation and activation of transcription factors in the nucleus to initiate new programs of gene expression. Transcription factors directly activated by neurotrophin signalling are responsible for induction of immediate-early genes, many of which are transcription factors. These in turn are involved in the induction of delayed-early genes.
Self-assembly of basement membrane collagen
Neurotrophins (NGF, BDNF, NT-3, NT-4/5) play pivotal roles in survival, differentiation, and plasticity of neurons in the peripheral and central nervous system. They are produced, and secreted in minute amounts, by a variety of tissues. They signal through two types of receptors: TRK tyrosine kinase receptors (TRKA, TRKB, TRKC), which specifically interact with the different neurotrophins, and p75NTR, which interacts with all neurotrophins. TRK receptors are reported in a variety of tissues in addition to neurons. p75NTRs are also widespread. Neurotrophins and their receptors are synthesized as several different splice variants, which differ in terms of their biological activities. The nerve growth factor (NGF) was the first growth factor to be identified and has served as a model for studying the mechanisms of action of neurotrophins and growth factors. The mechanisms by which NGF generates diverse cellular responses have been studied extensively in the rat pheochromocytoma cell line PC12. When exposed to NGF, PC12 cells exit the cell cycle and differentiate into sympathetic neuron-like cells. Current data show that signalling by the other neurotrophins is similar to NGF signalling.
Type XIX collagen purified from human umbilical cord is characterized by multiple sharp kinks delineating collagenous subdomains and by intermolecular aggregates via globular, disulfide-linked, and heparin-binding amino termini
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On phosphorylation, ERK5 translocates to the nucleus.
The location of neurotrophin stimulation appears to determine the nature of the transcriptional response through differential uses of individual MAP kinases. The ERK5 pathway has a unique function in retrograde signalling; in contrast, ERK1/2, which mediate nuclear responses following direct cell body stimulation, does not transmit a retrograde signal. Following neurotrophin stimulation of distal axons, phosphorylated TRK receptors are endocytosed and transported to the cell bodies, where MEK5 phosphorylates ERK5, leading to ERK5 nuclear translocation, phosphorylation of transcription factors, and neuronal survival. In contrast, neurotrophin stimulation of the cell bodies causes concurrent activation and nuclear transport of ERK1/2 as well as ERK5. Several distinctive features of the ERK5 pathway might be important for retrograde signalling. The ERK5 cascade does not depend on activation of the G-protein RAS. Instead, this pathway may use other G-proteins such as RAP that are associated with vesicles, or may not require any G-protein intermediate. Another distinctive feature is that the MEK5 isoform, which is expressed in the nervous system, exhibits a punctate staining pattern, suggesting a vesicular localization. ERK5 itself significantly differs from ERK1/2, and its substrate specificity also differs from ERK1/2. For instance, ERK5 directly activates transcription factors, including MEF2, that are not phosphorylated by ERK1/2. Conversely, ERK1/2, but not ERK5, activate transcription factors such as ELK1 and MITF.
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The biology of cyclic GMP-dependent protein kinases
MSK1 (Ribosomal protein S6 kinase alpha-5) is a serine/threonine kinase that is localised in the nucleus. It contains two protein kinase domains in a single polypeptide. It can be activated 5-fold by ERK1/2 through phosphorylation at four key residues.
Following translocation to the nucleus, ERK1/2 directly phosphorylates key effectors, including the ubiquitous transcription factors ELK1 (Ets like protein 1). At least five residues in the C terminal domain of ELK1 are phosphorylated upon growth factor stimulation. ELK1 can form a ternary complex with the serum response factor (SRF) and consensus sequences, such as serum response elements (SRE), on DNA, thus stimulating transcription of a set of immediate early genes like c fos.
Neurotrophin-TRK complexes can be internalized and enter signalling vesicles, which travel retrogradely over long distances from distal nerve terminals to neuronal cell bodies. Such retrograde signalling by neurotrophin-TRK complexes regulates survival, synaptogenesis and maintenance of proper neural connectivity. The neurotrophin-TRK complex may use three distinct internalization pathways. Although Clathrin-mediated endocytosys appears to be the major internalization route, it is controversial whether it also represents the dominant pathway for retrograde transport and signalling. Pyncher-mediated endocytosis might be more relevant in this regard. Moreover, also caveolin-mediated endocytosis may play a role in NGF-TrkA internalization. Retrograde transport of TRKs is microtubule-dependent: TRKs remain activated and bound to neurotrophins during retrograde transport. The current view is reflected in the signalling endosome model. It is a specialized vesicle containing ligand (NGF, BDNF) bound to its activated TRK receptor, together with activated downstream signalling proteins, transported by motor proteins (dyneins) from nerve terminals to remote cell bodies, where the receptors trigger signalling cascades.
Of the internalized NGF:TRK complexes, many undergo recycling and/or proteolysis. Only a small fraction is retrogradely transported. Vesicles containing neurotrophin, activated receptors and downstream kinases are transported through axons by the action of dynein, which produces a force towards the end of microtubules.
Over 10 dual specificity phosphatases (DUSPs) active on MAP kinases are known. Among them, some possess good ERK docking sites and so are more specific for the ERKS (DUSP 3, 4, 6, 7), others are more specific for p38MAPK (DUSP1 and 10), while others do not seem to discriminate. It is noteworthy that transcription of DUSP genes is induced by growth factor signaling itself, so that these phosphatases provide feedback attenuation of signaling. Moreover, differential activation of DUSPs by different stimuli is thought to contribute to pathway specificity.
ERKs are inactivated by the protein phosphatase 2A (PP2A). The PP2A holoenzyme is a heterotrimer that consists of a core dimer, composed of a scaffold (A) and a catalytic (C) subunit that associates with a variety of regulatory (B) subunits. The B subunits have been divided into gene families named B (or PR55), B0 (or B56 or PR61) and B00 (or PR72). Each family comprises several members. B56 family members of PP2A in particular, increase ERK dephosphorylation, without affecting its activation by MEK. Induction of PP2A is involved in the extracellular signal-regulated kinase (ERK) signalling pathway, in which it provides a feedback control, as well as in a broad range of other cellular processes, including transcriptional regulation and control of the cell cycle.This diversity of functions is conferred by a diversity of regulatory subunits, the combination of which can give rise to over 50 different forms of PP2A. For example, five distinct mammalian genes encode members of the B56 family, called B56a, b, g, d and e, generating at least eight isoforms. Whether a specific holoenzyme dephosphorylates ERK and whether this activity is controlled during mitogenic stimulation is unknown.
The MEF2 (Myocyte-specific enhancer factor 2) proteins constitute a family of transcription factors: MEF2A, MEF2B, MEF2C, and MEF2D. MEF2A and MEF2C are known substrates of ERK5, and their transactivating activity can be stimulated by ERK5 via direct phosphorylation. MEF2A and MEF2C are expressed in developing and adult brain including cortex and cerebellum.
MSK1 (Ribosomal protein S6 kinase alpha-5) is a serine/threonine kinase that is localised in the nucleus. It contains two protein kinase domains in a single polypeptide. It can be activated 5-fold by p38MAPK through phosphorylation at four key residues.
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C3G is a guanine nucleotide exchange factor for Rap1, which is recruited by Crk adaptor proteins.
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abacavir [cytosol] + ATP + H2O => abacavir[extracellular] + ADP + phosphate
Neurotrophins utilize multiple pathways to activate ERKs (ERK1 and ERK2), a subgroup of the large MAP kinase (MAPK) family, from the plasma membrane. The major signalling pathways to ERKs are via RAS, ocurring from caveolae in the plasma membrane or from clathrin-coated vesicles, and via RAP1, taking place in early endosomes. Whereas RAS activation by NGF is transient, RAP1 activation by NGF is sustained for hours.
abacavir monophosphate + H2O => carbovir monophosphate + cyclopropylamine
Deamination of abacavir monophosphate to form carbovir monophosphate
The activation of phosphlipase C-gamma (PLC-gamma) and subsequent mobilization of calcium from intracellular stores are essential for neurotrophin secretion. PLC-gamma is activated through the phosphorylation by TrkA receptor kinase and this form hydrolyses PIP2 to generate inositol tris-phosphate (IP3) and diacylglycerol (DAG). IP3 promotes the release of Ca2+ from internal stores and this results in activation of enzymes such as protein kinase C and Ca2+ calmodulin-regulated protein kinases.
Carbonic anhydrase IV dehydrates bicarbonate to water and carbon dioxide
Several guanine exchange factors (GEFs) for the Rho family of GTPases contain PH domains that bind to PIP3. RhoA protein activation is a mechanism whereby PI3K acts independently of AKT.
Cross-talk between the endocytic pathway and the endoplasmic reticulum in cross-presentation by MHC class I molecules
OCT (organic cation transporter)-mediated abacavir uptake
abacavir [extracellular] => abacavir [cytosol]
PI3K/AKT signalling is a major regulator of neuron survival. It blocks cell death by both impinging on the cytoplasmic cell death machinery and by regulating the expression of genes involved in cell death and survival. In addition, it may also use metabolic pathways to regulate cell survival.The PI3K/AKT pathway also affects axon diameter and branching (Marcus et al, 2002) and regulates small G proteins like RhoA (Vanhaesebroeck, B and Waterman, MD, 1999), which control the behaviour of the F-actin cytoskeleton. Moreover, through its connection with the TOR pathway, it promotes translation of a subset of mRNAs.
carbovir diphosphate + ATP => carbovir triphosphate + ADP
Rap1 is a small G protein, necessary for prolonged ERK activity in PC12 cells. In such cells, NGF triggers a program of neuronal differentiation through the activation of a Rap1:B-RAF:ERK module Rap1 is activated by NGF, but not by epidermal growth factor (EGF), although both growth factors cause transient activation of RAS. Activation of Rap1 by NGF requires internalization of TRKA to intracellular vesicles, mostly endosomes, containing Rap1, B-RAF, MEK and ERKs. Rap1 does not co-localize with RAS. Therefore, the ability of Rap1 to bind RAF-1 without activating it might sequester RAF-1 from RAS. Activation of GEFs that couple to Rap1 as well as RAS might provide a mechanism to limit signals to RAS.
Carbonic anhydrase hydrates carbon dioxide (cytosol)
Rap1 binds to B-RAF; as a consequence, B-RAF is recruited to endosomes. The binding event of Rap1 to B-RAF is thought to be very similar to the binding of RAS to RAF-1. In neuronal cells that express B-Raf, NGF induced activation of Rap1 promotes a sustained activation of ERKs and is required for the induction of electrical excitability and a subset of neuron-specific genes. As regards morphological differentiation (e. g. neurite outgrowth in PC12 cells), things are more complex. The transient activation of ERKs via RAS is not sufficient for neurite outgrowth in the absence of additional signals. On the contrary, constitutive activation of Rap1 is sufficient to trigger neurite outgrowth, but it is not necessary for this response. Clearly, morphological differentiation of PC12 cells involves the activation of multiple pathways by NGF. Rap1 activates B-Raf, but inhibits RAF-1. Consequently, Rap1 could have two opposing functions: to limit ERK activation in B-RAF-negative cells and to increase ERK activation in B-Raf-positive cells.
carbovir + IMP => carbovir monophosphate + inosine
Conversion of carbovir to carbovir monophosphate
ARMS (Ankyrin-Rich Membrane Spanning/Kidins 220) is a 220kD tetraspanning adaptor protein which becomes rapidly tyrosine phosphorylated by active Trk receptors. ARMS is another adaptor protein which is involved in the activation of Rap1 and the subsequent prolonged activation of the MAPK cascade.
carbovir monophosphate + ATP => carbovir diphosphate + ADP
Phosphorylation of carbovir monophosphate
After NGF binding, activated Trk receptors provide multiple docking sites for adaptor proteins and enzymes. Two docking proteins, the Ankyrin-Rich Membrane Spanning protein (ARMS/Kidins220) and Fibroblast growth factor receptor substrate 2 (Frs2), target signaling molecules in response to NGF stimulation and link receptor activation with the MAP kinase (also called the Extracellular signal-Regulated Kinase cascade, ERK) cascade, an essential process for growth factor-induced cell proliferation and differentiation. A feature of NGF signaling is the sustained activation of the MAPK cascade. This is achieved by the small G protein, Rap1 which binds to and activates B-Raf, an activator of the MAPK cascade. Rap1 is a member of the Ras family of G proteins and like all G proteins, Rap1 is in an inactive state when bound to GDP and is active when bound to GTP. A specific GEF (guanine nucleotide exchange factor) called C3G can activate Rap1 by exchanging GDP for GTP.
Band 3 Anion Exchanger (AE1, SLC4A1) exchanges cytosolic chloride for extracellular bicarbonate
Extracellular signal-regulated kinase 5 (ERK5) is a member of the mitogen-activated protein kinase family. ERK5 is twice the size of the ERK1/2, containing a conserved amino terminal kinase domain that is 53% identical to ERK1/2, and a unique carboxyterminal region which contains potential binding sites for signalling molecules such as CRK, PI3 kinase and SRC. The second proline-rich region may interact with actin, targeting the kinase to a specific location in the cell. In contrast to ERK1 and ERK2, which are activated by neurotrophins (NTs), cAMP, and neuronal activity in neurons, ERK5 appears to be activated only by neurotrophins. The small GTPase Rap1 and the MEKK2 or MEKK3 kinases are critical upstream signaling molecules mediating neurotrophin stimulation of ERK5 in neurons. MEKK2 or MEKK3 activate MEK5, which appears to be localised in intracellular vesicles. MEK5 then activates ERK5. Once phosphorylated, ERK5 translocates to the nucleus.
Carbonic anhydrase I/II dehydrates bicarbonate
N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: a novel enzyme of the beta-lactamase fold family releasing anandamide and other N-acylethanolamines
Band 3 Anion Exchanger (AE1, SLC4A1) exchanges cytosolic bicarbonate for extracellular chloride
ACY:Zn2+ dimers hydrolyse mercapturic acids
Mitoferrin translocates iron from the mitochondrial intermembrane space to the mitochondrial matrix
RIT and RIN are two small guanine nucleotide binding proteins that share more than 50% sequence identity with RAS, including highly conserved core effector domains. Unlike RAS, the C termini of RIT and RIN lack a typical prenylation motif (CAAX, XXCC, or CXC) required for the association of RAS proteins with the plasma membrane. RIT is expressed in all tissues, whereas RIN is neuron-specific. They have similar signalling properties and are activated by NGF through unknown exchange factors. They signal to ERKs and p38 MAP kinase. They mainly lead to p38 activation via the BRAF-MEK kinase cascade.
Error-prone DNA polymerases: novel structures and the benefits of infidelity.
NGF induces sustained activation of p38, a member of the MAPK family (Morooka T, Nishida E, 1998). Both p38 and the ERKs appear to be involved in neurite outgrowth and differentiation caused by NGF in PC12 cells. As a matter of fact, PC12 cell differentiation appears to involve activation of both ERK/MAPK and p38. Both ERK/MAPK and p38 pathways contribute to the phosphorylation of the transcription factor CREB and the activation of immediate-early genes (Xing J, 1998). p38 activation by NGF may occur by at least two mechanisms, involving SRC or MEK kinases.
FXN:NFS1:ISD11:ISCU assembles iron-sulfur cluster
Signalling through Shc adaptor proteins appears to be identical for both NGF and EGF. It leads to a fast, but transient, MAPK/ERK activation, which is insufficient to explain the prolonged activation of MAPK found in NGF-treated cells.
Carbonic anhydrase IV hydrates carbon dioxide to bicarbonate and a proton
p38 MAPK is known to activate the Ser/Thr protein kinase MAPKAP kinase 2 and a closely related kinase, MAPKAP kinase 3, through phosphorylation at multiple sites. According to some authors, NGF does not induce any significant activation of MAPKAPK2 activity in PC12 cells. Potential p38 signaling effectors include transcription factors, such as cAMP-response element-binding protein and MEF2, cytoskeleton modulators, and a number of protein kinases. After activation, MAPKAP kinase 2 and 3 move to the nucleus.
Carbonic anhydrase I/II hydrates carbon dioxide
Activated p38 MAPK has been shown to phosphorylate and activate Ser/Thr protein kinase MAP kinase-activated protein kinase 2 (MAPK2/MAPKAPK2) and a closely related kinase, MAPK3. MAPK2 is phosphorylated on T222, S272, and T334 (Ben-Levy et al. 1995). MAPK3 shows 75% sequence identity to MAPK2 and, like MAPK2, is phosphorylated by p38 but the exact phosphorylation sites are not determined.
The adaptor protein Frs2 (Fibroblast growth factor receptor substrate 2) can mediate the prolonged activation of the MAPK (ERK) cascade.
GGTs hydrolyse glutamate from AFXBO-SG, AFNBO-SG
Phosphorylation of ARMS by Trk receptor (on tyrosine 1096) enables ARMS to recruit Crk via it's SH2 domain and freeing the SH3 domain. The SH3 domain of Crk is then free to bind C3G for MAP kinase activation.
Concerted evolution of human amylase genes
Aflatoxin B1 oxidized to Aflatoxin-8,9-oxide
CYP1A2,3A4,3A5,2A13 oxidise AFB1 to AFXBO
In certain cell types, ligand binding to p75NTR leads to ceramide production, which can mediate either cell survival (e.g. in noecotical subplate neurons) or apoptosis (e.g. in oligodendrocytes). Low levels of ceramide are also able to stimulate axonal outgrowth in hippocampal neurons.
5-oxoproline can be formed from gamma-glutamyl-AA products
RhoA is activated by guanine nucleotide exchange factors (RhoGEF), exchanging GDP for GTP. RHOA, activated following binding of MDGIs to the NgR:p75NTR complex, rigidifies the actin cytoskeleton, thereby inhibiting axonal elongation and causing growth cone collapse.
GST dimers conjugate GSH with cytosolic substrates
Glutathione conjugation of cytosolic substrates
p75NTR can also form a receptor complex with the Nogo receptor (NgR). Such complexes mediates axonal outgrowth inhibitory signals of MDGIs (myelin-derived growth-inhibitors), such as Nogo66, myelin-associated glycoprotein (MAG), and oligodendrocyte myelin glycoprotein (OMGP).
gamma-glutamylcysteine combines with glycine to form glutathione
p75NTR modulates axonal growth by regulating the activity of small GTPases like RHOA and RHOB, that control the state of actin polymerization. The best studied is RHOA. In its active, GTP-bound form, RHOA rigidifies the actin cytoskeleton, thereby inhibiting axonal elongation and causing growth cone collapse. Depending on the ligand that binds to it, p75NTR can either promote or inhibit axonal growth, Neurotrophin binding leads to inhibition of RHOA activity and axonal growth. Axonal growth inhibition is caused by myelin molecules named MDGIs (myelin-derived growth inhibitors), such as NOGO, MAG, OMGP. MDGIs bind to a complex made up of p75NTR and the NOGO receptor, causing RHOA activation and axonal growth inhibition.
Besides signalling through the tyrosine kinase receptors TRK A, B, and C, the mature neurotrophins NGF, BDNF, and NT3/4 signal through their common receptor p75NTR. NGF binding to p75NTR activates a number of downstream signalling events controlling survival, death, proliferation, and axonogenesis, according to the cellular context. p75NTR is devoid of enzymatic activity, and signals by recruiting other proteins to its own intracellular domain. p75 interacting proteins include NRIF, TRAF2, 4, and 6, NRAGE, necdin, SC1, NADE, RhoA, Rac, ARMS, RIP2, FAP and PLAIDD. Here we annotate only the proteins for which a clear involvement in p75NTR signalling was demonstrated. A peculiarity of p75NTR is the ability to bind the pro-neurotrophins proNGF and proBDNF. Proneurotrophins do not associate with TRK receptors, whereas they efficiently signal cell death by apoptosis through p75NTR. The biological action of neurotrophins is thus regulated by proteolytic cleavage, with proforms preferentially activating p75NTR, mediating apoptosis, and mature forms activating TRK receptors, to promote survival. Moreover, the two receptors are utilised to differentially modulate neuronal plasticity. For instance, proBDNF-p75NTR signalling facilitates LTD, long term depression, in the hippocampus (Woo NH, et al, 2005), while BDNF-TRKB signalling promotes LTP (long term potentiation). Many biological observations indicate a functional interaction between p75NTR and TRKA signaling pathways.
Cleavage of 5-oxoproline to form glutamate
Adenosine, acting through A2A receptors can induce TrkA activation. The mechanism of this activation is not understood.
Formation of 5-oxoproline from gamma-glutamylcysteine
TRK receptors can also be activated by at least two G-protein-coupled receptors (GPCR), the adenosine A2a receptor and the PACAP type I receptor, without involvement of neurotrophins. Activity of both receptors is mediated by G proteins that activate adenyl cyclase. How this leads to TRKA activation has not been fully elucidated, although a SRC-family tyrosine kinase and intracellular Ca2+ appear to play a role. TRKA activation through GPCRs occurs with slow kinetics (over 1 hr adenosine or PACAP treatment is required) in an intracellular location (probably the Golgi apparatus), and requires transcriptional and protein synthesis events that may influence the processing and activation of the receptors. GPCR-mediated transactivation of TRK receptors causes the preferential activation of AKT versus ERKs. This leads to a cell survival response.
Trk receptors can either be activated by neurotrophins or by two G-protein-coupled receptors (GPCRs) although the biological relevance of GPCRs remains to be shown.
Besides the RAF kinase, RAS can activate several ral guanine nucleotide dissociation stimulators (RALGDSs). Binding of RALGDS with RAS competes with RAF binding to RAS.
The Ras-related protein, RAL becomes activated once GDP is replaced by GTP.
S-atom dealkylation of 6-methylmercaptopurine
Adenosine 3',5'-bisphosphate (PAP) + H2O => AMP + orthophosphate
estrone + PAPS => estrone 3-sulfate + PAP
The effect of the proton pump is to allow entry of [H+] ions into the lumen of the endosome. The net effect of this is to lower the pH of the lumen from pH 7.4 (the pH at the plasma membrane) to pH 6.0 (documented with studies using FITC-labeled insulin - a pH dependent fluorescence marker).
dehydroepiandrosterone (DHEA) + PAPS => DHEA sulfate + PAP
The endosome fuses with the plasma membrane allowing the insulin receptor to re-integrate there. Any degraded insulin remnants which remained in the endosome are also expelled (The majority having been excreted into the cytoplasm and secreted out of the cell via other mechanisms). The cycle is complete with the dephosphorylated receptor now back in the plasma membrane available to bind the next insulin molecule presented to it. There is some insulin receptor degradation over time when damaged insulin receptors are not recycled but fuse instead with the lysosomes where they are degraded. However the majority of insulin receptors are recycled back to the plasma membrane with greater than 95% efficiency.
lithocholate + PAPS => lithocholate sulfate + PAP
taurolithocholate + PAPS => taurolithocholate sulfate + PAP
Following NGF binding, p75NTR activates the RAC (Ras-related C3 botulinum toxin substrate) GTPase.
cholesterol + PAPS => cholesterol sulfate + PAP
RAC activation was described as essential for p75NTR to induce JNK and apoptosis in cortical oligodendrocytes. The simultaneous activation of TRKA counteracts the apoptotic action of p75, by modulating the kinetics of p75-mediated RAC activation.
27-hydroxycholesterol + PAPS => 27-hydroxycholesterol 3-sulfate + PAP
Triggered by acidification of the endosome, insulin dissociates from the receptor and is degraded. The receptor is dephosphorylated and re-integrated into the plasma membrane, ready to be activated again by the binding of insulin molecules.
pregnenolone + PAPS => pregnenolone sulfate + PAP
Insulin binding to its receptor results in receptor autophosphorylation on tyrosine residues and the tyrosine phosphorylation of insulin receptor substrates (e.g. IRS and Shc) by the insulin receptor tyrosine kinase. This allows association of IRSs with downstream effectors such as PI-3K via its Src homology 2 (SH2) domains leading to end point events such as Glut4 (Slc2a4) translocation. Shc when tyrosine phosphorylated associates with Grb2 and can thus activate the Ras/MAPK pathway independent of the IRSs. Signal transduction by the insulin receptor is not limited to its activation at the cell surface. The activated ligand-receptor complex initially at the cell surface, is internalised into endosomes itself a process which is dependent on tyrosine autophosphorylation. Endocytosis of activated receptors has the dual effect of concentrating receptors within endosomes and allows the insulin receptor tyrosine kinase to phosphorylate substrates that are spatially distinct from those accessible at the plasma membrane. Acidification of the endosomal lumen, due to the presence of proton pumps, results in dissociation of insulin from its receptor. (The endosome constitutes the major site of insulin degradation). This loss of the ligand-receptor complex attenuates any further insulin-driven receptor re-phosphorylation events and leads to receptor dephosphorylation by extra-lumenal endosomally-associated protein tyrosine phosphatases (PTPs). The identity of these PTPs is not clearly established yet. A discussion of candidates will be added in the near future.
p75NTR is a key regulator of neuronal apoptosis, both during development and after injury. Apoptosis is triggered by binding of either mature neurotrophin or proneurotrophin (proNGF, proBDNF). ProNGF is at least 10 times more potent than mature NGF in inducing apoptosis. TRKA signalling protects neurons from apoptosis. The molecular mechanisms involved in p75NTR-apoptosis are not well understood. The death signalling requires activation of c-JUN N-terminal Kinase (JNK), as well as transcriptional events. JNK activation appears to involve the receptor interacting proteins TRAF6, NRAGE, and Rac. The transcription events are thought to be regulated by another p75-interacting protein, NRIF. Two other p75-interacting proteins, NADE and Necdin, have been implicated in apoptosis, but their role is less clear.
Sphingomyielinase promotes the conversion of sphingomyelin to ceramide. Ceramide can activate JNK and other targets. The molecular details of the p75NTR-activated ceramide signalling cascade are only partially understood.
The different molecules listed (NRAGE, NRIF, NADE, TRAF6) mediate, through unclear mechanisms, JNK activation by threonine and tyrosine phosphorylation. While active JNK does move to the nucleus and phosphorylates and activate transcription factors such as c-JUN and ATF2, these have not been implicated in p75-mediated cell death, but rather the direct activation of the cell death machinery by JNK has been implicated. p75 activates the intrinsic caspase pathway (involving mitochondrial release of cytochrome c, Apaf-1, and caspases-9) rather than the extrinsic (caspase-8) pathway activated by most other death receptors.
Once bound by either NGF or proNGF, p75NTR interacts with NRAGE, thus leading to phosphorylation and activation of JUN Kinase (JNK). JNK controls apoptosis in two ways: it induces transcription of pro-apoptotic genes, and directly activates the cell death machinery. Only NGF-bound p75NTR is shown here.
Activation of Ca impermeable AMPA receptors
Ca impermeable AMPA receptor ligand binding
Multiple Gi protein subtypes regulate a single effector mechanism
Activation of Ca permeable AMPA receptors
NMD: RNA biology meets human genetic medicine
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Mutant human adenosine deaminase alleles and their expression by transfection into fibroblasts
Plasma membrane adapto AP-2 17 kDa protein
Adaptor protein complex AP-2 subunit sigma
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Membrane depolarization upon activation of Ca impermeable AMPA receptors
Adaptor protein complex 2 (AP-2) large adaptins
Phosphorylation of CREB by ribosomal protein S6 kinase
GABR heteropentamers:GABA transport Cl- from extracellular region to cytosol
Activation of Ca-permeable Kainate receptors
G alpha-olf:GTP binds to Gi alpha1:GTP:adenylate cyclase complex
Adenylate cyclase increases the GTPase activity of G alpha-olf
Activation of Ca2+ activated Potassium channels with Intermeidtance conductance
GABRR pentamer:GABA transports extracellular Cl- to cytosol
Regulation of collagen fibril nucleation and initial fibril assembly involves coordinate interactions with collagens V and XI in developing tendon
Activation of Ca2+ activated Potassium channels with small conductance
Adenylate cyclase increases the GTPase activity of Gi alpha
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Dissociation of the Gi alpha:G olf complex
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Structural biology of shared cytokine receptors
Activation of Potassium transport channels
KCNJs transport K+ from cytosol to extracellular region
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Carbonic anhydrase hydrates carbon dioxide (mitochondria)
Carbonic anhydrase dehydrates bicarbonate (plasma membrane)
Carbonic anhydrase hydrates carbon dioxide (plasma membrane)
Carbonic anhydrase dehydrates bicarbonate (cytosol)
Carbonic anhydrase VI dehydrates bicarbonate to water and carbon dioxide
Carbonic Anhydrase VI hydrates carbon dioxide to bicarbonate and a proton
Carbonic anhydrase dehydrates bicarbonate (mitochondria)
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KDM1A, KDM1B demethylate MeK5/Me2K5 histone H3
KAT6A, KAT6B-containing ING5 complexes acetylate replicative histone H3
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KDM2A, KDM2B, KDM4A demethylate MeK37/Me2K37 histone H3
KDM5A-D demethylate Me2K5/Me3K5 histone H3
KDM4A, KDM4B, KDM4C, KDM4D demethylate Me2K10/Me3K10 histone H3
CDK4 in CCND1:CDK4:PRMT5:WDR77 phosphorylates WDR77
KDM6A, KDM6B, KDM7A demethylate Me2K28/Me3K28 histone H3
PRMT5:WDR77, PRMT7 methylate histone H3 arginine-3 (H3R2)
CCND1:CDK4:PRMT5:pT5-WDR77 methylates histone H3 arginine-9 (H3R8)
WDR5 binds Me2sR3-replicative histone H3
RBBP7 binds histone H3 arginine-3 (H3R2).
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Loading of dopamine into synaptic veiscles
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loading of Serotonin in synaptic vesicles
Conversion of GABA to Succinate Semialdehyde
GAT1-3 mediate Na+/Cl- dependent GABA transport
Loading of GABA into clathrin sculpted GABA transport vesicle lumen
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Proline to arginine mutations in FGF receptors 1 and 3 result in Pfeiffer and Muenke craniosynostosis syndromes through enhancement of FGF binding affinity
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Conversion of succinate semialdehyde to succinate
5-hydroxyindole acetaldehyde to 5-hydroxyindole acetic acid
Activation of highly calcium permeable postsynaptic nicotinic acetylcholine receptors
Binding of acetylcholine to highly calcium permeable postsynaptic nicotinic acetylcholine receptors
Ca permeable AMPA receptor ligand binding
Activation of highly calcium permeable nicotinic acetylcholine receptors
Binding of acetylcholine to highly calcium permeable acetylcholine receptors
Mutational analysis of the hormone-sensitive lipase translocation reaction in adipocytes
Activation of highly sodium permeable nicotinic acetylcholine receptors
Binding of acetylcholine to highly sodium permeable acetylcholine receptors
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Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria
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Nephrin and CD2AP associate with phosphoinositide 3-OH kinase and stimulate AKT-dependent signaling
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NOD-like receptors: role in innate immunity and inflammatory disease
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Purification, characterization, and biosynthesis of human acid ceramidase
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Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity
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Type XIII collagen: a novel cell adhesion component present in a range of cell-matrix adhesions and in the intercalated discs between cardiac muscle cells
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Cloning of the human MCCA and MCCB genes and mutations therein reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency.
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PDGF stimulates an increase in GTP-Rac via activation of phosphoinositide 3-kinase
Mutations in PMM2, a phosphomannomutase gene on chromosome 16p13, in carbohydrate-deficient glycoprotein type I syndrome (Jaeken syndrome)
VEGF controls endothelial-cell permeability by promoting the beta-arrestin-dependent endocytosis of VE-cadherin
Structure, function, and formation of biological iron-sulfur clusters
NOD-LRR proteins: role in host-microbial interactions and inflammatory disease
At the beginning of this reaction, 3 molecules of 'ATP', and 1 molecule of 'eIF4G' are present. At the end of this reaction, 3 molecules of 'ADP', and 1 molecule of 'eIF4G-P' are present. This reaction takes place in the 'cytosol' and is mediated by the 'kinase activity' of 'S6K1-P'.
At the beginning of this reaction, 1 molecule of '3',5'-Cyclic AMP' is present. At the end of this reaction, 1 molecule of 'AMP' is present. This reaction is mediated by the 'hydrolase activity' of 'Phosphorylated PDE3B'.
At the beginning of this reaction, 2 molecules of 'ATP', and 1 molecule of 'PDE3B' are present. At the end of this reaction, 1 molecule of 'Phosphorylated PDE3B', and 2 molecules of 'ADP' are present. This reaction is mediated by the 'kinase activity' of 'PIP3:Phosphorylated PKB complex'.
Phosphorylation of eEF2 kinase by S6K1-P results in decreased activity of this kinase. eEF2 kinase normally phosphorylates and deactivates eEF2, preventing its binding to the ribosome.
Once phosphorylated, S6K1-P phosphorylates and activates ribosomal protein S6 (rpS6), which in turn selectively increases the translation of 5ââ¬â¢TOP mRNAs. These mRNAs encode exclusively for components of the translation machinery (PMID 15809305).
S6K1 contains a TOS motif. mTORC1 requires an intact TOS motif to bind and phosphorylate S6K1 (PMID 15809305).
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Tyrosine receptor kinase stimulation phosphorylates Shc which recruits the SH2 domain of the adaptor protein GRB2, which is complexed with SOS, an exchange factor for p21ras and RAC, through its SH3 domain. Besides SOS, the GRB2 SH3 domain can associate with other intracellular targets, including GAB1. Erk and Rsk mediated phosphorylation results in dissociation of the SOS-GRB2 complex. This may explain why Erk activation through Shc and SOS-GRB2 is transient. Inactive p21ras-GDP is found anchored to the plasma membrane by a farnesyl residue. As Shc is phosphorylated by the the stimulated receptor near to the plasma membrane, the SOS-GRB2:Shc interaction brings the SOS enzyme into close proximity to p21ras.
SOS promotes the formation of GTP-bound RAS, thus activating this protein. RAS activation results in activation of the protein kinases RAF1, B-Raf, and MAP-ERK kinase kinase (MEKK), and the catalytic subunit of PI3K, as well as of a series of RALGEFs. The activation cycle of RAS GTPases is regulated by their interaction with specific guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). GEFs promote activation by inducing the release of GDP, whereas GAPs inactivate RAS-like proteins by stimulating their intrinsic GTPase activity. NGF-induced RAS activation via SHC-GRB2-SOS is maximal at 2 min but it is no longer detected after 5 min. Therefore, the transient activation of RAS obtained through SHC-GRB2-SOS is insufficient for the prolonged activation of ERKs found in NGF-treated cells.
Release of phospho-SHC from the insulin receptor triggers a cascade of signalling events via SOS, RAF and the MAP kinases.
SHC is one of the mediators of insulin signalling events. It is activated by phosphorylation and triggers a cascade of events involving SOS, RAF and the MAP kinases.
At the beginning of this reaction, 1 molecule of 'Phosphatidyl-myo-inositol 4,5-bisphosphate', and 1 molecule of 'ATP' are present. At the end of this reaction, 1 molecule of 'Phosphatidylinositol-3,4,5-trisphosphate', and 1 molecule of 'ADP' are present. This reaction takes place in the 'cell' and is mediated by the 'kinase activity' of 'phospho-IRS:PI3K'.
The latent endonuclease activity of MLH1:PMS2 (MutLalpha) is activated by interaction with MSH2:MSH3 (MutSbeta) (Zhang et al. 2005, and inferred from activation of MLH1:PMS2 by MSH2:MSH6). MLH1:PMS2 makes a nick in the strand of DNA that will be repaired (Kadyrov et al. 2006).
MSH2:MSH3 (MutSbeta) binds unpaired loops of 2 or more nucleotides (Palombo et al. 1996, Genschel et al. 1998). Human cells contain about 6-fold more MSH2:MSH6 than MSH2:MSH3 (MutSbeta) and an imbalance in the ratio can cause a mutator phenotype (Drummond et al. 1997, Marra et al. 1998). Binding of the mismatch activates MSH2:MSH3 to exchange ADP for ATP, adopt the conformation to allow movement along the DNA, and interact with downstream effectors PCNA, MLH1:PMS2 and EXO1. The interaction with PCNA initiates excision of the recently replicated strand. MLH1:PMS2 makes a nick that is enlarged to a gap of hundreds of nucleotides by EXO1. DNA is polymerized across the gap by DNA polymerase delta and the remaining nick is sealed by DNA ligase I.
EXO1 interacts with MSH2 and MLH1 (and therefore is presumed to interact with their respective heterodimers MSH2:MSH3 and MLH1:PMS2), forming a ternary complex with MLH1:PMS2 (Nielsen et al. 2004). EXO1 also interacts with PCNA in S phase (Nielsen et al. 2004, Zhang et al. 2005, Constantin et al. 2005, Knudsen et al. 2007, Liberti et al. 2011)
DNA repair is a phenomenal multi-enzyme, multi-pathway system required to ensure the integrity of the cellular genome. These cellular mechanisms that must cope with the plethora of DNA base pair adducts that arise. DNA damage can arise spontaneously in the cellular milieu through chemical alteration of base nucleotides or as a consequence of errors during DNA replication. For example, it is well known that normal cellular pH and temperature offer an environment, which is hostile to the integrity of DNA and its nucleotide components. Additionally, DNA damage may be induced in response to environmental exposures, including exposure to physical agents such as ionizing or ultraviolet (UV) radiation. Finally, specific chemical agents are known to alkylate or cross-link DNA bases, produce bulky adducts on DNA bases, or break DNA phosphate-sugar backbone. The pioneering work from a number of laboratories have elucidated the basic mechanisms underlying distinct DNA repair pathways that include nucleotide excision repair (NER), base excision repair (BER), DNA strand break repair (DSBR), direct reversal of DNA damage, and the replication past DNA lesions by specialized DNA bypass polymerases (bypass replication). Defects in most of these repair pathways have been associated with one or more specific human diseases. Additionally, the repair of damaged DNA is intimately associated with a number of other distinct cellular processes such as DNA replication, DNA recombination, cell cycle checkpoint arrest, and other basic cellular mechanisms as outlined herein.
The mismatch repair (MMR) system corrects single base mismatches and small insertion and deletion loops (IDLs) of unpaired bases. MMR is primarily associated with DNA replication and is highly conserved across prokaryotes and eukaryotes. MMR consists of the following basic steps: a sensor (MutS homologue) detects a mismatch or IDL, the sensor activates a set of proteins (a MutL homologue and an exonuclease) that select the nascent DNA strand to be repaired, nick the strand, exonucleolytically remove a region of nucleotides containing the mismatch, and finally a DNA polymerase resynthesizes the strand and a ligase seals the remaining nick (reviewed in Kolodner and Marsischkny 1999, Iyer et al. 2006, Li 2008, Fukui 2010, Jiricny 2013). Humans have 2 different MutS complexes. The MSH2:MSH6 heterodimer (MutSalpha) recognizes single base mismatches and small loops of one or two unpaired bases. The MSH2:MSH3 heterodimer (MutSbeta) recognizes loops of two or more unpaired bases. Upon binding a mismatch, the MutS complex becomes activated in an ATP-dependent manner allowing for subsequent downstream interactions and movement on the DNA substrate. (There are two mechanisms proposed: a sliding clamp and a switch diffusion model.) Though the order of steps and structural details are not fully known, the activated MutS complex interacts with MLH1:PMS2 (MutLalpha) and PCNA, the sliding clamp present at replication foci. The role of PCNA is multifaceted as it may act as a processivity factor in recruiting MMR proteins to replicating DNA, interact with MLH1:PMS2 and Exonuclease 1 (EXO1) to initiate excision of the recently replicated strand and direct DNA polymerase delta to initiate replacement of bases. MLH1:PMS2 makes an incision in the strand to be repaired and EXO1 extends the incision to make a single-stranded gap of up to 1 kb that removes the mismatched base(s). (Based on assays of purified human proteins, there is also a variant of the mismatch repair pathway that does not require EXO1, however the mechanism is not clear. EXO1 is almost always required, it is possible that the exonuclease activity of DNA polymerase delta may compensate in some situations and it has been proposed that other endonucleases may perform redundant functions in the absence of EXO1.) RPA binds the single-stranded region and a new strand is synthesized across the gap by DNA polymerase delta. The remaining nick is sealed by DNA ligase I (LIG1). Concentrations of MMR proteins MSH2:MSH6 and MLH1:PMS2 increase in human cells during S phase and are at their highest level and activity during this phase of the cell cycle (Edelbrock et al. 2009). Defects in MSH2, MSH6, MLH1, and PMS2 cause hereditary nonpolyposis colorectal cancer (HNPCC, also known as Lynch syndrome) (reviewed in Martin-Lopez and Fishel 2013).
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Complete amino acid sequence of human phosphoglycerate kinase. Cyanogen bromide peptides and complete amino acid sequence.
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Disruption of normal Watson-Crick base pairing and altered chemistry in the damaged strand involving bases may act as signals of damage that are recognized by XPC:HR23B complex.
Several subunits of the NER multiprotein repair machinery are required for the recognition of damage in DNA. Mainly, XPC, HR23B, XPA and RPA are implicated in this process. XPA and RPA are thought to be binding to the damage site after the binding of XPC-HR23B complex.
At the beginning of this reaction, 1 molecule of 'ERCC1, DNA excision repair protein', and 1 molecule of 'XPF protein' are present. At the end of this reaction, 1 molecule of 'ERCC1:XPF complex' is present. This reaction takes place in the 'nucleus'.
Two DNA helicases XPG and XPD, which are part of TFIIH, unwind DNA duplex around this lesion to form an open bubble structure that exposes the damaged site.
Binding of XPC complex to the damaged site on the DNA substrate is followed by XPA and RPA recruitment. XPA is a metalloprotein that binds to different types of DNA damage. Binding of RPA, or Replicative protein A, a heterotrimer, initiates the formation of incision complex. This includes a serial assembly of the rest of the NER machinery consisting of TFIIH, XPG etc. Action of helicases in TFIIH complex opens up a bubble structure in the DNA template, exposing a fragment of DNA with lesion for endonuclease activity.
Crystal structure of Homo sapiens protein LOC79017
ERCC1-XPF complex with 5ââ¬â¢ endonuclease activity binds to this pre-incision complex around the bubble structure to form an active incision complex.
Dual incision at defined positions flanking the DNA damage is carried out by XPG (3' -incision) and ERCC1-XPF (5'-incision) complex. The resulting excised fragment is ~27-30 bp long and contains the lesion.
The cleavage of the damaged strand of DNA 3' to the site of damage occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex is unwound. The incision is carried out by XPG.
The resultant gap is filled by polymerase activities of Pol delta and Pol epsilon. Accessory replication protein complexes of RPA, PCNA and RFC play a role in this synthesis. DNA Ligase 1 seals the gap restoring the covalent integrity of the repaired strand.
DNA Ligase 1 ligates the newly synthesized fragment to the gap in the template DNA.
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1909-1963
Isolation and characterization of a hydroxyacid-oxoacid transhydrogenase from rat kidney mitochondria
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The RAD51-ssDNA nucleoprotein filament is a right-hand helical nucleoprotein filament referred to as the presynaptic filament. This nucleoprotein complex contains a binding site for the double-stranded homologous DNA molecule with which it interacts during strand exchange. Loading of RAD51 onto ssDNA is thought to be facilitated by recombination mediator RAD52 (McIlwraith et al., 2000), RAD51 paralogs: RAD51B, RAD51C, RAD51D, XRCC2 and XRCC3 (Sigurdsson et al., 2001), by the association of RAD52 with ssDNA (Parsons et al., 2000) and by the association of RAD51 with BRCA2 (Tarsounas et al., 2003).
Following the synthesis of new DNA at resected 5' ends of the DSB, the heterologous DNA molecules may be ligated resulting in the formation of Holliday junctions. The Holliday structures are then cleaved resulting in reciprocal exchange of sequence between sister chromatids.
Ligation of the crossed-strand intermediate results in the formation of Holliday structures with two crossovers. In humans, the identity of this ligase activity involved in this process is not known.
The presynaptic phase of homologous DNA pairing and strand exchange begins with the displacement of RPA from ssDNA, followed by the association of RAD51 with BRCA2, formation of RAD52 heptameric ring structure complexes on ssDNA, association of RAD52 with the RPA complex, association of RAD52 with ssDNA at resected ends of double-strand break and assembly of the RAD51-ssDNA nucleoprotein complex. Stable synaptic pairing between recombining DNA molecules involves the invasion of homologous duplex DNA by the processed single-stranded ends of the double-strand break, followed by displacement of the non-complimentary strand of the duplex. This results in the formation of a D-loop structure. Invasion of the heteroduplex DNA by RAD51 nucleoprotein filament involves the identification of a region of homology between these two molecules. The mechanism by which this occurs is not yet known. RAD51 catalyses the invasion of the nucleoprotein filament into homologous double-stranded DNA. Watson-Crick hydrogen bonding between the ssDNA within the nucleoprotein filament and the homologous strand of the invaded DNA duplex result in the displacement of the non-pairing strand (strand displacement) and formation of the D-loop structure (Sung et al., 2003). The RAD51 nucleoprotein filament has independent binding sites for the ssDNA strand upon which it assembles and the recombining homologous duplex DNA. The repair proteins RPA, RAD52, and RAD54 appear to promote RAD51 mediated invasion and homologous DNA pairing reaction (McIlwraith et al, 2000 and Sigurdsson et al., 2002). The conformation of the RAD52-ssDNA complex is thought to place the ssDNA on an exposed surface of the protein, in a configuration that may promote the DNA-DNA annealing of complementary DNA strands. RAD54 may function in the transient separation of the duplex DNA strands via its ATP hydrolysis-mediated DNA supercoiling function (Sigurdsson et al., 2002). Branch migration or strand exchange occurs as the complimentary duplex DNA strand is progressively taken up into the nucleoprotein filament to base pair with the invading single-strand sequence (Sung et al., 2003).
The presynaptic phase of homologous DNA pairing and strand exchange begins with the displacement of RPA from ssDNA, followed by the association of RAD51 with BRCA2, formation of RAD52 heptameric ring structure complexes on ssDNA, association of RAD52 with the RPA complex, association of RAD52 with ssDNA at resected ends of double-strand break and assembly of the RAD51-ssDNA nucleoprotein complex.
Numerous types of DNA damage can occur within a cell due to the endogenous production of oxygen free radicals, normal alkylation reactions, or exposure to exogenous radiations and chemicals. Double-strand breaks (DSBs), one of the most dangerous type of DNA damage along with interstrand crosslinks, are caused by ionizing radiation or certain chemicals such as bleomycin, and occur normally during the processes of DNA replication, meiotic exchange, and V(D)J recombination. Two distinct mechanisms for DSB repair are the error-free homologous recombination repair (HRR) pathway and the error-prone nonhomologous end-joining (NHEJ) pathway. The choice of pathway may be determined by whether the DNA region has already replicated and the precise nature of the break. NHEJ functions at all stages of the cell cycle, but plays the predominant role in both the G1 phase and in S-phase regions of DNA that have not yet replicated (Rothkamm et al. 2003). HRR functions primarily in repairing both one-sided DSBs that arise at DNA replication forks and two-sided DSBs arising in S or G2-phase chromatid regions that have replicated.
The HRR pathway is an "error free" DNA repair mechanism that utilizes information encoded by homologous sequence to repair double-strand breaks (DSBs). HRR acts on DSBs occurring within replicated DNA (replication-independent DSBs) or on DSBs that are generated at broken replication forks (replication-dependent DSBs). Repair by homologous recombination involves processing of the ends of the DNA double-strand break, homologous DNA pairing and strand exchange, repair DNA synthesis, and resolution of the heteroduplex molecules.
Homologous recombination repair of replication-independent double-strand breaks requires the activation of ATM followed by ATM mediated phosphorylation of DNA repair proteins. DNA repair and signaling proteins are then recruited to double-strand breaks. The ends of the DNA double strand breaks must be resectioned and RPA complexes associate with the resulting ssDNA. Homologous DNA pairing and strand exchange then occurs followed by DNA repair synthesis and resolution of D-loop structures.
Once repair synthesis has occurred, the D-loop structure may be resolved either through Holliday junction intermediates of through synthesis-dependent strand-annealing.
XPC is mutated in individuals with xeroderma pigmentosum from genetic Complementation Group C (XP-C). It forms a tight heterodimeric complex with human Rad 23B homolog, HR23B and is thought to bind to the damaged site with lesion first triggering subsequent reactions
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At the beginning of this reaction, 1 molecule of 'Stalled Pol II in TC-NER', and 1 molecule of 'repaired DNA template:nascent mRNA hybrid' are present. At the end of this reaction, 1 molecule of 'Active Pol II complex with repaired DNA template:mRNA hybrid' is present. This reaction takes place in the 'nucleus'.
The preferential repair of UV-induced damage in transcribed strands of active genes is known as Transcription-coupled NER (TC-NER). Impairment of the ability for TC-NER results in the onset of a severe hereditary disorder called Cockayne's syndrome, an autosomal recessive disease characterized by hypersensitivity to UV light . Many types of helix distorting lesions can block the movement of elongating RNA Pol II leading to its stalling and subsequent triggering of repair mechanisms. The repair of DNA damage in active genes occurs much faster compared to the repair in non-transcribed genomic regions (via GG-NER). Also, the non-transcribed strand of the same gene is repaired at a similar rate as that of non-transcribed genomic regions. The transcriptional responses to DNA damage in terms of stalling of Pol II, its displacement from the lesion site etc. are not well elucidated. The following annotation in GK provides an overall picture of TC-NER and will be updated as and when new insights are obtained about these crucial steps.
NER was first described in the model organism E. coli in the early 1960s as a process whereby bulky base damage is enzymatically removed from DNA, facilitating the recovery of DNA synthesis and cell survival. Deficient NER processes have been identified from the cells of cancer-prone patients with different variants of xeroderma pigmentosum (XP), trichothiodystrophy (TTD), and Cockayne's syndrome. These XP cells exhibited an ultraviolet radiation hypersensitivity leading to a hypermutability response to UV, offering a direct connection between deficient NER, increased mutations, and cancer. While the NER pathway in prokaryotes is unique, the pathway utilized in yeast and higher eukaryotes is highly conserved and includes a variety of proteins that interact to form complexes. NER is involved in the repair of bulky adducts in DNA, such as UV-induced photo lesions [of both 6-4 photoproducts (6-4 pps) and cyclobutane pyrimidine dimer (CPDs)], intrastrand cross-links, large chemical adducts formed from exposure to aflatoxin, benzopyrene and other genotoxic agents. Specific proteins have been identified that participate in base damage recognition, cleavage of the damaged strand on both sides of the lesion, excision of the oligonucleotide bearing the lesion, and accessory proteins necessary for efficient function. Polymerization and ligation restore the strand to its original state. NER consists of two related pathways called global genomic repair (GG-NER) and transcription-coupled NER (TC-NER). The pathways differ in the way in which DNA damage is initially recognized, but the majority of the participating molecules are shared between these two branches of NER. GG-NER is considered to be transcription-independent, removing lesions from non-transcribed regions of genome in addition to non-transcribed strands of transcribed regions. The preferential repair of UV-induced damage in transcribed strands of active genes is known as Transcription-coupled NER (TC-NER). Several of the proteins involved in NER are key components of the basal transcription complex TFIIH. NER proteins have also been shown to interact with the 19S regulatory subunit of the proteasome, suggesting a role in cellular regulation signal pathways. The establishment of mutant mouse models for NER genes and other DNA repair-related genes have been useful in demonstrating the associations between NER defects and cancer.
The MSH2:MSH6 (MutSalpha) heterodimer binds single base mismatches and insertion or deletion loops (IDLs) of 1-2 bases (Drummond et al. 1997, Genschel et al. 1998, Gradia et al. 2000, Zhang et al. 2005, Constantin et al. 2005, Tian et al. 2009, reviewed in Edelbrock et al. 2013). The MSH6 subunit contains a Phe-X-Glu motif that binds the mismatched base (Dufner et al 2000, Warren et al. 2007). During replication most nuclear MSH2:MSH6 is observed to colocalize with PCNA via an interaction between PCNA and MSH6 at replication forks during S phase (Kleczkowska et al. 2001), presumably coupling mismatch repair to DNA replication. The MSH6 subunit of MSH2:MSH6 also binds histone H3 methylated at lysine-36, which is enriched in chromatin during G1 and early S phase (Li et al. 2013).
MSH2:MSH6 (MutSalpha) binds single base mismatches and unpaired loops of 1-2 nucleotides (reviewed in Edelbrock et al. 2013). Human cells contain about 6-fold more MSH2:MSH6 than MSH2:MSH3 (MutSbeta), which mediates repair of larger mismatches, and an imbalance in the ratio can cause a mutator phenotype (Drummond et al. 1997, Marra et al. 1998). The MSH6 subunit is responsible for binding the mismatch, which activates MSH2:MSH6 to exchange ADP for ATP, adopt the conformation to allow movement on the DNA, and interact with downstream effectors PCNA, MLH1:PMS2 and EXO1. The interaction with PCNA initiates excision of the recently replicated strand. MLH1:PMS2 has endonucleolytic activity and makes a nick that is enlarged to a gap of hundreds of nucleotides by EXO1. DNA is polymerized across the gap by DNA polymerase delta and the remaining nick is sealed by DNA ligase I.
LIG1 (DNA ligase I) catalyzes the formation of a phosphodiester bond between a 3' hydroxyl group and a 5' phosphate group to form an intact DNA strand (Bhat and Grossman 1986). ATP is hydrolyzed to AMP and pyrophosphate in a reaction mechanism that involves adenylylation of a lysine residue of the enzyme, transfer of the adenylyl group to the 5' phosphate of DNA, and nick sealing by nucleophilic attack of the 3' hydroxyl group on the adenylylated 5' phosphate (Taylor et al. 2011, reviewed in Tomkinson et al. 2006). RPA stimulates the activity of LIG1 about 15-fold (Ranalli et al. 2002). LIG1 is recruited to repair sites by interaction with PCNA (Mortusewicz et al. 2006). Ligation is the final step in mismatch repair (Zhang et al. 2005, Constantin et al. 2005).
After being activated by a mismatch, MSH2:MSH6 (MutSalpha) recruits MLH1:PMS2 (MutLalpha) to form a ternary complex with mismatched DNA (Gu et al. 1998, Blackwell et al. 2001, Plotz et al. 2002). As inferred from yeast, multiple MLH1:PMS2 complexes may be loaded at each mismatch (Hombauer et al. 2011). MSH2:MSH6 and MLH1:PMS2 interact with PCNA (Gu et al. 1998, Clark et al. 2000, Kleczkowska et al. 2001, Zhang et al. 2005, Constantin et al. 2005, Iyer et al. 2008, Masih et al. 2008, Iyer et al. 2010). The binding sites for MLH1:PMS2 and PCNA are distinct on MSH2:MSH6 so it is possible that both can bind simultaneously (Iyer et al. 2010). The interaction with PCNA appears to direct the orientation of the repair complex so as to determine which strand will be used as template and which strand will be repaired. In vivo, the recently replicated strand is repaired. In vitro, the strand containing a nick is repaired (Zhang et al. 2005, Constantin et al. 2005), possibly due to the ability of the nick to orient the loading of PCNA onto DNA by RFC (Pluciennik et al. 2010).
After binding a mismatch, the MSH2:MSH6 (MutSalpha) heterodimer exchanges ADP for ATP, which alters its conformation to a sliding clamp or molecular switch able to diffuse in one direction along duplex DNA (Gradia et al. 1997, Blackwell et al. 1998, Gradia et al. 1999, Gradia et al. 2000). Each heterodimer can bind 2 molecules of ATP or ADP or a combination of ADP and ATP. The affinities and hydrolysis rates of the binding sites differ (Tian et al. 2009, Heinen et al. 2011). However, the exact location of a given adenosine at a given binding location and the conferred function is unclear but believed to control downstream events. Hydrolysis of the ATP by MSH2:MSH6 is not required for mismatch binding but is required for subsequent mismatch repair (Gu et al. 1998, Tian et al. 2009, Geng et al. 2012).
EXO1 interacts with MSH2 and MLH1 (and therefore is presumed to interact with their respective heterodimers MSH2:MSH6 and MLH1:PMS2), forming a ternary complex with MLH1:PMS2 (Nielsen et al. 2004). EXO1 also interacts with PCNA in S phase (Nielsen et al. 2004, Zhang et al. 2005, Constantin et al. 2005, Knudsen et al. 2007, Liberti et al. 2011)
The latent endonuclease activity of MLH1:PMS2 (MutLalpha) is activated by interaction with MSH2:MSH6 and PCNA (Kadyrov et al 2006). MLH1:PMS2 makes a nick in the replicated strand of DNA. As inferred from yeast, more than one MLH1:PMS2 may bind per MSH2:MSH6 (Hombauer et al. 2011). Strand selection of the nick is determined by interaction with PCNA, though the exact mechanism is unknown (Pluciennik et al 2010).
Ectopic expression of Cdc25A accelerates the G(1)/S transition and leads to premature activation of cyclin E- and cyclin A-dependent kinases
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1777-1805
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An active Pol II complex consisting mainly of the Pol II holoenzyme transcribes the damaged DNA template.
At the site of damage, the Pol II complex is arrested resulting in reduced levels of transcription. Several models have been proposed to explain the mechanism of this transcriptional downregulation. These include a. hyperphosphorylation of Pol II resulting in aborted entry to new pre-initiation complexes b. sequestration of TATA-binding proteins (TBP) c. enhanced use of TFIIH complexes for repair purposes precluding their use in transcription.
GG-NER is considered to be transcription-independent, removing lesions from non-transcribed regions of genome in addition to non-transcribed strands of transcribed regions. The three events that characterize NER are well characterized in GG-NER: damage recognition, bimodal incision of DNA via repair protein complex, resulting excision of DNA fragment with the lesion. Post-excision polymerization and ligation restore back the native chemistry and configuration to the damaged DNA.
Polymerization is carried out by DNA polymerases, delta and epsilon.
At the beginning of this reaction, 1 molecule of 'newly synthesized DNA fragment ', 1 molecule of 'DNA ligase I ', and 1 molecule of 'damaged DNA substrate:nascent mRNA hybrid with dual incisions' are present. At the end of this reaction, 1 molecule of 'repaired DNA template:nascent mRNA hybrid', and 1 molecule of 'DNA ligase I ' are present. This reaction takes place in the 'nucleus' and is mediated by the 'DNA ligase activity' of 'DNA ligase I '.
Dual incisions are carried out by XPG, and ERCC1-XPF complex as seen in GG-NER.
At the beginning of this reaction, 1 molecule of 'Transcription-coupled (TC) repair complex', and 1 molecule of 'damaged DNA substrate:nascent mRNA hybrid with 3' incision' are present. At the end of this reaction, 1 molecule of 'Transcription-coupled (TC) repair complex', 1 molecule of 'excised DNA fragment with lesion', and 1 molecule of 'damaged DNA substrate:nascent mRNA hybrid with dual incisions' are present. This reaction takes place in the 'nucleus' and is mediated by the 'endodeoxyribonuclease activity' of 'Transcription-coupled (TC) repair complex'.
At the beginning of this reaction, 1 molecule of 'Transcription-coupled (TC) repair complex', and 1 molecule of 'damaged DNA substrate:nascent mRNA hybrid' are present. At the end of this reaction, 1 molecule of 'Transcription-coupled (TC) repair complex', and 1 molecule of 'damaged DNA substrate:nascent mRNA hybrid with 3' incision' are present. This reaction takes place in the 'nucleus' and is mediated by the 'endodeoxyribonuclease activity' of 'Transcription-coupled (TC) repair complex'.
At the beginning of this reaction, 1 molecule of 'Transcription-coupled (TC) repair complex', and 1 molecule of 'Stalled Pol II complex with damaged DNA hybrid' are present. At the end of this reaction, 1 molecule of 'Transcription-coupled (TC) repair complex', 1 molecule of 'Stalled Pol II in TC-NER', and 1 molecule of 'damaged DNA substrate:nascent mRNA hybrid' are present. This reaction takes place in the 'nucleus'.
The 'road block' induced by the DNA damage to the transcription machinery triggers assembly of a transcription couple repair complex, whose composition and function are yet to fully understood. Damage recognition is achieved by the arrest of Pol II active complex. Subsequently various factors like CSA, CSB, TFIIH, XPG, XPF-ERCC1 complexes are recruited. The importance of active CSA and CSB are known from the mutation profile of the patients bearing the corresponding disease phenotypes. CSB can act as a 'repair-transcription uncoupling factor' that may use its DNA translocase activity to remove the Pol II activity from the lesion site. TFIIS may cleave up to 35 nucleotides from the 3' end of the nascent RNA product leading to the enhanced access to damage site on the corresponding template DNA.
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K+-independent Li+/Ca2+ exchanger transport
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During removal of DNA patch containing abasic residue, DNA glycosylase is displaced by APE1 which endonucleolytically cleaves the 5' side of the base-free deoxyribose residue. POL Beta is recruited to the AP site where it mediates incorporation of the first replacement nucleotide. Association of POL delta with the AP site displaces POL Beta. DNA strand displacement synthesis then follows and flap structures are cleaved.
ABC7, mABC1 and mABC2 mediate heme transport
While the single-nucleotide replacement pathway appears to facilitate the repair of most damaged bases, an alternative BER pathway is evoked when the structure of the terminal sugar phosphate is such that it can not be cleaved through the AP lyase activity of DNA polymerase, POL Beta. Under these circumstances, a short stretch of residues containing the abasic site is excised and replaced (Dianov et al., 1999). Following DNA glycosylase mediated cleavage of the damaged base, the endonuclease APE1 is recruited to the site of damage where it cleaves the 5' side of the base-free deoxyribose residue. POL Beta then displaces the DNA glycosylase and synthesizes the first replacement residue. DNA polymerase, POL Delta replaces POL Beta and mediates the synthesis of several additional residues resulting in the displacement of a DNA flap containing the abasic sugar phosphate and 3' flanking residues. The flap structure is recognized and cleaved by the flap endonuclease, FEN1 and the replacement residues are then ligated by the DNA ligase, LIG1 (Klungland and Lindahl, 1997; Matsumoto et al., 1999).
Resolution of AP sites can occur through the single-nucleotide replacement pathway or through the multiple-nucleotide patch replacement pathway.
Of the three major pathways involved in the repair of nucleotide damage in DNA, base excision repair (BER) involves the greatest number of individual enzymatic activities. This is the consequence of the numerous individual glycosylases, each of which recognizes and removes a specific modified base(s) from DNA. BER is responsible for the repair of the most prevalent types of DNA lesions, alterations, which arise intracellularly as a consequence of normal mitochondrial metabolism or by oxidative free radicals resulting from ionizing radiation, lipid peroxidation or activated phagocytic cells. BER is a two-step process initiated by one of the DNA glycosylases that recognizes a specific modified base(s) and removes that base through the catalytic cleavage of the glycosylic bond, leaving an abasic site without disruption of the phosphate-sugar DNA backbone. Subsequently, abasic sites are resolved by a series of enzymes that cleave the backbone, synthesize the replacement residue(s), and ligate the DNA strand. BER may occur by either a single-nucleotide replacement pathway or a multiple-nucleotide patch replacement pathway, depending on the structure of the terminal sugar phosphate residue. The glycosylases found in human cells recognize "foreign adducts" and not standard functional modifications such as DNA methylation.
K+-dependent Na+/Ca2+ exchanger transport
At the beginning of this reaction, 1 molecule of 'DNA containing an APE1-bound AP site' is present. At the end of this reaction, 1 molecule of 'APE1-bound DNA strand break containing an incision 5' to an AP site' is present. This reaction takes place in the 'nucleus' and is mediated by the 'endodeoxyribonuclease activity' of 'APE1'.
Na+-driven Cl-/HCO3- exchanger transport
Base-free sugar-phosphate removal via the single-nucleotide replacement pathway requires displacement of DNA glycosylase by APE1, APE1 mediated endonucleolytic cleavage at the 5' side of the base-free deoxyribose residue, recruitment of POL Beta to the AP site and Excision of the abasic sugar phosphate (dRP) residue at the strand break (Lindahl and Wood, 1999).
ABCA8, B1 and B5 mediate xenobiotic efflux
The single-nucleotide replacement pathway of base excision repair appears to facilitate the repair of most damaged bases. Following DNA glycosylase mediated cleavage of the damaged base, the endonuclease, APE1 is recruited to the site of damage where it cleaves the 5' side of the base-free deoxyribose residue. DNA polymerase, POL Beta then displaces the DNA glycosylase and cleaves the 3' side of the sugar phosphate. APE1 is subsequently released, the XRCC1:LIG3 complex is recruited and POL Beta mediates the synthesis of the replacement residue. Following LIG3 ligase mediated ligation of the replaced residue, the XRCC1:LIG3 complex dissociates (see Lindahl and Wood, 1999). An alternative BER pathway is employed when the structure of the terminal sugar phosphate is such that it can not be cleaved through the AP lyase activity of POL Beta.
At the beginning of this reaction, 1 molecule of 'APE1', and 1 molecule of 'DNA ligase I ' are present. At the end of this reaction, 1 molecule of 'APE1:DNA ligase I complex' is present. This reaction takes place in the 'nucleus'.
MTABC3 transports porphyrin into mitochondria
At the beginning of this reaction, 1 molecule of 'APE1', and 1 molecule of 'Flap endonuclease-1 ' are present. At the end of this reaction, 1 molecule of 'APE1:FEN1complex' is present. This reaction takes place in the 'nucleus'.
The ABCC family mediates organic anion transport
At the beginning of this reaction, 1 molecule of 'PCNA', and 1 molecule of 'Flap endonuclease-1 ' are present. At the end of this reaction, 1 molecule of 'FEN1:PCNA complex' is present. This reaction takes place in the 'nucleus'.
Cyclic-AMP-dependent transcription factor ATF-1
The proto-oncogene product c-Cbl becomes tyrosine phosphorylated by stimulation with GM-CSF or Epo and constitutively binds to the SH3 domain of Grb2/Ash in human hematopoietic cells
ABCD1/D2/D3 mediate long chain fatty acid transport in to peroxisomes
Base excision repair is initiated by DNA glycosylases that hydrolytically cleave of the base-deoxyribose glycosyl bond of a damaged nucleotide residue releasing the damaged base (Lindahl and Wood, 1999).
At the beginning of this reaction, 1 molecule of 'DNA containing a hNTH1-bound apurinic/apyrimidinic site', and 1 molecule of 'APE1' are present. At the end of this reaction, 1 molecule of 'hNTH1', and 1 molecule of 'DNA containing an APE1-bound AP site' are present. This reaction takes place in the 'nucleus'.
Damaged pyrimidines are first cleaved by pyrimide-specific glycosylases (see Lindahl and Wood 1999).
Depyrimidination of a damaged nucleotide is mediated by a pyrimidine-specific DNA glycosylase. The glycosylase cleaves the N-C1' glycosidic bond between the damaged DNA base and the deoxyribose sugar generating a free base and an apyrimidinic (AP) site.
Following cleavage of the damaged base, DNA glycosylase is displaced by APE1.
Base excision repair is initiated by a DNA glycosylase which first recognizes and removes a damaged or incorrect (e.g. mismatched) base.
Activation of tandem pore domain in a weak inwardly rectifying K+ channels
At the beginning of this reaction, 1 molecule of 'hNTH1 glycosylase:dihydrouracil complex' is present. At the end of this reaction, 1 molecule of 'DNA containing a hNTH1-bound apurinic/apyrimidinic site', and 1 molecule of '5,6-Dihydrouracil' are present. This reaction takes place in the 'nucleus' and is mediated by the 'pyrimidine-specific oxidized base lesion DNA N-glycosylase activity' of 'hNTH1'.
Activation of TWIK-related K+ channel (TREK)
At the beginning of this reaction, 1 molecule of 'hNTH1 glycosylase: foramidopyrimidine complex' is present. At the end of this reaction, 1 molecule of 'formamidopyrimidine', and 1 molecule of 'DNA containing a hNTH1-bound apurinic/apyrimidinic site' are present. This reaction takes place in the 'nucleus' and is mediated by the 'pyrimidine-specific oxidized base lesion DNA N-glycosylase activity' of 'hNTH1'.
At the beginning of this reaction, 1 molecule of 'hNTH1 glycosylase:thymine glycol' is present. At the end of this reaction, 1 molecule of 'Thymine glycol', and 1 molecule of 'DNA containing a hNTH1-bound apurinic/apyrimidinic site' are present. This reaction takes place in the 'nucleus' and is mediated by the 'pyrimidine-specific oxidized base lesion DNA N-glycosylase activity' of 'hNTH1'.
At the beginning of this reaction, 1 molecule of 'hNTH1 glycosylase:cytosine glycol complex' is present. At the end of this reaction, 1 molecule of 'cytosine glycol', and 1 molecule of 'DNA containing a hNTH1-bound apurinic/apyrimidinic site' are present. This reaction takes place in the 'nucleus' and is mediated by the 'pyrimidine-specific oxidized base lesion DNA N-glycosylase activity' of 'hNTH1'.
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Dual specificity protein phosphatase 6 ecNumber3.1.3.16/ecNumber ecNumber3.1.3.48/ecNumber
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Following exposure to ionizing radiation, a number of recombination/repair proteins and complexes relocalize to nuclear foci that are believed to correspond to the sites of double-strand breaks. These proteins include gamma-H2AX, ATM, RAD51, BRCA1, BRCA2, NBS1, RPA, and MDC1/NFBD1 and the MRE11-RAD50-NBS1. Gamma-H2AX, the phosphorylated form of H2AX, is one of the first proteins to appear within nuclear foci and plays an essential role in recruiting other repair proteins (Paull et al., 2000). One model illustrating the organization of the recruited repair proteins (Van den Bosch et al., 2003) is shown here. (A) Undamaged section of a chromosome, showing two chromatin loops and an inactive ATM dimer. (B,C) Induction of a DNA double-stranded break (DSB), modification of chromatin, activation of ATM and recruitment of both ATM and MRE11/RAD50/NBS1(MRN). The possibility that MRN binds before ATM is shown, but the activation of ATM appears to require the MDC1 and the MRN complex (Uziel, et al 2003; Mochan et al. 2003). The thin black line indicates modified chromatin. (D,E) Following DNA damage, a wave of H2AX phosphorylation occurs and the mediator proteins (mediator of DNA damage checkpoint protein 1 (MDC1), p53-binding protein 1(53BP1), and breast-cancer-associated protein 1(BRCA1)) are recruited to the growing focus where they are phosphorylated in an ATM-dependent manner. The molecular architecture of the focus is unknown. (F) Disassembly of the focus, ATM inactivation and chromatin remodeling. The model suggests at least two distinct forms of soluble ATM: an inactive oligomer and an active monomer, and at least two distinct active, insoluble forms: one directly at the lesion and another integral to the growing focus. Note that the MRN complex is also a component of the growing focus, but for clarity, has been omitted here. Complex persistent lesions are thought to be more difficult to repair, and this is reflected in the size attained by the growing focus.
At the beginning of this reaction, 1 molecule of 'RAD51', and 1 molecule of '3' overhanging DNA at resected DSB ends' are present. At the end of this reaction, 1 molecule of 'RAD51:resected ends of DNA double-strand break' is present. This reaction takes place in the 'nucleus'.
Detection of DNA double-strand breaks involves sensor proteins that become activated setting off of signaling cascades. This signaling leads to the recruitment of repair proteins and subsequent repair of the damaged DNA. ATM is one of the primary candidate sensors in double-strand break repair.
MRE11 has both manganese dependent ss DNA 3'-5' exonuclease and endonuclease activities. MRE11 associates with RAD50 resulting in increased 3'-5' exonuclease activity.
Assembly of the RAD50-MRE11-NBS1 complex at DNA double-strand breaks involves the formation of RAD50:MRE11 complex, association of RAD50:MRE11 complex with NBS1 through MRE11 and association of the MRN with sites of DSB.
MRN complexes localize to nuclear foci in response to double-strand breaks and have been implicated in DNA end-processing during homologous recombination repair (Trujillo et al., 1998). The MRN complex may function as a bridge between double-strand break ends through interactions between the coiled-coil domains of RAD50 (Hoptner et al., 2002).
Reactive cellular catabolites can cause DNA damage by 6-O-methylation of guanine. 6-O-methylguanine can pair ambiguously with both C and T, and can cause transition mutations. Active reversal of such damage can be facilitated by proteins having 6-O-methylguanine-DNA methyltransferase (MGMT) activity. MGMT removes the methyl group from the guanine and transfers it to the cysteine residue at position 145 on the protein itself. MGMT thus methylated is not regenerated, as the S-methylcysteine is very stable. This is an energetically expensive approach to DNA repair as one entire protein molecule is sacrificed per lesion that is corrected in this manner (Yang et al. 2011).
DNA damage can be directly reversed by dealkylation.
ATM is present in unirradiated cells as a dimer or higher-order multimer. Following irradiation, ATM undergoes rapid intermolecular autophosphorylation of serine 1981.
Autophosphorylation of ATM results in the dissociation of the dimeric/multimeric ATM complex and initiation of ATM kinase activity. Autophosphorylation does not directly regulate ATM kinase activity. Instead, it is the resulting dissociation of ATM oligomers that allows substrates access to the ATM kinase domain.
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Mitogen-activated protein kinase 1 (EC 2.7.1.-) (Extracellular signal- regulated kinase 2) (ERK-2) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2) (p42-MAPK) (ERT1)
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Microtubule- associated protein-2 kinase
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In addition to various processes for removing damaging lesions from the DNA, cells have developed specific mechanisms for tolerating unexcised damages during the replication of the genome. Such processes are collectively called DNA damage bypass pathways. Several proteins including novel Y-family polymerases that have been recently identified in multitude of organisms are involved in this process. Translesion synthesis (TLS) or replicative bypass of damaged bases that are known to arrest high fidelity, highly processive polymerases involved in DNA replication is carried out by error-prone polymerases Pol zeta, Pol eta and Rev3 protein among others. TLS is implicated in UV and chemical induced mutagenesis of normal human cells where lesions in the replicating genome are carried over to the newly formed daughter cells. All these 3 enzymes are found to lack 3'->5' exonuclease activity, while exhibiting low fidelity, weak processivity and sufficient polymerase activities. An outline of the bypass synthesis by these 3 enzymes is annotated here. Complete details of damage recognition and discrimination, initiation of specific polymerase activity and the finer mechanisms are yet to be elucidated.
Pol eta consists of 713 amino acids and can bypass thymidine-thymidine dimers adding two A's correctly opposite to the lesion. Mutations in Pol eta gene result in the loss of this bypass activity in accounting for the XP variant phenotype (XPV) among human xeroderma pigmentosum disorder patients. Pol eta can carry out TLS past various UV and chemical induced lesions via two steps: a. preferential incorporation of correct bases opposite to the lesion b. conditional elongation only at the sites where such correct bases are inserted.
Ubiquitous environmental and endogenous genotoxic agents cause lesions that can interfere with normal DNA metabolism including DNA replication, eventually resulting in mutations that lead to carcinogenesis and/or cell death. While cells posses repair mechanisms like nucleotide excision and base excision repair pathways to maintain the integrity of the genome, not all lesions on the genome can be repaired efficiently by these processes in time for DNA replication, and some types of lesion are repaired very inefficiently. To prevent acute cell death through arrested DNA replication at unrepaired lesions, cells have a mechanism, referred to as translesion synthesis, which allows DNA synthesis to proceed past lesions (Masutani et al., 2000).
At the beginning of this reaction, 1 molecule of 'Pol eta:damaged DNA template complex' is present. At the end of this reaction, 1 molecule of 'Pol eta:lesioned DNA template inserted with correct base complement' is present. This reaction takes place in the 'nucleus' and is mediated by the 'eta DNA polymerase activity' of 'Pol eta:damaged DNA template complex'.
At the beginning of this reaction, 1 molecule of 'Pol eta:lesioned DNA template inserted with correct base complement' is present. At the end of this reaction, 1 molecule of 'Pol eta protein', and 1 molecule of 'Elongated DNA template with bypassed lesion' are present. This reaction takes place in the 'nucleus' and is mediated by the 'eta DNA polymerase activity' of 'Pol eta:lesioned DNA template inserted with correct base complement'.
HREV1 encodes a template dependent dCMP transferase activity that can insert a C residue opposite an abasic site.
At the beginning of this reaction, 1 molecule of 'damaged DNA substrate ', and 1 molecule of 'Pol eta protein' are present. At the end of this reaction, 1 molecule of 'Pol eta:damaged DNA template complex' is present. This reaction takes place in the 'nucleus'.
At the beginning of this reaction, 1 molecule of 'HREV1:damaged DNA template complex' is present. At the end of this reaction, 1 molecule of 'HREV1:lesioned DNA template with misinserted bases' is present. This reaction takes place in the 'nucleus' and is mediated by the 'DNA-directed DNA polymerase activity' of 'HREV1:damaged DNA template complex'.
At the beginning of this reaction, 1 molecule of 'HREV1:lesioned DNA template with misinserted bases' is present. At the end of this reaction, 1 molecule of 'HREV1 protein', and 1 molecule of 'Elongated DNA template with bypassed lesion' are present. This reaction takes place in the 'nucleus' and is mediated by the 'DNA-directed DNA polymerase activity' of 'HREV1:lesioned DNA template with misinserted bases'.
At the beginning of this reaction, 1 molecule of 'damaged DNA substrate ', and 1 molecule of 'HREV1 protein' are present. At the end of this reaction, 1 molecule of 'HREV1:damaged DNA template complex' is present. This reaction takes place in the 'nucleus'.
Localization of a thrombin-binding site on human platelet membrane glycoprotein Ib determined by a monoclonal antibody
Heteroduplex DNA with D-loop structure with extended pairing between invading strand and complementary heteroduplex strand and containing newly synthesized ends
damaged DNA substrate:nascent mRNA hybrid
Expression of Gs alpha in Escherichia coli. Purification and properties of two forms of the protein
Mechanism of the nucleotide exchange reaction in eukaryotic polypeptide chain initiation. Characterization of the guanine nucleotide exchange factor as a GTP-binding protein.
Dicer is dispensable for asymmetric RISC loading in mammals
Molecular cloning of PEPT 2, a new member of the H+/peptide cotransporter family, from human kidney
Intracellular Phosphorylated Trk receptors
Regulation of phagocytosis by Rho GTPases
damaged DNA substrate:nascent mRNA hybrid with 3' incision
repaired DNA template:nascent mRNA hybrid
damaged DNA substrate:nascent mRNA hybrid with dual incisions
DNA containing IDL greater than 1 base and single strand incision
DNA containing single strand nick (5' phosphate, 3' hydroxyl)
DNA containing 1-2 base mismatch and single-strand incision
Phosphatidylethanolamine is the donor of the phosphorylethanolamine linked to the alpha1,4-linked mannose of yeast GPI structures
Receptor specificity of the fibroblast growth factor family
Regulation of molecular chaperone gene transcription involves the serine phosphorylation, 14-3-3 epsilon binding, and cytoplasmic sequestration of heat shock factor 1
Thrombin and lysophosphatidic acid receptors utilize distinct rhoGEFs in prostate cancer cells
Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa gene
6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase: a metabolic signaling enzyme.
Characterization of the advanced glycation end-product receptor complex in human vascular endothelial cells
K48-polyubiquitinated partially digested Ag
Identification of Tcf4 residues involved in high-affinity beta-catenin binding
Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10
Proc. Natl. Acad. Sci. U.S.A. 104:20764-9
alpha Actin Chain (name copied from entity in Homo sapiens)
DNA Containing an Activin Response Element
Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation
Reduced half-life of holocarboxylase synthetase from patients with severe multiple carboxylase deficiency
Activation of NMDA receptor upon glutamate binding and postsynaptic events
F-actin (name copied from entity in Homo sapiens)
HSP27 oligomer (name copied from entity in Homo sapiens)
TCF dependent signaling in response to WNT
Wnt regulation of planar cell polarity (PCP)
Protein kinase C conventional and novel isoforms
Endostatins derived from collagens XV and XVIII differ in structural and binding properties, tissue distribution and anti-angiogenic activity
Groups II and III Metabotropic glutamate receptors
Phosphodiesterases, cyclic AMP-selective
Plk1 promotes nuclear translocation of human Cdc25C during prophase
Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins
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Innate immune recognition of an AT-rich stem-loop DNA motif in the Plasmodium falciparum genome
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Functional characterization of three novel tissue-specific anion exchangers SLC26A7, -A8, and -A9
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Phosphorylation of p40AUF1 regulates binding to A + U-rich mRNA-destabilizing elements and protein-induced changes in ribonucleoprotein structure
Regulation of A + U-rich element-directed mRNA turnover involving reversible phosphorylation of AUF1
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A 40-bp RNA element that mediates stabilization of vascular endothelial growth factor mRNA by HuR
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Complementation cloning identifies CDG-IIc, a new type of congenital disorders of glycosylation, as a GDP-fucose transporter deficiency
Antigen presentation and the ubiquitin-proteasome system in host-pathogen interactions
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Organic anion-transporting polypeptide B (OATP-B) and its functional comparison with three other OATPs of human liver
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Clearance of p16Ink4a-positive senescent cells delays ageing-associated disorders
Smad3-Smad4 and AP-1 complexes synergize in transcriptional activation of the c-Jun promoter by transforming growth factor beta
Physicochemical characterization and molecular organization of the collagen A and B chains
Another look at collagen V and XI molecules
Human taste cells express the G protein alpha-gustducin and neuron-specific enolase
A human homolog of the vaccinia virus HindIII K4L gene is a member of the phospholipase D superfamily
Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter
AXIN mutants destabilize the destruction complex, activating WNT signaling
In situ visualization of DNA double-strand break repair in human fibroblasts.
Nascent pre-mRNA with 5'-GMP dissociated from CE
Nascent pre-mRNA with 5'-GMP associated with CE
Platelet-collagen interaction: is GPVI the central receptor?
The role of flavin-containing monooxygenases in drug metabolism and development
Molecular cloning and functional expression of the K-Cl cotransporter from rabbit, rat, and human. A new member of the cation-chloride cotransporter family
2-acyl-sn-glycero-3-phosphoserine [ChEBI:37646]
ChEBI:37642 (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA
ChEBI:37643 (25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA
Cholesterol homeostasis in human brain: turnover of 24S-hydroxycholesterol and evidence for a cerebral origin of most of this oxysterol in the circulation
Nanomechanical heterogeneity in the gap and overlap regions of type I collagen fibrils with implications for bone heterogeneity
Mitochondrial aspartyl-tRNA synthetase deficiency causes leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation
Regulation of the biosynthesis of 4,7,10,13,16,19-docosahexaenoic acid
Double-strand DNA containing a thymine glycol
DNA strand break containing an incision 5' to an AP site
DNA containing an apurinic/apyrimidinic (AP) site
Double-strand DNA containing a dihydrouracil
Double-strand DNA containing a cytosine glycol
Proteins Inserted into Inner Membrane by TIMM23 SORT
Precursors Inserted into Mitochondrial Inner Membrane by TIMM23 SORT
Double-strand DNA containing a formamidopyrimidine
Glycoprotein with fucosyl alpha-1,6-GlcNAc
Isoforms of mammalian adenylyl cyclase: multiplicities of signaling
Glycans (no glucose) bound to unfolded protein
(ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI
Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria.
nascent polypeptide with signal sequence
The platelet P2 receptors in arterial thrombosis
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Genetic evidence that phosphatidylserine synthase II catalyzes the conversion of phosphatidylethanolamine to phosphatidylserine in Chinese hamster ovary cells
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mRNA Transcript Targeted by HuR Phosphorylated on Ser158 and Ser318.
mRNA Transcript Targeted by Tristetraproline
mRNA Transcript Targeted by HuR Phosphorylated on Ser221 and Ser318
mRNA Transcript Targeted by HuR with Unknown Phosphorylation
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Analysis of heparin, alpha-dystroglycan and sulfatide binding to the G domain of the laminin alpha1 chain by site-directed mutagenesis
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RNA-binding protein in RNP (ribonucleoprotein) complexes
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Expression and function of the human androgen-responsive gene ADI1 in prostate cancer
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mRNA with premature termination codon not preceding exon junction
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mature miRNA (double-stranded), 21-24 nucleotides
mature miRNA (single-stranded), 21-24 nucleotides
siRNA (double-stranded) 21-24 nucleotides
siRNA (single-stranded) 21-24 nucleotides
Groucho binds two conserved regions of LEF-1 for HDAC-dependent repression
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Cleaved RNA with 5' Phosphate and 3' Hydroxyl
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mRNA Transcript Targeted by AUF1(hnRNP D0)
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Molecular cloning and characterization of a full-length complementary DNA encoding human acid ceramidase. Identification Of the first molecular lesion causing Farber disease
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oligoribonucleotide with a 5'-diphosphate
mature mRNA (eukaryotic, capped and deadenylated)
Products of the grg (Groucho-related gene) family can dimerize through the amino-terminal Q domain
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Structure, function, and regional distribution of the organic cation transporter OCT3 in the kidney
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mRNA with premature termination codon preceding exon junction
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Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1
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Mature intronless transcript derived mRNA
Kinetic analysis of the interactions between vaccinia virus complement control protein and human complement proteins C3b and C4b
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Cleavage and shedding of E-cadherin after induction of apoptosis
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WLS-dependent secretion of WNT3A requires Ser209 acylation and vacuolar acidification
The protein kinase/endoribonuclease IRE1alpha that signals the unfolded protein response has a luminal N-terminal ligand-independent dimerization domain
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Cloning of a putative human voltage-gated chloride channel (CIC-2) cDNA widely expressed in human tissues
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CREB phosphorylation through the activation of CaMKK
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Wnt signals across the plasma membrane to activate the beta-catenin pathway by forming oligomers containing its receptors, Frizzled and LRP
Induction of chondrogenesis in neural crest cells by mutant fibroblast growth factor receptors
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damaged DNA substrate inserted with correct base complement
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damaged DNA substrate with misinserted bases
Elongated DNA template with bypassed lesion
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Regulation of purine synthesis de novo in human fibroblasts by purine nucleotides and phosphoribosylpyrophosphate
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Sprouty-4 negatively regulates cell spreading by inhibiting the kinase activity of testicular protein kinase
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Interfacial kinetic and binding properties of mammalian group IVB phospholipase A2 (cPLA2beta) and comparison with the other cPLA2 isoforms
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Characterization of human D-amino acid oxidase
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The subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and nonphosphorylated monomers
Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagen
Collagens: molecular biology, diseases, and potentials for therapy
Cloning, expression, and pharmacology of four human 5-hydroxytryptamine 4 receptor isoforms produced by alternative splicing in the carboxyl terminus
Laminin network (name copied from entity in Homo sapiens)
Collagen type I, II, III, IV, V, XI fibrils
Collagen type V fibre (name copied from entity in Homo sapiens)
Collagen type XI fibre (name copied from entity in Homo sapiens)
Collagen type XXIV fibre (name copied from entity in Homo sapiens)
Collagen type XXVII fibre (name copied from entity in Homo sapiens)
Collagen type II fibre (name copied from entity in Homo sapiens)
Collagen type III fibre (name copied from entity in Homo sapiens)
Cyclic GMP-dependent protein kinases (PKGs)
Collagen alpha-1(XVII) transmembrane regions
Cleaved collagen type XV multimer (name copied from entity in Homo sapiens)
Collagen type XVIII multimer (name copied from entity in Homo sapiens)
Collagen type XV multimer (name copied from entity in Homo sapiens)
Collagen alpha-1(XVIII) chain endostatin-like fragments
Cleaved collagen type XVIII multimer (name copied from entity in Homo sapiens)
Pig-n, a mammalian homologue of yeast Mcd4p, is involved in transferring phosphoethanolamine to the first mannose of the glycosylphosphatidylinositol
May the force be with you: Myosin-X in phagocytosis
Platelet releasate (inferred) cytosolic proteins
C-terminal EH domain containing proteins
Two conserved sequence blocks within eukaryotic tRNA genes are major promoter elements
Mapping ligand binding domains in chimeric fibroblast growth factor receptor molecules. Multiple regions determine ligand binding specificity
Subcellular localization and lysophospholipase/transacylation activities of human group IVC phospholipase A2 (cPLA2gamma)
Phosphorylation and activation of a cAMP-specific phosphodiesterase by the cAMP-dependent protein kinase. Involvement of serine 54 in the enzyme activation.
Competitive binding of AUF1 and TIAR to MYC mRNA controls its translation
The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase
Wilms tumor suppressor WTX negatively regulates WNT/beta-catenin signaling
IL-7-induced proliferation of recent thymic emigrants requires activation of the PI3K pathway
Collagenous transmembrane proteins: recent insights into biology and pathology
Analysis of deletions of the carboxyl terminus of the epidermal growth factor receptor reveals self-phosphorylation at tyrosine 992 and enhanced in vivo tyrosine phosphorylation of cell substrates
3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate [ChEBI:37393]
1,2-Diacyl-sn-glycero-3-phospho-sn-glycerol 3'-phosphate
3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphates
3(3-Phosphatidyl-)L-glycerol 1-phosphate
3(3-sn-Phosphatidyl)-sn-glycerol 1-phosphate
3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate
Idiopathic chronic megaloblastic anemia in children
Myeloproliferative disorder FOP-FGFR1 fusion kinase recruits phosphoinositide-3 kinase and phospholipase Cgamma at the centrosome
Myelin-associated inhibitors of axonal regeneration in the adult mammalian CNS
Congenital disorder of glycosylation id presenting with hyperinsulinemic hypoglycemia and islet cell hyperplasia
TICAM-1, an adaptor molecule that participates in Toll-like receptor 3-mediated interferon-beta induction
Role of aquaporin-7 and aquaporin-9 in glycerol metabolism; involvement in obesity
The human phosphatidylinositol phosphatase SAC1 interacts with the coatomer I complex
The nuclear lamins: flexibility in function
VEGF receptor expression and signaling in human bladder tumors
Discovery of the aquaporins and development of the field
Type beta transforming growth factor in human platelets: release during platelet degranulation and action on vascular smooth muscle cells
Muscarinic Acetylcholine Receptor M3 activates Gq
Gq alpha:G beta:G gamma dissociates to Gq alpha:GTP and G beta:G gamma
Alpha-2 adrenoceptors bind catecholamines
Acetylcholine binds Muscarinic Acetylcholine Receptor M3
Diacylgycerol activates Protein kinase C, alpha type
Metalloproteinase/Presenilin1 processing of ephrinB regulates EphB-induced Src phosphorylation and signaling
Activated Phospholipase C beta-1 hydrolyzes 1-Phosphatidyl-D-myo-inositol 4,5-bisphosphate
K63polyUb (name copied from entity in Homo sapiens)
DMQ10H2 is hydroxylated to DeMQ10H2 by COQ7
Transport of Extracellular Glucose to the Cytosol by GLUT1 and GLUT2
ADP-ATP translocase maintains a high ADP:ATP ratio in the matrix
Calcium Influx through Voltage-gated Calcium Channels
Activated Adenylyl cyclase synthesizes cyclic AMP
Potassium voltage-gated channels close in reponse to PKA
ER calcium channels open in response to activated PKA
Sphingomyelin phosphodiesterase (SMPD1) hydrolyses sphingomyelin to ceramide (lysosome)
Galactocerebrosidase cleaves the galactosyl bond of galactocerebroside to form ceramide
Both hexosaminidase A and B can cleave GalNAc from globoside
Alpha-galactosidase A removes a terminal galactose from alpha-D-galactoside oligomers
Beta-galactosidase hydrolyses GM1 to GM2
Cloning and initial characterization of a new subunit for mammalian serine-palmitoyltransferase
Beta-galactosidase can also hydrolyse globosides to form cerebrosides
sphingosine 1-phosphate + H2O => sphingosine + orthophosphate [extracellular]
sphingosine 1-phosphate => phosphoethanolamine + hexadec-2-enal
sphingosine +ATP => sphingosine 1-phosphate + ADP
sphingosine 1-phosphate + H2O => sphingosine + orthophosphate [cytosolic - PPAP]
MDMQ10H2 is methylated to DMQ10H2 by COQ5
IA1 is NGN3-dependent and essential for differentiation of the endocrine pancreas
Ceramide glucosyltransferase (UGCG) catalyses the transfer of glucose to ceramide
PHB and all-E-10PrP2 are combined into DHB by COQ2
Glucosylceramidase 2 cleaves the glucosidic bond of glucocerebroside to form ceramide (plasma membrane)
Acid ceramidase hydrolyses ceramide into sphingosine and free fatty acid (lysosome)
Ectonucleotide pyrophosphatase/phosphodiesterase 7 (ENPP7) hydrolyses sphingomyelin
Steryl sulfatase hydrolyses sulfate from steroid sulfates
Sphingomyelin phosphodiesterase 2 and 3 (SMPD2 and 3) hydrolyse sphingomyelin to ceramide (plasma membrane)
ceramide + H2O <=> stearate + sphingosine [endoplasmic reticulum]
Arachidonic acid is epoxidated to 5,6-EET by CYP(4)
Arachidonic acid is epoxidated to 8,9/11,12/14,15-EET by CYP(5)
p-Y179,Y191-SDC2 cluster (name copied from entity in Homo sapiens)
p-EPH:ephrin oligomers (name copied from entity in Homo sapiens)
12R-HpETE is reduced to 12R-HETE by GPX1/2/4
Characterization of yeast methyl sterol oxidase (ERG25) and identification of a human homologue
5S-HpETE is reduced to 5S-HETE by GPX1/2/4
Arachidonic acid is hydroxylated to 20-HETE by CYP(3)
Arachidonic acid is hydroxylated to 19-HETE by CYP(2)
EPH-ephrin oligomers (name copied from entity in Homo sapiens)
Arachidonic acid is hydroxylated to 16/17/18-HETE by CYP(1)
12S-HpETE is reduced to 12S-HETE by GPX1/2/4
sphinganine (dihydrosphingosine) +ATP => sphinganine 1-phosphate + ADP
Phosphorylation of RasGRP3 on threonine 133 provides a mechanistic link between PKC and Ras signaling systems in B cells
sphinganine + stearyl-CoA => dihydroceramide + CoASH
sphinganine 1-phosphate => phosphoethanolamine + hexadecanal
ditrans,polycis-polyprenol [ChEBI:67132]
ceramide + H2O => stearate + sphingosine [Golgi]
dihydroceramide + NADPH + H+ + O2 => phytoceramide + NADP+ + H2O
dihydroceramide + NAD(P)H + H+ + O2 => ceramide + NAD(P)+ + H2O
palmitoyl-CoA + serine => 3-ketosphinganine + CoASH + CO2
monophospho-CERT + 2 ATP => multiphospho-CERT + 2 ADP
phosphatidylcholine + ceramide <=> sphingomyelin + diacylglycerol [SGMS2]
phosphatidylcholine + ceramide <=> sphingomyelin + diacylglycerol [SGMS1]
Activation of linoleic acid to linoleoyl-CoA
Desaturation of Linoleoyl-CoA to gamma-linolenoyl-CoA
Formation of DHA-CoA catalysed by 3-ketoacyl-CoA thiolase
Conversion of DHA-CoA to docosahexaenoic acid (DHA)
Dehydrogenation of 3-hydroxy tetracosahexaenoyl-CoA
Formation of DHA-CoA catalysed by sterol carrier protein X (SCPx)
Tyrosine phosphorylation of the c-cbl proto-oncogene protein product and association with epidermal growth factor (EGF) receptor upon EGF stimulation
Collagen type II fibril (name copied from entity in Homo sapiens)
Collagen type V fibril (name copied from entity in Homo sapiens)
Collagen type III fibril (name copied from entity in Homo sapiens)
Hydration of delta2-tetracosaheptaenoyl-CoA to 3-hydroxy tetracosahexaenoyl-CoA
Smooth muscle/non-muscle myosin 2 heavy chains
Oxidation of tetracosapentaenoyl-CoA to delta2-tetracosaheptaenoyl-CoA
Translocation of tetracosahexaenoyl-CoA to peroxisomes
Desaturation of tetracosapentaenoyl-CoA to tetracosahexaenoyl-CoA
K48polyUb (name copied from entity in Homo sapiens)
Cleavage of the gamma-glutamyl bond of LTC4 forms LTD4
Thromboxane synthase (CYP5A1) mediates the isomerization of prostaglandin H2 to thromboxane A2
PGH2 is degraded to 12S-HHT and MDA by TBXAS1
LTC4 is exported from the cytosol by ABCC1
ABCC1 mediates LTC4 export from the cell
Translocation of tetracosapentaenoyl-CoA to peroxisomes
Ghost homologue of Activated WAVE2 and WASP/N-WASP
Desaturation of tetracosatetraenoyl-CoA to tetracosapentaenoyl-CoA
Prostaglandin E synthase isomerizes PGH2 to PGE2
poly(deoxyadenylic-deoxythymidylic) acid
Desaturation of dihomo-gamma-lenolenoyl-CoA to arachidonoyl-CoA
Collagen type XXIV fibril (name copied from entity in Homo sapiens)
Collagen type XXVII fibril (name copied from entity in Homo sapiens)
Collagen type I fibril (name copied from entity in Homo sapiens)
Collagen type XI fibril (name copied from entity in Homo sapiens)
Collagen type I fibril with deH-HLNL (name copied from entity in Homo sapiens)
Collagen type I fibril with allysines (name copied from entity in Homo sapiens)
Collagen type I fibril with dehydro-lysinonorleucine (name copied from entity in Homo sapiens)
Collagen type I fibril with lysyl-pyridinoline cross-links (name copied from entity in Homo sapiens)
Collagen type I fibril with hydroxylysino-5-ketonorleucine crosslinks (name copied from entity in Homo sapiens)
Collagen type I fibril with lysino-5-ketonorleucine cross-links (name copied from entity in Homo sapiens)
Collagen type I fibril with hydroxyallysines (name copied from entity in Homo sapiens)
Vitronectin receptor-mediated phagocytosis of cells undergoing apoptosis
Mutations in iron-sulfur cluster scaffold genes NFU1 and BOLA3 cause a fatal deficiency of multiple respiratory chain and 2-oxoacid dehydrogenase enzymes
Phosphorylation of ChREBP at Thr(666) by PKA
Activated Adenylate cyclase catalyses cAMP synthesis
Phosphorylation of pChREBP (Thr 666) at Ser(196) by PKA
PhosphoChREBP (Thr 666) is exported to cytosol
Dephosphorylation of pChREBP (Ser 196) by PP2A
Phosphorylation of ChREBP at Serine 568 by AMPK
Activation of PP2A by Xylulose-5-phosphate
Nuclear transport of pChREBP (Thr 666) protein
LKB1 phosphorylates the alpha subunit of AMPK heterotrimer
AMP binds to gamma subunit of AMP kinase heterotrimer
Function of the syndecan-4 cytoplasmic domain in oligomerization and association with ?-actinin in turkey muscle satellite cells
The cofactor BH4 is required for electron transfer in the eNOS catalytic cycle
Dephosphorylation of pChREBP (Thr 666) by PP2A
Dephosphorylation of pChREBP (Ser 568) by PP2A
STIM1 heteromultimerizes TRPC channels to determine their function as store-operated channels
Collagen type I fibre (name copied from entity in Homo sapiens)
Collagen type I fibril with lysyl-pyrrole cross-links (name copied from entity in Homo sapiens)
DHNTP is dephosphorylated by PTPS to PTHP
Collagen type I fibril with hydroxylysyl-pyridinoline cross-links (name copied from entity in Homo sapiens)
PTPS is phosphorylated by cGMP-dependant protein kinase II
Collagen type I fibril with histidino-hydroxylysinoleucine cross-links (name copied from entity in Homo sapiens)
GCH1 reduces GTP to dihydroneopterin triphosphate
Collagen type I fibril with hydroxylysyl-pyrrole cross-links (name copied from entity in Homo sapiens)
Uncoupled eNOS favours the formation of superoxide
The enzymes and control of eukaryotic mRNA turnover
Vertebrate agmatinases: what role do they play in agmatine catabolism?
Agmatine: at the crossroads of the arginine pathways
Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1
Mechanistic and kinetic analysis of the DcpS scavenger decapping enzyme
Purification and characterization of a soluble form of mammalian adenylyl cyclase
Cloning, characterization, and modeling of mouse and human guanylate kinases
Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration
Isolation and characterization of the faciogenital dysplasia (Aarskog-Scott syndrome) gene: a putative Rho/Rac guanine nucleotide exchange factor
Analysis of phosphoinositide binding domain properties within the myotubularin-related protein MTMR3
Subcellular locations of phosphatidylinositol 4-kinase isoforms
The cellular physiology of carbonic anhydrases
A unique fold of phospholipase C-beta mediates dimerization and interaction with G alpha q
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Interferon-inducible ubiquitin E2, Ubc8, is a conjugating enzyme for protein ISGylation
Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes
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FGF-receptor substrate 2 functions as a molecular sensor integrating external regulatory signals into the FGF pathway
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Identification of a mammalian mitochondrial porphyrin transporter
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Human Sos1: a guanine nucleotide exchange factor for Ras that binds to GRB2
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The mechanism of phospholipase C-gamma1 regulation
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A dimerization-dependent mechanism drives RAF catalytic activation
KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints
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Caspase-1-dependent processing of pro-interleukin-1beta is cytosolic and precedes cell death
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Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
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Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha
S33 mutants of beta-catenin aren't phosphorylated
Involvement of p90rsk in neurite outgrowth mediated by the cell adhesion molecule L1
Catalytic properties of human manganese superoxide dismutase
Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response
Structure and interactions of NCAM Ig1-2-3 suggest a novel zipper mechanism for homophilic adhesion
Synthesis of glycosylphosphatidylinositol (GPI)
An alternative branch of the nonsense-mediated decay pathway
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Metabolism, function and mass spectrometric analysis of bis(monoacylglycero)phosphate and cardiolipin
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L13a-mediated translational silencing of Ceruloplasmin expression
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An adjacent pair of human NUDT genes on chromosome X are preferentially expressed in testis and encode two new isoforms of diphosphoinositol polyphosphate phosphohydrolase
Immunohistochemical detection of K-sam protein in stomach cancer
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Molecular and biochemical characterization of lecithin retinol acyltransferase.
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FEEL-1, a novel scavenger receptor with in vitro bacteria-binding and angiogenesis-modulating activities
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Astrocytic Glutamate-Glutamine Uptake And Metabolism
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Regulation of PAK-2p34 activity by PS-GAP/RHG10
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The internally truncated LRP5 receptor presents a therapeutic target in breast cancer
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Neurotransmitter Receptor Binding And Downstream Transmission In The Postsynaptic Cell
Rho-associated kinase of chicken gizzard smooth muscle
Methionine regeneration and aspartate aminotransferase in parasitic protozoa
Peptide fragment of the m3 muscarinic acetylcholine receptor activates G(q) but not G(i2)
Nuclear-cytoplasmic shuttling of Axin regulates subcellular localization of beta-catenin
Proc. Natl. Acad. Sci. U.S.A. 101:2882-7
Immunohistochemical detection of alpha1E voltage-gated Ca(2+) channel isoforms in cerebellum, INS-1 cells, and neuroendocrine cells of the digestive system
Identification of a target RNA motif for RNA-binding protein HuR
Identification and characterization of a gene encoding human LPGAT1, an endoplasmic reticulum-associated lysophosphatidylglycerol acyltransferase
(Gal)1 (GalNAc)1 (Glc)1 (Neu5Ac)1 (Cer)1
N-acetyl-beta-D-galactosaminyl-(1->4)-[alpha-N-acetylneuraminosyl-(2->3)]-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide [ChEBI:51013]
The major sites of cellular phospholipid synthesis and molecular determinants of Fatty Acid and lipid head group specificity
The p24 family and selective transport processes at the ER-Golgi interface
Proteinases involved in matrix turnover during cartilage and bone breakdown
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Histone variants--ancient wrap artists of the epigenome
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Pathways of chaperone-mediated protein folding in the cytosol
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Molecular mechanisms of translational control
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Human Ehlers-Danlos syndrome type VII C and bovine dermatosparaxis are caused by mutations in the procollagen I N-proteinase gene
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Human complement factor I: analysis of cDNA-derived primary structure and assignment of its gene to chromosome 4
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Concerted dephosphorylation of the transcription factor NFAT1 induces a conformational switch that regulates transcriptional activity
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Differential role of human choline kinase alpha and beta enzymes in lipid metabolism: implications in cancer onset and treatment
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Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency
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Activation and signaling of the p38 MAP kinase pathway
Synapse formation is regulated by the signaling adaptor GIT1
Complete coding sequence, promoter region, and genomic structure of the human ABCA2 gene and evidence for sterol-dependent regulation in macrophages
Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases
Molecular cloning of human phosphomevalonate kinase and identification of a consensus peroxisomal targeting sequence
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Silencing mediator for retinoid and thyroid hormone receptor and nuclear receptor corepressor attenuate transcriptional activation by the beta-catenin-TCF4 complex
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Hereditary proteinuria syndromes and mechanisms of proteinuria
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Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes
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Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomics
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Cloning and characterization of a human type II receptor for bone morphogenetic proteins
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MOBKL1A/MOBKL1B phosphorylation by MST1 and MST2 inhibits cell proliferation
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Slit stimulation recruits Dock and Pak to the roundabout receptor and increases Rac activity to regulate axon repulsion at the CNS midline
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TAG-1/axonin-1 is a high-affinity ligand of neurocan, phosphacan/protein-tyrosine phosphatase-zeta/beta, and N-CAM
Human placental steroid sulfatase: purification and properties
Wnt signaling through Dishevelled, Rac and JNK regulates dendritic development
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A roller coaster ride with the mitotic cyclins
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Unspecific permeation and specific exchange of adenine nucleotides in
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_150776.1
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Characterization of the structure and function of a new mitogen-activated protein kinase (p38beta)
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In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2
Biochem. Biophys. Res. Commun. 254:693-8
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DNA damage signaling and p53-dependent senescence after prolonged beta-interferon stimulation
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Expression of adenylyl cyclase subtypes in pancreatic beta-cells
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Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1
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USP15 stabilizes TGF-? receptor I and promotes oncogenesis through the activation of TGF-? signaling in glioblastoma
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Quantitative studies on the release of platelet fibrinogen by thrombin
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Prominent expression of FRS2beta protein in neural cells and its association with intracellular vesicles
Molecular cloning and expression of a cDNA for human kidney cysteine conjugate beta-lyase
Transforming potential of alternatively spliced variants of fibroblast growth factor receptor 2 in human mammary epithelial cells
C-to-U RNA editing: mechanisms leading to genetic diversity.
Cloning, genomic organization, and characterization of a human cholinephosphotransferase
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RAF1-activated MEK1 is found on the Golgi apparatus in late prophase and is required for Golgi complex fragmentation in mitosis
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Variable effects of the conserved RNA hairpin element upon 3' end processing of histone pre-mRNA in vitro.
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Endofin, a FYVE domain protein, interacts with Smad4 and facilitates transforming growth factor-beta signaling
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T41 mutants of beta-catenin aren't phosphorylated
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PDGF stimulation of inositol phospholipid hydrolysis requires PLC-gamma 1 phosphorylation on tyrosine residues 783 and 1254
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The concentrative nucleoside transporter family, SLC28
A current review of fatty acid transport proteins (SLC27)
Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution
Demethylation of trimethylated histone H3 Lys4 in vivo by JARID1 JmjC proteins
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There are two transporters of this type; The genes SLC20A1 and SLC20A2 encode for PiT1 (phosphate transporter 1) and PiT2 respectively. They both have a broad tissue distribution and may play a general housekeeping role in phosphate transport such as absorbing phosphate from interstitial fluid and in extracellular matrix and cartilage calcification as well as in vascular calcification. These proteins were originally described as retroviral receptors for the gibbin ape leukemia virus receptor 1 (GLVR1, now called PiT1) (O'Hara B et al, 1990) and GLVR2 (now called PiT2) (van Zeijl M et al, 1994). However, they were found to possess Na+-coupled phosphate cotransporter function (Fernandes I et al, 1999). The transport is electrogenic with a stoichiometry of 2:1 (Na+:Pi).
SLC34A1 encodes Na+/Pi cotransporter (NaPi-IIa) which is expressed in the kidney in the renal proximal tubule (Magagnin S et al, 1993). SLC34A2 encodes NaPi-IIb which is abundantly expressed in lung and to a lesser degree in tissues of epithelial origin including small intestine, pancreas, prostate, and kidney (Field JA et al, 1999). Both NaPi-IIa and NaPi-IIb cotransport divalent Pi (HPO4[2-]) with three Na+ ions (electrogenic transport). Defects in SLC34A1 are the cause of hypophosphatemic nephrolithiasis/osteoporosis type 1 (NPHLOP1) (Prie D et al, 2002). Defects in SLC34A2 are a cause of pulmonary alveolar microlithiasis (Corut A et al, 2006).
The human SLC26 gene family consists of eleven members which encode multifunctional anion exchangers.These exchangers are capable of transporting a variety of anions such as sulphate, bicarbonate, oxalate, hydroxyl, formate, iodide and chloride. SLC26 members can be grouped according to functional similiarities and three groups can be classified this way. Group 1 are selective sulphate transporters and include SLC26A1 and 2. Group 2 are Cl-/HCO3- exchangers and include SLC26A3, 4 and 6. Group 3 function as ion channels and include SLC26A7 and 9.
The SLC34 family of type II Na+/Pi cotransporters consist of three members; NaPi-IIa (SLC34A1), NaPi-IIb (SLC34A2) and NaPi-IIc (SLC34A3) (Murer H et al, 2004). They are expressed mainly in the kidney and small intestine, located at the apical sites of epithelial cells although other areas of the body express them to a lesser extent. NaPi-IIa and b cotransports divalent Pi (HPO4[2-]) with three Na+ ions (electrogenic transport) whereas NaPi-IIc cotransports divalent Pi with two Na+ ions (electroneutral transport).
SLC34A3 is almost exclusively expressed in the kidney and encodes the Na+/Pi cotransporter NaPi-IIc (Segawa H et al, 2002). The protein is located at apical membranes of proximal tubules. It cotransports two Na+ ions with every Pi (electroneutral transport). Defects in SLC34A3 are the cause of hereditary hypophosphatemic rickets with hypercalciuria (HHRH) (Bergwitz C et al, 2006)
K+/Cl- cotransport is implicated not only in regulatory volume decrease, but also in transepithelial salt absorption, renal K+ secretion, myocardial K+ loss during ischemia and regulation of neuronal Cl- concentration. Four genes (SLC12A4-7) encode the K+/Cl- cotransporters KCC1-4 respectively. Cotransport of K+ and Cl- is electroneutral with a 1:1 stoichiometry. These cotransporters function as homomultimers or heteromultimers with other K+/Cl- cotransporters. SLC12A4 encodes KCC1 (Gillen CM et al, 1996). KCC1 is ubiquitously expressed, suggesting a housekeeping role in the regulation of cell volume. SLC12A5 encodes KCC2 (Song L et al, 2002). KCC2's expression is restricted to neurons in the CNS and retina. It is thought KCC2 is important for Cl- homeostasis in neurons. SLC12A6 encodes KCC3 (Race JE et al, 1999; Mount DB et al, 1999). KCC3 is highly expressed in heart, brain, spinal cord, kidney, muscle, pancreas and placenta. Defects in SLC12A6 are a cause of agenesis of the corpus callosum with peripheral neuropathy (ACCPN) (Howard HC et al, 2002). SLC12A7 encodes KCC4 (Mount DB et al, 1999) which is widely expressed, especially in the kidney. It is thought to play a role in transepithelial transport of Cl- by the proximal tubule.
The cation-chloride cotransporter family (SLC12 gene family) are membrane proteins that cotranslocate chloride (Cl-) with either Na+, K+, or both cations electroneutrally. The general topology of these proteins feature 12 transmembrane domains flanked by hydrophilic NH2 and COOH-terminal domains. They are secondary transporters and movement of these cations is determined by gradients established by primary transporters such as Na+-K+-ATPase. Cotransporters that use Na+ as the driving force move Cl- into the cell because Na+ concentration is higher in the extracellular region. Conversely, cotransporters that use K+ as the driving force move Cl- out of the cell because K+ concentration is higher inside the cell. The SLC12 gene family contains nine members, of which seven are clearly characterized genes and two are orphans. They encode cotransporter proteins which are 1) involved in Cl- homeostasis, 2) regulate cell volume, 3) involved in transepithelial ion movement (salt reabsorption in the kidney) and 4) involved in response to neurotransmitters such as GABA. Three different cotransporter subtypes are expressed by the seven characterized genes; one thiazide-sensitive Na+/Cl- cotransporter, two loop diuretic-sensitive Na+, K+/2Cl- cotransporters and four K+/Cl- cotransporters (Gamba G, 2005; Hebert SC et al, 2004).
The proteins responsible for the exchange of Cl- with HCO3- are members of the SLC4 (1-3) and SLC26 (3, 4 and 6) transporter families. SLC4 members are discussed in the section "Bicarbonate transporters". SLC26A3 (Chloride anion exchanger, Down-regulated in adenoma, DRA) is expressed in the mucosa of the colon and helps mediate electrolyte and fluid absorption (Schweinfest CW et al, 1993). Defects in SLC26A3 cause congenital chloride diarrhea (CLD), a disease characterized by watery stools containing an excess of chloride (Hoeglund P et al, 1996). SLC26A4 (Pendrin) is highly expressed in the adult thyroid and its activity is necessary for production of thyroid hormone. (Everett et al, 1997). Mutations in this gene are associated with Pendred syndrome, an autosomal-recessive disease. It is the most common form of syndromic deafness (Everett et al, 1997). Pendred syndrome is also characterized by hypothyroidism. SLC26A6 encodes a protein involved in transporting chloride, oxalate, sulfate and bicarbonate (Waldegger S et al, 2001). It is ubiquitously expressed, the highest levels present in kidney and pancreas.
Group 3 members (SLC26A7 and 9) function as ion channels. SLC26A7 encodes an ion channel which is abundantly expressed in medullary collecting duct cells of the kidney, high endothelial venule enothelial cells (HEVEC) and gastric parietal cells (Vincourt JB et al, 2002; Lohi H et al, 2002). SLC26A9 encodes an ion channel which is predominantly expressed on the lumenal side of the bronchiolar and alveolar epithelium of lung (Lohi H et al, 2002). Both these ion channels appear to transport Cl- without cotransport of HCO3- (Kim KH et al, 2005; Dorwart MR et al, 2007).
Two genes (SLC12A1 and SLC12A2) encode Na+,K+/2Cl- cotransporters (NKCC2 and NKCC1 respectively). SLC12A1 (Simon DB et al, 1996) is kidney-specific whilst SLC12A2 (Payne JA et al, 1995) is ubiquitously expressed. Two Cl- ions are electroneutrally transported into cells with a Na+ ion and a K+ ion.
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The SLC12A3 gene encodes for the Thiazide-sensitive sodium-chloride cotransporter (TSC). TSC mediates sodium and chloride removal from the distal convoluted tubule of the kidney (Mastroianni N et al, 1996). Defects in SLC12A3 are the cause of Gitelman syndrome (GS). GS is an autosomal recessive disorder that allows the kidneys to pass sodium, magnesium, chloride, and potassium into the urine, rather than being reabsorbed into the bloodstream (Simon DB et al, 1996). This cotransporter is the major target for thiazide-type diuretics, used in the treatment of hypertension, extracellular fluid overload and renal stone disease.
The SLC9 gene family encode proteins (sodium/proton exchangers, NHE or NHX) which exchange sodium (influx) for protons (efflux) electroneutrally. This mechanism is important because many metabolic processes generate acids which need to be removed to maintain pH. This is the major proton extruding system in cells, driven by the inward sodium ion chemical gradient. To date, there are eleven NHE genes, NHE1-11. NHE1-5 exchange cations at the cell membrane. NHE6-9 exchange cations at endosomal membranes or the trans-golgi network membranes.
NHE9 (SLC9A9) (Nakamura N et al, 2005) is expressed ubiquitously and thought to play a housekeeping role in pH homeostasis in the late endosome membrane.
NHE7 and 8 (SLC9A7,8) (Nakamura N et al, 2005) are expressed ubiquitously and thought to play a housekeeping role in pH homeostasis in the trans-golgi network.
NHE6 (SLC9A6) (Brett CL et al, 2002; Nakamura N et al, 2005) is expressed ubiquitously and thought to play a housekeeping role in pH homeostasis in early endosomes.
NHE1 (SLC9A1) is present in most cells and is the most extensively characterized member of this family (Sardet C et al, 1989). NHE2-4 (SLC9A2-4) (Malakooti J et al, 1999; Brant SR et al, 1995) are expressed mainly in the kidney and GI tract. NHE5 (SLC9A5) (Baird NR et al, 1999) is highly expressed in neuronal-enriched areas of the CNS.
SLC24A6 (NCKX6, NCLX) (Palty R et al, 2004) encodes a protein which can transport Li+ or Na+ in exchange for Ca2+ in an K+-independent manner (Cai X and Lytton J, 2004). Lithium exchange with calcium is shown here.
Calcium ions are used by cells as ubiquitous signalling molecules that control diverse physiological events. Three mammalian gene families control Ca2+ transport across plasma membranes and intracellular compartments (Lytton J, 2007). They are the Na+/Ca2+ exchanger family designated NCX (SLC8) (three members NCX1-3) (Quednau BD et al, 2004), the Na+/Ca2+-K+ exchanger family designated NCKX (SLC24) (five members NCKX1-5) (Schnetkamp PP, 2004) and a Ca2+/cation exchanger (NCKX6, NCLX) whose physiological function remains unclear.
The NCX (SCL8, Na+/Ca2+ exchanger) family is one of three families that control Ca2+ flux across the plasma membrane or intracellular compartments. They extrude Ca2+ from the cell, using the electrochemical gradient of Na+ as it flows into the cell. One Ca2+ is exchanged for three Na+. During this electrogenic exchange, the membrane potential is altered. NCX1 (SLC8A1) has a ubiquitous expression profile (highest expression in heart, brain and kidney) and was originally cloned and characterized from human cardiac muscle (Komuro I et al, 1992). Both NCX2 (SLC8A2) (Li Z et al, 1994) and NCX3 (SLC8A3) (Gabellini N et al, 2002) are expressed in the brain.
The five members of the NCKX (SLC24) family are all able to exchange one Ca2+ and one K+ for four Na+. They play a major role in the phototransduction cascade by controlling the Ca2+ concentration of the outer segments of retinal rod and cone cells during light and dark conditions. NCKX1 (SLC24A1) encodes an exchanger protein which is the most extensively studied member (Tucker JE et al, 1998). It is highly expressed in the eye. Other members are expressed in the brain and skin as well as the eye (Prinsen CF et al, 2000; Kraev A et al, 2001; Li XF et al, 2002; Lamason RL et al, 2005).
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Aquaporins: highways for cells to recycle water with the outside world
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Analysis of nucleocytoplasmic shuttling of NF kappa B proteins in human leukocytes
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Functional analysis of the purified anandamide-generating phospholipase D as a member of the metallo-beta-lactamase family
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Expression of prolyl 3-hydroxylase genes in embryonic and adult mouse tissues
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Characterization of human glucose transporter (GLUT) 11 (encoded by SLC2A11), a novel sugar-transport facilitator specifically expressed in heart and skeletal muscle
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The discoidin domain receptor tyrosine kinase DDR1 in arterial wound repair
Transfected muscarinic acetylcholine receptors selectively couple to Gi-type G proteins and Gq/11
Sphingosine kinase mediates vascular endothelial growth factor-induced activation of ras and mitogen-activated protein kinases
Tuberculosis - metabolism and respiration in the absence of growth
Grb4 and GIT1 transduce ephrinB reverse signals modulating spine morphogenesis and synapse formation
Tyrosine-phosphorylated Vav1 as a point of integration for T-cell receptor- and CD28-mediated activation of JNK, p38, and interleukin-2 transcription
Human multidrug-resistant cell lines: increased mdr1 expression can precede gene amplification
Newly made phosphatidylserine and phosphatidylethanolamine are preferentially translocated between rat liver mitochondria and endoplasmic reticulum
The secretory route of the leaderless protein interleukin 1beta involves exocytosis of endolysosome-related vesicles
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The human brain contains at least 100 billion neurons, each with the ability to influence many other cells. Clearly, highly sophisticated and efficient mechanisms are needed to enable communication among this astronomical number of elements. This communication occurs across synapses, the functional connection between neurons. Synapses can be divided into two general classes: electrical synapses and chemical synapses. Electrical synapses permit direct, passive flow of electrical current from one neuron to another. The current flows through gap junctions, specialized membrane channels that connect the two cells. Chemical synapses enable cell-to-cell communication using neurotransmitter release. Neurotransmitters are chemical agents released by presynaptic neurons that trigger a secondary current flow in postsynaptic neurons by activating specific receptor molecules. Neurotransmitter secretion is triggered by the influx of Ca2+ through voltage-gated channels, which gives rise to a transient increase in Ca2+ concentration within the presynaptic terminal. The rise in Ca2+ concentration causes synaptic vesicles (the presynaptic organelles that store neurotransmitters) to fuse with the presynaptic plasma membrane and release their contents into the space between the pre- and postsynaptic cells.
Potassium channels are tetrameric ion channels that are widely distributed and are found in all cell types. Potassium channels control resting membrane potential in neurons, contribute to regulation of action potentials in cardiac muscle and help release of insulin form pancreatic beta cells. Broadly K+ channels are classified into voltage gated K+ channels, Hyperpolarization activated cyclic nucleotide gated K+ channels (HCN), Tandem pore domain K+ channels, Ca2+ activated K+ channels and inwardly rectifying K+ channels.
Tandem pore domain K+ channels (K2p) produce leak K+ current which stabilizes negative membrane potential and counter balances depolarization. These channels are regulated by voltage independent mechanisms such as membrane stretch, pH, temperature. Tandem pore domain K+ channels have been classified into six subfamilies; tandem pore domains in weak rectifying K+ channel (TWIK), TWIK-related K+ channel (TREK), TWIK-related acid-sensitive K+ channel (TASK), TWIK-related alkaline pH-activated K+ channel (TALK), tandem pore domain halothane-inhibted K+ channel (THIK), TWIK-releated spinal cord K+ channel).
THIK channels are K+ leak channels that are not regulated by pH or temperature changes.
THIK subfamily has 2 members, THIK1 and THIK 2. THIK 1 forms functional homodimers whereas THIK2 function has not been demonstrated. THIK1 channels are inhibited by halothane. THICK1 channels form K+ leak channels and are not regulated by acidity or alkalanity changes.
A defined subset of the ABC transporter superfamily, the ABCA transporters, are highly expressed in monocytes and macrophages and are regulated by cholesterol flux which may indicate their role in in chronic inflammatory diseases (Schmitz and Kaminski 2001, Schmitz et al. 2000).
The 70-kDa peroxisomal membrane protein (PMP70) and the adrenoleukodystrophy protein (ALDP) are half ATP binding cassette (ABC) transporters in the peroxisome membrane. Mutations in the ALD gene encoding ALDP result in the X-linked neurodegenerative disorder adrenoleukodystrophy (Roerig et al. 2001). They are involved in metabolic transport of long and very long chain fatty acids into peroxisomes. ATP binding/hydrolysis by and phosphorylation of PMP70 and ALDP are involved in the regulation of fatty acid transport into peroxisomes (Tanaka et al. 2002).
ABCA3 plays an important role in the formation of pulmonary surfactant, probably by transporting lipids such as cholesterol (Klugbauer and Hofmann 1996, Yamano et al. 2001). Defects in ABCA3 are the cause of pulmonary surfactant metabolism dysfunction type 3 (SMDP3) [MIM:610921] (Shulenin et al. 2004). The exact roles of ABCA2 (Vulevic et al. 2001, Kaminski et al. 2001), ABCA6 (Kaminski & Wenzel et al. 2001), ABCA9 (Piehler et al. 2002), ABCA10 (Wenzel et al. 2003) and ABCA12 (Annilo et al. 2002), candidates for ABC lipid transporter-related activities, need to be elucidated. Even thought cholesterol-responsiveness has been noted in experimental systems, contribution of these proteins in regulation or in active transport is not yet clear.
Regulation of epithelial chloride flux, which is defective in patients with cystic fibrosis, may be mediated by phosphorylation of the cystic fibrosis transmembrane conductance regulator (CFTR) by cyclic AMP-dependent protein kinase (PKA) or protein kinase C (PKC). CFTR regulates both HCO(3)(-) secretion and HCO(3)(-) salvage in secretory epithelia.
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The multidrug resistance associated protein (MRPs) subfamily of the ABC transporter family can transport a wide and diverse range of organic anions that can be endogenous compounds and xenobiotics and their metabolites. All human MRPs (except MRP9) can mediate these transport reactions (Deeley et al. 2006). Separately, specific reactions have also been annotated to describe the roles of ABCC4 in platelet dense granule assembly, of ABCC1 in LTC4 export (an aspect of leukotriene synthesis), and of ABCC3 in bile salt efflux.
Mammalian ABC transporters are usually found on the plasma membrane and on organelles such as the ER and peroxisome but a small number are also located on the mitochondria. Here they are thought to play roles in heme biosynthesis and iron-sulphur cluster synthesis (Burke & Ardehali 2007).
The ATP-binding cassette (ABC) superfamily of active transporters involves a large number of functionally diverse transmembrane proteins. They transport a variety of compounds through membranes against steep concentration gradients at the cost of ATP hydrolysis. These substrates include amino acids, lipids, inorganic ions, peptides, saccharides, peptides for antigen presentation, metals, drugs, and proteins. The ABC transporters not only move a variety of substrates into and out of the cell, but are also involved in intracellular compartmental transport. Energy derived from the hydrolysis of ATP is used to transport the substrate across the membrane against a concentration gradient. Human genome contains 48 ABC genes; 16 of these have a known function and 14 are associated with a defined human disease (Dean et al. 2001, Borst and Elferink 2002, Rees et al. 2009).
Some members of the ABC transporter superfamily are able to mediate the efflux of a broad range of cytotoxic drugs from cells, leading to the name multidrug resistance (MDR) proteins (Seeger and van Veen 2009). The ABCB1 (P-glycoprotein 1[PGP], multidrug resistance protein 1 [MRP1]) is the most characterised MDR (Shen et al. 1986, Gottesman & Pastan 1988). ABCB5 (Frank et al. 2005) and ABCA8 (Tsuruoka et al. 2002) are newer members of MDRs.
The human gene ABCB6 encodes a mitochondrial half-type ATP-binding cassette (ABC) protein MTABC3 which is uniquely located on the outer mitochondrial membrane and is functional as a homodimer (Krishnamurthy et al. 2006). It plays a crucial role in heme synthesis by mediating porphyrin uptake into mitochondria (Mitsuhashi et al. 2000, Krishnamurthy et al. 2006).
Mitochondrial ABC transporters are thought to play a key role in iron metabolism and heme biosynthesis. All mitochondrial ABC transporters described to date are of the half-transporter type and would probably function as dimers (Ramjeesingh et al. 2003) but their dimerization partners have not yet been identified. ABC7 is the functional human orthologue of yeast Atm1p (Csere et al. 1998), is predicted to dimerize in the same way as Atm1p (Chloupková et al. 2004) and is probably involved in iron homeostasis. Defects in ABCB7 are the cause of X-linked sideroblastic anemia with ataxia (ASAT) [MIM:301310] (Allikmets et al. 1999). Human genes ABCB8 and ABCB10 encode mABC1 and mABC2 respectively (Hogue et al. 1999, Zhang et al 2000 respectively). They would be expected to dimerize, as demonstrated for mABC2 (Graf et al. 2004). Both are believed to have similar functionality to ABC7 although this has not been demonstrated yet.
Some members of the SLC4A family couple the transport of bicarbonate (HCO3-) to the movement of sodium ions (Na+), they being members 4, 5, 7 and 9. SLC4A4 (NBCe1) is an electrogenic sodium/bicarbonate cotransporter with a Na+:HCO3- stoichiometry of 1:3, although it can also be 1:2 (Burnham CE et al, 1997). SLC4A4 encodes a protein which is expressed in the kidney and pancreas, with lesser expression in many other tissues (Abuladze N et al, 1998). Mutations in SLC4A4 cause permanent isolated proximal renal tubular acidosis (pRTA) (results in accumulation of acid in the body due to a failure of the kidneys to effectively acidify urine) with ocular abnormalities (Igarashi T et al, 1999). SLC4A5 encodes a protein which is expressed in liver, spleen and testes, with lower levels expressed in parts of the brain and kidney (Sassani P et al, 2002). It may have a housekeeping function in regulating the pH of these tissues (Pushkin A et al, 2000). SLC4A7 (NBC3, NBCn1) encodes a protein which performs electroneutral cotransport of Na+ and HCO3- with a 1:1 stoichiometry. It is highly expressed in testes and spleen and, to a lesser extent, in many other tissues including heart, muscle, kidney and GI tract (Pushkin A et al, 1999). SLC4A9 (AE4) was originally thought to exchange Cl- with HCO3- (hence the name AE4) but this has not been reported. Consensus has emerged that it is indeed a Na+/HCO3- co-transporter (Lipovich L et al, 2001). It is predominantly expressed in the kidney, salivary glands, testes, thyroid glands and trachea (Parker MD et al, 2001).
The proteins responsible for the exchange of Cl- with HCO3- are members of the SLC4 (1-3) and SLC26 (3, 4, 6, 7 and 9) transporter families. The SLC26 members are discussed under the section "Multifunctional anion exchangers". SLC4A1 (Band 3, AE1, anion exchanger 1) was the first bicarbonate transporter gene to be cloned and sequenced (Lux SE et al, 1989). It is ubiquitous throughout vertebrates and in humans, is present on erythrocytes and the basolateral surfaces of kidney cells. The erythrocyte and kidney forms are different isoforms of the same protein (Kollert-Jons A et al, 1993). Mutations of erythroid AE1 determine the Diego blood group system (Bruce LJ et al, 1994). A more serious consequence of mutated erythroid AE1 is Hereditary spherocytosis (a disorder leading to haemolytic anaemia) (Jarolim P et al, 1995). Defects in the kidney form of AE1 cause distal (type1) renal tubular acidosis (an inability to acidify urine) (Bruce LJ et al, 1997). SLC4A2 (Non-erythroid band 3-like protein, AE2, anion exchanger 2) is widely expressed and is considered to be the 'housekeeping' isoform of the bicarbonate transporters (Demuth DR et al, 1986). SLC4A3 (Cardiac/brain band 3-like protein, AE3) is expressed in heart and brain (Yannoukakos D et al, 1994).
Respiratory oxidation in the mitochondria produces carbon dioxide (CO2) as a waste product. CO2 is in equilibrium with bicarbonate (HCO3-) and is the body's central pH buffering system. HCO3- is charged so cannot move across membranes unaided. The bicarbonate transport proteins move bicarbonate across the membrane. There are 14 genes which encode these transport proteins in mammals. Applying the Human Genome Organization's sytematic nomenclature to human genes, the bicarbonate transporters belong to the SLC4A and SLC26A families. Within SLC4A, there are two distinct subfamilies, functionally corresponding to the electroneutral Cl-/HCO3- exchangers and Na+-coupled HCO3- co-transporters (Romero MF et al, 2004; Cordat E and Casey JR, 2009).
Two genes encode Na+-dependent Cl-/HCO3- exchangers; SLC4A8 (NDCBE1) and 10 (NCBE). SLC4A8 (NDCBE1) encodes a exchanger protein which mediates Na+:HCO3- transport with a stoichiometry of 1:2:1 (Na+/HCO3-/Cl-). This protein is highly expressed in brain and spine and moderately expressed in trachea, thyroid, and kidney (Amlal H et al, 1999). SLC4A10 (NCBE, NBCn2) encodes a Na+-driven Cl-/HCO3- exchanger protein (Parker MD et al, 2008). It transports extracellular Na+ and HCO3- into cells in exchange for intracellular Cl- and H+, thus raising the intracellular pH.
Once the intrinsic GTPase hydrolyzes GTP to GDP, Galpha-i dissociates from adenylate cyclase, allowing it to re-associate with G-beta-gamma and starting a new cycle.
Guanine nucleotide-binding protein G(i) alpha (Gi-alpha) inhibits adenylate cyclase, thus inhibiting the production of cAMP from ATP and ultimately decreasing the activity of cAMP-dependent protein kinase.
GABA B receptors are G protein coupled receptors that are activated by GABA binding to the B1 subunit and B2 subunit alters the activity of adenylate cyclase by interacting with the G alpha i/alpha 0 subunit of the pertussis toxin sensitive G protein. The activation of GABA B receptors results in the inhibition of adenylate cyclase activity decreasing the levels of cyclic AMP production and hence the activity of Protein kinase A.
Binding of G beta gamma activates the GIRK/Kir3 channels that allow the efflux of K+ out of the cell resulting in a hyperpolarized membrane potential. This negative membrane potential prevents the activation of voltage dependent Ca2+ channels.
G-proteins in the Gi class inhibit adenylate cyclase activity, decreasing the production of cAMP from ATP, which has many consequences but classically results in decreased activity of Protein Kinase A (PKA). cAMP also activates the cyclic nucleotide-gated ion channels, a process that is particularly important in olfactory cells.
The chronic activation of mu-opioid receptors, which, when coupled to pertussis toxin-sensitive Galpha-i/o proteins, inhibit adenylyl cyclase (AC).
G proteins can deactivate themselves via their intrinsic GTPase activity, which hydrolyzes GTP to GDP. Effectors such as adenylate cyclase can increase the G protein GTPase rate, acting like GTPase-activating proteins (GAPs).
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Gamma-aminobutyric acid (GABA) is the chief inhibitory neurotransmitter in the mammalian central nervous system. GABA exerts its effects through two ligand-gated channels and a the GPCR GABAB (Kaupmann K et al, 1998), which acts through G proteins to regulate potassium and calcium channels. GABAB can only bind GABA once it forms a heterodimer composed of the GABABR1 and GABABR2 receptors (White JH et al, 1998). The effects of this dimer are mediated by coupling to the G protein alpha i subunit, which inhibits adenylyl cyclase.
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Genomic organization, tissue distribution and deletion mutation of human pyridoxine 5'-phosphate oxidase
GABA B receptors are coupled to Gproteins and function by increasing the K+ and decreasing the Ca2+ inside the cell. The increase in K+ increases the negative membrane potential of the cell thereby hyper polarizing the cell which inhibits the release of neurotransmitters. The decrease in Ca2+ also inhibits neurotransmitter in two ways; first by preventing the fusion of synaptic vesicles containing the neurotransmitter with the plasma membrane and second by decreasing the Ca2+ dependent recruitment of synaptic vesicles to the plasma membrane. In particular GABA B receptors inhibit voltage gated Ca2+ channels via the activity of Gbeta/Ggamma subunits of G proteins.
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Small conductance Ca2+ activated potassium channels (SKca) are solely activated by intracellular Ca2+ concentration. SKca channels form functional tetramers. SKca channels control the contractility of uterus, maintian vascular tone, modulate hormone secretion, control cell volume in red blood cells and activation of microglia and lymphocytes. Actiavtion of SKca channels is triggered by increase in the intracellular Ca2+ ion concentration. Activation of Skca channels leads to relatively small K+ ion effluxes.
Ca2+ activated potassium channels are expressed in neuronal and non-neuronal tissue such as smooth muscle, epithelial cell and sensory cells. Ca2+ activated potassium channels are activated when the Ca2+ ion concentration increased, The efflux of K+ via these channels leads to repolarization/hyperpolarization of the membrane potential which limits the Ca2+ influx though voltage activated Ca2+ channels (VGCC) thereby regulating the influx of Ca2+ flow via VGCC.
Chemical synapses are specialized junctions that are used for communication between neurons, neurons and muscle or gland cells. The synapse involves a pre-synaptic neuron and a post-synaptic neuron, muscle cell or glad cell. The pre and the post-synaptic cell are separated by a gap of 20nm called the synaptic cleft. The signals pass in a unidirection from pre-synaptic to post-synaptic. The pre-synaptic neuron communicates via the release of neurotransmitter which bind the receptors on the post-synaptic cell.
Intermediate conductance K+ channels are restricted to non neuronal tissues like epithelia, blood cells and are activated by intracellular Ca2+ ion concentration. Activation of Ca2+ activated K+ channels with intermediate conductance leads to K+ efflux in to the extracellular space.
Gamma aminobutyric acid (GABA) receptors are the major inhibitory receptors in human synapses. They are of two types. GABA A receptors are fast-acting ligand gated chloride ion channels that mediate membrane depolarization and thus inhibit neurotransmitter release (G Michels et al Crit Rev Biochem Mol Biol 42, 2007, 3-14). GABA B receptors are slow acting metabotropic Gprotein coupled receptors that act via the inhibitory action of their Galpha/Go subunits on adenylate cyclase to attenuate the actions of PKA. In addition, their Gbeta/gamma subunits interact directly with N and P/Q Ca2+ channels to decrease the release of Ca2+. GABA B receptors also interact with Kir3 K+ channels and increase the influx of K+, leading to cell membrane hyperpolarization and inhibition of channels such as NMDA receptors (A Pinard et al Adv Pharmacol, 58, 2010, 231-55).
The neurotransmitter in the synaptic cleft released by the pre-synaptic neuron binds specific receptors located on the post-synaptic terminal. These receptors are either ion channels or G protein coupled receptors that function to transmit the signals from the post-synaptic membrane to the cell body.
The GABA(A)-rho receptor (GABRR) is expressed in many areas of the brain, but in contrast to other GABA(A) receptors, has especially high expression in the retina. It is functional as a homopentamer and is permeable to chloride ions when GABA binds to it (Cutting et al. 1991, Cutting et al. 1992, Bailey et al. 1990).
GABA A (rho) receptors are highly expressed in the retina and are functional homopentamers of rho subunits. These receptors are formerly called GABA C receptors.
GABA B receptors are metabotropic receptors that are functionally linked to C type G protein coupled receptors.? GABA B receptors are activated upon ligand binding. The GABA B1 subunit binds ligand and GABA B2 subunit modulates the activity of adenylate cyclase via the intracellular loop.? GABA B receptors show inhibitory activity via Galpha/G0 subunits via the inhibition of adenylate cyclase or via the activity of Gbeta/gamma subunits that mediate the inhibition of voltage gated Ca2+ channels.
Functional GABA B receptors are heteromers of GABA B1 and B2 subunits, complexed with G protein alpha-i, 0, beta, and gamma subunits. They function as metabotropic receptors. When GABA is bound to the B1 sub-unit, the B2 subunit undergoes a conformational change that releases the G alpha-i G0 dimer (which binds and inactivates cytosolic adenylate cyclase) and the G beta G gamma dimer (which activates the GIRK (KIR3) potassium channel) (Pinard et al. 2010).
The D-Box-activating domain (DAD) is a new proteolysis signal that stimulates the silent D-Box sequence of Aurora-A
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Activation of Kir 3 channels occurs after binding of G beta gamma subunits of GPCR. Activation of Kir3/GIRK leads to K+ efflux. The dissociation of GPCR into G alpha and G beta gamma subunits is activated by the activation of GABA B receptor by GABA binding.
Inwardly rectifying G protein activated K+ channels (GIRK) are tetrameric assemblies of Ki3 3 family subunits (Kir 3.1, 3.2 3.3 and 3.4). The activation of G protein coupled receptor by ligand results in the liberation of G alpha and G beta gamma subunits. Gbeta gamma subunits interact and activate GIRK channels.
Homotetramers of Kir 1.1 function as inwardly rectifying potassium transport channels. Ki 1.1 are found on the apical side of the cells in the ascending limp of loop of henle and upon activation transport K+ into the extracellular space. Heterotetramers of Kir 4.1 and Ki 5.1 are found on the basolateral side of cells in the distal convoluted tube. Activation of kir 4.1 and 5.1 heterotetramers leads to efflux of K+ into the extracellular space.
Inwardly rectifying potassium transport are tetrameric channels that are found in kidney in the nephron. Kir 1.1 works as a homotetramer, however, Kir 4.1 and 5.1 work as heterotetramers. These channels transport K+ from cytosol to the lumen of the tubules.
Activation of classical kir channels results in K+ efflux which contributes to repolarization and resetting of the membrane potential.
Classical Kir channels are inwardly rectifying K+ channels with strong inwardly rectifying currents that contribute to highly negative resting membrane potential, prolonged action potential plateau and rapid repolarization in the final stage of action potential. Classical Kir channels are found in various cells such as cardiac myocytes, purkinje fibers, atrial and ventricular tissues. Rectification is caused by intracellular Mg2+ ions and polyamines.
Inwardly rectifying K+ channels (Kir channels) show an inward rather than outward (like the voltage gated K+ channels) flow of K+ thereby contributing to maintenance of resting membrane potential and regulation of action potential in excitable tissue. Kir channels are found in a variety of cell types such as cardiac myocytes, neurons, blood cells, osteoblasts, glial cells, epithelial cells, and oocytes. Kir channels can be functionally divided into ATP sensitive K+ channels (Kir 6.1 and Kir 6.2), classical kir channels (Kir 2.1, 2.2, 2.3, 2.4, 5.1) G protein gated K+ channels (Kir 3.1, 3.2, 3.3, 3.4) and K+ transport channels (Kir1.1, 7.1, 4.2, 4.1).
HCN channels require cAMP binding and hyperpolarization of membrane potential for channel opening.
HCN channels are activated upon hyperpolarization of membrane potential and cAMP binding leading to K+ efflux.
Hyperpolarization-activated and cyclic nucleotide gated (HCN) channel are activated by membrane hyperpolarization and cAMP binding. HCN channels are homotetramers of four subunits HCN1-4. HCN channels conduct Na and K current with a permeability of 1:4. The current flowing through HCN channels is call funny current. HCN channels are involved in controlling the rhythmic activity of pacemaker current in autorythymic cells in heart and neuronal processes such as dendritic integration and synaptic transmission.
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Wnt and calcium signaling: beta-catenin-independent pathways
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TALK is activated by increase in pH alkalinity in the extracellular fluid. Potassium is pumped out into the extracellular fluid.
TWIK related alkaline pH activated K+ channels are activated by increase in the extracellular pH. TALK1 and TALK 2 are members of the TALK subfamily and are both are activated by rise in extracellular pH. TALK 2 is expressed in proximal tubule cells and collecting duct cells. TASK 2 is involved in the resorption of bicarbonate.
TASK are tandem repeat K+ channels that are sensitive to extracellular pH. Activation of TASK results in efflux of K+ into the extracellular space.
TASK 1 and 3 are closely related both structurally and functionally. TASK1 and TASK3 are activated by extracellular acidification and inhibited by decrease in pH. TASK 1 and Task 3 form functional homodimers and heterodimers, however the biophysical properties of TAS1 and TASK3 heteromers are different form parent subunit properties.
TRESK is expressed in spinal cord and brain and is involved in K+ efflux. TRESK activation may be mediated by calcineurin.
TRESK subfamily of tandem domain K+ channels has one only member. TRESK is regulated by Ca/calmodulin dependent protein phosphatase, calcineurin.
TREK channels are activated by mechanical stretch, pH temperature and arachidonic acid which leads to efflux of K+ into the extracellular space resulting in membrane hyperpolarization.
TREK1 and TREK 2 are activated by physiochemical changes like stretch, convex deformation of the plasma membrane, depolarization, heat and intracellular acidosis. Polyunsaturated fatty acids (PUFA) including arachidonic acid open TREK channels.
Activation of TWIK channels results in low outward K+ currents.
TWIK channels exhibit very low current and comprise of TWIK1, TWIK2 and KCNK7 members. TWIK current may be low due to rapid recycling of the channels from the plasma membrane.
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AMPA receptors are functionally either Ca permeable or Ca impermeable based on the subunit composition. Ca permeability is determined by GluR2 subunit which undergoes post-transcriptional RNA editing that changes glutamine (Q) at the pore to arginine (R). Incorporation of even a single subunit in the AMPA receptor confers Ca-limiting properties. Ca permeable AMPA receptors permit Ca and Na whereas Ca impermeable AMPA receptors permit only Na. In general, glutamatergic neurons contain Ca impermeable AMPA receptors and GABAergic interneurons contain Ca permeable AMPA receptors. However, some synapses do contain a mixture of Ca permeable and Ca impermeable AMPA receptors. GluR1-4 are encoded by four genes however, alternative splicing generates several functional subunits namely long and short forms of GluR1 and GluR2. GluR4 has long tail only and GluR3 has short tail only. Besides the differences in the tail length, flip/flop isoforms are generated by an interchangeable exon that codes the fourth membranous domain towards the C terminus. The fip/flop isoforms determine rate of desensitization/resensitization and the rate of channel closing. Receptors homomers or heteromers assembled from the combination of GluR1-4 subunits that vary in C tail length and flip/flop versions generates a whole battery of functionally distinct AMPA receptors.
Each AMPA receptor subunit binds one glutamate molecule in the ligand binding site in the N terminus. Each receptor is capable of binding four glutamate molecules however, channel opens when two sites are occupied by the ligand and the current increases with increased ligand binding. Ca impermeable AMPA receptors containing GluR2 subunit conduct Na currents upon activation by either glutamate binding or agonist, AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) binding. The Na currents mainly lead to depolarization of the membrane leading to activation of voltage gated channels such as NMDA receptors that require both agonist binding and depolarization for their activation.
Membrane depolarization occurs due to glutamate dependent activation of Ca-impermeable AMPA receptors, which permit the influx of Na+ ions. The depolarization triggers the removal of Mg2+ from the NMDA receptor pore to facilitate its activation. Therefore activation of AMPA receptors by glutamate precedes activation of NMDA receptors.
Excitatory synaptic transmission in the brain is carried out by glutamate receptors through the activation of both ionotropic and metabotropic receptors. Ionotropic glutamate receptors are of three subtypes based on distinct physiologic properties and their differential binding of exogenous ligands namely NMDA (N-methyl D-aspartate), AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) and Kainate . The ionotropic receptors are glutamate gated ion channels that initiate signaling by influx of ions, and are comprised of subunits with distinct structures and distinguished based on their agonist binding. Even though all three types of receptors are found at the glutamatergic synapses yet they exhibit great diversity in the synaptic distribution. The metabotropic glutamate receptors are a family of G-protein coupled receptors that are slow acting. Fast excitatory synaptic transmission is carried out through AMPA receptors. Post-synaptic transmission involves binding of the ligand such as glutamate/AMPA to the AMPA receptor resulting in the Na influx which causes depolarization of the membrane. NMDA receptors are blocked by Mg at resting membrane potential. NMDA receptors are activated upon coincident depolarization and glutamate binding are activated following AMPA receptor activation.NMDA receptors are blocked by Mg at resting membrane potential. NMDA receptors are Ca permeable and their activity leads to increase in Ca which, leads to upregulation of AMPA receptors at the synapse which causes the long lasting excitatory post-synaptic potential (EPSP) which forms the basis of long term potentiation (LTP). LTP is one form of synaptic plasticity wherein the strength of the synapses is enhanced by either change in the number, increase in the efficacy by phosphorylation or change in the type of receptors. Phosphorylation of AMPA receptors changes the localization of the receptors, increases the single channel conductance, and increases the probability of open channel. GluR1 has four phosphorylation sites; serine 818 (S818) is phosphorylated by PKC and is necessary for LTP, serine 831 (S831) is phosphorylated by CaMKII that increases the delivery of receptors to the synapse and also increased their single channel conductance, threonine (T840) is implicated in LTP. Serine 845 (S845) is phosphorylated by PKA which regulates open channel probability. Long term depression is another form of plasticity wherein the number of AMPA receptors is diminished by either phosphorylation of GluR2 at Ser880 or dephosphorylation of GluR1 by protein phosphatase1, protein phosphatase 2A and protein phosphatase 2B (calcineurin).
Raf is a downstream effector of ras. Raf is activated upon phosphorylation at S338, oligomerization and membrane localization. Membrane localization is facilitated by ras. Interaction of ras with raf is a necessary step but not sufficient for raf activation. Other unknown protein partner interactions are required for raf activation. Raf further activates MAP kinase.
NMDA receptors are activated in a two step mechanism; first by the removal of the voltage dependent Mg2+ block and then by the ligand dependent activation of the unblocked NMDA receptor. At resting membrane potential NMDA receptors can not be activated by ligand alone due to the presence of Mg2+ ion in the pore of the channel. Due to the activation of other membrane resident channels that allow the influx of Na+ the membrane is depolarized which triggers the removal of Mg2+ form the NMDA receptor pore. Once the Mg2+ is expelled NMDA receptors are ready to be activated by the agonist (glutamate) and the co-agonist (glycine).
NMDA receptors require binding of two ligands; the agonist, glutamate and co-agonist, glycine. The N terminal extracellular ligand binding domain in NR1 subunits binds co-agonist glycine and the N terminal extracellular ligand binding domain in NR2 binds glutamate.
NMDA receptors are activated upon binding of two ligands, glutamate and glycine. The activation leads to Ca2+ influx into the post-synaptic cell. The local rise in the Ca2+ ion concentration further leads to activation of several Ca2+ dependent pathways leading to long term changes in the synapse.
At resting membrane potential the NMDA receptor is blocked by extracellular Mg2+ ions and therefore is not activated in this state by ligands (glutamate, glycine, NMDA). The voltage block is removed upon depolarization of the post-synaptic cell membrane by the influx of Na+ and efflux of K+ from the cell, Mg2+ is expelled from the NMDA receptor can now be activated by the ligands. The depolarization of the membrane maybe due to activation of Ca2+ impermeable AMPA receptors, which facilitates Na+ influx, contributing to the unblocking of NMDA receptors.
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Ca2+ influx through the NMDA receptor initiates subsequent molecular pathways that have a defined role in establishing long-lasting synaptic changes. The molecular signaling initiated by a rise in Ca2+ within the spine leads to phosphorylation of Cyclic AMP Response Element binding protein (CREB) at serine 133 which is involved in the transcription of genes that results in long lasting changes in the synapse. The phosphorylation of CREB by increased Ca2+ can be brought about by distinct molecular pathways that may involve MAP kinase, activation of adenylate cyclase, activation of CaMKII and/or the activation of CaMKIV.
CREB is phosphorylated at serine 133 by any of the four isoforms of ribosomal S6 kinase.
Ribosomal S6 kinase has four isoforms in humans and each of the isoforms have sic conserved phosphorylation sites (S221, S363, S380,S749, T359,T573) out of which four are important for its activity (S221, S363, 380,T573). Phosphorylation and activation of ribosomal S6 Kinase (RSK) occurs at the plasma membrane, cytoplasm and in the nucleus. Phosphorylation of RSK first occurs at residue T573 followed by S363 an S380 by activated MAPK/ERK . This form is then phosphorylated by PDK1, which is active in the plasm membrane by an autophosphorylation event.
PDK1 activates ribosomal S6 kinase (RSK) by phosphorylating S221. The binding site for PDK1 on RSK is available after RSK phosphorylation by MAPK/ERK. PDK1 is present in the activated form at the plasma membrane where the phosphorylation occurs. The activation of RSK occurs in the cytoplasm, plasma membrane and in the nucleus where it finally activates CREB by phosphorylation.
Activated MAPK/ERK activates RSK in its C terminal kinase domain by sequentially phosphorylating T573, S363 and 380.
MAPK/ERK is phosphorylated at threonine 185 and tyrosine 187 by membrane associated activated raf kianse leading to the activation of MAPK/ERK kinase. The activated MAPK/ERK in turn activates ribosomal S6 kinase.
Ca2+ signal generated through NMDA receptor in the post-synaptic neuron activates adenylate cyclase signal transduction, leading to the activation of PKA and phosphorylation and activation of CREB-induced transcription. The isoforms of adenylate cyclase that are activated by Ca2+ in the brain are I, III and IX.
CaMKII is fully activated upon Ca2+/Calmodulin binding. In addition to Ca2+/Calmodulin activation, CaMKII undergoes multiple autophosphorylation events leading Ca2+/Calmodulin independent activity of the enzyme.
Ca2+ fluxes through NMDA receptors in the post-synaptic neuron facilitate binding of Ca2+/Calmodulin to adenylate cyclase type 1, 3 or 8, resulting in its activation. Once activated, cAMP is produced which further activates PKA.
Protein kinase A has two regulatory subunits and two catalytic subunits which are held together to form the holoenzyme and is activated upon binding of cAMP within the regulatory subunits. Once cAMP binds the regulatory subunits, the catalytic subunits are released to carry out phosphorylation of CREB at serine133.
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CaMKII gets activated upon Ca2+ influx through the NMDA receptor and moves from plasma membrane to cytoplasm and then nucleus where it phosphorylates CREB at serine 133.
CaMKII is an important regulator of neuronal plasticity. CaMKII shows distinct subcellular localization and acts quickly in a spatio-temporal manner. CaMKII shows fast synaptic localization upon synaptic activity and also nuclear localization, where it phosphorylates CREB at serine 133 to activate transcription of set of genes that results in long lasting structural changes at the synapse.
Nuclear targeting of CaMKII depends on several factors including the phosphorylation in the regulatory domain of CaMKII and induction of other signal transduction pathways.
CaMKK is fully activated upon binding Ca2+/Calmodulin after intracellular Ca2+ levels increase. Once CaMKK binds Ca2+/Calmodulin it autophosphorylates, resulting in activation. CaMKK is negatively regulated by phosphorylation of S74 and T108 by PKA. Once activated CaMKK phosphorylates CaMKIV in a Ca2+/Calmodulin dependent manner.
Transient increase in intracellular Ca2+ concentration after NMDA receptor activation leads to the activation of the CaMKIV via the activation of CaM-kinase kinase. CaM-kinase kinase and CaMKIV are both activated upon binding Ca2+/Calmodulin after Ca2+ influx through activated NMDA receptor.
NMDA receptors are a subtype of ionotropic glutamate receptors that are specifically activated by a glutamate agonist N-methyl-D-aspartate (NMDA). Activation of NMDA receptor involves opening of the ion channel that allows the influx of Ca2+. NMDA receptors are central to activity dependent changes in synaptic strength and are predominantly involved in the synaptic plasticity that pertain to learning and memory. A unique feature of NMDA receptor unlike other glutamate receptors is the requirement of dual activation of the NMDA receptor, which require both voltage dependent and ligand dependent activation. At resting membrane potential the NMDA receptors are blocked by Mg2+. The voltage dependent Mg2+ block is relieved upon depolarization of the post-synpatic membrane . The ligand dependent activation of the NMDA receptor requires co-activation by two ligands, namely glutamate and glycine. NMDA receptors are coincidence detector, and are activated only if there is simultaneous activation of both pre and post-synaptic cell. Upon activation NMDA receptors allow the influx of Ca2+ that initiates various molecular signaling cascades that are involved in the process of learning and memory.
Kainate receptors bind glutamate in the ligand binding domain in the extracellular, N terminal region.
The activation of Kainate receptors by glutamate in the postsynaptic neuron leads to influx of Na+ ions resulting in depolarization of the postsynaptic membrane.
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Kainate receptors that are assembled with subunits GRIK1-5, are Ca2+ permeable if GRIK1 and GRIK2 are not edited at the Q/R or other sites. These channels permit Ca2+ upon activation by glutamate or other agonists.
Kainate receptors that are formed by subunits GRIK1 and or GRIK2 that are edited at the Q/R and other editing sites in GRIK2 are Ca2+ impermeable. They permit the passage of Na+ ions. Glutamine in GRIK1 at position 636 is replaced by arginine by an editing step which occurs posttranscriptioanlly. GRIK2 is glutamine 621 is edited to arginine. GRIK2 is also edited at 571 (Y/C) where a tyrosine residue is changed to cysteine and 567 (I/V) where an isoleucine is changed to valine. All three sites are edited postranscriptionally. A fully edited GRIK2 at all three sites is impermeable to calcium ions.
Kainate receptors are found both in the presynaptc terminals and the postsynaptic neurons. Kainate receptor activation could lead to either ionotropic activity (influx of Ca2+ or Na+ and K+) in the postsynaptic neuron or coupling of the receptor with G proteins in the presynaptic and the postsynaptic neurons. Kainate receptors are tetramers made from subunits GRIK1-5 or GluR5-7 and KA1-2. Activation of kainate receptors made from GRIK1 or KA2 release Ca2+ from the intracellular stores in a G protein-dependent manner. The G protein involved in this process is sensitive to pertussis toxin.
Kainate receptors in the presynaptic neuron are involved in modulating the release of neurotransmitters like glutamate and gamma amino butyric acid (GABA). This activity of Kainate receptors is independent of ionic fluxes through the channel. Homomeric kainate receptors containing GRIK3 are shown to be involved in this process. Kainate receptors in these neurons bind G-protein coupled receptors that activate phospholipase C which eventually triggers the release of Ca2+ from the intracellular stores. The released Ca2+ further initiates the fusion and release of vesicles containing the neurotransmitter.
Kainate receptors are either Ca2+ permeable or impermeable depending on the composition of the receptor and the editing status of subunits GluR5 and GluR6 (GRIK1 and 2).
The GABA(A) receptor (GABR) family belongs to the ligand-gated ion channel superfamily (LGIC). Its endogenous ligand is gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the central nervous system. There are six alpha subunits (GABRA) (Garrett et al. 1988, Schofield et al. 1989, Hadingham et al. 1993, Edenberg et al. 2004, Hadingham et al. 1993, Yang et al. 1995, Wingrove et al. 1992, Hadingham et al. 1996), three beta subunits (GABRB) (Schofield et al. 1989, Hadingham et al. 1993, Wagstaff et al. 1991), 2 gamma subunits (GABRG) (Khan et al. 1993, Hadingham et al. 1995) and a theta subunit (Bonnert et al. 1999) characterised to date. GABA(A) functions as a heteropentamer, the most common structure being 2 alpha subunits, 2 beta subunits and a gamma subunit (2GABRA:2GABRB:GABRG). An alternative heteropentamer with much less affinity for GABA is 2GABRA:GABRB:GABRG:GABRQ (Bonnert et al. 1999). Upon binding of GABA, both GABR complexes conduct chloride ions through their pore, resulting in hyperpolarisation of the neuron. This causes an inhibitory effect on neurotransmission by reducing the chances of a successful action potential occurring.
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Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein
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Coordinate changes in heat shock element-binding activity and HSP70 gene transcription rates in human cells
Characterization of collagen types XII and XIV from fetal bovine cartilage
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Phosphorylation of cyclin D1 at Thr 286 during S phase leads to its proteasomal degradation and allows efficient DNA synthesis
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Internal control regions for transcription of eukaryotic tRNA genes
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Transport mechanism and substrate specificity of human organic anion transporter 2 (hOat2 [SLC22A7])
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LAB/NTAL/Lat2: a force to be reckoned with in all leukocytes?
Identification of mutations that disrupt phosphorylation-dependent nuclear export of cyclin D1
The Rsu-1-PINCH1-ILK complex is regulated by Ras activation in tumor cells
On the discovery of precursor processing
The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36
The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3
Glyceraldehyde-3-phosphate dehydrogenase from human tissues.
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The cytosolic nucleic acid sensor LRRFIP1 mediates the production of type I interferon via a beta-catenin-dependent pathway
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5' exon interactions within the human spliceosome establish a framework for exon junction complex structure and assembly
Native structure and physical properties of bovine brain kinesin and identification of the ATP-binding subunit polypeptide
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Interactions between the endoplasmic reticulum, mitochondria, plasma membrane and other subcellular organelles
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[Gene cloning of human dopaminergic D3 receptor and identification of its chromosome]
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Conserved roles of Sam50 and metaxins in VDAC biogenesis
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Organic anion transporters of the SLC22 family: biopharmaceutical, physiological, and pathological roles
Congenital hypothyroidism caused by a mutation in the Na+/I- symporter
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Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons.
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ABC transporters in cellular lipid trafficking
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Phospholipase D signaling: orchestration by PIP2 and small GTPases
Naunyn Schmiedebergs Arch Pharmacol 374:399-411
Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is selectively eliminated from the nucleus at the onset of S phase.
Role of NAD(+) in the deacetylase activity of the SIR2-like proteins
Biochem. Biophys. Res. Commun. 278:685-90
Mammalian BMP-1/Tolloid-related metalloproteinases, including novel family member mammalian Tolloid-like 2, have differential enzymatic activities and distributions of expression relevant to patterning and skeletogenesis
Beta oxidation of palmitoyl-CoA to myristoyl-CoA
Phosphorylation of tyrosine residues in the kinase domain and juxtamembrane region regulates the biological and catalytic activities of Eph receptors
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Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPase
Multisite autophosphorylation of p21-activated protein kinase gamma-PAK as a function of activation
Calmodulin-binding sites on adenylyl cyclase type VIII
Extracellular matrix dynamics in development and regenerative medicine
Identification of potent and selective human carbonic anhydrase VII (hCA VII) inhibitors
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Retinal stimulates ATP hydrolysis by purified and reconstituted ABCR, the photoreceptor-specific ATP-binding cassette transporter responsible for Stargardt disease
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Caspase activation of mammalian sterile 20-like kinase 3 (Mst3). Nuclear translocation and induction of apoptosis
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Carbonic anhydrase inhibitors. Interaction of 2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide with 12 mammalian isoforms: kinetic and X-ray crystallographic studies
Cloning and expression of mutations demonstrating intragenic complementation in mut0 methylmalonic aciduria
Genetic linkage and radiation hybrid mapping of the three human GABA(C) receptor rho subunit genes: GABRR1, GABRR2 and GABRR3
The role of mast cells in allergic inflammation
Biochemistry of mammalian peroxisomes revisited
Protein misfolding, functional amyloid, and human disease
Functional interaction of glutathione S-transferase pi and peroxiredoxin 6 in intact cells
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2-Methylbutyryl-coenzyme A dehydrogenase deficiency: a new inborn error of L-isoleucine metabolism.
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Diverse functions of vertebrate gap junctions
SLC2A9 is a newly identified urate transporter influencing serum urate concentration, urate excretion and gout
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Regulation of the PAI-1 promoter by circadian clock components: differential activation by BMAL1 and BMAL2
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Molecular cloning, expression pattern, and chromosomal localization of the human Na-Cl thiazide-sensitive cotransporter (SLC12A3)
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Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates
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FARP2 triggers signals for Sema3A-mediated axonal repulsion
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Cdk2-dependent and -independent pathways in E2F-mediated S phase induction
Limiting role of 6-phosphogluconolactonase in erythrocyte hexose monophosphate pathway metabolism
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Alkyl-dihydroxyacetonephosphate synthase. Presence and role of flavin adenine dinucleotide
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How synaptotagmin promotes membrane fusion
Platelet-monocyte complexes support monocyte adhesion to endothelium by enhancing secondary tethering and cluster formation
Mismatch Repair proteins are recruited to replicating DNA through interaction with Proliferating Cell Nuclear Antigen (PCNA)
The presence and release of alpha 2-antiplasmin from human platelets
Cloning, characterization, and chromosome mapping of the human GlcAT-S gene
Effects of mutational loss of adenosine kinase and deoxycytidine kinase on deoxyATP accumulation and deoxyadenosine toxicity in cultured CEM human T-lymphoblastoid cells
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Identification and characterization of a putative human iodide transporter located at the apical membrane of thyrocytes
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Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis
Rapid association of cytoskeletal remodeling proteins with the developing phagosomes of human neutrophils
Complement escape of human pathogenic bacteria by acquisition of complement regulators
CDC6 association with the ORC:origin complex
Human beta-galactosidase gene mutations in morquio B disease
ATP activates a reactive oxygen species-dependent oxidative stress response and secretion of proinflammatory cytokines in macrophages
Cori Cycle (interconversion of glucose and lactate)
The p300/CBP acetyltransferases function as transcriptional coactivators of beta-catenin in vertebrates
The arrangement of intra- and intermolecular disulfide bonds in the carboxyterminal, non-collagenous aggregation and cross-linking domain of basement-membrane type IV collagen
Characterization of the interactions of the nephrin intracellular domain
Phosphorylation of tyrosine 1214 on VEGFR2 is required for VEGF-induced activation of Cdc42 upstream of SAPK2/p38
Multiple forms of gamma-butyrobetaine hydroxylase (EC 1.14.11.1).
Severe osteogenesis imperfecta in cyclophilin B-deficient mice
Update on the molecular physiology of organic anion transporters
Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of Nck and activation of Fyn leading to SAPK2/p38 activation and endothelial cell migration in response to VEGF
TWIK-related alkaline pH activated K+ channel (TALK)
Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_184802.3
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Structure, function and regulation of pyruvate carboxylase
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Hypertension and impaired glycine handling in mice lacking the orphan transporter XT2
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Mapping the functional domains of the Golgi stacking factor GRASP65
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Hyaluronidase and its substrate hyaluronan: biochemistry, biological activities and therapeutic uses
The characterization of a human RHAMM cDNA: conservation of the hyaluronan-binding domains
The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-beta signalling
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DEx/H-box helicases activate type I IFN and inflammatory cytokines production
Groucho oligomerization is required for repression in vivo
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Endonucleolytic function of MutLalpha in human mismatch repair
The APC tumor suppressor counteracts beta-catenin activation and H3K4 methylation at Wnt target genes
Control of translation and mRNA degradation by miRNAs and siRNAs
The fibroblast growth factor receptor-4 Arg388 allele is associated with prostate cancer initiation and progression
RNA primer:origin duplex with DNA damage
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Ghost homologue of Phosphorylated Fibroblast growth factor receptor 1b
f-actin (ADP) (name copied from entity in Homo sapiens)
Ghost homologue of Lysosome Destined Cargo
Mechanism of activation of the Formin protein Daam1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_230734.1
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Regulation of the MST1 kinase by autophosphorylation, by the growth inhibitory proteins, RASSF1 and NORE1, and by Ras
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_260063.1
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Chk1 and Chk2 kinases in checkpoint control and cancer
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Ca2+ stores and Ca2+ entry differentially contribute to the release of IL-1 beta and IL-1 alpha from murine macrophages
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Electron-microscopical approach to a structural model of intima collagen
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HA polymer (name copied from entity in Homo sapiens)
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The catalytic properties of human carbonic anhydrase IX
Reversible anti-EGFR tyrosine kinase inhibitors
Non-covalent EGFR tyrosine kinase inhibitors
Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases
Phospho-Forkhead box transcription factor
Irreversible anti-EGFR tyrosine kinase inhibitors
Covalent EGFR tyrosine kinase inhibitors
Gelsolin amyloid fibril (name copied from entity in Homo sapiens)
ABri/ADan amyloid fibril (name copied from entity in Homo sapiens)
Systemic amyloid fibril main peptide chains
Variant apolipoprotein AII fibril (name copied from entity in Homo sapiens)
Beta amyloid fibril (name copied from entity in Homo sapiens)
Cloning and expression of a cDNA encoding the human GABA-A receptor alpha 5 subunit
phosphorylated nuclear Cyclin B1:Cdc2 substrates
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633892
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633848
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633751
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633714
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633696
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633634
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632095
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640615
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632074
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640915
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640989
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640607
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625889
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625886
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625888
Alternate exon insertion controls selective ubiquitination and degradation of different AUF1 protein isoforms
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625905
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625897
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625904
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15573.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631601
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631594
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635061
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631596
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631597
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379792
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635078
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635055
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635073
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634549
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634478
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634534
trp, a novel mammalian gene family essential for agonist-activated capacitative Ca2+ entry
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634481
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634225
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634424
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634589
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634591
Purification and characterization of 5'-deoxy-5'-methylthioadenosine phosphorylase from human placenta
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634407
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634560
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634416
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631583
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634234
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634249
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630557
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631326
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631334
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631342
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631355
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652657
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_255128.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652731
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_262622.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652732
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_239768.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625197
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_255270.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625195
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625196
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_17447.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_206117.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631627
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631625
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631624
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_23144.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379743
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625194
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_254780.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625190
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625191
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625189
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625187
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625198
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625188
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625200
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_256949.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631652
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631651
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_222132.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631654
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379763
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15882.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379765
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625182
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625209
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625176
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625181
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_254735.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625183
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625172
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625175
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625166
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625169
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_218433.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631641
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631639
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631638
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_17415.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379783
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15966.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379749
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625180
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625206
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625152
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625159
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625160
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625161
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625207
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625204
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625205
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631602
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_223867.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631604
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_17419.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379738
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379762
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_16106.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625901
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625917
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625916
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631880
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625914
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625912
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_16098.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625910
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_210621.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15639.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625903
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625884
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_207883.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=374064
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625902
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379708
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379727
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_17365.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627837
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_250258.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627839
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627794
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627790
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631820
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627801
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631818
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627800
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627811
Expression of the MAPK kinases MKK-4 and MKK-7 in rheumatoid arthritis and their role as key regulators of JNK
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_229714.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620478
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652563
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_224713.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_236789.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653051
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379729
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15767.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379730
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15557.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620477
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627831
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627830
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627829
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627828
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627772
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627768
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627833
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627832
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627782
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627778
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620474
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620475
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_227089.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631658
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631660
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15717.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627786
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379790
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652620
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628913
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_251967.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_257718.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628914
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_254102.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653039
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627826
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627825
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627827
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379793
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15833.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631631
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631632
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631634
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_227468.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379785
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_18116.1
Biological & physiological aspects of action of insulin-like growth factor peptide family
Purification and characterization of a novel alpha-class glutathione transferase from human liver
Proteolysis-independent regulation of PI3K by Cbl-b-mediated ubiquitination in T cells
The primary structure of human dopamine-beta-hydroxylase: insights into the relationship between the soluble and the membrane-bound forms of the enzyme
Distinct primary structures, ligand-binding properties and tissue-specific expression of four human muscarinic acetylcholine receptors
Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo
Both G i and G o heterotrimeric G proteins are required to exert the full effect of norepinephrine on the beta-cell K ATP channel
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_262066.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652730
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625201
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625202
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625203
Interleukin-1 alpha activates an NF-kappaB-like factor in osteoclast-like cells
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_239580.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625375
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635067
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635193
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635184
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635175
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635181
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635171
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635165
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635333
HER4-mediated biological and biochemical properties in NIH 3T3 cells. Evidence for HER1-HER4 heterodimers
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635300
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635276
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635240
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635395
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635297
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635286
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635279
Identification of SLC39A4, a gene involved in acrodermatitis enteropathica
Cloning of another human serotonin receptor (5-HT1F): a fifth 5-HT1 receptor subtype coupled to the inhibition of adenylate cyclase
Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities
Metabolism of propionic acid in animal tissues. IX. Methylmalonyl coenzyme A racemase
Molecular cloning of human amidophosphoribosyltransferase
Back in the water: the return of the inositol phosphates
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637404
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637406
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637380
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637391
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625369
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_12248.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_244326.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625398
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625395
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_233734.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625368
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=190066
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_12259.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625396
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=190071
Collagen type IX: evidence for covalent linkages to type II collagen in cartilage
Somatic mutations of the APC gene in colorectal tumors: mutation cluster region in the APC gene
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637363
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623237
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623260
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637300
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637313
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637326
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637334
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625394
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625386
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625385
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625378
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625381
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625376
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625377
Tyrosine phosphorylation of netrin receptors in netrin-1 signaling
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625384
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625382
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625383
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623272
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634840
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634852
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635730
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636739
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636734
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636731
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637500
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637551
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637509
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625372
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625373
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=190019
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11839.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625370
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625371
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637548
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637528
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_16009.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379715
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15813.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638167
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631886
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631888
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_219646.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638132
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638123
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634197
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379698
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633267
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633247
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641602
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637953
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637943
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637968
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622331
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379744
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15607.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631868
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631870
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_227133.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379740
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15900.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649055
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649144
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649176
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649041
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649010
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648899
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_16074.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631895
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_224542.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631892
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631893
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15650.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648845
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379754
GlycoVis: visualizing glycan distribution in the protein N-glycosylation pathway in mammalian cells
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638464
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648767
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638213
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638384
Electrical properties of the light-sensitive conductance of rods of the salamander Ambystoma tigrinum
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652998
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_250935.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_259316.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652993
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_238467.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652999
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_258073.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626285
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631903
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15671.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379764
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_17378.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379752
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379695
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_211235.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631916
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631914
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631913
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15734.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379781
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_209885.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631922
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_16111.1
Role of two residues proximal to the active site of Ubc9 in substrate recognition by the Ubc9.SUMO-1 thiolester complex
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15807.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379753
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631920
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626294
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626295
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626292
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626293
Expression and functional contribution of hTHTR-2 in thiamin absorption in human intestine
Am J Physiol Gastrointest Liver Physiol 286:G491-8
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626301
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626298
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626299
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626296
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626297
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379773
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_17073.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631812
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631811
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379788
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_213227.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631814
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626286
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626287
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626288
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626289
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626283
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626290
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626291
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626281
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_16053.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379769
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631809
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_222292.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631905
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379750
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15750.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626310
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626309
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_254531.1
Cloning of a water channel homolog expressed in brain meningeal cells and kidney collecting duct that functions as a stilbene-sensitive glycerol transporter
Functional analysis of mRNA scavenger decapping enzymes
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625441
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_248734.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625448
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625446
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625445
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625444
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631899
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631900
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_16107.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379795
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379747
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_17942.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631902
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625405
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625404
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625407
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625406
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652961
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_243741.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652962
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_230571.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625402
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_249086.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631845
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631847
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631848
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_18097.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631843
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631850
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_203397.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637027
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625393
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625392
The ubiquitin-editing enzyme A20 restricts nucleotide-binding oligomerization domain containing 2-triggered signals
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625390
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_229782.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652735
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_252276.1
Red blood cell pH, the Bohr effect, and other oxygenation-linked phenomena in blood O2 and CO2 transport
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625380
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623267
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637079
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623251
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637108
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637066
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_255121.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652925
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626329
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626328
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_243614.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626331
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626312
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626311
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626327
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626324
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379741
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_16039.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379705
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652656
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379780
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15919.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637012
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631788
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637039
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637000
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637016
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635559
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635567
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635543
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625668
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642059
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642085
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625610
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632221
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637703
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632234
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632232
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625650
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629341
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629418
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632212
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632197
Structural analysis of cross-linking domains in cartilage type XI collagen. Insights on polymeric assembly
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621038
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629389
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629411
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629402
The cDNA and protein sequences of human lactate dehydrogenase B
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629396
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620996
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=71994
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629348
Latent infection of Homo sapiens with Mycobacterium tuberculosis
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639693
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3227.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639686
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639670
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621034
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620997
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620992
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620988
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621009
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639700
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624406
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624418
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639668
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639707
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621001
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621013
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621012
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621011
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621005
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620768
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620746
Formation of mRNA 3' ends in eukaryotes: mechanism, regulation, and interrelationships with other steps in mRNA synthesis.
RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate
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High-resolution x-ray structure of human aquaporin 5
Purification and characterization of kynurenine aminotransferase I from human brain
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Histone H4 acetylation differentially modulates arginine methylation by an in Cis mechanism
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Glucagon and regulation of glucose metabolism
Am J Physiol Endocrinol Metab 284:E671-8
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Human fatty acid synthase: properties and molecular cloning
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Identification of a viability domain in the granulocyte/macrophage colony-stimulating factor receptor beta-chain involving tyrosine-750
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Cloning and expression of a cDNA for human cytochrome P-450aldo as related to primary aldosteronism
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Identification of the alpha-aminoadipic semialdehyde synthase gene, which is defective in familial hyperlysinemia.
The chemistry of the collagen cross-links. Age-related changes in the reducible components of intact bovine collagen fibres
Characterization of the enzymatic defect in late-onset muscle phosphofructokinase deficiency. New subtype of glycogen storage disease type VII.
Syndecan-4 regulates localization, activity and stability of protein kinase C-alpha
Hyaluronate binding and CD44 expression in human glioblastoma cells and astrocytes
Synthesis of PIPs at the plasma membrane
XTcf-3 transcription factor mediates beta-catenin-induced axis formation in Xenopus embryos
Groucho-mediated repression may result from a histone deacetylase-dependent increase in nucleosome density
Human sodium phosphate transporter 4 (hNPT4/SLC17A3) as a common renal secretory pathway for drugs and urate
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Regional differences in the response of human pre-adipocytes to PPARgamma and RXRalpha agonists
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The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase
ZnT-2, a mammalian protein that confers resistance to zinc by facilitating vesicular sequestration
AU-rich elements and associated factors: are there unifying principles?
FGFR2-amplified gastric cancer cell lines require FGFR2 and Erbb3 signaling for growth and survival
The joining of ribosomal subunits in eukaryotes requires eIF5B.
Functional analysis of human P5, a protein disulfide isomerase homologue
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In vitro reconstitution of the human RISC-loading complex
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Identification of the human and bovine ATP:Cob(I)alamin adenosyltransferase cDNAs based on complementation of a bacterial mutant
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Induction by cyclic GMP of cationic conductance in plasma membrane of retinal rod outer segment
Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex
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Structure-function relationships of the liver and muscle isoforms of carnitine palmitoyltransferase I
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Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase
Characterization of orphan human cytochromes P450
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Identification and characterization of a novel inositol hexakisphosphate kinase
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Molecular characterization of human and mouse photoreceptor guanylate cyclase-activating protein (GCAP) and chromosomal localization of the human gene.
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623156
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623154
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=112165
Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621089
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_245910.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621087
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620750
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620887
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621086
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3713.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=71998
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621085
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29626
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5617.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623027
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623028
Mechanisms of digestion and absorption of dietary vitamin A
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623026
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_245144.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623024
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_251014.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623023
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5790.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111341
Identification of autophosphorylation sites of HER2/neu
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5393.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623022
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_251782.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=72084
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652574
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_212501.2
The human telomere terminal transferase enzyme is a ribonucleoprotein that synthesizes TTAGGG repeats
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652573
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_207406.2
Expression, purification, and characterization of histidine-tagged rat and human flavoenzyme dihydroorotate dehydrogenase.
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652572
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_224765.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623159
5,10-methenyltetrahydrofolate polyglutamate [ChEBI:65049]
5,10-methenyltetrahydrofolate polyglutamate
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621046
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621047
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621048
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621040
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621042
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621044
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620763
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620767
Immunoglobulin E receptor signaling and asthma
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620883
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620891
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620895
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620899
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620900
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=72073
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5157.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621030
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621058
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621057
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621056
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621052
GRASP55 regulates Golgi ribbon formation
Regulation of cholesterol biosynthesis by SREBP (SREBF)
Nuclear Events (kinase and transcription factor activation)
The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649699
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5651398
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5651440
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5651455
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5651573
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5649707
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5651855
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652145
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630634
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629519
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631189
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629431
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637619
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637628
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637647
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630042
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635554
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637820
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629516
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637607
Thrombin and phorbol esters cause the selective phosphorylation of a G protein other than Gi in human platelets
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637288
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637166
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637201
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646524
STING mediated induction of host immune responses
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646526
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646483
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646485
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641127
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646528
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5650371
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639652
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641110
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641139
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622143
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622152
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636775
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622201
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623279
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622172
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622180
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622998
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646479
Phosphorylation of Cbl following stimulation with interleukin-3 and its association with Grb2, Fyn, and phosphatidylinositol 3-kinase
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620791
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621746
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623219
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621686
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621698
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621705
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621796
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622213
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621733
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623553
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621759
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621723
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621652
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621636
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621712
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621645
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621638
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621656
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622823
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622187
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621654
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620696
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620700
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620701
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620709
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620733
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648158
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648645
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=71916
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620692
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648648
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648651
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620732
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620727
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620705
Protein kinase C-theta (PKC theta): a key enzyme in T cell life and death
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620722
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621782
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636667
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636574
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620717
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623736
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623718
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620455
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620651
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620653
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620655
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620657
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620658
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623714
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636681
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621789
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621768
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621624
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621837
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620713
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620904
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620932
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620675
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620673
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620649
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620676
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4-(4-(dimethylamino)styryl)-N-methylpyridinium [ChEBI:65133]
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Mutational analysis in longest known survivor of mucopolysaccharidosis type VII
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The mammalian Zip5 protein is a zinc transporter that localizes to the basolateral surface of polarized cells
Function of human cytochrome P450s: characterization of the orphans
In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis
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Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution
Pyruvate dehydrogenase kinase isoform 2 activity limited and further inhibited by slowing down the rate of dissociation of ADP
Post-translational modification: synthesis of GPI-anchored proteins
Differences in regulatory properties between human and rat glucokinase regulatory protein
TRAF6 Mediated Induction of proinflammatory cytokines
Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation
Novel fibroblast growth factor receptor 3 (FGFR3) mutations in bladder cancer previously identified in non-lethal skeletal disorders
High-throughput mass spectrometry screening for inhibitors of phosphatidylserine decarboxylase
Wnt trafficking: new insights into Wnt maturation, secretion and spreading
Syndecan-4 proteoglycan cytoplasmic domain and phosphatidylinositol 4,5-bisphosphate coordinately regulate protein kinase C activity
Identification and characterization of human ethanolaminephosphotransferase1
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Molecular cloning of cDNAs from human kidney coding for two alternatively spliced products of the cardiac Ca2+-ATPase gene
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Code for collagen's stability deciphered
Pyridinoline, a non-reducible crosslink of collagen. Quantitative determination, distribution, and isolation of a crosslinked peptide
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The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes.
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Complete primary structure of a human plasma membrane Ca2+ pump
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Involvement of ACSL in local synthesis of neutral lipids in cytoplasmic lipid droplets in human hepatocyte HuH7
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Interactions between the L1 cell adhesion molecule and ezrin support traction-force generation and can be regulated by tyrosine phosphorylation
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A mechanism for Wnt coreceptor activation
The role of complement in danger sensing and transmission
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The tyrosine kinase network regulating mast cell activation
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Identification of extracellular matrix ligands for the heparan sulfate proteoglycan agrin
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The regulation of human factor XIIa by plasma proteinase inhibitors
Unifying concepts in CD28, ICOS and CTLA4 co-receptor signalling
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Structure of human serum lipoproteins in solution. II. Small-angle x-ray scattering study of HDL3 and LDL.
A revised picture of the E2F transcriptional network and RB function.
Abnormalities of the APC/beta-catenin pathway in endometrial cancer
Regulation of NMDA receptors by phosphorylation
Site-directed mutagenesis of the distal basic cluster of pancreatic bile salt-dependent lipase
Still a puzzle: why is haem covalently attached in c-type cytochromes?
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620598
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620603
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620602
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620601
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620622
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620620
The human hyaluronan receptor for endocytosis (HARE/Stabilin-2) is a systemic clearance receptor for heparin
Cloning and recombinant expression of rat and human kynureninase.
Characterization of the human SLC2A11 (GLUT11) gene: alternative promoter usage, function, expression, and subcellular distribution of three isoforms, and lack of mouse orthologue
Molecular cloning and functional expression of the human glycine transporter GlyT2 and chromosomal localisation of the gene in the human genome
Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620100
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620085
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620093
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620072
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637695
Cloning and characterization of PDK4 on 7q21.3 encoding a fourth pyruvate dehydrogenase kinase isoenzyme in human
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620138
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620114
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619608
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620107
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_237186.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642350
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642345
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642332
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642331
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642306
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_220415.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642548
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178411.3
Phosphorylated JNKs: MAPK8, MAPK9, MAPK10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642471
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642472
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642473
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642474
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642558
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178317.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642469
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642470
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642329
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_256267.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642351
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642307
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642613
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642288
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642328
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642326
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642330
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_235030.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642327
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178324.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=202247
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642552
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642554
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642550
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642551
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623290
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642549
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642289
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642342
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642343
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_208480.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_176030.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645782
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642312
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_240895.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642361
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642313
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629637
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_233646.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645783
Reconstitution of two recombinant LSm protein complexes reveals aspects of their architecture, assembly, and function
Pyruvate dehydrogenase phosphatase deficiency: identification of the first mutation in two brothers and restoration of activity by protein complementation
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_244541.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642314
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642316
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642315
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_255769.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645779
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645778
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645781
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645780
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_254242.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642281
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642305
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626709
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=192087
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10957.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10392.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1806290
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=192030
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10258.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642573
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=191980
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178528.3
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_256581.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178367.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626711
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642510
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642508
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642530
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642518
Biogenesis and regulation of insulin-responsive vesicles containing GLUT4
DNA-directed RNA polymerase I largest subunit
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626723
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_230111.1
Purification and characterization of human liver "high Km" aldehyde dehydrogenase and its identification as glutamic gamma-semialdehyde dehydrogenase.
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178518.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642507
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642505
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642504
DNA-directed RNA polymerase I subunit RPA12
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642502
DNA-directed RNA polymerase I 135 kDa polypeptide
DNA-directed RNA polymerases I, II, and III 7.0 kDa polypeptide
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642503
DNA-directed RNA polymerase I and III 16 kDa polypeptide
DNA-directed RNA polymerases I and III subunit RPAC2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_125341.1
DNA-directed RNA polymerases I and III subunit RPAC1
DNA-directed RNA polymerase I and III 40 kDa polypeptide
DNA-directed RNA polymerase II 14.4 kDa polypeptide (EC 2.7.7.6) (RPB6) (RPB14.4)
DNA-directed RNA polymerase II 14.4 kDa polypeptide
DNA-directed RNA polymerase III subunit RPC3
DNA-directed RNA polymerase III subunit C
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642334
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_175128.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642344
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642333
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642335
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178537.3
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_251139.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642514
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642282
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1806165
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642353
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_202739.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642352
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642283
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642544
DNA-directed RNA polymerases I, II, and III 17.1 kDa polypeptide
DNA-directed RNA polymerase II 23 kDa polypeptide (EC 2.7.7.6) (RPB25) (XAP4) (RPB5)
DNA-directed RNA polymerase II 23 kDa polypeptide
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178571.3
DNA-directed RNA polymerase II 7.6 kDa polypeptide
DNA-directed RNA polymerase II 7.6 kDa polypeptide (EC 2.7.7.6) (RPB10) (RPB7.6)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_124713.1
DNA-directed RNA polymerase III subunit RPC10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1806230
DNA-directed RNA polymerase III largest subunit
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642512
DNA-directed RNA polymerase III subunit 127.6 kDa polypeptide
Pyrimidine pathways in health and disease
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642511
DNA-directed RNA polymerases III 80 kDa polypeptide
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642392
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642336
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_223342.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642337
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653424
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_197719.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632990
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_197738.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642390
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653425
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=192064
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10393.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642455
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642454
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_123549.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_197728.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653429
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178841.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642457
Cbl escapes Cdc42-mediated inhibition by downregulation of the adaptor molecule betaPix
Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642323
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642324
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642325
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642319
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642320
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642321
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642322
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_246161.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642317
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642318
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642359
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642311
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642309
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642310
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642341
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642308
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642339
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642340
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_255415.1
Endocytosis of beta1 integrins is an early event in migration promoted by the cell adhesion molecule L1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642338
Iron and oxygen: a biologically damaging mixture
Properties of intramolecular proton transfer in carbonic anhydrase III
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641934
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634454
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634465
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641945
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641953
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642212
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641968
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641988
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626933
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5643356
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642206
1.3-A resolution structure of human glutathione S-transferase with S-hexyl glutathione bound reveals possible extended ligandin binding site
GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5
A plus-end-directed motor enzyme that moves antiparallel microtubules in vitro localizes to the interzone of mitotic spindles
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646552
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646554
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646544
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646561
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646550
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646537
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633042
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5633046
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636671
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632004
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630215
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628390
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630250
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628837
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630266
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653001
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_247725.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628389
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646487
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653000
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_246059.1
Identification of heme as the ligand for the orphan nuclear receptors REV-ERBalpha and REV-ERBbeta
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628402
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634573
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628401
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628844
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646500
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_260022.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628842
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628843
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628841
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646518
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628839
The alpha- and beta-tubulin folding pathways
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634582
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628395
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628396
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628397
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634347
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628405
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628910
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_249191.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634287
Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628403
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634345
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628404
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634332
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634321
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628394
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634315
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634442
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634349
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634625
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634618
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5634329
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_247705.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642536
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627415
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627417
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642537
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642538
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642539
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642540
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642542
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178568.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627414
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627413
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627412
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627411
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627410
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627409
A complex secretory program orchestrated by the inflammasome controls paracrine senescence
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642402
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627044
Purification and characterization of kidney and intestinal brush-border membrane trehalases from the rabbit
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642583
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627045
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627046
A proposed role for the Azotobacter vinelandii NfuA protein as an intermediate iron-sulfur cluster carrier
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642603
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_241659.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642585
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178388.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642534
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642535
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642423
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627041
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627043
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627042
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627037
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627039
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645753
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178785.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642618
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178419.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627057
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642403
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627059
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642476
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178860.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642405
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178894.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642417
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642419
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642439
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627052
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642490
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627051
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627050
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645751
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627056
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645748
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627055
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627054
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645755
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627053
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_123499.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_248079.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642441
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622978
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1806240
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642580
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178386.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1806224
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_122144.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642443
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178831.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645789
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627060
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624171
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627061
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627063
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627062
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627065
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646494
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627064
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627418
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630103
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_239380.1
Clinical findings and biochemical and molecular analysis of four patients with holocarboxylase synthetase deficiency
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627379
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627381
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627376
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627378
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627370
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627371
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627372
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642398
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642400
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642399
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_241121.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642587
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_121667.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1806276
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627391
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178355.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627387
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627386
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627393
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627392
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627384
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627385
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627382
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627383
Smooth muscle contraction and relaxation
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642564
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642562
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642563
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_240940.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642529
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178879.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642394
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_12881.1
Crystal structure of a covalent intermediate of endogenous human arylsulfatase A
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627404
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627403
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627408
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627394
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627395
Acetylation of beta-catenin by p300 regulates beta-catenin-Tcf4 interaction
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627400
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642565
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642567
Transcription initiation factor TFIID 30 kDa subunit
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_242401.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626924
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10890.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_240950.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626748
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10835.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=192356
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193472
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10969.1
Transcription initiation factor TFIID 135 kDa subunit
Transcription initiation factor TFIID 28 kDa subunit
Transcription initiation factor TFIID 250 kDa subunit
Transcription initiation factor TFIID 105 kDa subunit
Transcription initiation factor IIB (General transcription factor TFIIB) (S300-II)
Transcription initiation factor IIA gamma chain
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_229852.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626925
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10619.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193451
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_261077.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626918
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193446
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10649.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193513
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10291.2
Transcription initiation factor TFIID 70 kDa subunit
Transcription elongation factor A protein 1 (Transcription elongation factor S-II protein 1) (Transcription elongation factor TFIIS.o)
Transcription elongation factor A protein 1
Transcription elongation factor S-II protein 1
80 kDa nuclear cap binding protein (NCBP 80 kDa subunit) (CBP80)
Chromatin-specific transcription elongation factor 80 kDa subunit
Recombination signal sequence recognition protein
Structure-specific recognition protein 1 (SSRP1) (Recombination signal sequence recognition protein) (T160) (Chromatin-specific transcription elongation factor 80 KDA subunit
Structure-specific recognition protein 1
RNA polymerase II transcription factor SIII subunit A1
Transcription elongation factor B polypeptide 3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626725
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10585.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193512
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10474.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193483
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626724
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_221310.2
Achondroplasia is defined by recurrent G380R mutations of FGFR3
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626726
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626728
Transcription initiation factor TFIID 20/15 kDa subunits
Transcription initiation factor TFIID 18 kDa subunit
T cell growth factor receptors. Quantitation, specificity, and biological relevance
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X-linked liver phosphorylase kinase deficiency is associated with mutations in the human liver phosphorylase kinase alpha subunit.
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10177.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10407.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193484
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=159435
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10195.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=159432
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10657.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626923
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_215868.2
Transcription initiation factor TFIID 100 kDa subunit
20 kDa nuclear cap binding protein (NCBP 20 kDa subunit) (CBP20) (NCBP interacting protein 1) (NIP1)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=159422
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10759.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=192332
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10828.1
(S)-2-Amino-3-(p-hydroxyphenyl)propionic acid
beta-Nicotinamide adenine dinucleotide phosphate
Nicotinamide adenine dinucleotide phosphate
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626873
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624622
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626880
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626879
Modulation of Wnt signaling by Axin and Axil
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626882
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_262016.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652984
Complement factor H binds malondialdehyde epitopes and protects from oxidative stress
1,2-Dihydroxy-3-oxo-methylthiopentene (1-)
Skeletal muscle injury--molecular changes in the collagen during healing
Molecular cloning and functional expression of human 3-hydroxyanthranilic-acid dioxygenase.
(HCE) (HCAP1) (Includes: Polynucleotide 5'- triphosphatase (EC 3.1.3.33) (mRNA 5'-triphosphatase) (TPase); mRNA guanylyltransferase (EC 2.7.7.50) (GTP--RNA guanylyltransferase) (GTase))
VEGF receptor signalling - in control of vascular function
Neuronal TRP channels: thermometers, pathfinders and life-savers
DNA-directed RNA polymerase III subunit RPC7
DNA-directed RNA polymerases III 39 kDa polypeptide
DNA-directed RNA polymerase III subunit 22.9 kDa polypeptide
DNA-directed RNA polymerase III subunit RPC7-like
RNA polymerase III subunit C7-likeRNA polymerase III subunit C7-like
DNA-directed RNA polymerase III subunit RPC9
TATA box-binding protein-associated factor, RNA polymerase III, subunit 2
Transcription factor IIIB 90 kDa subunit
Transcription initiation factor TFIID TBP subunit
TATA box binding protein (Transcription initiation factor TFIID) (TATA-box factor) (TATA sequence-binding protein) (TBP)
DNA-directed RNA polymerase II 33 kDa polypeptide
DNA-directed RNA polymerase II 140 kDa polypeptide
Molecular organization and function of the complement system
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10443.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=192316
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10934.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626722
DNA-directed RNA polymerase II 19 kDa polypeptide
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_260606.1
DNA-directed RNA polymerase II 13.3 kDa polypeptide
DNA-directed RNA polymerase II 14.5 kDa polypeptide
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193429
RNA Pol II (unphosphorylated) largest subunit
DNA-directed RNA polymerase II largest subunit
Transcription initiation factor IIF, alpha subunit
DNA-directed RNA polymerase II 16 kDa polypeptide
TFIIH basal transcription factor complex helicase XPB subunit (EC 3.6.1.-) (Basic transcription factor 2 89 kDa subunit) (BTF2-p89) (TFIIH 89 kDa subunit) (DNA-repair protein complementing XP-B cells) (Xeroderma pigmentosum group B complementing protein) (DNA excision repair protein ERCC-3)
Xeroderma pigmentosum group B complementing protein
Basic transcription factor 2 89 kDa subunit
DNA-repair protein complementing XP-B cells
TFIIH basal transcription factor complex helicase XPB subunit
Transcription initiation factor IIF, beta subunit
Basic transcription factor 52 kDa subunit
General transcription factor IIH polypeptide 4
TFIIH basal transcription factor complex p52 subunit (Basic transcription factor 52 kDa subunit) (BTF2-p52) (General transcription factor IIH polypeptide 4)
TFIIH basal transcription factor complex p52 subunit
General transcription factor IIH polypeptide 3
TFIIH basal transcription factor complex p34 subunit
TFIIH basal transcription factor complex p34 subunit (Basic transcription factor 2 34 kDa subunit) (BTF2-p34) (General transcription factor IIH polypeptide 3)
Basic transcription factor 2 34 kDa subunit
Hormonal regulation of hepatic gluconeogenesis and glycolysis
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193442
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10853.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10532.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=192342
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626919
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_234131.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_99262.4
General transcription factor IIH polypeptide 1
TFIIH basal transcription factor complex p62 subunit
Basic transcription factor 62 kDa subunit
Xeroderma pigmentosum group D complementing protein
TFIIH basal transcription factor complex helicase subunit
TFIIH basal transcription factor complex helicase subunit (EC 3.6.1.-) (DNA-repair protein complementing XP-D cells) (Xeroderma pigmentosum group D complementing protein) (CXPD) (DNA excision repair protein ERCC-2)
DNA-repair protein complementing XP-D cells
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10191.2
TFIIH basal transcription factor complex p44 subunit
General transcription factor IIH polypeptide 2
Basic transcription factor 2 44 kDa subunit
TFIIH basal transcription factor complex p44 subunit (Basic transcription factor 2 44 kDa subunit) (BTF2-p44) (General transcription factor IIH polypeptide 2)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626742
Transcription initiation protein SPT4 homolog 1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_88619.4
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193422
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10198.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193459
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10685.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626883
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626735
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_258212.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193403
Ca2+ permeability of nicotinic acetylcholine receptors
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10827.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626921
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=192339
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626926
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_245646.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193388
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10857.1
Transcription initiation factor IIE, alpha subunit
General transcription factor IIE 56 kDa subunit
Transcription initiation factor IIE, beta subunit
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_244574.1
Human lung enolase: cloning and sequencing of cDNA and its inducibility with dexamethasone
Inflammatory mediators regulate cathepsin S in macrophages and microglia: A role in attenuating heparan sulfate interactions
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627369
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627366
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621872
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627365
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627368
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621879
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627367
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627362
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621881
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627361
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627364
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621887
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627363
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621893
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627359
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623683
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621850
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621843
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621865
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621863
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637577
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627330
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627331
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637587
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627332
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624685
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627333
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627334
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637571
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627335
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627336
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627337
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627338
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627339
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625104
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625110
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627345
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621904
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627343
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627350
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621897
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627346
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621895
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627354
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627355
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619872
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636256
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627309
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627310
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636264
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627311
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627312
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627305
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619858
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627307
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619865
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627313
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627314
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619978
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627315
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620493
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619886
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627329
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627324
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627325
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627320
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619928
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627316
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619912
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642517
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642509
Dissociation of cohesin from chromosome arms and loss of arm cohesion during early mitosis depends on phosphorylation of SA2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626339
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626340
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642515
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627287
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626335
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627285
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626337
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627286
Biotransformation of Aflatoxin B1 and Its Relationship with the Differential Toxicological Response to Aflatoxin in Commercial Poultry Species,
Aflatoxins - Biochemistry and Molecular Biology (Book)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627280
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641000
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627278
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641144
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627284
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641018
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627282
isovaleryl-CoA, a-methylbutyryl-CoA, isobutyryl-CoA
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641554
a-ketoisocaproate, a-keto b-methylvalerate, a-ketoisovalerate
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642516
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626346
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626347
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5626344
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_121538.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1806159
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627303
p38 MAPK signalling cascades: ancient roles and new functions
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178371.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627289
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620211
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627288
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627291
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630597
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627290
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627295
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629090
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627299
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629004
Expression of fibroblast growth factor and FGF-receptor family genes in human myeloma cells, including lines possessing t(4;14)(q16.3;q32. 3) and FGFR3 translocation
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619495
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642495
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642497
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642589
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178390.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642499
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178524.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642571
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642578
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627265
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627263
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624853
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627259
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642588
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624855
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627258
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624772
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627256
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624704
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627252
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630166
Differential recruitment of DNA Ligase I and III to DNA repair sites
Receptor-mediated phagocytosis elicits cross-presentation in nonprofessional antigen-presenting cells
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642409
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642614
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_122405.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1806221
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_123497.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642616
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178418.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627272
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1806217
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641558
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627276
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627269
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628862
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627268
Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627271
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627270
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624801
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627267
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624824
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642496
(S)-alpha-amino-beta-(3-indolyl)-propionic acid
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627247
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627249
Expression and characterization of recombinant fungal acetyl-CoA carboxylase and isolation of a soraphen-binding domain
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627251
Phosphorylation relieves autoinhibition of the kinetochore motor Cenp-E
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627240
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627241
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627245
Mucopolysaccharidosis type III (Sanfilippo Syndrome): emerging treatment strategies
Mucopolysaccharidosis Type II (Hunter Syndrome): clinical picture and treatment
(S)-alpha-Amino-1H-imidazole-4-propionic acid
Articular cartilage collagen: an irreplaceable framework?
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_123619.1
Transient receptor potential cation channel subfamily M member 5
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Endothelial PAS domain-containing protein 1
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Transient receptor potential cation channel subfamily M member 4
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Transient receptor potential cation channel subfamily V member 6
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FEEL-1 and FEEL-2 are endocytic receptors for advanced glycation end products
EPAS1 (HIF2A) with hydroxyproline-405 and -531
Cloning and expression of human uridine phosphorylase
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_194420.3
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alpha(2A)-adrenergic receptor stimulation potentiates calcium release in platelets by modulating cAMP levels
Transient receptor potential cation channel subfamily V member 3
Transient receptor potential cation channel subfamily V member 4
Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase
Control of the senescence-associated secretory phenotype by NF-?B promotes senescence and enhances chemosensitivity
Transient receptor potential cation channel subfamily V member 5
Crystal structure of human synbindin reveals two conformations of longin domain
Biochem. Biophys. Res. Commun. 378:338-43
Localization of GAR transformylase in Escherichia coli and mammalian cells
Alternative splicing of the Robo3 axon guidance receptor governs the midline switch from attraction to repulsion
Neuronal nicotinic receptors: from protein structure to function
A refined structure of human aquaporin-1
Histone modifying enzymes: structures, mechanisms, and specificities
latheo encodes a subunit of the origin recognition complex and disrupts neuronal proliferation and adult olfactory memory when mutant.
Molecular cloning and expression of human carnitine octanoyltransferase: evidence for its role in the peroxisomal beta-oxidation of branched-chain fatty acids
Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo
Proc. Natl. Acad. Sci. U.S.A. 104:19262-6
Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates
RNA polymerase III transcribes human microRNAs
Role of miR-204 in the regulation of apoptosis, endoplasmic reticulum stress response, and inflammation in human trabecular meshwork cells
Complement classical pathway components are all important in clearance of apoptotic and secondary necrotic cells
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_124023.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_194633.3
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_194541.3
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_121859.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_123396.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_121841.1
Transient receptor potential cation channel subfamily V member 1
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Transient receptor potential cation channel subfamily V member 2
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_197642.3
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_197641.3
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Sequence variants of the axin gene in breast, colon, and other cancers: an analysis of mutations that interfere with GSK3 binding
Cloning and expression of human 75-kDa inositol polyphosphate-5-phosphatase
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Transient receptor potential cation channel subfamily M member 3
Transient receptor potential cation channel subfamily M member 2
Transient receptor potential cation channel subfamily M member 1
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Distribution and functional characterization of equilibrative nucleoside transporter-4, a novel cardiac adenosine transporter activated at acidic pH
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Short transient receptor potential channel 4
Short transient receptor potential channel 5
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Short transient receptor potential channel 7
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=265287
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15804.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630104
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_225787.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622936
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622940
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622932
Transient receptor potential cation channel subfamily M member 8
Transient receptor potential cation channel subfamily M member 7
Mechanism of coenzyme binding to human methionine synthase reductase revealed through the crystal structure of the FNR-like module and isothermal titration calorimetry
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4569.2
Transient receptor potential cation channel subfamily M member 6 ecNumber2.7.11.1/ecNumber
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622924
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622920
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_124222.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1806259
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642428
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642424
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642561
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642559
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1806199
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178339.3
Peptidyl-prolyl cis-trans isomerase FKBP4
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Phosphorylation of GRK2 by protein kinase C abolishes its inhibition by calmodulin.
Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_122226.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178387.3
Mitogen-activated protein kinase kinase kinase 5
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178551.3
Mitogen-activated protein kinase kinase 3
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mitogen-activated protein kinase kinase 6
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_197739.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653426
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_125493.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1806238
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178550.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642533
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_124533.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1806200
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_231345.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642602
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642609
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642607
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642604
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642606
The Arp2/3 complex branches filament barbed ends: functional antagonism with capping proteins
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642611
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178404.3
CalDAG-GEFI integrates signaling for platelet aggregation and thrombus formation
Nasopharyngeal carcinoma-associated antigen 13
SUMO protease SENP1 induces isomerization of the scissile peptide bond
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628413
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_231479.1
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628442
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628406
Peroxiredoxin-6 ecNumber1.11.1.15/ecNumber
Transitional endoplasmic reticulum ATPase
Thioredoxin-dependent peroxide reductase, mitochondrial ecNumber1.11.1.15/ecNumber
Thioredoxin reductase 2, mitochondrial ecNumber1.8.1.9/ecNumber
Homologues of L-selenocysteine residue-GPX3
Peroxiredoxin-2 ecNumber1.11.1.15/ecNumber
Peroxiredoxin-1 ecNumber1.11.1.15/ecNumber
Uridine kinase activities and pyrimidine nucleoside phosphorylation in fluoropyrimidine-sensitive and -resistant cell lines of the Novikoff hepatoma
Reconstitution of the B cell antigen receptor signaling components in COS cells
Superoxide dismutase [Mn], mitochondrial ecNumber1.15.1.1/ecNumber
NUDT9, a member of the Nudix hydrolase family, is an evolutionarily conserved mitochondrial ADP-ribose pyrophosphatase
Bridging structure with function: structural, regulatory, and developmental role of laminins
Mutations in the gene encoding lecithin retinol acyltransferase are associated with early-onset severe retinal dystrophy
Intramolecular proton shuttle supports not only catalytic but also noncatalytic function of carbonic anhydrase II
Ligand-independent activation of fibroblast growth factor receptors by point mutations in the extracellular, transmembrane, and kinase domains
Mast cell signaling: the role of protein tyrosine kinase Syk, its activation and screening methods for new pathway participants
Recurrent FGFR1 amplification and high FGFR1 protein expression in oral squamous cell carcinoma (OSCC)
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P-glycoprotein-mediated active efflux of the anti-HIV1 nucleoside abacavir limits cellular accumulation and brain distribution
Matrix metalloproteinases: old dogs with new tricks
Regulation of Endoplasmic Reticulum Stress-induced Cell Death by ATF4 in Neuroectodermal Tumor Cells
The structure and function of carbonic anhydrase isozymes in the respiratory system of vertebrates
Serotonin clearance from the synaptic cleft
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_197730.3
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Messenger RNA decay in mammalian cells: the exonuclease perspective
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_125114.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_178327.3
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Identification of a human histone acetyltransferase related to monocytic leukemia zinc finger protein
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_125583.1
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Lithium-calcium exchange is mediated by a distinct potassium-independent sodium-calcium exchanger
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_125283.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_197727.3
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p84, a new Gbetagamma-activated regulatory subunit of the type IB phosphoinositide 3-kinase p110gamma
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_107985.4
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_236581.1
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631743
Integrins: dynamic scaffolds for adhesion and signaling in platelets
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_124125.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_82528.4
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_80758.4
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_82731.4
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632665
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632678
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632677
Copper chaperone for superoxide dismutase
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Superoxide dismutase [Cu-Zn] ecNumber1.15.1.1/ecNumber
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645742
Extracellular superoxide dismutase [Cu-Zn]
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Emerging roles for E2F: beyond the G1/S transition and DNA replication.
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_197282.3
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628372
Access of soluble antigens to the endoplasmic reticulum can explain cross-presentation by dendritic cells
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4717.2
Osteonectin, a bone-specific protein linking mineral to collagen
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3165.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2046052
Transcription elongation factor B polypeptide 1
RNA polymerase II transcription factor SIII subunit C
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_125598.1
RNA polymerase II transcription factor SIII subunit B
Transcription elongation factor B polypeptide 2
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=194697
Aryl hydrocarbon receptor nuclear translocator
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113534
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628378
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628443
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628384
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628385
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_197518.3
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ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Igamma
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Characterization of the gene encoding human cone transducin alpha-subunit (GNAT2)
Tyrosine-phosphorylated forms of Ig beta, CD22, TCR zeta and HOSS are major ligands for tandem SH2 domains of Syk
Effect of transmembrane and kinase domain mutations on fibroblast growth factor receptor 3 chimera signaling in PC12 cells. A model for the control of receptor tyrosine kinase activation
Vav regulates activation of Rac but not Cdc42 during FcgammaR-mediated phagocytosis
Acquired and inherited disorders of cobalamin and folate in children
Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis--Golgi tethering
Novel aspects of tetramer assembly and N-terminal domain structure and function are revealed by recombinant expression of human AMP deaminase isoforms
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Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases
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Distinct roles for recombinant cytosolic 5'-nucleotidase I and -II in AMP and IMP catabolism in COS-7 and H9c2 rat myoblast cell lines
Phase 1 - Functionalization of compounds
Tandem pore domain halothane-inhibited K+ channel (THIK)
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Na+/Ca2+ exchangers: three mammalian gene families control Ca2+ transport
Sequence and expression of human GABAA receptor alpha 1 and beta 1 subunits
Cloning of cDNA sequences encoding human alpha 2 and alpha 3 gamma-aminobutyric acidA receptor subunits and characterization of the benzodiazepine pharmacology of recombinant alpha 1-, alpha 2-, alpha 3-, and alpha 5-containing human gamma-aminobutyric acidA receptors
AMP kinase and malonyl-CoA: targets for therapy of the metabolic syndrome
Serine/threonine-protein kinase WNK2 ecNumber2.7.11.1/ecNumber
Identification of a homophilic binding site in immunoglobulin-like domain 2 of the cell adhesion molecule L1
The prosthetic group of crystalline d-glyceraldehyde-3-phosphate dehydrogenase
The reaction between the superoxide anion radical and cytochrome c
Endogenous synthesis of coenzyme Q in eukaryotes
Serine/threonine-protein kinase WNK4 ecNumber2.7.11.1/ecNumber
Serine/threonine-protein kinase WNK3 ecNumber2.7.11.1/ecNumber
Aspartate-glutamate-alanine-histidine box motif (DEAH)/RNA helicase A helicases sense microbial DNA in human plasmacytoid dendritic cells
Proc. Natl. Acad. Sci. U.S.A. 107:15181-6
Identification of inflammatory gene modules based on variations of human endothelial cell responses to oxidized lipids
p21-activated protein kinase: a crucial component of morphological signaling?
Amiloride-sensitive sodium channel subunit gamma
C4b-binding protein and factor H compensate for the loss of membrane-bound complement inhibitors to protect apoptotic cells against excessive complement attack
Amiloride-sensitive sodium channel subunit beta
Protein disulfide isomerase and glutathione are alternative substrates in the one Cys catalytic cycle of glutathione peroxidase 7
Amiloride-sensitive sodium channel subunit alpha
Amiloride-sensitive sodium channel subunit delta
Hyperhomocysteinemia due to methionine synthase deficiency, cblG: structure of the MTR gene, genotype diversity, and recognition of a common mutation, P1173L
Rabenosyn-5 and EHD1 interact and sequentially regulate protein recycling to the plasma membrane
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Principles of bioactive lipid signalling: lessons from sphingolipids
Coregulation of estrogen receptor by ERBB4/HER4 establishes a growth-promoting autocrine signal in breast tumor cells
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Membrane lipids: where they are and how they behave
Membrane recognition by phospholipid-binding domains
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Human G(olf) alpha: complementary deoxyribonucleic acid structure and expression in pancreatic islets and other tissues outside the olfactory neuroepithelium and central nervous system
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Resolution of AP sites via the multiple-nucleotide patch replacement pathway
Critical role for tetrahydrobiopterin recycling by dihydrofolate reductase in regulation of endothelial nitric-oxide synthase coupling: relative importance of the de novo biopterin synthesis versus salvage pathways
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Serine/threonine-protein kinase Sgk2 ecNumber2.7.11.1/ecNumber
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Serine/threonine-protein kinase Sgk1 ecNumber2.7.11.1/ecNumber
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Serine/threonine-protein kinase Sgk3 ecNumber2.7.11.1/ecNumber
NEDD4-like E3 ubiquitin-protein ligase WWP1
Serine/threonine-protein kinase WNK1 ecNumber2.7.11.1/ecNumber
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Transcriptional regulation by calcium, calcineurin, and NFAT
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Proximity of the poly(A)-binding protein to a premature termination codon inhibits mammalian nonsense-mediated mRNA decay
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Importance of extra- and intracellular domains of TLR1 and TLR2 in NFkappa B signaling
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Netrin-1: interaction with deleted in colorectal cancer (DCC) and alterations in brain tumors and neuroblastomas
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_184113.3
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_244297.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_151747.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_151277.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2142830
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_150648.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_256551.1
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5643492
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_248531.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_263255.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2334.1
Frequent deletions at Xq28 indicate genetic heterogeneity in Hunter syndrome
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652044
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Amino acid and oligopeptide SLC transporters
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632147
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632146
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624167
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_240948.1
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640619
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646516
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646515
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5640633
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_151106.1
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=266010
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15596.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2142733
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629217
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653472
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_241789.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_260325.1
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652647
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_237067.1
The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response
Mechanical properties of adult vertebral cancellous bone: correlation with collagen intermolecular cross-links
The role of Akt in the signaling pathway of the glycoprotein Ib-IX induced platelet activation
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_207723.2
Sinauer Associates, Inc., P.O. Box 407 23 Plumtree Road, Sunderland, MA 01375 U.S.A.
Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro.
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628029
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628031
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628027
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628039
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628035
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_214601.2
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C1 domains exposed: from diacylglycerol binding to protein-protein interactions
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Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with Oct-4 in regulating transcription
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628961
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628959
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628958
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628957
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_208178.2
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_183795.3
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_196774.3
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628020
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628023
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628022
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_242972.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_225580.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628069
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628025
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628024
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628026
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628065
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628063
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628061
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628060
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628070
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_231663.1
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628066
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628072
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guanosine 5'-(3-(alpha-D-mannopyranosyl) dihydrogen diphosphate)
The sugar is sIRVed: sorting Glut4 and its fellow travelers
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628074
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628077
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628076
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628079
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628078
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628081
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628080
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628083
Separate SCF(CDC4) recognition elements target Cdc6 for proteolysis in S phase and mitosis.
Negative regulation of the PI3K/AKT network
Lowe syndrome, a deficiency of phosphatidylinositol 4,5-bisphosphate 5-phosphatase in the Golgi apparatus
The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay
Short transient receptor potential channel 3
Transient receptor potential cation channel subfamily A member 1
Short transient receptor potential channel 1
Sodium-dependent phosphate transport protein 4
Mitochondrial sodium/hydrogen exchanger 9B2
NOD-like receptors (NLRs): bona fide intracellular microbial sensors
Sodium leak channel non-selective protein
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630199
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630212
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630202
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630207
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630211
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630210
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630209
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653112
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_204697.2
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The transport of pyruvate in rat liver mitochondria
Synthesis of PIPs at the late endosome membrane
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_150975.1
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Phosphorylation-dependent scaffolding role of JSAP1/JIP3 in the ASK1-JNK signaling pathway. A new mode of regulation of the MAP kinase cascade
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Heparin and heparan sulfate: biosynthesis, structure and function
Disease-causing missense mutations affect enzymatic activity, stability and oligomerization of glutaryl-CoA dehydrogenase (GCDH)
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Dissecting and manipulating the pathway for glycosylphosphatidylinositol-anchor biosynthesis
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15722.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_211365.2
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Cleavage and activation of p21-activated protein kinase gamma-PAK by CPP32 (caspase 3). Effects of autophosphorylation on activity
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Phosphoinositide phosphatases in a network of signalling reactions
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Tryptophan metabolism in the central nervous system: medical implications
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MCM8 is an MCM2-7-related protein that functions as a DNA helicase during replication elongation and not initiation
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Myosin II activation promotes neurite retraction during the action of Rho and Rho-kinase
The C-terminal cytoplasmic Lys-thr-X-X-X-Trp motif in frizzled receptors mediates Wnt/beta-catenin signalling
Direct interaction of Cbl with pTyr 1045 of the EGF receptor (EGFR) is required to sort the EGFR to lysosomes for degradation
FGFR1 is fused with a novel zinc-finger gene, ZNF198, in the t(8;13) leukaemia/lymphoma syndrome
Domain structure and organisation in extracellular matrix proteins
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Purification, characterization and inhibition of D-3-aminoisobutyrate aminotransferase from the rat liver
Fatty acid, triacylglycerol, and ketone body metabolism
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Mammalian frataxin: an essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19850.2
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Highly sodium permeable acetylcholine nicotinic receptors
Kit- and Fc epsilonRI-induced differential phosphorylation of the transmembrane adaptor molecule NTAL/LAB/LAT2 allows flexibility in its scaffolding function in mast cells
(S)-alpha-amino-beta-phenylpropionic acid
Human hexokinase II gene: exon-intron organization, mutation screening in NIDDM, and its relationship to muscle hexokinase activity
Phospholipid meets all-trans-retinal: the making of RPE bisretinoids
Benzo(a)pyrene-7,8-diol-glutathione conjugate
Phorbol esters modulate the Ras exchange factor RasGRP3
Purine ribonucleoside monophosphate biosynthesis
Regulation of ubiquitin protein ligase activity in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations
RNA sequence elements required for high affinity binding by the zinc finger domain of tristetraprolin: conformational changes coupled to the bipartite nature of Au-rich MRNA-destabilizing motifs
A pharmacological map of the PI3-K family defines a role for p110alpha in insulin signaling
Emerging role of ISG15 in antiviral immunity
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Age related changes in the reducible cross-links of collagen
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Regulation of fructose-6-phosphate 2-kinase by phosphorylation and dephosphorylation: possible mechanism for coordinated control of glycolysis and glycogenolysis
Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein
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Epidermal growth factor receptors with tyrosine kinase domain mutations exhibit reduced Cbl association, poor ubiquitylation, and down-regulation but are efficiently internalized
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Role of semaphorins during axon growth and guidance
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Solute carrier organic anion transporter family member 4C1
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Solute carrier organic anion transporter family member 2B1
Plasma membrane calcium-transporting ATPase 1
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Plasma membrane calcium-transporting ATPase 2
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misspliced GSK3beta mutants stabilize beta-catenin
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Integrated signalling pathways for mast-cell activation
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Mechanism of RNA polymerase II--specific initiation of transcription in vitro: ATP requirement and uncapped runoff transcripts.
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Neuronal phosphoproteins. Mediators of signal transduction
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Human ESCRT-II complex and its role in human immunodeficiency virus type 1 release
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A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: implications for filovirus budding
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Sterol transfer by ABCG5 and ABCG8: in vitro assay and reconstitution
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Molecular mechanism of phase I and phase II drug-metabolizing enzymes: implications for detoxification
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ChREBP activates metabolic gene expression
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Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant
GPD1L links redox state to cardiac excitability by PKC-dependent phosphorylation of the sodium channel SCN5A
Am J Physiol Heart Circ Physiol 297:H1446-52
Transport of phosphoenolpyruvate by the tricarboxylate transporting system in mammalian mitochondria
Allelism, non-allelism, and genetic compounds among the mucopolysaccharidoses
Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex
High-affinity glutamate transporter ligands
Human mitochondrial pyrophosphatase: cDNA cloning and analysis of the gene in patients with mtDNA depletion syndromes
Potassium-transporting ATPase alpha chain 1
Potassium-transporting ATPase alpha chain 2
Calcium-transporting ATPase type 2C member 2
Involvement of the ERK signaling cascade in protein kinase C-mediated cell cycle arrest in intestinal epithelial cells
Calcium-transporting ATPase type 2C member 1
Probable phospholipid-transporting ATPase IA
Potassium-transporting ATPase subunit beta
Mitochondrial metabolic states regulate nitric oxide and hydrogen peroxide diffusion to the cytosol
The affinity threshold for human B cell activation via the antigen receptor complex is reduced upon co-ligation of the antigen receptor with CD21 (CR2)
Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
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Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
Mammalian ABC transporters in health and disease
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Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
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Plasma membrane calcium-transporting ATPase 4
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Plasma membrane calcium-transporting ATPase 3
Aflatoxin B1 exo-N-acetylcysteine conjugate
Aflatoxin B1 endo-N-acetylcysteine conjugate
Aflatoxin B1 exo-cysteinylglycine conjugate
Aflatoxin B1 endo-cysteinylglycine conjugate
STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1
Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product
High-resolution single nucleotide polymorphism array analysis of epithelial ovarian cancer reveals numerous microdeletions and amplifications
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Atherosclerosis and sterol 27-hydroxylase: evidence for a role of this enzyme in elimination of cholesterol from human macrophages
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Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer
Cloning of a human nucleoside transporter implicated in the cellular uptake of adenosine and chemotherapeutic drugs
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20344.2
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Phagosomal maturation (early endosomal stage)
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The human tumour suppressor gene SLC5A8 expresses a Na+-monocarboxylate cotransporter
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_184111.3
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Targeting death and decoy receptors of the tumour-necrosis factor superfamily
The impact of single nucleotide polymorphisms on human aldehyde oxidase
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Shared as well as distinct roles of EHD proteins revealed by biochemical and functional comparisons in mammalian cells and C. elegans
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The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate kinase
RNA editing by adenosine deaminases that act on RNA.
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On the molecular basis and regulation of cellular capacitative calcium entry: roles for Trp proteins
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Probable phospholipid-transporting ATPase IC
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20257.1
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Probable phospholipid-transporting ATPase VA
Probable phospholipid-transporting ATPase ID
Cloning of the human cDNA which can complement the defect of the yeast mannosyltransferase I-deficient mutant alg 1
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hMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA
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Control of elongation by RNA polymerase II.
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From the background to the spotlight: TASK channels in pathological conditions
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Probable phospholipid-transporting ATPase VD
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AMP (dAMP) kinase from human erythrocytes
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Guanylate kinases from human erythrocytes, hog brain, and rat liver
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Structural and functional organization of the animal fatty acid synthase.
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Mechanistic insights into the superoxide-cytochrome c reaction by lysine surface scanning
Activation of NF-kappa B requires proteolysis of the inhibitor I kappa B-alpha: signal-induced phosphorylation of I kappa B-alpha alone does not release active NF-kappa B
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Cloning, characterization, and chromosomal localization of a human 5-HT6 serotonin receptor
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Chapter 3 Activation of TRP Channels in Mammalian Systems
Human erythrocyte pyrimidine 5'-nucleotidase, PN-I
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Functional characterization of a novel mammalian zinc transporter, ZnT6
Molecular basis for ADP-induced platelet activation. II. The P2Y1 receptor mediates ADP-induced intracellular calcium mobilization and shape change in platelets
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Chain gangs: new aspects of hyaluronan metabolism
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Functional studies of human intestinal alkaline sphingomyelinase by deglycosylation and mutagenesis
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Multidrug resistance- associated protein MGr1-Ag
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Cellular distribution, post-translational modification, and tumorigenic potential of human group III secreted phospholipase A(2)
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Eukaryotic translation initiation factor 4 gamma
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Generation and degradation of human endostatin proteins by various proteinases
Seven novel mutations in the methylenetetrahydrofolate reductase gene and genotype/phenotype correlations in severe methylenetetrahydrofolate reductase deficiency
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4,4-dimethylcholesta-8(9),24-dien-3beta-ol, NADPH + H+, and O2 react to form 4-methyl,4-carboxycholesta-8(9),24-dien-3beta-ol, NADP+, and H2O. This reaction, in the endoplasmic reticulum, is catalyzed by SC4MOL (C-4 methylsterol oxidase). The human enzyme has been identified based on its sequence similarity to yeast methyl sterol oxidase (ERG25) and the ability of the cloned human gene to rescue ERG25-deficient yeast cells (Li and Kaplan 1996). The mechanism and stoichiometry of the reaction have been inferred from studies of partially purified rat enzyme (Gaylor et al. 1975; Fukushima et al. 1981).
Further condensation of an isopentenyl pyrophosphate with geranyl pyrophosphate to form farnesyl pyrophosphate is catalyzed by the prenyltransferases FPP synthase and GGPP synthase. (Kavanagh et al, 2006)
The family of enzymes called prenyltransferases is involved in the biosynthesis of isoprenoids. Two members of this family are known to catalyse the sequential condensation of isopentenyl pyrophosphate to DMAPP: farnesyl pyrophosphate synthase (FPPS) and geranylgeranyl pyrophosphate synthetase (GGPPS) (Kavanaugh et al, 2006).
Cytosolic isopentenyl diphosphate isomerase (IPP isomerase) catalyzes an essential activation step in the isoprenoid biosynthetic pathway. It rearranges isopentenyl pyrophosphate into its highly electrophilic isomer, dimethylallyl pyrophosphate (DMAPP). IPP isomerase may also be located in human peroxisomes but it's function there is not clear.
In low concentrations of cholesterol SCAP interacts with Sec24 of the CopII coat complex causing SCAP:SREBP1A/1C/2 to be transported with the CopII complex from the endoplasmic reticulum to the Golgi.
SREBPs (SREBP1A, SREBP1C, SREBP2, also known as SREBFs) are transmembrane proteins that bind SCAP in the endoplasmic reticulum membrane. In the presence of cholesterol or oxysterols SCAP:SREBP1A/1C/2 binds INSIG and is retained in the endoplasmic reticulum. At cholesterol concentrations below 5 mol% SCAP changes conformation, SCAP:SREBP1A/1C/2 loses interaction with INSIG, binds the CopII coat complex, and is translocated to the Golgi.
Cholesterol is synthesized de novo from from acetyl CoA. The overall synthetic process is outlined in the figure below. Enzymes whose regulation plays a major role in determining the rate of cholesterol synthesis in the body are highlighted in red, and connections to other metabolic processes are indicated. The transformation of lanosterol into cholesterol requires multiple steps, including the removal of three methyl groups, the reduction of one double bond and the migration of another. These reactions may not occur in a single fixed order in the body, so the linear pathway laid out here following the work of Gaylor and colleagues (Gaylor 2002) is an oversimplification of the process that occurs in vivo. Defects in several of the enzymes involved in this process are associated with human disease and have provided useful insights into the regulatory roles of cholesterol and its synthetic intermediates in human development (Herman 2003; Song et al. 2005).
Desmosterol is reduced by NADPH + H+ to form cholesterol and NADP+, catalyzed by DHCR24 associated with the endoplasmic reticulum membrane.
(1R,2S)-1-Hydroxypropane-1,2,3-tricarboxylate [ChEBI:151]
Cholesta-5,7,24-trien-3beta-ol and NADPH + H+ react to form desmosterol and NADP+. This reaction is catalyzed by DHCR7, associated with the endoplasmic reticulum membrane. The biochemical details of the reaction are inferred from those of the reaction catalyzed by the well-studied rat enzyme (Bae et al. 1999).
4-methylcholesta-8(9),24-dien-3beta-ol, NADPH + H+, and O2 react to form 4-carboxycholesta-8(9),24-dien-3beta-ol, NADP+, and H2O. This reaction, in the endoplasmic reticulum, is catalyzed by SC4MOL (C-4 methylsterol oxidase). The human enzyme has been identified based on its sequence similarity to yeast methyl sterol oxidase (ERG25) and the ability of the cloned human gene to rescue ERG25-deficient yeast cells (Li and Kaplan 1996). The mechanism and stoichiometry of the reaction have been inferred from studies of partially purified rat enzyme (Gaylor et al. 1975; Fukushima et al. 1981).
Human peroxiredoxin 1 and 2 are not duplicate proteins: the unique presence of CYS83 in Prx1 underscores the structural and functional differences between Prx1 and Prx2
Carboxylation of acetyl-CoA and decarboxylation of malonyl-CoA are two processes that can control the amount of the signal transducer malonyl-CoA in the cell. The decarboxylation is catalysed by MCD enzyme in the peroxisomal matrix (Sacksteder et al, 1999).
In humans, the catabolism of phytanate, pristanate, and very long chain fatty acids as well as the first four steps of the biosynthesis of plasmalogens are catalyzed by peroxisomal enzymes. Defects in any of these enzymes or in the assembly of peroxisomes are associated with severe developmental disorders (Wanders and Watherham 2006).
3-hydroxy-3-methylglutaryl Coenzyme A synthase (HMG-CoA synthase) catalyzes the condensation of acetyl CoA with acetoacetyl CoA to produce HMG-CoA. There are two forms of this enzyme, cytosolic and mitochondrial. The cytosolic form is ubiquitous in the body and is involved in cholesterol biosynthesis and synthesis of other isoprenoid products. The mitochondrial form, found solely in the liver and kidney, is involved in the ketogenic pathway.
3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) catalyzes the four-electron reduction of HMG-CoA to mevalonate. Mevalonate concentrations in the cell are tightly controlled through the activity of HMGR, which is one of the most highly regulated enzymes known (Goldstein and Brown 1990).
Mevalonate kinase (MK) catalyzes the phosphorylation of mevalonate to mevalonate-5-phosphate.
acylglucosaminylphosphatidylinositol [ChEBI:52572]
Phosphomevalonate kinase (PMK) catalyzes the reversible, ATP-dependent phosphorylation of mevalonate-5-phosphate, producing mevalonate-5-pyrophosphate.
Mevalonate pyrophosphate decarboxylase (MPD) decarboxylates mevalonate-5-pyrophosphate (MVA5PP) into isopentenyl pyrophosphate (IPPP) while hydrolysing ATP to ADP and orthophosphate (Toth & Huwyler 1996).
Peroxisomal IDH1 (isocitrate dehydrogenase 1) homodimer catalyzes the reaction of isocitrate and NADP+ to form 2-oxoglutarate, CO2, and NADPH + H+. The same enzyme can also localize to the cytosol in at least some cell types (Geisbrecht and Gould 1999; Xu et al. 2004).
Cytosolic IDH1 (isocitrate dehydrogenase 1) homodimer catalyzes the reaction of isocitrate and NADP+ to form 2-oxoglutarate, CO2, and NADPH + H+. The same enzyme can also localize to peroxisomes (Geisbrecht and Gould 1999; Xu et al. 2004).
The conversion of isocitrate to 2-oxoglutarate (alpha-ketoglutarate) with the concomitant synthesis of NADPH from NADP+ is thought to play a significant role in supplying NADPH for other reactions in both the cytosol and the peroxisome (Geisbrecht and Gould 1999).
Linear fatty acids containing more than 18 carbons are broken down by beta-oxidation in peroxisomes to yield acetyl-CoA and medium chain-length fatty acyl CoA's such as octanoyl-CoA (Wanders and Waterham 2006).
Peroxisomal fatty acyl-CoA reductase 1 (FAR1) catalyzes the reaction of palmitoyl-CoA and 2 NADPH + 2 H+ to form hexadecanol, CoASH, and 2 NADP+. As judged from mRNA levels, FAR1 is widely expressed in the body (Cheng and Russell 2004).
Peroxisomal HSD17B4 dimer catalyzes the reaction of 3-hydroxyhexacosanoyl-CoA and NAD+ to form 3-ketohexacosanoyl-CoA and NADH + H+. The enzyme is bifunctional - an aminoterminal domain catalyzes the dehydrogenation of a variety of 3-hydroxyacyl-CoA's, the reaction annotated here, and a carboxyterminal domain catalyzes the hydration of a variety of trans-2,3-dehydroacyl-CoA's (Jiang et al. 1996, 1997). Defects in the enzyme are associated with a severe disorder of peroxisomal fatty acid metabolism in humans (Ferdinandusse et al. 2006).
Peroxisomal ACAA1 catalyzes the reaction of 3-ketohexacosanoyl-CoA and CoASH to form tetracosanoyl-CoA + acetyl-CoA (Bout et al. 1991).
Peroxisomal alkylglycerone phosphate synthase (AGPS) catalyzes the reaction of 1-palmitoylglycerone phosphate and hexadecanol to form O-hexadecylglycerone phosphate and palmitate. The active form of the enzyme is post-translationally cleaved to remove its 58 aminoterminal residues, has a molecule of FAD as a cofactor, and occurs in the peroxisome as a complex with glyceronephosphate O-acyltransferase (GNPAT) (Biermann et al. 1999; Bierman and van den Bosch 1999; de Vet et al. 2000).
1-Acylglycerol-3-phosphate is synthesized from dihydroxyacetone phosphate, an acyl CoA molecule and NADPH + H+ in four reactions catalyzed by peroxisomal enzymes, either in the matrix of the organelle or associated with its membrane. These reactions are annotated here for palmityl (C16:0) CoA. In a series of less well-characterized reactions in the cytosol and endoplasmic reticulum, these molecules are converted to ether lipids (plasmalogens). The functions of plasmalogens are not well understood. They are an abundant subclass of phospholipids, however, and defects in their metabolism are associated with serious human disease (de Vet et al. 1999; Nagan and Zoeller 2001).
Peroxisomal fatty acyl-CoA reductase 2 (FAR2) catalyzes the reaction of palmitoyl-CoA and 2 NADPH + 2 H+ to form hexadecanol, CoASH, and 2 NADP+. As judged from mRNA levels, FAR2 is not widely expressed in the body but is abundant in brain (Cheng and Russell 2004).
Peroxisomal glyceronephosphate O-acyltransferase (GNPAT) catalyzes the reaction of palmitoyl-CoA and DHAP to form 1-palmitoyl glycerone phosphate (1-palmitoyl dihydroxyacetone phosphate) and CoASH. The active form of the enzyme is one subunit of a heterotrimer with two molecules of the alkylglycerone phosphate synthase (AGPS) enzyme (Biermann et al. 1999). It was first purified and characterized biochemically by Ofman and Wanders (1994). Mutations in the GNPAT gene are associated with rhizomelic chondrodysplasia type 2 (Ofman et al. 1998, 2001).
Peroxisomal ACOX1 catalyzes the reaction of hexacosanoyl-CoA and O2 to form trans-2,3-dehydrohexacosanoyl-CoA and H2O2. The active form of the enzyme is a homodimer with FAD as a cofactor (Chu et al. 1995). Mutations in the ACOX1 gene are asociated with accumulation of very long chain fatty acids. Two isoforms of ACOX1, generated by alternative splicing are known; a mutation affecting specifically the second isoform blocks the oxidation of very long chain fatty acids (Ferdinandusse et al. 2007).
Peroxisomal HSD17B4 dimer catalyzes the reaction of trans-2,3-dehydrohexacosanoyl-CoA and H2O to form 3-hydroxyhexacosanoyl-CoA. The enzyme is bifunctional - an aminoterminal domain catalyzes the dehydrogenation of a variety of 3-hydroxyacyl-CoA's and a carboxyterminal domain catalyzes the hydration of a variety of trans-2,3-dehydroacyl-CoA's, the reaction annotated here (Jiang et al. 1996, 1997). Defects in the enzyme are associated with a severe disorder of peroxisomal fatty acid metabolism in humans (Ferdinandusse et al. 2006).
Peroxisomal carnitineacetyltransferase (CRAT) catalyzes the reaction of acetyl-CoA and carnitine to form acetylcarnitine and CoASH. The active form of the enzyme is a monomer (Bloisi et al. 1990; Wu et al. 2003).
Peroxisomal ACOT8 catalyzes the hydrolysis of acetyl-CoA to form acetate and CoASH (Jones et al. 1999; Wanders and Waterham 2006).
Peroxisomal carnitineacetyltransferase (CRAT) catalyzes the reaction of propionyl-CoA and carnitine to form propionylcarnitine and CoASH. The active form of the enzyme is a monomer (Bloisi et al. 1990; Wu et al. 2003).
N-retinylidene-N-retinylphosphatidylethanolamine [ChEBI:52592]
Pristanoyl-CoA, generated in the peroxisome by alpha-oxidation of dietary phytanic acid, is further catabolized by three cycles of peroxisomal beta-oxidation to yield 4,8-dimethylnonanoyl-CoA, acetyl-CoA and two molecules of propionyl-CoA. These molecules in turn are converted to carnitine conjugates, which can be transported to mitochondria (Wanders and Waterham 2006, Verhoeven et al. 1998, Ferdinandusse et al. 1999).
Peroxisomal HSD17B4 dimer catalyzes the reaction of trans-2,3-dehydropristanoyl-CoA and H2O to form 3-hydroxypristanoyl-CoA. The enzyme is bifunctional - an aminoterminal domain catalyzes the dehydrogenation of a variety of 3-hydroxyacyl-CoA's and a carboxyterminal domain catalyzes the hydration of a variety of trans-2,3-dehydroacyl-CoA's, the reaction annotated here (Jiang et al. 1996, 1997). Defects in the enzyme are associated with a severe disorder of peroxisomal fatty acid metabolism in humans (Ferdinandusse et al. 2006).
Peroxisomal HSD17B4 dimer catalyzes the reaction of 3-hydroxypristanoyl-CoA and NAD+ to form 3-ketoxypristanoyl-CoA and NADH + H+. The enzyme is bifunctional - an aminoterminal domain catalyzes the dehydrogenation of a variety of 3-hydroxyacyl-CoA's, the reaction annotated here, and a carboxyterminal domain catalyzes the hydration of a variety of trans-2,3-dehydroacyl-CoA's (Jiang et al. 1996, 1997). Defects in the enzyme are associated with a severe disorder of peroxisomal fatty acid metabolism in humans (Ferdinandusse et al. 2006).
Peroxisomal SCPx (Non-specific lipid transfer protein; SCP2) catalyzes the reaction of 3-ketopristanoyl-CoA and CoASH to form 4,8,12-trimethyltridecanoyl-CoA and propionyl-CoA. Both intact SCPx and an SCPx fragment corresponding to approximately the 430 aminoterminal residues of the protein are catalytically active in vitro; the latter form may predominate in vivo. Consistent with the role of SCPx in the beta-oxidation of branched-chain fatty acids in vitro, mutations in the protein are associated with elevated levels of pristanic acid in the blood in vivo and the development of neurological defects (Ferdinandusse et al. 2000, 2006).
Peroxisomal CROT catalyzes the reaction of 4,8-dimethylnonanoyl-CoA and carnitine to form 4,8-dimethylnonanoylcarnitine and CoASH (Ferdinandusse et al. 1999).
Peroxisomal ACOX3 catalyzes the reaction of (2S)-pristanoyl-CoA and O2 to form trans-2,3-dehydropristanoyl-CoA and H2O2. ACOX3 protein and enzyme activity have been observed in prostate tumors, but are undetectable in normal prostate tissue as well as in liver and kidney (where ACOX2 catalyzes the oxidation of pristanoyl-CoA) (Zha et al. 2005; Vanhooren et al. 1997). The physiological consequences of this differential gene expression are unknown.
TAX-responsive enhancer element binding protein 107
Homodimeric ABCD1 associated with the peroxisomal membrane mediates the uptake of cytosolic very long chain fatty acyl CoAs such as hexacosanoyl-CoA into the peroxisomal matrix. While the requirement for this uptake step in the catabolism of very long chain fatty acids is well-established, direct evidence for the function of ABCD1 as a transporter comes only from studies of its ability to restore peroxisomal long chain fatty acid catabolism in yeast strains whose endogenous transporters have been disrupted by mutation. ABCD1 is inferred to function as a dimer like other members of the ABCD transporter family. The energy requirements of peroxisomal fatty acid uptake (other ABCD transporter-mediated reactions are coupled to ATP hydrolysis) have not been established (van Roermund et al. 2008).
Peroxisomal HACL1 catalyzes the reaction of 2-hydroxyphytanoyl-CoA to form pristanal and formyl-CoA. The active form of the enzyme is a homotetramer, with one Mg++ and one molecule of thiamin pyrophosphate bound to each monomer (Croes et al. 1997; Foulon et al. 1999).
Phytanic acid arises through ruminant metabolism of chlorophyll and enters the human diet as a constituent of dairy products (Baxter 1968). It can act as an agonist for PPAR and other nuclear hormone receptors, but its normal role in human physiology, if any, is unclear. It is catabolized via a five-step alpha-oxidation reaction sequence that yields pristanoyl-CoA, which is turn is a substrate for beta-oxidation. These reactions take place in the peroxisomal matrix and their failure is associated with Refsum disease (Wanders et al. 2003).
The reactions involved in the metabolism of fatty acids and of the triacylglycerols and ketone bodies derived from them form a closely interrelated, coordinately regulated module that plays a central role in human energy metabolism.
Peroxisomal phytanoyl-CoA dioxygenase catalyzes the reaction of phytanoyl-CoA, 2-oxoglutarate, and O2 to form 2-hydroxyphytanoyl-CoA, succinate, and CO2. The mature form of the enzyme lacks the first 30 amino acid residues of the full-length polypeptide and is complexed with Fe++. Mutations in this enzyme are the commonest cause of Refsum disease (Mukherji et al. 2001; McDonough et al. 2005).
The set of genes regulated by PPAR-alpha is not fully known in humans, however many examples have been found in mice. Genes directly activated by PPAR-alpha contain peroxisome proliferator receptor elements (PPREs) in their promoters and include: 1) genes involved in fatty acid oxidation and ketogenesis (Acox1, Cyp4a, Acadm, Hmgcs2); 2) genes involved in fatty acid transport (Cd36, , Slc27a1, Fabp1, Cpt1a, Cpt2); 3) genes involved in producing fatty acids and very low density lipoproteins (Me1, Scd1); 4) genes encoding apolipoproteins (Apoa1, Apoa2, Apoa5); 5) genes involved in triglyceride clearance ( Angptl4); 6) genes involved in glycerol metabolism (Gpd1 in mouse); 7) genes involved in glucose metabolism (Pdk4); 8) genes involved in peroxisome proliferation (Pex11a); 9) genes involved in lipid storage (Plin, Adfp). Many other genes are known to be regulated by PPAR-alpha but whether their regulation is direct or indirect remains to be found. These genes include: ACACA, FAS, SREBP1, FADS1, DGAT1, ABCA1, PLTP, ABCB4, UGT2B4, SULT2A1, Pnpla2, Acsl1, Slc27a4, many Acot genes, and others (reviewed in Rakhshandehroo et al. 2010).
Peroxisome proliferator-activated receptor alpha (PPAR-alpha) is the major regulator of fatty acid oxidation in the liver. PPARalpha is also the target of fibrate drugs used to treat abnormal plasma lipid levels. PPAR-alpha is a type II nuclear receptor (its subcellular location does not depend on ligand binding). PPAR-alpha forms heterodimers with Retinoid X receptor alpha (RXR-alpha), another type II nuclear receptor. PPAR-alpha is activated by binding fatty acid ligands, especially polyunsaturated fatty acids having 18-22 carbon groups and 2-6 double bonds. The PPAR-alpha:RXR-alpha heterodimer binds peroxisome proliferator receptor elements (PPREs) in and around target genes. Binding of fatty acids and synthetic ligands causes a conformational change in PPAR-alpha such that it releases the corepressors and binds coactivators (CBP-SRC-HAT complex, ASC complex, and TRAP-Mediator complex) which initiate transcription of the target genes. Target genes of PPAR-alpha participate in fatty acid transport, fatty acid oxidation, triglyceride clearance, lipoprotein production, and cholesterol homeostasis.
The TRIB3 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The TXNRD1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
MTMR4 attenuates transforming growth factor beta (TGFbeta) signaling by dephosphorylating R-Smads in endosomes
Negative regulation of dE2F1 by cyclin-dependent kinases controls cell cycle timing
In human liver and kidney tissue, monomeric peroxisomal ACOX2 catalyzes the reaction of (2S)-pristanoyl-CoA and O2 to form trans-2,3-dehydropristanoyl-CoA and H2O2 (Vanhove et al. 1993; Baumgart et al. 1996).
Peroxisomal 2-methylacyl-CoA racemase (AMACR) catalyzes the isomerization of (2R)-pristanoyl-CoA to form (2S)-pristanoyl-CoA. The active form of the enzyme is a monomer (Schmitz et al. 1995; Amery et al. 2000; Ferdinandusse et al. 2000).
Progesterone, NADPH + H+, and O2 react to form 17alpha-hydroxyprogesterone, NADP+, and H2O, catalyzed by CYP17 (steroid 17alpha-monooxygenase), associated with the endoplasmic reticulum membrane.
17Alpha-hydroxyprogesterone, NADPH + H+, and O2 react to form 4-Androstene-3, 17-dione, NADP+, H2O, and acetaldehyde. CYP17 (which also catalyzes 17-alpha-hydroxylation) catalyzes this lyase reaction. There are marked species differences in which substrate is used for this lyase activity.
The 17HSD family of enzymes catalyze the final step in the synthesis of estradiol and testosterone. They convert inactive 17-ketosteroids to their active 17beta-hydroxy forms. Androstenedione, a ketosteroid, is reduced to testosterone, a highly potent androgen, by the enzyme 17beta-hydroxysteroid dehydrogenase isoform III (17HSD3). The other human isoforms of 17HSDs to take part in the final steps of active steroid biosynthesis are types 1 and VII, which reduce estrone to estradiol. Corticotropin (Adrenocorticotropic hormone, ACTH) acts through the ACTH receptor called melanocortin receptor type 2 (MC2R) to stimulate steroidogenesis, increasing the production of androgens (McKenna et al, 1997). In males, Lutropin (LH) stimulates testosterone production.
18-Hydroxycorticosterone and NADPH + H+ react to form aldosterone, NADP+, and H2O. This reaction is catalyzed by CYP11B2 associated with the inner mitochondrial membrane.
Corticosterone, NADPH + H+, and O2 react to form 18-hydroxycorticosterone, NADP+, and H2O. This reaction is catalyzed by CYP11B2 associated with the inner mitochondrial membrane.
17-alpha-hydroxypregnenolone, NADPH + H+, and O2 react to form DHA (dehydroepiandrostenedione), NADP+, H2O, and acetaldehyde. CYP17 (which also catalyzes 17-alpha-hydroxylation) catalyzes this lyase reaction. There are marked species differences in which substrate is used for this lyase activity. The human enzyme prefers 17alpha-pregnenolone (delta5 steroid) as substrate (Brock, BJ, Waterman, MR, 1999). Corticotropin (Adrenocorticotropic hormone, ACTH) acts through the ACTH receptor called melanocortin receptor type 2 (MC2R) to stimulate steroidogenesis, increasing the production of androgens (McKenna et al, 1997).
Aldosterone, the major human mineralocorticoid, is synthesized in the zona glomerulosa of the adrenal cortex from pregnenolone. Pregnenolone is converted to progesterone in two reactions, both catalyzed by 3-beta-hydroxysteroid dehydrogenase/isomerase. Progesterone is hydroxylated by CYP21A2 to form deoxycorticosterone, which in turn is converted to aldosterone in a three-reaction sequence catalyzed by CYP11B2 (Payne and Hales 2004).
17-Hydroxyprogesterone, NADPH + H+, and O2 react to form 11-deoxycortisol, NADP+, and H2O. This reaction is catalyzed by CYP21A2 (steroid 21-hydroxylase) associated with the endoplasmic reticulum membrane.
Progesterone, NAPDH + H+, and O2 react to form 11-deoxycorticosterone, NADP+ and H2O. This reaction is catalyzed by CYP21A2 associated with the endoplasmic reticulum membrane.
Cortisol, the major human glucocorticoid, is synthesized in the zona fasciculata of the adrenal cortex from pregnenolone. Pregnenolone is converted to 17alpha-hydoxyprogesterone in two reactions, both catalyzed by 3-beta-hydroxysteroid dehydrogenase/isomerase. 17Alpha-hydroxyprogesterone is hydroxylated by CYP21A2 to form 11-deoxycortisol, which in turn is converted to cortisol by CYP11B1. The conversion of the active steroid hormone, cortisol, to inactive cortisone occurs in many tissues, notably the liver (Payne and Hales 2004).
At the outer mitochondrial (OM) membrane, phosphatidic acid (PA) is hydrolyzed, and has one of its acyl chains cleaved off, by phospholipase A2 alpha/beta/delta/zeta (PLA2G4A/B/D/F) to form 1-acyl lysophosphatidic acid (LPA) (Ghomashchi et al. 2010).
Phosphatidylcholine (PC) is hydrolyzed to phosphatidic acid (PA) and choline (Cho) by the enzymes phospholipase D1/2 (PLD1/2), at the endoplasmic reticulum (ER) membrane (Lopez et al. 1998, Hammond et al. 1995).
At the outer mitochondrial (OM) membrane, 1-acyl lysophosphatidic acid (LPA) is acylated to phosphatidic acid (PA) by the enzyme 1-acyl-sn-glycerol-3-phosphate acyltransferases epsilon (AGPAT5) (Prasad et al. 2011).
Glycerol-3-phosphate (G3P) is acylated to 1-acyl lysophosphatidic acid (LPA) by the enzymes glycerol-3-phosphate acyltransferase 1 (GPAT, also known as GPAM) and glycerol-3-phosphate acyltransferase 2 (GPAT2), at the outer mitochondrial (OM) membrane (Shindou & Shimizu 2009, Chen et al. 2008, Takeuchi & Reue 2009).
At the endoplasmic reticulum (ER) membrane, phosphatidic acid (PA) is hydrolyzed, and has one of its acyl chains cleaved off, by membrane-associated phospholipase A2 gamma 2A (PLA2G2A), to form 1-acyl lysophosphatidic acid (LPA) (Singer et al. 2002).
At the endoplasmic reticulum (ER) membrane, phosphatidic acid (PA) is hydrolyzed, and has one of its acyl chains cleaved off, by phospholipase A2 alpha/beta/delta/zeta (PLA2G4A/B/D/F) to form 1-acyl lysophosphatidic acid (LPA) (Ghomashchi et al. 2010).
Dihydroxyacetone phosphate (DHAP) is converted to 1-acyl glycerone 3-phosphate (GO3P) by the enzyme dihydroxyacetone phosphate acyltransferase (GNPAT) (de Vet et al. 1999, Ofman et al. 1994). This reaction step links Glycerolipid metabolism to Ether lipid metabolism.
Steroid hormones are synthesized primarily in the adrenal gland and gonads. They regulate energy metabolism and stress responses (glucocorticoids), salt balance (mineralocorticoids), and sexual development and function (androgens and estrogens). All steroids are synthesized from cholesterol. Steroid hormone synthesis is largely regulated at the initial steps of cholesterol mobilization and transport into the mitochondrial matrix for conversion to pregnenolone. In the body, the fate of pregnenolone is tissue-specific: in the zona fasciculata of the adrenal cortex it is converted to cortisol, in the zona glomerulosa to aldosterone, and in the gonads to testosterone and then to estrone and estradiol. These pathways are outlined in the figure below, which also details the sites on the cholesterol molecule that undergo modification in the course of these reactions. Vitamin D3 (cholecalciferol) is a steroid hormone that plays a role in regulating calcium and bone metabolism. The processes by which it is synthesized, modified, and transported in the body are annotated here.
Androgens are the determining factors for male development and behaviour in vertebrates (Miller 2002).
Unstable kinetochore-microtubule capture and chromosomal instability following deletion of CENP-E
The conversion of testosterone to the most potent androgen, 5-alpha-dihydrotestosterone (DHT), is catalyzed by the microsomal 5alpha-steroid reductase enzymes, of which there are three reported types in humans to date (SRD5A1-3) (Andersson S and Russell DW, 1990; Andersson S et al, 1991; Uemura M et al, 2008 respectively). These enzymes are expressed in the prostate and other androgen target sites. Defects in SRD5A2 are the cause of pseudovaginal perineoscrotal hypospadias, also known as male pseudohermaphroditism (Anwar R et al, 1997). Corticotropin (Adrenocorticotropic hormone, ACTH) acts through the ACTH receptor called melanocortin receptor type 2 (MC2R) to stimulate steroidogenesis, increasing the production of androgens (McKenna et al, 1997).
5Beta-cholesten-7alpha,24(S)-diol-3-one and NADPH + H+ form 5beta-cholestan-3alpha,7alpha,24(S)-triol and NAPDP+. The reaction is catalyzed by 3alpha-hydroxysteroid dehydrogenase (AKR1C4), a cytosolic enzyme belonging to the aldo-keto reductase family (Dufort et al. 2001). Biochemical studies with rat proteins raise the possibility that other related enzymes may also carry out this reaction in vivo (Russell 2003).
The isomerization of 25(R) TetraHCA-CoA to (24R, 25R) 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA, catalyzed by 2-methylacyl-CoA racemase, occurs in the peroxisomal matrix.
The isomerization of 3,7,24THCA-CoA to (24R, 25R) 3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA, catalyzed by 2-methylacyl-CoA racemase, occurs in the peroxisomal matrix.
In the body, 24-hydroxycholesterol is synthesized in the brain, exported to the liver, and converted there to bile acids and bile salts. This pathway is only a minor source of bile acids and bile salts, but appears to be critical for the disposal of excess cholesterol from the brain (Bjorkhem et al. 1998; Javitt 2002). In the liver, conversion of 24-hydroxycholesterol to bile acids and bile salts is initiated with hydroxylation and oxidoreductase reactions to form 4-cholesten-7alpha,24(S)-diol-3-one. The pathway then branches: hydroxylation of 4-cholesten-7alpha,24(S)-diol-3-one to 4-cholesten-7alpha,12alpha,24(S)-triol-3-one leads ultimately to the formation of cholate, while its reduction to 5beta-cholestan-7alpha,24(S)-diol-3-one leads to chenodeoxycholate formation. In both branches, reactions in the cytosol, the mitochondrial matrix, and the peroxisomal matrix result in modifications to the ring structure, shortening and oxidation of the side chain, conversion to a Coenzyme A derivative, and conjugation with the amino acids glycine or taurine (Russell 2003). These reactions are outlined in the figure below. The final three reactions are identical to ones of bile salt synthesis initiated by 7alpha-hydroxylation and are shown as arrows with no substrates.
5Beta-cholesten-7alpha,12a,27-triol-3-one and NADPH + H+ form 5beta-cholestan-3alpha,7alpha,12a,27-tetrol and NAPDP+. The reaction is catalyzed by 3alpha-hydroxysteroid dehydrogenase (AKR1C4), a cytosolic enzyme belonging to the aldo-keto reductase family (Dufort et al. 2001). Biochemical studies with rat proteins raise the possibility that other related enzymes may also carry out this reaction in vivo (Russell 2003).
Choloyl CoA reacts with glycine or taurine to form glycocholate or taurocholate, releasing CoASH. This reaction, which completes the de novo synthesis of bile salts from cholesterol in vivo, is catalyzed by BAAT (Bile acid CoA:amino acid N-acyltransferase - Falany et al. 1994) and occurs in the peroxisomal matrix (Solaas et al. 2000; Mihalik et al. 2002). In vivo, the relative amounts of glycocholate and taurocholate synthesized appear to be determined solely by the intracellular abundances of glycine and taurine (Russell 2003).
A molecule of glycocholate, glycochenodeoxycholate, taurocholate, or taurochenodeoxycholate is transported from the cytosol to the extracellular space, coupled to the hydrolysis of a molecule of cytosolic ATP to ADP and orthophosphate. This reaction is mediated by ABCB11 (bile salt export pump). In the body, this reaction mediates the release of bile salts from the liver cells into the bile (Kullak-Ublick et al. 2004); the role of ABCB11 in the reaction is confirmed by the observed failure of bile salt export in patients in whom the transporter is defective (Noe et al. 2005).
Chenodeoxycholoyl CoA reacts with glycine or taurine to form glycochenodeoxycholate or taurochenodeoxycholate, releasing CoASH. This reaction, which completes the de novo synthesis of bile salts from cholesterol in vivo, is catalyzed by BAAT (Bile acid CoA:amino acid N-acyltransferase - Falany et al. 1994) and occurs in the peroxisomal matrix (Solaas et al. 2000; Mihalik et al. 2002). In vivo, the relative amounts of glycochenodeoxycholate and taurochenodeoxycholate synthesized appear to be determined solely by the intracellular abundances of glycine and taurine (Russell 2003).
5Beta-cholesten-7alpha,12alpha,24(S)-triol-3-one and NADPH + H+ form 5beta-cholestan-3alpha,7alpha,12alpha,24(S)-tetrol and NAPDP+. The reaction is catalyzed by 3alpha-hydroxysteroid dehydrogenase (AKR1C4), a cytosolic enzyme belonging to the aldo-keto reductase family (Dufort et al. 2001). Biochemical studies with rat proteins raise the possibility that other related enzymes may also carry out this reaction in vivo (Russell 2003).
In the liver, synthesis of bile acids and bile salts is initiated with the conversion of cholesterol to 7alpha-hydroxycholesterol and of 7alpha-hydroxycholesterol to 4-cholesten-7alpha-ol-3-one. The pathway then branches: hydroxylation of 4-cholesten-7alpha-ol-3-one to 4-cholesten-7alpha, 12alpha-diol-3-one leads ultimately to the formation of cholate, while its reduction to 5beta-cholestan-7alpha-ol-3-one leads to chenodeoxycholate formation. The amounts of substrate following each branch appear to be determined by abundance of the hydroxylase enzyme: in human liver, cholate synthesis predominates. In both branches, reactions in the cytosol, the mitochondrial matrix, and the peroxisomal matrix result in modifications to the ring structure, shortening and oxidation of the side chain, conversion to a Coenzyme A derivative, and conjugation with the amino acids glycine or taurine. In the body, glycocholate, taurocholate, glycochenodeoxycholate, and taurochenodeoxycholate are released from hepatocytes into the bile and ultimately into the lumen of the small intestine, where they function as detergents to solubilize dietary fats. The liver synthetic pathway also yields small amounts of bile acids, cholate and deoxycholate, which may play a feedback role in regulating the bile acid synthetic pathway (Russell 2003). These reactions are outlined in the figure below.
The first process in the synthesis of all steroid hormones is the synthesis of pregnenolone from cholesterol. In this process, cholesterol mobilized from cytosolic lipid droplets or from lysosomes is transported to mitochondria and becomes localized to the inner mitochondrial membrane. Cholesterol transport appears to be rate-limiting for steroid hormone synthesis and its regulation, at the step of StAR-mediated traversal of the mitochondrial membrane, plays a central role in determining the amounts and identities of steroid hormones made in the body. In the inner mitochondrial membrane, cholesterol is converted to pregnenolone in a sequence of three reactions, all catalyzed by CYP11A (side chain cleavage enzyme). Finally, pregnenolone re-enters the cytosol (Payne and Hales 2004; Stocco 2001).
Pregnenolone and NADPH + H+ react to form 17alpha-hydroxypregnenolone, NADP+, and H2O. CYP17A1 (steroid 17alpha-monooxygenase) associated with the endoplasmic reticulum membrane catalyzes this reaction.
In a healthy adult human, about 500 mg of cholesterol is converted to bile salts daily. Newly synthesized bile salts are secreted into the bile and released into the small intestine where they emulsify dietary fats (Russell 2003). About 95% of the bile salts in the intestine are recovered and returned to the liver (Kullak-Ublick et al. 2004; Trauner and Boyer 2002). The major pathway for bile salt synthesis in the liver begins with the conversion of cholesterol to 7alpha-hydroxycholesterol. Bile salt synthesis can also begin with the synthesis of an oxysterol - 24-hydroxycholesterol or 27-hydroxycholesterol. In the body, the initial steps of these two pathways occur in extrahepatic tissues, generating intermediates that are transported to the liver and converted to bile salts via the 7alpha-hydroxycholesterol pathway. These extrahepatic pathways contribute little to the total synthesis of bile salts, but are thought to play important roles in extrahepatic cholesterol homeostasis (Javitt 2002).
Isocaproaldehyde is reduced by NADPH + H+ to yield 4-methylpentan-1-ol and NADP+. This cytosolic reaction is catalyzed by AKR1B1 (aldose reductase). The purified human enzyme has been shown to catalyze this reaction efficiently in vitro; its abundance in adrenal tissue in humans and other mammals and its concordant expression with other enzymes of steroid hormone synthesis are consistent with it performing this role in vivo as well (Matsuura et al. 1996; Lefrancois-Martinez et al. 2004). The metabolic fate of 4-methylpentan-1-ol is unknown.
Substrate specificity of SIRT1-catalyzed lysine Nepsilon-deacetylation reaction probed with the side chain modified Nepsilon-acetyl-lysine analogs
In the body, 27-hydroxycholesterol is synthesized in multiple tissues, exported to the liver, and converted there to bile acids and bile salts. This pathway is only a minor source of bile acids and bile salts, but may play a significant role particularly in the mobilization of cholesterol from lung phagocytes (Bjorkhem et al. 1994; Babiker et al. 1999; Javitt 2002). In the liver, conversion of 27-hydroxycholesterol to bile acids and bile salts is initiated with hydroxylation and oxidoreductase reactions to form 4-cholesten-7alpha,27-diol-3-one. The pathway then branches: hydroxylation of 4-cholesten-7alpha,27-diol-3-one to 4-cholesten-7alpha,12alpha,27-triol-3-one leads ultimately to the formation of cholate, while its reduction to 5beta-cholestan-7alpha,27-diol-3-one leads to chenodeoxycholate formation. In both branches, reactions in the cytosol, the mitochondrial matrix, and the peroxisomal matrix result in modifications to the ring structure, shortening and oxidation of the side chain, conversion to a Coenzyme A derivative, and conjugation with the amino acids glycine or taurine (Russell 2003). These reactions are outlined in the figure below. The final nine reactions are identical to ones of bile salt synthesis initiated by 7alpha-hydroxylation and are shown as arrows with no substrates.
5Beta-cholesten-7alpha,27-diol-3-one and NADPH + H+ form 5beta-cholestan-3alpha,7alpha,27-triol and NAPDP+. The reaction is catalyzed by 3alpha-hydroxysteroid dehydrogenase (AKR1C4), a cytosolic enzyme belonging to the aldo-keto reductase family (Dufort et al. 2001). Biochemical studies with rat proteins raise the possibility that other related enzymes may also carry out this reaction in vivo (Russell 2003).
Of the 20-40 grams of bile salts released daily by the liver, all but approximately 0.5 grams are reabsorbed from the intestine, returned to the liver, and re-used. This recycling involves a series of transport processes: uptake by enterocytes mediated by ASBT (SLC10A2), traversal of the enterocyte cytosol mediated by ileal bile acid binding protein (I-BABP - FABP6), efflux from enterocytes mediated by MRP3 (ABCC3), travel through the portal blood as a complex with albumin, and uptake by hepatocytes mediated by Na+-taurocholate transporting protein (NTPC - SLC10A1) and, to a lesser extent by organic anion transporting proteins A, C, and 8 (OATPA - SLCO1A2, OATPC - SLCO1B1, and OATP-8 - SLCO1B3). Once returned to the hepatocyte cytosol, bile acids (generated in the intestine by the action of bacteria on secreted bile salts) are activated by conjugation with coenzyme A, then coupled to glycine or taurine, regenerating bile salts for re-export into the bile, mediated by the bile salt export pump, ABCB11 (Kullak-Ublick et al. 2004; Mihalik et al. 2002; Trauner and Boyer 2003). Unmodified bile salts returned to the hepatocyte cytosol can be re-exported by ABCB11 without further modification.
Cytosolic bile acid-CoA conjugates (choloyl-CoA; chenodeoxycholoyl-CoA) react with the amino acids glycine and taurine, generating the corresponding bile salts and coenzyme A, catalyzed by BAAT (bile acid-CoA:amino acid N-acetyltransferase). In the body, this reaction occurs in hepatocytes and is the means by which bile acids recovered from the intestine are converted to bile salts before being released again into the bile (Kullak-Ublick et al. 2004; Trauner and Boyer 2002).
In a healthy adult human, about 500 mg of cholesterol is converted to bile salts daily (Russell 2003). The major pathway for bile salt synthesis in the liver begins with the conversion of cholesterol to 7alpha-hydroxycholesterol. Bile salt synthesis can also begin with the synthesis of an oxysterol - 24-hydroxycholesterol or 27-hydroxycholesterol. In the body, the initial steps of these two pathways occur in extrahepatic tissues, generating intermediates that are transported to the liver and converted to bile salts via the 7alpha-hydroxycholesterol pathway. These extrahepatic pathways contribute little to the total synthesis of bile salts, but are thought to play important roles in cholesterol homeostasis (Javitt 2002).
The microsomal enzyme cholesterol 25-hydroxylase is a member of a lipid metabolizing enzyme family that utilizes oxygen and diiron-oxygen cofactor to hydroxylate, desaturate, epoxidate and acetylate substrates.
5Beta-cholesten-7alpha-ol-3-one and NADPH + H+ form 5beta-cholestan-3alpha,7alpha-diol and NAPDP+. The reaction is catalyzed by 3alpha-hydroxysteroid dehydrogenase (AKR1C4), a cytosolic enzyme belonging to the aldo-keto reductase family (Dufort et al. 2001). Biochemical studies with rat proteins raise the possibility that other related enzymes may also carry out this reaction in vivo (Russell 2003).
5Beta-cholesten-7alpha,12alpha-diol-3-one and NADPH + H+ form 5beta-cholestan-3alpha,7alpha,12alpha-triol and NAPDP+. The reaction is catalyzed by 3alpha-hydroxysteroid dehydrogenase (AKR1C4), a cytosolic enzyme belonging to the aldo-keto reductase family (Dufort et al. 2001). Biochemical studies with rat proteins raise the possibility that other related enzymes may also carry out this reaction in vivo (Russell 2003).
The isomerization of 25(R) THCA-CoA to 25(S) THCA-CoA, catalyzed by 2-methylacyl-CoA racemase, occurs in the peroxisomal matrix.
The PMVK gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The MVK gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Sterol regulatory element binding proteins (SREBPs, SREBFs) respond to low cholesterol concentrations by transiting to the nucleus and activating genes involved in cholesterol and lipid biosynthesis (reviewed in Brown and Goldstein 2009, Osborne and Espenshade 2009, Weber et al. 2004). Newly synthesized SREBPs are transmembrane proteins that bind SCAP in the endoplasmic reticulum (ER) membrane. SCAP binds cholesterol which causes a conformational change that allows SCAP to interact with INSIG, retaining the SCAP:SREBP complex in the ER. INSIG binds oxysterols, which cause INSIG to bind SCAP and retain SCAP:SREBP in the endoplasmic reticulum. In low cholesterol (below about 5 mol%) SCAP no longer interacts with cholesterol or INSIG and binds Sec24 of the CopII coat complex instead. Thus SCAP:SREBP transits with the CopII complex from the ER to the Golgi. In the Golgi SREBP is cleaved by S1P and then by S2P, releasing the N-terminal fragment of SREBP into the cytosol. The N-terminal fragment is imported to the nucleus by importin-beta and then acts with other factors, such as SP1 and NF-Y, to activate transcription of target genes. Targets of SREBP include the genes encoding all enzymes of cholesterol biosynthesis and several genes involved in lipogenesis. SREBP2 most strongly activates cholesterol biosynthesis while SREBP1C most strongly activates lipogenesis.
1-acyl-sn-glycero-3-phosphoserine [ChEBI:52603]
After transiting to the nucleus SREBPs (SREBP1A/1C/2, SREBFs) bind short sequences, sterol regulatory elements (SREs), in the promoters of target genes (reviewed in Eberle et al. 2004, Weber et al. 2004). SREBPs alone are relatively weak activators of transcription, with SREBP1C being significantly weaker than SREBP1A or SREBP2. In combination with other transcription factors such as SP1 and NF-Y the SREBPs are much stronger activators. SREBP1C seems to more specifically target genes involved in fatty acid synthesis while SREBP2 seems to target genes involved in cholesterol synthesis (Pai et al. 1998).
The FASN gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The GPAM gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The IDI1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Compartmentation of hexokinase in human blood cells. Characterization of soluble and particulate enzymes.
Choloyl-CoA and water react to form cholate and CoASH. This reaction, catalyzed by acyl-coenzyme A thioesterase 8, occurs in the peroxisomal matrix (Jones et al. 1999; Hunt et al. 2002). While bile salts are the major product of the de novo biosynthetic pathway in the normal human liver, bile acids are major feedback regulators of this pathway and this hydrolysis reaction is thought to play a role in generating them (Russell 2003).
3alpha,7alpha-dihydroxy-5beta-cholan-24-one-CoA and CoASH react to form chenodeoxycholoyl-CoA (3alpha,7alpha-dihydroxy-5beta-cholan-24-one-CoA) and propionyl CoA. This reaction, in the peroxisomal matrix, is catalyzed by peroxisomal thiolase 2 (sterol carrier protein 2).
3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-one-CoA and CoASH react to form choloyl-CoA (3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-one-CoA) and propionyl CoA. This reaction, in the peroxisomal matrix, is catalyzed by peroxisomal thiolase 2 (sterol carrier protein 2).
(24R, 25R) 3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA and NAD+ react to form 3alpha,7alpha-dihydroxy-5beta-cholest-24-one-CoA, NADH, and H+. This oxidation reaction, catalyzed by the peroxisomal D-bifunctional enzyme (Huyghe et al. 2006), occurs in the peroxisomal matrix.
(24R, 25R) 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA and NAD+ react to form 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-one-CoA, NADH, and H+. This oxidation reaction, catalyzed by the peroxisomal D-bifunctional enzyme (Huyghe et al. 2006), occurs in the peroxisomal matrix.
25(S) 3alpha,7alpha-dihydroxy-5beta-cholest-24-enoyl-CoA is hydrated to form (24R, 25R) 3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA. This reaction, catalyzed by the peroxisomal D-bifunctional enzyme (Huyghe et al. 2006), occurs in the peroxisomal matrix.
25(S) DHCA-CoA and O2 react to form 25(S) 3alpha,7alpha-dihydroxy-5beta-cholest-24-enoyl-CoA and H2O2. This dehydrogenation reaction occurs in the peroxisomal matrix. It is catalyzed by the FAD-containing peroxisomal enzyme branched chain acyl-CoA oxidase (ACOX2). The enzyme transfers electrons to molecular oxygen and hydrogen peroxide is produced as a byproduct.
3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA (THCA-CoA) is hydrated to form (24R, 25R) 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA. This reaction, catalyzed by the peroxisomal D-bifunctional enzyme (Huyghe et al. 2006), occurs in the peroxisomal matrix.
The isomerization of 25(R) DHCA-CoA to 25(S) DHCA-CoA, catalyzed by 2-methylacyl-CoA racemase, occurs in the peroxisomal matrix.
25(S) THCA-CoA and O2 react to form 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA (THCA-CoA) and H2O2. This dehydrogenation reaction occurs in the peroxisomal matrix. It is catalyzed by the FAD-containing peroxisomal enzyme branched chain acyl-CoA oxidase (ACOX2). The enzyme transfers electrons to molecular oxygen and hydrogen peroxide is produced as a byproduct.
Stoichiometry of 4-methyl sterol oxidase of rat liver microsomes
Human HRD1 promoter carries a functional unfolded protein response element to which XBP1 but not ATF6 directly binds
Loss-of-function fibroblast growth factor receptor-2 mutations in melanoma
RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease
The DHCR7 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
SREBP1A/1C/2 (SREBF1A/1C/2) dimer dissociates from Importin beta-1 in response to Ran-GTP in the nucleoplasm (Nagoshi et al. 1999).
The N-terminal domain of SREBP1A/1C/2 (SREBF1A/1C/2) dimerizes and is imported from the cytosol into the nucleus by importin-beta (Nagoshi et al. 1999, Nagoshi and Yoned 2001, Lee et al. 2003). In the nucleus the dimers bind DNA (Parraga et al. 1998) and activate transcription (Datta and Osborne 2005).
SREBP1A/1C/2 (SREBF1A/1C/2) dimer binds Importin beta-1 via the helix-loop-helix leucine zipper domain of SREBP1A/1C/2 (Nagoshi et al. 1999).
The FDPS gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The ELOVL6 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The MVD gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The ACACA gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Expression, purification and kinetic properties of human recombinant phospholipase C delta 3
S2P(MBTPS2), a membrane-bound protease in the Golgi, cleaves within the transmembrane region of SREBP1A/1C/2 (SREBF1A/1C/2), releasing the N-terminal domain of SREBP1A/1C/2 into the cytosol.
The N-terminal domains of SREBPs (SREBP1A/1C/2, SREBFs) dimerize via interaction of their helix-loop-helix leucine zipper domains (Nagoshi and Yoneda 2001).
Dehydroascorbic acid transport by GLUT4 in Xenopus oocytes and isolated rat adipocytes
Cloning and characterization of two human polyspecific organic cation transporters
Multiple splice variants of the human HIF-3 alpha locus are targets of the von Hippel-Lindau E3 ubiquitin ligase complex
Characterization and expression of the human A2a adenosine receptor gene
Tgfbr1 haploinsufficiency is a potent modifier of colorectal cancer development
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Cdc42 regulates Fc gamma receptor-mediated phagocytosis through the activation and phosphorylation of Wiskott-Aldrich syndrome protein (WASP) and neural-WASP
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Inwardly rectifying potassium channels: their structure, function, and physiological roles
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Distribution of aquaporin water channels AQP1 and AQP5 in the ductal system of the human pancreas
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Core exosome-independent roles for Rrp6 in cell cycle progression
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Comparison of the conversion rates of alpha-linolenic acid (18:3(n - 3)) and stearidonic acid (18:4(n - 3)) to longer polyunsaturated fatty acids in rats
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Heparan sulfate N-acetyl-alpha-D-glucosaminide
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Cloning and characterization of three human cDNAs encoding mRNA (guanine-7-)-methyltransferase, an mRNA cap methylase.
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Epstein-Barr virus small RNA associated protein
Cell surface heparin binding protein HIP
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Novel mutations in COX15 in a long surviving Leigh syndrome patient with cytochrome c oxidase deficiency
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Eukaryotic peptide chain release factor subunit 1
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Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance
At the beginning of this reaction, 1 molecule of 'Lauroyl-CoA', and 1 molecule of 'FAD' are present. At the end of this reaction, 1 molecule of 'FADH2', and 1 molecule of '2-trans-Dodecenoyl-CoA' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'acyl-CoA dehydrogenase activity' of 'LCAD acyl-CoA dehydrogenase homotetramer'.
The second pass through the beta-oxidation spiral starts with the saturated fatty acid myristoyl-CoA (from the first swing through the beta oxidation spiral) and produces lauroyl-CoA. Four enzymatic steps are required starting with LCAD CoA dehydrogenase (Long Chain) activity, followed by three enzymatic steps, enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and ketoacyl-CoA thiolase activities, all present in the mitochondrial membrane associated trifunctional protein.
At the beginning of this reaction, 1 molecule of 'trans-Tetradec-2-enoyl-CoA', and 1 molecule of 'H2O' are present. At the end of this reaction, 1 molecule of '(S)-3-Hydroxytetradecanoyl-CoA' is present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'enoyl-CoA hydratase activity' of 'Trifunctional Protein'.
At the beginning of this reaction, 1 molecule of 'myristoyl-CoA', and 1 molecule of 'FAD' are present. At the end of this reaction, 1 molecule of 'FADH2', and 1 molecule of 'trans-Tetradec-2-enoyl-CoA' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'acyl-CoA dehydrogenase activity' of 'LCAD acyl-CoA dehydrogenase homotetramer'.
At the beginning of this reaction, 1 molecule of '3-Oxotetradecanoyl-CoA', and 1 molecule of 'CoA' are present. At the end of this reaction, 1 molecule of 'Lauroyl-CoA', and 1 molecule of 'Acetyl-CoA' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'transferase activity' of 'Trifunctional Protein'.
U6 snRNA-associated Sm-like protein LSm1
At the beginning of this reaction, 1 molecule of 'NAD+', and 1 molecule of '(S)-3-Hydroxytetradecanoyl-CoA' are present. At the end of this reaction, 1 molecule of 'H+', 1 molecule of '3-Oxotetradecanoyl-CoA', and 1 molecule of 'NADH' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the '3-hydroxyacyl-CoA dehydrogenase activity' of 'Trifunctional Protein'.
At the beginning of this reaction, 1 molecule of 'NAD+', and 1 molecule of '(S)-3-Hydroxyhexadecanoyl-CoA' are present. At the end of this reaction, 1 molecule of '3-Oxopalmitoyl-CoA', 1 molecule of 'H+', and 1 molecule of 'NADH' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the '3-hydroxyacyl-CoA dehydrogenase activity' of 'Trifunctional Protein'.
At the beginning of this reaction, 1 molecule of 'H2O', and 1 molecule of 'trans-Hexadec-2-enoyl-CoA' are present. At the end of this reaction, 1 molecule of '(S)-3-Hydroxyhexadecanoyl-CoA' is present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'enoyl-CoA hydratase activity' of 'Trifunctional Protein'.
This first pass through the beta-oxidation spiral starts with the saturated fatty acid palmitoyl-CoA and produces myristoyl-CoA. Four enzymatic steps are required, starting with VLCAD CoA dehydrogenase (Very Long Chain) activity, followed by three enzymatic steps, enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and ketoacyl-CoA thiolase activities, all present in the mitochondrial membrane associated trifunctional protein.
At the beginning of this reaction, 1 molecule of '3-Oxopalmitoyl-CoA', and 1 molecule of 'CoA' are present. At the end of this reaction, 1 molecule of 'Acetyl-CoA', and 1 molecule of 'myristoyl-CoA' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'transferase activity' of 'Trifunctional Protein'.
The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen
Three conformationally distinct domains in the amino-terminal segment of type III procollagen and its rapid triple helix leads to and comes from coil transition
At the beginning of this reaction, 1 molecule of 'palmitoyl-CoA', and 1 molecule of 'FAD' are present. At the end of this reaction, 1 molecule of 'FADH2', and 1 molecule of 'trans-Hexadec-2-enoyl-CoA' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'acyl-CoA dehydrogenase activity' of 'VLCAD acyl-CoA dehydrogenase homodimer'.
The mitochondrial carnitine system catalyzes the transport of long-chain fatty acids into the mitochondrial matrix where they undergo beta oxidation. This transport system consists of the malonyl-CoA sensitive carnitine palmitoyltransferase I (CPT-I) localized in the mitochondrial outer membrane, the carnitine:acylcarnitine translocase, an integral inner membrane protein, and carnitine palmitoyltransferase II localized on the matrix side of the inner membrane. (Kerner and Hoppel, 2000).
The phosphorylated AMPK inactivates ACC2 in muscle cells by phophorylation. This results in decreased levels of malonyl CoA.
Cytosolic acetyl-CoA carboxylase 1 (ACACA) catalyzes the reaction of bicarbonate, ATP, and acetyl-CoA to form malonyl-CoA, ADP, and orthophosphate. The reaction is positively regulated by citrate. The human ACACA cDNA has been cloned (Abu-Elheiga et al. 1995) and the biochemical properties of the human enzyme have recently been described (Cheng et al. 2007; Locke et al. 2008). Four ACACA isoforms generated by alternative splicing have been identified as mRNAs - the protein product of the first has been characterized experimentally.
CPT2, associated with the inner mitochondrial membrane, catalyzes the reaction of palmitoylcarnitine and CoASH to form palmitoyl-CoA and carnitine (Verderio et al. 1995).
The carnitine-acylcarnitine transporter (SLC25A20 / CACT), embedded in the inner mitochondrial membrane, mediates the exchange of palmitoyl-carnitine (and other acylcarnitine esters) and carnitine across the inner mitochondrial membrane (Huizing et al., 1997).
Carnitine palmitoyl transferase 1 (CPT1) associated with the inner mitochondrial membrane, catalyzes the reaction of palmitoyl-CoA from the cytosol with carnitine in the mitochondrial intermembrane space to form palmitoylcarnitine and CoASH. Two CPT1 isoforms exist, encoded by two different genes. In the body, CPT1A is most abundant in liver while CPT1B is abundant in muscle. Both CPT1A and CPT1B are inhibited by malonyl-CoA (Morillas et al. 2002, 2004; Zammit et al. 2001; Zhu et al. 1997). Mutations in CPT1A are associated with defects in fatty acid metabolism and fasting intoilerance, consistent with the role assigned to CPT1 from studies in vitro and in animal models (IJlst et al. 1998; Gobin et al. 2003). In the nucleus, cellular retinoic acid-binding protein 1 or 2 (CRABP1 or 2), bound to all-trans-retinoic acid (atRA), directly binds to the heterodimeric complex of retinoic acid receptor alpha RXRA) and peroxisome proliferator-activated receptor delta (PPARD). When bound to PPARD, atRA can significantly increase the expression of proteins involved in fatty acid oxidation such as CPT1A via its induction of PPARD (Amengual et al. 2012).
The overall process of triglyceride (triacylglycerol) biosynthesis consists of four biochemical pathways: fatty acyl-CoA biosynthesis, conversion of fatty acyl-CoA to phosphatidic acid, conversion of phosphatidic acid to diacylglycerol, and conversion fo diacylglycerol to triacylglycerol.
U6 snRNA-associated Sm-like protein LSm2
Diacylglycerol O-acyltransferase 1 (DGAT2) associated with the endoplasmic reticulum membrane catalyzes the reaction of 1,2-diacyl-glycerol and acyl-CoA to form triacylglycerol + CoASH (Cases et al. 2001, Wakimoto et al. 2003).
U6 snRNA-associated Sm-like protein LSm4
Tetrameric diacylglycerol O-acyltransferase 1 (DGAT1) associated with the endoplasmic reticulum membrane catalyzes the reaction of 1,2-diacyl-glycerol and acyl-CoA to form triacylglycerol + CoASH (Cheng et al. 2001).
U6 snRNA-associated Sm-like protein LSm6
U6 snRNA-associated Sm-like protein LSm3
U6 snRNA-associated Sm-like protein LSm5
U6 snRNA-associated Sm-like protein LSm7
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653288
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_188892.3
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_217127.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621780
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5643844
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627109
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5643869
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_187446.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5643868
The fourth pass through the beta-oxidation spiral picks up where the last left off with the saturated fatty acid decanoyl-CoA and produces octanoyl-CoA. Four enzymatic steps are required starting with MCAD CoA dehydrogenase (Medium Chain) activity, followed by the enoyl-CoA hydratase activity of crotonase, the 3-hydroxyacyl-CoA dehydrogenase activity of the short chain 3-hydroxyacyl-CoA dehydrogenase (SCHAD), and completed by the ketoacyl-CoA thiolase activity, present in the mitochondrial membrane associated trifunctional protein. Note that the 3-hydroxyacyl-CoA dehydrogenase activity of SCHAD is not actually limited to short chain fatty acids, in fact SCHAD has a broad substrate specificity.
At the beginning of this reaction, 1 molecule of '3-Oxodecanoyl-CoA', and 1 molecule of 'CoA' are present. At the end of this reaction, 1 molecule of 'Acetyl-CoA', and 1 molecule of 'Octanoyl-CoA' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'transferase activity' of 'Trifunctional Protein'.
At the beginning of this reaction, 1 molecule of '(S)-Hydroxydecanoyl-CoA', and 1 molecule of 'NAD+' are present. At the end of this reaction, 1 molecule of 'H+', 1 molecule of '3-Oxodecanoyl-CoA', and 1 molecule of 'NADH' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the '3-hydroxyacyl-CoA dehydrogenase activity' of 'short chain 3-hydroxyacyl-CoA dehydrogenase homodimer'.
At the beginning of this reaction, 1 molecule of 'trans-Dec-2-enoyl-CoA', and 1 molecule of 'H2O' are present. At the end of this reaction, 1 molecule of '(S)-Hydroxydecanoyl-CoA' is present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'enoyl-CoA hydratase activity' of 'enoyl-CoA hydratase hexamer'.
Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase
At the beginning of this reaction, 1 molecule of 'Octanoyl-CoA', and 1 molecule of 'FAD' are present. At the end of this reaction, 1 molecule of 'FADH2', and 1 molecule of 'trans-Oct-2-enoyl-CoA' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'acyl-CoA dehydrogenase activity' of 'MCAD acyl-CoA dehydrogenase homotetramer'.
At the beginning of this reaction, 1 molecule of '2-trans-Dodecenoyl-CoA', and 1 molecule of 'H2O' are present. At the end of this reaction, 1 molecule of '(S)-3-Hydroxydodecanoyl-CoA' is present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'enoyl-CoA hydratase activity' of 'enoyl-CoA hydratase hexamer'.
Inorganic pyrophosphatase 2, mitochondrial
At the beginning of this reaction, 1 molecule of 'Decanoyl-CoA', and 1 molecule of 'FAD' are present. At the end of this reaction, 1 molecule of 'trans-Dec-2-enoyl-CoA', and 1 molecule of 'FADH2' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'acyl-CoA dehydrogenase activity' of 'MCAD acyl-CoA dehydrogenase homotetramer'.
The third pass through the beta-oxidation spiral picks up where the last left off with the saturated fatty acid lauroyl-CoA and produces decanoyl-CoA. Four enzymatic steps are required starting with LCAD CoA dehydrogenase (Long Chain) activity, followed by the enoyl-CoA hydratase activity of crotonase, the 3-hydroxyacyl-CoA dehydrogenase activity of the short chain 3-hydroxyacyl-CoA dehydrogenase (SCHAD), and completed by the ketoacyl-CoA thiolase activity, present in the mitochondrial membrane associated trifunctional protein. Note that the 3-hydroxyacyl-CoA dehydrogenase activity of SCHAD is not actually limited to short chain fatty acids, in fact SCHAD has a broad substrate specificity.
At the beginning of this reaction, 1 molecule of '3-Oxododecanoyl-CoA', and 1 molecule of 'CoA' are present. At the end of this reaction, 1 molecule of 'Decanoyl-CoA', and 1 molecule of 'Acetyl-CoA' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'transferase activity' of 'Trifunctional Protein'.
At the beginning of this reaction, 1 molecule of '(S)-3-Hydroxydodecanoyl-CoA', and 1 molecule of 'NAD+' are present. At the end of this reaction, 1 molecule of 'H+', 1 molecule of '3-Oxododecanoyl-CoA', and 1 molecule of 'NADH' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the '3-hydroxyacyl-CoA dehydrogenase activity' of 'short chain 3-hydroxyacyl-CoA dehydrogenase homodimer'.
Glycosylation and palmitoylation of Wnt-3a are coupled to produce an active form of Wnt-3a
In primary adipocytes from young rats and in adipocytes derived from 3T3-L1 cells in vitro, phosphorylated hormone-sensitive lipase translocates from the cytosol to the surfaces of lipid particles following the phosphorylation of perilipin (Clifford et al. 2000; Su et al. 2003; Sztalryd et al. 2003) The human reaction is inferred from the well-studied rat one.
Rat HSL is inactivated by dephosphorylation. The catalyst of this reaction is unknown. Protein phosphatases 1 and 2A are both abundant in rat adipocytes and both are active on HSL (Olsson and Belfrage 1987; Wood et al. 1993). Whether these enzymes act on phosphate groups attached to serine residues 659 and 660 of HSL is unknown, however (Holm et al. 2000). Although the reaction is annotated as though the phosphatase acts on phosphorylated HSL monomers, this also is unknown: does the HSL:FABP complex dissociate before HSL dephosphorylation (as implied here), or does dephosphorylation of HSL drive dissociation of the complex? Dephosphorylation of human HSL has not been studied in detail, so the human reaction is inferred from the well-studied rat one.
Triacylglycerol is a major energy store in the body and its hydrolysis to yield fatty acids and glycerol is a tightly regulated part of energy metabolism. A central part in this regulation is played by hormone-sensitive lipase (HSL), a neutral lipase abundant in adipocytes and skeletal and cardiac muscle, but also abundant in ovarian and adrenal tissue, where it mediates cholesterol ester hydrolysis, yielding cholesterol for steroid biosynthesis. The hormones to which it is sensitive include catecholamines (e.g., epinephrine), ACTH, and glucagon, all of which trigger signaling cascades that lead to its phosphorylation and activation, and insulin, which sets off events leading to its dephosphorylation and inactivation (Holm et al. 2000; Kraemer and Shen 2002). The processes of triacylglycerol and cholesterol ester hydrolysis are also regulated by subcellular compartmentalization: these lipids are packaged in cytosolic particles and the enzymes responsible for their hydrolysis, and perhaps for additional steps in their metabolism, are organized at the surfaces of these particles (e.g., Brasaemle et al. 2004). This organization is dynamic: the inactive form of HSL is not associated with the particles, but is translocated there after being phosphorylated. Conversely, perilipin, a major constituent of the particle surface, appears to block access of enzymes to the lipids within the particle; its phosphorylation allows greater access. Here, HSL-mediated triacylglycerol hydrolysis is described as a pathway containing twelve reactions. The first six of these involve activation: phosphorylation of HSL, dimerization of HSL, disruption of CGI-58:perilipin complexes at the surfaces of cytosolic lipid particles, phosphorylation of perilipin, association of phosphorylated HSL with FABP, and translocation of HSL from the cytosol to the surfaces of lipid particles. The next four reactions are the hydrolysis reactions themselves: the hydrolysis of cholesterol esters, and the successive removal of three fatty acids from triacylglycerol. The last two reactions, dephosphorylation of perilipin and HSL, negatively regulate the pathway. These events are outlined in the figure below. Inputs (substrates) and outputs (products) of individual reactions are connected by black arrows; blue lines connect output activated enzymes to the other reactions that they catalyze. Despite the undoubted importance of these reactions in normal human energy metabolism and in the pathology of diseases such as type II diabetes, they have been studied only to a limited extent in human cells and tissues. Most experimental data are derived instead from two rodent model systems: primary adipocytes from rats, and mouse 3T3-L1 cells induced to differentiate into adipocytes.
Processes annotated here include the digestion of dietary lipids, sterol uptake, the formation and turnover of lipoproteins (chylomicrons, VLDL, LDL, and HDL), and the mobilization of fatty acids through the action of hormone-sensitive lipase.
LDL (low density lipoproteins) are complexes of a single molecule of apoprotein B-100 (apoB-100) non-covalently associated with triacylglycerol, free cholesterol, cholesterol esters, and phospholipids. LDL complexes contain single molecules of apoB-100, but their content of lipids is variable (Chapman et al. 1988; Mateu et al. 1972; Tardieu et al. 1976). High levels of LDL in the blood are strongly correlated with increased risk of atherosclerosis, and recent studies have raised the possibility that this risk is further increased in individuals whose blood LDL population is enriched in high-density (low lipid content) LDL complexes (Rizzo and Berneis 2006). The LDL complex annotated here is given a lipid composition that is the average of those measured in the studies by Chapman, Mateu, Tardieu and their colleagues. Annotation of LDL biology in Reactome to date is largely centered on the process of LDL endocytosis. As outlined in the figure below, extracellular low density lipoprotein (LDL) complexes bind to LDL receptors associated with coated pits at the cell surface (a), forming complexes that are internalized and passed via clathrin-coated vesicles (b) to endosomes (c), where they dissociate. The LDL particles move into lysosomes (d) and are degraded while the LDL receptors are returned to the cell surface (e). This process occurs in most cell types but is especially prominent in hepatocytes. It plays a major role in returning cholesterol from peripheral tissues to the liver. Familial hypercholesterolemia due to mutations affecting the LDL receptor (or, rarely, the apolipoprotein B-100 (apoB-100) component of LDL or the LDLRAP1 accessory protein involved in receptor uptake into clathrin-coated vesicles) is one of the commonest human genetic diseases, affecting approximately one person in 500 in many populations worldwide (Hobbs et al. 1990; Jeon and Blacklow 2005).
Because of their hydrophobicity, lipids are found in the extracellular spaces of the human body primarily in the form of lipoprotein complexes. Chylomicrons form in the small intestine and transport dietary lipids to other tissues in the body. Very low density lipoproteins (VLDL) form in the liver and transport triacylglycerol synthesized there to other tissues of the body. As they circulate, VLDL are acted on by lipoprotein lipases on the endothelial surfaces of blood vessels, liberating fatty acids and glycerol to be taken up by tissues and converting the VLDL first to intermediate density lipoproteins (IDL) and then to low density lipoproteins (LDL). IDL and LDL are cleared from the circulation via a specific cell surface receptor, found in the body primarily on the surfaces of liver cells. High density lipoprotein (HDL) particles, initially formed primarily by the liver, shuttle several kinds of lipids between tissues and other lipoproteins. Notably, they are responsible for the so-called reverse transport of cholesterol from peripheral tissues to LDL for return to the liver. Three aspects of lipoprotein function are currently annotated in Reactome: chylomicron-mediated lipid transport, LDL endocytosis and degradation, and HDL-mediated lipid transport.
Cytosolic rat HSL is phosphorylated on serine residues 659 and 660 by protein kinase A catalytic subunit (Anthonsen et al. 1998; Su et al. 2003). Three isoforms of protein kinase A are known, but with no known differences in substrate specificity or tissue specific expression patterns, so a generic PKA (with all three forms as instances) is annotated as the catalyst of this reaction. Other serine residues in HSL can be phosphorylated both in vitro and in vivo, and while these other phosphorylations appear not to affect triacylglycerol hydrolysis by HSL directly, they may affect the efficiency with which serines 659 and 660 themselves are phosphorylated, or affect the efficiency with which HSL is translocated to cytosolic lipid particles (Holm et al. 2000). Phosphorylation of human HSL has not been studied in detail, so the human reaction is inferred from the well-studied rat one. By BLAST alignment, human HSL residues 649 and 650 correspond to rat serines 659 and 660.
While both monomeric and homodimeric forms of rat HSL protein have been detected, the predominant species, and the one with substantially greater catalytic activity when activated by phosphorylation, is the homodimer so HSL-mediated lipolysis is annotated in Reactome with dimeric phosphorylated enzyme as the catalyst. Phosphorylation appears to be required for dimerization to proceed (Shen et al. 2000). Dimerization of human HSL has not been studied in detail, so the human reaction is inferred from the well-studied rat one.
While fatty acid synthesis from acetyl CoA proceeds in the cytosol, most acetyl CoA in the cell is generated within the mitochondria, by oxidative decarboxylation of the pyruvate derived from glycolysis, as well as from a number of reactions of amino acid catabolism. Mitochondrial Acetyl-CoA is transported to cytoplasm as citrate to participate in fatty acid biosynthesis. Mitochondrial citrate synthase, a tricarboxylic acid transporter in the inner mitochondrial membrane, and cytosolic citrate lyase are involved in this transport.
SLC25A1, in the inner mitochondrial membrane, mediates the exchange of mitochondrial citrate for cytosolic malate.
Human NPC1L1, associated with the plasma membrane, binds ezetimibe and becomes incapable of mediating cholesterol uptake. The molecular mechanisms of cholesterol transport and ezetimibe inhibition, however, remain unclear (Garcia-Calvo et al. 2005; Weinglass et al. 2008).
NPC1L1 protein mediates the uptake of dietary sterols from the gut lumen. These include cholesterol and plant sterols (phytosterols). Half to two-thirds of the 250-500 milligrams of cholesterol consumed daily from a typical western diet is taken up by this route and exported from enterocytes into the lymph in chylomicrons. Of the 200-400 milligrams of dietary phytosterol, only about 5% is absorbed.The drug ezetimibe interferes with NPC1L1-mediated sterol uptake (Oram and Vaughan 2006). Both cholesterol and phytosterols are secreted from the liver into the bile (Salen et al. 1970). Mutations affecting the ABCG5/8 transporter complex inhibit this process (e.g., Berge et al. 2000), while the molecular details of sterol export in human cells have not been worked out, they can be inferred from the properties of the homologous mouse proteins (Graf et al. 2003; Wang et al. 2006).
Dietary cholesterol is taken up into enterocytes from the gut lumen in a reaction mediated by plasma membrane-associated NPC1L1 protein. This role for NPC1L1 was first observed in studies of a mouse model system (Altman et al. 2004). Subsequent studies of human cultured cells confirmed the participation of NPC1L1 in cholesterol transport across membranes but suggested that this transport process might not be a major factor in dietary cholesterol uptake (Davies et al. 2005). Detailed studies in Maden-Darby canine kidney cells, both mediated by endogenous (canine) NPC1L1 and by overexpressed human protein, indicate a major role for NPC1L1 in the uptake of extracellular cholesterol. These studies have also shown that ezetimibe binds both human and canine proteins and renders them incapable of mediating cholesterol uptake. The molecular mechanisms of cholesterol transport and ezetimibe inhibition, however, remain unclear (Weinglass et al. 2008).
Dietary phytosterols (sterols derived from plants) are taken up into enterocytes from the gut lumen. The reaction is thought to be mediated by plasma membrane-associated NPC1L1 protein. Detailed studies in Maden-Darby canine kidney cells, both mediated by endogenous (canine) NPC1L1 and by overexpressed human protein, indicate a major role for NPC1L1 in the uptake of extracellular sterol. These studies have also shown that ezetimibe binds both human and canine proteins and renders them incapable of mediating sterol uptake. The molecular mechanisms of cholesterol transport and ezetimibe inhibition, however, remain unclear (Weinglass et al. 2008).
CEL (bile salt-dependent lipase) catalyzes the hydrolysis of extracellular monoacylglycerols to yield glycerol and a long-chain fatty acid. This reaction, in the lumen of the small intestine, is essential for the complete digestion of milk-derived triacylglycerols in the nursing infant (Bernback et al. 1990). Its importance in adult fat digestion is unclear. While alternative splicing gives rise to two CEL isoforms, only the longer one encodes all of the residues that form the active site of the enzyme (Reue et al. 1991). In vitro, monomeric CEL protein is active even in the absence of bile salts. its activity is greatly increased when it is complexed with two molecules of cholate, chenodeoxycholate, or their glycine or taurine conjugates (Lombardo and Guy 1980), and the predominant form of the enzyme active on lipid micelles in the gut is a dimer of two such complexes (Aubert-Jousset et al. 2004). CEL is synthesized in pancreatic acinar cells and released into the small intestine. It is also synthesized in the mammary gland and is a constituent of breast milk (Lombardo 2001; Bernback et al. 1990).
Dietary lipids such as long-chain triacylglycerols and cholesterol esters are digested in the stomach and small intestine to yield long-chain fatty acids, monoacylglycerols, glycerol and cholesterol through the action of a variety of lipases, and are then absorbed into enterocytes.
LDL receptors in the endosome membrane are quickly returned to the cell surface (Goldstein et al. 1979).
HDL particles play a central role in the reverse transport of cholesterol, the process by which cholesterol in tissues other than the liver is returned to the liver for conversion to bile salts and excretion from the body and provided to tissues such as the adrenals and gonads for steroid hormone synthesis (Tall et al. 2008). HDL particles are heterogeneous and can be fractionated into sub-populations based on their electrophoretic mobility, their density, or their content of various apolipoproteins. Sub-populations yielded by any one fractionation strategy, however, remain heterogeneous with respect to the other two parameters (Kontush and Chapman 2006). All HDL particles share two key features: they are assembled on a protein scaffold provided by apolipoprotein A-I (apoA-I), and they are recycled to allow a net flow of lipids from peripheral tissues to the liver and steroidogenic tissues while allowing apoA-I molecules to be re-used. The HDL life cycle annotated here does not capture the full complexity of HDL structure and function but rather is an attempt to outline the key steps by which HDL particles assemble and transfer their lipid content. These steps include the assembly of nascent (discoidal) HDL particles on newly synthesized apoA-I, a process that in the body occurs primarily in the liver, the loading of discoidal HDL with additional lipid through interaction with cells carrying excess cholesterol (transformation to spherical HDL), the conversion of HDL-associated cholesterol to cholesterol esters (remodeling of spherical HDL), the transfer of HDL lipids to target cells with the regeneration of pre-beta HDL (lipid-poor apoA-I), and the conversion of pre-beta HDL to discoidal HDL to complete the cycle. Additional reactions provide houekeeping functions needed for the efficient operation of the cycle: binding and release of CETP, dispersal of byproducts of the CETP reaction, and export and degradation of excess apoA-I protein. Finally, the function of torcetrapib as an inhibitor of CETP function is annotated.
LCAT activated by apoA-I catalyzes the reaction of cholesterol and phosphatidylcholine to yield cholesterol esterified with a long-chain fatty acid and 2-lysophosphatidylcholine. While this reaction was first studied in vitro using purified proteins in solution, it occurs in vivo on the surfaces of HDL particles where transiently-bound LCAT is activated by HDL-associated apoA-I protein and consumes HDL-associated cholesterol and phosphatidylcholine. The cholesterol ester reaction product is strongly associated with the HDL particle because of its increased hydrophobicity, while the 2-lysophosphatidylcholine product is released from the particle (Fielding et al. 1972 [2 references]; Adimoolam et al. 1998).
Hydroxysteroid (17-beta) dehydrogenase 12 (HSD17B12) catalyzes the reaction of 3-oxooctadecanoyl-CoA (3-oxostearoyl-CoA) and NADPH + H+ to form 3-hydroxyoctadecanoyl-CoA and NADP+. This activity of HSD17B12 protein and its localization to the endoplasmic reticulum membrane was established in studies of transfected cells expressing the protein (Moon and Horton 2003).
Trans-2,3-enoyl-CoA reductase (TECR) catalyzes the reaction of trans-octadec-2-enoyl-CoA and NADPH + H+ to form stearoyl-CoA and NADP+. This activity of TECR protein and its localization to the endoplasmic reticulum membrane was established in studies of transfected cells expressing the protein (Moon and Horton 2003).
Very long-chain fatty acyl-CoA molecules are synthesized from palmitic acid (C16) or other fatty acids that are synthesized de novo or obtained from the diet. Before they can be elongated, these fatty acids are activated by conversion to fatty acyl-CoAs in reactions catalyzed by the five members of the ACSL (acyl-CoA synthetase long-chain) enzyme family. Elongation proceeds by a four-step reaction sequence parallel to that responsible for the synthesis of palmitate (C16) from acetyl-CoA and malonyl-CoA: a molecule of malonyl-CoA condenses with the long chain fatty acyl-CoA forming a 3-oxoacyl-CoA containing two more carbon atoms than the starting long chain fatty acyl-CoA and CO2. This reaction is catalyzed by one of the seven members of the ELOVL (Elongation of very long chain fatty acids protein) enzyme family. The 3-oxoacyl-CoA is reduced to a 3-hydroxyacyl-CoA by HSD17B12 (hydroxysteroid (17-beta) dehydrogenase 12), 3-hydroxyacyl-CoA is dehydrated to a trans-2,3-enoyl-CoA, and the trans-2,3-enoyl-CoA is reduced to a fatty acid two carbon atoms longer than the input one by TECR (trans-2,3-enoyl-CoA reductase) enzyme. All of these enzyme activities are associated with separate polypeptides associated with the endoplasmic reticulum membrane, unlike the multifunctional and cytosolic FAS complex responsible for synthesis of palmitic acid (Jakobsson ea 2006; Nugteren 1965). The specific reactions annotated here mediate the synthesis of stearoyl-CoA (3-hydroxyoctadecanoyl-CoA) from palmitate, as well as the activation and condensation with malonyl-CoA of arachidonic acid, a 20-carbon unsaturated fatty acid that plays a central role in the synthesis of prostaglandins and related hormones. Human cells contain a wide range of very long chain fatty acids, and the enzymes involved in these reactions are believed to have broader substrate specificities than are shown in these annotations, but few direct experimental data are available to support more extensive annotations.
Fatty acyl-CoA biosynthesis involves following steps: -Palmitate synthesis catalyzed by Acetyl-CoA carboxylase and Fatty acid synthase -Conversion of palmitic acid to long chain fatty acids and -Conversion of long chain fatty acids to fatty acyl-CoA by acyl-CoA synthases.
Dihydroxyacetone phosphate (DHAP) is converted to glycerol-3-phosphate (G3P) by glycerol-3-phosphate dehydrogenase (GPD1) or by glycerol-3-phosphate dehydrogenase-like (GPD1L) enzymes (Ou et al. 2006, Valdivia et al. 2009). The active forms of both enzymes are homodimers. This reaction may be found in white adipose tissues where glycerol-3-kinase activity is not observed in sufficient levels. GPD1/GPD1L reduces dihydroxyacetone phosphate with NADH donating electrons to this reduction.
Glycerol can be a source for glycerol-3-phosphate, in which case, a phosphate form ATP is transferred to glycerol by glycerol kinase forming glycerol-3-phosphate and ADP.
Glycerol-3-phosphate (G3P) is acylated to 1-acyl lysophosphatidic acid (LPA) by the enzymes glycerol-3-phosphate acyltransferase 4 (AGPAT6) at the endoplasmic reticulum (ER) membrane (Cao et al., 2006; Chen et al., 2008).
Either of GPAM or GPAT2 (glycerol-3-phosphate acyltransferase, mitochondrial; glycerol-3-phosphate acyltransferase 2, mitochondrial) associated with the outer mitochondrial membrane catalyzes the reaction of cytosolic glycerol 3-phosphate and acyl-CoA to form 1-acylglycerol 3-phosphate and CoASH. The biochemical properties and location of human GPAM have been established through studies of the recombinant protein (Chen et al. 2008); those features of GPAT2 have been inferred from the properties of its rat homologue and those of GPAM. GPAM and GPAT2 differ in their their preferences for acyl-CoA substrates (Shindou & Shimizu 2009) and in their expression patterns in the body (Takeuchi & Reue 2009).
At the endoplasmic reticulum (ER) membrane, 1-acyl-lysophosphatidic acid (LPA) is acylated to phosphatidic acid (PA) by the enzymes 1-acyl-sn-glycerol-3-phosphate acyltransferases (AGPAT1 through 11), and lysophosphatidylcholine acyltransferase (LPCAT1) (Aguado and Campbell 1998). See recent review by Agarwal (2012, in press). AGPAT1, 2, 3 and LPCAT1 have been characterized biochemically (AGPAT1, 2: Yamashita et al. 2007, West et al. 1997, Aguado and Campbell 1998, Gale et al. 2006; AGPAT3: Agarwal et al. 2006; LPCAT1: Nakanishi et al. 2006, Chen et al. 2006). Two additional proteins, AGPAT4 and AGPAT5, are inferred to have such activity based on studies of homologous mouse enzymes (Lu et al. 2005). These enzymes differ in their tissue specific patterns of expression in the body and in their preferences for specific acyl CoA molecules (Shindou and Shimizu 2009; Takeuchi and Reue 2009).
Lipin proteins LPIN1, 2, and 3, associated with the endoplasmic reticulum membrane, can each catalyze the hydrolysis of phosphatidate to yield 1,2-diacyl-glycerol and orthophosphate. The activities of LPIN1 and LPIN2 have been established experimentally (Grimsey et al. 2008); that of LPIN3 is inferred from its structural similarities both to its human paralogues and to its mouse ortholog (Donkor et al. 2007). Only LPIN1 has been shown to be stably associated with the endoplasmic reticulum, but all three enzymes appear to be catalytically active at that location (Grimsey et al. 2008; Donkor et al. 2007).
Membrane-associated acyl-CoA synthetase long-chain family member 1 (ACSL1) catalyzes the reaction of palmitate, CoASH, and ATP to form palmitoyl-CoA, AMP, pyrophosphate, and water. Human ACSL1 has not been characterized in detail, but available data suggest that it is associated specifically with the membrane of the endoplasmic reticulum and that it can act on oleic acid as well as on palmitic acid (Malhotra et al. 1999).
Membrane-associated acyl-CoA synthetase long-chain family member 3 (ACSL3) catalyzes the reaction of palmitate, CoASH, and ATP to form palmitoyl-CoA, AMP, pyrophosphate, and water. The enzyme is probably associated specifically with the endoplasmic reticulum membrane, and can also associate with lipid droplets. It is active on oleic acid as well as on palmitic acid (Fujimoto ea 2007).
Association of cytosolic FAS into multimers is linked to increased catalytic activity (Locke et al. 2008).
Cytosolic fatty acid synthase (FAS) complex catalyzes the reaction of acetyl-CoA with 7 malonyl-CoA and 14 NADHP + 14 H+ to form a molecule of palmitate and 7 CO2, 14 NADP+, 8 CoASH, and 6 H2O. The process proceeds via the successive condensations of malonyl groups onto the growing acyl chain,each followed by loss of CO2 and three steps of reduction (Smith et al. 2003).
Acyl-CoA synthetase long-chain family member 6 (ACSL6) associated with the plasma membrane catalyzes the reaction of palmitate, CoASH, and ATP to form palmitoyl-CoA, AMP, pyrophosphate, and water. In the body, ACSL6 is found in red blood cells. It is active on oleic acid as well as palmitic acid (Malhotra et al. 1999).
Elongation of very long chain fatty acids protein 3 (ELOVL3) catalyzes the reaction of palmitoyl-CoA and malonyl-CoA to form 3-oxooctadecanoyl-CoA (3-oxostearoyl-CoA), CO2, and CoASH. Indirect data from studies of transfected cells expressing ELOVL3 are consistent with its localization to the endoplasmic reticulum and activity on palmitoyl-CoA (Kobayashi et al. 2007).
Acyl-CoA synthetase long-chain family member 4 (ACSL4) associated with the endoplasmic reticulum membrane catalyzes the reaction of arachidonate, CoASH, and ATP to form arachidonyl-CoA, AMP, pyrophosphate, and water (Longo et al. 2003; Meloni et al. 2003).
Acyl-CoA synthetase long-chain family member 5 (ACSL5) associated with the endoplasmic reticulum membrane catalyzes the reaction of palmitate, CoASH, and ATP to form palmitoyl-CoA, AMP, pyrophosphate, and water (Gassler et al. 2007).
Elongation of very long chain fatty acids protein 6 (ELOVL6) catalyzes the reaction of palmitoyl-CoA and malonyl-CoA to form 3-oxooctadecanoyl-CoA (3-oxostearoyl-CoA), CO2, and CoASH (Shimamura et al. 2009). The localization of ELOVL6 to the endoplasmic reticulum membrane is inferred from that experimentally determined for the homologous mouse protein (Moon et al. 2001; Matsuzaka et al. 2002).
Expression, purification, and kinetic characterization of recombinant human adenylosuccinate lyase
The complete beta-oxidation spiral produces and consumes intermediates with a trans configuration. Mitochondrial beta-oxidation of unsaturated fatty acids leads to intermediates not compatible with the four enzymatic steps responsible for the beta-oxidation of saturated fatty acids. Unsaturated fatty acids that have bonds in the cis configuration require three separate enzymatic steps to prepare these molecules for the beta-oxidation pathway. The further processing of these intermediates requires additional enzymes, depending on the position of the double bonds in the original fatty acids. Described here is the beta-oxidation of linoleoyl-CoA.
Propionyl CoA carboxylase in the mitochondrial matrix catalyzes the reaction of propionyl-CoA, CO2, and ATP to form D-methylmalonyl-CoA, ADP, and orthophosphate. The active form of the enzyme is a heteromultimer, probably consisting of six alpha subunits each bound to a biotin molecule and six beta subunits (Kaziro et al. 1961; Kalousek et al. 1980; Fenton et al. 2001). Both alpha and beta subunits are posttranslationally modified to remove amino-terminal mitochondrial import sequences (Stadler et al. 2005).
At the beginning of this reaction, 1 molecule of 'D-methylmalonyl-CoA' is present. At the end of this reaction, 1 molecule of 'L-methylmalonyl-CoA' is present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'methylmalonyl-CoA epimerase activity' of 'methylmalonyl-CoA epimerase'.
Propionyl-CoA is a product of the catabolism of the amino acids, leucine, methionine, and threonine, and of the beta-oxidation of fatty acids with odd numbers of carbon atoms. The three reactions of this pathway convert propionyl-CoA to succinyl-CoA, an intermediate of the citric acid cycle. Through these reactions, carbon atoms from these sources can be fully oxidized to produce energy, or can be directed to gluconeogenesis. The three reactions of propionyl-CoA catabolism take place in the mitochondrial matrix.
Beta-oxidation begins once fatty acids have been imported into the mitochondrial matrix by carnitine acyltransferases. The beta-oxidation spiral of fatty acids metabolism involves the repetitive removal of two carbon units from the fatty acyl chain. There are four steps to this process: oxidation, hydration, a second oxidation, and finally thiolysis. The last step releases the two-carbon acetyl-CoA and a ready primed acyl-CoA that takes another turn down the spiral. In total each turn of the beta-oxidation spiral produces one NADH, one FADH2, and one acetyl-CoA. Further oxidation of acetyl-CoA via the tricarboxylic acid cycle generates additional FADH2 and NADH. All reduced cofactors are used by the mitochondrial electron transport chain to form ATP. The complete oxidation of a fatty acid molecule produces numerous ATP molecules. Palmitate, used as the model here, produces 129 ATPs. Beta-oxidation pathways differ for saturated and unsaturated fatty acids. The beta-oxidation of saturated fatty acids requires four different enzymatic steps. Beta-oxidation produces and consumes intermediates with a trans configuration; unsaturated fatty acids that have bonds in the cis configuration require three separate enzymatic steps to prepare these molecules for the beta-oxidation pathway.
Acetyl-CoA acetyltransferase tetramer (ACAT1) in the mitochondrial matrix catalyzes the reversible reaction of two molecules of acetyl-CoA to form acetoacetyl-CoA and CoA (Middleton et al. 1986).
Once fatty acids have been imported into the mitochondrial matrix by the carnitine acyltransferases, the beta-oxidation spiral begins. Each turn of this spiral concludes with the repetitive removal of two carbon units from the fatty acyl chain. beta-oxidation of saturated fatty acids (fatty acids with even numbered carbon chains and no double bonds) involves four different enzymatic steps: oxidation, hydration, a second oxidation, and a concluding thiolysis step, resulting in the two-carbon acetyl-CoA and a newly CoA primed acyl-CoA for the next turn of the spiral.
The seventh and final pass through the beta-oxidation spiral picks up where the last left off with the saturated fatty acid butanoyl-CoA and at the third step produces acetoacetyl-CoA, which can be used to generate 2 acetyl-CoA molecules or can be turned toward the synthesis of ketone bodies pathway. Four enzymatic steps are required starting with SCAD CoA dehydrogenase (Short Chain) activity, followed by the enoyl-CoA hydratase activity of crotonase, the 3-hydroxyacyl-CoA dehydrogenase activity of the short chain 3-hydroxyacyl-CoA dehydrogenase (SCHAD). The final enzymatic step, creating two acetyl-CoA molecules requires a specific ketoacyl-CoA thiolase, Acetoacetyl-CoA thiolase.
The second of the two accessory enzymes, 2,4-dienoyl-CoA reductase catalyses an oxidation-reduction (redox) reaction to yield 3-trans-decenoyl-CoA.
4-cis-decenoyl-CoA transits through the first step of the saturated beta-oxidation spiral to yield 2-trans-4-cis-decadienoyl-CoA.
FAD-linked mitochondrial glycerol 3-phosphate dehydrogenase (GPD2, alias: mGPDH) and its NAD-linked cytosolic isoform (GPD1, alias:cGPDH) constitute glycerol phosphate shuttle. GPD2 catalyzes the unidirectional conversion of glycerol-3-phosphate (G-3-P) to dihydroxyacetone phosphate (DHAP) with concomitant reduction of the enzyme-bound FAD. Impaired activity of GPD2 has been suggested to be one of the primary causes of insulin secretory defects in beta-cells and thus it is a candidate gene for type 2 diabetes.
The HMGCR gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The levels of acetone in ketone bodies are much lower than those of acetoacetic acid and beta-hydroxybutyric acid. Acetone cannot be converted back to acetyl-CoA, and is excreted in urine, or breathed out through the lungs. Extrahepatic tissues utilize ketone bodies by converting the beta-hydroxybutyrate successively to acetoacetate, acetoacetatyl-CoA, finally to acetyl-CoA (Sass 2011).
Acetoacetate, beta-hydroxybutyrate, and acetone collectively are called ketone bodies. The first two are synthesized from acetyl-CoA, in the mitochondria of liver cells; acetone is formed by spontaneous decarboxylation of acetoacetate. Ketone body synthesis in liver is effectively irreversible because the enzyme that catalyzes the conversion of acetoacetate to acetoacetyl-CoA is not present in liver cells. Ketone bodies, unlike fatty acids and triglycerides, are water-soluble. They are exported from the liver, and are taken up by other tissues, notably brain and skeletal and cardiac muscle. There, they are broken down to acetyl-CoA which is oxidized via the TCA cycle to yield energy. In a normal person, this pathway of ketone body synthesis and utilization is most active during extended periods of fasting. Under these conditions, mobilization and breakdown of stored fatty acids generates abundant acetyl-CoA acetyl-CoA in liver cells for synthesis of ketone bodies, and their utilization in other tissues minimizes the demand of these tissues for glucose (Sass 2011).
The ABCA1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Hydroxymethylglutaryl-CoA synthase tetramer (HMGCS2) in the mitochondrial matrix catalyzes the reaction of acetoacetyl-CoA and acetyl-CoA to form beta-hydroxy-beta-methylglutaryl coenzyme A (HMG CoA) and CoA (Aledo et al. 2001).
Acetyl-CoA acetyltransferase tetramer (ACAT1) in the mitochondrial matrix catalyzes the reversible reaction of acetoacetyl-CoA and CoA to form two molecules of acetyl-CoA (Middleton et al. 1986).
3-Oxoacid CoA-transferase dimer (OXCT1) in the mitochondrial matrix catalyzes the reversible reaction of acetoacetate and succinyl-CoA to form acetoacetyl-CoA and succinate (Kassovska-Bratinova et al. 1996).
In a healthy, well-nourished individual, the production of ketone bodies occurs at a relatively low rate. During periods of normal physiological responses to carbohydrate shortages, the liver increases the production of ketone bodies from acetyl-CoA generated from fatty acid oxidation. This allows heart and skeletal muscle to use ketone bodies as the primary source of energy, thereby preserving the limited glucose supply for use in brain tissue. In untreated diabetes mellitus, a huge buildup of ketone bodies occurs due to an increase in fatty acid oxidation. The production of ketone bodies exceeds the ability of peripheral tissues to oxidize them, and results in lowering the pH of blood. Blood acidification is dangerous, chiefly as it impairs the ability of hemoglobin to bind oxygen. Ketone body synthesis proceeds via the synthesis of ccetoacetic acid in three steps from acetyl CoA, followed by the reduction of acetoacetic acid to beta-hydroxybutyrate. In the body, these reactions occur in the mitochondria of liver cells (Sass 2011).
Hydroxymethylglutaryl-CoA lyase dimer (HMGCL) in the mitochondrial matrix catalyzes the reaction of beta-hydroxy-beta-methylglutaryl coenzyme A (HMG CoA) to form acetyl-CoA and acetoacetate (Mitchell et al. 1993).
Cloning and characterization of a novel class II phosphoinositide 3-kinase containing C2 domain
The CPT2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The CYP1A1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The FADS1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The FATP1 (SLC27A1) gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm)
The ACSL1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The ACOX1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The CPT1A gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The Platelet glycoprotein IV gene (CD36, PAS IV, GPIV) is transcribed to yield mRNA and the mRNA is translated to yield proteind.
The ACADM gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The ABCB4 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Evidence for a new biosynthetic pathway of sphingomyelin in SV 40 transformed mouse cells
The TIAM2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The RGL1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The SULT2A1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The PPARA gene is transcribed to yield mRNA and the mRNA is translated to yield protein. As inferred from mouse, BMAL1:CLOCK (ARNTL:CLOCK) heterodimers bind the scond intron of the PPARA gene and activate transcription of PPARA.
The ME1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The HMGCS2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The HMGCS1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The GRHL1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The GLIPR1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The FHL2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The role of EF-hand domains and C2 domain in regulation of enzymatic activity of phospholipase Czeta
Immunolocalization of the mercurial-insensitive water channel and glycerol intrinsic protein in epithelial cell plasma membranes
Biosynthesis of A2E, implicated in retinal degradation
At the beginning of this reaction, 1 molecule of 'NAD+', and 1 molecule of '(S)-3-Hydroxybutanoyl-CoA' are present. At the end of this reaction, 1 molecule of 'acetoacetyl-CoA', 1 molecule of 'H+', and 1 molecule of 'NADH' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the '3-hydroxyacyl-CoA dehydrogenase activity' of 'short chain 3-hydroxyacyl-CoA dehydrogenase homodimer'.
At the beginning of this reaction, 1 molecule of 'Crotonoyl-CoA', and 1 molecule of 'H2O' are present. At the end of this reaction, 1 molecule of '(S)-3-Hydroxybutanoyl-CoA' is present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'enoyl-CoA hydratase activity' of 'enoyl-CoA hydratase hexamer'.
The sixth pass through the beta-oxidation spiral picks up where the last left off with the saturated fatty acid hexanoyl-CoA and produces butanoyl-CoA. Four enzymatic steps are required starting with SCAD CoA dehydrogenase (Short Chain) activity, followed by the enoyl-CoA hydratase activity of crotonase, the 3-hydroxyacyl-CoA dehydrogenase activity of the short chain 3-hydroxyacyl-CoA dehydrogenase (SCHAD), and completed by the ketoacyl-CoA thiolase activity, present in the mitochondrial membrane associated trifunctional protein.
At the beginning of this reaction, 1 molecule of '3-Oxohexanoyl-CoA', and 1 molecule of 'CoA' are present. At the end of this reaction, 1 molecule of 'Acetyl-CoA', and 1 molecule of 'Butanoyl-CoA' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'transferase activity' of 'Trifunctional Protein'.
At the beginning of this reaction, 1 molecule of 'NAD+', and 1 molecule of '(S)-Hydroxyhexanoyl-CoA' are present. At the end of this reaction, 1 molecule of '3-Oxohexanoyl-CoA', 1 molecule of 'H+', and 1 molecule of 'NADH' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the '3-hydroxyacyl-CoA dehydrogenase activity' of 'short chain 3-hydroxyacyl-CoA dehydrogenase homodimer'.
At the beginning of this reaction, 1 molecule of 'trans-Hex-2-enoyl-CoA', and 1 molecule of 'H2O' are present. At the end of this reaction, 1 molecule of '(S)-Hydroxyhexanoyl-CoA' is present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'enoyl-CoA hydratase activity' of 'enoyl-CoA hydratase hexamer'.
The fifth pass through the beta-oxidation spiral picks up where the last left off with the saturated fatty acid octanoyl-CoA and produces hexanoyl-CoA. Four enzymatic steps are required starting with MCAD CoA dehydrogenase (Medium Chain) activity, followed by the enoyl-CoA hydratase activity of crotonase, the 3-hydroxyacyl-CoA dehydrogenase activity of the short chain 3-hydroxyacyl-CoA dehydrogenase (SCHAD), and completed by the ketoacyl-CoA thiolase activity, present in the mitochondrial membrane associated trifunctional protein.
At the beginning of this reaction, 1 molecule of 'NAD+', and 1 molecule of '(S)-Hydroxyoctanoyl-CoA' are present. At the end of this reaction, 1 molecule of '3-Oxooctanoyl-CoA', 1 molecule of 'H+', and 1 molecule of 'NADH' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the '3-hydroxyacyl-CoA dehydrogenase activity' of 'short chain 3-hydroxyacyl-CoA dehydrogenase homodimer'.
At the beginning of this reaction, 1 molecule of '3-Oxooctanoyl-CoA', and 1 molecule of 'CoA' are present. At the end of this reaction, 1 molecule of 'Hexanoyl-CoA', and 1 molecule of 'Acetyl-CoA' are present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'transferase activity' of 'Trifunctional Protein'.
At the beginning of this reaction, 1 molecule of 'H2O', and 1 molecule of 'trans-Oct-2-enoyl-CoA' are present. At the end of this reaction, 1 molecule of '(S)-Hydroxyoctanoyl-CoA' is present. This reaction takes place in the 'mitochondrial matrix' and is mediated by the 'enoyl-CoA hydratase activity' of 'enoyl-CoA hydratase hexamer'.
A novel molecular mechanism to explain biotin-unresponsive holocarboxylase synthetase deficiency
The CCT/TRiC chaperonin is required for maturation of sphingosine kinase 1
Laminin gamma3 chain binds to nidogen and is located in murine basement membranes
Tandem phosphorylation of serine 221 and 318 by PKC{delta} coordinates mRNA binding and nucleo-cytoplasmic shuttling of HuR
Fibroblast growth factor receptor-4 shows novel features in genomic structure, ligand binding and signal transduction
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Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans
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A second mammalian N-myristoyltransferase
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Defective TCN2 causes hereditary megaloblastic anemia
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Studies on the initiation and elongation reactions in the simian virus 40 DNA replication system.
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1,2-Diacyl-sn-glycerol 3-phospho-L-serine
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TCF: Lady Justice casting the final verdict on the outcome of Wnt signalling
Hypothetical UPF0123 protein BK223H9.2/MGC1346
Splicing factor 3B subunit 4 (Spliceosome associated protein 49) (SAP 49) (SF3b50) (Pre-mRNA splicing factor SF3b 49 kDa subunit)
Pre-mRNA splicing factor SF3b 49 kDa subunit
Pre-mRNA splicing factor SF3b 130 kDa subunit
Splicing factor 3B subunit 3 (Spliceosome associated protein 130) (SAP 130) (SF3b130) (Pre-mRNA splicing factor SF3b 130 kDa subunit)
High mobility group-like nuclear protein 2 homolog 1
U4/U6 small nuclear ribonucleoprotein Prp4
Hypothetical protein CGI-110 (Protein HSPC175)
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CD2 antigen cytoplasmic tail-binding protein 2
Splicing factor 3B subunit 1 (Spliceosome associated protein 155) (SAP 155) (SF3b155) (Pre-mRNA splicing factor SF3b 155 kDa subunit)
Pre-mRNA splicing factor SF3b 155 kDa subunit
Pre-mRNA splicing factor SF3b 145 kDa subunit
Splicing factor 3B subunit 2 (Spliceosome associated protein 145) (SAP 145) (SF3b150) (Pre-mRNA splicing factor SF3b 145 kDa subunit)
Heterogenous nuclear ribonucleoprotein U
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EGFR and FGFR signaling through FRS2 is subject to negative feedback control by ERK1/2
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Small nuclear ribonuclear protein D homolog
U5 small nuclear ribonucleoprotein 200 kDa helicase
116 kDa U5 small nuclear ribonucleoprotein component (U5 snRNP- specific protein, 116 kDa) (U5-116 kDa)
116 kDa U5 small nuclear ribonucleoprotein component
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Initiation of Nuclear Envelope Reformation
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Phenylalanyl-tRNA synthetase alpha chain
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International Union of Basic and Clinical Pharmacology. LXXVI. Current progress in the mammalian TRP ion channel family
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Nucleotide-sugar transporters: structure, function and roles in vivo
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Cytokines and chemokines in autoimmune disease: an overview
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Evolution of leptin structure and function
Mutations in the gene encoding fibroblast growth factor receptor-3 in achondroplasia
p15INK4B is a potential effector of TGF-beta-induced cell cycle arrest
Demonstration that mutation of the type II transforming growth factor beta receptor inactivates its tumor suppressor activity in replication error-positive colon carcinoma cells
Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis
Requirement of the MRN complex for ATM activation by DNA damage.
Molecular diversity of glutamate receptors and implications for brain function
Mutant fibroblast growth factor receptor 3 induces intracellular signaling and cellular transformation in a cell type- and mutation-specific manner
Synthesis of pyrophosphates in the cytosol
Activation of sphingosine kinase 1 by ERK1/2-mediated phosphorylation
Heterogeneous nuclear ribonucleoprotein F
CCAAT-binding transcription factor I subunit A
Nuclease sensitive element binding protein 1
Heterogeneous nuclear ribonucleoprotein A1
Heterogeneous nuclear ribonucleoprotein I
CHD8 is an ATP-dependent chromatin remodeling factor that regulates beta-catenin target genes
The role of calcium-independent phospholipase A2 in cardiolipin remodeling in the spontaneously hypertensive heart failure rat heart
Functions of site-specific histone acetylation and deacetylation
Diphosphoinositol polyphosphate phosphohydrolases, also known as nucleoside diphosphate-linked moiety X motif (NUDT) proteins, dephosphorylate inositol diphospho-pentakisphosphate (PP-IP5) to inositol 1,2,3,4,5,6-hexakisphosphate (IP6). The NUDT proteins involved are: nucleoside diphosphate-linked moiety X motif 3 (NUDT3), 4 (NUDT4), 10 (NUDT10), and 11 (NUDT11). The reactants consumed are: inositol 1-diphospho-2,3,4,5,6-pentakisphosphate (1-PP-IP5) and 3-diphospho-1,2,4,5,6-pentakisphosphate (3-PP-IP5). The following lists the above proteins with their corresponding literature references: NUDT3 (Safrany et al. 1999, Safrany et al. 1998, Yang et al. 1999, Caffrey et al. 2000), NUDT4 (Caffrey et al. 2000), NUDT10 (Leslie et al. 2002, Hidaka et al. 2002) and NUDT11 (Leslie et al. 2002, Hidaka et al. 2002).
Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1/2 (PPIP5K1) and 2 (PPIP5K2) phosphorylate inositol 1,2,3,4,5,6-hexakisphosphate (IP6) to inositol 1-diphospho-2,3,4,5,6-pentakisphosphate (1-PP-IP5)) (Fridy et al. 2007, Mulugu et al. 2007, Choi et al. 2007, Lin et al. 2009; Wang et al. 2011).
Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1/2 (PPIP5K1) and 2 (PPIP5K2) phosphorylate inositol 5-diphospho-1,2,3,4,6-pentakisphosphate (5-PP-IP5) to inositol 1,5-bisdiphospho-2,3,4,6-tetrakisphosphate (1,5-(PP)2-IP4) (Fridy et al. 2007, Mulugu et al. 2007, Choi et al. 2007, Lin et al. 2009).
Inositol hexakisphosphate kinase 1 (IP6K1) and 3 (IP6K3) phosphorylate inositol 5-diphospho-1,2,3,4,6-pentakisphosphate (5-PP-IP5) to inositol 5-triphospho- 1,2,3,4,6-pentakisphosphate (5-PPP-IP5). The following lists the above proteins with their corresponding literature references: IP6K1 (Saiardi et al. 2001, Draskovic et al. 2008) and IP6K3 (Saiardi et al. 2001, Draskovic et al. 2008).
Diphosphoinositol polyphosphate phosphohydrolases (DIPP), also known as nucleoside diphosphate-linked moiety X motif (NUDT) proteins, dephosphorylate inositol 5-diphospho-1,2,3,4,6-pentakisphosphate (5-PP-IP5) to inositol 1,2,3,4,5,6-hexakisphosphate (IP6). The NUDT proteins involved are: nucleoside diphosphate-linked moiety X motif 3 (NUDT3), 4 (NUDT4), 10 (NUDT10), and 11 (NUDT11). The following lists the above proteins with their corresponding literature references: NUDT3 (Safrany et al. 1999, Safrany et al. 1998, Yang et al. 1999, Caffrey et al. 2000), NUDT4 (Caffrey et al. 2000), NUDT10 (Leslie et al. 2002, Hidaka et al. 2002) and NUDT11 (Leslie et al. 2002, Hidaka et al. 2002).
A group of inositol phosphatases dephosphorylate inositol 1,4,5-trisphosphate (I(1,4,5)P3) to inositol 1,4-bisphosphate (I(1,4)P2). The group of inositol phosphatases involved are: inositol polyphosphate 5-phosphatase OCRL-1 (OCRL), phosphatidylinositol 4,5-bisphosphate 5-phosphatase A (INPP5J), and synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1 (SYNJ1). The following lists the above proteins with their corresponding literature references: OCRL (Zhang et al. 1995, Zhang et al. 1998, Schmid et al. 2004); INPP5J (Mochizuki & Thompson 1999); SYNJ1 (Schmid et al. 2004).
Diphosphoinositol polyphosphate phosphohydrolases (DIPP), also known as nucleoside diphosphate-linked moiety X motif (NUDT) proteins, dephosphorylate inositol bisdiphospho-tetrakisphosphate ((PP)2-IP4) to inositol 5-diphospho-1,2,3,4,6-pentakisphosphate (5-PP-IP5). The NUDT proteins involved are: nucleoside diphosphate-linked moiety X motif 3 (NUDT3), 4 (NUDT4), 10 (NUDT10), and 11 (NUDT11). The reactants consumed are: inositol 1,5-bisdiphospho-2,3,4,6-tetrakisphosphate (1,5-(PP)2-IP4) and inositol 3,5-bisdiphospho-1,2,4,6-tetrakisphosphate (3,5-(PP)2-IP4). The following lists the above proteins with their corresponding literature references: NUDT3 (Safrany et al. 1999, Safrany et al. 1998, Yang et al. 1999, Caffrey et al. 2000), NUDT4 (Caffrey et al. 2000), NUDT10 (Leslie et al. 2002, Hidaka et al. 2002) and NUDT11 (Leslie et al. 2002, Hidaka et al. 2002).
Inositol hexakisphosphate kinase 1 (IP6K1) and 3 (IP6K3) phosphorylate 1-diphospho-2,3,4,5,6-pentakisphosphate (1-PP-IP5) to form inositol 1,5-bisdiphospho-2,3,4,6-tetrakisphosphate (1,5-(PP)2-IP4) (Saiardi et al. 2001, Mulugu et al. 2007).
Diphosphoinositol polyphosphate phosphohydrolases (DIPP), also known as nucleoside diphosphate-linked moiety X motif (NUDT) proteins, dephosphorylate inositol bisdiphospho-tetrakisphosphate ((PP)2-IP4) to inositol diphospho-pentakisphosphate (PP-IP5). The NUDT proteins involved are: nucleoside diphosphate-linked moiety X motif 3 (NUDT3), 4 (NUDT4), 10 (NUDT10), and 11 (NUDT11). The reactants consumed are: inositol 1,5-bisdiphospho-2,3,4,6-tetrakisphosphate (1,5-(PP)2-IP4) and inositol 3,5-bisdiphospho-1,2,4,6-tetrakisphosphate (3,5-(PP)2-IP4). The products made are: inositol 1-diphospho-2,3,4,5,6-pentakisphosphate (1-PP-IP5) and 3-diphospho-1,2,4,5,6-pentakisphosphate (3-PP-IP5). The following lists the above proteins with their corresponding literature references: NUDT3 (Safrany et al. 1999, Safrany et al. 1998, Yang et al. 1999, Caffrey et al. 2000), NUDT4 (Caffrey et al. 2000), NUDT10 (Leslie et al. 2002, Hidaka et al. 2002) and NUDT11 (Leslie et al. 2002, Hidaka et al. 2002).
Inositol phosphates such as IP4, IP5 and IP6 are converted to an even wider variety of IPs including the di- and triphospho inositol phosphates, also known as pyrophosphates (Irvine & Schell 2001, Alcazar-Romain & Wente 2008, York 2006, Monserrate and York 2010, Ho et al. 2002, Saiardi et al. 2001, Draskovic et al. 2008, Choi et al. 2007, Caffrey et al. 2000, Leslie et al. 2002).
Inositol-3-phosphate synthase 1 (ISYNA1) aka hIPS isomerises glucose 6-phosphate (Glc6P) to inositol 3-phosphate (I3P) (Ju et al. 2004).
Type I (INPP4A) and type II inositol-3,4-bisphosphate 4-phosphatase (INPP4B) dephosphorylate inositol 3,4-bisphosphate (I(3,4)P2) to inositol 3-phosphate (I3P) (Norris et al. 1995, Norris et al. 1997).
Type I (INPP4A) and type II inositol-3,4-bisphosphate 4-phosphatase (INPP4B) dephosphorylate inositol 1,3,4-trisphosphate (I(1,3,4)P3) to inositol 1,3-bisphosphate (I(1,3)P2) (Norris et al. 1995, Norris et al. 1997).
Inositol monophosphatase 1 (IMPA1) and 2 (IMPA2) homodimers dephosphorylate inositol 1-phosphate (I1P) to inositol (Ins). In vitro, IMPA1 and 2 differ in their pH optima and IMPA1 has a significantly greater activity on IP4 than does IMPA2 (McAllister et al. 1992, Ohnishi et al. 2007).
Inositol monophosphatase 1 (IMPA1) and 2 (IMPA2) homodimers dephosphorylate inositol 4-phosphate (I4P) to inositol (Ins). In vitro, IMPA1 and 2 differ in their pH optima and IMPA1 has a significantly greater activity on IP4 than does IMPA2 (Ohnishi et al. 2007).
Type I inositol-1,4,5-trisphosphate 5-phosphatase (INPP5A) and the Type II phosphatase (INPP5B) are isoprenylated to the plasma membrane and act as a lipid anchor. Here they dephosphorylate inositol 1,4,5-trisphosphate (I(1,4,5)P3) to inositol 1,4-bisphosphate I(1,4)P2. ). The following lists the above proteins with their corresponding literature references: INPP5A (Laxminarayan et al. 1994); INPP5B (Jefferson & Majerus 1995, Ross et al. 1991, Schmid et al. 2004).
Inositol phosphates (IPs) are molecules involves in signalling processes in eukaryotes. myo-Inositol consists of a six-carbon cyclic alcohol with an axial 2-hydroxy and five equatorial hydroxyls. Mono-, di-, and triphosphorylation of the inositol ring generates a wide variety of stereochemically distinct signalling entities. Inositol 1,4,5-trisphosphate (I(1,4,5)P3), is formed when the phosphoinositide phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) is hydrolysed by a phospholipase C isozyme. An array of inositol trisphosphate (IP3) and tetrakisphosphate (IP4) molecules are synthesised by the action of various kinases and phosphatases in the cytosol. These species then transport between the cytosol and the nucleus where they are acted on by inositol polyphosphate multikinase (IPMK), inositol-pentakisphosphate 2-kinase (IPPK), inositol hexakisphosphate kinase 1 (IP6K1) and 2 (IP6K2), to produce IP5, IP6, IP7, and IP8 molecules. Some of these nuclear produced IPs transport back to the cytosol where they are converted to an even wider variety of IPs, by kinases and phosphatases, including the di- and triphospho inositol phosphates aka pyrophosphates (Irvine & Schell 2001, Bunney & Katan 2010, Alcazar-Romain & Wente 2008, York 2006, Monserrate and York 2010).
CEL (bile salt-dependent lipase) catalyzes the hydrolysis of extracellular cholesterol esters to yield cholesterol and a long-chain fatty acid. This reaction, in the lumen of the small intestine, is part of the process of digestion of dietary fats. While alternative splicing gives rise to two CEL isoforms, only the longer one encodes all of the residues that form the active site of the enzyme (Reue et al. 1991). In vitro, monomeric CEL protein is active even in the absence of bile salts. Its activity is greatly increased when it is complexed with two molecules of cholate, chenodeoxycholate, or their glycine or taurine conjugates (Lombardo and Guy 1980), and the predominant form of the enzyme active on lipid micelles in the gut is a dimer of two such complexes (Aubert-Jousset et al. 2004). CEL is synthesized in pancreatic acinar cells and released into the small intestine. It is also synthesized in the mammary gland and is a constituent of breast milk. The milk CEL is thought to play a role in digestion of milk fat in newborn infants, whose own pancreatic synthesis of the enzyme is low (Lombardo 2001; Bernback et al. 1990).
Inositol monophosphatase 1 (IMPA1) and 2 (IMPA2) homodimers dephosphorylate inositol 3-phosphate (I3P) to inositol (Ins). In vitro, IMPA1 and 2 differ in their pH optima and IMPA1 has a significantly greater activity on IP4 than does IMPA2 (Ohnishi et al. 2007).
Inositol phosphates IP2, IP and the six-carbon cyclic alcohol inositol (Ins) are produced by various phosphatases and the inositol-3-phosphate synthase 1 (ISYNA1) (Ju et al. 2004, Ohnishi et al. 2007, Irvine & Schell 2001, Bunney & Katan 2010).
A recurrent mutation in the tyrosine kinase domain of fibroblast growth factor receptor 3 causes hypochondroplasia
Activation of the phototransduction cascade
In the nucleus, inositol hexakisphosphate kinase 1 (IP6K1) and 2 (IP6K2) phosphorylate 1-diphospho-2,3,4,5,6-pentakisphosphate (1-PP-IP5) to make inositol 1,5-bisdiphospho-2,3,4,6-tetrakisphosphate (1,5-(PP)2-IP4) (Saiardi et al. 2001, Mulugu et al. 2007).
In the nucleus, inositol hexakisphosphate kinase 1 (IP6K1) and 2 (IP6K2) phosphorylate inositol 5-diphospho-1,2,3,4,6-pentakisphosphate (5-PP-IP5) to inositol 5-triphospho- 1,2,3,4,6-pentakisphosphate (5-PPP-IP5) (Saiardi et al. 2001, Draskovic et al. 2008) and IP6K2 (Saiardi et al. 2001, Draskovic et al. 2008). While this reaction has been demonstrated to occur in vitro, the extent to which it occurs in vivo is less clear.
In the nucleus, inositol hexakisphosphate kinase 1 (IP6K1) and 2 (IP6K2) phosphorylate inositol 1,2,3,4,5,6-hexakisphosphate (IP6) to inositol 5-diphospho-1,2,3,4,6-pentakisphosphate (5-PP-IP5). The following lists the above proteins with their corresponding literature references: IP6K1 (Saiardi et al. 2001, Mulugu et al. 2007, Draskovic et al. 2008) and IP6K2 (Saiardi et al. 2001, Mulugu et al. 2007, Draskovic et al. 2008).
In the nucleus, inositol hexakisphosphate kinase 1 (IP6K1) and 2 (IP6K2) phosphorylate5-diphospho-1,3,4,6-tetrakisphosphate (5-PP-IP4) to inositol 1,5-bisdiphospho-3,4,6-trisphosphate (1,5-(PP)2-IP3) (Saiardi et al. 2001, Saiardi et al. 2000, Draskovic et al. 2008).
Inositol hexakisphosphate kinase 1 (IP6K1) and 3 (IP6K3) phosphorylate inositol 1,3,4,5,6-pentakisphosphate (I(1,3,4,5,6)P5) to inositol 5-diphospho-(1,3,4,6)-tetrakisphosphate (5-PP-IP4) (Saiardi et al. 2001, Saiardi et al. 2000, Draskovic et al. 2008).
Diphosphoinositol polyphosphate phosphohydrolase 2, also known as nucleoside diphosphate-linked moiety X motif 4 (NUDT4), dephosphorylates diphospho- tetrakisphosphate (PP-IP4) to inositol 1,3,4,5,6-pentakisphosphate (I(1,3,4,5,6)P5). The products made are: inositol 5-diphospho-1,3,4,6-tetrakisphosphate (5-PP-IP4); inositol 1-diphospho-3,4,5,6-tetrakisphosphate (1-PP-IP4); and inositol 3-diphospho-1,4,5,6-tetrakisphosphate (3-PP-IP4). The following lists the above protein with its corresponding literature references: NUDT4 (Saiardi et al. 2001, Saiardi et al. 2000).
Within the nucleus, inositol polyphosphate multikinase (IPMK), inositol-pentakisphosphate 2-kinase (IPPK), inositol hexakisphosphate kinase 1 (IP6K1) and 2 (IP6K2) produce IP5, IP6, IP7, and IP8 inositol phosphate molecules (Irvine & Schell 2001, Alcazar-Romain & Wente 2008, York 2006, Monserrate and York 2010, Nalaskowski et al. 2002, Chang et al. 2002, Chang & Majerus 2006, Saiardi et al. 2001, Saiardi et al. 2000, Draskovic et al. 2008, Mulugu et al. 2007).
The class II phosphoinositide 3-kinase PI3K-C2alpha is concentrated in the trans-Golgi network and present in clathrin-coated vesicles
Inositolpentakisphosphate 2-kinase (IPPK), also known as IP52K, phosphorylates inositol 1,3,4,5,6-pentakisphosphate (I(1,3,4,5,6)P5) to inositol 1,2,3,4,5,6-hexakisphosphate (IP6) (Verbski et al. 2002, Brehm et al. 2007, Choi et al. 2007).
Inositol hexakisphosphate kinase 1 (IP6K1) and 3 (IP6K3) phosphorylate inositol 1-diphospho-3,4,5,6-tetrakisphosphate (1-PP-IP4) to form inositol 1,5-bisdiphospho-3,4,6-trisphosphate (1,5-(PP)2-IP3) (Saiardi et al. 2001, Saiardi et al. 2000, Draskovic et al. 2008).
Inositol hexakisphosphate kinase 1 (IP6K1) and 3 (IP6K3) phosphorylate inositol 1,2,3,4,5,6-hexakisphosphate (IP6) to inositol 5-diphospho-1,2,3,4,6-pentakisphosphate (5-PP-IP5). The following lists the above proteins with their corresponding literature references: IP6K1 (Saiardi et al. 2001, Mulugu et al. 2007, Draskovic et al. 2008; Lin et al. 2009) and IP6K3 (Saiardi et al. 2001, Draskovic et al. 2008).
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The cystic fibrosis transmembrane conductance regulator interacts with and regulates the activity of the HCO3- salvage transporter human Na+-HCO3- cotransport isoform 3
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Purification and functional characterization of aquaporin-8
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Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation
Splicing factor, arginine/serine-rich 5 (Pre-mRNA splicing factor SRP40) (Delayed-early protein HRS)
Splicing factor, arginine/serine-rich 1 (pre-mRNA splicing factor SF2, P33 subunit) (Alternative splicing factor ASF-1)
pre-mRNA splicing factor SF2, P33 subunit
Pre-mRNA splicing factor ATP-dependent RNA helicase PRP16 (ATP- dependent RNA helicase DDX38) (DEAH-box protein 38)
Pre-mRNA splicing factor ATP-dependent RNA helicase PRP16
Splicing factor, arginine/serine-rich 4 (Pre-mRNA splicing factor SRP75) (SRP001LB)
Pre-mRNA splicing factor PRP17 (hPRP17) (EH-binding protein 3) (Ehb3)
Direct phosphorylation of IkappaB by IKKalpha and IKKbeta: discrimination between free and NF-kappaB-bound substrate
Pre-mRNA cleavage complex II protein Clp1
Pre-mRNA cleavage complex II protein Pcf11
Cleavage and polyadenylation specificity factor, 100 kDa subunit
Cleavage and polyadenylation specificity factor, 160 kDa subunit
Cleavage and polyadenylation specificity factor, 73 kDa subunit
Cleavage stimulation factor, 50 kDa subunit
Cleavage stimulation factor, 64 kDa subunit
Polynucleotide adenylyltransferase alpha
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The molecular basis of Sanfilippo syndrome type B
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JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor
Splicing factor, arginine/serine-rich 9 (Pre-mRNA splicing factor SRp30C)
Splicing factor, arginine/serine-rich 6 (Pre-mRNA splicing factor SRP55)
Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases
The 5-HT3B subunit is a major determinant of serotonin-receptor function
Recapitulation of embryonic neuroendocrine differentiation in adult human pancreatic duct cells expressing neurogenin 3
ATP-dependent RNA helicase A (Nuclear DNA helicase II) (NDH II) (DEAD-box protein 9)
Heterogeneous nuclear ribonucleoprotein A3
E1B-AP5 nucleocytoplasmic transport protein
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U1 small nuclear ribonucleoprotein 70 kDa
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Transformation upregulated nuclear protein
Heterogeneous nuclear ribonucleoprotein K
Small nuclear ribonucleoprotein associated proteins B and B'
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FRS2 alpha attenuates FGF receptor signaling by Grb2-mediated recruitment of the ubiquitin ligase Cbl
DnaJ homolog subfamily C member 8 (Splicing protein spf31) (HSPC315)
Heterogeneous nuclear ribonucleoprotein R
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NF449 is a novel inhibitor of fibroblast growth factor receptor 3 (FGFR3) signaling active in chondrocytes and multiple myeloma cells
Molecular cloning, functional expression, and mRNA tissue distribution of the human 5-hydroxytryptamine2B receptor
A tetrasaccharide linker sequence is required for GAG synthesis
Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation
Target-derived matricryptins organize cerebellar synapse formation through ?3?1 integrins
EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer
mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI
mannose (a1-2) mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI
ditrans, polycis-polyprenol pyrophosphate
Xeroderma pigmentosum variant (XP-V) correcting protein from HeLa cells has a thymine dimer bypass DNA polymerase activity.
Speed, sensitivity, and stability of the light response in rod and cone photoreceptors: facts and models
HSFY genes and the P4 palindrome in the AZFb interval of the human Y chromosome are not required for spermatocyte maturation
Cobalamin (Cbl, vitamin B12) transport and metabolism
WNT ligand secretion is abrogated by the PORCN inhibitor LGK974
Plk1- and beta-TrCP-dependent degradation of Bora controls mitotic progression
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Toxic proteins released from mitochondria in cell death
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A defect in dolichol phosphate biosynthesis causes a new inherited disorder with death in early infancy
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Mutations in cohesin complex members SMC3 and SMC1A cause a mild variant of cornelia de Lange syndrome with predominant mental retardation
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Heterogeneous nuclear ribonucleoproteins A2/B1
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Heterogeneous nuclear ribonucleoprotein M
Heterogeneous nuclear ribonucleoprotein L
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7alpha,26-dihydroxy-5beta-cholestan-3-one [ChEBI:48778]
Heterogeneous nuclear ribonucleoprotein H
Heterogeneous nuclear ribonucleoprotein A0
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Lysine hydroxylation and crosslinking of collagen
The GABAA receptor beta 3 subunit gene: characterization of a human cDNA from chromosome 15q11q13 and mapping to a region of conserved synteny on mouse chromosome 7
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_108273.4
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The role of endocytic l1 trafficking in polarized adhesion and migration of nerve growth cones
Interaction of nephrin with adherens junction-associated proteins
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Heterodimerization of nephrin and NEPH2/NEPH3
p85 associates with both p-Nephrin and CD2AP
Cis-Heterodimerization of nephrin and NEPH1
MigFilin associates with Filamin and F-actin
Cloning of a human renal p-aminohippurate transporter, hROAT1
Mig-2 recruits Migfilin to the cell-ECM adhesions
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Gap junction turnover, intracellular trafficking, and phosphorylation of connexin43 in brefeldin A-treated rat mammary tumor cells
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NVP-BEZ235, a dual PI3K/mTOR inhibitor, prevents PI3K signaling and inhibits the growth of cancer cells with activating PI3K mutations
Succinyl CoA: 3-oxoacid CoA transferase (SCOT): human cDNA cloning, human chromosomal mapping to 5p13, and mutation detection in a SCOT-deficient patient
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2-Methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency is caused by mutations in the HADH2 gene.
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HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells
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A transcription factor regulatory circuit in differentiated pancreatic cells
Peroxisome proliferator-activated receptor alpha (PPARalpha ) turnover by the ubiquitin-proteasome system controls the ligand-induced expression level of its target genes
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Dihydropyrimidinase deficiency: structural organization, chromosomal localization, and mutation analysis of the human dihydropyrimidinase gene
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Mutations in the gene encoding peroxisomal sterol carrier protein X (SCPx) cause leukencephalopathy with dystonia and motor neuropathy
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The identification of a phospholipase B precursor in human neutrophils
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A syndrome with congenital neutropenia and mutations in G6PC3
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Mycobacterium tuberculosis activates the DNA-dependent cytosolic surveillance pathway within macrophages
Wnt signaling in oncogenesis and embryogenesis--a look outside the nucleus
Changes in histones H2A and H3 variant composition in differentiating and mature rat brain cortical neurons
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7alpha,12alpha,26-trihydroxy-5beta-cholestan-3-one [ChEBI:48834]
Analysis of Gas6 in human platelets and plasma
The PtdIns3P phosphatase myotubularin is a cytoplasmic protein that also localizes to Rac1-inducible plasma membrane ruffles
Beyond calcium: new signaling pathways for Tec family kinases
Recombinational DNA repair and human disease.
Cytosolic CTP synthase 2 (CTPS) catalyzes the reaction of UTP, glutamine, ATP and water to form CTP, glutamate, ADP, and orthophosphate (Han et al. 2005; van Kuilenberg et al. 2000). Unpublished X-ray crystallographic data suggest that the enzyme is a tetramer (PDB 3IHL). Both CTPS2 and a second human gene product, CPTS, have CTP synthase activity in various test systems; their relative contributions to CTP metabolism in the body is not clear.
Cytosolic ribonucleotide reductase catalyzes the reduction of adenine, guanine, cytidine, and uridine ribonucleoside 5'-diphosphates to form the corresponding deoxyribonucleoside 5'-diphosphates, coupled to the oxidation of glutaredoxin (Eklund et al. 2001). Ribonucleotide reductase is a tetramer of two large and two small subunits (Shao et al. 2004; Zhou et al. 2005). The overall activity of the enzyme is regulated allosterically: ATP binding is stimulatory while dATP binding is inhibitory (Reichard et al. 2000). The reducing equivalents needed for ribonucleotide reductase activity can be provided by either of two small proteins, glutaredoxin and thioredoxin (Holmgren 1989; Sun et al. 1998). Both are re-reduced with NADPH as the donor of reducing equivalents, and so are active in catalytic amounts. The relative contributions of glutaredoxin and thioredoxin in vivo are unknown.
Cytosolic ribonucleotide reductase catalyzes the reduction of adenine, guanine, cytidine, and uridine ribonucleoside 5'-diphosphates to form the corresponding deoxyribonucleoside 5'-diphosphates, coupled to the oxidation of thioredoxin (Holmgren 1989; Eklund et al. 2001). Ribonucleotide reductase is a tetramer of two large and two small subunits (Shao et al. 2004; Zhou et al. 2005). The overall activity of the enzyme is regulated allosterically: ATP binding is stimulatory while dATP binding is inhibitory (Reichard et al. 2000). The reducing equivalents needed for ribonucleotide reductase activity can be provided by either of two small proteins, glutaredoxin and thioredoxin (Holmgren 1989; Sun et al. 1998). Both are re-reduced with NADPH as the donor of reducing equivalents, and so are active in catalytic amounts. The relative contributions of glutaredoxin and thioredoxin in vivo are unknown.
Deoxyribonucleotides needed for DNA repair are synthesized de novo by the reduction of ribonucleoside 5'-diphosphates. This reaction is catalyzed by a nuclear form of ribonucleotide reductase active throughout the cell cycle. The reducing equivalents needed for these reactions can be provided directly by thioredoxin.
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Cytosolic nucleoside diphosphate kinases catalyze the reversible reaction of ribonucleoside and deoxyribonucleoside 5'-diphosphates with ATP to form the corresponding nucleoside 5'-triphosphates and ADP. These kinases are ubiquitously expressed enzymes with broad substrate specificities (Berg and Joklik 1954; Parks and Agarwal 1973). Three human cytosolic nucleoside diphosphate kinase proteins, NME1, 2, and 3, have been characterized biochemically (Gilles et al. 1991; Schaertl et al. 1998; Erent et al. 2001; Chen et al. 2003). All are catalytically active as hexamers: homohexamers of NME1, 2, and 3 have been described, as have heterohexamers containing all possible combinations of NME1 and 2 (Gilles et al. 1991; Erent et al. 2001). While cytosolic nucleoside diphosphate kinases can efficiently use several nucleotide triphosphates as a phosphate donor, the high concentrations of ATP relative to other nucleoside triphosphates in vivo makes it the likely major phosphate donor in these reactions and only reactions with ATP as the phosphate donor are annotated. All of these phosphorylation reactions are freely reversible in vitro (Parks and Agarwal 1973; Schaertl et al. 1998), but the high ratio of ATP to ADP concentrations in the cytosol should favor the conversion of (d)NDP and ATP to (d)NTP and ADP.
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In this reaction, 1 molecule of 'Thioredoxin' is translocated from cytosol to nucleoplasm. This movement of the molecule occurs through the 'nuclear pore'.
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Cytosolic glutathione reductase catalyzes the reaction of glutathione (oxidized) and NADPH + H+ to form two molecules of glutathione (reduced) and NADP+ (Scott et al. 1963, Loos et al. 1976). Deficiency of glutathione reductase can cause hemolytic anemia.
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Cytosolic glutaredoxin (oxidized) and glutathione (reduced) react to form glutaredoxin (reduced) and glutathione (oxidized) (Padilla et al. 1995).
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Cytosolic thioredoxin reductase catalyzes the reaction of thioredoxin, oxidized and NADPH + H+ to form thioredoxin, reduced and NADP+ (Urig et al. 2006).
In this reaction, 1 molecule of 'thioredoxin, oxidized' is translocated from nucleoplasm to cytosol. This movement of the molecule occurs through the 'nuclear pore'.
Human SGBS cells - a unique tool for studies of human fat cell biology
Mitochondrial adenylate kinase 2 (AK2) catalyzes the reaction of AMP and ATP to form two molecules of ADP (Hamade et al. 1982). Localization of AK2 specifically to the mitochondrial intermembrane space is inferred from studies of the homologous rat enzyme (Criss 1970).
Mitochondrial adenylate kinase 2 (AK2) catalyzes the reaction of two molecules of ADP to form AMP and ATP (Hamade et al. 1982). Localization of AK2 specifically to the mitochondrial intermembrane space is inferred from studies of the homologous rat enzyme (Criss 1970).
Cytosolic adenylate kinase 1 (AK1) catalyzes the reversible reactions of ADP and dADP with ADP to form AMP and dAMP respectively, plus ATP (Tsuboi 1978; Matsuura et al. 1989).
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Cytosolic CTP synthase 1 (CTPS) catalyzes the reaction of UTP, glutamine, ATP and water to form CTP, glutamate, ADP, and orthophosphate (Han et al. 2005). The active form of the enzyme is a tetramer (Kursala et al. 2006). Both CTPS and a second human gene product, CPTS2, have CTP synthase activity in various test systems; their relative contributions to CTP metabolism in the body is not clear.
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Cytosolic deoxythymidylate kinase (DTYMK) catalyzes the reversible reaction of either dUDP or TDP with ADP to form dUMP or TMP. The active form of the enzyme is a homodimer (Lee and Cheng 1977).
Cytosolic deoxythymidylate kinase (DTYMK) catalyzes the reversible reaction of either dUMP or TMP with ATP to form dUDP or TDP. The active form of the enzyme is a homodimer (Lee and Cheng 1977).
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Cytosolic UMP-CMP kinase (CMPK1) catalyzes the reversible reaction of CDP, dCDP, or UDP and ADP to form CMP, dCMP, or UMP and ATP (Liou et al. 2002; Scott and Wright 1979).
Cytosolic UMP-CMP kinase (CMPK1) catalyzes the reversible reaction of CMP, dCMP, or UMP and ATP to form CDP, dCDP, or UDP and ADP (Liou et al. 2002; Scott and Wright 1979).
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Cytosolic guanylate kinase 1 (GUK1) catalyzes the reversible reactions of GDP and dGDP with ADP to form GMP and dGMP respectively and ATP. While native gel electrophoretic studies of whole cell extracts suggested the existence of multiple human enzymes with guanylate kinase activity (Jamil et al. 1975), only one has been purified and biochemically characterized (Agarwal et al. 1978; Brady et al. 1996). The enzyme is of clinical importance as it is a target of antitumor drugs and antiviral drugs such as acyclovir (Miller and Miller 1980).
Cytosolic guanylate kinase 1 (GUK1) catalyzes the reversible reactions of GMP and dGMP with ATP to form GDP and dGDP respectively and ADP. While native gel electrophoretic studies of whole cell extracts suggested the existence of multiple human enzymes with guanylate kinase activity (Jamil et al. 1975), only one has been purified and biochemically characterized (Agarwal et al. 1978; Brady et al. 1996). The enzyme is of clinical importance as it is a target of antitumor drugs and antiviral drugs such as acyclovir (Miller and Miller 1980).
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Mechanisms underlying differential responses to FGF signaling
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Cytosolic dihydropyrimidinase tetramer catalyzes the reaction of 5,6-dihydrouracil and water to form 3-ureidopropionate (Hamajima et al. 1998).
Cytosolic 3-ureidopropionase catalyzes the reaction of 3-ureidopropionate and water to form beta-alanine, CO2, and NH3 (van Kuilenberg et al. 2004).
Cytosolic dihydropyrimidine dehydrogenase catalyzes the reaction of thymine and NADPH + H+ to form 5,6-dihydrothymine and NADP+. The mechanism of the human reaction is inferred from that of the well-characterized pig enzyme (Yokota et al. 1994).
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Mitochondrial AGXT2 tetramer catalyzes the reaction of beta-alanine and pyruvate to form 3-oxopropanoate and alanine. While the human mitochondrial AGXT2 enzyme has been characterized experimentally in other respects (Rodionov et al. 2010), its ability to catalyze this transamination reaction is inferred from the properties of its rat homologue.
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Cytosolic UPB1 (beta-ureidopropionase) catalyzes the reaction of 3-ureidoisobutyrate and H2O to form (R)-3-aminoisobutyrate, CO2, and NH3 (Tamaki et al. 2000; van Kuilenburg et al. 2004).
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Cytosolic dihydropyrimidinase tetramer catalyzes the reaction of 5,6-dihydrothymine and water to yield 3-ureidoisobutyrate (Hamajima et al. 1998).
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In parallel sequences of three reactions each, thymine is converted to beta-aminoisobutyrate and uracil is converted to beta-alanine. Both of these molecules are excreted in human urine and appear to be normal end products of pyrimidine catabolism (Griffith 1986; Webster et al. 2001). Mitochondrial AGXT2, however, can also catalyze the transamination of both molecules with pyruvate, yielding 2-oxoacids that can be metabolized further by reactions of branched-chain amino acid and short-chain fatty acid catabolism (Tamaki et al. 2000). The importance of these reactions in normal human pyrimidine catabolism has not been well worked out.
Mitochondrial AGXT2 tetramer catalyzes the reaction of (R)-3-aminoisobutyric acid and pyruvate to form 2-methyl-3-oxopropanoate and alanine. While the human mitochondrial AGXT2 enzyme has been characterized experimentally in other respects (Rodionov et al. 2010), its ability to catalyze this transamination reaction is inferred from the properties of its rat homologue.
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Cytosolic adenylate kinase 1 (AK1) catalyzes the reversible reactions of AMP and dAMP with ATP to form ADP and dADP respectively, plus ADP (Tsuboi 1978; Matsuura et al. 1989).
The events of human pyrimidine metabolism are conveniently, if somewhat arbitrarily, grouped into four pathways: de novo synthesis of the pyrimidine ring and its conversion to uridine 5'-monophosphate (UMP), the biosynthesis of other pyrimidine ribo- and deoxyribonucleotides, pyrimidine salvage reactions, and pyrimidine catabolism (Loffler et al. 2005). De novo synthesis of the pyrimidine ring and its conversion to UMP. The pyrimidine base orotate is synthesized from glutamine, bicarbonate, and aspartate. Orotate reacts with 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) and is then decarboxylated to form the pyrimidine nucleotide UMP. Pyrimidine biosynthesis [interconversion]. Pyrimidine ribo- and deoxyribonucleotide di- and triphosphates are synthesized, both from UMP and from pyrimidine ribonucleotide monophosphates generated in salvage reactions. Pyrimidine salvage reactions. Pyrimidine nucleosides and free bases generated by DNA and RNA breakdown are converted to nucleotide monophosphates. Pyrimidine catabolism. The pyrimidine bases thymine and uracil are degraded to beta-aminoisobutyrate and beta-alanine, respectively, which are excreted from the body.
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Catecholamines: role in health and disease
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The pyrimidine orotate (orotic acid) is synthesized in a sequence of four reactions, deriving its atoms from glutamine, bicarbonate, and aspartate. A single multifunctional cytosolic enzyme catalyzes the first three of these reactions, while the last one is catalyzed by an enzyme associated with the inner mitochondrial membrane. In two further reactions, catalyzed by a bifunctional cytosolic enzyme, orotate reacts with 1-phosphoribosyl 5-pyrophosphate (PRPP) to yield orotidine 5'-monophosphate, which is decarboxylated to yield uridine 5'-monophosphate (UMP). While several individual reactions in this pathway are reversible, other irreversible reactions drive the pathway in the direction of UMP biosynthesis in the normal cell. All reactions are thus annotated here only in the forward direction. This pathway has been most extensively analyzed at the genetic and biochemical level in hamster cell lines. All three enzymes have also been purified from human sources, however, and the key features of these reactions have been confirmed from studies of this human material (Jones 1980; Webster et al. 2001). All other pyrimidines are synthesized from UMP. The reactions annotaed here, catalyzed by dCMP deaminase and dUTP diphosphatase yield dUMP, which in turn is converted to TMP by thymidylate synthase.
Cytosolic thymidine kinase 1 (TK1) catalyzes the reaction of thymidine and ATP to form TMP (thymidine 5'-monophosphate) and ADP. TK1 has been purified from human spleen and from cultured cells. The enzyme is active as a homotetramer, and phosphorylates thymidine and deoxyuridine using ATP as a phosphate donor in vitro (Sherley and Kelly 1988a; Munch-Petersen et al. 1991; Birringer et al. 2005). Divalent cations are required for enzyme activity (Mg++ is preferred) (Lee and Cheng 1986), and ATP stabilizes the tetrameric form of the enzyme (Munch-Petersen et al. 1993). In cells, enzyme activity is high during S phase of the cell cycle and low otherwise, correlated with intracellular levels of thymidine kinase 1 protein (Sherley and Kelly 1988b), and consistent with a requirement for TMP synthesis in normal cells only as part of DNA replication.
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Cytosolic uridine-cytidine kinase 2 (UCK2) catalyzes the reactions of cytidine or uridine with ATP to form CMP or UMP and ADP (Greenberg et al. 1977; Van Rompay et al. 2001). Crystallographic data show the enzyme to be a tetramer (Suzuki et al. 2004). When it is expressed as a fusion construct with green fluorescent protein, the protein localizes primarily to the cytosol of transfected CHO cells (Van Rompay et al. 2003).
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An interferon-induced protein with release factor activity is a tryptophanyl-tRNA synthetase
Cytosolic uridine-cytidine kinase 1 (UCK1) catalyzes the reactions of cytidine or uridine with ATP to form CMP or UMP and ADP (Greenberg et al. 1977; Van Rompay et al. 2001). Unpublished crystallographic data show the enzyme to be a tetramer (PDB - 2JEO).
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Cytosolic uridine phosphorylase (isoforms UPP1 and UPP2) catalyzes the reversible reactions of uracil with ribose 1-phosphate or deoxyribose 1-phosphate to yield uridine or deoxyuridine and orthophosphate (Watanabe and Uchida 1995; Johansson, 2003). The active form of UPP1 is a dimer (Rooslid et al. 2009).
Cytosolic uridine phosphorylase (isoforms UPP1 and UPP2) catalyzes the reversible reactions of uridine or deoxyuridine with orthophosphate to yield uracil and ribose 1-phosphate or deoxyribose 1-phosphate (Watanabe and Uchida 1995; Johansson, 2003). The active form of UPP1 is a dimer (Rooslid et al. 2009).
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Cytosolic 5'-nucleotidase 3 (NT5C3) catalyzes the hydrolysis of pyrimidine nucleoside monophosphates (d)CMP, TMP, and (d)UMP to nucleosides plus orthophosphate. While the enzyme appears to be present in many tissues, it is especially abundant in erythrocytes, where it may function to remove excess pyrimidine nucleotides generated by nucleic acid breakdown, while sparing purine nucleotides needed for red cell energy metabolism. Deficiencies in the enzyme are associated with a form of hemolytic anemia and its inactivation by heavy metals may be responsible for some hematological abnormalities associated with lead poisoning (Marinaki et al. 2001; Rees et al. 2003). The active form of the enzyme is a monomer. It has an absolute requirement for Mg++, and is inactive against purine nucleotides (Amici et al. 1997; Amici and Magni 2002).
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In pyrimidine salvage reactions, nucleosides and free bases generated by DNA and RNA breakdown are converted back to nucleotide monophosphates, allowing them to re-enter the pathways of pyrimidine biosynthesis (interconversion).
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Cytosolic cytidine deaminase catalyzes the hydrolysis of cytidine or dexoycytidine to form uridine or deoxyuridine and ammonia (Laliberte and Momparler 1994). The active form of the enzyme is a tetramer (Chung et al. 2005).
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Fc gamma receptor-mediated activation of phospholipase D regulates macrophage phagocytosis of IgG-opsonized particles
Cytosolic dihydropyrimidine dehydrogenase catalyzes the reaction of uracil and NADPH + H+ to form 5,6-dihydrouracil and NADP+. The mechanism of the human reaction is inferred from that of the well-characterized pig enzyme (Yokota et al. 1994).
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Deoxyuridine triphosphatase (DUT) catalyzes the hydrolysis of dUTP to form dUMP and pyrophosphate. Two isoforms of DUT are expressed, generated by alternative splicing. The major one, annotated here, is localized to the nucleoplasm (Ladner et al. 1996). The enzyme is a homotrimer (Mol et al. 1996). In the cell, this reaction depletes the supply of dUTP, preventing its incorporation into DNA, while generating dUMP, the immediate precursor of thymidine nucleotides.
Cytosolic thymidylate synthase catalyzes the reaction of dUMP and N5,N10-methylene tetrahydrofolate to form TMP and dihydrofolate (Davisson et al. 1989). The enzyme is a homodimer (Phan et al. 2001).
Dihydroorotate dehydrogenase catalyzes the oxidation of dihydroorotate to orotate (orotic acid). The enzyme is located in the inner mitochondrial membrane oriented so that cytosolic dihydroorotate molecules have access to it, and orotate is released into the cytosol. The reducing equivalents generated by the reaction are transferred by ubiquinone (Coenzyme Q) to the electron transport chain within the inner mitochondrial membrane. There is no evidence for the involvement of NAD+ as an acceptor of reducing equivalents in this reaction in mammalian cells (Jones 1980). In contrast, the reaction catalyzed by the enzyme isolated from the anaerobic bacterium Clostridium oroticum requires NAD+ as a cofactor but also proceeds strongly in the direction of dihydroorotate synthesis consistent with the greater electronegativity of NAD+ (Lieberman and Kornberg 1953). Early studies of purified rat liver enzyme by Forman and Kennedy suggested the presence of flavin mononucleotide and iron-sulfur complexes as cofactors. More recent work by Bader, Beuneu, and their colleagues with recombinant human protein expressed in insect cells has confirmed the presence of flavin mononucleotide, at a stoichiometry of one molecule per molecule of apoenzyme but suggests that iron-sulfur complexes, if indeed they are involved in the oxidation and electron transport process, are not an integral part of the dihydroorotate dehydrogenase holoenzyme.
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The synthesis of orotidine 5'-monophosphate (OMP) from orotate and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) is catalyzed by the orotate phosphoribosyltransferase activity of the bifunctional "uridine monophosphate synthetase (orotate phosphoribosyl transferase and orotidine 5'-decarboxylase)" protein. The reaction itself is freely reversible, but is pulled in the forward direction in vivo by the irreversible hydrolysis of pyrophosphate. While purified human protein has not been characterized in detail, the close similarity of the human gene to that encoding the well-studied hamster protein, and the demonstration that mutations in the human gene are associated with failure to convert orotate to UMP in vivo, provide convincing evidence that the human uridine monophosphate synthetase protein indeed catalyzes these two reactions (McClard et al. 1980; Suchi et al. 1997). The active form of the human protein is a dimer (Yablonski et al. 1996; Wittmann et al. 2008).
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The decarboxylation of orotidine 5'-monophosphate (OMP) to form uridine 5'-monophosphate (UMP) is catalyzed by the orotidine 5'-phosphate decarboxylase activity of the bifunctional "uridine monophosphate synthetase (orotate phosphoribosyl transferase and orotidine 5'-decarboxylase)" protein. While purified human protein has not been characterized in detail, the close similarity of the human gene to that encoding the well-studied hamster protein, and the demonstration that mutations in the human gene are associated with failure to convert orotate to UMP in vivo, provide convincing evidence that the human uridine monophosphate synthetase protein indeed catalyzes these two reactions (McClard et al. 1980; Suchi et al. 1997). The active form of the human protein is a dimer (Yablonski et al. 1996; Wittmann et al. 2008).
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Cytosolic deoxycytidylate deaminase (DCTD) catalyzes the hydrolysis of dCMP (2'-deoxyuridine 5'-monophosphate) to yield dUMP (2'-deoxyuridine 5'-monophosphate) and ammonia. The active enzyme is a homohexamer (Maley et al. 1993; Weiner et al. 1993; unpublished crystallography data - PDB 2W4L).
The events of human purine metabolism are conveniently, if somewhat arbitrarily, grouped into four pathways: de novo synthesis of inosine 5'-monophosphate (IMP), the biosynthesis of other purine ribo- and deoxyribonucleotides, purine salvage reactions, and purine catabolism (Watts 1974). De novo synthesis of inosine 5'-monophosphate (IMP). The purine ribonucleotide IMP is assembled on 5-phospho-alpha-D-ribose 1-diphosphate (PRPP). Purine biosynthesis [interconversion]. Purine ribo- and deoxyribonucleotide di- and triphosphates are synthesized, both from IMP and from guanosine and adenosine ribo- and deoxyribonucleotide monophosphates generated in salvage reactions. Purine salvage reactions. Purine nucleosides and free bases generated by DNA and RNA breakdown are converted to nucleotide monophosphates. Purine catabolism. The purine bases guanine and hypoxanthine are degraded to uric acid, which is excreted from the body.
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The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985).
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The synthesis of N-carbamoyl L-aspartate from carbamoyl phosphate and L-aspartate is catalyzed by the aspartate carbamoyltansferase activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985).
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The synthesis of dihydroorotate from N-carbamoyl L-aspartate is catalyzed by the dihydroorotase activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein. This activity has not been directly demonstrated in experimental studies of the purified human protein, but has been inferred from the behavior of the purified hamster protein and the high degree of sequence similarity between the cloned hamster and human genes (Iwahana et al. 1996). Also on the basis of this similarity, the active human protein is annotated as a hexamer (Lee et al. 1985).
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Structural basis for fibroblast growth factor receptor activation
The KEN box: an APC recognition signal distinct from the D box targeted by Cdh1
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The purine bases guanine and hypoxanthine (derived from adenine by events in the purine salvage pathways) are converted to xanthine and then to uric acid, which is excreted from the body (Watts 1974). The end-point of this pathway in humans and hominoid primates is unusual. Most other mammals metabolize uric acid further to yield more soluble end products, and much speculation has centered on possible roles for high uric acid levels in normal human physiology.
Cytosolic xanthine dehydrogenase (XDH) catalyzes the reaction of xanthine with H2O to form urate and H2O2. The active form of the enzyme is a dimer (Saksela and Raivio 1996; Yamaguchi et al. 2007).
Hydrogen peroxide is generated in the course of peroxisomal fatty acid oxidation and purine catabolism, and is rapidly converted to water and molecular oxygen by the enzyme catalase. This enzyme is widely distributed in the body, but is especially abundant in liver, kidney, and red blood cells.
Cytosolic nucleoside phosphorylase (NP) trimer catalyzes the reversible reaction of inosine or deoxyinosine with orthophosphate to form hypoxanthine and ribose 1-phosphate or deoxyribose 1-phosphate (Ealick et al. 1990; Wiginton et al. 1980). While NP is active with either nuckeotide in vitro, levels of deoxyinosine are normally low in vivo, limiting the extent of this reaction. NP deficiency in vivo is associated with defects in purine nucleotide salvage and leads to immunodeficiency (Williams et al. 1987).
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Cytosolic xanthine dehydrogenase (XDH) catalyzes the reaction of hypoxanthine with H2O and oxygen to form xanthine and H2O2. The active form of the enzyme is a dimer (Saksela and Raivio 1996; Yamaguchi et al. 2007).
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Cytosolic purine 5'-nucleotidase (NT5C2) catalyzes the hydrolysis of GMP, dGMP, IMP, and dIMP to yield the corresponding nucleosides and orthophosphate (Bianchi and Spychala 2003; Spychala et al. 1988). The active form of the enzyme is a tetramer and has an absolute requirement for magnesium ions (Spychala et al. 1988; Wallden et al. 2007). Consistent with the biochemical properties of purified enzyme, cultured cells overexpressing the enzyme from a recombinant DNA clone showed enhanced activity against inosine and guanosine monophosphates, but not adenosine monophosphate (Gazziola et al. 2001; Sala-Newby et al. 2000).
Cytosolic nucleoside phosphorylase (NP) trimer catalyzes the reversible reaction of guanosine or deoxyguanosine with orthophosphate to form guanine and ribose 1-phosphate or deoxyribose 1-phosphate (Ealick et al. 1990; Wiginton et al. 1980). While NP is active with either nuckeotide in vitro, levels of deoxyguanosine are normally low in vivo, limiting the extent of this reaction. NP deficiency in vivo is associated with defects in purine nucleotide salvage and leads to immunodeficiency (Williams et al. 1987).
Cytosolic GMP reductase (GMPR) catalyzes the reaction of GMP and NADPH + H+ to yield IMP and NADP+ + NH4+ (Spector et al. 1979; Deng et al. 2002). Two GMPR proteins have been identified, GMPR and GMPR2. Both proteins form homotetramers (GMPR - unpublished crstallographic data PDB 2BLE; GMPR2 - Li et al. 2006).
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Nucleosides and free bases generated by DNA and RNA breakdown are converted back to nucleotide monophosphates, allowing them to re-enter the pathway of purine biosynthesis. Nucleosides and free bases generated by DNA breakdown are converted back to nucleotide monophosphates, allowing them to re-enter the pathway of purine biosynthesis. Nucleosides and free bases generated by RNA breakdown are converted back to nucleotide monophosphates, allowing them to re-enter the pathways of purine biosynthesis. Under normal conditions, DNA turnover is limited and deoxyribonucleotide salvage operates at a correspondingly low level (Watts 1974).
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Cellular signaling by fibroblast growth factor receptors
Cytosolic hypoxanthine-guanine phosphoribosyltransferase (HPRT1) tetramer catalyzes the reactions of guanine or hypoxanthine with PRPP to form GMP ir IMP and pyrophosphate (Holden and Kelley 1978; Jolly et al. 1983).
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Cytosolic ADAL (Adenosine DeAminase-Like) catalyzes the reaction of N6-methyl-AMP and water to form IMP and methylamine. The active form of the enzyme is a protein monomer complexed with a zinc ion (Murakami et al. 2011).
Cytosolic nucleoside phosphorylase (NP) trimer catalyzes the reversible reaction of guanine with ribose 1-phosphate or deoxyribose 1-phosphate to form guanosine or deoxyguanosine and orthophosphate (Ealick et al. 1990; Wiginton et al. 1980). While NP is active with either ribose 1-phosphate or deoxyribose 1-phosphate in vitro, levels of deoxyribose 1-phosphate are normally low in vivo, limiting the extent of this reaction. NP deficiency in vivo is associated with defects in purine nucleotide salvage and leads to immunodeficiency (Williams et al. 1987).
Cytosolic nucleoside phosphorylase (NP) trimer catalyzes the reversible reaction of hypoxanthine with ribose 1-phosphate or deoxyribose 1-phosphate to form inosine or deoxyinosine and orthophosphate (Ealick et al. 1990; Wiginton et al. 1980). While NP is active with either ribose 1-phosphate or deoxyribose 1-phosphate in vitro, levels of deoxyribose 1-phosphate are normally low in vivo, limiting the extent of this reaction. NP deficiency in vivo is associated with defects in purine nucleotide salvage and leads to immunodeficiency (Williams et al. 1987).
Cytosolic APRT dimer catalyzes the reaction of adenine and 5-phospho-alpha-D-ribose 1-diphosphate to form AMP and pyrophosphate (Holden et al. 1979).
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Two isoforms of adenylosuccinate synthetase, ADSS and ADSSL1, catalyze the reaction of IMP, aspartate, and GTP to form adenylosuccinate, GDP, and orthophosphate (Powell et al. 1992; Sun et al. 2005). ADSS is a homotetramer (unpublished crystallographic data - PDB 2V40) and ADSSL1 is inferred to be a tetramer likewise.
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The irreversible conversion of adenylosuccinate to adenosine 5'-monophosphate and fumarate is catalyzed by adenylosuccinate lyase. The active form of this enzyme is a cytosolic tetramer (Stone et al. 1993). The enzyme also catalyzes the conversion of 5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide (SAICAR) to 5'-phosphoribosyl-5-aminoimidazole-4-carboxamide (AICAR) and fumarate. Humans lacking the enzyme accumulate dephosphorylated forms of both substrates, indicating that the enzyme mediates both reactions in vivo as well (Race et al. 2000).
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The purine ribonucleotide inosine 5'-monophosphate (IMP) is assembled on 5-phospho-alpha-D-ribose 1-diphosphate (PRPP), with atoms derived from aspartate, glutamine, glycine, N10-formyl-tetrahydrofolate, and carbon dioxide. Although several of the individual reactions in this sequence are reversible, as indicated by the double-headed arrows in the diagram, other irreversible steps drive the pathway in the direction of IMP synthesis in the normal cell. All of these reactions are thus annotated here only in the direction of IMP synthesis. Guanosine 5'-monophosphate (GMP) and adenosine 5'-monophosphate (AMP) are synthesized from IMP.
Cytosolic adenosine deaminase (ADA) catalyzes the hydrolysis of 2'deoxyadenosine and adenosine to yield deoxyinosine and inosine, respectively, plus ammonia (Akeson et al. 1988). Unpublished crystallographic data (PDB 3IAR) indicate that the human enzyme is a monomer.
Cytosolic adenosine linase (ADK) catalyzes the reactions of adenosine and deoxyadenosine with ATP to yield the corresponding nucleotide monophosphates and ADP (Andres and Fox 1979). The enzyme is substantially more active on adenosine than deoxyadenosine in vitro (Hurley at al. 1985) though studies of cultured cells suggest that both reactions may be physiologically relevant (Hershfield et al. 1982). The enzyme is a monomer complexed with magnesium (Mathews et al. 1998).
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RasGRP1 and RasGRP3 regulate B cell proliferation by facilitating B cell receptor-Ras signaling
Cytosolic AMP deaminase (AMPD) catalyzes the hydrolysis of AMP to yield IMP and ammonia. Three isoforms of AMPD, E, L, and M, have been identified that differ in their expression patterns in the body. All occur as tetramers and all have qualitatively the same catalytic activity, however (Bausch-Jurken et al. 1992; Mahnke-Zizelman et al. 1998).
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The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin. Mediation of neurite outgrowth and co-expression of rage and amphoterin in the developing nervous system
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Atrial amyloid deposits in the failing human heart display both atrial and brain natriuretic peptide-like immunoreactivity
The type 1 insulin-like growth factor receptor pathway
Mitochondrial glutamate dehydrogenase 1 (GLUD1) catalyzes the reversible reaction of glutamate and NAD(P)+ to form 2-oxoglutarate, NAD(P)H + H+, and ammonia (Fang et al. 2002). Mature GLUD1 protein lacks the 53 aminoterminal residues of the nascent protein (Julliard and Smith 1979), which function as a mitochondrial import signal. The active form of the enzyme is a hexamer, allosterically activated by ADP and inhibited by GTP (Fang et al. 2002; Smith et al. 2002).
Cytosolic glutamine synthetase (glutamate-ammonia ligase - GLUL) catalyzes the reaction of glutamate, ammonia, and ATP to form glutamine, ADP, and orthophosphate. The enzyme is a decamer (Krajewski et al. 2008). Mutations in the gene encoding GLUL cause glutamine deficiency in vivo (Haberle et al. 2005).
Mitochondrial glutaminase (GLS) catalyzes the hydrolysis of glutamine to yield glutamate and ammonia. Two GLS enzymes have been identified, one abundantly expressed in the liver (GLS - Elgadi et al. 1999) and one abundantly expressed in kidney (GLS2 - Gomez-Fabre et al. 2000). Their biochemical properties are similar. The enzymes are inferred to function as dimers based on unpublished crystallographic data for GLS (PDB 3CZD) and studies of glutaminase enzyme purified from Ehrlich Ascites cells (Quesada et al. 1988).
Pyrroline-5-carboxylate reductase 1 (PYCR1) catalyzes the reaction of (S)-1-pyrroline-5-carboxylate with NADPH + H+ to form proline and NADP+ (Merrill et al. 1989). The active enzyme is a homodecamer (Meng et al. 2006). Recent immunofluoresence studies show that PYCR1 colocalizes with mitochondrial markers including pyrroline 5-carboxylate synthase in cultured human fibroblasts (Reversade et al. 2009).
Delta-1-pyrroline-5-carboxylate synthetase associated with the inner mitochondrial membrane catalyzes the two-step reaction that converts glutamate, ATP, and NADPH + H+ to L-glutamate gamma-semialdehyde, NADP+, ADP, and orthophosphate. Two P5CS isoforms have been identified; both are active when expressed in enzyme-deficient cells in culture (Hu et al. 1999). Unpublished crystallographic data (PDB 2H5G) indicate that the enzyme is a dimer.
Mitochondrial glutamate dehydrogenase 1 (GLUD1) catalyzes the reversible reaction of 2-oxoglutarate, NAD(P)H + H+, and ammonia to form glutamate and NAD(P)+ (Fang et al. 2002). Mature GLUD1 protein lacks the 53 aminoterminal residues of the nascent protein (Julliard and Smith 1979), which function as a mitochondrial import signal. The active form of the enzyme is a hexamer, allosterically activated by ADP and inhibited by GTP (Fang et al. 2002; Smith et al. 2002).
Cytosolic asparagine synthase (ASNS) catalyzes the reaction of aspartate, glutamine, and ATP to form asparagine, glutamate, AMP, and pyrophosphate. Studies of the recombinant protein expressed in E. coli suggest that the active form of the enzyme is a dimer (Van Heeke and Schuster 1989).
Mitochondrial glutamate oxaloacetate transaminase 2 (aspartate aminotransferase 2 - GOT2) catalyzes the reversible reaction of aspartate and 2-oxoglutarate (alpha-ketoglutarate) to form oxaloacetate and glutamate (Martini et al. 1985). The active form of the enzyme is inferred to be a dimer with one molecule of pyridoxal phosphate associated with each monomer.
Mitochondrial ornithine aminotransferase (OAT) catalyzes the reversible reaction of glutamate semialdehyde and glutamate to form ornithine and alpha-ketoglutarate (Ohura et al. 1982). The active enzyme is a hexamer (Shen et al. 1998). Inherited OAT deficiency leads to ornithine accumulation in vivo and gyrate atrophy of the choroid and retina (Brody et al. 1992; Vallee and Simell 2001).
Mitochondrial ornithine aminotransferase (OAT) catalyzes the reversible reaction of ornithine and alpha-ketoglutarate to form glutamate semialdehyde and glutamate (Ohura et al. 1982). The active enzyme is a hexamer (Shen et al. 1998). Inherited OAT deficiency leads to ornithine accumulation in vivo and gyrate atrophy of the choroid and retina (Brody et al. 1992; Valle and Simell 2001).
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Glutamic-pyruvate transaminase 2 (alanine aminotransferase 2) (GPT2) catalyzes the reversible reaction of pyruvate and glutamate to form alanine and 2-oxoglutarate (alpha-ketoglutarate) (Yang et al. 2002). Unpublished crystallographic data are consistent with a homodimeric structure for the enzyme with one molecule of pyridoxal phosphate associated with each monomer (PDB 3IHJ). Recent studies of organelles purified from cultured human muscle cells suggest that GPT2 is localized to mitochondria (Glinghammar et al. 2009).
Cytosolic aspartate aminotransferase (glutamate oxaloacetate transaminase 1 - GOT1) catalyzes the reversible reaction of oxaloacetate and glutamate to form aspartate and 2-oxoglutarate (alpha-ketoglutarate) (Doyle et al. 1990). Unpublished crystallographic data (PBD 3IIO) suggest the enzyme is a homodimer.
Cytosolic glutamic-pyruvate transaminase (alanine aminotransferase) (GPT) catalyzes the reversible reaction of pyruvate and glutamate to form alanine and 2-oxoglutarate (alpha-ketoglutarate) (Sohocki et al. 1997; Yang et al. 2002). The active form of the enzyme is a dimer (Ishiguro et al. 1991) and is inferred to have a molecule of pyridoxal phosphate associated with each monomer. This reaction allows the synthesis of alanine from intermediates of glucose metabolism in a well-fed person. Under fasting conditions, alanine, derived from protein breakdown, can be converted to pyruvate and used to synthesize glucose via the gluconeogenic pathway in liver, or fully oxidized via the TCA cycle in other tissues.
Glutamic-pyruvate transaminase 2 (alanine aminotransferase 2) (GPT2) catalyzes the reversible reaction of alanine and 2-oxoglutarate (alpha-ketoglutarate) to form pyruvate and glutamate (Yang et al. 2002). Unpublished crystallographic data are consistent with a homodimeric structure for the enzyme with one molecule of pyridoxal phosphate associated with each monomer (PDB 3IHJ). Recent studies of organelles purified from cultured human muscle cells suggest that GPT2 is localized to mitochondria (Glinghammar et al. 2009).
Mitochondrial NUDT9 (ADP-ribose pyrophosphatase) catalyzes the hydrolysis of ADP-ribose to form AMP and D-ribose 5-phosphate. The active enzyme is the longer of two isoforms generated by alternative splicing and is a monomer complexed with two magnesium ions (Perraud et al. 2003; Shen et al. 2003).
Cytosolic NUDT5 dimer (ADP-ribose pyrophosphatase) catalyzes the hydrolysis of ADP-ribose to form AMP and D-ribose 5-phosphate. Each NUDT5 subunit is associated with three magnesium ions (Zha et al. 2006, 2008). NUDT5 also catalyzes the hydrolysis of 8-oxo-dGTP but with a strongly alkaline pH optimum (Ito et al. 2011) so the physiological relevance of this reaction is unclear and it is not annotated here.
Cytosolic glutamic-pyruvate transaminase (alanine aminotransferase) (GPT) catalyzes the reversible reaction of alanine and 2-oxoglutarate (alpha-ketoglutarate) to form pyruvate and glutamate (Sohocki et al. 1997; Yang et al. 2002). The active form of the enzyme is a dimer (Ishiguro et al. 1991) and is inferred to have a molecule of pyridoxal phosphate associated with each monomer. This reaction allows the synthesis of alanine from intermediates of glucose metabolism in a well-fed person. Under fasting conditions, alanine, derived from protein breakdown, can be converted to pyruvate and used to synthesize glucose via the gluconeogenic pathway in liver, or fully oxidized via the TCA cycle in other tissues.
Vitamins are a diverse group of organic compounds, required in small amounts in the diet. They have distinct biochemical roles, often as coenzymes, and are either not synthesized or synthesized only in limited amounts by human cells. Vitamins are classified according to their solubility, either fat-soluble or water-soluble. The physiological processes dependent on vitamin-requiring reactions include many aspects of intermediary metabolism, vision, bone formation, and blood coagulation, and vitamin deficiencies are associated with a correspondingly diverse and severe group of diseases. The metabolism of water-soluble vitamins and of vitamin D are annotated in Reactome.
Nucleotides and their derivatives are used for short-term energy storage (ATP, GTP), for intra- and extra-cellular signaling (cAMP; adenosine), as enzyme cofactors (NAD, FAD), and for the synthesis of DNA and RNA. Most dietary nucleotides are consumed by gut flora; the human body's own supply of these molecules is synthesized de novo. Additional metabolic pathways allow the interconversion of nucleotides, the salvage and reutilization of nucleotides released by degradation of DNA and RNA, and the catabolism of excess nucleotides (Rudolph 1994). These pathways are regulated to control the total size of the intracellular nucleotide pool, to balance the relative amounts of individual nucleotides, and to couple the synthesis of deoxyribonucleotides to the onset of DNA replication (S phase of the cell cycle). These pathways are also of major clinical interest as they are the means by which nucleotide analogues used as anti-viral and anti-tumor drugs are taken up by cells, activated, and catabolized (Weilin and Nordlund 2010). As well, differences in nuclotide metabolic pathways between humans and aplicomplexan parasites like Plasmodium have been exploited to design drugs to attack the latter (Hyde 2007). The movement of nucleotides and purine and pyrimidine bases across lipid bilayer membranes, mediated by SLC transporters, is annotated as part of the module "transmembrane transport of small molecules".
Enzymes that belong to the NUDT (Nudix) superfamily catalyze the hydrolysis of phosphodiester bonds in molecules including nucleoside triphosphates and diphosphates and nucleotide sugars. Family members are defined by the presence of an amino acid sequence motif shared with the E. coli MutT gene product, and are involved in diverse physiological processes (Mildvan et al. 2005; McLennan 2006). The hydrolysis of nucleoside di and triphosphates whose purine bases have been oxidized or deaminated may protect the cell from the mutational damage that would occur if modified deoxyribonucleotides were incorporated into DNA and from the aberrant protein synthesis that would occur if modified ribonucleotides were incorporated into mRNA (Iyama et al. 2010; Takagi et al. 2012). The hydrolysis of ADP ribose may prevent the aberrant spontaneous ADP ribosylation of cellular proteins that could occur were this molecule to accumulate to high levels in the cell (Perraud et al. 2003; Shen et al. 2003). This hypothesis is further supported by the demonstration that mice lacking NUDT1 show an increased lifetime incidence of liver and other tumors compared to normal controls, and that rapidly metabolizing tumor cells in culture are killed under conditions where synthesis of NUDT1 protein is suppressed or its catalytic activity is inhibited (Gad et al. 2014; Huber et al. 2014).
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Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme
Cytosolic ITPA dimer catalyzes the reaction of dITP and water to form dIMP and PPi (pyrophosphate). Mg++ is required for enzymatic activity. The hydrolysis of dITP is thought to prevent its incorporation into DNA, which would be mutagenic (Lin et al. 2001; Abolhassani et al. 2010).
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Cytosolic ITPA dimer catalyzes the reaction of XTP and water to form XMP and PPi (pyrophosphate). Mg++ is required for enzymatic activity. The hydrolysis of XTP is thought to prevent its incorporation into mRNA, which would lead to aberrant protein synthesis (Lin et al. 2001; Abolhassani et al. 2010).
NUDT18 (MTH3) catalyzes the reaction of 8-oxo-dGDP and water to form 8-oxo-dGMP and Pi (orthophosphate) (Takagi et al. 2012). The subcellular location of NUDT18 has not been established but is assumed to be cytosolic like NUDT1.
NUDT18 (MTH3) catalyzes the reaction of 8-oxo-GDP and water to form 8-oxo-GMP and Pi (orthophosphate) (Takagi et al. 2012). The subcellular location of NUDT18 has not been established but is assumed to be cytosolic like NUDT1.
NUDT18 (MTH3) catalyzes the reaction of 8-hydroxy-dADP and water to form 8-hydroxy-dAMP and Pi (orthophosphate) (Takagi et al. 2012). The subcellular location of NUDT18 has not been established but is assumed to be cytosolic like NUDT1.
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Cytosolic nucleoside diphosphate kinases catalyze the reversible reaction of ribonucleoside and deoxyribonucleoside 5'-diphosphates with ADP to form the corresponding nucleoside 5'-diphosphates and ATP. These kinases are ubiquitously expressed enzymes with broad substrate specificities (Berg and Joklik 1954; Parks and Agarwal 1973). Three human cytosolic nucleoside diphosphate kinase proteins, NME1, 2, and 3, have been characterized biochemically (Gilles et al. 1991; Schaertl et al. 1998; Erent et al. 2001; Chen et al. 2003). All are catalytically active as hexamers: homohexamers of NME1, 2, and 3 have been described, as have heterohexamers containing all possible combinations of NME1 and 2 (Gilles et al. 1991; Erent et al. 2001). While the high ratio of ATP to ADP concentrations in the cytosol normally favors the conversion of (d)NDP and ATP to (d)NTP and ADP, the reversibility of the reactions and the overlapping substrate specificities of the enzymes suggest that this group of reverse reactions can buffer the intracellular nucleotide pool and regulate the relative concentrations of individual nucleoside di- and tri-phosphates in the pool.
Nucleoside diphosphate kinase NME4 associated with the inner mitochondrial membrane (Tokarska-Schlattner et al. 2008) catalyzes the reversible reaction of ribonucleoside and deoxyribonucleoside 5'-diphosphates with ADP to form the corresponding nucleoside 5'-diphosphates and ATP. The active form of the enzyme is a hexamer of NME4 polypeptides whose amino-terminal 33 residues, a mitochondrial translocation signal, have been removed (Milon et al. 2000). The substrate specificity of NME4 has not been examined in detail, but is inferred to be broad like that of the homologous NME1, 2, and 3 kinases (Schaertl et al. 1998).
Nucleoside diphosphate kinase NME4 associated with the inner mitochondrial membrane (Tokarska-Schlattner et al. 2008) catalyzes the reversible reaction of ribonucleoside and deoxyribonucleoside 5'-diphosphates with ATP to form the corresponding nucleoside 5'-triphosphates and ADP. The active form of the enzyme is a hexamer of NME4 polypeptides whose amino-terminal 33 residues, a mitochondrial translocation signal, have been removed (Milon et al. 2000). The substrate specificity of NME4 has not been examined in detail but is inferred to be broad like that of the homologous NME1, 2, and 3 kinases (Schaertl et al. 1998).
Cytosolic ITPA dimer catalyzes the reaction of ITP and water to form IMP and PPi (pyrophosphate). Mg++ is required for enzymatic activity. The hydrolysis of ITP is thought to prevent its incorporation into mRNA, which would lead to aberrant protein synthesis (Lin et al. 2001; Abolhassani et al. 2010).
An array of kinases catalyze the reversible phosphorylation of nucleotide monophosphates to form nucleotide diphosphates and triphosphates. Nucleoside monophosphate kinases catalyze the reversible phosphorylation of nucleoside and deoxynucleoside 5'-monophosphates to form the corresponding nucleoside 5'-diphosphates. Most appear to have restricted specificities for nucleoside monophosphates, and to use ATP preferentially (Van Rompay et al. 2000; Anderson 1973; Noda 1973). The total number of human enzymes that catalyze these reactions in vivo is not clear. In six cases, a well-defined biochemical activity has been associated with a purified protein, and these are annotated here. However, additional nucleoside monophosphate kinase-like human proteins have been identified in molecular cloning studies whose enzymatic activities are unknown, and several distinctive nucleoside monophosphate kinase activities detected in cell extracts, e.g., a GTP-requiring adenylate kinase activity (Wilson et al. 1976) and one or more guanylate kinase activities (Jamil et al. 1975) have not been unambiguously associated with specific human proteins. The nucleoside monophosphates against which each of the six well-characterized enzymes is active is shown in the table (Van Rompay et al. 2000). All six efficiently use ATP as a phosphate donor, but have some activity with other nucleoside triphosphates as well in vitro. The high concentrations of ATP relative to other nucleoside triphosphates in vivo makes it the likely major phosphate donor in these reactions under most conditions. All of these phosphorylation reactions are freely reversible in vitro when carried out with purified enzymes and substrates, having equilibrium constants near 1. In vivo, high ratios of ATP to ADP are likely to favor the forward direction of these reactions, i.e., the conversion of (d)NMP and ATP to (d)NDP and ADP. At the same time, the reversibility of the reactions and the overlapping substrate specificities of the enzymes raises the possibility that this group of reactions can buffer the intracellular nucleotide pool and regulate the relative concentrations of individual nucleotides in the pool: if any one molecule builds up to unusually high levels, multiple routes appear to be open not only to dispose of it but to use it to increase the supply of less abundant nucleotides. Ribonucleotide reductase catalyzes the synthesis of deoxyribonucleotide diphosphates from ribonucleotide diphosphates.
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STING Recognition of Cytoplasmic DNA Instigates Cellular Defense
Rous sarcoma virus transforming protein lacking myristic acid phosphorylates known polypeptide substrates without inducing transformation
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Manipulation of EphB2 regulatory motifs and SH2 binding sites switches MAPK signaling and biological activity
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The mechanism of axon growth: what we have learned from the cell adhesion molecule L1
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T cell receptor signaling: beyond complex complexes
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8p11 myeloproliferative syndrome with a novel t(7;8) translocation leading to fusion of the FGFR1 and TIF1 genes
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A complete inventory of all enzymes in the eukaryotic methionine salvage pathway
Effects of synthetic analogues of phosphoenolpyruvate on muscle and liver pyruvate kinase, muscle enolase, liver phosphoenolpyruvate carboxykinase and on the intra-/extra-mitochondrial tricarboxylic acid carrier transport system
P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II.
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Novel function of alternatively activated macrophages: stabilin-1-mediated clearance of SPARC
Regulation of IkappaB kinase-related kinases and antiviral responses by tumor suppressor CYLD
Phosphomevalonate kinase: functional investigation of the recombinant human enzyme
The stress-activated protein kinase subfamily of c-Jun kinases
8p11 myeloproliferative syndrome: a review
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One of the downstream effects of insulin, mediated via protein phosphatase 2A (PP2A), is increased synthesis of Fructose-2,6-bisphosphate, an allosteric activator of phosphofructokinase 1 (PFK1). PFK1 in turn catalyzes the committed step of glycolysis so the net effect of this whole sequence of events set off by insulin is to increase cytosolic concentrations of the small molecules formed in the course of glycolysis. This in turn drives the increased synthesis of Xylulose-5-phosphate, itself a positive regulator of PP2A.
A member of the PP2A family of phosphatases dephosphorylates both cytosolic and nuclear forms of ChREBP (Carbohydrate Response Elemant Binding Protein). In the nucleus, dephosphorylated ChREBP complexes with MLX protein and binds to ChRE sequence elements in chromosomal DNA, activating transcription of genes involved in glycolysis and lipogenesis. The phosphatase is activated by Xylulose-5-phosphate, an intermediate of the pentose phosphate pathway (Kabashima et al. 2003). The rat enzyme has been purified to homogeneity and shown by partial amino acid sequence analysis to differ from previously described PP2A phosphatases (Nishimura and Uyeda 1995) - the human enzyme has not been characterized.
Characterization of human iodothyronine sulfotransferases
Purification and characterization of a novel xylulose 5-phosphate-activated protein phosphatase catalyzing dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase
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At the beginning of this reaction, 1 molecule of 'AMPK heterotrimer (inactive)', and 1 molecule of 'AMP' are present. At the end of this reaction, 1 molecule of 'AMPK heterotrimer:AMP' is present. This reaction takes place in the 'nucleus'.
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Xylulose-5-phosphate binds to Protein phosphatase 2A (PP2A), activating it. This regulatory step may be the crucial physiological link explaining the coordinately increased rates of glycolysis and lipogenesis generally observed in individuals consuming high-carbohydrate diets.
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In the nucleus, activated AMPK phosphorylates serine residue 568 of ChREBP (Carbohydrate Response Element Binding Protein). Phosphorylated ChREBP does not bind to ChRE chromosomal DNA sequence elements and thus loses its ability to promote transcription of genes involved in glycolysis and lipogenesis.
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LKB1 phosphorylates threonine residue 172 of the alpha subunit of the AMPK heterotrimer, activating it. LKB1, a serine/threonine kinase, was first identified as the gene whose mutation is associated with the Peutz-Jeghers familial cancer syndrome. This disease phenotype is consistent with the hypothesis that the interaction between LKB1 and AMPK normally plays a key role in the negative regulation of cell growth (Hardie 2004).
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At the beginning of this reaction, 1 molecule of 'pChREBP (Ser 196, Thr 666)' is present. At the end of this reaction, 1 molecule of 'Orthophosphate', and 1 molecule of 'pChREBP (Thr 666)' are present. This reaction takes place in the 'cytosol' and is mediated by the 'phosphatidate phosphatase activity' of 'PP2A-ABdeltaC complex'.
AMP-activated protein kinase (AMPK) is a sensor of cellular energy levels. A high cellular ratio of AMP:ATP triggers the phosphorylation and activation of AMPK. Activated AMPK in turn phosphorylates a wide array of target proteins, as shown in the figure below (reproduced from (Hardie et al. 2003), with the permission of D.G. Hardie). These targets include ChREBP (Carbohydrate Response Element Binding Protein), whose inactivation by phosphorylation reduces transcription of key enzymes of the glycolytic and lipogenic pathways.
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At the beginning of this reaction, 1 molecule of 'pChREBP (Thr 666)' is present. At the end of this reaction, 1 molecule of 'Orthophosphate', and 1 molecule of 'ChREBP protein' are present. This reaction takes place in the 'nucleus' and is mediated by the 'phosphatidate phosphatase activity' of 'PP2A-ABdeltaC complex'.
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At the beginning of this reaction, 1 molecule of 'pChREBP(Ser 568)' is present. At the end of this reaction, 1 molecule of 'Orthophosphate', and 1 molecule of 'ChREBP protein' are present. This reaction takes place in the 'nucleus' and is mediated by the 'phosphatidate phosphatase activity' of 'PP2A-ABdeltaC complex'.
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Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II
Upon dissociation of protein kinase A (PKA) tetramers in the presence of cAMP, the released PKA catalytic monomers phosphorylate specific serine and threonine residues of several metabolic enzymes. These target enzymes include glycogen phosphorylase kinase, glycogen synthase and PF2K-Pase. PKA also phosphorylates ChREBP (Carbohydrate Response Element Binding Protein), preventing its movement into the nucleus and thus its function as a positive transcription factor for genes involved in glycolytic and lipogenic reactions.
ChREBP (Carbohydrate Response Element Binding Protein) doubly phosphorylated at threonine 666 and serine 196 is inactive and is localized to the cytosol. Removal of the phosphate residue at serine 196 allows ChREBP to translocate between the cytosol and the nucleoplasm.
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Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia
Adenylate cyclase catalyses the synthesis of cyclic AMP (cAMP) from ATP. In the absence of cAMP, protein kinase A (PKA) exists as inactive tetramers of two catalytic subunits and two regulatory subunits. cAMP binding to PKA tetramers causes them to dissociate and release their catalytic subunits as active monomers. Four isoforms of the regulatory subunit are known, that differ in their tissue specificity and functional characteristics, but the specific isoform activated in response to glucagon signaling has not yet been identified.
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Activated adenylate cyclase associated with the plasma membrane catalyzes the reaction of cytosolic ATP to form 3',5'-cyclicAMP and pyrophosphate.
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G(s)-alpha:GTP binds to inactive adenylate cyclase, causing a conformational transition in adenylate cyclase exposing the catalytic site and activating it.
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Pancreatic beta cells integrate signals from several metabolites and hormones to control the secretion of insulin. In general, glucose triggers insulin secretion while other factors can amplify or inhibit the amount of insulin secreted in response to glucose. Factors which increase insulin secretion include the incretin hormones Glucose-dependent insulinotropic polypeptide (GIP and glucagon-like peptide-1 (GLP-1), acetylcholine, and fatty acids. Factors which inhibit insulin secretion include adrenaline and noradrenaline. Increased blood glucose levels from dietary carbohydrate play a dominant role in insulin release from the beta cells of the pancreas. Glucose catabolism in the beta cell is the transducer that links increased glucose levels to insulin release. Glucose uptake and glycolysis generate cytosolic pyruvate; pyruvate is transported to mitochondria and converted both to oxaloacetate which increases levels of TCA cycle intermediates, and to acetyl-CoA which is oxidized to CO2 via the TCA cycle. The rates of ATP synthesis and transport to the cytosol increase, plasma membrane ATP-sensitive inward rectifying potassium channels (KATP channels) close, the membrane depolarizes, and voltage-gated calcium channels in the membrane open (Muoio and Newgard 2008; Wiederkehr and Wollheim 2006). Elevated calcium concentrations near the plasma membrane cause insulin secretion in two phases: an initial high rate within minutes of glucose stimulation and a slow, sustained release lasting longer than 30 minutes. In the initial phase, 50-100 insulin granules already docked at the membrane are exocytosed. Exocytosis is rendered calcium-dependent by Synaptotagmin V/IX, a calcium-binding membrane protein located in the membrane of the docked granule, although the exact action of Synapototagmin in response to calcium is unknown. Calcium also causes a translocation of reserve granules within the cell towards the plasma membrane for release in the second, sustained phase of secretion. Human cells contain L-type (continually reopening), P/Q-type (long burst), R-type (long burst), and T-type (short burst) calcium channels and these partly account for differences between the two phases of secretion. Other factors that distinguish the two phases are not yet fully known (Bratanova-Tochkova et al. 2002; Henquin 2000; MacDonald et al. 2005).
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Phosphorylation of ChREBP (Carbohydrate Response Element Binding Protein) at serine 196 by PKA inhibits its nuclear translocation. This reaction has been studied in detail using mouse proteins (Kawaguchi et al. 2001); the human version of the reaction is inferred from these studies.
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In its active (unphosphorylated) form, ChREBP (Carbohydrate Response Element Binding Protein) binds so-called ChRE (Carbohydrate Response Element) DNA sequence motifs found upstream of several genes involved in glucose utilization and lipid synthesis, activating transcription of these genes. Phosphorylation of ChREBP at threonine residue 666 by PKA (protein kinase A) blocks this binding activity, and thus has the effect of down-regulating expression of the target genes. ChREBP phosphorylation can be reversed by the action of protein phosphatase 2A (PP2A).
Intestinal tumorigenesis in compound mutant mice of both Dpc4 (Smad4) and Apc genes
Glucagon and insulin are peptide hormones released from the pancreas into the blood, that normally act in complementary fashion to stabilize blood glucose concentration. When blood glucose levels rise, insulin release stimulates glucose uptake from the blood, glucose breakdown (glycolysis), and glucose storage as glycogen. When blood glucose levels fall, glucagon release stimulates glycogen breakdown and de novo glucose synthesis (gluconeogenesis), while inhibiting glycolysis and glycogen synthesis. At a molecular level, the binding of glucagon to the extracellular face of its receptor causes conformational changes in the receptor that allow the dissociation and activation of subunits Gs and Gq. The activation of Gq leads to the activation of phospholipase C, production of inositol 1,4,5-triphosphate, and subsequent release of intracellular calcium. The activation of Gs leads to activation of adenylate cyclase, an increase in intracellular cAMP levels, and activation of protein kinase A (PKA). Active PKA phosphorylates key enzymes of glycogenolysis, glycogenesis, gluconeogenesis, and glycolysis, modifying their activities. These signal transduction events, and some of their downstream consequences, are illustrated below (adapted from Jiang and Zhang, 2003).
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Nitric oxide (NO) is produced from L-arginine by the family of nitric oxide synthases (NOS) enzymes, forming the free radical NO and citrulline as byproduct. The cofactor tetrahydrobiopterin (BH4) is an essential requirement for the delivery of an electron to the intermediate in the catalytic cycle of NOS.
BH2 may compete with BH4 to bind eNOS, uncoupling eNOS leading to the formation of superoxide rather than nitric oxide. BH2, the oxidised form of BH4, cannot contribute electrons to heme in the reductase domain of eNOS, thereby uncoupling it from arginine oxidation and producing superoxide from oxygen instead (Vasquez-Vivar et al. 2002).
eNOS activity is regulated by numerous post-translational modifications including phosphorylation and acylation, which also modulate its interactions with other proteins and its subcellular localization. In general, following myristoylation and palmitoylation, eNOS localizes to caveolae in the plasma membrane, where in resting cells, it is bound to caveolin and remains inactive. Several agonists that raise intracellular calcium concentrations promote calmodulin binding to eNOS and the dissociation of caveolin from the enzyme, leading to an activated eNOS-calmodulin complex. Phosphorylation plays a significant role in regulating eNOS activity, especially the phosphorylation of Ser1177, located within the reductase domain, which increases enzyme activity by enhancing reductase activity and calcium sensitivity. In unstimulated, cultured endothelial cells, Ser1177 is rapidly phosphorylated following a variety of stimuli: fluid shear stress, insulin, estrogen, VEGF, or bradykinin. The kinases involved in this process depend upon the stimuli applied. For instance, shear stress phosphorylates Ser1177 by activating Akt and PKA; insulin activates both Akt and the AMP-activated protein kinase (AMPK); estrogen and VEGF mainly phosphorylate eNOS via Akt; whereas the bradykinin-induced phosphorylation of Ser1177 is mediated by CaMKII. When Ser1177 is phosphorylated, NO production is increased several-fold above basal levels. The phosphorylation of a threonine residue (Thr 495), located in the CaM binding domain, is associated with a decrease in eNOS activity. When this residue is dephosphorylated, substantially more CaM binds to eNOS and elevates enzyme activity. Stimuli associated with dephosphorylation of Thr495 (e.g., bradykinin, histamine, and Ca2+ ionophores) also increase Ca2+ levels resulting in the phosphorylation of Ser1177. Additional phosphorylation sites, such as Ser114 and Ser633, and tyrosine phosphorylation have all been detected, but their functional relevance remains unclear. It is speculated that the tyrosine phosphorylation of eNOS is unlikely to affect enzyme activity directly, but more likely to impact the protein-protein interactions with associated scaffolding and regulatory proteins.
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In the second salvage step, dihydrofolate reductase (DHFR) can regenerate BH4 from BH2, a process which increases the BH4:BH2 ratio providing BH4 for coupled eNOS production of NO. In mice cell lines, DHFR inhibition or knockdown diminishes the BH4:BH2 ratio and exacerbates eNOS uncoupling (Crabtree et al. 2009).
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High levels of the end product, BH4, negatively regulates GCH1. It does this via GTP cyclohydrolase 1 feedback regulatory protein (GCHFR). BH4-dependant GCHFR in the form of a homopentamer complexes with the decameric GCH1 enzyme in the ratio 2:1 to inactivate it. L-phenylalanine reverses this inhibition. These regulatory steps control the biosynthesis of BH4. (Swick & Kapatos 2006, Chavan et al. 2006, Harada et al. 1993).
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Tetrahydrobiopterin (BH4) is an essential co-factor for the aromatic amino acid hydroxylases and glycerol ether monooxygenase and it regulates nitric oxide synthase (NOS) activity. Inherited BH4 deficiency leads to hyperphenylalaninemia, and dopamine and neurotransmitter deficiency in the brain. BH4 maintains enzymatic coupling to L-arginine oxidation to produce NO. Oxidation of BH4 to BH2 results in NOS uncoupling, resulting in superoxide (O2.-) formation rather than NO. Superoxide rapidly reacts with NO to produce peroxynitrite which can further uncouple NOS. These reactive oxygen species (superoxide and peroxynitrite) can contribute to increased oxidative stress in the endothelium leading to atherosclerosis and hypertension (Thony et al. 2000, Crabtree and Channon 2011,Schulz et al. 2008, Schmidt and Alp 2007). The synthesis, recycling and effects of BH4 are shown here. Three enzymes are required for the de novo biosynthesis of BH4 and two enzymes for the recycling of BH4.
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6-pyruvoyl tetrahydrobiopterin synthase (PTPS) requires phosphorylation on Ser-19 for enzyme activity (Scherer-Oppliger et al. 1999).
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The first and rate-limiting enzyme in tetrahydrobiopterin de novo biosynthesis is GTP cyclohydrolase I (GCH1, GTPCHI). Three different isoforms are produced but only isoform 1 is functionally active (Gütlich et al. 1994). GCH1 is functional as a homodecamer. First, a monomer of GCH1 forms a dimer. Then five dimers arrange into a ring-like structure to form the homodecamer (Nar et al. 1995).
The oxidation product of BH4, 7,8-dihydrobiopterin (BH2), can compete with BH4 for binding to eNOS. This can lead to the uncoupling of eNOS and can result in the formation of reactive oxygen species (Vasquez-Vivar et al. 2002).
6-pyruvoyl tetrahydrobiopterin synthase (PTPS) (Takikawa et al. 1986) catalyses the second step in BH4 biosynthesis, the dephosphorylation of DHNTP to 6-pyruvoyl-tetrahydropterin (PTHP). PTPS is believed to function as a homohexamer (Nar et al. 1994, Bürgisser et al. 1994) and has a requirement for Zn2+ (one Zn2+ ion bound per subunit) and Mg2+ ions for activity (Bürgisser et al. 1995). The phosphorylation of Ser-19 is an essential modification for enzyme activity (Scherer-Oppliger et al. 1999).
At the end of this reaction, 1 molecule of 'pyruvate kinase, liver and RBC' is present. This reaction takes place in the 'nucleus'.
The PKLR gene is transcribed, its mRNA is translated, spliced, and translated to yield the L isoform of PKLR protein. PKLR expression is positively regulated by HNF1A. Mutations in HNF1A are associated with a form of MODY (maturity onset diabetes of the young) (Fanjans et al. 2001) but the molecular details of PKLR expression in intact pancreatic beta cells have not been studied in humans, and are inferred from corresponding ones worked out in the mouse.
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Self-association of N-syndecan (syndecan-3) core protein is mediated by a novel structural motif in the transmembrane domain and ectodomain flanking region
The cofactor tetrahydrobiopterin (BH4) ensures endothelial nitric oxide synthase (eNOS) couples electron transfer to L-arginine oxidation (Berka et al. 2004). During catalysis, electrons derived from NADPH transfer to the flavins FAD and FMN in the reductase domain of eNOS and then on to the ferric heme in the oxygenase domain of eNOS. BH4 can donate an electron to intermediates in this electron transfer and is oxidised in the process, forming the BH3 radical. This radical can be reduced back to BH4 by iron, completing the cycle and forming ferrous iron again. Heme reduction enables O2 binding and L-arginine oxidation to occur within the oxygenase domain (Stuehr et al. 2009).
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HSP90 serves as a scaffold to promote productive interaction between AKT1 and eNOS. Due to the proximity of these proteins once complexed with HSP90, AKT1 phosphorylates eNOS at Ser1177. When Ser1177 is phosphorylated, the level of NO production is elevated two- to three-fold above basal level.
Many hormones that affect individual physiological processes including the regulation of appetite, absorption, transport, and oxidation of foodstuffs influence energy metabolism pathways. While insulin mediates the storage of excess nutrients, glucagon is involved in the mobilization of energy resources in response to low blood glucose levels, principally by stimulating hepatic glucose output. Small doses of glucagon are sufficient to induce significant glucose elevations. These hormone-driven regulatory pathways enable the body to sense and respond to changed amounts of nutrients in the blood and demands for energy. Glucagon and Insulin act through various metabolites and enzymes that target specific steps in metabolic pathways for sugar and fatty acids. The processes responsible for the long-term control of fat synthesis and short term control of glycolysis by key metabolic products and enzymes are annotated in this module as six specific pathways: Pathway 1. Glucagon signalling in metabolic pathways: In response to low blood glucose, pancreatic alpha-cells release glucagon. The binding of glucagon to its receptor results in increased cAMP synthesis, and Protein Kinase A (PKA) activation. Pathway 2. PKA mediated phosphorylation:PKA phosphorylates key enzymes, e.g., 6-Phosphofructo-2-kinase /Fructose-2,6-bisphosphatase (PF2K-Pase) at serine 36, and regulatory proteins, e.g., Carbohydrate Response Element Binding Protein (ChREBP) at serine 196 and threonine 666. Insulin mediated responses to high blood glucose will be annotated in future versions of Reactome. In brief, the binding of insulin to its receptor leads to increased protein phosphatase activity and to hydrolysis of cAMP by cAMP phosphodiesterase. These events counteract the regulatory effects of glucagon. Pathway 3: Insulin stimulates increased synthesis of Xylulose-5-phosphate (Xy-5-P). Activation of the insulin receptor results indirectly in increased Xy-5-P synthesis from Glyceraldehyde-3-phosphate and Fructose-6-phosphate. Xy-5-P, a metabolite of the pentose phosphate pathway, stimulates protein phosphatase PP2A. Pathway 4: AMP Kinase (AMPK) mediated response to high AMP:ATP ratio: In response to diet with high fat content or low energy levels, the cytosolic AMP:ATP ratio is increased. AMP triggers a complicated cascade of events. In this module we have annotated only the phosphorylation of ChREBP by AMPK at serine 568, which inactivates this transcription factor. Pathway 5: Dephosphorylation of key metabolic factors by PP2A: Xy-5-P activated PP2A efficiently dephosphorylates phosphorylated PF2K-Pase resulting in the higher output of F-2,6-P2 that enhances PFK activity in the glycolytic pathway. PP2A also dephosphorylates (and thus activates) cytosolic and nuclear ChREBP. Pathway 6: Transcriptional activation of metabolic genes by ChREBP: Dephosphorylated ChREBP activates the transcription of genes involved in glucose metabolism such as pyruvate kinase, and lipogenic genes such as acetyl-CoA carboxylase, fatty acid synthetase, acyl CoA synthase and glycerol phosphate acyl transferase. The illustration below summarizes this network of events. Black lines are metabolic reactions, red lines are negative regulatory events, and green lines are positive regulatory events (figure reused with permission from Veech (2003) - Copyright (2003) National Academy of Sciences, U.S.A.).
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ChREBP (Carbohydrate Response Element Binding Protein) is a large multidomain protein containing a nuclear localization signal near its amino terminus, polyproline domains, a basic helix-loop-helix-leucine zipper domain, and a leucine-zipper-like domain (Uyeda et al., 2002). Its dephosphorylation in response to molecular signals associated with the well-fed state allows it to enter the nucleus, interact with MLX protein, and bind to ChRE DNA sequence motifs near Acetyl-CoA carboxylase, Fatty acid synthase, and Pyruvate kinase (L isoform) genes (Ishi et al.2004). This sequence of events is outlined schematically in the picture below (adapted from Kawaguchi et al. (2001) - copyright (2001) National Academy of Sciences, U.S.A.).
At the end of this reaction, 1 molecule of '1-acyl-sn-glycerol-3-phosphate acyltransferase alpha ' is present. This reaction takes place in the 'nucleus'.
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At the end of this reaction, 1 molecule of 'Acetyl-CoA carboxylase 2 ' is present. This reaction takes place in the 'nucleus'.
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At the end of this reaction, 1 molecule of 'Fatty acid synthase ' is present. This reaction takes place in the 'nucleus'.
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At the end of this reaction, 1 molecule of 'citrate lyase monomer' is present. This reaction takes place in the 'nucleus'.
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PKC beta regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1
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Each molecule of Epac1 binds 1 molecule of cAMP. Epac1 binds cAMP less tightly than PKA binds cAMP so it is believed that Epac1 binds cAMP after PKA is saturated. The binding of cAMP by Epac1 activates the guanyl nucleotide exchange activity of Epac1. Epac1 has also been shown to bind the SUR1 subunit of ATP-gated potassium channels (KATP channels) in beta cells so Epac1 may participate in direct regulation of potassium transport. Epac1 also interacts with the calcium sensor Piccolo in a complex with Rim2 at the cell membrane. This may influence exocytosis of insulin.
Each molecule of Epac2 binds 2 molecules of cAMP. Epac2 binds cAMP less tightly than PKA binds cAMP so it is believed that Epac2 binds cAMP after PKA is saturated. The binding of cAMP by Epac2 activates the guanyl nucleotide exchange activity of Epac2. Epac2 has also been shown to directly bind the SUR1 subunits of ATP-gated potassium channels (KATP channels) in beta cells so Epac2 may regulate potassium transport. Epac2 interacts with the calcium sensor Piccolo in a complex with Rim2 at the cell membrane. This may influence exocytosis of insulin. Epac2 also interacts with the ryanodine-sensitive calcium channel on the ER membrane and may cause release of calcium from the ER into the cytosol.
EPAC1 and EPAC2 are activated by binding cAMP and positively regulate the exchange of GDP for GTP by the small GTPase RAP1A. The downstream effects of RAP1A:GTP in beta cells are uncertain but may involve increasing the number of "restless newcomer" secretory granules near the plasma membrane and thereby increasing secretion of insulin. Other effects of RAP1A :GTP may include regulating beta cell proliferation through activation of the Raf/MEK/ERK mitogenic cascade and activation of the PI3 Kinase/PDK/PKC cell growth pathway.
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Glucagon-like Peptide-1 (GLP-1) is secreted by L-cells in the intestine in response to glucose and fatty acids. GLP-1 circulates to the beta cells of the pancreas where it binds a G-protein coupled receptor, GLP-1R, on the plasma membrane. The binding activates the heterotrimeric G-protein G(s), causing the alpha subunit of G(s) to exchange GDP for GTP and dissociate from the beta and gamma subunits. The activated G(s) alpha subunit interacts with Adenylyl Cyclase VIII (Adenylate Cyclase VIII, AC VIII) and activates AC VIII to produce cyclic AMP (cAMP). cAMP then has two effects: 1) cAMP activates Protein Kinase A (PKA), and 2) cAMP activates Epac1 and Epac2, two guanyl nucleotide exchange factors. Binding of cAMP to PKA causes the catalytic subunits of PKA to dissociate from the regulatory subunits and become an active kinase. PKA is known to enhance insulin secretion by closing ATP-sensitive potassium channels, closing voltage-gated potassium channels, releasing calcium from the endoplasmic reticulum, and affecting insulin secretory granules. The exact mechanisms for PKA's action are not fully known. After prolonged increases in cAMP, PKA translocates to the nucleus where it regulates the PDX-1 and CREB transcription factors, activating transcription of the insulin gene. cAMP produced by AC VIII also activates Epac1 and Epac2, which catalyze the exchange of GTP for GDP on G-proteins, notably Rap1A.. Rap1A regulates insulin secretory granules and is believed to activate the Raf/MEK/ERK mitogenic pathway leading to proliferation of beta cells. The Epac proteins also interact with RYR calcium channels on the endoplasmic reticulum, the SUR1 subunits of ATP-sensitive potassium channels, and the Piccolo:Rim2 calcium sensor at the plasma membrane.
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Activated adenylyl cyclase catalyzes the conversion of one molecule of ATP to one molecule of 3',5'-cyclic AMP (cAMP) and one molecule of pyrophosphate.
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Protein kinase A acts to antagonize voltage-gated potassium channels (Kv channels) by increasing the polarizing voltage required to open them. Maintenance of the Kv channels in the closed state prolongs depolarization and insulin secretion. The exact mechanism of the interaction between PKA and the Kv channels is unknown.
Activated Protein Kinase A promotes the release of calcium from the endoplasmic reticulum into the cytosol. This may be due to phosphorylation of ER calcium channels by PKA, however this has not been demonstrated.
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Human pancreatic beta cells express glucose transporters 1 and (GLUT1, GLUT2), which are responsible for uptake of glucose from the extracellular medium into the cytosol. (Rodent pancreatic beta cells express only Glut2.)
A family of antiport, ATP-ADP translocases, preferentially export ATP from the matrix while importing ADP from the cytosol, thereby maintaining a high ADP:ATP ratio in the matrix. When there are increased energy demands on the body, such as under heavy exercise, cytosolic ADP rises and is exchanged with mitochondrial matrix ATP via the transmembrane ADP:ATP translocase. Increased ADP causes the proton-motive force to be discharged and protons enter via ATPase, thereby regenerating the ATP pool. There are 3 isoforms of translocases in humans; isoform 1 is the heart/skeletal muscle form, isoform 2 is the fibroblast form and isoform 3 is the liver form. All isoforms exist as homodimers. The translocase can adopt 2 different conformations, called the CATR (carboxyatractyloside) and BA (bongkrekic acid) conformations. Amongst the endogenous nucleotides, only ADP and ATP can trigger the rapid conversion between the CATR and BA conformations. The reaction can be summed as below: ADPout + ATPin <-> ADPin + ATPout
Voltage-gated calcium channels respond to a change in voltage across the plasma membrane by opening and allowing free movement of calcium ions. In an unstimulated cell the concentration of calcium ions outside the cells is higher than inside due to calcium transporters so channel opening results in an influx of calcium into the cytosol. In the cytosol the calcium ions cause an immediate exocytosis of the readily releasable pool of docked insulin granules as well as a migration of reserve granules toward the plasma membrane where they will be released during the second, sustained phase of insulin secretion. Mouse and human beta cells are known to contain L type channels Cav1.2 and Cav1.3, both of which have been shown to physically associate with docked insulin granules via Syntaxin1A. Cav1.2 and Cav1.3 predominate in the initial rapid release of insulin. Human beta cells also contain the P/Q type channel Cav2.1 and the R type channel Cav2.3. Cav2.3 is involved in regulating the second, sustained phase of insulin release but signaling and regulatory differences between the two phases of secretion are not fully characterized. Human cells also exhibit T-type (brief burst) calcium currents but the responsible channel has not been identified.
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Sphingomyelin synthase 2 is palmitoylated at the COOH-terminal tail, which is involved in its localization in plasma membranes
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Stable dimeric assembly of the second membrane-spanning domain of CFTR (cystic fibrosis transmembrane conductance regulator) reconstitutes a chloride-selective pore
Insulin/IGF-I and related signaling pathways regulate aging in nondividing cells: from yeast to the mammalian brain
Cytosolic GMP synthase (GMPS) catalyzes the reaction of xanthosine 5'-monophosphate (XMP), ATP, glutamine and water to form guanosine 5'-monophosphate (GMP), AMP, glutamate and pyrophosphate. GMPS is a monomer (Hirst et al. 1994; Nakamura and Lou 1995).
Two human isoenzymes, IMP dehydrogenase 1 and 2 (IMPDH1,2) catalyze the irreversible dehydrogenation of inosine 5'-monophosphate (IMP) to form xanthosine 5'-monophosphate (XMP). The active forms of both isoenzymes are homotetramers, and they are nearly identical in their catalytic efficiencies and their susceptibility to inhibition by XMP (Carr et al. 1993; Colby et al. 1999; Hager et al. 1995). Both enzymes occur as homotetramers (Colby et al. 1999 - IMPDH2; unpubliched data in PDB 1JCN IMPDH1). A variety of experiments suggest that IMPDH1 and 2 have distinct functions in vivo. While IMPDH1 is expressed at constant levels, IMPDH2 is expressed at elevated levels in tumor cells and in mitotic normal cells. In humans, heterozygosity for mutant forms of IMPDH1 is associated with a form of retinitis pigmentosa (Bowne et al. 2002). In laboratory mice, mutations that disrupt the homologue of IMPDH1 have no obvious effect at the level of the whole organism, while ones that disrupt IMPDH2 are lethal (Gu et al. 2003). This reaction is the rate limiting step in the synthesis of guanosine 5'-monophosphate (GMP) from IMP, and GMP competitively inhibits the well-characterized bacterial IMP dehydrogenase enzyme. Evidence for an inhibitory effect of GMP on the human isoenzymes has not been reported. Rather, they appear to be inhibited by XMP; in addition, transcription of one or both IMP dehydrogenase mRNAs may be inhibited by high cellular GMP concentrations (Glesne et al. 1991).
Characterization of kynurenine aminotransferase III, a novel member of a phylogenetically conserved KAT family
The irreversible transfer of a formyl group to cytosolic 5-phosphoribosylglycinamide (GAR) to form 5'-phosphoribosylformylglycinamide (FGAR) is catalyzed by the phosphoribosylglycinamide formyltransferase domain of the trifunctional protein, "phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase" (GART) (Aimi et al. 1990; Zhang et al. 2002). Fluoresence microscopy studies of cultured human cells have shown that GART is cytosolic and suggest that it may co-localize with other enzymes of de novo IMP biosynthesis under some metabolic conditions (Gooljarsingh et al. 2001; An et al. 2008).
The irreversible transfer of an amino group from L-glutamine to 5'-phosphoribosylformylglycinamide (FGAR), forming 5'-phosphoribosylformylglycinamidine (FGAM) and glutamate, accompanied by the conversion of ATP to ADP and orthophosphate, is catalyzed by phosphoribosylformylglycinamidine synthetase. The human enzyme has been purified and characterized biochemically (Barnes et al. 1994). Fluoresence microscopy studies of cultured human cells have shown that the enzyme is cytosolic and suggest that it may co-localize with other enzymes of de novo IMP biosynthesis under some metabolic conditions (An et al. 2008).
The irreversible synthesis of cytosolic 5'-phosphoribosyl-5-aminoimidazole (AIR) from 5'-phosphoribosylformylglycinamidine (FGAM), accompanied by the conversion of ATP to ADP and orthophosphate, is catalyzed by the phosphoribosylaminoimidazole synthetase domain of the trifunctional protein, "phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase" (GART) (Aimi et al. 1990). The active form of the protein is cytosolic and may co-localize with other enzymes of de novo IMP biosynthesis under some metabolic conditions (Gooljarsingh et al. 2001; An et al. 2008).
The reversible carboxylation of 5'-phosphoribosyl-5-aminoimidazole (AIR) to form 5'-phosphoribosyl-5-aminoimidazole-4-carboxylate (CAIR) is catalyzed by the phosphoribosylaminoimidazole carboxylase domain of the bifunctional protein "phosphoribosylaminoimidazole carboxylase, phosphoribosylaminoimidazole succinocarboxamide synthetase" (PAICS) (Schild et al. 1990). The enzyme is an octamer (Li et al. 2007); it may associate in the cytosol with other enzymes of de novo IMP biosynthesis under some metabolic conditions (An et al. 2008).
The conversion of 5'-phosphoribosyl-5-aminoimidazole-4-carboxylate (CAIR) and aspartate to 5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide (SAICAR), accompanied by the conversion of ATP to ADP and orthophosphate, is catalyzed by the phosphoribosylaminoimidazole succinocarboxamide synthetase domain of the bifunctional protein "phosphoribosylaminoimidazole carboxylase, phosphoribosylaminoimidazole succinocarboxamide synthetase" (PAICS) (Schild et al. 1990). The enzyme is an octamer (Li et al. 2007); it may associate in the cytosol with other enzymes of de novo IMP biosynthesis under some metabolic conditions (An et al. 2008).
The reversible conversion of 5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide (SAICAR) to 5'-phosphoribosyl-5-aminoimidazole-4-carboxamide (AICAR) and fumarate is catalyzed by adenylosuccinate lyase. The active form of this enzyme is a cytosolic tetramer (Stone et al. 1993), and fluoresence microscopy of cultured human cells suggests that it may associate with other enzymes of de novo IMP biosynthesis under some metabolic conditions (An et al. 2008). The enzyme also catalyzes the conversion of adenylosuccinate to adenosine 5'-monophosphate and fumarate. Humans lacking the enzyme accumulate dephosphorylated forms of both substrates, indicating that the enzyme mediates both reactions in vivo as well (Race et al. 2000).
The irreversible transfer of a formyl group to 5'-phosphoribosyl-5-aminoimidazole-4-carboxamide (AICAR), to yield 5'-phosphoribosyl-5-formaminoimidazole-4-carboxamide (FAICAR), is catalyzed by the phosphoribosylaminoimidazolecarboxamide formyltransferase activity of the bifunctional 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase enzyme. This cytosolic protein occurs primarily as a dimer (Rayl et al. 1996; Vergis et al. 2001) and may further associate with other enzymes of de novo IMP biosynthesis under some metabolic conditions (An et al. 2008).
The reversible synthesis of inosine 5'-monophosphate from 5'-phosphoribosyl-5-formaminoimidazole-4-carboxamide (FAICAR) is catalyzed by the IMP cyclohydrolase activity of the bifunctional 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase enzyme. This cytosolic protein occurs primarily as a dimer (Rayl et al. 1996; Vergis et al. 2001) and may further associate with other enzymes of de novo IMP biosynthesis under some metabolic conditions (An et al. 2008).
Regulation of heat shock factor trimer formation: role of a conserved leucine zipper
Exploring the role of the active site cysteine in human muscle creatine kinase
Mitochondrial succinate CoA ligase (ADP-forming) catalyzes the reversible conversion of succinyl CoA to succinate plus Coenzyme A, coupled to the conversion of ADP and orthophosphate to ATP. The enzyme is a heterodimer containing SUCLG1 and SUCLA2 monomers. The enzyme catalyzing the reaction in vertebrates is a heterodimer that occurs in two isoforms. The enzymes have been purified from pigeon and rat tissue and characterized in detail. Both isoforms, an alpha:betaA heterodimer and an alpha:betaG heterodimer, catalyze the reversible conversion of succinyl CoA to succinate plus Coenzyme A. The alpha:betaA heterodimer couples this conversion to the synthesis of ATP from ADP and orthophosphate, while the alpha:betaG heterodimer couples it to the synthesis of GTP from GDP and orthophosphate (Johnson et al. 1998a,b; Lambeth et al. 2004). Consistent with these results in model systems, patients homozygous for a mutant allele of the gene encoding the ADP enzyme beta subunit, SUCLA2, are deficient in succinyl CoA ligase activity (Elpeleg et al. 2005). Both isoforms are found in vivo, and appear to be expressed at different levels in various tissues. Their relative contributions to the flux of carbon atoms through the TCA cycle are unknown. Genetic and biochemical data suggest that the alpha:betaA isoform may be required to catalyze the reverse reaction, conversion of succinate, Coenzyme A, and ATP to succinyl CoA, ADP, and orthophosphate for heme biosynthesis (Furuyama and Sassa 2000).
NNT (nicotinamide nucleotide transhydrogenase) associated with the inner mitochondrial membrane catalyzes the reaction of mitochondrial NADPH and NAD+ to form NADP+ and NADH. The reaction is coupled to the translocation of a proton across the inner mitochondrial membrane into the mitochondrial matrix (White et al, 2000). The active form of NNT is inferred to be a homodimer based on the known structure of its bovine homolog (Yamaguchi and Hatefi 1991).
The mitochondrial alpha-ketoglutarate dehydrogenase complex catalyzes the reaction of alpha-ketoglutarate, CoASH, and NAD+ to form succinyl-CoA, CO2, and NADH. The enzyme complex contains multiple copies of three different proteins, E1 (OGDH), E2 (DLST), and E3 (DLD), each with distinct catalytic activities (Reed and Hackert 1990; Zhou et al 2001). The reaction starts with the oxidative decarboxylation of alpha ketoglutarate catalyzed by E1alpha and beta (alpha ketoglutarate dehydrogenase). Lipoamide cofactor associated with E1 is reduced at the same time. Next, the succinyl group derived from alpha ketoglutarate is transferred to coenzyme A in two steps catalyzed E2 (dihydrolipolyl transacetylase). Finally, the oxidized form of lipoamide is regenerated and electrons are transferred to NAD+ in two steps catalyzed by E3 (dihydrolipoyl dehydrogenase). The biochemical details of this reaction have been worked out with alpha ketoglutarate dehydrogenase complex and subunits purified from bovine tissue (McCartney et al. 1998). While all of the human proteins are known as predicted protein products of cloned genes, direct experimental evidence for their functions is available only for E3 (DLD) (Brautigam et al. 2005).
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The succinate dehydrogenase complex, associated with the inner mitochondrial membrane, catalyzes the dehydrogenation of succinate to fumarate, reducing the FAD cofactor bound to the enzyme. This redox potential is then used in the electron transfer chain to drive a proton motive force to generate ATP.
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Mitochondrial citrate synthase dimer catalyzes the irreversible reaction of acetyl-CoA, water, and oxaloacetate to form citrate and coenzyme A. This reaction is the entry point of two-carbon units into the citric acid cycle. The reaction is subject to allosteric regulation. The gene encoding the human enzyme has been cloned (Goldenthal et al. 1998), but the enzyme has not been characterized in detail - its properties are inferred from those of the well-studied homologous pig enzyme (e.g., Morgunov and Srere 1998).
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Mitochondrial isocitrate dehydrogenase IDH2 catalyzes the irreversible reaction of isocitrate and NADP+ to form alpha ketoglutarate, CO2, and NADPH + H+ (Hartong et al. 2008). The structure of the active human enzyme has not been determined experimentally, but is inferred to be a homodimer with one Mn++ bound to each subunit based on detailed studies of the homologous pig enzyme (Ceccarelli et al. 2002). NADP-specific IDH2 was the first isocitrate dehydrogenase isoenzyme to be characterized in biochemical studies of the mammalian TCA cycle (Ochoa 1948). Later work with yeast revealed the existence of both NADP-specific (IDH2-homologous) and NAD-specific (IDH3-homologous) enzymes and demonstrated the ADP-dependence of the latter (Kornberg and Pricer 1951), consistent with the now widely accepted view that IDH3 mediates the conversion of isocitrate to alpha-ketoglutarate in the TCA cycle. The physiological function of IDH2 is thus unclear. The recent observation that individuals homozygous for IDH3 mutations that sharply reduce its activity do not show symptoms of deficient energy metabolism in most tissues raises the possibility that the IDH2 reaction may play an accessory role in the TCA cycle (Hartong et al. 2008).
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Mitochondrial isocitrate dehydrogenase IDH3 catalyzes the irreversible reaction of isocitrate and NAD+ to form alpha ketoglutarate, CO2, and NADH + H+. The enzyme is a heteromer containing four polypeptide chains, two IDH3A, one IDH3B, and one IDH3G, and two Mn++ (Dange and Colman 2010). It is activated by ADP (Soundar et al. 2003, 2006; Bzymek and Colman 2007). This is the first of four oxidation reactions in the citric acid cycle, and the first decarboxylation.
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Mitochondrial aconitase reversibly converts isocitrate to citrate via a cis-aconitate intermediate. Mitochondrial aconitase activity has been demonstrated in diverse human tissue extracts (Slaughter et al. 1975) and a protein homologous to the well-characterized porcine enzyme has been purified from human tissues (Baldwin et al. 1991).
Mitochondrial aconitase reversibly converts citrate to isocitrate via a cis-aconitate intermediate. Mitochondrial aconitase activity has been demonstrated in diverse human tissue extracts (Slaughter et al. 1975) and a protein homologous to the well-characterized porcine enzyme has been purified from human tissues (Baldwin et al. 1991).
Pyruvate (PYR) and a proton are transported from the cytosol into the mitochondrial matrix, mediated by a complex of MCP1 and MCP2 in the inner mitochondrial membrane. Studies of pyruvate uptake in rat indicate that it is specific, saturable, and competitively inhibitable, indicating a specific role for a membrane transport protein (Papa et al. 1971; Halestrap and Denton 1974), and the stoichiometry of the human reaction is inferred from this work. MCP1 and MCP2 have been identified as essential components of the transporter based on the observation that expression of both proteins (but not either one alone) restored mitochondrial pyruvate uptake in mutant budding yeast. The proteins form a multimeric complex; its stoichiometry is unknown (Bricker et al. 2012).
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The mitochondrial pyruvate dehydrogenase complex catalyzes the reaction of pyruvate, CoASH, and NAD+ to form acetylCoA, CO2, and NADH. The enzyme complex contains multiple copies of three different proteins, E1 alpha, E1 beta, E2, and E3, each with distinct catalytic activities (Reed and Hackert 1990; Zhou et al 2001). The reaction starts with the oxidative decarboxylation of pyruvate catalyzed by E1 alpha and beta (pyruvate dehydrogenase). Lipoamide cofactor associated with E1 is reduced at the same time. Next, the acetyl group derived from pyruvate is transferred to coenzyme A in two steps catalyzed by E2 (dihydrolipolyl transacetylase). Finally, the oxidized form of lipoamide is regenerated and electrons are transferred to NAD+ in two steps catalyzed by E3 (dihydrolipoyl dehydrogenase). The biochemical details of this reaction have been worked out with pyruvate dehydrogenase complex and subunits purified from bovine tissue and other non-human sources. Direct evidence for the roles of the corresponding human proteins comes from studies of patients expressing mutant forms of E1 alpha (Lissens et al. 2000), E1 beta (Brown et al. 2004), E2 (Head et al. 2005), and E3 (Brautigam et al. 2005).
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Pyruvate Dehydrogenase Kinase (PDK) in the mitochondrial matrix catalyzes the phosphorylation of serine residues of the E1 alpha subunit of the pyruvate dehydrogenase complex, inactivating it. Pyruvate negatively regulates this reaction, and NADH and acetyl CoA positively regulate it (Bao et al. 2004). Four PDK isoforms have been identified and shown to catalyze the phosphorylation of E1 alpha in vitro (Gudi et al. 1995; Kolobova et al. 2001; Rowles et al. 1996). They differ in their expression patterns and quantitative responses to regulatory small molecules. All four isoforms catalyze the phosphorylation of serine residues 293 ("site 1") and 300 ("site 2"); PDK1 also catalyzes the phosphorylation of serine 232 ("site 3"). Phosphorylation of a single site in a single E1 alpha subunit is sufficient for enzyme inactivation (Bowker-Kinley et al. 1998; Gudi et al. 1995; Kolobova et al. 2001; Korotchkina and Patel, 2001). In the nucleus, cellular retinoic acid-binding protein 1 or 2 (CRABP1 or 2), bound to all-trans-retinoic acid (atRA), directly binds to the heterodimeric complex of retinoic acid receptor alpha RXRA) and peroxisome proliferator-activated receptor delta (PPARD). When bound to PPARD, atRA can significantly increase the expression of proteins involved in energy metabolism such as PDK via its induction of PPARD (Wolf 2010).
Pyruvate dehydrogenase phosphatase (PDP) in the mitochondrial matrix catalyzes the hydrolytic removal of phosphate groups from phosphoserine residues in the E1 alpha subunit of the pyruvate dehydrogenase complex. The active form of PDP is a heterodimer of a catalytic subunit and a regulatory one. Two isoforms of the catalytic subunit have been identified and biochemically characterized (Huang et al. 1998) and mutations in PDP1 have been associated with PDP deficiency in vivo (Maj et al. 2005). The properties of the human regulatory subunit have been deduced from those of its bovine homologue (Lawson et al. 1997). The activity of PDP1 is greatly enhanced through Ca2+ -dependent binding of the catalytic subunit (PDP1c) to the L2 (inner lipoyl) domain of dihydrolipoyl acetyltransferase (E2), which is also integrated in the pyruvate dehydrogenase complex. PDP activity requires Mg2+ (Huang et al. 1998).
The mitochondrial pyruvate dehydrogenase (PDH) complex catalyzes the oxidative decarboxylation of pyruvate, linking glycolysis to the tricarboxylic acid cycle and fatty acid synthesis. PDH inactivation is crucial for glucose conservation when glucose is scarce, while adequate PDH activity is required to allow both ATP and fatty acid production from glucose. The mechanisms that control human PDH activity include its phosphorylation (inactivation) by pyruvate dehydrogenase kinases (PDK 1-4) and its dephosphorylation (activation, reactivation) by pyruvate dehydrogenase phosphate phosphatases (PDP 1 and 2). Isoform-specific differences in kinetic parameters, regulation, and phosphorylation site specificity of the PDKs introduce variations in the regulation of PDC activity in differing endocrine and metabolic states (Sugden and Holness 2003).
Pyruvate sits at an intersection of key pathways of energy metabolism. It is the end product of glycolysis and the starting point for gluconeogenesis, and can be generated by transamination of alanine. It can be converted by the pyruvate dehydrogenase complex to acetyl CoA (Reed and Hackert 1990) which can enter the TCA cycle or serve as the starting point for the syntheses of long chain fatty acids, steroids, and ketone bodies depending on the tissue and metabolic state in which it is formed. It also plays a central role in balancing the energy needs of various tissues in the body. Under conditions in which oxygen supply is limiting, e.g., in exercising muscle, or in the absence of mitochondria, e.g., in red blood cells, re-oxidation of NADH produced by glycolysis cannot be coupled to generation of ATP. Instead, re-oxidation is coupled to the reduction of pyruvate to lactate. This lactate is released into the blood, and is taken up primarily by the liver, where it is oxidized to pyruvate and can be used for gluconeogenesis (Cori 1981).
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AKT/PKB signaling: navigating downstream
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Nitric oxide (NO), a multifunctional second messenger, is implicated in physiological functions in mammals that range from immune response and potentiation of synaptic transmission to dilation of blood vessels and muscle relaxation. NO is a highly active molecule that diffuses across cell membranes and cannot be stored inside the producing cell. Its signaling capacity must be controlled at the levels of biosynthesis and local availability. Indeed, NO production by NO synthases is under complex and tight control, being regulated at transcriptional and translational levels, through co- and posttranslational modifications, and by subcellular localization. NO is synthesized from L-arginine by a family of nitric oxide synthases (NOS). Three NOS isoforms have been characterized: neuronal NOS (nNOS, NOS1) primarily found in neuronal tissue and skeletal muscle; inducible NOS (iNOS, NOS2) originally isolated from macrophages and later discovered in many other cells types; and endothelial NOS (eNOS, NOS3) present in vascular endothelial cells, cardiac myocytes, and in blood platelets. The enzymatic activity of all three isoforms is dependent on calmodulin, which binds to nNOS and eNOS at elevated intracellular calcium levels, while it is tightly associated with iNOS even at basal calcium levels. As a result, the enzymatic activity of nNOS and eNOS is modulated by changes in intracellular calcium levels, leading to transient NO production, while iNOS continuously releases NO independent of fluctuations in intracellular calcium levels and is mainly regulated at the gene expression level (Pacher et al. 2007). The NOS enzymes share a common basic structural organization and requirement for substrate cofactors for enzymatic activity. A central calmodulin-binding motif separates an oxygenase (NH2-terminal) domain from a reductase (COOH-terminal) domain. Binding sites for cofactors NADPH, FAD, and FMN are located within the reductase domain, while binding sites for tetrahydrobiopterin (BH4) and heme are located within the oxygenase domain. Once calmodulin binds, it facilitates electron transfer from the cofactors in the reductase domain to heme enabling nitric oxide production. Both nNOS and eNOS contain an additional insert (40-50 amino acids) in the middle of the FMN-binding subdomain that serves as autoinhibitory loop, destabilizing calmodulin binding at low calcium levels and inhibiting electron transfer from FMN to the heme in the absence of calmodulin. iNOS does not contain this insert. Because NOS enzymatic activity is modulated by the presence of its substrates and cofactors within the cell, under certain conditions, NOS may generate superoxide instead of NO, a process referred to as uncoupling (uncoupling of NADPH oxidation and NO synthesis). The molecular details of eNOS function are annotated here.
Originally identified as endothelium-derived relaxing factor, eNOS derived NO is a critical signaling molecule in vascular homeostasis. It regulates blood pressure and vascular tone, and is involved in vascular smooth muscle cell proliferation, platelet aggregation, and leukocyte adhesion. Loss of the bioavailability of endothelium derived NO is a key feature of endothelial dysfunction and is implicated in the pathogenesis of cardiovascular disease such as hypertension and atherosclerosis. The endothelial isoform eNOS is unique among the nitric oxide synthase (NOS) family in that it is co-translationally modified at its amino terminus by myristoylation and is further acylated by palmitoylation (two residues next to the myristoylation site). These modifications target eNOS to the plasma membrane caveolae and lipid rafts. eNOS activation and subsequent nitric oxide (NO) production is stimulated by a variety of stimuli, such as fluid shear stress generated by blood flow, vascular endothelial growth factor (VEGF), bradykinin, estrogen, insulin, and angiopoietin. The activity of eNOS is further regulated by numerous post-translational modifications, including protein-protein interactions, phosphorylation, and subcellular localization. Following activation, eNOS shuttles between caveolae and other subcellular compartments such as the noncaveolar plasma membrane portions, Golgi apparatus, and perinuclear structures. This subcellular distribution is variable depending upon cell type and mode of activation. Subcellular localization of eNOS has a profound effect on its ability to produce NO as the availability of its substrates and cofactors will vary with location. eNOS is primarily particulate, and depending on the cell type, eNOS can be found in several membrane compartments: plasma membrane caveolae, lipid rafts, and intracellular membranes such as the Golgi complex. In addition, it has been reported that eNOS can also be detected in the nucleus, however, the conditions associated with nuclear localization of eNOS and its precise role in this cell compartment remains to be determined. Several stimuli can trigger a transient displacement of eNOS from the plasma membrane to other subcellular locations. This process can be mediated through various protein-protein interactions and/or changes in post-translational modifications. Knowledge of the precise molecular mechanisms governing the intracellular redistribution process is still rather limited.
Cytosolic lactate dehydrogenase catalyzes the freely reversible reaction of lactate and NAD+ to form pyruvate and NADH + H+. In liver parenchymal cells, this reaction allows lactate from red blood cells and exercising muscle to be converted to pyruvate which in turn is typically used for gluconeogenesis which also consumes the NADH from the reaction. Lactate dehydrogenase is active as a tetramer. Two isoforms of lactate dehydrogenase, A and B, are widely expressed in human tissues, and all five tetramers - A4, A3B, A2B2, AB3, and B4 - are found. A third isoform, C, and its tetramer, C4, are found in testis.
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Cytosolic lactate dehydrogenase catalyzes the reversible reaction of pyruvate and NADH + H+ to form lactate and NAD+. In the body under anaerobic conditions such as are found in red blood cells or rapidly exercising skeletal muscle, this reaction regenerates NAD+, allowing the continuation of glycolysis. Lactate dehydrogenase is active as a tetramer. Two isoforms of lactate dehydrogenase, A and B, are widely expressed in human tissues, and all five tetramers - A4, A3B, A2B2, AB3, and B4 - are found. A third isoform, C, and its tetramer, C4, are found in testis.
The synthesis of cytosolic 5-phosphoribosylglycinamide from 5-phosphoribosylamine and glycine, accompanied by the conversion of ATP to ADP and orthophosphate, is catalyzed by the phosphoribosylglycinamide synthetase domain of the trifunctional protein, "phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase" (GART) (Aimi et al. 1990). The active form of the protein is cytosolic (Gooljarsingh et al. 2001; An et al. 2008).
PRPP stimulates the dissociation of phosphoribosyl pyrophosphate amidotransferase tetramers to form dimers (Holmes et al. 1973a,b).
Cytosolic PPAT (phosphoribosyl pyrophosphate amidotransferase) catalyzes the reaction of 5-phospho-alpha-D-ribose 1-diphosphate (PRPP), water, and L-glutamine to form 5-phosphoribosylamine, L-glutamate, and pyrophosphate. This event is the committed step in de novo purine synthesis. The reaction itself is reversible, but it is pulled strongly in the direction of 5'-phosphoribosylamine synthesis by the irreversible hydrolysis of the pyrophosphate that is also formed in the reaction. Fluoresence microscopy studies of cultured human cells have shown that PPAT is cytosolic and suggest that it may co-localize with other enzymes of de novo IMP biosynthesis under some metabolic conditions (An et al. 2008). The PPAT enzyme is inferred to be an iron-sulfur protein, like its well-characterized B. subtilis homologue, because incubation of purified enzyme with molecular oxygen or chelating agents inactivates it, and activity can be restored by incubation with ferrous iron and inorganic sulfide. The stoichiometry of the iron-sulfur moiety and its role in enzyme activity remain unknown (Itakura and Holmes 1979). The fully active form of the enzyme is a dimer, which can associate further to form a tetramer with sharply reduced activity (Holmes et al. 1973b; Iwahana et al. 1993). Interaction of the enzyme with inosine 5'-monophosphate (IMP), guanosine 5'-monophosphate (GMP), and adenosine 5'-monophosphate (AMP), end products of de novo purine biosynthesis, favors tetramer formation, while interaction with 5-phospho-alpha-D-ribose 1-diphosphate (PRPP), a required substrate, favors formation of the active dimer. Kinetic studies suggest that the enzyme's binding site for GMP and IMP is separate from its AMP binding site (Holmes et al. 1973a).
Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation
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Kinetic analysis of the liver-type (GLUT2) and brain-type (GLUT3) glucose transporters in Xenopus oocytes: substrate specificities and effects of transport inhibitors
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Cytosolic AMP, GMP, and IMP stimulate the association of phosphoribosyl pyrophosphate amidotransferase (PPAT) dimers to form tetramers (Holmes et al. 1973a,b).
The metabolism of pyruvate provides one source of acetyl-CoA which enters the citric acid (TCA, tricarboxylic acid) cycle to generate energy and the reducing equivalent NADH. These reducing equivalents are re-oxidized back to NAD+ in the electron transport chain (ETC), coupling this process with the export of protons across the inner mitochondrial membrane. The chemiosmotic gradient created is used to drive ATP synthesis.
Oxidation of fatty acids and pyruvate in the mitochondrial matrix yield large amounts of NADH. The respiratory electron transport chain couples the re-oxidation of this NADH to NAD+ to the export of protons from the mitochonrial matrix, generating a chemiosmotic gradient across the inner mitochondrial membrane. This gradient is used to drive the synthesis of ATP; it can also be bypassed by uncoupling proteins to generate heat, a reaction in brown fat that may be important in regulation of body temperature in newborn children.
Mitochondria are often described as the "powerhouse" of a cell as it is here that energy is largely released from the oxidation of food. Reducing equivalents generated from beta-oxidation of fatty acids and from the Krebs cycle enter the electron transport chain (also called the respiratory chain). During a series of redox reactions, electrons travel down the chain releasing their energy in controlled steps. These reactions drive the active transport of H+ ions from the mitochondrial matrix , through the inner membrane to the intermembrane space. The respiratory chain consists of five main types of carrier; flavins, iron-sulfur centres, quinones, cytochromes (heme proteins) and copper. The two main reducing equivalents entering the respiratory chain are NADH and FADH2. NADH is linked through the NADH-specific dehydrogenase whereas FADH2 is reoxidised within succinate dehydrogenase and a ubiquinone reductase of the fatty acid oxidation pathway. Oxygen is the final acceptor of electrons and with H+ ions, is converted to form water, the end product of aerobic cellular respiration. A proton electrochemical gradient (often called protonmotive force) is established across the inner membrane, with positive charge in the intermembrane space relative to the matrix. Protons driven by the proton-motive force, can enter ATP synthase thus returning to the mitochondrial matrix. ATP synthases use this exergonic flow to form ATP in the matrix, a process called chemiosmotic coupling. A by-product of this process is heat generation. An antiport, ATP-ADP translocase, preferentially exports ATP from the matrix thereby maintaining a high ADP:ATP ratio in the matrix. The tight coupling of electron flow to ATP synthesis means oxygen consumption is dependent on ADP availability (termed respiratory control). High ADP (low ATP) increases electron flow thereby increasing oxygen consumption and low ADP (high ATP) decreases electron flow and thereby decreases oxygen consumption. There are many inhibitors of mitochondrial ATP synthesis. Most act by either blocking the flow of electrons (eg cyanide, carbon monoxide, rotenone) or uncoupling electron flow from ATP synthesis (eg dinitrophenol). Thermogenin is a natural protein found in brown fat. Newborn babies have a large amount of brown fat and the heat generated by thermogenin is an alternative to ATP synthesis (and thus electron flow only produces heat) and allows the maintenance of body temperature in newborns. The electron transport chain is located in the inner mitochondrial membrane and comprises some 80 proteins organized in four enzymatic complexes (I-IV). Complex V generates ATP but has no electron transfer activity. In addition to these 5 complexes, there are also two electron shuttle molecules; Coenzyme Q (also known as ubiquinone, CoQ) and Cytochrome c (Cytc). These two molecules shuttle electrons between the large complexes in the chain. How many ATPs are generated by this process? Theoretically, for each glucose molecule, 32 ATPs can be produced. As electrons drop from NADH to oxygen in the chain, the number of protons pumped out and returning through ATP synthase can produce 2.5 ATPs per electron pair. For each pair donated by FADH2, only 1.5 ATPs can be formed. Twelve pairs of electrons are removed from each glucose molecule; 10 by NAD+ = 25 ATPs 2 by FADH2 = 3 ATPs. Making a total of 28 ATPs. However, 2 ATPs are formed during the Krebs' cycle and 2 ATPs formed during glycolysis for each glucose molecule therefore making a total ATP yield of 32 ATPs. In reality, the energy from the respiratory chain is used for other processes (such as active transport of important ions and molecules) so under conditions of normal respiration, the actual ATP yield probably does not reach 32 ATPs. The reducing equivalents that fuel the electron transport chain, namely NADH and FADH2, are produced by the Krebs cycle (TCA cycle) and the beta-oxidation of fatty acids. At three steps in the Krebs cycle (isocitrate conversion to oxoglutarate; oxoglutarate conversion to succinyl-CoA; Malate conversion to oxaloacetate), a pair of electrons (2e-) are removed and transferred to NAD+, forming NADH and H+. At a single step, a pair of electrons are removed from succinate, reducing FAD to FADH2. From the beta-oxidation of fatty acids, one step in the process forms NADH and H+ and another step forms FADH2. Cytoplasmic NADH, generated from glycolysis, has to be oxidized to reform NAD+, essential for glycolysis, otherwise glycolysis would cease to function. There is no carrier that transports NADH directly into the mitochondrial matrix and the inner mitochondrial membrane is impermeable to NADH so the cell uses two shuttle systems to move reducing equivalents into the mitochondrion and regenerate cytosolic NAD+. The first is the glycerol phosphate shuttle, which uses electrons from cytosolic NADH to produce FADH2 within the inner membrane. These electrons then flow to Coenzyme Q. Complex I is bypassed so only 1.5 ATPs can be formed per NADH via this route. The overall balanced equation, summing all the reactions in this system, is NADHcytosol + H+cytosol + NAD+mito -> NAD+cytosol + NADHmito + H+mito The malate-aspartate shuttle uses the oxidation of malate to generate NADH in the mitochondrial matrix. This NADH can then be fed directly to complex I and thus can form 3 ATPs via the respiratory chain. The overall balanced equation is NADHcytosol + H+cytosol + FADinner memb -> NAD+cytosol + FADH2 inner memb Both of these shuttle systems regenerate cytosolic NAD+. The entry point for NADH is complex I (NADH dehydrogenase) and the entry point for FADH2 is Coenzyme Q. The input of electrons from fatty acid oxidation via ubiquinone is complicated and not shown in the diagram.
ETF-ubiquinone oxidoreductase (ETF-QO), catalyzes the re-oxidation of reduced ETF, with ubiquinone as the electron acceptor.
Electron transfer flavoprotein, ETF, a 63kDa heterodimer composed of alpha and beta subunit, binds one FAD and one AMP per dimer. ETF resides on the matrix face of the mitochondrial inner membrane. Reducing equivalents from the beta-oxidation of fatty acyl CoAs are transferred to ETF, reducing the ETF-bound FAD to FADH2.
This event is deduced on the basis of bovine experimental data. Complex II (succinate dehydrogenase) transfers electrons from the TCA cycle to ubiquinone. The 6th step in the TCA cycle is where succinate is dehydrogenated to fumarate with subsequent reduction of FAD to FADH2. FADH2 provides the electrons for the transport chain. Succinate dehydrogenase belongs to subclass 1 of the SQR family (succinate:quinone reductase) (classified by Hagerhall, C and Hederstedt, L [1996]). It consists of 4 subunits (referred to as A, B, C and D), all nuclear-encoded and is located on the matrix side of the inner mitochondrial membrane. Subunits A and B are hydrophilic whereas subunits C and D are integral proteins of the inner membrane. SQRs usually contain 3 Fe-S clusters bound by the B subunit. Succinate dehydrogenase contains one [2Fe-2S] cluster, one [4Fe-4S] cluster and one [3Fe-4S] cluster. Additionally, the A subunit has a covalently-bound FAD group. Reduced complex II has this FAD converted to FADH2. The electrons from complex II are transferred to ubiquinone (also called Q, Coenzyme Q or CoQ), a small mobile carrier of electrons located within the inner membrane. Ubiquinone is reduced to ubiquinol during this process.
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Mitotic lamin disassembly is triggered by lipid-mediated signaling
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ADHFE1 catalyzes the reversible reaction of (R)-2-hydroxyglutarate and succinate semialdehyde to form 2-oxoglutarate and 4-hydroxybutyrate (Struys et al. 2005). The localization of human ADHFE1 to the mitochondrial matrix is inferred from the location determined experimentally for its rat homolog (Kaufman et al. 1988).
ADHFE1 catalyzes the reversible reaction of 2-oxoglutarate and 4-hydroxybutyrate to form (R)-2-hydroxyglutarate and succinate semialdehyde (Struys et al. 2005). The localization of human ADHFE1 to the mitochondrial matrix is inferred from the location determined experimentally for its rat homolog (Kaufman et al. 1988).
The two stereoisomers of 2-hydroxyglutarate are normally converted to 2-oxoglutarate in the mitochondrial matrix, and can then be metabolized by the citric acid cycle. The physiological sources of 2-hydroxyglutarate have not been established although plausible hypotheses are that it is generated by lysine breakdown or as a byproduct of delta-aminolevulinate metabolism. The stereoisomers are oxidized to 2-oxoglutarate in FAD-dependent reactions catalyzed by the enzymes D2HGDH (specific for R(-)-2-hydroxyglutarate) and L2HGDH (specific for S(-)-2-hydroxyglutarate). An inherited deficiency in either enzyme is associated with accumulation of 2-hydroxyglutarate and variable neurological symptoms. R(-)-2-hydroxyglutarate also reacts reversibly with succinate semialdehyde to form 4-hydroxybutyrate and 2-oxoglutarate, catalyzed by ADHFE1. No deficiencies of this enzyme have been found in patients with elevated 2-hydroxyglutarate levels (Struys 2006).
Pyruvate metabolism and the citric acid (TCA) cycle together link the processes of energy metabolism in a human cell with one another and with key biosynthetic reactions. Pyruvate, derived from the reversible oxidation of lactate or transamination of alanine, can be converted to acetyl CoA. Other sources of acetyl CoA include breakdown of free fatty acids and ketone bodies in the fasting state. Acetyl CoA can enter the citric acid cycle, a major source of reducing equivalents used to synthesize ATP, or enter biosynthetic pathways. In addition to its role in energy generation, the citric acid cycle is a source of carbon skeletons for amino acid metabolism and other biosynthetic processes. One such process included here is the interconversion of 2-hydroxyglutarate, probably derived from porphyrin and amino acid metabolism, and 2-oxoglutarate (alpha-ketoglutarate), a citric acid cycle intermediate.
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In the citric acid or tricarboxylic acid (TCA) cycle, the acetyl group of acetyl CoA (derived primarily from oxidative decarboxylation of pyruvate, beta-oxidation of long-chain fatty acids, and catabolism of ketone bodies and several amino acids) can be completely oxidized to CO2 in reactions that also yield one high-energy phosphate bond (as GTP or ATP) and four reducing equivalents (three NADH + H+, and one FADH2). The NADH and FADH2 are then oxidized by the electron transport chain to yield nine more high-energy phosphate bonds (as ATP). All reactions of the citric acid cycle take place in the mitochondrion. Eight canonical reactions mediate the synthesis of citrate from acetyl-CoA and oxaloacetate and the metabolism of citrate to re-form oxaloacetate. Six additional reactions are included here. Three reversible reactions, the interconversions of citrate and isocitrate, of fumarate and malate, and of malate and oxaloacetate are annotated in both their canonical (forward) and reverse directions. The synthesis of succinate from succinyl-CoA can be coupled to the phosphorylation of either GDP (the canonical reaction) or ADP; both reactions are annotated. Two mitochondrial isocitrate dehydrogenase isozymes catalyze the oxidative decarboxylation of isocitrate to form alpha-ketoglutarate (2-oxoglutarate): IDH3 catalyzes the canonical reaction coupled to the reduction of NAD+, while IDH2 catalyzes the same reaction coupled to reduction of NADP+, a reaction whose normal physiological function is unclear. Both reactions are annotated. Finally, a reaction is annotated in which reducing equivalents are transferred from NADPH to NAD+ coupled to proton import across the inner mitochondrial membrane. The cyclical nature of the reactions responsible for the oxidation of acetate was first suggested by Hans Krebs, from biochemical studies of pigeon breast muscle (Krebs et al. 1938; Krebs and Eggleston 1940). Many of the molecular details of individual reactions were worked out by Ochoa and colleagues, largely through studies of enzymes purified from pig heart (Ochoa 1980). While the human homologues of these enzymes have all been identified, their biochemical characterization has in general been limited and many molecular details of the human reactions are inferred from those worked out in studies of the model systems.
Mitochondrial malate dehydrogenase catalyzes the reversible reaction of malate and NAD+ to form oxaloacetate and NADH + H+ (Luo et al. 2006). This reaction is highly endergonic but is pulled in the direction annotated here when the TCA cycle is operating. Unpublished crystallographic data indicate that the protein is a dimer (PDB 3E04).
D2HDGH associated with the mitochondrial inner membrane catalyzes the FAD-dependent reaction of (R)-2-hydroxyglutarate to form 2-oxoglutarate (Achouri et al. 2004). D2HDGH mutations are associated with high levels of (R)-2-hydroxyglutarate in vivo and variable neurological symptoms (Struys et al. 2005; Wanders and Mooyer 1995)).
L2HDGH associated with the mitochondrial inner membrane catalyzes the FAD-dependent reaction of (S)-2-hydroxyglutarate to form 2-oxoglutarate (Rzem et al. 2006). L2HDGH mutations are associated with high levels of (S)-2-hydroxyglutarate in vivo and variable neurological symptoms (Rzem et al. 2004; Topcu et al. 2004).
Mitochondrial fumarate hydratase catalyzes the reversible reaction of malate to form fumarate and water (Bourgeron et al. 1994). Unpublished crystallographic data indicate that the protein is a tetramer (PDB 3E04).
Mitochondrial fumarate hydratase catalyzes the reversible reaction of fumarate and water to form malate, the seventh step of the TCA cycle (Bourgeron et al. 1994). Unpublished crystallographic data indicate that the protein is a tetramer (PDB 3E04).
Cell lines from kidney proximal tubules of a patient with Lowe syndrome lack OCRL inositol polyphosphate 5-phosphatase and accumulate phosphatidylinositol 4,5-bisphosphate
Isozymes of human phosphofructokinase in blood cells and cultured cell lines: molecular and genetic evidence for a trigenic system
At the late endosome membrane, the PAS complex, consisting of FYVE finger-containing phosphoinositide kinase (PIKFYVE), yeast VAC14 homologue (VAC14), and polyphosphoinositide phosphatase aka SAC3 (FIG4), binds to the membrane via PIKFYVE's FYVE finger. The FIG4 phosphatase component dephosphorylates phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) to phosphatidylinositol 3-phosphate (PI3P) (Sbrissa et al. 2007, Sbrissa et al. 2008).
At the late endosome membrane, the PAS complex, consisting of FYVE finger-containing phosphoinositide kinase (PIKFYVE), yeast VAC14 homologue (VAC14), and polyphosphoinositide phosphatase aka SAC3 (FIG4), binds to the membrane via PIKFYVE's FYVE finger (Sbrissa et al. 2002, Cao et al. 2007). The PIKFYVE kinase component phosphorylates phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol 3,5-bisphosphate PI(3,5)P2 (Sbrissa et al. 1999). The PAS complex is present in the cytosol and is recruited to the membrane (Sbrissa et al. 2007).
At the early endosome membrane, phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) is generated in two steps from phosphatidylinositol 3,4-bisphosphate PI(3,4)P2 by the action of various kinases and phosphatases (Sbrissa et al. 2007, Sbrissa et al. 2008, Cao et al. 2007, Cao et al. 2008, Arcaro et al. 2000, Kim et al. 2002).
At the early endosome membrane, phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha (PIK3C2A) (Kraq et al. 2010, Arcaro et al. 2000) phosphorylates phosphatidylinositol 4-phosphate (PI4P) to phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2).
At the early endosome membrane, phosphatidylinositol 4-kinase type 2-alpha/beta (PI4K2A/B) (Balla et al. 2002) phosphorylates phosphatidylinositol (PI) to produce phosphatidylinositol 4-phosphate (PI4P).
At the early endosome membrane, myotubularin (MTM1), myotubularin-related protein 2 (MTMR2), and myotubularin-related protein 4 (MTMR4) dephosphorylate phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol (PI). The following lists the above proteins with their corresponding literature references: MTM1 (Cao et al. 2007, Cao et al. 2008, Kim et al. 2002), MTMR2 (Cao et al. 2008, Kim et al. 2002), and MTMR4 (Lorenzo et al. 2006, Zhao et al. 2001).
At the early endosome membrane, phosphatidylinositol 3-kinase catalytic subunit type 3 (PIK3C3) aka VPS34 binds to phosphoinositide 3-kinase regulatory subunit 4 (PIK3R4). The PIK3C3:PIK3R4 complex and phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha (PIK3C2A) phosphorylate phosphatidylinositol (PI) to phosphatidylinositol 3-phosphate (PI3P). The following lists the above proteins with their corresponding literature references: PIK3C3:PIK3R4 complex (Panaretou et al. 1997, Volinia et al. 1995, Cao et al. 2007) and PIK3C2A (Arcaro et al. 2000, Domin et al. 2000).
At the early endosome membrane, myotubularin (MTM1), myotubularin-related protein 2 (MTMR2) and myotubularin-related protein 4 (MTMR4) dephosphorylate phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) to phosphatidylinositol 5-phosphate (PI5P). The following lists the above proteins with their corresponding literature references: MTM1 (Cao et al. 2007, Cao et al. 2008), MTMR2 (Cao et al. 2008), and MTMR4 (Lorenzo et al. 2006).
At the early endosome membrane, the PAS complex, consisting of FYVE finger-containing phosphoinositide kinase (PIKFYVE), yeast VAC14 homologue (VAC14), and polyphosphoinositide phosphatase aka SAC3 (FIG4), binds to the membrane via PIKFYVE's FYVE finger. The FIG4 phosphatase component dephosphorylates phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) to phosphatidylinositol 3-phosphate (PI3P) (Sbrissa et al. 2007, Sbrissa et al. 2008).
Deletion of mouse Porcn blocks Wnt ligand secretion and reveals an ectodermal etiology of human focal dermal hypoplasia/Goltz syndrome
Proc. Natl. Acad. Sci. U.S.A. 108:12752-7
At the early endosome membrane, the PAS complex, consisting of FYVE finger-containing phosphoinositide kinase (PIKFYVE), yeast VAC14 homologue (VAC14), and polyphosphoinositide phosphatase aka SAC3 (FIG4), binds to the membrane via PIKFYVE's FYVE finger (Sbrissa et al. 2002, Cao et al. 2007). The PIKFYVE kinase component phosphorylates phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol 3,5-bisphosphate PI(3,5)P2 (Sbrissa et al. 1999). The PAS complex is present in the cytosol and is recruited to the membrane (Sbrissa et al. 2007).
The TRPC3/6/7 subfamily of cation channels
LDL receptor-related proteins 5 and 6 in Wnt/beta-catenin signaling: arrows point the way
Selective inhibition of heterotrimeric Gs signaling. Targeting the receptor-G protein interface using a peptide minigene encoding the Galpha(s) carboxyl terminus
Tyrosine residues in phospholipase Cgamma 2 essential for the enzyme function in B-cell signaling
Ankyrins link voltage-gated sodium and potassium channels to spectrin and L1
L1 linked to actin cytoskeleton by ankyrin
Nuclear translocation of hypoxia-inducible factors (HIFs): involvement of the classical importin alpha/beta pathway
A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers
ITSN1 exchanges GTP for GDP on CDC42, activating it
p120-RasGAP exchanges GTP for GDP on RAS, inactivating it
Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1
p-TIAM1 exchanges GTP for GDP on RAC1, activating it
p190RhoGEF exchanges GTP for GDP on RHOA, activating it
LIMK phosphorylates CFL1, inactivating it
Cis-heterodimerization of L1 and Axonin-1
Cis-heterodimerization of L1 and Contactin-1/F3/F11
FYVE-DSP2, a FYVE domain-containing dual specificity protein phosphatase that dephosphorylates phosphotidylinositol 3-phosphate
Neurofascin and NrCAM heterodimerization
Doublecortin binds phosphorylated neurofascin
Ephrin-B ligands interacts with EPHB receptors
Stabilin-1 mediates phosphatidylserine-dependent clearance of cell corpses in alternatively activated macrophages
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Removal of fibrillar collagen C-propeptides
Formation of dehydro-hydroxylysino-norleucine cross-links
Formation of lysino-5-ketonorleucine cross-links
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Formation of dehydro-lysinonorleucine cross-links
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Formation of hydroxylysyl-pyridinoline cross-links
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Formation of hydroxylysino-5-ketonorleucine cross-links
Formation of lysyl-pyridinoline cross-links
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Formation of hydroxylysyl-pyrrole cross-links
Collagen prolyl 3-hydroxylase converts proline to 3-hydroxyproline
Procollagen lysyl hydrolases convert lysine to 5-hydroxylysine
Galactosylation of collagen propeptide hydroxylysines by procollagen galactosyltransferases 1, 2.
Galactosylation of collagen propeptide hydroxylysines by PLOD3
Glucosylation of collagen propeptide hydroxylysines
Removal of fibrillar collagen N-propeptides
Cloning of the human kidney PAH transporter: narrow substrate specificity and regulation by protein kinase C
Characterization of a cDNA encoding a novel human Golgi alpha 1, 2-mannosidase (IC) involved in N-glycan biosynthesis
Phosphorylated FOXO1A is excluded from the nucleus
Phosphorylation of E proteins by p38 MAPK
Heterodimerization of E proteins with Myod
VAV exchanges GTP for GDP on RAC1, activating it
Collagen prolyl 4-hydroxylase converts proline to 4-hydroxyproline
PDI is a chaperone for collagen peptides
Phospho R-SMAD(SMAD2/3):CO-SMAD(SMAD4):FOXO3 binds FoxO3a-binding elements
bPIX exchanges GTP for GDP on RAC, activating it
Characterization of the monomethylarsonate reductase and dehydroascorbate reductase activities of Omega class glutathione transferase variants: implications for arsenic metabolism and the age-at-onset of Alzheimer's and Parkinson's diseases
Prostaglandin D2 (PGD2) is a structural isomer of prostaglandin E2 (PGE2). There is a 9-keto and 11-hydroxy group on PGE2 with these substituents reversed on PGD2. PGD2 is formed by two evolutionarily distinct, but functionally convergent, prostaglandin D synthases: lipocalin-type prostaglandin-D synthase aka Prostaglandin-H2 D-isomerase (PTDGS) and hematopoietic prostaglandin D synthase (HPGDS). One of the main differences between these two proteins is that HPGDS requires glutathione (GSH) for catalysis while PTDGS can function without this cofactor. Here, HPGDS with GSH promotes the isomerisation of prostaglandin H2 (PGH2) to prostaglandin D2 (PGD2) (Jowsey et al. 2001, Inoue et al. 2003).
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Prostaglandin E2 (PGE2) is the most abundant prostanoid in the body and is a major mediator of inflammation in diseases such as osteoarthritis and rheumatoid arthritis. The product of arachidonic acid, prostaglandin H2 (PGH2) serves as the substrate for the isomerization to PGE2. The conversion is carried out by prostaglandin E synthase (PGES), of which there are three forms. Two are membrane-bound enzymes and are designated as mPGES-1 (functionally linked with COX-2) and mPGES-2 (golgi membrane-associated, functionally coupled with both COX-1 and COX-2). The other is cytosolic (cPGES, PTGES3) and functionally linked to COX-1 to produce PGE2 immediately. In this reaction, cPGES is used for conversion of PGH2 to PGE2.
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Thromboxane synthase (TBXAS1) aka CYP5A1 facilitates rearrangement of the PGH2 endoperoxide bridge by a complementary mechanism to prostacyclin synthase, interacting with the C-9 oxygen to promote endoperoxide bond cleavage. The C-11 oxygen radical initiates intramolecular rearrangement, resulting in either the formation of thromboxane A2 (TXA2) or 12-hydroxyheptadecatrienoic acid (12S-HHT) and malonaldehyde (MDA) (Wang et al. 2001).
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Thromboxane synthase (TBXAS1) aka CYP5A1 mediates the isomerization of prostaglandin H2 (PGH2) to thromboxane A2 (TXA2) (Miyata et al. 2001, Chevalier et al. 2001). This reaction is not coupled with any P450 reductase proteins nor consumes NADPH.
Prior to this reaction all the enzymes involved in the desaturation and elongation of linoleic acid are located in the ER, but for this last step tetracosapentaenoyl-CoA must be transferred to the peroxisomes for partial beta-oxidation to docosapentaenoyl-CoA (DPA-CoA, 4,7,10,13,16-22:5(n-6)) (Su et al. 2001).
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Tetracosatetraenoyl-CoA is further desaturated by delta 6-desaturase (FADS2) to tetracosapentaenoyl-CoA (TPA-CoA, 6,9,12,15,18-24:5(n-6)).
Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.
There are two major classes of polyunsaturated fatty acids (PUFAs): the omega-3 (n-3) and the omega-6 (n-6) fatty acids, where the number corresponds to the position of the first double bond proximate to the methyl end of the fatty acid. Omega-3 and omega-6 fatty acids are considered essential fatty acids. Humans cannot synthesize them, instead they are supplied through diet. Linoleic acid (LA, 18:2(n-6)), a major component of omega-6 fatty acids and alpha-linolenic acid (ALA, 18:2(n-3)) a major component of omega-3 fatty acids are the two main dietary essential fatty acids (EFAs) in humans. ALA and LA obtained from diet are converted in the body into their longer chain and more unsaturated omega-3 and omega-6 products by a series of desaturation and elongation steps. Metabolism of ALA and LA to their corresponding products is mediated via common enzyme systems. In humans ALA is finally converted to docosahexaenoic acid (DHA, C22:6(n-3)), and LA is converted to docosapentaenoic acid (DPA, C22:5(n-6)). The intermediary omega-3 and omega-6 series fatty acids play a significant role in health and disease by generating potent modulatory molecules for inflammatory responses, including eicosanoids (prostaglandins, and leukotrienes), and cytokines (interleukins) and affecting the gene expression of various bioactive molecules (Kapoor & Huang 2006, Sprecher 2002, Burdge 2006).
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Linoleic acid (LA, 18:2(n-6)) is an omega-6 fatty acid obtained through diet, mainly from vegetable oils. Omega-6 fatty acids helps stimulate skin and hair growth, maintain bone health, regulate metabolism, and maintain the reproductive system. All the desaturation and elongation steps occur in the endoplasmic reticulum (ER) except for the final step which requires translocation to peroxisomes for partial beta-oxidation. The linoleic acid pathway involves the following steps: 18:2(n-6)-->18:3(n-6)--> 20:3(n-6)-->20:4(n-6)-->22:4(n-6)-->24:4(n-6)-->24:5(n-6)-->22:5(n-6). Two desaturation enzymes are involved in this process: delta-6 desaturase which converts 18:2(n-6) to 18:3 (n-6) and 24:4(n-6) to 24:5(n-6) respectively, and delta-5 desaturase which converts 20:3(n-6) to 20:4(n-6). (Sprecher 2002).
Casein kinase II phosphorylates the neural cell adhesion molecule L1
The first major step in the metabolism of linoleic acid (LA) is desaturation of delta 9,12-octadecadienoyl CoA/linoleoyl CoA (LA-CoA) to delta 6,9,12-octodecatrienoyl CoA/gamma-lenoleoyl CoA (GLA-CoA). This step is catalyzed by delta-6-destaurase (fatty acid desaturase-2, FADS2) which introduces a cis-double bond between carbons 6 and 7. This is the rate limiting step in LA metabolism (Horrobin 1993).
DGL-CoA (8,11,14-eicosatrienoyl-CoA) undergoes desaturation by delta 5-desaturase (D5-desaturase) forming arachidonoyl-CoA (AA-CoA, 5,8,11,14-Eicosatetraenoic acid). D5-desaturase has 62% sequence identity with D6-desaturase but desaturates a different carbon atom, adding a double bond at position C5 in arachidonoyl-CoA (AA-CoA). AA can be metabolized by variety of oxygenases (including cyclo-oxygenase and lipoxygenase systems) to form a family of varying products known as eicosanoids, prostaglandins, leukotrines and thromboxanes thus playing important role in inflamation response.
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Alpha-linolenic acid (ALA, 18:3(n-3)) is an omega-3 fatty acid, supplied through diet as it cannot be synthesized by humans. ALA has an important role in human health. It is converted to long chain more unsaturated n-3 fatty acids by a series of alternating desaturation and elongation reactions. Omega-3 products of ALA such as eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) reduce inflammation and may help lower risk of chronic diseases, such as heart disease and arthritis. All the desaturation and elongation steps occur in the endoplasmic reticulum (ER) except for the final step which requires translocation to peroxisomes for partial beta-oxidation. The alpha-linolenic acid pathway involves the following steps: 18:3(n-3)--> 18:4(n-3)-->20:4(n-3)-->20:5(n-3)-->22:5(n-3)-->24:5(n-3)-->24:6(n-3)-->22:6(n-3). Two desaturation enzymes are involved in this process: delta-6 desaturase that converts 18:3(n-3) to 18:4(n-3) and 24:5(n-3) to 24:6(n-3) respectively, delta-5 desaturase 20:4(n-3) to 20:5(n-3). (Sprecher 2002).
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DHA-CoA preferentially moves back to the ER, perhaps as a free fatty acid. This conversion is usually catalysed by acyl-CoA thioesterases (ACOTs). No specific acyl-CoA thioesterase enzyme has been identified for the peroxisomal metabolism of DHA-CoA, but the peroxisomal ACOT8 has a wide substrate specificity and is likely to be responsible (Ferdinandusse et al. 2003, Hunt & Alexson. 2008).
The final step in the beta-oxidation process is the thiolytic cleavage of 1-(3-oxo-6Z,9Z,12Z,15Z,18Z,21Z-tetracosahexaenoyl)-CoA to form docosahexaenoyl-CoA (DHA-CoA). This step is catalysed by both sterol carrier protein X (SCPx) and the classic 3-ketoacyl-CoA thiolase (this reaction) (Ferdinandusse et al. 2001).
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The final step in the beta-oxidation process is the thiolytic cleavage of 1-(3-oxo-6Z,9Z,12Z,15Z,18Z,21Z-tetracosahexaenoyl)-CoA to form docosahexaenoyl-CoA (DHA-CoA). This step is catalysed by both sterol carrier protein X (SCPx) (this reaction) and the classic 3-ketoacyl-CoA thiolase (Ferdinandusse et al. 2001).
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3-hydroxy tetracosahexaenoyl-CoA undergoes dehydrogenation to form 1-(3-oxo-6Z,9Z,12Z,15Z,18Z,21Z-tetracosahexaenoyl)-CoA, catalysed by DBP. DBP is a bifunctional enzyme, involved in the hydration of a variety of trans-2,3-dehydroacyl-CoA's but also mediating dehydrogenation of a variety of 3-hydroxyacyl-CoA's (Jiang et al. 1997).
Delta2-THA-CoA is hydrated to 3-hydroxyacyl-CoA intermediate 1-(3-hydroxy-6Z,9Z,12Z,15Z,18Z,21Z-tetracosahexaenoyl)-CoA by HSD17B4/DBP (d-bifunctional protein) dimer.
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Retroconversion of C24:6(n-3) to docosahexaenoic acid (22:6(n-3) involves the initial oxidation of tetracosahexaenoyl-CoA to an intermediate 1-(2E,6Z,9Z,12Z,15Z,18Z,21Z-tetracosaheptaenoyl)-CoA (delta2-THA-CoA). This step is catalysed by the peroxisomal enzyme Straight-chain acyl-CoA oxidase (SCOX) (Ferdinandusse et al. 2001).
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The 24-carbon tetracosahexaenoyl-CoA (6,9,12,15,18,21-24:6(n-3) is transported to peroxisomes to undergo a putative single cycle of peroxisomal beta-oxidation, producing Docosahexaenoic Acid (DHA) (Sprecher 2002, Luthria et al. 1996).
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The dietary essential fatty acid (EFA) linoleic acid (LA) is activated to a high energy form known as linoleoyl-CoA by the action of long-chain acyl-CoA synthetases (ACSLs). Thioesterification of long-chain fatty acids into their acyl-CoA derivatives is considered to be the first committed step in fatty acid metabolism. Formation of acyl-CoA allows an otherwise non-reactive fatty acid to participate in biosynthetic or catabolic pathways. This acyl CoA form is converted to its longer-chain polyunsaturated products by a series of desaturation and elongation reactions (Ellis et al. 2010, Watkins 2008).
Tetracosapentaenoyl-CoA (9,12,15,18,21-24:5(n-3)) is further converted by delta 6-desaturase (FADS2) to tetracosahexaenoyl-CoA (6,9,12,15,18,21-24:6(n-3)).
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At the late endosome membrane, the PAS complex, consisting of FYVE finger-containing phosphoinositide kinase (PIKFYVE), yeast VAC14 homologue (VAC14), and polyphosphoinositide phosphatase aka SAC3 (FIG4), binds to the membrane via PIKFYVE's FYVE finger. The PIKFYVE kinase component phosphorylates phosphatidylinositol (PI) to phosphatidylinositol 5-phosphate (PI5P) (Sbrissa et al. 1999, Sbrissa et al. 2002). The PAS complex is present in the cytosol and is recruited to the membrane.
At the late endosome membrane, myotubularin (MTM1), myotubularin-related protein 2 (MTMR2), myotubularin-related protein 4 (MTMR4), and myotubularin-related protein 7 (MTMR7) dephosphorylate phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) to phosphatidylinositol 5-phosphate (PI5P). The following lists the above proteins with their corresponding literature references: MTM1 (Cao et al. 2007, Cao et al. 2008, Tsujita et al. 2004, Tronchere et al. 2004), MTMR2 (Cao et al. 2008), MTMR4 (Lorenzo et al. 2006), and MTMR7 (Mochizuki & Majerus 2003, Lorenzo et al. 2006).
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At the late endosome membrane, myotubularin (MTM1), myotubularin-related protein 2 (MTMR2), myotubularin-related protein 4 (MTMR4), and myotubularin-related protein 7 (MTMR7) dephosphorylate phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol (PI). The following lists the above proteins with their corresponding literature references: MTM1 (Cao et al. 2007, Cao et al. 2008, Tsujita et al. 2004, Tronchere et al. 2004, Kim et al. 2002); MTMR2 (Cao et al. 2008, Kim et al. 2002); MTMR4 (Lorenzo et al. 2006); and MTMR7 (Mochizuki & Majerus 2003, Lorenzo et al. 2006).
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At the late endosome membrane, phosphatidylinositol 3-kinase catalytic subunit type 3 (PIK3C3) aka VPS34 binds to phosphoinositide 3-kinase regulatory subunit 4 (PIK3R4). The PIK3C3:PIK3R4 complex and phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha (PIK3C2A) phosphorylate phosphatidylinositol (PI) to phosphatidylinositol 3-phosphate (PI3P). The following lists the above proteins with their corresponding literature references: PIK3C3:PIK3R4 (Panaretou et al. 1997, Volinia et al. 1995, Cao et al. 2007) and PIK3C2A (Arcaro et al. 2000, Domin et al. 2000).
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Phosphatidylinositol (PI), a membrane phospholipid, can be reversibly phosphorylated at the 3, 4, and 5 positions of the inositol ring to generate seven phosphoinositides: phosphatidylinositol 3-phosphate (PI3P), phosphatidylinositol 4-phosphate (PI4P), phosphatidylinositol 5-phosphate (PI5P), phosphatidylinositol 3,4-bisphosphate PI(3,4)P2, phosphatidylinositol 4,5-bisphosphate PI(4,5)P2, phosphatidylinositol 3,5-bisphosphate PI(3,5)P2, and phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3). These seven phosphoinositides, which are heterogeneously distributed within cells, can serve as signature components of different intracellular compartment membranes and so help to mediate specificity of membrane interactions. Phosphoinositide levels are tightly regulated spatially and temporally by the action of various kinases and phosphatases whilst PI(4,5)P2 is also a substrate for phospholipase C. The differential localisation of each of these enzymes on specific compartment membranes ensures maintenance of the heterogeneous distribution of phosphoinositides despite the continuous membrane flow from one compartment to another. PI is primarily synthesised in the endoplasmic reticulum from where the phospholipid is exported to other compartments via membrane traffic or via cytosolic phospholipid transfer proteins. Phosphorylation of PI to PI4P primarily occurs in the Golgi, where PI4P plays an important role in the biogenesis of transport vesicles such as the secretory vesicle involved in its transport to the plasma membrane. At this place, PI4P has a major function acting as a precursor of PI(4,5)P2, which is located predominantly at this membrane. PI(4,5)P2 binds and regulates a wide range of proteins that function on the cell surface and serves as a precursor for second messengers. Additionally, it helps define this membrane as a target for secretory vesicles, functions as a coreceptor in endocytic processes, and functions as a cofactor for actin nucleation. At the plasma membrane, PI(4,5)P2 is further phosphorylated to PI(3,4,5)P3, another phosphoinositide with important signalling functions including stimulating cell survival and proliferation. The inositol 3-phosphatase, phosphatase and tensin homolog (PTEN) regenerates PI (4,5)P2, while the 5-phosphatases convert PI(3,4,5)P3 into the phosphoinositide, PI(3,4)P2, propagating the signal initiated by PI(3,4,5)P3. PI(3,4)P2 is further dephosphorylated in the endocytic pathway by inositol 4-phosphatases to PI3P, the signature phosphoinositide of the early endosomal compartment and a ligand for numerous endosomal proteins. However, the bulk of PI3P is generated directly in the endosomes by phosphorylation of PI. The subsequent endosomal phosphorylation of PI3P to PI(3,5)P2 is believed to generate docking sites for recruitment of cytosolic factors responsible for the control of outgoing traffic from the endosomes. The main localisation and function of the low abundance phosphoinositide PI5P, that can be generated by several pathways, remains to be determined (Krauss & Haucke 2007, Leventis & Grinstein 2010, Roth 2004, Gees et al. 2010, De Matteis & Godi 2004, van Meer et al. 2008, Vicinanza et al. 2008, Lemmon 2008, Kutaleladze 2010, Robinson & Dixon 2006, Blero et al. 2007, Liu & Bankaitis 2010, McCrea & De Camilli 2009, Vicinanza et al. 2008, Di Paolo & De Camilli, 2006).
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At the late endosome membrane, the primary event is the dephosphorylation of the phosphoinositide phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) to phosphatidylinositol 3-phosphate (PI3P) and phosphatidylinositol 5-phosphate (PI5P) (Sbrissa et al. 2007, Sbrissa et al. 2008, Cao et al. 2007, Cao et al. 2008, Arcaro et al. 2000, Kim et al. 2002).
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In the first step the precursor apha-linolenic (9,12,15-18:3(n-3)) acid is activated to a high energy form known as alpha-linolenoyl-CoA (9Z,12Z,15Z-octadecatrienoyl-CoA) by the iron enzyme long-chain-fatty-acid-CoA-ligase (acyl-CoA synthetase 1, ACSL1) and coenzyme A.
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Phospholipids contain a polar head group and two long-chain fatty acyl moieties, one of which is generally unsaturated. The head group is a glycerol or serine phosphate attached to a polar group such as choline. These molecules are a major constituent of cellular membranes, where their diverse structures and asymmetric distributions play major roles in determining membrane properties (Dowhan 1997). The four major classes of phospholipids in human plasma membranes are phosphatidylethanolamine, phosphatidylserine, phosphatidylcholine, and sphingomyelin. The first three are derivatives of glycerol while sphingomyelin is a derivative of serine. Here, pathways for the metabolism of glycerophospholipids, phosphphatidylinositol (PI), and sphingolipids are annotated.
Eicosatetraenoyl-CoA (ETA-CoA) is desaturated by an additional carbon-carbon bond to form 5Z,8Z,11Z,14Z,17Z-eicosapentaenoyl-CoA (EPA-CoA, 5,8,11,14,17-20:5(n-3)). Delta-5-desaturase is required for this conversion. EPA-CoA has health benefits due to its anti-inflammatory actions. It is a precursor for the anti-inflammatory series-3 prostaglandins (PG), the series-5 leukotrienes (LT) and the series-3 thromboxanes (TA), which are anti-atherogenic and anti-thrombogenic (Ross et al. 2009).
Alpha-linoloyl-CoA is converted to Stearidonoyl-CoA (SDA, 6,9,12,15-18:3(n-3)) by delta-6-destaurase (fatty acid desaturase-2, FADS2). FADS2 uses the cytochrome b5 system to add a double bond at position 6. This is the rate limiting step in alpha-linolenic acid (ALA) metabolism (Horrobin 1993).
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DDR1 binds collagen type I, II, III, IV, V, XI fibrils
Discoidin domain receptor 1 binds collagens
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Collagen IX is cross-linked to the surface of collagen type II fibrils
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Collagen XI cross-links with collagen II
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Type XII and XIV collagens associate with type I and type II fibrils.
Formation of histidino-hydroxylysinonorleucine cross-links
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Gangliosides are glycosphingolipids in which oligosaccharide chains containing N-acetylneuraminic acid (NeuNAc) are attached to a ceramide. The prototypical ganglioside GM1 can be hydrolysed to the GM2 ganglioside by beta-galactosidase (GLB1), cleaving off the terminal galactose (Asp et al. 1969). Defects in GLB1 causes the lysosomal storage diseases GM1-gangliosidosis (Yoshida et al. 1991) and Morquio syndrome B (Oshima et al. 1991).
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The main steps involved in de novo sphingolipid synthesis are annotated here (Merrill 2002, Gault et al. 2010).
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SGPL1 (sphingosine-1-phosphate lyase 1), associated with the endoplasmic reticulum membrane, catalyzes the cleavage of cytosolic sphingosine 1-phosphate to form phosphoethanolamine and hexadec-2-enal (Van Veldhoven et al. 2000; Fyrst and Saba 2008).
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PPAP2A (phosphatidate phosphohydrolase type 2A) enzyme associated with the plasma membrane catalyzes the hydrolysis of extracellular sphingosine 1-phosphate to form sphingosine and orthophosphate (Roberts et al 1998).
PPAP2A, B, and C (phosphatidate phosphohydrolase type 2A, B, and C) enzymes associated with the plasma membrane catalyze the hydrolysis of cytosolic sphingosine 1-phosphate to form sphingosine and orthophosphate (Roberts et al 1998).
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SPHK1 and 2 (sphingosine kinases 1 and 2) catalyze the reaction of sphingosine and ATP to form sphingosine 1-phosphate and ADP. Both enzymes are found in the cytosol (although they are also present in membrane-associated forms). Both enzymes also catalyze the phosphorylation of sphinganine (dihydrosphingosine) (Liu et al. 2000; Nava et al. 2000; Pitson et al. 2000).
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Alpha-galactosidase A (GLA) (Bishop et al. 1986) removes the terminal galactose residue from glycolipids or glycoproteins resulting in galactose and an alcohol. An example is the Fabry disease substrate globotriaosylceramide (Gb3Cer) which is hydrolysed to form galactose and lactosylceramide. GLA functions as a homodimer (Garman & Garboczi 2004) and defects in this enzyme lead to Fabry disease (FD) (MIM:301500), a rare X-linked sphingolipidosis disease where glycolipids such as GB3 accumulate in many tissues (Garman & Garboczi 2004, Eng et al. 1993). Multiple mutations in GLA can cause the disease symptoms of Fabry disease (Shabeer et al. 2006).
Galactocerebrosidase (GALC) hydrolyses the galactosyl moiety from galactocerebroside (also called galactosylceramide, GalCer) to form ceramide (Sakai et al. 1994). Defects in GALC are the cause of leukodystrophy globoid cell (GLD) (MIM:245200), also called Krabbe disease (Wenger et al. 1997).
Beta-galactosidase can hydrolyse a galactose moeity from globosides to form cerebrosides. Here, lactosylceramide is hydrolysed to glucosylceramide (Asp et al. 1969).
There are two major forms of bHEX: hexosaminidase A and B. The A form is a trimer of the subunits alpha, beta A and beta B. The B form is a tetramer of 2 beta A and 2 beta B subunits (O'Dowd et al. 1988, Mahuran et al. 1988). Both are able to cleave GalNAc from globoside (a glycosphingolipid with more than one sugar attached as the side chain). Here, globoside is cleaved to form Gb3Cer (a globotriaosylceramide) (Mark et al. 2003).
DEGS2 (sphingolipid C4-hydroxylase 2 / âdegenerative spermatocyte homolog 2â) enzyme associated with the cytosolic face of the endoplasmic reticulum catalyzes the hydroxylation of dihydroceramide to form phytoceramide (Mizutani et al. 2004). Sequence similarity to the bifunctional mouse DEGS2 enzyme suggests that human DEGS2 protein might also catalyze the C4-dehydrogenation of dihydroceramide, but this hypothesis has not been tested experimentally.
DEGS1 (sphingolipid delta(4)-desaturase 1 / âdegenerative spermatocyte homolog 1â) enzyme associated with the cytosolic face of the endoplasmic reticulum catalyzes the desaturation of dihydroceramide to form ceramide (Cadena et al. 1997; Ternes et al. 2002). The stoichiometry and cofactor requirements of the reaction are inferred from those observed in studies of ceramide synthesis in vitro catalyzed by rat liver microsomes (Michel et al. 1997). DEGS1 may also catalyze the 4-hydroxylation of dihydroceramide to form 4-hydroxysphinganine, but with low efficiency.
SPTLC (serine palmitoyltransferase) enzyme complexes associated with the endoplasmic reticulum membrane catalyze the reaction of palmitoyl-CoA and serine to form 3-ketosphinganine. SPTLC2 and SPTLC3 polypeptides exhibit enzyme activity when either is complexed with SPTLC1. SPTLC1 and 2 are abundant and widely expressed in human tissues, while SPTLC3 is expressed only in a smaller group of tissues and at variable levels. Results of studies in which siRNA was used to reduce levels of the three endogenous mRNAs differentially suggest that SPTLC2 and 3 both encode active serine palmitoyltransferases (Hornemann et al. 2006). Neither human nor mouse SPTLC1 has detectable enzyme activity, but the protein has an essential function, as mutations that disrupt it are associated with hereditary neuropathy (Dawkins et al. 2001). Studies of mouse and hamster proteins support the hypothesis that heterodimerization with SPTLC1 stabilizes SPTLC2 (or 3) and mediates its localization to the endoplasmic reticulum membrane (Hanada et al. 2000; Weiss and Stoffel 1997). Analyses of complexes extracted from human placenta, and of cultured human cells over-expressing various SPTLC constructs, suggest that these heterodimers may associate into larger complexes (Hanada et al. 2000; Weiss and Stoffel 1997; Hornemann et al. 2006, 2007).
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Cytosolic CSNK1G2 (casein kinase 1, gamma 2) catalyzes the phosphorylation of multiple serine and threonine residues of âCERTâ (ceramide transfer protein) already phosphorylated on serine-132 (Tomishige et al. 2009). This reaction has the effect of inhibiting ceramide transport from the endoplasmic reticulum to the Golgi apparatus as multiphospho-CERT is unable to bind ceramides or associate with the Golgi membrane.
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ACER2 (alkaline ceramidase 2), associated with the membrane of the Golgi apparatus, catalyzes the hydrolysis of ceramide to yield a free fatty acid (annotated here as stearate) and sphingosine. ACER2 mRNA is widely expressed in the body, although only at low levels except in placenta (Xu et al. 2006).
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Role of platelet-derived growth factors in physiology and medicine
SGPL1 (sphingosine-1-phosphate lyase 1), associated with the endoplasmic reticulum membrane, catalyzes the cleavage of cytosolic sphinganine (dihydrosphingosine) 1-phosphate to form phosphoethanolamine and hexadecanal (Van Veldhoven et al. 2000; Fyrst and Saba 2008).
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Assignment of human beta-galactosidase-A gene to 3p21.33 by fluorescence in situ hybridization
SGMS1 (sphingomyelin synthase 1) associated with the membrane of the Golgi apparatus catalyzes the reversible reaction of phosphatidylcholine and ceramide to form sphingomyelin and diacylglycerol. Phosphatidylcholine was identified as the source of the phosphocholine moiety donated to ceramide in this reaction, in studies of the mouse enzyme in the 1970s (Diringer et al. 1972; Ullman and Radin 1974). SGMS1 is widely expressed in the body and studies of cultured cells indicate that this reaction provides the major source of cellular sphingomyelin (Yamaoka et al. 2004; Huitema et al. 2004; Tafesse et al. 2007).
SGMS2 (sphingomyelin synthase 2) catalyzes the reversible reaction of phosphatidylcholine and ceramide to form sphingomyelin and diacylglycerol. Most SGMS2 actitiy is associated with the plasma membrane, although active enzyme is also present in the Golgi apparatus (Tafesse et al. 2007; Villani et al. 2008; Ding et al. 2008). Phosphatidylcholine was identified as the source of the phosphocholine moiety donated to ceramide in this reaction, in studies of the mouse enzyme in the 1970s (Diringer et al. 1972; Ullman and Radin 1974). Palmitoylation of at least two cysteine residues near the carboxy terminus of SGMS2 appears to be required for association of the protein with the plasma membrane (Tani and Kuge 2009). SGMS2 is widely expressed in the body and while studies of cultured cells indicate that this is a minor source of cellular sphingomyelin, blockage of SGMS2 activity inhibits cell growth (Huitema et al. 2004; Tafesse et al. 2007).
SPHK1 and 2 (sphingosine kinases 1 and 2) each catalyze the reaction of sphinganine (dihydrosphingosine) and ATP to form dihydrosphingosine 1-phosphate and ADP. Both enzymes are found in the cytosol (although they are also present in membrane-associated forms). Both enzymes also catalyze the phosphorylation of sphingosine (Liu et al. 2000; Nava et al. 2000; Pitson et al. 2000).
LASS (âlongevity assurance homologâ, also known as ceramide synthase, CerS) enzymes associated with the endoplasmic reticulum membrane catalyze the reaction of sphinganine (dihydrosphingosine) and a long-chain fatty acyl CoA such as stearyl-CoA to form a dihydroceramide and CoASH (Pewzner-Jung et al. 2006). Six human LASS genes have been identified; they differ in the identities of the fatty acyl CoAs that they use most efficiently as substrates (Lahiri and Futerman 2005; Laviad et al. 2008).
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Similar to the lipoxygenases, cytochrome P450 (CYP) enzymes catalyse the hydroxylation and epoxygenation of arachidonic acid. However, whereas lipoxygenases use an active non-heme iron to abstract hydrogen directly from arachidonic acid, CYPs contain a heme-iron active site that oxidizes its substrate by a different mechanism. They hydroxylate arachidonic acid between C-5 and C-15 to produce lipoxygenase-like hydroxyeicosatetraenoic acids (HETEs) and add a hydroxyl moiety to the sp3-hybridized omega-carbons to form a unique class of HETEs. The transfer of oxygen to the unstable arachidonic acid intermediate terminates the reaction by forming HETE or epoxy-eicosatrienoic acid (EETs), respectively (Capdevila et al. 2000, Buczynski et al. 2009, Vance & Vance 2008).
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Several cytochrome P450s (CYPs) convert arachidonic acid to 20-hydroxyeicosatetraenoic acid (20-HETE). The CYPs and their references are as follows: CYP4A11 (Gainer et al. 2005, Powell 1998); CYP4F2 (Powell et al. 1998, Kikuta et al. 2002); CYP2U1 (Chuang et al. 2004); CYP1A1, CYP1A2, CYP1B1 (Choudhary et al. 2004).
Several cytochrome P450s (CYPs) convert arachidonic acid to 19-hydroxyeicosatetraenoic acid (19-HETE). The CYPs and their references are as follows: CYP2C8 (Bylund et al. 1998); CYP2C9 (Bylund et al. 1998); CYP2C19 (Bylund et al. 1998); CYP4A11 (Gainer et al. 2005); CYP2U1 (Chuang et al. 2004); CYP1A1, CYP1A2, CYP1B1 (Choudhary et al. 2004).
Cytochrome P450s 1A1 (CYP1A1), 1A2 (CYP1A2), and 1B1 (CYP1B1) convert arachidonic acid to 16-, 17-, and 18-hydroxyeicosatetraenoic acids (16-, 17-, and 18-HETEs) (Choudhary et al. 2004).
The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits
The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
The epoxidation of arachidonic acid by cytochrome P450s (CYPs) results in the formation of unique bioactive lipid mediators termed epoxyeicosatrienoic acids (EETs). Each double bond has been shown to be susceptible to oxidation, resulting in 5,6-EET, 8,9-EET, 11,12-EET, and 14,15-EET. The majority of the EET biological activities are diminished by the hydrolysis to the corresponding dihydroxyeicosatrienoic acids (DHET) (Capdevila et al. 2000, Buczynski et al. 2009, Vance & Vance 2008).
Eicosanoids, oxygenated, 20-carbon fatty acids, are autocrine and paracrine signaling molecules that modulate physiological processes including pain, fever, inflammation, blood clot formation, smooth muscle contraction and relaxation, and the release of gastric acid. Eicosanoids are synthesized in humans primarily from arachidonic acid (all-cis 5,8,11,14-eicosatetraenoic acid) that is released from membrane phospholipids. Once released, arachidonic acid is acted on by prostaglandin G/H synthases (PTGS, also known as cyclooxygenases (COX)) to form prostaglandins and thromboxanes, by arachidonate lipoxygenases (ALOX) to form leukotrienes, epoxygenases (cytochrome P450s and epoxide hydrolase) to form epoxides such as 15-eicosatetraenoic acids, and omega-hydrolases (cytochrome P450s) to form hydroxyeicosatetraenoic acids (Buczynski et al. 2009, Vance & Vance 2008). Levels of free arachidonic acid in the cell are normally very low so the rate of synthesis of eicosanoids is determined primarily by the activity of phospholipase A2, which mediates phospholipid cleavage to generate free arachidonic acid. The enzymes involved in arachidonic acid metabolism are typically constitutively expressed so the subset of these enzymes expressed by a cell determines the range of eicosanoids it can synthesize. Eicosanoids are unstable, undergoing conversion to inactive forms with half-times under physiological conditions of seconds or minutes. Many of these reactions appear to be spontaneous.
Several cytochrome P450s (CYPs) convert arachidonic acid to 5,6-epoxyeicosatrienoic acid (5,6-EET). The CYPs and their references are as follows: CYP1A1, CYP1A2, CYP1B1 (Choudhary et al. 2004); CYP2J2 (Wu et al. 1996).
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Several cytochrome P450s (CYPs) convert arachidonic acid to 8,9-, 11,12-, and 14,15-epoxyeicosatrienoic acids (8,9-, 11,12-, 14,15-EETs). The CYPs and their references are as follows: CYP1A1, CYP1A2, CYP1B1 (Choudhary et al. 2004); CYP2C8, CYP2C9 (Rifkind et al. 1995); CYP2C19 (Bylund et al. 1998, Rifkind et al. 1995); CYP2J2 (Wu et al. 1996).
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Cytosolic PRKD1 (protein kinase D1) catalyzes the phosphorylation of serine residue 132 of âCERTâ (ceramide transfer protein) (Fugmann et al. 2007).
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ACER1 (alkaline ceramidase 1), associated with the endoplasmic reticulum membrane, catalyzes the reversible hydrolysis of ceramide to yield a free fatty acid (annotated here as stearate) and sphingosine (Sun et al. 2008).
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Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6
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The bioactive prostaglandin (PG) signalling molecules, including PGA2, PGE2, PGF2a, and PGI2 (prostacyclin) are synthesised from arachidonic acid and its products by various prostaglandin synthase type enzymes. Prostaglandin H2 (PGH2) is the starting point for the synthesis of Thromboxanes (TXs) (Buczynski et al. 2009, Vance & Vance 2008). PGs and TXs are collectively known as the prostanoids. Two enzymes, PTGS1 and 2 (COX1 and 2) both catalyze the two-step conversion of arachidonic acid to PGH2. PTGS1 is constitutively expressed in many cell types while PTGS2 is induced in response to stress and mediates the syntheses of prostaglandins associated with pain, fever, and inflammation. Aspirin irreversibly inactivates both enzymes (though it acts more efficiently on PTGS1), explaining both its antiinflammatory effects and side effects like perturbed gastic acid secretion. Drugs like celecoxib, by specifically inhibiting PTGS2, have a strong anti-inflammatory effect with fewer side effects. These PTGS2-specific drugs, however, probably because of their effects on the balance of prostaglandin synthesis in platelets and endothelial cells, can also promote blood clot formation (Buczynski et al. 2009; Stables & Gilroy 2011).
On formation, leukotriene C4 (LTC4) is exported to the extracellular region by the ABCC1 transporter (Sjolinder et al. 1999, Lam et al. 1989) and processed further by cleavage reactions.
Leukotriene A4 hydrolase (LTA4H) is a monomeric, soluble enzyme that catalyzes the hydrolysis of the allylic epoxide leukotriene A4 (LTA4) to the dihydroxy acid leukotriene B4 (LTB4) (Radmark et al. 1984, McGee & Fitzpatrick 1985).
Activation of Cu,Zn-superoxide dismutase in the absence of oxygen and the copper chaperone CCS
The reversible conversion of leukotriene C4 (LTC4) to leukotriene D4 (LTD4) is catalysed by gamma-glutamyl transferases 1 (GGT1) and 5 (GGT5). GGTs are present on the outer surface of plasma membranes and are a heterodimer of a heavy and a light chain. Its action involves the cleavage of the gamma-glutamyl peptide bond of glutathione conjugates, releasing glutamate (Anderson et al. 1982, Wickham et al. 2011).
Leukotrienes (LTs) are biologically active molecules formed in response to inflammatory stimuli. They cause contraction of bronchial smooth muscles, stimulation of vascular permeability, and attraction and activation of leukocytes. LTs were discovered in 1938 and were termed the "slow release substance" (SRS) until their structures were determined in 1979 and they were then renamed to leukotrienes. LTs are derived from arachidonic acid through action by arachidonate 5-lipoxygenase (ALOX5). Cysteinyl leukotrienes (LTC4, LTD4, and LTE4) are generated as products derived from leukotriene A4 (LTA4). Eoxins are generated from leukotrienes (LTs) and resemble cysteinyl leukotrienes but have a different three-dimensional structure (Murphy & Gijon 2007, Hammarstrom 1983, MA.Claesson 2009, Vance & Vance 2008, Buczynski et al. 2009).
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Glutathione peroxidase 1 (GPX1) (Bryant et al. 1982, Sutherland et al. 2001), 2 (GPX2) (Chu et al. 1993), and 4 (Bryant et al. 1982, Sutherland et al. 2001) reduce 5-hydroperoxyeicosatetraenoic acid (5-HpETE) to 5-hydroxyeicosatetraenoic acid (5-HETE) in the presence of glutathione (GSH). This reaction is inferred from the event in rabbit involving the protein GPX1 (Chiba et al. 1999).
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5-hydroperoxy-eicosatetraenoic acid (5-HpETE), 5-hydroxyeicosatetraenoic acid (5S-HETE) and 5-oxo-eicosatetraenoic acid (5-oxoETE) are formed after the initial step of arachidonic acid oxidation by arachidonate 5-lipoxygenase (ALOX5) (Buczynski et al. 2009, Vance & Vance 2008).
Glutathione peroxidase 1 (GPX1) (Bryant et al. 1982, Sutherland et al. 2001), 2 (GPX2) (Chu et al. 1993), and 4 (Bryant et al. 1982, Sutherland et al. 2001) are involved in converting 12R-hydroperoxy-eicosatetraenoic acid (12R-HpETE) to 12R-hydro-eicosatetraenoic acid (12R-HETE).
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Glutathione peroxidase 1 (GPX1) (Bryant et al. 1982, Sutherland et al. 2001), 2 (GPX2) (Chu et al. 1993), and 4 (Bryant et al. 1982, Sutherland et al. 2001) are involved in converting 12S-hydroperoxy-eicosatetraenoic acid (12S-HpETE) to 12S-hydro-eicosatetraenoic acid (12S-HETE). GPXs are selenoenzymes that are responsible for reducing the cellular peroxide. Cellular GPXs compete with hepoxilins A3 (HXA3) synthase for 12S-HpETE as substrate either to produce 12S-HETE or to convert to HXA3, respectively.
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The 12-eicosatetraenoic acids: 12-hydroperoxy-eicosatetraenoic acid (12-HpETE), 12-hydroxyeicosatetraenoic acid (12-HETE) and 12-oxo-eicosatetraenoic acid (12-oxoETE) are formed after the initial step of arachidonic acid oxidation by the arachidonate 12 and 15 lipoxygenases (ALOX12, ALOX12B and ALOX15 respectively). This part of the pathway is bifurcated at the level of 12S-hydroperoxy-eicosatetraenoic acid (12S-HpETE), which can either be reduced to 12S-hydro-eicosatetraenoic acid (12S-HETE) or converted to hepoxilins (Buczynski et al. 2009, Vance & Vance 2008).
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glucosaminylphosphatidylinositol [ChEBI:24275]
Peroxisome proliferator-activated receptors: a nuclear receptor signaling pathway in lipid physiology
Intrapancreatic parasympathetic (vagal) nerve endings release acetylcholine during preabsorptive and absorptive phases of feeding. The acetylcholine binds Muscarinic Acetylcholine Receptor M3 on pancreatic islet beta cells (inferred from experiments with knockout mice).
Molecular mechanism of neuronal plasticity: induction and maintenance of long-term potentiation in the hippocampus
Diacylglycerol, produced by PLC beta-mediated PIP2 hydrolysis in G alpha (q) signalling, remains in the plasma membrane and binds Protein Kinase C alpha (PKC-alpha), causing PKC-alpha to translocate from the cytosol to the plasma membrane. PKC-alpha is thereby activated and phosphorylates target proteins.
Acetylcholine released by parasympathetic nerve endings in the pancreas causes a potentiation of insulin release when glucose is present at concentrations greater than about 7 mM. Acetylcholine binds the Muscarinic Acetylcholine Receptor M3 on pancreatic beta cells. The binding has two effects: an increase in permeability of the cell to Na+ ions through an unknown mechanism, and the activation of Phospholipase C beta-1 through a heterotrimeric G protein, G(q). After acetylcholine binds the Muscarinic Acetycholine Receptor M3, the receptor activates the G protein Gq by causing the alpha subunit of Gq to exchange GDP for GTP. Activation of Gq in turn activates Phospholipase C beta-1. Phospholipase C beta-1 hydrolyzes the phosphodiester bond at the third position of phosphoinositol 4,5-bisphosphate, producing diacylglycerols (DAG) and inositol 1,4,5-trisphosphate. DAG remains in the cell membrane and causes Protein Kinase C alpha (PKC alpha) to translocate from the cytosol to the membrane. This results in the activation of PKC alpha which then phosphorylates target proteins on serine and threonine residues. One known target of PKC alpha is Myristoylated Alanine-rich C Kinase Substrate (MARCKS), which is believed to affect vesicle transport and may be responsible for the increased traffic of insulin granules seen in response to acetylcholine. Inositol trisphophate binds a receptor, the IP3 receptor, on calcium stores in the cell (probably the endoplasmic reticulum). The release of calcium into the cytosol stimulates the exocytosis of insulin granules.
Fatty acids augment the glucose triggered secretion of insulin through two mechanisms: intracellular metabolism and activation of FFAR1 (GPR40), a G-protein coupled receptor. Based on studies with inhibitors of G proteins such as pertussis toxin FFAR1 is believed to signal through Gq/11. Binding of free fatty acids by FFAR1 activates the heterotrimeric Gq complex which then activates Phospholipase C, producing inositol 1,4,5-trisphosphate and eventually causing the release of intracellular calcium into the cytosol. From experiments in knockout mice it is estimated that signaling through FFAR1 is responsible for about 50% of the augmentation of insulin secretion produced by free fatty acids.
Free fatty acids augment the glucose-triggered secretion of insulin. The augmentation is believed to be due to the additive effects of the activation of the free fatty acid receptor 1 (FFAR1 or GPR40) and the metabolism of free fatty acids within the pancreatic beta cell. This module describes each pathway.
The binding of acetylcholine to the Muscarinic Acetylcholine Receptor M3 activates the heterotrimeric G protein, Gq, associated with the M3 receptor. Activation occurs through protein-protein interaction and results in the alpha subunit of Gq exchanging GDP for GTP (i.e releasing GDP and binding GTP). The 3 subunits of the G protein then dissociate into an alpha:GTP complex and a beta:gamma complex.
In the non-activated state heterotrimeric G proteins exist at membranes as heterotrimeric complexes of alpha, beta, and gamma subunits, with the alpha subunit bound to GDP. Upon activation by a receptor coupled to the heterotrimer, exchange of GDP for GTP by the Gq alpha subunit causes the alpha subunit to lose affinity for the beta and gamma subunits. The alpha subunit with bound GTP then dissociates from the beta and gamma subunits.
The Gq alpha:GTP complex activates Phospholipase C beta-1 through protein interaction (inferred from homologues in Bos taurus). The activation by Gq alpha is insensitive to pertussis toxin whilst activation of PLC beta by the G beta-gamma complex is sensitive to pertussis toxin.
Phospholipase C beta-1 associated with the G(q) complex in the plasma membrane catalyzes the hydrolysis of 1-Phosphatidyl-D-myo-inositol 4,5-bisphosphate to yield D-myo-Inositol 1,4,5-trisphosphate and 1,2-Diacylglycerol.
By analogy with adenylyl cyclases I and II, adenylyl cyclase VIII is activated by G(s) alpha:GTP by protein-protein interaction between G(s) alpha and the C2 region of adenylyl cyclase VIII, forming a complex. Adenylyl cyclase VIII is present in beta cells of rat and is activated by both G(s) alpha:GTP and calcium:calmodulin, thus integrating signals from both GLP-1 via G(s) alpha and glucose via calcium. Human beta cells contain adenylyl cyclases V and VI, which are also activated by G(s) alpha:GTP, and may contain additional adenylyl cyclases.
2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial (COQ5) catalyses the C-methyltransferase conversion of 2-methoxy-6-decaprenyl-1,4-benzoquinol (MDMQ10H2) to 6-methoxy-3-methyl-2-decaprenyl-1,4-benzoquinol (DMQ10H2). This reaction is inferred from the equivalent reaction in yeast (Barkovich et al. 1997).
Ubiquinone biosynthesis protein COQ7 homolog (COQ7) (Vajo et al. 1999) catalyses the hydroxylation of 6-methoxy-3-methyl-2-decaprenyl-1,4-benzoquinol (DMQ10H2) to 3-demethylubiquinol-10 (DeMQ10H2). This reaction is inferred from the equivalent reaction in yeast (Marbois & Clarke 1996, Tran et al. 2006).
A flavin-dependent monooxygenase involved in ubiquinone/ubiquinol biosynthesis, COQ6 (Heeringa et al. 2011) catalyses the C5-hydroxylation of 3-decaprenyl-4-hydroxybenzoic acid (DHB) to 3,4-dihydroxy-5-decaprenylbenzoic acid (DHDB). COQ6 is a peripheral membrane protein that localizes to the matrix side of the inner mitochondrial membrane (Gin et al. 2003). This reaction involving COQ6 is inferred from the equivalent reaction in yeast (Ozeir et al. 2011, Gin et al. 2003).
Mitochondrial COQ3 is an O-methyltransferase required in the reaction to convert 3,4-dihydroxy-5-decaprenylbenzoic acid (DHDB) to 3-methoxy-4-hydroxy-5-decaprenylbenzoic acid (MHDB) (Jonassen & Clarke 2000).
Lipids are hydrophobic but otherwise chemically diverse molecules that play a wide variety of roles in human biology. They include ketone bodies, fatty acids, triacylglycerols, phospholipids and sphingolipids, eicosanoids, cholesterol, bile salts, steroid hormones, and fat-soluble vitamins. They function as a major source of energy (fatty acids, triacylglycerols, and ketone bodies), are major constituents of cell membranes (cholesterol and phospholipids), play a major role in their own digestion and uptake (bile salts), and participate in numerous signaling and regulatory processes (steroid hormones, eicosanoids, phosphatidylinositols, and sphingolipids). Because of their poor solubility in water, most lipids in extracellular spaces in the human body are found as complexes with specific carrier proteins. Regulation of the formation and movement of these lipoprotein complexes is a critical aspect of human lipid metabolism, and lipoprotein abnormalities are associated with major human disease processes including atherosclerosis and diabetes. The central steroid in human biology is cholesterol, obtained from animal fats consumed in the diet or synthesized de novo from acetyl-coenzyme A. (Vegetable fats contain various sterols but no cholesterol.) Cholesterol is an essential constituent of lipid bilayer membranes and is the starting point for the biosyntheses of bile acids and salts, steroid hormones, and vitamin D. Bile acids and salts are mostly synthesized in the liver. They are released into the intestine and function as detergents to solubilize dietary fats. Steroid hormones are mostly synthesized in the adrenal gland and gonads. They regulate energy metabolism and stress responses (glucocorticoids), salt balance (mineralocorticoids), and sexual development and function (androgens and estrogens). At the same time, chronically elevated cholesterol levels in the body are associated with the formation of atherosclerotic lesions and hence increased risk of heart attacks and strokes. The human body lacks a mechanism for degrading excess cholesterol, although an appreciable amount is lost daily in the form of bile salts and acids that escape recycling. Aspects of lipid metabolism currently annotated in Reactome include lipid digestion, mobilization, and transport; fatty acid, triacylglycerol, and ketone body metabolism; peroxisomal lipid metabolism; phospholipid and sphingolipid metabolism; cholesterol biosynthesis; bile acid and bile salt metabolism; and steroid hormone biosynthesis.
Alpha-2 adrenoceptors couple with G protein alpha-i subtype which decreases adenylyl cyclase activity, thus reducing cAMP intracellular levels resulting in smooth muscle contraction. There are three alpha-2 subtypes in humans; 2A (Kobilka BK et al, 1987), 2B (Weinshank RL et al, 1990) and 2C (Hirasawa A et al, 1993).
Mitochondrial COQ3 is an O-methyltransferase required in the reaction to convert 3-demethylubiquinol-10 (DeMQ10H2) to ubiquinol-10 (Q10H2) (Jonassen & Clarke 2000).
The length of the polyisoprenoid chain of ubiquinone aka coenzyme Q (Q), varies depending on the species involved: it is 6 in budding yeast, Saccharomyces cerevisiae, (Q6) and 10 in humans (Q10). Most ubiquinone is naturally reduced to ubiquinol (Q10H2 in humans) and it is this form which dominates in most human tissues. It functions as an ubiquitous coenzyme in redox reactions and its ability both to associate with complexes I and III of the electron transport chain and to move freely in the inner mitochondrial membrane are central to its role in electron transport. In eukaryotes ubiquinones/ubiquinols are also found in other membranes such as the endoplasmic reticulum, Golgi vesicles, lysosomes and peroxisomes. Ubiquinol/ubiquinone is synthesized in the following way. Initially, the polyisoprenoid tail is assembled by a polyprenyl diphosphate synthase. Next, 4 hydroxybenzoate polyprenyltransferase (COQ2) catalyses the formation of the covalent linkage between the benzoquinone head group and the tail to produce 4 hydroxy 3 polyprenyl benzoic acid intermediate (DHB, 3 decaprenyl 4 hydroxybenzoic acid in humans). There follows modifications of the aromatic ring starting with hydroxylation, followed by O methylation, and decarboxylation to form the 2 methoxy 6 polyprenyl phenol intermediate (DMPhOH ; 2 methoxy 6 decaprenylphenol in humans). Following this, two additional methylations, one C methylation, and one O methylation step, finally generate the fully substituted hydroquinone, ubiquinol (Szkopinska 2000, Kagan & Quinn 2000, Tran & Clarke 2007, Kawamukai 2009).
The catecholamines adrenaline (epinephrine) and noradrenaline (norepinephrine) inhibit insulin secretion from pancreatic beta cells. Four effects are seen in the cells: 1. Inhibition of exocytosis of secretory granules, the major effect. 2. Opening of ATP-sensitive potassium channels (KATP channels) and repolarization of the cell. 3. Closing of L-type voltage-dependent calcium channels and inhibition of calcium influx. 4. Inhibition of adenylyl cyclase activity. The first event in adrenaline/noradrenaline signaling in beta cells is the binding of adrenaline or noradrenaline to alpha-2 adrenergic receptors, which are G-protein coupled receptors. Binding activates the alpha subunits in heterotrimeric Gi and Go complexes to exchange GDP for GTP, forming the active G alpha:GTP complex. Experiments using specific antibodies against the alpha subunits in mice show that Gi alpha-1, Gi alpha-2, and Go alpha-2 are responsible for adrenergic effects. The exact beta and gamma subunits of the heterotrimeric G-proteins are unknown. After activation by GTP, the heterotrimeric complex dissociates into the G alpha:GTP complex and the beta:gamma complex. The G alpha:GTP complex causes the inhibition of exocytosis by an unknown mechanism that involves protein acylation. This is responsible for most of the observed inhibition of insulin secretion. Additionally, the G alpha:GTP complex activates (opens) KATP channels, allowing the cell to repolarize. The beta:gamma complex inhibits (closes) voltage-dependent calcium channels, reducing the intracellular calcium concentration, and inhibits adenylyl cyclase, reducing the intracellular cAMP concentration.
The pancreatic beta cell contains Alpha2A and Alpha2C Adrenergic Receptors. These are G-protein coupled receptors that can bind either adrenaline or noradrenaline.
Tetrahydrobiopterin biosynthesis, regeneration and functions
Sphingomyelin phosphodiesterase (SMPD1), also called acid sphingomyelinase (ASM), is a lysosomal phosphodiesterase that hydrolyses sphingomyelin to ceramide and phosphocholine (Schuchman et al. 1991, Schuchman et al. 1992). Defects in SMPD1 are the cause of two types of Niemann-Pick disease. Type A (NPDA, Niemann-Pick disease classical infantile form) (MIM:257200) (Ferlinz et al. 1991) and type B (NPDB, Niemann-Pick disease visceral form) (MIM:607616) (Rodriguez-Pascau et al. 2009).
The mammalian brain-specific, Mg2+-dependent, neutral sphingomyelin phosphodiesterases 2 (Tomiuk et al. 1998, Hofmann et al. 2000) and 3 (Marchesini et al. 2003) (SMPD2 and 3) hydrolyse sphingomyelin (SPHM) to ceramide (CERA) at the plasma membrane.
Human glucosylceramidase 2 (GBA2) hydrolyses the glucosidic bond of glucocerebrosides to form ceramide at the plasma membrane (Matern et al. 2001, Boot et al. 2007).
Acid ceramidase (ASAH1) is a lysosomal enzyme that catalyses the hydrolysis of ceramide to sphingosine and free fatty acid. It functions as a heterodimer of one alpha and one beta subunit (Bernardo et al. 1995). Defects in ASAH1 are the cause of Farber lipogranulomatosis (FL) (MIM:228000), also called Farber disease (FD) (Zhang et al. 2000, Koch et al. 1996).
Membrane-bound ectonucleotide pyrophosphatase/phosphodiesterase 7 (ENPP7) mediates the hydrolysis of sphingomyelin to ceramide and choline phosphate (Duan et al. 2003, Wu et al. 2005).
Steryl sulfatase (formerly arylsulfatase C, ARSC) hydrolyses sulfate from steroid sulfates (Noel et al. 1983, Vaccaro et al. 1987, Suzuki et al. 1992). It is located on the ER membrane (Stein et al. 1989) and functions as a homodimer, using calcium as a cofactor. Defects in STS are the cause of ichthyosis X-linked (IXL) (MIM:308100), a keratinisation disorder (Basler et al. 1992, Alperin & Shapiro 1997).
Ceramide glucosyltransferase (UGCG) catalyses the first glycosylation step in glycosphingolipid biosynthesis by the transfer of glucose to ceramide (Ichikawa et al. 1996).
Sphingolipids are derivatives of long chain sphingoid bases such as sphingosine (trans-1,3-dihydroxy 2-amino-4-octadecene), an 18-carbon unsaturated amino alcohol which is the most abundant sphingoid base in mammals. Amide linkage of a fatty acid to sphingosine yields ceramides. Esterification of phosphocholine to ceramides yields sphingomyelin, and ceramide glycosylation yields glycosylceramides. Introduction of sialic acid residues yields gangliosides. These molecules appear to be essential components of cell membranes, and intermediates in the pathways of sphingolipid synthesis and breakdown modulate processes including apoptosis and T cell trafficking. While sphingolipids are abundant in a wide variety of foodstuffs, these dietary molecules are mostly degraded by the intestinal flora and intestinal enzymes. The body primarily depends on de novo synthesis for its sphingolipid supply (Hannun and Obeid 2008; Merrill 2002). De novo synthesis proceeds in four steps: the condensation of palmitoyl-CoA and serine to form 3-ketosphinganine, the reduction of 3-ketosphinganine to sphinganine, the acylation of sphinganine with a long-chain fatty acyl CoA to form dihydroceramide, and the desaturation of dihydroceramide to form ceramide. Other sphingolipids involved in signaling are derived from ceramide and its biosynthetic intermediates. These include sphinganine (dihydrosphingosine) 1-phosphate, phytoceramide, sphingosine, and sphingosine 1-phosphate. Sphingomyelin is synthesized in a single step in the membrane of the Golgi apparatus from ceramides generated in the endoplasmic reticulum (ER) membrane and transferred to the Golgi by CERT (ceramide transfer protein), an isoform of COL4A3BP that is associated with the ER membrane as a complex with PPM1L (protein phosphatase 1-like) and VAPA or VAPB (VAMP-associated proteins A or B). Sphingomyelin synthesis appears to be regulated primarily at the level of this transport process through the reversible phosphorylation of CERT (Saito et al. 2008).
The steps involved in the synthesis of glycosphingolipids (sphingolipids with one or more sugars attached) are annotated here (Gault et al. 2010).
4-hydroxybenzoate polyprenyltransferase, mitochondrial (COQ2) catalyses the combination of 4-hydroxybenzoic acid, aka para-hydroxybenzoic acid (PHB) with the polyisoprenoid tail all-trans-decaprenyl diphosphate (all-E-10PrP2) to form 3-decaprenyl-4-hydroxybenzoic acid (DHB) (Forsgren et a l. 2004, Tekle et al. 2008). This reaction is irreversible and occurs in the mitochondria.
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_257325.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622794
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=549167
At the endoplasmic reticulum (ER) membrane, active membrane-bound ethanolamine-phosphate cytidylyltransferase (PCY2) dimer condenses phosphoethanolamine (PETA) and cytidine triphosphate (CTP) to produce CDP-ethanolamine (CDP-ETA) (Zhu et al. 2008, Nakashima et al. 1997).
At the plasma membrane, phosphatidic acid (PA) is hydrolyzed, removing one of its acyl groups, to 1-acyl lysophosphatidic acid (LPA) by secretory phospholipase A2 proteins (Singer et al. 2002, Ishizaki et al. 1999). These include: Group IB (PLA2G1B) (Grataroli et al. 1982); Group IIA (PLA2G2A) (Seilhamer et al. 1989); Group IID (PLA2G2D) (Ishizaki et al. 1999); Group IIE (PLA2G2E) (Suzuki et al. 2000); Group IIF (PLA2G2F) (Valentin et al. 2000); Calcium-dependent Group V (PLA2G5) (Chen et al. 1994); Group X (PLA2G10) (Cupillard et al. 1997, Pan et al. 2002); and Group XIIA (PLA2G12A) (Gelb et al. 2000, Murakami et al. 2003).
In the cytosol, ethanolamine (ETA) is phosphorylated to phosphoethanolamine (PETA) by choline kinase (CHK) dimer or by ethanolamine kinase 1/2 (ETNK1/2) (Lykidis et al. 2001, Gallego-Ortega et al. 2009). CHK dimer consists of either choline kinase alpha subunit (CHKA) or beta subunit (CHKB) homodimer, or of CHKA:CHKB heterodimer.
Acyl chain remodeling of triacylglycerol (TAG) and diacylglycerol (DAG) progresses through their hydrolysis by patatin-like phospholipase domain-containing proteins 2/3 (PNPLA2/3). DAG is reacylated back to TAG by acylglycerol O-acyltransferase 1/2 (DGAT1/2), while DAG and its hydrolysis product 2-monoacylglycerol (2-MAG) are transacylated back to TAG by PNPLA2/3. In addition, the DAG hydrolysis product 2-MAG is subsequently hydrolyzed to fatty acid and glycerol by monoglyceride lipase (MGLL) (Jenkins et al. 2004).
At the endoplasmic reticulum (ER) membrane, a 2-monoacylglycerol (2-MAG) molecule and a diacylglycerol (DAG) molecule are transacylated by patatin-like phospholipase domain-containing proteins 2/3 (PNPLA2/3). This forms triacylglycerol (TAG) and glycerol (Jenkins et al. 2004).
At the endoplasmic reticulum (ER) membrane, two 2-monoacylglycerol (2-MAG) molecules are transacylated by patatin-like phospholipase domain-containing proteins 2/3 (PNPLA2/3) to form diacylglycerol (DAG) and glycerol (Jenkins et al. 2004).
At the endoplasmic reticulum (ER) membrane, patatin-like phospholipase domain-containing proteins 2/3 (PNPLA2/3) hydrolyze diacylglycerol (DAG), removing an acyl group to form 2-monoacylglycerol (2-MAG) (He et al. 2010, Jenkins et al. 2004, Basantani et al. 2011).
At the endoplasmic reticulum (ER) membrane, diacylglycerol (DAG) is acylated and forms triacylglycerol (TAG) by the action of diacylglycerol O-acyltransferase 1 (DGAT1) tetramer or by diacylglycerol O-acyltransferase 2 (DGAT2) (Wakimoto et al. 2003, Oelkers et al. 1998, Cases et al. 2001).
At the endoplasmic reticulum (ER) membrane, triacylglycerol (TAG) is hydrolyzed, removing one of its acyl groups to form diacylglycerol (DAG) by patatin-like phospholipase domain-containing protein 2/3 (PNPLA2/3) (He et al. 2010, Jenkins et al. 2004, Basantani et al. 2011).
In the de novo synthesis of phosphatidic acid (PA), lysophosphatidic acid (LPA) is initially formed by the esterification of sn-1 by glycerol 3-phosphate acyltransferase (GPAT) from glycerol 3-phosphate (G3P). Next, LPA is converted to PA by a LPA acyltransferase (AGPAT, also known as LPAAT). In addition to this, PA is also formed when phosphatidylcholine (PC) is hydrolyzed by phospholipase D1/2 (PLD1/2). PA is involved in acyl chain remodeling via cleavage by phospholipases followed by reacylation by acyltransferases (Ghomashchi et al. 2010, Singer et al. 2002, Prasad et al. 2011, Shindou & Shimizu 2009, Cao et al. 2006).
At the endoplasmic reticulum (ER) membrane, choline/ethanolaminephosphotransferase 1 (CEPT1) or ethanolaminephosphotransferase 1 (EPT1) converts CDP- ethanolamine (CDP-ETA) and diacylglycerol (DAG) to phosphatidylethanolamine (PE) and cytidine monophosphate (CMP) (Horibata et al. 2007, Wright et al. 2002, Henneberry et al. 1999, Henneberry et al. 2002, Henneberry et al. 2000).
At the endoplasmic reticulum (ER) membrane, phosphatidate phosphatase 1-3 (LPIN) dephosphorylates phosphatidic acid (PA) to form diacylglycerol (DAG) (Grimsey et al. 2008, Donkor et al. 2007).
At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferases acylate 2-acyl lysophosphatidylethanolamine (LPE) to form phosphatidylethanolamine (PE). The lysophospholipid acyltransferases involved are: lysophospholipid acyltransferase 1 (MBOAT1) aka LPEAT1 (Gijon et al. 2008, Hishikawa et al. 2008); lysophospholipid acyltransferase LPCAT4 (LPCAT4) aka LPEAT2 (Cao et al. 2008, Ye et al. 2005); lysophospholipid acyltransferase 2 (MBOAT2) aka LPCAT4 (Hishikawa et al. 2008, Gijon et al. 2008); lysophospholipid acyltransferase 5 (LPCAT3) (Hishikawa et al. 2008, Zhao et al. 2008, Gijon et al. 2008, Jain et al. 2009, Kazachkov et al. 2008).
At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferases acylate 1-acyl lysophosphatidylethanolamine (LPE) to form phosphatidylethanolamine (PE). The lysophospholipid acyltransferases involved are: lysophospholipid acyltransferase 1 (MBOAT1) aka LPEAT1 (Gijon et al. 2008, Hishikawa et al. 2008); lysophospholipid acyltransferase LPCAT4 (LPCAT4) aka LPEAT2 (Cao et al. 2008, Ye et al., 2005); lysophospholipid acyltransferase 2 (MBOAT2) aka LPCAT4 (Hishikawa et al. 2008, Gijon et al. 2008); lysophospholipid acyltransferase 5 (LPCAT3) (Hishikawa et al. 2008, Zhao et al. 2008, Gijon et al. 2008, Jain et al. 2009, Kazachkov et al. 2008).
In the acyl chain remodelling pathway (Lands cycle), phosphatidylethanolamine (PE) is hydrolyzed by phopholipases and subsequently reacylated by acyltransferases. These cycles modify the fatty acid composition of glycerophospholipids to generate diverse molecules asymmetrically distributed in the cell membrane (Ghomashchi et al. 2010, Singer et al. 2002, Cao et al. 2008, Zhao et al. 2008, Hishikawa et al. 2008).
At the plasma membrane, phosphatidylethanolamine (PE) is hydrolyzed, removing one of its acyl groups, to 1-acyl phosphatidylethanolamine (LPE) by secretory phospholipase A2 proteins (Singer et al. 2002, Ishizaki et al. 1999). These include: Group IB (PLA2G1B) (Grataroli et al. 1982); Group IIA (PLA2G2A) (Seilhamer et al. 1989); Group IID (PLA2G2D) (Ishizaki et al. 1999); Group IIE (PLA2G2E) (Suzuki et al. 2000); Group IIF (PLA2G2F) (Valentin et al. 2000); Group III (PLA2G3) (Murakami et al. 2003, Murakami et al. 2005); Calcium-dependent Group V (PLA2G5) (Chen et al. 1994); Group X (PLA2G10) (Cupillard et al. 1997, Pan et al. 2002); and Group XIIA (PLA2G12A) (Gelb et al. 2000, Murakami et al. 2003).
De novo (Kennedy pathway) synthesis of phosphatidylethanolamine (PE) involves phosphorylation of ethanolamine (ETA) to phosphoethanolamine (PETA) followed by condensing with cytidine triphosphate (CTP) to form CDP-ethanolamine (CDP-ETA). Diacylglycerol (DAG) and CDP-ETA together then form PE. Alternatively, PE is formed when phosphatidylserine (PS) is decarboxylated by phosphatidylserine decarboxylase proenzyme (PISD) (Henneberry et al. 2002, Vance 1991, Vance 1990).
At the inner mitochondrial (IM) membrane, phosphatidylserine decarboxylase proenzyme (heterodimer of two chains from the same protein) (PISD) decarboxylates phosphatidylserine (PS) to phosphatidylethanolamine (PE). This event has been inferred from rats and limited data for a human PISD (Forbes et al. 2007).
At the endoplasmic reticulum (ER) membrane, phosphatidylethanolamine (PE) is hydrolyzed, and has one of its acyl chains cleaved off, by membrane-associated phospholipase A2 gamma 2A, (PLA2G2A) or by calcium-independent phospholipase A2-gamma (PNPLA8), to form 1-acyl lysophosphatidylethanolamine (LPE) (Murakami et al. 2005, Kramer et al. 1989, Singer et al. 2002).
At the endoplasmic reticulum (ER) membrane, phosphatidylethanolamine (PE) is hydrolyzed, and has one of its acyl chains cleaved off, by phospholipase A2 to form 1-acyl lysophosphatidylethanolamine (LPE). The phospholipases are either cytosolic phospholipase A2 alpha/beta/delta/epsilon/zeta (PLA2G(4A/B/D/E/F) (Ghosh et al. 2006, Yamashita et al. 2009, Yamashita et al. 1999, Ghomashchi et al. 2010), 85 kDa calcium-independent phospholipase A2 (PLA2G6) (Larsson et al. 1998, Ma et al. 1999, Larsson Forsell et al. 1999), group XVI phospholipase A2 (PLA2G16) (Duncan et al. 2008), or Phospholipase B-like 1 (PLBD1) (Xu et al. 2009). PLBD1 acts as a phospholipase A2 but in addition has the propensity to hydrolyze the lysophospholipid formed in its initial reaction.
Acetylcholinesterase (ACHE) oligomers (comprising monomers, dimers and tetramers), anchored to the extracellular side of the plasma membrane, hydrolyze acetylcholine (AcCho) to form choline (Cho) and acetate (Weinstock & Groner 2008, Velan et al. 1991, Kryger et al. 2000). Acetylcholine from the synaptic cleft is degraded into inactive molecules, Cho and acetate by ACHE, which is located in the synaptic cleft (Weinstock & Groner 2008).
Lysophosphatidylethanolamine (LPE) is hydrolyzed by phospholipases to produce glycerophosphoethanolamine (GPETA) which is in turn hydrolyzed by glycerophosphocholine phosphodiesterase to produce ethanolamine (ETA) and glycerol-3-phosphate (G3P) (Yamashita et al. 2009, Yamashita et al. 2005).
In the cytosol, glycerophosphocholine phosphodiesterase (GPCPD1, also known as GDE5) hydrolyzes glycerophosphoethanolamine (GPETA) to produce ethanolamine (ETA) and glycerol-3-phosphate (G3P). This event has been inferred from mice. GPCPD1 has also been characterized in humans (Ota et al. 2004).
At the endoplasmic reticulum (ER) membrane, active membrane-bound choline-phosphate cytidylyltransferase A (PCYT1A) or B (PCYT1B) homodimer condenses phosphocholine (PCho) and cytidine triphosphate (CTP) to produce CDP-choline (CDP-Cho) (Lykidis et al. 1998).
In the cytosol, choline O-acetyltransferase (CHAT) acetylates choline (Cho) to produce acetylcholine (AcCho) (Toussaint 1992). AcCho is synthesised in the cytoplasm of cholinergic neurons from acetyl-CoA and Cho by CHAT enzyme.
In the cytosol, choline kinase alpha subunit (CHKA) homodimer, choline kinase beta subunit (CHKB) dimer, or CHKA:CHKB heterodimer phosphorylates choline (Cho) to produce phosphocholine (PCho) (Malito et al. 2006, Gallego-Ortega et al. 2009).
Choline (Cho) transports from the extracellular space through the plasma membrane via the choline transporter-like proteins (SLC44A1-5 also known as CTL1-5) to the cytosol (Okuda & Haga 2000, Traiffort et al. 2005, O'Regan et al. 2000). CTL1 is broadly expressed on leukocytes and endothelial cells (Wille et al. 2001). CTL2 is highly expressed in human inner ear and is the target of antibody-induced hearing loss (Nair et al. 2004).
De novo (Kennedy pathway) synthesis of phosphatidylcholine (PC) involves phosphorylation of choline (Cho) to phosphocholine (PCho) followed by condensing with cytidine triphosphate (CTP) to form CDP-choline (CDP-Cho). Diacylglycerol (DAG) and CDP-ETA together then form PC. Alternatively, PC is formed when phosphatidylethanolamine (PE) is methylated by phosphatidylethanolamine N-methyltransferase (PEMT) (Henneberry et al. 2002; Wright & McMaster 2002).
At the Golgi membrane, cholinephosphotransferase 1 (CHPT1) converts CDP-choline (CDP-Cho) and diacylglycerol (DAG) to phosphatidylcholine (PC) and cytidine monophosphate (CMP) (Wright et al. 2002, Henneberry et al. 1999, Henneberry et al. 2002, Henneberry et al. 2000).
At the endoplasmic reticulum (ER) membrane, choline/ethanolaminephosphotransferase (CEPT1) converts CDP-choline (CDP-Cho) and diacylglycerol (DAG) to phosphatidylcholine (PC) and cytidine monophosphate (CMP) (Wright et al. 2002, Henneberry et al. 1999, Henneberry et al. 2002, Henneberry et al. 2000).
Human intestinal sucrase-isomaltase. Identification of free sucrase and isomaltase and cleavage of the hybrid into active distinct subunits.
The inositol hexakisphosphate kinase family. Catalytic flexibility and function in yeast vacuole biogenesis
Structure of S6 kinase 1 determines whether raptor-mTOR or rictor-mTOR
A novel gene oriented in a head-to-head configuration with the human histidyl-tRNA synthetase (HRS) gene encodes an mRNA that predicts a polypeptide homologous to HRS
Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway
Cloning of a gene for a novel epithelium-specific cytosolic phospholipase A2, cPLA2delta, induced in psoriatic skin
Characterization of a Wnt-binding site of the WIF-domain of Wnt inhibitory factor-1
Reconstitution, activities, and structure of the eukaryotic RNA exosome
SPARC binds Collagen type I fibril, hydroxylapatite and Ca2+
AGRN binds Beta amyloid fibril via GAG chains
Syndecan-1 binds collagen types I, III, V
DDR2 binds collagen type I, II, III, V, X fibrils
Discoidin domain receptor 2 binds collagens
Syndecan-4:PI(4,5)P2 binds PKC alpha:DAG
Endostatin binds integrin alphaVbeta3, alphaVbeta5, alpha3beta1, alpha5beta1
HSPG2 (perlecan) is cleaved by BMP1, TLL1, TLL2, Cathepsin L1
HSPG2 (perlecan) degradation by MMP13, CTSS
Deficiency of the first mannosylation step in the N-glycosylation pathway causes congenital disorder of glycosylation type Ik
Proteolytic PAK-2p34 fragment translocates to the nucleus
Autophosphorylation of PAK-2p34 in the activation loop
Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197
Recruitment of ABLIM to the plasma membrane
Unc-115/AbLIM is a key regulator of lamellipodia and filopodia in the growth cone during axon pathfinding and acts downstream of Rac GTPase signaling. It acts as a scaffold to recruit other actin-modulating complexes involved in lamellipodia and filopodia. Unc-115/AbLIM is locally recruited to the plasma membrane by activated Rac1 and subsequently dephosphorylated on serine 617. Dephosphorylated Unc-115/AbLIM then might interact with other molecules at the plasma membrane to induce formation of lamellipodia and filopodia by reorganization of the actin cytoskeleton.
Association of HMGB1/HMGB2 with chromatin
Release of Cytochrome c from mitochondria
Agrin binds Integrins alphaVbeta1 (Other beta1-containing integrins)
AGRN binds Integrins alphaVbeta1 (Other beta1-containing integrins)
Soluble guanylate cyclase converts GTP to cGMP
Interaction of PAK-2p34 with RGH10/ PS-GAP results in accumulation of PAK-2p34 in the perinuclear region
Rho GTPase-activating protein 10 (RHG10) interacts with caspase-activated PAK-2p34
Proteasome mediated degradation of PAK-2p34
Nuclear translocation of catalytic domain of Mst3
Endotoxin induces rapid protein tyrosine phosphorylation in 70Z/3 cells expressing CD14
PI3K alpha, beta, gamma convert PIP2 to PIP3
Activation of conventional Protein Kinase C
Genomic organisation and functional expression of the gene encoding the human serotonin 5-HT2C receptor
VAV1 is a GEF for Rho/Rac family kinases
P2Y purinoceptor 1 activates MAP kinase p38 alpha
VAV3 is a GEF for Rho/Rac family kinases
VAV2 is a GEF for Rho/Rac family kinases
Quasi-native chaperonin-bound intermediates in facilitated protein folding
Release of 78 kDa glucose-regulated protein
Mechanism of action and in vivo role of platelet-derived growth factor
Release of (inferred) platelet cytosolic components
Surface deployment of platelet alpha granule membrane components
Release of platelet cytosolic components
Exocytosis of platelet alpha granule contents
Surface deployment of platelet dense granule membrane components
ABCC4 accumulation of dense granule contents
Regulation of the extracellular antioxidant selenoprotein plasma glutathione peroxidase (GPx-3) in mammalian cells
Mitofusins trans-interact linking mitochondria prior to fusion
F-actin capping protein is a heterodimer
fibrin multimer, crosslinked:tissue plasminogen activator (one-chain) + plasminogen activator inhibitor 1 -> fibrin multimer, crosslinked:tissue plasminogen activator (one-chain):plasminogen activator inhibitor 1
fibrin multimer, crosslinked:tissue plasminogen activator (two-chain) + plasminogen activator inhibitor 1 -> fibrin multimer, crosslinked:tissue plasminogen activator (two-chain):plasminogen activator inhibitor 1
Dual-specific AKAPs bind type I and II PKA regulatory subunits
Sos-mediated nucleotide exchange of Ras (Tie2 receptor:Grb2:Sos)
crosslinked fibrin multimer + tissue plasminogen activator (one-chain) -> crosslinked fibrin multimer:tissue plasminogen activator (one-chain)
factor XIIa + C1Inh -> factor XIIa:C1Inh
Truncated Alpha-1-Microglobulin binds heme
Kinesin-6 and RACGAP1 form the heterotetrameric complex centralspindlin
The gene mutated in adult-onset type II citrullinaemia encodes a putative mitochondrial carrier protein
Hyperornithinaemia-hyperammonaemia-homocitrullinuria syndrome is caused by mutations in a gene encoding a mitochondrial ornithine transporter.
F-actin capping protein binds to the barbed end of elongating F-actin
Adenylate Kinase 3 is a GTP-AMP phosphotransferase
Mechanism for fatty acid sparing effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase
Formation of molecular iodine during oxidation of iodide by the peroxidase/H2O2 system. Implications for antithyroid therapy
Carnitine biosynthesis. beta-Hydroxylation of trimethyllysine by an alpha-ketoglutarate-dependent mitochondrial dioxygenase.
Beta-TrCP1 binds phosphorylated PER proteins
BTRC:CUL1:SKP1 (SCF-beta-TrCP1) ubiquitinylates PER proteins
Formation of the PINCH-ILK-parvin complex
K-sam, an amplified gene in stomach cancer, is a member of the heparin-binding growth factor receptor genes
NR1D1 (REV-ERBA) binds heme and corepressors
Amyloid beta-protein assembly and Alzheimer disease
Trimerization and triple helix stabilization of the collagen XIX NC2 domain
The transforming growth factor beta receptors types I, II, and III form hetero-oligomeric complexes in the presence of ligand
Human homologue of murine tumor rejection antigen gp96: 5'-regulatory and coding regions and relationship to stress-induced proteins
At the plasma membrane, phosphatidylcholine (PC) is hydrolyzed, removing one of its acyl groups, to 1-acyl lysophosphatidylcholine (LPC) by secretory phospholipase A2 proteins (Singer et al. 2002, Ishizaki et al. 1999). These include: Group IB (PLA2G1B) (Grataroli et al. 1982); Group IIA (PLA2G2A) (Seilhamer et al. 1989); Group IID (PLA2G2D) (Ishizaki et al. 1999); Group IIE (PLA2G2E) (Suzuki et al. 2000); Group IIF (PLA2G2F) (Valentin et al. 2000); Group III (PLA2G3) (Murakami et al. 2003, Murakami et al. 2005); Calcium-dependent Group V (PLA2G5) (Chen et al. 1994); Group X (PLA2G10) (Cupillard et al. 1997, Pan et al. 2002); and Group XIIA (PLA2G12A) (Gelb et al. 2000, Murakami et al. 2003).
At the endoplasmic reticulum (ER) membrane, phosphatidylcholine (PC) is hydrolyzed, and has one of its acyl chains cleaved off, by a membrane-associated phospholipase A2 to form 1-acyl lysophosphatidylcholine (LPC). The phospholipases are either phospholipase A2 group II alpha (PLA2G2A) (Seihamer et al. 1989, Singer et al. 2002), cytosolic phospholipase A2 group IV gamma (PLA2G4C) (Yamashita et al. 2005, Pickard et al. 1999, Ghomashchi et al. 2010, Yamashita et al. 2009), or calcium-independent phospholipase A2-gamma (PNPLA8) (Murakami et al. 2005, Underwood et al. 1998).
At the endoplasmic reticulum (ER) membrane, phosphatidylcholine (PC) is hydrolyzed and has one of its acyl chains cleaved off by a phospholipase A2 to form 1-acyl lysophosphatidylcholine (LPC). The phospholipases are either cytosolic phospholipase A2 alpha/beta/delta/zeta (PLA2G4A/B/D/F) (Ghomashchi et al. 2010, Clarke et al. 1991, Sharp et al. 1994, Song et al. 1999, Chiba et al. 2004), 85 kDa calcium-independent phospholipase A2 (PLA2G6) (Larsson et al. 1998, Ma et al. 1999, Larsson Forsell et al. 1999), group XVI phospholipase A2 (PLA2G16) (Duncan et al. 2008), or Phospholipase B-like 1 (PLBD1) (Xu et al. 2009). PLBD1 acts as a phospholipase A2 but in addition has the propensity to hydrolyze the lysophospholipid formed in its initial reaction.
At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferases acylate 2-acyl lysophosphatidylcholine (LPC) to form phosphatidylcholine (PC). The lysophospholipid acyltransferases involved are: lysophosphatidylcholine acyltransferase 1 (LPCAT1) (Nakanishi et al. 2006, Chen et al. 2006); lysophosphatidylcholine acyltransferase 2 (LPCAT2) (Shindou et al. 2006); lysophospholipid acyltransferase 5 (LPCAT3) (Hishikawa et al. 2008, Zhao et al. 2008, Gijon et al. 2008, Jain et al. 2009, Kazachkov et al. 2008); lysophospholipid acyltransferase LPCAT4 (LPCAT4) aka LPEAT2 (Cao et al. 2008, Ye et al. 2005); or lysophospholipid acyltransferase 2 (MBOAT2) aka LPCAT4 (Hishikawa et al. 2008, Gijon et al. 2008).
At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferases acylate 1-acyl lysophosphatidylcholine (LPC) to form phosphatidylcholine (PC). The lysophospholipid acyltransferases involved are: lysophosphatidylcholine acyltransferase 1 (LPCAT1) (Nakanishi et al. 2006, Chen et al. 2006); lysophosphatidylcholine acyltransferase 2 (LPCAT2) (Shindou et al. 2006); lysophospholipid acyltransferase 5 (LPCAT3) (Hishikawa et al. 2008, Zhao et al. 2008, Gijon et al. 2008, Jain et al. 2009, Kazachkov et al. 2008); lysophospholipid acyltransferase LPCAT4 (LPCAT4) aka LPEAT2 (Cao et al. 2008, Ye et al. 2005); or lysophospholipid acyltransferase 2 (MBOAT2) aka LPCAT4 (Hishikawa et al. 2008, Gijon et al. 2008).
The complex between phosphatidylcholine (PC) and phosphatidylinositol transfer protein beta isoform (PITPNB) transports from the Golgi membrane to the ER membrane (Carvou et al. 2010, Shadan et al. 2008).
At the Golgi membrane, phosphatidylinositol (PI) is exchanged for phosphatidylcholine (PC) within the phosphatidylinositol transfer protein beta isoform (PITPNB) complex (Tilley et al. 2004, Yolder et al. 2001, Carvou et al. 2010, Schouten et al. 2002, Vordtriede et al. 2005, Shadan et al. 2008).
The phosphatidylinositol transfer protein beta isoform (PITPNB) bound to phosphatidylinositol (PI) complex transports from the endoplasmic reticulum (ER) membrane to the Golgi membrane, where phosphatidylcholine (PC) is exchanged for PI. PITPNB now in complex with PC transports back to the ER membrane where PI is now exchanged for PC, and the cycle repeats. This process has been characterized in detail in bovine and rodent model systems (e.g., Wirtz et al. 2006; Ghosh and Bankaitis 2011), which provide a framework for organizing the more limited data available for the very well conserved human proteins and processes( Carvou et al. 2010, Shadan et al. 2008).
At the ER membrane, phosphatidylcholine (PC) is exchanged for phosphatidylinositol (PI) within the phosphatidylinositol transfer protein beta isoform (PITPNB) complex (Tilley et al. 2004, Yolder et al. 2001, Carvou et al. 2010, Schouten et al. 2002, Vordtriede et al. 2005, Shadan et al. 2008).
The phosphatidylinositol transfer protein beta isoform (PITPNB) bound to phosphatidylinositol (PI) complex transports from the endoplasmic reticulum (ER) membrane to the Golgi membrane (Carvou et al. 2010, Shadan et al. 2008).
In the acyl chain remodelling pathway (Lands cycle), phosphatidylserine (PS) is hydrolysed by phopholipases and subsequently reacylated by acyltransferases. These cycles modify the fatty acid composition of glycerophospholipids to generate diverse molecules asymmetrically distributed in the cell membrane (Ghomashchi et al. 2010, Singer et al. 2002, Cao et al. 2008; Hishikawa et al. 2008).
At the plasma membrane, phosphatidylserine (PS) is hydrolyzed, removing one of its acyl groups, to 1-acyl lysophosphatidylserine (LPS) by secretory phospholipase A2 proteins (Singer et al. 2002, Ishizaki et al. 1999). These include: Group IB (PLA2G1B) (Grataroli et al. 1982); Group IIA (PLA2G2A) (Seilhamer et al. 1989); Group IID (PLA2G2D) (Ishizaki et al. 1999); Group IIE (PLA2G2E) (Suzuki et al. 2000); Group IIF (PLA2G2F) (Valentin et al. 2000); Calcium-dependent Group V (PLA2G5) (Chen et al. 1994); Group X (PLA2G10) (Cupillard et al. 1997, Pan et al. 2002); and Group XIIA (PLA2G12A) (Gelb et al. 2000, Murakami et al. 2003).
At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferases acylate 2-acyl lysophosphatidylserine (LPS) to form phosphatidylserine (PS). The lysophospholipid acyltransferases involved are: lysophospholipid acyltransferase 5 (LPCAT3) (Gijon et al. 2008, Hishikawa et al. 2008); lysophospholipid acyltransferase LPCAT4 (LPCAT4) aka LPEAT2 (Cao et al. 2008); or lysophospholipid acyltransferase 1 (MBOAT1) aka LPEAT1 (Hishikawa et al. 2008, Gijon et al. 2008).
Phosphatidylinositol (PI) is synthesized when phosphatidic acid (PA) and cytidine triphosphate (CTP) are converted into cytidine diphosphate-diacylglycerol (CDP-DAG) followed by conversion into PI and cytidine monophosphate (CMP) (Stuhne-Sekalec et al 1986, Lykidis et al. 1997).
At the endoplasmic reticulum (ER) membrane, phosphatidylinositol (PI) is hydrolyzed, and has one of its acyl chains cleaved off, by a phospholipase A2 to form 1-acyl lysophosphatidylinositol (LPI). The phospholipases are either cytosolic phospholipase A2 alpha/beta/zeta (PLA2G4A/D/F) (Ghomashchi et al. 2010), group XVI phospholipase A2 (PLA2G16) (Duncan et al. 2008), or Phospholipase B-like 1 (PLBD1) (Xu et al. 2009). PLBD1 also acts as a phospholipase A2 but in addition has the propensity to hydrolyze the lysophospholipid formed in its initial reaction.
At the endoplasmic reticulum (ER) membrane, phosphatidate cytidylyltransferase 1 (CDS1) converts phosphatidic acid (PA) and cytidine triphosphate (CTP) into cytidine diphosphate-diacylglycerol (CDP-DAG). Both ER and mitochondrial membranes have the capability to synthesize cytidine diphosphate-diacylglycerol (CDP-DAG) with phosphatidate cytidylyltransferase 1 and 2 (CDS1 and CDS2) (Lykidis et al. 1997). However, transport of CDP-DAG between organelles cannot be ruled out (Stuhne-Sekalec et al. 1986).
At the endoplasmic reticulum (ER) membrane, CDP-diacylglycerol-inositol 3-phosphatidyltransferase (CDIPT) converts cytidine diphosphate-diacylglycerol (CDP-DAG) and inositol (Ins) into phosphatidylinositol (PI) and cytidine monophosphate (CMP) (Lykidis et al. 1997).
At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferase 7 (MBOAT7) aka LPIAT acylates 2-acyl lysophosphatidylinositol (LPI) to form phosphatidylinositol (PI) (Gijon et al. 2008, Lee et al. 2008).
Cdc25 cell-cycle phosphatase as a target of c-myc
At the endoplasmic reticulum (ER) membrane, phosphatidylinositol (PI) is hydrolyzed, and has one of its acyl chains cleaved off, by membrane-associated phospholipase A2 gamma 2A (PLA2G2A) (Singer et al. 2002) or by cytosolic phospholipase A2 gamma (PLA2G4C) (Ghomashchi et al. 2010), to form 1-acyl lysophosphatidylinositol (LPI).
At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferase 7 (MBOAT7) aka LPIAT acylates 1-acyl lysophosphatidylinositol (LPI) to form phosphatidylinositol (PI) (Gijon et al. 2008, Lee et al. 2008).
Tyrosine phosphorylation of phospholipase C induced by membrane immunoglobulin in B lymphocytes
In the acyl chain remodelling pathway (Lands cycle), phosphatidylcholine (PC) is hydrolysed by phopholipases and subsequently reacylated by acyltransferases. These cycles modify the fatty acid composition of glycerophospholipids to generate diverse molecules asymmetrically distributed in the cell membrane (Ghomashchi et al. 2010, Singer et al. 2002, Cao et al. 2008, Zhao et al. 2008).
At the plasma membrane, phosphatidylcholine (PC) is hydrolyzed, removing one of its acyl groups, to 1-acyl lysophosphatidylcholine (LPC) by membrane-associated phospholipase B1 (PLB1) (Maury et al. 2002, Gassama-Diagne et al. 1992).
At the endoplasmic reticulum (ER) membrane, 1-acyl lysophosphatidylcholine (LPC) is hydrolyzed to glycerophosphocholine (GPCho) by cytosolic phospholipase A2 alpha/beta/delta/epsilon/zeta (PLA2G4A/B/D/E/F) (Yamashita et al. 2005, Ghomashchi et al. 2010, Yamashita et al. 2009, Sharp et al. 1994) or by Phospholipase B1-like (PLBD1) (Xu et al. 2009). PLBD1 also acts as a phospholipase A2 but in addition has the propensity to hydrolyze the lysophospholipid formed in its initial reaction.
At the endoplasmic reticulum (ER) membrane, 2-acyl lysophosphatidylcholine (LPC) is hydrolyzed to glycerophosphocholine (GPCho) by cytosolic phospholipase A2 alpha/beta/delta/epsilon/zeta (PLA2G4A/B/D/E/F) (Yamashita et al. 2005, Ghomashchi et al. 2010, Yamashita et al. 2009, Sharp et al. 1994) or by Phospholipase B1-like (PLBD1) (Xu et al. 2009). PLBD1 also acts as a phospholipase A2 but in addition has the propensity to hydrolyze the lysophospholipid formed in its initial reaction.
In the cytosol, glycerophosphocholine phosphodiesterase (GPCPD1, also known as GDE5) hydrolyzes glycerophosphocholine (GPCho) to produce choline (Cho) and glycerol-3-phosphate (G3P). This event has been inferred from mice. GPCPD1 has also been characterized in humans (Ota et al. 2004).
Lysophosphatidylcholine (LPC) is hydrolyzed by phospholipases to produce glycerophosphocholine (GPCho) which is in turn hydrolyzed by glycerophosphocholine phosphodiesterase to produce choline (Cho) and glycerol-3-phosphate (G3P) (Yamashita et al. 2009, Yamashita et al. 2005, Ghomashchi et al. 2010).
At the endoplasmic reticulum (ER) membrane, phosphatidylserine synthase 1 (PTDSS1) converts phosphatidylcholine (PC) into phosphatidylserine (PS) by facilitating the exchange of L-Serine (L-Ser) with the choline (Cho) head group (Saito et al. 1998, Tomohiro et al. 2009).
Phosphatidylserine (PS) is synthesized by facilitating the exchange of L-Serine (L-Ser) with the choline (Cho) head group in phosphatidylcholine (PC) and with the ethanolamine (ETA) head group in phosphatidylethanolamine (PE) (Saito et al. 1998, Tomohiro et al. 2009).
At the endoplasmic reticulum (ER) membrane, phosphatidylserine (PS) is hydrolyzed, and has one of its acyl chains cleaved off, by membrane-associated phospholipase A2 gamma 2A, PLA2G2A, to form 1-acyl lysophosphatidylserine (LPS) (Singer et al. 2002).
At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferases acylate 1-acyl lysophosphatidylserine (LPS) to form phosphatidylserine (PS). The lysophospholipid acyltransferases involved are: lysophospholipid acyltransferase 5 (LPCAT3) (Gijon et al. 2008, Hishikawa et al. 2008); lysophospholipid acyltransferase LPCAT4 (LPCAT4) aka LPEAT2 (Cao et al. 2008); or lysophospholipid acyltransferase 1 (MBOAT1) aka LPEAT1 (Hishikawa et al. 2008, Gijon et al. 2008).
In the acyl chain remodelling pathway (Lands cycle), phosphatidylglycerol (PG) is hydrolyzed by phopholipases and subsequently reacylated by acyltransferases. These cycles modify the fatty acid composition of glycerophospholipids to generate diverse molecules asymmetrically distributed in the cell membrane. The events occur additionally in the inner mitochondria membranes (IM) as well as in the endoplasmic reticulum (ER) membrane (Ghomashchi et al. 2010, Singer et al. 2002, Cao et al. 2008, Yang et al. 2004, Nie et al. 2010).
At the plasma membrane, phosphatidylglycerol (PG) is hydrolyzed, removing one of its acyl groups, to 1-acyl lysophosphatidylglycerol (LPG) by secretory phospholipase A2 proteins (Singer et al. 2002, Ishizaki et al. 1999). These include: Group IB (PLA2G1B) (Grataroli et al. 1982); Group IIA (PLA2G2A) (Seilhamer et al. 1989); Group IID (PLA2G2D) (Ishizaki et al. 1999); Group IIE (PLA2G2E) (Suzuki et al. 2000); Group IIF (PLA2G2F) (Valentin et al. 2000); Group III (PLA2G3) (Murakami et al. 2003, Murakami et al. 2005); Calcium-dependent Group V (PLA2G5) (Chen et al. 1994); Group X (PLA2G10) (Cupillard et al. 1997, Pan et al. 2002); and Group XIIA (PLA2G12A) (Gelb et al. 2000, Murakami et al. 2003).
At the inner mitochondrial membrane (IM), cardiolipin synthase (CRLS1) acylates 2-acyl lysophosphatidylglycerol (LPG) to form phosphatidylglycerol (PG) (Nie et al. 2010).
At the inner mitochondrial (IR) membrane, cardiolipin synthase (CRLS1) acylates 1-acyl lysophosphatidylglycerol (LPG) to form phosphatidylglycerol (PG) (Nie et al. 2010).
At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferases acylate 2-acyl lysophosphatidylglycerol (LPG) to form phosphatidylglycerol (PG). The lysophospholipid acyltransferases involved are: lysophosphatidylcholine acyltransferase 1 (LPCAT1) (Nakanishi et al. 2006, Chen et al. 2006), lysophospholipid acyltransferase LPCAT4 (LPCAT4) aka LPEAT2 (Cao et al. 2008, Ye et al. 2005); or acyl-CoA:lysophosphatidylglycerol acyltransferase (LPGAT1) (Yang et al. 2004).
At the inner mitochondrial membrane (IM), tafazzin (TAZ) converts cardiolipin (CL) and 1-acyl lysophosphatidylcholine (LPC) to monolysocardiolipin (MLCL) and phosphatidylcholine (PC) (Xu et al. 2003, Xu et al. 2006, Malhotra et al. 2009).
At the inner mitochondrial membrane (IM), calcium-independent phospholipase A2 gamma (PLA2G6) hydrolyzes, removing one of the acyl chains, cardiolipin (CL) to form monolysocardiolipin (MLCL). This reaction is inferred from rats. PLA2G6 has also been characterized in humans (Larsson et al. 1998, Ma et al. 1999, Larsson Forsell et al. 1999).
At the inner mitochondrial membrane (IM), tafazzin (TAZ) converts monolysocardiolipin (MLCL) and phosphatidylcholine (PC) to cardiolipin (CL) and 1-acyl lysophosphatidylcholine (LPC) (Xu et al. 2003, Xu et al. 2006, Malhotra et al. 2009). Although this reaction is reversible, the net effect of the phospholipase A and acyltransferase reactions drives it towards the formation of LPC and CL.
At the inner mitochondrial membrane (IM), cardiolipin synthase (CRLS1) converts phosphatidylglycerol (PG) and cytidine diphosphate-diacylglycerol (CDP-DAG) into cardiolipin (CL) (Lu et al. 2006, Houtkooper et al. 2006).
Cardiolipin(CL) is synthesized in the inner mitochondrial membrane (IM), when phosphatidylglycerol (PG) and cytidine diphosphate-diacylglycerol (CDP-DAG) are converted into CL (Lu et al. 2006, Houtkooper et al. 2006).
In the acyl chain remodelling pathway (Lands cycle), phosphatidylinositol (PI) is hydrolyzed by phospholipases and subsequently reacylated by acyltransferases. These cycles modify the fatty acid composition of glycerophospholipids to generate diverse molecules asymmetrically distributed in the cell membrane (Ghomashchi et al. 2010, Singer et al. 2002, Gijon et al. 2008, Lee et al. 2008).
At the plasma membrane, phosphatidylinositol (PI) is hydrolyzed, removing one of its acyl groups, to 1-acyl lysophosphatidylinositol (LPI) by secretory phospholipase A2 proteins (Singer et al. 2002, Ishizaki et al. 1999). These include: Group IB (PLA2G1B) (Grataroli et al. 1982); Group IIA (PLA2G2A) (Seilhamer et al. 1989); Group IID (PLA2G2D) (Ishizaki et al. 1999); Group IIE (PLA2G2E) (Suzuki et al. 2000); Group IIF (PLA2G2F) (Valentin et al. 2000); Calcium-dependent Group V (PLA2G5) (Chen et al. 1994); Group X (PLA2G10) (Cupillard et al. 1997, Pan et al. 2002); and Group XIIA (PLA2G12A) (Gelb et al. 2000, Murakami et al. 2003).
At the inner mitochondrial (IM) membrane, phosphatidate cytidylyltransferase 2 (CDS2) converts phosphatidic acid (PA) and cytidine triphosphate (CTP) into cytidine diphosphate-diacylglycerol (CDP-DAG). Both ER and mitochondrial membranes have the capability to synthesise cytidine diphosphate-diacylglycerol (CDP-DAG) with phosphatidate cytidylyltransferase 1 and 2 (CDS1 and CDS2) (Lykidis et al. 1997, Schlame & Haldar 1993). However, transport of CDP-DAG between organelles cannot be ruled out (Stuhne-Sekalec et al. 1986).
In the endoplasmic reticulum (ER) membrane, phospholipase D1-4,6 (PLD1-4,6) transphosphatidylates phosphatidylcholine (PC) with glycerol to displace choline (Cho) and form phosphatidylglycerol (PG). This reaction is inferred from rats, but PLD enzymes are present in humans (Hammond et al. 1995, Steed et al. 1998, Cao et al. 1997).
At the endoplasmic reticulum (ER) membrane, phosphatidylglycerol (PG) is hydrolyzed, and has one of its acyl chains cleaved off, by membrane-associated phospholipase A2 gamma 2A, PLA2G2A (Singer et al. 2002), to form 1-acyl lysophosphatidylglycerol (LPG).
At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferases acylate 1-acyl lysophosphatidylglycerol (LPG) to form phosphatidylglycerol (PG). The lysophospholipid acyltransferases involved are: lysophosphatidylcholine acyltransferase 1 (LPCAT1) (Nakanishi et al. 2006, Chen et al. 2006), lysophospholipid acyltransferase LPCAT4 (LPCAT4) aka LPEAT2 (Cao et al. 2008, Ye et al. 2005); or acyl-CoA:lysophosphatidylglycerol acyltransferase (LPGAT1) (Yang et al. 2004).
At the inner mitochondrial (IM) membrane, CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (PGS1) converts cytidine diphosphate-diacylglycerol (CDP-DAG) and glycerol-3-phosphate (G3P) to phosphatidylglycerophosphate (PGP) and cytidine monophosphate (CMP). This event is inferred from rats. The enzyme PGS1 has been characterized in humans (Ota et al. 2004).
At the inner mitochondrial (IM) membrane, PTPMT1 (phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1) catalyzes the dephosphorylation of phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). The biochemical properties of human PTPMT1 have not been determined; this reaction is inferred from the one catalyzed by the homologous mouse protein (Zhang et al. 2011).
Phosphatidylglycerol (PG) is synthesised at the inner mitochondrial (IM) membrane, phosphatidic acid (PA) and cytidine triphosphate (CTP) are converted into cytidine diphosphate-diacylglycerol (CDP-DAG), which in turn is converted with glycerol-3-phosphate (G3P) into phosphatidylglycerophosphate (PGP) and cytidine monophosphate (CMP). Finally, PGP is dephosphorylated to PG. In addition, PG can be synthesised at the endoplamic reticulum (ER) membrane when phospholipase D transphosphatidylates phosphatidylcholine (PC) with glycerol to displace choline (Cho) and form PG (Piazza & Marmer 2007, Stuhne-Sekalec et al. 1986, Lykidis et al. 1997, Cao & Hatch 1994).
At the endoplasmic reticulum (ER) membrane, phosphatidylglycerol (PG) is hydrolyzed, and has one of its acyl chains cleaved off, by cytosolic phospholipase A2 alpha/beta/delta/zeta (PLA2G4A/B/D/F) (Ghomashchi et al. 2010) to form 1-acyl lysophosphatidylglycerol (LPG).
At the Golgi membrane, ADP-ribosylation factor 1 and 3 (ARF1 and ARF3) complexed to GTP bind to phosphatidylinositol 4-kinase beta (PI4KB) and activate it (Haynes et al. 2007, Wong et al. 1997, Godi et al. 1999).
At the Golgi membrane, activated phosphatidylinositol 4-kinase beta (PI4KB) complexed to ADP-ribosylation factor 1/3 (ARF1/3) phosphorylates phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) (Suzuki et al. 1997).
At the Golgi membrane, phosphatidylinositol 4-kinase alpha (PI4KA) (Gehrmann et al. 1999, Godi et al. 1999), or phosphatidylinositol 4-kinase type 2-alpha/beta (PI4K2A/B) (Balla et al. 2002, Minogue et al. 2001, Wei et al. 2002) phosphorylate phosphatidylinositol (PI) to produce phosphatidylinositol 4-phosphate (PI4P).
At the Golgi membrane, phosphatidylinositide phosphatase SAC1 (SACM1L) dephosphorylates phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol (PI) but not as efficiently as phosphatidylinositol 4-phosphate (PI4P) dephosphorylation. No significant activity of this enzyme towards phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) was detected (Rohde et al. 2003).
At the Golgi membrane, the PAS complex, consisting of FYVE finger-containing phosphoinositide kinase (PIKFYVE), yeast VAC14 homologue (VAC14), and polyphosphoinositide phosphatase aka SAC3 (FIG4), binds to the membrane via PIKFYVE's FYVE finger (Sbrissa et al. 2002). The PIKFYVE kinase component phosphorylates phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol 3,5-bisphosphate PI(3,5)P2 (Sbrissa et al. 1999, McEwen et al. 1999). The PAS complex is present in the cytosol and is recruited to the membrane (Sbrissa et al. 2007). VAC14 acts as a scaffolding protein via its C-terminal domain (Sbrissa et al. 2008).
At the Golgi membrane, phosphatidylinositide phosphatase SAC1 (SACM1L) efficiently dephosphorylates phosphatidylinositol 4-phosphate (PI4P), and to a lesser extent phosphatidylinositol 3-phosphate (PI3P), to phosphatidylinositol (PI). No significant activity of this enzyme towards phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) was detected (Rohde et al. 2003).
At the Golgi membrane, phosphatidylinositol 3-kinase catalytic subunit type 3 (PIK3C3) aka VPS34 is bound to phosphoinositide 3-kinase regulatory subunit 4 (PIK3R4). This PIK3C3:PIK2R4 complex and phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha (PIK3C2A) phosphorylate phosphatidylinositol (PI) to phosphatidylinositol 3-phosphate (PI3P). The following lists the above proteins with their corresponding literature references: PIK3C3:PIK2R4 (Panaretou et al. 1997, Volinia et al. 1995) and PIK3C2A (Arcaro et al. 2000, Domin et al. 2000).
At the Golgi membrane, phosphatidylinositol 4-phosphate (PI4P) inositol polyphosphate 5-phosphatase OCRL-1 (OCRL) (Choudhury et al. 2009, Suchy et al. 1995, Zhang et al. 1995) and 72 kDa inositol polyphosphate 5-phosphatase (INPP5E) (Bilas et al. 2009) dephosphorylate phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) to form phosphatidylinositol 4-phosphate (PI4P). INPP5E is located in the Golgi membrane, mediated by its N-terminal proline-rich domain (Kong et al. 2000).
At the Golgi membrane, phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha (PIK3C2A) (Domin et al. 2000, Arcaro et al. 2000) and phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit gamma (PIK3C2G) (Ono et al. 1998, Rozycka et al. 1998, Misawa et al. 1998) phosphorylate phosphatidylinositol 4-phosphate (PI4P) to phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2). PIK3C2G phosphorylates phosphatidylinositol (PI) and PI4P but not phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2).
At the Golgi membrane, the PAS complex, consisting of FYVE finger-containing phosphoinositide kinase (PIKFYVE), yeast VAC14 homologue (VAC14), and polyphosphoinositide phosphatase aka SAC3 (FIG4), binds to the membrane via PIKFYVE's FYVE finger. The FIG4 phosphatase component dephosphorylates phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) to phosphatidylinositol 3-phosphate (PI3P) (Sbrissa et al. 2007, Sbrissa et al. 2008).
At the inner mitochondrial membrane (IM), tafazzin (TAZ) converts monolysocardiolipin (MLCL) and phosphatidylethanolamine (PE) to cardiolipin (CL) and 1-acyl lysophosphatidylethanolamine (LPE) (Xu et al. 2003, Xu et al. 2006, Malhotra et al. 2009). Although this reaction is reversible, the net effect of the phospholipase A and acyltransferase reactions drives it towards the formation of LPE and CL.
At the inner mitochondrial membrane (IM), tafazzin (TAZ) converts cardiolipin (CL) and 1-acyl lysophosphatidylethanolamine (LPE) to monolysocardiolipin (MLCL) and phosphatidylethanolamine (PE) (Xu et al. 2003, Xu et al. 2006, Malhotra et al. 2009).
At the inner mitochondrial membrane (IM), the trifunctional enzyme HADH (3-hydroxyacyl-CoA dehydrogenase), an octamer of four alpha (HADHA) and four beta (HADHB) subunits, acylates monolysocardiolipin (MLCL) to cardiolipin (CL) (Taylor & Hatch 2009).
At the endoplasmic reticulum (ER) membrane, lysocardiolipin acyltransferase 1 (LCLAT1) aka ALCAT1 acylates monolysocardiolipin (MLCL) to cardiolipin (CL) (Cao et al. 2004, Zhao et al. 2009).
At the endoplasmic reticulum (ER) membrane, lysocardiolipin acyltransferase 1 (LCLAT1) aka ALCAT1 acylates dilysocardiolipin (DLCL) to produce monolysocardiolipin (MLCL) (Zhao et al. 2009).
Acyl chain remodeling of cardiolipin (CL) occurs in the inner mitochondria membranes (IM) via hydrolysis by phopholipases and subsequent reacylation by acyltransferases. At the endoplasmic reticulum (ER) membrane the situation is more complicated with monolysocardiolipin (MLCL) involved in hydrolysis and subsequent reacylation back to CL (Zachman et al. 2010, Malhotra et al. 2009, Xu et al. 2003, Taylor & Hatch 2009, Cao et al. 2004, Zhao et al. 2009, Buckland et al. 1998).
Eukaryotic protein synthesis: still a mystery
At the endoplasmic reticulum (ER) membrane, phosphatidylinositol 4-kinase alpha (PI4KA) (Wong et al. 1997, Gehrmann et al. 1999) or phosphatidylinositol 4-kinase type 2-beta (PI4K2B) (Wei et al. 2002) phosphorylate phosphatidylinositol (PI) to produce phosphatidylinositol 4-phosphate (PI4P).
Glycerophospholipids are important structural and functional components of biological membranes and constituents of serum lipoproteins and the pulmonary surfactant. In addition, glycerophospholipids act as precursors of lipid mediators such as platelet-activating factor and eicosanoids. Cellular membranes contains a distinct composition of various glycerophospholipids such as phosphatidic acid (PA), phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylserine (PS), phosphatidylglycerol (PG), phosphatidylinositol (PI), cardiolipin (CL), lysophosphatidic acid (LPA) and lysobisphosphatidic acid (also known as bis(monoacylglycerol) hydrogen phosphate - BMP). Glycerophospholipids are first formed by the de novo (Kennedy) pathway using fatty acids activated as acyl-CoA donors. However, the acyl groups of glycerophospholipids are highly diverse and distributed in an asymmetric manner. Saturated and monounsaturated fatty acids are usually esterified at the sn-1 position, whereas polyunsaturated acyl groups are esterified at the sn-2 position. Subsequent acyl chain remodeling (Lands cycle) generates the diverse glycerophospholipid composition and asymmetry characteristic of cell membranes. In the de novo pathway of glycerophospholipid biosynthesis, lysophosphatidic acid (LPA) is initially formed from glycerol 3-phosphate (G3P). Next, LPA is converted to PA by a LPA acyltransferase (AGPAT, also known as LPAAT), then PA is metabolized into two types of glycerol derivatives. The first is diacylglycerol (DAG) which is converted to triacylglycerol (TAG), PC, and PE. Subsequently, PS is synthesized from PC or PE. The second is cytidine diphosphate-diacylglycerol (CDP-DAG), which is processed into PI, PG, CL, and BMP. Each glycerophospholipid is involved in acyl chain remodeling via cleavage by phospholipases followed by reacylation by an acyltransferase. Most of the glycerophospholipids are synthesized at the endoplasmic reticulum (ER), however, some, most notably cardiolipin, and BMP are synthesized in the mitochondrial and endosomal membranes respectively. Since the most of the glycerophospholipids are found in all membrane compartments, there must be extensive network of transport of glycerophospholipids from one membrane compartment to another via various mechanisms including diffusion through the cytosol, formation of transportation complexes, and diffusion via membrane contact sites (MCS) (Osman et al. 2011, Lebiedzinska et al. 2009, Lev 2010, Scherer & Schmitz 2011, Orso et al. 2011, Hermansson et al. 2011, Vance & Vance 2008).
At the endoplasmic reticulum (ER) membrane, phosphatidylinositol (PI) and phosphatidylinositol 4-phosphate (PI4P) are interconverted (Wong et al. 1997, Gehrmann et al. 1999, Wei et al. 2002, Rohde et al. 2003).
At the endoplasmic reticulum (ER) membrane, transmembrane protein phosphatidylinositide phosphatase SAC1 (SACM1L) efficiently dephosphorylates phosphatidylinositol 4-phosphate (PI4P), and to a lesser extent phosphatidylinositol 3-phosphate (PI3P), to phosphatidylinositol (PI). No significant activity of this enzyme towards phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) was detected (Rohde et al. 2003).
At the plasma membrane, synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1 aka Synaptojanin-1 (SYNJ1) (Guo et al. 1999, Mani et al. 2007, Johenning et al. 2004) and -2 (SYNJ2) (Malecz et al. 2000) dephosphorylate phosphatidylinositol 4-phosphate (PI4P) phosphatidylinositol (PI). The SAC1 domains of SYNJ1 and SYNJ2 demonstrate 4-phosphatase activity.
At the plasma membrane, subsequent phosphorylation of phosphatidylinositol 4-phosphate (PI4P) produces phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) and phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) while the actions of various other kinases and phosphatases produces phosphatidylinositol 3-phosphate (PI3P), phosphatidylinositol 5-phosphate (PI5P), phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2), and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) (Zhang et al. 1997, Gurung et al. 2003, Guo et al. 1999, Vanhaesebroeck et al. 1997, Tolias et al. 1998, Schaletzky et al. 2003, Kim et al. 2002, Clarke et al. 2010).
At the plasma membrane, phosphatidylinositol-5-phosphate 4-kinase type-2 alpha (PIP4K2A) and beta (PIP4K2B) homodimers and heterodimers (Clarke et al. 2010) phosphorylate phosphatidylinositol 5-phosphate (PI5P) to phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). The following lists the above proteins with their corresponding literature references: PIP4K2A (Rameh et al. 1997, Clarke et al. 2008) and PIP4K2B (Rameh et al. 1997).
At the plasma membrane, phosphatidylinositol 4-kinase type 2-alpha (PI4K2A) (Balla et al. 2002, Minogue et al. 2001) and beta (PI4K2B) (Balla et al. 2002, Wei et al. 2002) phosphorylate phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P).
At the plasma membrane, synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1 aka synaptojanin-1 (SYNJ1) (Guo et al. 1999, Mani et al. 2007) and -2 (SYNJ2) (Malecz et al. 2000) dephosphorylate phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) to phosphatidylinositol 3-phosphate (PI3P).
At the plasma membrane, synaptojanin-1 aka Synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1 (SYNJ1) (Guo et al. 1999), -2 (SYNJ2) and some myotubularins (MTMs) dephosphorylate phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) to phosphatidylinositol 5-phosphate (PI5P). The MTMs involved are: myotubularin (MTM1) (Cao et al. 2007, Tronchere et al. 2004, Schaletzky et al. 2003, Laporte et al. 2002) and myotubularin-related proteins 1 (MTMR1) (Tronchere et al. 2004), 3 (MTMR3) (Walker et al. 2001, Lorenzo et al. 2005), 6 (MTMR6) (Schaletzky et al. 2003, Choudhury et al. 2006), and 14 (MTMR14) (Tosch et al. 2006).
At the plasma membrane, phosphatidylinositol-4-phosphate 5-kinase type-1 alpha (PIP5K1A) and beta (PIP5K1B) phosphorylate phosphatidylinositol (PI) to produce phosphatidylinositol 5-phosphate (PI5P) (Tolias et al. 1998).
At the plasma membrane, phosphatidylinositol-4-phosphate 5-kinase type-1 alpha (PIP5K1A) and beta (PIP5K1B) phosphorylate phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) (Tolias et al. 1998).
At the plasma membrane, synaptojanin-1 aka Synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1 (SYNJ1) (Guo et al. 1999), -2 (SYNJ2) and some myotubularins (MTMs) dephosphorylate phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol (PI). The MTMs involved are: myotubularin (MTM1) (Cao et al. 2007, Tronchere et al. 2004, Schaletzky et al. 2003, Laporte et al. 2002, Kim et al. 2002) and myotubularin-related proteins 1 (MTMR1) (Kim et al. 2002, Tronchere et al. 2004), 3 (MTMR3) (Kim et al. 2002, Zhao et al. 2001, Walker et al. 2001, Lorenzo et al. 2005), 6 (MTMR6) (Schaletzky et al. 2003, Kim et al. 2002, Choudhury et al. 2006), and 14 (MTMR14) (Tosch et al. 2006).
At the early endosome membrane, type I (INPP4A) (Norris et al. 1995, Ivetac et al. 2005) and type II inositol-3,4-bisphosphate 4-phosphatase (INPP4B) (Norris et al. 1997) colocalise with early and recycling endosomes through their C2 domains which bind to the phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) present in these membranes. It is here that phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) is dephosphorylated by INPP4A/B to phosphatidylinositol 3-phosphate (PI3P).
At the plasma membrane, phosphatidylinositol-4-phosphate 5-kinase type-1 alpha (PIP5K1A), beta (PIP5K1B), and gamma (PIP5K1C) phosphorylate phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) to produce phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3). This is a minor reaction, however, and its physiological role is uncertain. The following lists the above proteins with their corresponding literature references: PIP5K1A (Zhang et al. 1997, Tolias et al. 1998), PIP5K1B (Zhang et al. 1997, Tolias et al. 1998), and PIP5K1C (Wenk et al. 2001, Di Paolo et al. 2002, Krauss et al. 2003).
At the plasma membrane, phosphatidylinositol 5-phosphatases dephosphorylate phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) to phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2). The phosphatidylinositol 5-phosphatases involved are: inositol polyphosphate 5-phosphatase K (INPP5K) aka SKIP (Ijuin et al. 2000, Gurung et al. 2003), phosphatidylinositol 4,5-bisphosphate 5-phosphatase A (INPP5J) aka PIPP (Gurung et al. 2003, Mochizuki & Takenawa 1999), phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) aka SHIP1 (Drayer et al. 1995, Kavanaugh et al. 1996, Dunant et al. 2000), and phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2 (INPPL1) aka SHIP2 (Habib et al. 1998, Wisniewski et al. 1999, Pesesse et al. 2001).
At the plasma membrane, phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2) 3-kinase catalytic subunits form complexes with regulatory subunits. These complexes along with phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunits alpha (PIK3C2A), beta (PIK3C2B), and gamma (PIK3C2G) phosphorylate phosphatidylinositol 4-phosphate (PI4P) to phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2). The PI(4,5)P2 3-kinase complexes involved are: PI(4,5)P2 3-kinase catalytic subunit alpha isoform (PIK3CA) bound to PI 3-kinase regulatory subunit alpha/beta/gamma (PIK3R1/2/3); beta (PIK3CB) bound to PIK3R1/2/3; delta (PIK3CD) bound to PIK3R1/2/3; and gamma (PIK3CG) bound to PI 3-kinase regulatory subunit 5 (PIK3R5) or 6 (PIK3R6). The following lists the above proteins with their corresponding literature references: PIK3C2A (Arcaro et al. 2000); PIK3C2B (Arcaro et al. 2000, Arcaro et al. 1998); PIK3C2G (Misawa et al. 1998, Ono et al. 1998); PIK3CA:PIK3R1, PIK3CA:PIK3R2, PIK3CA:PIK3R3 (Vanhaesebroeck et al. 1997); PIK3CB:PIK3R1, PIK3CB:PIK3R2, PIK3CB:PIK3R3 (Meier et al. 2004, Guo et al. 1997); PIK3CD:PIK3R1, PIK3CD:PIK3R2, PIK3CD:PIK3R3 (Vanhaesebroeck et al. 1997); and PIK3CG:PIK3R5, PIK3CG:PIK3R6 (Suire et al. 2005, Stoyanov et al. 1995).
At the plasma membrane, phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase aka phosphatase and tensin homolog (PTEN) dephosphorylates phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) to phosphatidylinositol 4-phosphate (PI4P) (Myers et al. 1998, Das et al. 2003).
At the Golgi membrane, phosphatidylinositol 4-phosphate (PI4P) is primarily generated from phosphorylation of phosphatidylinositol (PI). Other phosphoinositides are also generated by the action of various kinases and phosphatases such as: phosphatidylinositol 3-phosphate (PI3P), phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2), phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) (Godi et al. 1999, Minogue et al. 2001, Rohde et al. 2003, Sbrissa et al. 2007, Sbrissa et al. 2008, Domin et al. 2000, Arcaro et al. 2000).
At the plasma membrane, phosphatidylinositol-4-phosphate 5-kinase type-1 alpha (PIP5K1A), beta (PIP5K1B), and gamma (PIP5K1C) phosphorylate phosphatidylinositol 4-phosphate (PI4P) to produce phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). The following lists the above proteins with their corresponding literature references: PIP5K1A (Halstead et al. 2006, Zhang et al. 1997), PIP5K1B (Zhang et al. 1997), and PIP5K1C (Di Paolo et al. 2002). This reaction is of particular interest because its regulation by small GTPases of the RHO and ARF families, not yet annotated here, ties the process of phosphatidylinositol phosphate biosynthesis to regulation of the actin cytoskeleton and vesicular trafficking, and hence to diverse aspects of cell motility and signalling (Oude Weernink et al., 2004, 2007).
At the plasma membrane, Synaptojanin-1 (SYNJ1) and -2 (SYNJ2), inositol polyphosphate 5-phosphatase K (INPP5K) aka SKIP, phosphatidylinositol 4,5-bisphosphate 5-phosphatase A (INPP5J) aka PIPP dephosphorylate phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) to form phosphatidylinositol 4-phosphate (PI4P). SYNJ1/2 both have an N-terminal Sac1-like domain, a central 5-phosphatase domain and a C-terminal proline-rich segment, with this latter part being the most divergent part of the protein sequence. The following lists the above proteins with their corresponding literature references: SYNJ1 (Johenning et al. 2004, Haffner et al. 1997, Guo et al. 1999, Mani et al. 2007), SYNJ2 (Malecz et al. 2000), INPP5K (Injuin et al. 2000, Gurung et al. 2003), and INPP5J (Gurung et al. 2003, Mochizuki & Takenawa 1999).
At the plasma membrane, phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunits form complexes with regulatory subunits. These complexes phosphorylate phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) to phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) (Stephens et al. 1997). The PI(4,5)P2 3-kinase complexes involved are: PI(4,5)P2 3-kinase catalytic subunit alpha isoform (PIK3CA) bound to PI 3-kinase regulatory subunit alpha/beta/gamma (PIK3R1/2/3); beta (PIK3CB) bound to PIK3R1/2/3; delta (PIK3CD) bound to PIK3R1/2/3; and gamma (PIK3CG) bound to PI 3-kinase regulatory subunit 5 (PIK3R5) or 6 (PIK3R6). The following lists the above proteins with their corresponding literature references: PIK3CA:PIK3R1, PIK3CA:PIK3R2, PIK3CA:PIK3R3 (Dey et al. 1998, Vanhaesebroeck et al. 1997, Meier et al. 2004); PIK3CB:PIK3R1, PIK3CB:PIK3R2, PIK3CB:PIK3R3 (Meier et al. 2004); PIK3CD:PIK3R1, PIK3CD:PIK3R2, PIK3CD:PIK3R3 (Vanhaesebroeck et al. 1997, Meier et al. 2004); and PIK3CG:PIK3R5, PIK3CG:PIK3R6 (Voigt et al. 2006, Suire et al. 2005, Stoyanov et al. 1995).
At the plasma membrane, type I and type II inositol-3,4-bisphosphate 4-phosphatase (INPP4A) (Norris et al. 1995, Ivetac et al. 2005) and (INPP4B) (Norris et al. 1997) dephosphorylate phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) to phosphatidylinositol 3-phosphate (PI3P).
At the plasma membrane, phosphatidylinositol-5-phosphate 4-kinase type-2 alpha (PIP4K2A) and beta (PIP4K2B) homodimers and heterodimers (Clarke et al. 2010), along with phosphatidylinositol-4-phosphate 5-kinase type-1 alpha (PIP5K1A), beta (PIP5K1B), and gamma (PIP5K1C) phosphorylate phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2). The following lists the above proteins with their corresponding literature references: PIP4K2A (Zhang et al. 1997, Rameh et al. 1997, Clarke et al. 2008), PIP4K2B (Zhang et al. 1997, Rameh et al. 1997), PIP5K1A (Zhang et al. 1997, Tolias et al. 1998), PIP5K1B (Zhang et al. 1997, Tolias et al. 1998), and PIP5K1C (Wenk et al. 2001, Di Paolo et al. 2002).
Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit
Branching and elongation of mother and daughter filaments
Phosphorylation of nucleosides and nucleoside analogs by mammalian nucleoside monophosphate kinases
Production of AA by iPLA2 upon FCGR activation
Extension of pseudopodia by myosin-X in a PI3K dependent manner
The human and mouse replication-dependent histone genes
Syndromic craniosynostosis: from history to hydrogen bonds
Isolation of a family of organic anion transporters from human liver and kidney
Biosynthesis of chondroitin sulfate: from the early, precursor discoveries to nowadays, genetics approaches
Egress of internalized antigen to the cytosol via sec61
Interaction of particulate antigens with dendritic cell receptors
Engulfment of particulate antigen into phagocytic vesicle
Trimming of N-ter extended precursor fragments by cytosolic aminopeptidases
p-RasGRP1,3:DAG cause RAS to exchange GDP for GTP
Activation of RAS by RasGRP1 and RasGRP3
Rap1 sequesters Raf1 to inhibit ERK cascade
XBP1 controls diverse cell type- and condition-specific transcriptional regulatory networks
Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator
14-3-3 proteins beta and zeta bind and inhibit Rap1Gap2
Antigen processing by cathepsin S in endosoytic vesicle
Proteasomal clevage of exogenous antigen
Reduction of disulphide bonds in MHC II antigens
Translocation of antigenic peptides back to phagosomes via TAP
Inactivation of NF-kappa B inhibitor I kappa B alpha: ubiquitin-dependent proteolysis and its degradation product
TXNIP is released from oxidized thioredoxin
Activated TRAF6 synthesizes unanchored polyubiquitin chains upon TLR stimulation
Nuclear export of human p38 MAPK mediated by its substrate MAPKAPK2 or 3
RNA polymerase III transcribes microbial dsDNA to dsRNA
LRR FLII-interacting protein 1 associates with beta-catenin
Five-hour half-life of mouse liver gap-junction protein
Phosphorylation of beta-catenin at Ser552
Activation of CDC42 by unknown mechanism
Attachment of preexisting mother filament and initiation of branching
Phosphorylation of MOB1A and B by p-STK3 (p-MST2)
Phosphorylation of MOB1A and B by p-STK3(MST2)/N
Phosphorylation of LATS1 and 2 by p-STK4 (p-MST1)
Phosphorylation of LATS1 and 2 by p-STK4(MST1)/N
Phosphorylation of LATS1 and 2 by p-STK3 (p-MST2)
Phosphorylation of LATS1 and 2 by p-STK3 (MST2)/N
Extracellular-signal-regulated kinase signalling in neurons
Phosphorylation of STK4 (MST1) and SAV1 by STK4
Phosphorylation of STK3 (MST2) and SAV1 by STK3
Characterization of MTMR3. an inositol lipid 3-phosphatase with novel substrate specificity
STAT5 dimers translocate to the nucleus and bind to specific DNA sequences
Activation of Rap1 by membrane-associated GEFs
Translocation of RIAM to plasma membrane
Phosphorylated MOB1A proteins associate with LATS proteins
Phosphorylation of MOB1A and B by p-STK4(MST1)/N
Phospho R-SMAD(SMAD2/3):CO-SMAD(SMAD4):FOXH1 binds Activin Response Element
Phosphorylation of MOB1A and B by p-STK4 (p-MST1)
Translocation of PDK1 to Plasma membrane
Translocation of PKC theta to plasma membrane
Release of arachidonate from diglyceride in human platelets requires the sequential action of a diglyceride lipase and a monoglyceride lipase
SHC1 bound to integrin alphaIIb beta3 is phosphorylated somehow
TRPC1 translocates calcium from the extracellular region to the cytosol
PRKCB (Protein kinase C beta, PKC-beta) binds diacylglycerol and phosphatidylserine
Protein Kinase C beta (PKC-beta, PRKCB) is activated
RasGRP1 and RasGRP3 binds diacylglycerol and is phosphorylated
CRAC translocates calcium from the extracellular region to the cytosol
STIM1 binds TRPC1 forming STIM1:TRPC1 complex
A second canon. Functions and mechanisms of beta-catenin-independent Wnt signaling
FZD2, FZD5 and ROR2 are internalized in a WNT5A and clathrin-dependent manner
A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells
dissociation of CaM and CAMK2 autophosphorylation
autophosphorylation and activation of CAMK2
translocation of NFATC1:CaN:CaM to nucleus
translocation and activation of PKC alpha in response to WNT signaling
Phospholipase C-gamma 1 and phospholipase C-gamma 2 are substrates of the B cell antigen receptor associated protein tyrosine kinase
Human liver long-chain 3-hydroxyacyl-coenzyme A dehydrogenase is a multifunctional membrane-bound beta-oxidation enzyme of mitochondria.
Type II phosphatidylinositol 4-kinase beta is a cytosolic and peripheral membrane protein that is recruited to the plasma membrane and activated by Rac-GTP
NPT4, a new microsomal phosphate transporter: mutation analysis in glycogen storage disease type Ic
Molecular structure of a novel cholesterol-responsive A subclass ABC transporter, ABCA9
RNA binding properties of the AU-rich element-binding recombinant Nup475/TIS11/tristetraprolin protein
Human epidermis is a novel site of phospholipase B expression
Import, maturation, and function of SOD1 and its copper chaperone CCS in the mitochondrial intermembrane space
Dynamics of the phosphoinositide 3-kinase p110? interaction with p85? and membranes reveals aspects of regulation distinct from p110?
A conserved family of enzymes that phosphorylate inositol hexakisphosphate
Molecular cloning and characterization of a novel 3'-phosphoadenosine 5'-phosphosulfate transporter, PAPST2
mTORC1 links protein quality and quantity control by sensing chaperone availability
Regulation of repair of alkylation damage in mammalian genomes.
Prog Nucleic Acid Res Mol Biol 44:109-42
TGIF2 interacts with histone deacetylase 1 and represses transcription
Rsk-2 activity is necessary for epidermal growth factor-induced phosphorylation of CREB protein and transcription of c-fos gene
Tissue-differential expression of two distinct genes for phosphoribosyl pyrophosphate synthetase and existence of the testic-specific transcript
Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1).
CRTAP is required for prolyl 3- hydroxylation and mutations cause recessive osteogenesis imperfecta
Primary megakaryocytes reveal a role for transcription factor NF-E2 in integrin alpha IIb beta 3 signaling
VEGF signaling through NADPH oxidase-derived ROS
PI 3-kinase p110beta: a new target for antithrombotic therapy
Syndecan-2 induces filopodia and dendritic spine formation via the neurofibromin-PKA-Ena/VASP pathway
Activation of phospholipase C gamma by PI 3-kinase-induced PH domain-mediated membrane targeting
The complex route to MHC class I-peptide complexes
PURIFICATION AND PROPERTIES OF GLUTATHIONE REDUCTASE OF HUMAN ERYTHROCYTES
Cardiolipin is synthesized on the matrix side of the inner membrane in rat liver mitochondria
ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules
The crystal structure of the beta-catenin/ICAT complex reveals the inhibitory mechanism of ICAT
Robo3 antagonizes Robo1/Robo2 to allow floor plate crossing
Neogenin binds repulsive guidance molecules (RGDs)
Molecular, functional, and genomic characterization of human KCC2, the neuronal K-Cl cotransporter
Organization and sequence of the human gene for the mitochondrial citrate transport protein
Translocation of Ezrin to plasma membrane
Casein kinase 2 associates with and phosphorylates dishevelled
Inhibition of integrin activation by sequestering PIP5KIgamma
Myosin regulatory light chain phosphorylation by ROCK
IL3 stimulation induces Vav binding to Tec kinase
Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity
NCAM1:pFAK:Grb2:Sos-mediated nucleotide exchange of Ras
Recruitment of FAK to NCAM1:Fyn in lipid rafts
Interaction of ISG15 with NEDD4 and inhibition of Ebola virus budding
ISGylation of protein translation regulator 4EHP
Molecular interplay between endostatin, integrins, and heparan sulfate
Caspase-1 precursor is cleaved releasing p10 and p20 subunits
Competitive inhibition of translation initiation by ISGylated 4EHP
Interaction of E3 ligase with ISG15:E2 complex
Translocation of CaN:CaM:NFAT to nucleus
Beta oxidation of hexanoyl-CoA to butanoyl-CoA
FoxM1 promotes ?-catenin nuclear localization and controls Wnt target-gene expression and glioma tumorigenesis
SOS mediated nucleotide exchange of RAS (SHC)
Phosphorylation of PLC-gamma by p-BTK/p-SYK
Interaction of GRB2:SOS complex with p-SHC1
Recruitment of PAK to the membrane by binding active RAC1
Stepwise proteolytic activation of type I procollagen to collagen within the secretory pathway of tendon fibroblasts in situ
Identification and characterization of NVP-BKM120, an orally available pan-class I PI3-kinase inhibitor
Nephrolithiasis and osteoporosis associated with hypophosphatemia caused by mutations in the type 2a sodium-phosphate cotransporter
Requirement of p38 mitogen-activated protein kinase for neuronal differentiation in PC12 cells
Molecular cloning and expression of the human delta7-sterol reductase
Subcellular localization and secretion of factor V from human platelets
A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system
ERKs are inactivated by dual-specific phosphatases (DUSPs)
RSK1/2/3 phosphorylates CREB at Serine 133
ERKs are inactivated by protein phosphatase 2A
ERK5 activates the transcription factor MEF2
Growth-related renal type II Na/Pi cotransporter
Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein
Dre2, a conserved eukaryotic Fe/S cluster protein, functions in cytosolic Fe/S protein biogenesis
MAPKAPK2 phosphorylates CREB at Serine 133
VEGFA dimer:p-6Y-VEGFR2 dimer:PI3K phosphorylates PIP2 to PIP3
VEGF induces CDC42 activation by unknown mechanism
DAG and Ca+2 bind to PKC and tether it to membrane
PKC alpha interacts with and phosphorylates KIT
SHC1 phosphorylation by ERBB2 heterodimers
SHC1 binds phosphorylated ERBB2 heterodimers
Trans-autophosphorylation of ERBB2 heterodimers
Trans-autophosphorylation of p-Y877-ERBB2 heterodimers
RAS guanyl-nucleotide exchange mediated by SOS1 in complex with GRB2 and phosphorylated EGFR:ERBB2 heterodimers.
GRB2:SOS1 complex binds phosphorylated EGFR:ERBB2 heterodimer
RAS guanyl-nucleotide exchange mediated by SOS1 in complex with GRB2 and p-SHC1:Phosphorylated ERBB2 heterodimers
Recruitment of GRB2:SOS1 to p-SHC1 in complex with phosphorylated ERBB2 heterodimers
RAS guanyl nucleotide exchange mediated by SOS1 bound to GRB2 in complex with phosphorylated ERBB4:ERBB2 heterodimers
CHIP (STUB1) mediates ubiquitination of ERBB2
RAS guanyl-nucleotide exchange mediated by SOS1 in complex with GRB2 and p-Y349,350-SHC1:p-ERBB4
Binding of PI3K subunit p85 (PIK3R1) to GRB2:GAB1 in complex with phosphorylated heterodimer of ERBB2 and EGFR.
Recruitment of catalytic PI3K subunit p110 (PIK3CA) by PIK3R1 bound to GRB2:GAB1 in complex with phosphorylated heterodimer of ERBB2 and EGFR
PIP2 to PIP3 conversion by PI3K bound to GRB2:GAB1 in complex with phosphorylated heterodimer of ERBB2 and EGFR
Phospholipase C gamma 1 (PLCG1) binds to phosphorylated ERBB2:EGFR heterodimer
Recruitment of PI3K subunit p110 (PIK3CA) by PIK3R1 bound to phosphorylated heterodimer of ERBB2 and ERBB3.
Conversion of PIP2 into PIP3 by PI3K bound to p-ERBB4cyt1 homodimers
Sequential actions of myotubularin lipid phosphatases regulate endosomal PI(3)P and growth factor receptor trafficking
Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation
The formation of a disulfide cross-link between the two subunits demonstrates the dimeric structure of the mitochondrial oxoglutarate carrier
Severe phenotype of phosphorylase kinase-deficient liver glycogenosis with mutations in the PHKG2 gene
Binding of NCK to SOS and activation of ras-dependent gene expression
Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design
c-Cbl is tyrosine-phosphorylated by interleukin-4 and enhances mitogenic and survival signals of interleukin-4 receptor by linking with the phosphatidylinositol 3'-kinase pathway
Phosphorylation of I kappa B alpha precedes but is not sufficient for its dissociation from NF-kappa B
The localization of human cyclins B1 and B2 determines CDK1 substrate specificity and neither enzyme requires MEK to disassemble the Golgi apparatus
5' incision leading to excision of DNA fragment with lesion in TC-NER
Resumption of transcription after TC-NER
Ligation of newly synthesized repair patch to incised DNA in TC-NER
MSH2:MSH6 binds 1 base mismatch or 1-2 base insertion/deletion loop
MutSalpha binds mismatch or 1-2 base insertion/deletion loop
MSH2:MSH6 recruits MLH1:PMS2 to mismatch and interacts with PCNA
MutSalpha binds ATP and recruits MutLalpha to mismatch
Synaptic uptake and beyond: the sodium- and chloride-dependent neurotransmitter transporter family SLC6
MLH1:PMS2 makes single strand incision near 1-2 base mismatch
EXO1 interacts with MSH2:MSH6 (MutSalpha) and MLH1:PMS2 (MutLalpha)
DNA ligase I ligates single stranded nick in double stranded DNA
MLH1:PMS2 makes single strand incision near insertion/deletion loop of 2 bases or more
Hydrolysis of cAMP to 5' AMP by Phosphorylated PDE3B
EXO1 interacts with MSH2:MSH3 (MutSbeta) and MLH1:PMS2 (MutLalpha)
Phosphorylation and activation of eIF4G by activated S6K1
Phosphorylation and inactivation of eEF2K by activated S6K1
Phosphorylation of Ribosomal protein S6 by activated S6K1
LKB1 forms a trimeric complex with STRAD and MO25
Activation of cytosolic AMPK by phosphorylation
Mutation and polymorphism spectrum of the GALNS gene in mucopolysaccharidosis IVA (Morquio A)
SOS phosphorylation and dissociation (SHC)
GTP-bound RAC contributes to JNK activation
Active JNK moves to the nucleus and phosphorylates different transcription factors
Re-integration of insulin receptor into plasma membrane
p75NTR indirectly activates RAC and Cdc42 via a guanyl-nucleotide exchange factor
TRKA activation by adenosine A2a receptor
Production of ceramide which can activate JNK and other targets
RhoA is activated by nucleotide exchange and inhibits axonal growth
Translational control by the 3'-UTR: the ends specify the means
MAP kinase activates MAPKAPK2, MAPKAPK3 and MSK1
A GIT1/PIX/Rac/PAK signaling module regulates spine morphogenesis and synapse formation through MLC
Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits
(Frs2)C3G stimulates nucleotide exchange on Rap1
(Frs2)Rap1-GTP binds to and activates B-Raf
ARMS is phosphorylated by active TrkA receptor
C3G stimulates nucleotide exchange on Rap1
(ARMS)Rap1-GTP binds and activates B-Raf
Identification of the anti-inflammatory protein tristetraprolin as a hyperphosphorylated protein by mass spectrometry and site-directed mutagenesis
Identification of amino acid residues responsible for the pyrimidine and purine nucleoside specificities of human concentrative Na+ nucleoside cotransporters hCNT1 and hCNT2
MCD encodes peroxisomal and cytoplasmic forms of malonyl-CoA decarboxylase and is mutated in malonyl-CoA decarboxylase deficiency
Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase
Mutations in the gene for the E1beta subunit: a novel cause of pyruvate dehydrogenase deficiency
ADP and platelets: the end of the beginning
Mitochondrial regulation of cell cycle and proliferation
Cloning and characterization of novel mouse and human secretory phospholipase A(2)s
Insights from retinitis pigmentosa into the roles of isocitrate dehydrogenases in the Krebs cycle
MyD88: an adapter that recruits IRAK to the IL-1 receptor complex
Water permeability and characterization of aquaporin-11
Effect of the -Gly-3(S)-hydroxyprolyl-4(R)-hydroxyprolyl- tripeptide unit on the stability of collagen model peptides
CD28 costimulation: a source of Vav-1 for TCR signaling with the help of SLP-76?
WNT5A binding to FZD promotes PRICKLE1 degradation
p-DVL2 recruits AP-2 and beta-arrestin 2 to promote clathrin-mediated endocytosis
VANGL2 is required for asymmetric membrane localization of FZD3
SCRIB is required for asymmetric membrane localization of VANGL2
Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure
Impaired CD8 T cell memory and CD4 T cell primary responses in IL-7R alpha mutant mice
G alpha (12/13) auto-inactivates by hydrolysing GTP to GDP
PIP3 recruits PDK1 and AKT to the membrane
SOS1-mediated nucleotide exchange of RAS (HB-EFG-initiated)
Inactive catalytic PP2B is activated by the binding of calmodulin
The G alpha-olf:GDP:Adenylate cyclase complex dissociates
Adenylaye cyclase increases the GTPase activity of G alpha-olf
Adenylate cyclase converts ATP into cyclic AMP
Galpha-olf:GTP binds to adenylate cyclase and activates it
NEDD4 ubiquitinates ERBB4jmAcyt1s80 dimer
Dissociation of Rho GTP:GDP from GDI complex
GAPs inactivate Rho GTPase:GTP by hydrolysis
Type II receptor phosphorylates type I receptor
The ligand trap binds the ligand BMP2, blocking BMP signalling
Formation of a heteromeric BMP receptor complex
An anchoring protein, Endofin, recruits R-Smad1/5/8
Phospho-R-Smad1/5/8 dissociates from the receptor complex
Activated type I receptor phosphorylates R-Smad1/5/8 directly
Phospho-R-Smad1/5/8 forms a complex with Co-Smad
I-Smad competes with Co-Smad for R-Smad1/5/8
I-Smad competes with R-Smad1/5/8 for type I receptor
The phospho-R-Smad1/5/8:Co-Smad transfers to the nucleus
Interleukin 1alpha-induced NFkappaB activation and chemokine mRNA stabilization diverge at IRAK1
M1, M3 and M5 receptors bind acetylcholine
Alpha-1 adrenoceptors bind catecholamines
D1-like dopamine receptors bind to dopamine
Translocation of ERBB4s80 to the nucleus
Cleavage of ERBB4m80 by gamma-scretase complex
ERBB4s80:STAT5A complex translocates to the nucleus
ERBB4s80 forms a complex with estrogen receptor ESR1
Translocation of cytosolic ERBB4s80 to mitochondrial matrix
E2F4/5 and p107 as Smad cofactors linking the TGFbeta receptor to c-myc repression
G alpha (q) binds to Trio family RhoGEFs
G alpha (z) auto-inactivates by hydrolysing GTP to GDP
Transport of Ca++ from platelet dense tubular system to cytoplasm
Calcium and Diacylglycerol activate CalDAG-GEFs (RasGRPs)
Activation of Protein Kinase C novel isoforms
DAG kinase produces phosphatidic acid from DAG
G alpha (q) auto-inactivates by hydrolysing GTP to GDP
Liganded G12/13-activating GPCR acts as a GEF for G12/13
G alpha (13) activates Rho guanine nucleotide exchange factor 1 (p115-RhoGEF)
Kinesin-2 is a motor for late endosomes and lysosomes
5-HT4, 6 and 7 receptors can bind serotonin
5-HT1 and 5A receptors can bind serotonin
D2-like dopamine receptors bind to dopamine
Integrin alpha(IIb)beta(3) signaling in platelet adhesion and aggregation
Mechanism of diacylglycerol-induced membrane targeting and activation of protein kinase Ctheta
G alpha (s) auto-inactivates by hydrolysing GTP to GDP
Liganded Gi-activating GPCR acts as a GEF for Gi
G alpha (i) auto-inactivates by hydrolysing GTP to GDP
EGF-TM7 receptors bind chondroitin sulphate
Metabotropic glutamate receptors bind glutamate
Adenylate cyclase converts ATP to 3',5'-cyclic AMP (cAMP) and pyrophosphate
Multiple self-healing squamous epithelioma
Birth Defects Orig. Artic. Ser. 7:157-63
Liganded Gz-activating GPCR acts as a GEF for Gz
Targeting mutant fibroblast growth factor receptors in cancer
Molecular identification of a novel mammalian brain isoform of acyl-CoA:lysophospholipid acyltransferase with prominent ethanolamine lysophospholipid acylating activity, LPEAT2
Cellular arachidonate-releasing function of novel classes of secretory phospholipase A2s (groups III and XII)
An estimate of the mean length of collagen fibrils in rat tail-tendon as a function of age
Collagen cross-linking. Purification and substrate specificity of lysyl oxidase
Human TLR10 is a functional receptor, expressed by B cells and plasmacytoid dendritic cells, which activates gene transcription through MyD88
Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts
Disruption of the checkpoint kinase 1/cell division cycle 25A pathway abrogates ionizing radiation-induced S and G2 checkpoints.
Molecular mechanism of the Syk activation switch
Acetylation of beta-catenin by CREB-binding protein (CBP)
Prefoldin mediated transfer of substrate to CCT/TriC
The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology
The molecular defect leading to Fabry disease: structure of human alpha-galactosidase
Inositol polyphosphate multikinase regulates inositol 1,4,5,6-tetrakisphosphate
Cloning, sequencing, and expression of cDNA for human beta-glucuronidase
STRAP and Smad7 synergize in the inhibition of transforming growth factor beta signaling
Inward rectifier potassium channel Kir 2.3 is inhibited by internal sulfhydryl modification
Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig alpha/Ig beta immunoreceptor tyrosine activation motif binding and autophosphorylation
Hypoxia-inducible factor-1 alpha (HIF-1 alpha) escapes O(2)-driven proteasomal degradation irrespective of its subcellular localization: nucleus or cytoplasm
Unraveling the mechanisms of glomerular ultrafiltration: nephrin, a key component of the slit diaphragm
Molecular basis of multidrug transport by ABC transporters
Human liver alcohol dehydrogenase: purification, composition, and catalytic features.
Loss of Hsp90 association up-regulates Src-dependent ErbB2 activity
Differential activation of cysteine-substitution mutants of fibroblast growth factor receptor 3 is determined by cysteine localization
BRF1 protein turnover and mRNA decay activity are regulated by protein kinase B at the same phosphorylation sites
Function and dysfunction of the PI system in membrane trafficking
Rat liver adenosine triphosphate:adenosine monophosphate phosphotransferase activity. II. Subcellular localization of adenylate kinase isozymes
Information networks in the mammary gland
Diversity of the pyruvate dehydrogenase kinase gene family in humans
Rapid destruction of human Cdc25A in response to DNA damage.
Assembly of a complex containing Cdc45p, replication protein A, and Mcm2p at replication origins controlled by S-phase cyclin-dependent kinases and Cdc7p-Dbf4p kinase.
Mechanism of filament nucleation and branch stability revealed by the structure of the Arp2/3 complex at actin branch junctions
Platelet hyperaggregability: impaired responsiveness to nitric oxide ("platelet NO resistance") as a therapeutic target
A human synaptic vesicle monoamine transporter cDNA predicts posttranslational modifications, reveals chromosome 10 gene localization and identifies TaqI RFLPs
Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II
Acta Crystallogr D Biol Crystallogr 56:1385-94
Nuclear CDKs drive Smad transcriptional activation and turnover in BMP and TGF-beta pathways
Biochemistry of soluble guanylate cyclase
Characterization of human A(2B) adenosine receptors: radioligand binding, western blotting, and coupling to G(q) in human embryonic kidney 293 cells and HMC-1 mast cells
Madin-Darby canine kidney II cells: a pharmacologically validated system for NPC1L1-mediated cholesterol uptake
The nature of the phagosomal membrane: endoplasmic reticulum versus plasmalemma
TAK1 is a ubiquitin-dependent kinase of MKK and IKK
Molecular basis for membrane phospholipid diversity: why are there so many lipids?
Highly potent inhibitors of methionine aminopeptidase-2 based on a 1,2,4-triazole pharmacophore
Phosphorylation of Mcm4 at specific sites by cyclin-dependent kinase leads to loss of Mcm4,6,7 helicase activity.
Groucho/TLE family proteins and transcriptional repression
Structural and functional modules in RNA interference
Identification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex
SnoN and Ski protooncoproteins are rapidly degraded in response to transforming growth factor beta signaling
Ras superfamily and interacting proteins database
Functional interaction of beta-catenin with the transcription factor LEF-1
Rap1 regulation of RIAM and cell adhesion
Structure of human isovaleryl-CoA dehydrogenase at 2.6 A resolution: structural basis for substrate specificity,.
Syndecans, heparan sulfate proteoglycans, maintain the proteolytic balance of acute wound fluids
The biochemistry, metabolism and inherited defects of the pentose phosphate pathway: a review
Casein kinase iepsilon in the wnt pathway: regulation of beta-catenin function
Protein kinase A-dependent activation of PDE4 (cAMP-specific cyclic nucleotide phosphodiesterase) in cultured bovine vascular smooth muscle cells
Stabilin-1/CLEVER-1, a type 2 macrophage marker, is an adhesion and scavenging molecule on human placental macrophages
AMPK inhibits chREBP transcriptional activation activity
Molecular characterization of two galactosemia mutations: correlation of mutations with highly conserved domains in galactose-1-phosphate uridyl transferase
HMG box transcription factor TCF-4's interaction with CtBP1 controls the expression of the Wnt target Axin2/Conductin in human embryonic kidney cells
Molecular cloning and functional analysis of SUT-1, a sulfate transporter from human high endothelial venules
A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency
Control of mRNA decay by heat shock-ubiquitin-proteasome pathway
(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA [ChEBI:52050]
Specific interaction of a purified transcription factor with an internal control region of 5S RNA genes
A structural basis for mutational inactivation of the tumour suppressor Smad4
Mutations increasing autoinhibition inactivate tumour suppressors Smad2 and Smad4
Characterization of a human and murine gene (CLCN3) sharing similarities to voltage-gated chloride channels and to a yeast integral membrane protein
Determinants of anion-proton coupling in mammalian endosomal CLC proteins
Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators
Hydrogen peroxide as a signaling molecule
IL-7 promotes T cell proliferation through destabilization of p27Kip1
Structural and catalytic properties and homology modelling of the human nucleoside diphosphate kinase C, product of the DRnm23 gene
Red cell pyruvate kinase deficiency: molecular and clinical aspects
Uptake of insulin and other ligands into receptor-rich endocytic components of target cells: the endosomal apparatus.
Regulation of cytoskeletal remodeling and cell spreading by IPP complex components
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Role of exon 2-encoded beta -domain of the von Hippel-Lindau tumor suppressor protein
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Glucagon signaling in metabolic regulation
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Ubiquitination of p21Cip1/WAF1 by SCFSkp2: substrate requirement and ubiquitination site selection
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Cloning and expression of human deoxyhypusine synthase cDNA. Structure-function studies with the recombinant enzyme and mutant proteins.
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Discovery of an arachidonoyl coenzyme A synthetase in human platelets
Oxidative protein folding in the mitochondrial intermembrane space
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Structure, function, and regulation of cellular tight junctions
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Structural basis for PAS domain heterodimerization in the basic helix--loop--helix-PAS transcription factor hypoxia-inducible factor
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Leptin therapy, insulin sensitivity, and glucose homeostasis
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Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors
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Phosphoribosylpyrophosphate synthesis from glucose decreases during amino acid starvation of human lymphoblasts
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The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response
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The human GCAP1 and GCAP2 genes are arranged in a tail-to-tail array on the short arm of chromosome 6 (p21.1)
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Uridine diphosphate glucose pyrophosphorylase. II
Isolation of the human phosphomannomutase gene (PMM1) and assignment to chromosome 22q13
Human glutamate pyruvate transaminase (GPT): localization to 8q24.3, cDNA and genomic sequences, and polymorphic sites.
Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator
Regulation of matrix metalloproteinase activity in health and disease
Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis
Pre-mRNA splicing: the discovery of a new spliceosome doubles the challenge.
Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav
Genetic complementation reveals a novel human congenital disorder of glycosylation of type II, due to inactivation of the Golgi CMP-sialic acid transporter
C-terminal EH-domain-containing proteins: consensus for a role in endocytic trafficking, EH?
Duodenal cytochrome b: a novel ferrireductase in airway epithelial cells
Am J Physiol Lung Cell Mol Physiol 291:L272-80
ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin
Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions
Crystal structure of human recombinant ornithine aminotransferase.
Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity.
Type II chaperonins, prefoldin, and the tubulin-specific chaperones
Regulation of C/EBPbeta1 by Ras in mammary epithelial cells and the role of C/EBPbeta1 in oncogene-induced senescence
A current view of the mammalian aquaglyceroporins
A unique signal transduction from FLT tyrosine kinase, a receptor for vascular endothelial growth factor VEGF
Glucose transporters (GLUT and SGLT): expanded families of sugar transport proteins
Gefitinib-sensitizing EGFR mutations in lung cancer activate anti-apoptotic pathways
Argonaute2 is the catalytic engine of mammalian RNAi
The versatility and universality of calcium signalling
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A review of the pharmacokinetics of abacavir
Functional and structural analysis of ClC-K chloride channels involved in renal disease
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Purified Argonaute2 and an siRNA form recombinant human RISC
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Targeting FGFR3 in multiple myeloma: inhibition of t(4;14)-positive cells by SU5402 and PD173074
TRF1 inhibits telomere C-strand DNA synthesis in vitro
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Trif-related adapter molecule is phosphorylated by PKC{epsilon} during Toll-like receptor 4 signaling
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clathrin-sculpted monoamine transport vesicle membrane
Regulation of mRNA stability by proteins that bind AU-rich elements
clathrin-sculpted monoamine transport vesicle lumen
Yorkie: the final destination of Hippo signaling
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The t(8;17)(p11;q23) in the 8p11 myeloproliferative syndrome fuses MYO18A to FGFR1
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Mammalian Cdh1/Fzr mediates its own degradation
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Collagen fibrillogenesis in vitro: interaction of types I and V collagen regulates fibril diameter
Tyrosine phosphorylation of the vav proto-oncogene product links FcepsilonRI to the Rac1-JNK pathway
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Purification, cDNA-cloning and expression of human diacylglycerol kinase
Identification and characterization of mutations in patients with holocarboxylase synthetase deficiency
Human acetyl-CoA carboxylase 2. Molecular cloning, characterization, chromosomal mapping, and evidence for two isoforms.
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Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal localization of the corresponding genes
Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI
The diastrophic dysplasia gene encodes a novel sulfate transporter: positional cloning by fine-structure linkage disequilibrium mapping
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Microbial biotin protein ligases aid in understanding holocarboxylase synthetase deficiency
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Signal transduction pathways used by NLR-type innate immune receptors
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Histone-modifying enzymes: regulators of developmental decisions and drivers of human disease
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An IL-2 response element in the human IL-2 receptor alpha chain promoter is a composite element that binds Stat5, Elf-1, HMG-I(Y) and a GATA family protein
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Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA
Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse
Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy
PP2A-regulatory subunit B55 alpha isoform
Rat liver cysteine sulfinate decarboxylase: purification, new appraisal of the molecular weight and determination of catalytic properties
Ankyrin repeat and LEM domain-containing protein 2
Myosin X is a downstream effector of PI(3)K during phagocytosis
Isolation and functional expression of human COQ2, a gene encoding a polyprenyl transferase involved in the synthesis of CoQ
Organic anion transporting polypeptides of the OATP/ SLC21 family: phylogenetic classification as OATP/ SLCO superfamily, new nomenclature and molecular/functional properties
Structural maintenance of chromosome 1-like 1 protein (SMC1alpha protein) (SB1.8/DXS423E protein) (Sb1.8)
Structural maintenance of chromosome 1-like 1 protein
Type I Collagen D-Spacing in Fibril Bundles of Dermis, Tendon, and Bone: Bridging between Nano- and Micro-Level Tissue Hierarchy
Genetics of lactase persistence and lactose intolerance
Cohesin loading complex subunit SCC4 homolog
Structural maintenance of chromosomes protein 3
Sister chromatid cohesion protein PDS5 homolog B
Sister chromatid cohesion protein PDS5 homolog A
COSMIC: mining complete cancer genomes in the Catalogue of Somatic Mutations in Cancer
D-2-hydroxyglutaric acidaemia: identification of a new enzyme, D-2-hydroxyglutarate dehydrogenase, localized in mitochondria
Conservation of the Caenorhabditis elegans timing gene clk-1 from yeast to human: a gene required for ubiquinone biosynthesis with potential implications for aging
Regulation of origin recognition complex conformation and ATPase activity: differential effects of single-stranded and double-stranded DNA binding.
Identification of two mammalian reductases involved in the two-carbon fatty acyl elongation cascade
Thanatophoric dysplasia (types I and II) caused by distinct mutations in fibroblast growth factor receptor 3
Inactivation, recovery and regulation of the phototransduction cascade
Genetic defects of folate and cobalamin metabolism
Association of the human SUMO-1 protease SENP2 with the nuclear pore
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Concepts and principles of O-linked glycosylation
Crit. Rev. Biochem. Mol. Biol. 33:151-208
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Identification of amino acids important for the catalytic activity of the collagen glucosyltransferase associated with the multifunctional lysyl hydroxylase 3 (LH3)
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Growth of collagen fibrils produced by human osteosarcoma cells: high-resolution scanning electron microscopy
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620179
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639745
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639733
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_203535.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639751
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639749
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639748
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639747
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2886.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620183
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29878
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624843
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620185
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620186
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620188
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_261728.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625848
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_261054.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625850
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_235907.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652936
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=76384
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5643.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=33153
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_256302.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622905
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5879.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=175979
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_7828.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=175973
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_7788.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625691
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351993
Enzymatic activities of the human AGPAT isoform 3 and isoform 5: localization of AGPAT5 to mitochondria
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351991
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_14554.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351966
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_14110.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=352001
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_14427.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351964
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_13924.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29996
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_14336.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_239988.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619330
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619328
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619327
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619326
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619325
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4982.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620156
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29732
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3483.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620150
Localization of MCM2-7, Cdc45, and GINS to the site of DNA unwinding during eukaryotic DNA replication
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_257694.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620152
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2623.2
Reverse transcriptase motifs in the catalytic subunit of telomerase
Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625657
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625658
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625660
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_254209.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5625661
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1247892
Binding site on macrophages that mediates uptake and degradation of acetylated low density lipoprotein, producing massive cholesterol deposition
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639734
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5639737
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_192396.3
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3046.2
Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and requires a novel Formin homology protein Daam1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29790
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_257926.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620166
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620164
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620163
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620159
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620157
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20291.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=212615
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_14416.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351973
A novel PtdIns3P and PtdIns(3,5)P2 phosphatase with an inactivating variant in centronuclear myopathy
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_14409.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351970
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_14453.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351980
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_76377.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351977
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=73578
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4214.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5523.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29882
Molecular basis of signaling specificity of insulin and IGF receptors: neglected corners and recent advances
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_237757.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_230998.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628012
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11802.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=198827
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=198852
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652493
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_211551.2
Serine/threonine-protein kinase greatwall
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652492
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_220774.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_13855.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=217320
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630014
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630013
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=217315
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_14663.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5627876
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_254288.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11982.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630012
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621678
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621680
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_227868.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652588
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623660
Inhibition of complement activation on the surface of cells after incorporation of decay-accelerating factor (DAF) into their membranes
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623662
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_260279.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630010
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_13844.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=217259
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630009
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630008
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630007
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630006
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652490
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_256715.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_242925.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621669
Identification of the gene responsible for methylmalonic aciduria and homocystinuria, cblC type
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621673
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621671
Double-strand-break repair protein rad21 homolog
Sterol mediated regulation of SREBP-1a,1b,1c and SREBP-2 in cultured human cells
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623661
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621677
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621676
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621675
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3275.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621661
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621663
Comparative study on the thermostability of collagen I of skin and bone: influence of posttranslational hydroxylation of prolyl and lysyl residues
Nuclear envelope phosphatase-regulatory subunit 1
Serine/threonine-protein phosphatase dullard
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2396.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=30373
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621665
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630017
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630016
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621667
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630015
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_236996.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630021
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630019
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630018
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110644
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_261919.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652502
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_235442.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=109386
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=73566
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5673.1
Targeting, import, and dimerization of a mammalian mitochondrial ATP binding cassette (ABC) transporter, ABCB10 (ABC-me)
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ChEBI:60125 N-epsilon-(1-(1-carboxy)ethyl)lysine
Anoctamins are a family of Ca2+ activated Cl- channels
Frequent frameshift mutations of the TCF-4 gene in colorectal cancers with microsatellite instability
Fibroblast growth factors: from molecular evolution to roles in development, metabolism and disease
Cloning of a TGF beta type I receptor that forms a heteromeric complex with the TGF beta type II receptor
A genome-wide RNAi screen for Wnt/beta-catenin pathway components identifies unexpected roles for TCF transcription factors in cancer
Substrate specificity and phosphorylation of antiviral and anticancer nucleoside analogues by human deoxyribonucleoside kinases and ribonucleoside kinases
Mechanism of metal activation of human hematopoietic prostaglandin D synthase
M-phase inducer phosphatase 3 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25C)
Synthesis of PIPs at the early endosome membrane
COPII (Coat Protein 2) Mediated Vesicle Transport
M-phase inducer phosphatase 2 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25B)
Channel-opening kinetics of GluR2Q(flip) AMPA receptor: a laser-pulse photolysis study
Serine/threonine protein phosphatase PP1-beta catalytic subunit
Protein phosphatase 1 regulatory subunit 12B
Myosin phosphatase small regulatory subunit
InsP3-mediated intracellular calcium signalling is altered by expression of synaptojanin-1
Molecular mechanisms involved in the regulation of the endothelial nitric oxide synthase
Am J Physiol Regul Integr Comp Physiol 284:R1-12
Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities.
Mitochondrial aquaporin-8 knockdown in human hepatoma HepG2 cells causes ROS-induced mitochondrial depolarization and loss of viability
Multiple self-healing squamous epithelioma is caused by a disease-specific spectrum of mutations in TGFBR1
The Ca-calmodulin-dependent protein kinase cascade
Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling.
Functional properties and genomics of glucose transporters
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Requirements for alpha-ketoglutarate, ferrous ion and ascorbate by collagen proline hydroxylase
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Primary structure of human triosephosphate isomerase
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Hemopexin: structure, function, and regulation
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Structural basis of Smad1 activation by receptor kinase phosphorylation
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Insulin and insulinomimetic agents induce activation of phosphatidylinositol 3'-kinase upon its association with pp185 (IRS-1) in intact rat livers
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Molecular genetics of Krabbe disease (globoid cell leukodystrophy): diagnostic and clinical implications
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Requirement of the DEAD-Box protein ded1p for messenger RNA translation.
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Cell division protein kinase 4 (EC 2.7.1.- ) (Cyclin-dependent kinase 4) (PSK-J3) (CDK4)
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5,10-methylenetetrahydrofolate polyglutamate
5,10-methylenetetrahydrofolate polyglutamate macromolecule
5,10-methylenetetrahydrofolate polyglutamate macromolecule [ChEBI:60473]
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DNA polymerase alpha holoenzyme-associated protein P1
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The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2.
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Cloning and expression of a human kinesin heavy chain gene: interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cells
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Cloning, sequencing and functional expression of a novel human thioredoxin reductase
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DNA polymerase epsilon, catalytic subunit A
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The oligomeric status of syndecan-4 regulates syndecan-4 interaction with alpha-actinin
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Ribonucleoside-diphosphate reductase M2 chain
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CDK-activating kinase assembly factor MAT1
CDK-activating kinase assembly factor MAT1 (RING finger protein MAT1) (Menage a trois) (CDK7/cyclin H assembly factor) (p36) (p35) (Cyclin G1 interacting protein)
Cell division protein kinase 7 (EC 2.7.1.-) (CDK-activating kinase) (CAK)(TFIIH) (basal transcription factor complex kinase subunit) (39 kDa protein kinase) (P39 Mo15)(STK1)(CAK1)
TFIIH basal transcription factor complex kinase subunit
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Heat shock gene regulation by nascent polypeptides and denatured proteins: hsp70 as a potential autoregulatory factor
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Multicatalytic endopeptidase complex delta chain
Proteasome subunit beta type 6 precursor
Multicatalytic endopeptidase complex chain Z
Proteasome subunit beta type 7 precursor
Multicatalytic endopeptidase complex subunit C13
Proteasome subunit beta type 8 precursor
Multicatalytic endopeptidase complex subunit C7-I
Multicatalytic endopeptidase complex beta chain
Proteasome subunit beta type 4 precursor
Multicatalytic endopeptidase complex epsilon chain
Proteasome subunit beta type 5 precursor
Signal transduction pathway of human fibroblast growth factor receptor 3. Identification of a novel 66-kDa phosphoprotein.
Multicatalytic endopeptidase complex subunit C8
Activator of multicatalytic protease subunit 2
Multicatalytic endopeptidase complex chain 7
Proteasome subunit beta type 9 precursor
Multicatalytic endopeptidase complex subunit C3
Activator of multicatalytic protease subunit 1
Interferon gamma up-regulated I-5111 protein
Activator of multicatalytic protease subunit 3
Multicatalytic endopeptidase complex subunit C5
26S proteasome non-ATPase regulatory subunit 10
26S proteasome non-ATPase regulatory subunit 11
Multicatalytic endopeptidase complex subunit C2
Probable 26S protease regulatory subunit 8
Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding, and angiogenesis activity
Production of phosphatidylinositol 5-phosphate by the phosphoinositide 3-phosphatase myotubularin in mammalian cells
26S proteasome non-ATPase regulatory subunit 12
Proteasome regulatory particle subunit p44S10
26S proteasome non-ATPase regulatory subunit 6
Tumor necrosis factor type 1 receptor associated protein 2
26S proteasome non-ATPase regulatory subunit 2
26S proteasome non-ATPase regulatory subunit 13
Multicatalytic endopeptidase complex subunit C9
Multicatalytic endopeptidase complex zeta chain
Multicatalytic endopeptidase complex iota chain
26S proteasome non-ATPase regulatory subunit 1
Multicatalytic endopeptidase complex subunit MECl-1
Proteasome subunit beta type 10 precursor
Human cytidine deaminase: purification of enzyme, cloning, and expression of its complementary DNA
Maternal genetic effects, exerted by genes involved in homocysteine remethylation, influence the risk of spina bifida
2,2'-dilyso diphosphatidyl glycerol
2,2'-dilyso cardiolipin [ChEBI:60431]
A GDP dissociation inhibitor that serves as a GTPase inhibitor for the Ras-like protein CDC42Hs
Wnt/Ca2+ signaling pathway: a brief overview
Acta Biochim. Biophys. Sin. (Shanghai) 43:745-56
Human intestinal glucose transporter expression and localization of GLUT5
Advances in collagen cross-link analysis
Tyrosine kinase inhibitors of FGFR2 mutants
Tyrosine kinase inhibitors of FGFR1 fusion mutants
Tyrosine kinase inhibitors of FGFR3 mutants
Tyrosine kinase inhibitors of overexpressed FGFR2
Tyrosine kinase inhibitors of overexpressed FGFR1
Irreversible TKI inhibitor afatinib generic inhibits EGFR and ERBB2 (HER2)
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'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of GFPT1'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of ARFGAP1 (GAP)'
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'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of EXTL3'
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'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of EDEM'
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'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of DNAJB11'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of DDX11'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of DCTN1'
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'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of Cullin-7'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of CXXC1'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of CTDSP2'
Caspase-3 activation triggers extracellular cathepsin L release and endorepellin proteolysis
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=217269
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_7485.2
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'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of PPP2R5B'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of PDIA6 (Protein disulfide-isomerase A6)'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of SERP1 (RAMP4)'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of GOSR2'
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'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of HDGF'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of GSK3A'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of KDELR3'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of HYOU1'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of PDIA5'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of KLHDC3'
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_257055.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=30321
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of Talin-1'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of TSPYL2'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of SSR1 (Trap alpha)'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of SRPRB (SRP Receptor subunit beta)'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of SRPR (SRP Receptor subunit alpha)'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of SHC1'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of TATDN2'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of Sec31A'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of Sec12'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of SYVN1 (HRD1)'
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'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of WIPI1'
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'ONECUT1 [nucleoplasm]' positively regulates 'HNF6-dependent synthesis of NEUROG3 protein during morphogenesis'
'NEUROG3 [nucleoplasm]' positively regulates 'NEUROG3-dependent synthesis of PAX4 protein'
'NEUROG3 [nucleoplasm]' positively regulates 'NEUROG3-dependent synthesis of NEUROD1'
'NEUROG3 [nucleoplasm]' positively regulates 'NEUROG3-dependent synthesis of NKX2-2'
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'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of YIF1A'
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'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of ZBTB17'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of DNAJC3 (p58IPK)'
'ONECUT1 [nucleoplasm]' positively regulates 'HNF6-dependent synthesis of ONECUT3 protein during early pancreas specification'
'NEUROG3 [nucleoplasm]' positively regulates 'NEUROG3-dependent synthesis of INSM1'
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'EBF1 [nucleoplasm]' positively regulates 'Maintenance of PPARG expression in differentiated adipocytes'
'NEUROD1 [nucleoplasm]' positively regulates 'NEUROD1- and PDX1-dependent synthesis of glucokinase (GCK) protein'
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'HIF1A [nucleoplasm]' positively regulates 'Expression of RORA (ROR-alpha)'
'NR1D1 (REV-ERBA):heme:Corepressor (name copied from entity in Homo sapiens) [nucleoplasm]' negatively regulates 'Expression of NR1D1 (REV-ERBA)'
'NR1D1 (REV-ERBA):heme:Corepressor (name copied from entity in Homo sapiens) [nucleoplasm]' negatively regulates 'Expression of ELOVL3'
'PPARG:RXRA:Corepressor Complex (name copied from entity in Homo sapiens) [nucleoplasm]' negatively regulates 'Expression of GLUT4'
Human Argonaute2 mediates RNA cleavage targeted by miRNAs and siRNAs
'NR3C1:Dexamethasone (name copied from entity in Homo sapiens) [nucleoplasm]' positively regulates 'Expression of PERIOD-2'
'Homologues of KLF5 [nucleoplasm]' positively regulates 'Maintenance of PPARG expression in differentiated adipocytes'
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'SREBF1A,2 [nucleoplasm]' positively regulates 'Maintenance of PPARG expression in differentiated adipocytes'
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Cloning of the cDNA and gene for a human D2 dopamine receptor
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Isolation and partial characterization of SAA-an amyloid-related protein from human serum
Protein kinase C-theta (PKCtheta) distribution analysis in hematopoietic cells: proliferating T cells exhibit high proportions of PKCtheta in the particulate fraction
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26S proteasome non-ATPase regulatory subunit 3
26S proteasome non-ATPase regulatory subunit 9
26S proteasome non-ATPase regulatory subunit 5
26S proteasome non-ATPase regulatory subunit 4
Role of nuclear and cytoplasmic localization in the tumour-suppressor activity of the von Hippel-Lindau protein
Cell division protein kinase 2 (EC 2.7.1.-)(p33 protein kinase)(CDK2)
26S proteasome non-ATPase regulatory subunit 8
26S proteasome non-ATPase regulatory subunit 7
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Mitochondrial phosphatase PTPMT1 is essential for cardiolipin biosynthesis
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Characterization of mammalian eIF4E-family members
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Transcription factor DP-1 (E2F dimerization partner 1)(DRTF1-polypeptide-1) (DRTF1)
Mutations of the Down-regulated in adenoma (DRA) gene cause congenital chloride diarrhoea
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Identification of the human sphingolipid C4-hydroxylase, hDES2, and its up-regulation during keratinocyte differentiation
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Mutations in the testis/liver isoform of the phosphorylase kinase gamma subunit (PHKG2) cause autosomal liver glycogenosis in the gsd rat and in humans
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Stat5 activation is uniquely associated with cytokine signaling in peripheral T cells
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Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta
G-strand Chromosome end with two additional single strand repeats - Telomeric
NNNNNNNNNNNTTAGGGTTATTAGGGTTATTAGGGTTA - 3' (in human)
1-phosphatidyl-1D-myo-inositol 4,5- bisphosphate
phosphatidylinositol 1,4,5-trisphosphate
Constitutive receptor activation by Crouzon syndrome mutations in fibroblast growth factor receptor (FGFR)2 and FGFR2/Neu chimeras
Gastrin-CREB signalling pathway via PKC and MAPK
Reversible EGFR-specific tyrosine kinase inhibitors
Reversible tyrosine kinase inhibitor erlotinib EGFR specific
DNA Replication factor A protein A1 (70kD)
Replication protein A 70 kDa DNA-binding subunit
Activator 1 36 kDa subunit (Replication factor C 36 kDa subunit) (A1 36 kDa subunit) (RF-C 36 kDa subunit) (RFC36)
Cell signalling diversity of the Gqalpha family of heterotrimeric G proteins
Heparan sulfate proteoglycans are ligands for receptor protein tyrosine phosphatase sigma
Reversible tyrosine kinase inhibitor gefitinib EGFR specific
Reversible anti-EGFRplus tyrosine kinase inhibitors
Reversible tyrosine kinase inhibitor lapatinib generic inhibits EGFR and ERBB2 (HER2)
Proteomic identification of proteins conjugated to ISG15 in mouse and human cells
Reversible tyrosine kinase inhibitor vandetanib generic inhibits EGFR and VEGFR
Irreversible EGFR-specific tyrosine kinase inhibitors
Irreversible tyrosine kinase inhibitor pelitinib EGFR specific
Irreversible tyrosine kinase inhibitor WZ4002 EGFR specific
Irreversible anti-EGFRplus tyrosine kinase inhibitors
Irreversible tyrosine kinase inhibitor HKI-272 generic inhibits EGFR and ERBB2 (HER2)
Irreversible TKI inhibitor canertinib generic pan-ERBB
Retinyl ester hydrolytic activity associated with human intestinal brush border membranes
Human TLR9 confers responsiveness to bacterial DNA via species-specific CpG motif recognition
Phosphatidylinositol transfer proteins: from closed for transport to open for exchange
Molecular cloning and the functional expression of two isoforms of human metabotropic glutamate receptor subtype 5
CYP2U1, a novel human thymus- and brain-specific cytochrome P450, catalyzes omega- and (omega-1)-hydroxylation of fatty acids
Formation of tubulin folding intermediates by CCT/TriC
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XVII) ectodomain
Homologues of 3x4Hyp-3Hyp-GalHyl-COL17A1(?-1497)
The predicted ATP-binding domains in the hexose transporter GLUT1 critically affect transporter activity.
Structural insights into the dehydroascorbate reductase activity of human omega-class glutathione transferases
Critical role of STAT5 activation in transformation mediated by ZNF198-FGFR1
Interleukin (IL)-3 and granulocyte/macrophage colony-stimulating factor, but not IL-4, induce tyrosine phosphorylation, activation, and association of SHPTP2 with Grb2 and phosphatidylinositol 3'-kinase
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NF-kappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase
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Human autoantibodies against the 54 kDa protein of the signal recognition particle block function at multiple stages
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_212164.2
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Structural determinants of heparan sulfate interactions with Slit proteins
Three-dimensional structure of 6-pyruvoyl tetrahydropterin synthase, an enzyme involved in tetrahydrobiopterin biosynthesis
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The mucopolysaccharidoses: a success of molecular medicine
Evidence that microRNAs are associated with translating messenger RNAs in human cells
Functional properties of a Drosophila homolog of the E2F1 gene
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Pnpla3/Adiponutrin deficiency in mice does not contribute to fatty liver disease or metabolic syndrome
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Molecular basis of mitochondrial fatty acid oxidation defects.
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Endorepellin laminin-like globular 1/2 domains bind Ig3-5 of vascular endothelial growth factor (VEGF) receptor 2 and block pro-angiogenic signaling by VEGFA in endothelial cells
Ryk-mediated Wnt repulsion regulates posterior-directed growth of corticospinal tract
Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator
Regulation of growth cone actin dynamics by ADF/cofilin
Activated Cdc42 sequesters c-Cbl and prevents EGF receptor degradation
RNA Pol II CTD phosphorylation and interaction with CE
N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-Asn residue [ChEBI:60625]
N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-Asn residue
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DNA mismatch repair and mutation avoidance pathways
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Serine/threonine-protein kinase Chk1 (EC 2.7.1.-)
Structural model of carnitine palmitoyltransferase I based on the carnitine acetyltransferase crystal
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Fcgamma receptors: old friends and new family members
Nuclear organization of DNA replication initiation proteins in mammalian cells.
A highly conserved repetitive DNA sequence, (TTAGGG)n, present at the telomeres of human chromosomes
Cloning and expression in vitro of human xanthine dehydrogenase/oxidase
Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1
3,4-Hyp 5-Hyl-collagen alpha-1(XVII) ectodomain
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3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XVII) ectodomain
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Homologues of 3x4Hyp-3Hyp-GlcGalHyl-COL17A1(?-1497)
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The Ski oncoprotein interacts with the Smad proteins to repress TGFbeta signaling
A functional interaction between the histone deacetylase Rpd3 and the corepressor groucho in Drosophila development
Molecular cloning and functional characterization of novel zinc transporter rZip10 (Slc39a10) involved in zinc uptake across rat renal brush-border membrane
VEGF-induced Rac1 activation in endothelial cells is regulated by the guanine nucleotide exchange factor Vav2
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Homologues of 3x4Hyp-3Hyp-5Hyl-COL17A1(?-1497)
Role of membrane cofactor protein (CD46) in regulation of C4b and C3b deposited on cells
3,4-hydroxyprolyl-collagen alpha-1(XVII) ectodomain
4-Hyp 5-Gal-Hyl-collagen alpha-1(XVII) ectodomain
Homologues of 3x4Hyp-GalHyl-COL17A1(?-1497)
Cross-linking and the molecular packing of corneal collagen
The human collagen beta(1-O)galactosyltransferase, GLT25D1, is a soluble endoplasmic reticulum localized protein
Homologues of 3x4Hyp-3Hyp-COL17A1(?-1497)
Homologues of 3x4Hyp-GlcGalHyl-COL17A1(?-1497)
4-Hyp 5-Hyl-collagen alpha-1(XVII) ectodomain
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XVII) ectodomain
Homologues of 3x4Hyp-5Hyl-COL17A1(?-1497)
Deciphering human heat shock transcription factor 1 regulation via post-translational modification in yeast
QLS motif in transmembrane helix VII of the glucose transporter family interacts with the C-1 position of D-glucose and is involved in substrate selection at the exofacial binding site.
Novel functions of acyl-CoA thioesterases and acyltransferases as auxiliary enzymes in peroxisomal lipid metabolism
Effects of the GABA-reuptake inhibitor tiagabine on panic and anxiety in patients with panic disorder
Stem cell factor and its receptor c-Kit as targets for inflammatory diseases
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The biochemical and structural basis for trans-to-cis isomerization of retinoids in the chemistry of vision
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Sustained entry of Ca2+ is required to activate Ca2+-calmodulin-dependent phosphodiesterase 1A
The genetics of mammalian circadian order and disorder: implications for physiology and disease
Mechanism underlying replication protein a stimulation of DNA ligase I
The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins
The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switch
Transcriptional activation domains stimulate initiation and elongation at different times and via different residues
Tau-crystallin/alpha-enolase: one gene encodes both an enzyme and a lens structural protein
Characterization of CDw92 as a member of the choline transporter-like protein family regulated specifically on dendritic cells
Cell cycle and death control: long live Forkheads
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Ral GTPase-activating protein subunit beta
PAK and other Rho-associated kinases--effectors with surprisingly diverse mechanisms of regulation
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Cloning and expression of a human serotonin 5-HT4 receptor cDNA
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Ral GTPase-activating protein subunit alpha-2
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The neuronal channel NALCN contributes resting sodium permeability and is required for normal respiratory rhythm
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Releasing cohesin from chromosome arms in early mitosis: opposing actions of Wapl-Pds5 and Sgo1
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Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases
Solute carrier family 2, facilitated glucose transporter member 4
Activation of ErbB4 by the bifunctional epidermal growth factor family hormone epiregulin is regulated by ErbB2
A uniform human Wnt expression library reveals a shared secretory pathway and unique signaling activities
Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis
Serine/threonine-protein kinase Chk2 (EC 2.7.1.-) (Cds1)
M-phase inducer phosphatase 1 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25A)
Dynamin II binds to the trans-Golgi network
Glucose transporter type 4, insulin-responsive
Solute carrier family 2, facilitated glucose transporter, member 4
4-hydroxyprolyl collagen alpha-1(XVII) ectodomain
ERK6, a mitogen-activated protein kinase involved in C2C12 myoblast differentiation
Regulators of neurite outgrowth: role of cell adhesion molecules
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5-Gal-Hyl-collagen alpha-1(XVII) ectodomain
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The protein that binds the 3' end of histone mRNA: a novel RNA-binding protein required for histone pre-mRNA processing.
5-hydroxylysyl-collagen alpha-1(XVII) ectodomain
Protein kinase C and a calcium-independent phospholipase are required for IgG-mediated phagocytosis by Mono-Mac-6 cells
NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression, purification, and kinetic properties
Glu-Gal-Hyl-collagen alpha-1(XVII) ectodomain
Expression, purification, and characterization of human and rat acetyl coenzyme A carboxylase (ACC) isozymes
Structural basis for engagement by complement factor H of C3b on a self surface
Preferential cleavage of chromatin-bound cohesin after targeted phosphorylation by Polo-like kinase
Role of liver sinusoidal endothelial cells and stabilins in elimination of oxidized low-density lipoproteins
Am J Physiol Gastrointest Liver Physiol 300:G71-81
SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin
Does cellular hydrogen peroxide diffuse or act locally?
Mutation analysis of the MCM gene in Israeli patients with mut(0) disease
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Lysyl oxidases in mammalian development and certain pathological conditions
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'E2F1:TFDP1 (name copied from entity in Homo sapiens) [nucleoplasm]' positively regulates 'Activation of E2F target genes at G1/S'
'E2F1/2/3 [nucleoplasm]' positively regulates 'CDC6 protein is synthesized under the control of E2F transcription factors'
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'ROS [cytosol]' positively regulates 'Expression of MINK1/TNIK is positively regulated by ROS'
Molecular cloning and characterization of multispecific organic anion transporter 4 expressed in the placenta
'HIF:CBP:p300 (name copied from entity in Homo sapiens) [nucleoplasm]' positively regulates 'Expression of Carbonic Anhydrase IX (CA9)'
'NF-Y (name copied from entity in Homo sapiens) [nucleoplasm]' positively regulates 'Expression of Xbp1(S)'
'NF-Y (name copied from entity in Homo sapiens) [nucleoplasm]' positively regulates 'Expression of BIP (78 kDa Glucose-regulated protein, GRP78, HSPA5)'
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'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of ADD1 (Adducin alpha)'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of ACADVL'
'Homologues of XBP1-2 [nucleoplasm]' positively regulates 'Expression of ATP6VOD1'
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The function of ascorbate with respect to prolyl 4-hydroxylase activity
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Mechanisms of phagocytosis in macrophages
The MuvB complex sequentially recruits B-Myb and FoxM1 to promote mitotic gene expression
Immunodeficiency in protein kinase cbeta-deficient mice
Protein-tyrosine phosphatase 1D modulates its own state of tyrosine phosphorylation
GAP Recruitment to the Coatomer:Arf1-GTP Complex
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Cargo, Sec31p:Sec13p, and v-SNARE recruitment
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Wnt-induced dephosphorylation of axin releases beta-catenin from the axin complex
G alpha 12 and G alpha 13 stimulate Rho-dependent stress fiber formation and focal adhesion assembly
The complement protein properdin binds apoptotic T cells and promotes complement activation and phagocytosis
Proc. Natl. Acad. Sci. U.S.A. 105:9023-8
Homologues of 3x4Hyp-GalHyl-COL25A1(1-?)
Cloning and expression of a novel Na(+)-dependent neutral amino acid transporter structurally related to mammalian Na+/glutamate cotransporters
A novel nuclear export signal in Smad1 is essential for its signaling activity
Homologues of 3x4Hyp-GlcGalHyl-COL25A1(1-?)
Homologues of 3x4Hyp-3Hyp-GalHyl-COL25A1(1-?)
Vacuolar protein sorting-associated protein 4B
Homologues of 3x4Hyp-3Hyp-GlcGalHyl-COL25A1(1-?)
Homologues of 3x4Hyp-3Hyp-5Hyl-COL25A1(1-?)
Vacuolar protein sorting-associated protein 4A
3,4-Hyp 5-Hyl-collagen alpha-1(XXIII) ectodomain
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXIII) ectodomain
3,4-hydroxyprolyl-collagen alpha-1(XXIII) ectodomain
4-Hyp 5-Gal-Hyl-collagen alpha-1(XXIII) ectodomain
4-Hyp 5-Hyl-collagen alpha-1(XXIII) ectodomain
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXIII) ectodomain
4-hydroxyprolyl collagen alpha-1(XXIII) ectodomain
Alteration of decreased plasma NO metabolites and platelet NO synthase activity by paroxetine in depressed patients
5-Gal-Hyl-collagen alpha-1(XXIII) ectodomain
5-hydroxylysyl-collagen alpha-1(XXIII) ectodomain
Endostatin: an endogenous inhibitor of angiogenesis and tumor growth
The mitochondrial ADP/ATP carrier: structural, physiological and
Glu-Gal-Hyl-collagen alpha-1(XXIII) ectodomain
Collagen alpha-1(XXIII) transmembrane regions
Vacuolar protein-sorting-associated protein 36
Hepatocyte growth factor-regulated tyrosine kinase substrate
Vacuolar protein-sorting-associated protein 25
Reversible ATP-dependent transition between two forms of human cytosolic thymidine kinase with different enzymatic properties
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XXIII) ectodomain
Histamine-H1-receptor-mediated phosphoinositide hydrolysis, Ca2+ signalling and membrane-potential oscillations in human HeLa carcinoma cells
cDNA cloning of carboxyl ester lipase from human pancreas reveals a unique proline-rich repeat unit
Beyond Wnt inhibition: new functions of secreted Frizzled-related proteins in development and disease
MHC class I endosomal and lysosomal trafficking coincides with exogenous antigen loading in dendritic cells
Transport of hypoxia-inducible factor HIF-1alpha into the nucleus involves importins 4 and 7
Evidence for association of GABA(B) receptors with Kir3 channels and regulators of G protein signalling (RGS4) proteins
The amino acid sequence of cytosolic aspartate aminotransferase from human liver
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XXV) ectodomain
Homologues of 3x4Hyp-3Hyp-GalHyl-COL25A1(?-654)
The E3 ligase Aip4/Itch ubiquitinates and targets ErbB-4 for degradation
Cloning and functional expression of a human Na(+) and Cl(-)-dependent neutral and cationic amino acid transporter B(0+)
Functional characterization of human aquaporin 9 as a facilitative glycerol carrier
Regulation of transcription by hypoxia requires a multiprotein complex that includes hypoxia-inducible factor 1, an adjacent transcription factor, and p300/CREB binding protein
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Intracellular signaling pathways activated by neurotrophic factors
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IL-5- and eosinophil-mediated inflammation: from discovery to therapy
Leptin receptor signaling: pathways to leptin resistance
Shc and a novel 89-kDa component couple to the Grb2-Sos complex in fibroblast growth factor-2-stimulated cells
Embryonic expression of type XIX collagen is transient and confined to muscle cells
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Mutation in the glutamate transporter EAAT1 causes episodic ataxia, hemiplegia, and seizures
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Glucose and cAMP regulate the L-type pyruvate kinase gene by phosphorylation/dephosphorylation of the carbohydrate response element binding protein
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Cellular localization of THIK-1 (K(2P)13.1) and THIK-2 (K(2P)12.1) K channels in the mammalian kidney
Mitochondrial ATP-binding cassette proteins
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Structure and function of laminin LG modules
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3,4-Hyp 5-Hyl-collagen alpha-1(XXV) ectodomain
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3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXV) ectodomain
Homologues of 3x4Hyp-3Hyp-GlcGalHyl-COL25A1(?-654)
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Homologues of 3x4Hyp-3Hyp-5Hyl-COL25A1(?-654)
Identification of differentiation-associated brain-specific phosphate transporter as a second vesicular glutamate transporter (VGLUT2)
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The role of adipokines in beta-cell failure of type 2 diabetes
Genetic disorders of vitamin B12 metabolism: eight complementation groups--eight genes
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Tissue-specific expression of the fibril-associated collagens XII and XIV
Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation
Glu-Gal-Hyl-collagen alpha-1(XXV) ectodomain
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Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control
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Basement membrane-specific heparan sulfate proteoglycan core protein
LASS5 is a bona fide dihydroceramide synthase that selectively utilizes palmitoyl-CoA as acyl donor
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Epithelial sodium channel regulated by differential composition of a signaling complex
Proc. Natl. Acad. Sci. U.S.A. 106:7804-9
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A protein cofactor of lecithin:cholesterol acyltransferase
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Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly
Heat shock factors: integrators of cell stress, development and lifespan
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A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP
Molecular mechanisms regulating hormone-sensitive lipase and lipolysis
Heat shock factor-1 protein in heat shock factor-1 gene-transfected human epidermoid A431 cells requires phosphorylation before inducing heat shock protein-70 production
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3,4-hydroxyprolyl-collagen alpha-1(XXV) ectodomain
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Homologues of 3x4Hyp-GalHyl-COL25A1(?-654)
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4-Hyp 5-Gal-Hyl-collagen alpha-1(XXV) ectodomain
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Homologues of 3x4Hyp-3Hyp-COL25A1(?-654)
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Multimerin is found in the alpha-granules of resting platelets and is synthesized by a megakaryocytic cell line
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4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXV) ectodomain
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Homologues of 3x4Hyp-GlcGalHyl-COL25A1(?-654)
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4-Hyp 5-Hyl-collagen alpha-1(XXV) ectodomain
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Making sense of latent TGFbeta activation
Homologues of 3x4Hyp-5Hyl-COL25A1(?-654)
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4-hydroxyprolyl collagen alpha-1(XXV) ectodomain
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5-Gal-Hyl-collagen alpha-1(XXV) ectodomain
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5-hydroxylysyl-collagen alpha-1(XXV) ectodomain
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The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation
Human pyridoxal kinase: overexpression and properties of the recombinant enzyme
Roles of glial p75NTR in axonal regeneration
An updated overview on Wnt signaling pathways: a prelude for more
Analysis of proteoglycan expression in developing chicken brain: characterization of a heparan sulfate proteoglycan that interacts with the neural cell adhesion molecule
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Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation
The TAK1-NLK mitogen-activated protein kinase cascade functions in the Wnt-5a/Ca(2+) pathway to antagonize Wnt/beta-catenin signaling
A structural model for the membrane-integral domain of succinate: quinone
Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase
Expression of two forms of human dopamine-beta-hydroxylase in COS cells
Nicotine and sympathetic neurotransmission
Modulation of human heat shock factor trimerization by the linker domain
Cross-presentation of particulate exogenous antigens (phagosomes)
Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta
Synergistic activation of the Wnt signaling pathway by Dvl and casein kinase Iepsilon
Peroxisomal branched chain fatty acid beta-oxidation pathway is upregulated in prostate cancer
Antigen activates B Cell Receptor (BCR) leading to generation of second messengers
CYP3A4, CYP3A5, and CYP3A43 genotypes and haplotypes in the etiology and severity of prostate cancer
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Mutations in the 3beta-hydroxysterol Delta24-reductase gene cause desmosterolosis, an autosomal recessive disorder of cholesterol biosynthesis
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Biochemical characterization of human collagenase-3
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Feedback regulation mechanisms for the control of GTP cyclohydrolase I activity
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The docking protein FRS2alpha controls a MAP kinase-mediated negative feedback mechanism for signaling by FGF receptors
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IRAK-2 participates in multiple toll-like receptor signaling pathways to NFkappaB via activation of TRAF6 ubiquitination
The ABCs of solute carriers: physiological, pathological and therapeutic implications of human membrane transport proteinsIntroduction
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Targeting the phosphoinositide 3-kinase pathway in cancer
RNA Polymerase II Transcription Initiation
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Missense FGFR3 mutations create cysteine residues in thanatophoric dwarfism type I (TD1)
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IL-3 signaling and the role of Src kinases, JAKs and STATs: a covert liaison unveiled
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The role of Stat5a and Stat5b in signaling by IL-2 family cytokines
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Human isopentenyl diphosphate: dimethylallyl diphosphate isomerase: overproduction, purification, and characterization
Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane
Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism
TGFbeta1 inhibits the formation of benign skin tumors, but enhances progression to invasive spindle carcinomas in transgenic mice
cyclic purine dinucleotide [ChEBI:47037]
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A mannosyltransferase gene at 11q23 is disrupted by a translocation breakpoint that co-segregates with bipolar affective disorder in a small family
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Antisense co-suppression of G(alpha)(q) and G(alpha)(11) demonstrates that both isoforms mediate M(3)-receptor-activated Ca(2+) signalling in intact epithelial cells
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AKT phosphorylates targets in the cytosol
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The NC1 domain of type XIX collagen inhibits in vivo melanoma growth
Molecular cloning and characterization of a novel chondroitin sulfate glucuronyltransferase that transfers glucuronic acid to N-acetylgalactosamine
Pontin52 and reptin52 function as antagonistic regulators of beta-catenin signalling activity
Separation of prolyl 3-hydroxylase and 4-hydroxylase activities and the 4-hydroxyproline requirement for synthesis of 3-hydroxyproline
Human GTP cyclohydrolase I: only one out of three cDNA isoforms gives rise to the active enzyme
Thioredoxin-interacting protein links oxidative stress to inflammasome activation
Characterization of the 5-HT6 receptor coupled to Ca2+ signaling using an enabling chimeric G-protein
Human lactase-phlorizin hydrolase: evidence of dimerization in the endoplasmic reticulum
Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases
Origin, Recognition, Signaling and Repair of DNA Double-Strand Breaks in Mammalian Cells
Damage Surveillance and Repair (Keith Caldecott, editor)1-40
Efficient activation of aflatoxin B1 by cytochrome P450 2A13, an enzyme predominantly expressed in human respiratory tract
Conservation of the human telomere sequence (TTAGGG)n among vertebrates
A gene encoding a putative FAD-dependent L-2-hydroxyglutarate dehydrogenase is mutated in L-2-hydroxyglutaric aciduria
mTOR is essential for the proteotoxic stress response, HSF1 activation and heat shock protein synthesis
Sex-dependent liver gene expression is extensive and largely dependent upon signal transducer and activator of transcription 5b (STAT5b): STAT5b-dependent activation of male genes and repression of female genes revealed by microarray analysis
Cell junction-associated proteins IQGAP1, MAGI-2, CASK, spectrins, and alpha-actinin are components of the nephrin multiprotein complex
System-wide investigation of ErbB4 reveals 19 sites of Tyr phosphorylation that are unusually selective in their recruitment properties
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Cloning of the human sodium lodide symporter
Endosomal proteolysis of internalized proteins.
Understanding specificity in metabolic pathways--structural biology of human nucleotide metabolism
ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways
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Type-III procollagen assembly in semi-intact cells: chain association, nucleation and triple-helix folding do not require formation of inter-chain disulphide bonds but triple-helix nucleation does require hydroxylation
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Biochemical characterization of DNA damage checkpoint complexes: clamp loader and clamp complexes with specificity for 5' recessed DNA
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The rate of bulk flow from the endoplasmic reticulum to the cell surface
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The nephrin-based slit diaphragm: new insight into the signalling platform identifies targets for therapy
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Regulation of mitochondrial antiviral signaling pathways
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Biosynthesis and bioproduction of coenzyme Q10 by yeasts and other organisms
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57 varieties: the human cytochromes P450
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Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin
formation of the beta-catenin:TCF transactivating complex
Neurotrophin signal transduction in the nervous system
Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton
Iron-sulfur protein maturation in human cells: evidence for a function of frataxin
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Reactions specific to the complex N-glycan synthesis pathway
Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism
Identification of the major intestinal fatty acid transport protein
The murine pantothenate kinase (Pank1) gene encodes two differentially regulated pantothenate kinase isozymes
Human ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways
Gap-filling DNA repair synthesis and ligation in TC-NER
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Na+:HCO(3-) cotransporters (NBC): cloning and characterization
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Identification and functional analysis of dual-specific A kinase-anchoring protein-2
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Total enzymic synthesis of cholesterol from lanosterol. Cytochrome b5-dependence of 4-methyl sterol oxidase.
Carbonic anhydrase IV activity is localized on the exterior surface of human erythrocytes
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Functional impairment of lens aquaporin in two families with dominantly inherited cataracts
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Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinase
Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb)
The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3'-Poly(A) tail of mRNA. Direct association of erf3/GSPT with polyadenylate-binding protein.
The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition
Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism
TRAM is specifically involved in the Toll-like receptor 4-mediated
Molecular characterization of cytosolic phospholipase A2-beta
Novel role of gp91(phox)-containing NAD(P)H oxidase in vascular endothelial growth factor-induced signaling and angiogenesis
Trk receptors: roles in neuronal signal transduction
PTEN1 is frequently mutated in primary endometrial carcinomas
Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B
Identification of a novel gene family encoding human liver-specific organic anion transporter LST-1
Neurotrophin-regulated signalling pathways
Philos Trans R Soc Lond B Biol Sci 361:1545-64
The faciogenital dysplasia gene product FGD1 functions as a Cdc42Hs-specific guanine-nucleotide exchange factor
Differential coupling of 5-HT(1) receptors to G proteins of the G(i) family
Characterization of myotubularin-related protein 7 and its binding partner, myotubularin-related protein 9
Erythrocytes take up carbon dioxide and release oxygen
ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles
Metabolism of arachidonic acid to 20-hydroxy-5,8,11, 14-eicosatetraenoic acid by P450 enzymes in human liver: involvement of CYP4F2 and CYP4A11
Structure and function of cartilage collagens
Mitochondrial GTP-AMP phosphotransferase. 2. Kinetic and equilibrium dialysis studies
Cloning and functional characterization of the human GLUT7 isoform SLC2A7 from the small intestine
Am J Physiol Gastrointest Liver Physiol 287:G236-42
Expression of complement regulatory proteins [membrane cofactor protein (CD46), decay accelerating factor (CD55), and protectin (CD59)] in endometrial stressed cells
The IRAK-1-BCL10-MALT1-TRAF6-TAK1 cascade mediates signaling to NF-kappaB from Toll-like receptor 4
Loss of types XV and XIX collagen precedes basement membrane invasion in ductal carcinoma of the female breast
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Molecular cloning, functional expression and pharmacological characterization of the human metabotropic glutamate receptor type 2
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Integrative molecular profiling of triple negative breast cancers identifies amplicon drivers and potential therapeutic targets
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Mechanisms of caspase-1 activation by P2X7 receptor-mediated K+ release
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644769
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644773
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644772
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644771
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644770
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644777
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644776
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644775
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644774
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644779
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Complement activation by apoptotic endothelial cells following hypoxia/reoxygenation
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644785
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644788
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644787
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644782
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644781
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644784
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644783
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644789
Getting in and out from calnexin/calreticulin cycles
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644798
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644797
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644796
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cblE type of homocystinuria due to methionine synthase reductase deficiency: functional correction by minigene expression
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644800
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644801
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644799
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644749
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644741
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644743
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644745
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644747
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644734
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644736
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644738
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644740
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Hsp90 increases LIM kinase activity by promoting its homo-dimerization
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644756
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644757
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644754
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644755
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644752
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644753
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644750
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644751
Clinical and molecular characterization of the first adult congenital disorder of glycosylation (CDG) type Ic patient
Diversity in protein-protein interactions of connexins: emerging roles
Regulation of connexin biosynthesis, assembly, gap junction formation, and removal
ZnT-3, a putative transporter of zinc into synaptic vesicles
Keratinocytes from patients lacking collagen XVII display a migratory phenotype
Transition state model and mechanism of nucleophilic aromatic substitution reactions catalyzed by human glutathione S-transferase M1a-1a
Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
A role for PtdIns(4,5)P2 and PIP5Kalpha in regulating stress-induced apoptosis
Regulation of the anaphase-promoting complex by the dual specificity phosphatase human Cdc14a
The NRAMP family of metal-ion transporters
ABCA10, a novel cholesterol-regulated ABCA6-like ABC transporter
Reaction mechanism and specificity of human GMP reductase. Substrates, inhibitors, activators, and inactivators
Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the International Society of Amyloidosis
Electrophysiological properties of AMPA receptors are differentially modulated depending on the associated member of the TARP family
Reversible inhibition of normal human prokeratinocyte proliferation by type beta transforming growth factor-growth inhibitor in serum-free medium
Cross-presentation of soluble exogenous antigens (endosomes)
Catecholamine biosynthesis and physiological regulation in neuroendocrine cells
Haptoglobin and CD163: captor and receptor gating hemoglobin to macrophage lysosomes
Identification of genetic mutations in Japanese patients with fructose-1,6-bisphosphatase deficiency
Genomic organization, coding sequence and functional expression of human 5-HT2 and 5-HT1A receptor genes
The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644930
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644931
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644932
C1-Tetrahydrofolate synthase from rabbit liver. Structural and kinetic properties of the enzyme and its two domains.
Identification of the cDNA encoding human 6-phosphogluconolactonase, the enzyme catalyzing the second step of the pentose phosphate pathway(1)
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644926
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644925
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644924
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644922
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644923
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644920
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644921
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644918
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644919
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644901
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644900
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644903
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644902
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644897
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644896
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644899
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644898
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644904
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644905
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truncations of AMER1 destabilize the destruction complex
Protein arginine methyltransferases and cancer
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644911
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644910
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644909
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644908
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644907
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644916
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644917
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644914
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644915
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644883
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644882
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644862
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644861
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644877
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644876
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644879
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644878
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644881
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644880
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644884
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644893
Frizzled/PCP signalling: a conserved mechanism regulating cell polarity and directed motility
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644887
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644886
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644885
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644892
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644891
ZNRF3 promotes Wnt receptor turnover in an R-spondin-sensitive manner
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644889
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644894
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644895
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644869
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644870
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644871
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644872
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644867
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644868
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644873
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644874
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644875
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644850
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644856
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644857
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644854
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644855
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644852
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644853
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644851
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644860
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644858
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644859
Identification of natural resistance-associated macrophage protein in peripheral blood lymphocytes
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644847
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644848
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644849
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_196773.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645253
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645254
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645255
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645256
Conserved docking site is essential for activation of mammalian MAP kinase kinases by specific MAP kinase kinase kinases
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_234839.1
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645258
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645260
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644864
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644865
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Deficiency of UDP-galactose:N-acetylglucosamine beta-1,4-galactosyltransferase I causes the congenital disorder of glycosylation type IId
Inhibition by C1INH of Hagemann factor fragment activation of coagulation, fibrinolysis, and kinin generation
A conserved family of prolyl-4-hydroxylases that modify HIF
Coupling of rotation and catalysis in F(1)-ATPase revealed by single-molecule imaging and manipulation
Synthesis and interconversion of nucleotide di- and triphosphates
Presence of three distinct molecular species of Gi protein alpha subunit. Structure of rat cDNAs and human genomic DNAs
Exosomes mediate stromal mobilization of autocrine Wnt-PCP signaling in breast cancer cell migration
Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products
Expression and characterization of a human mitochondrial phenylalanyl-tRNA synthetase
ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat
Attenuation of the heat shock response in HeLa cells is mediated by the release of bound heat shock transcription factor and is modulated by changes in growth and in heat shock temperatures
MGAT5 alters the severity of multiple sclerosis
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Properties and functions of diacylglycerol kinases
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Purification and properties of arylsulfatase C from human placenta
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The G473D mutation impairs dimerization and catalysis in human sulfite oxidase
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Trimethylamine N-oxide synthesis: a human variant
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Wnt/Fz signaling and the cytoskeleton: potential roles in tumorigenesis
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Endoplasmic reticulum (ER) chaperone regulation and survival of cells compensating for deficiency in the ER stress response kinase, PERK
Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins
Mutations in exon 3 of the glycogen debranching enzyme gene are associated with glycogen storage disease type III that is differentially expressed in liver and muscle.
Proline hydroxylation of collagens synthesized at different temperatures in vivo by two poikilothermic species
Multidrug resistance protein 4 (MRP4/ABCC4): a versatile efflux transporter for drugs and signalling molecules
GADD34-PP1c recruited by Smad7 dephosphorylates TGFbeta type I receptor
Vav family GEFs link activated Ephs to endocytosis and axon guidance
ABC transporters and cholesterol metabolism
The TREM receptor family and signal integration
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Renal physiology of SLC26 anion exchangers
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Repression of protein synthesis by miRNAs: how many mechanisms?
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Regulation of the MEF2 family of transcription factors by p38
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Cholesterol biosynthesis from lanosterol. Molecular cloning, tissue distribution, expression, chromosomal localization, and regulation of rat 7-dehydrocholesterol reductase, a Smith-Lemli-Opitz syndrome-related protein.
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Complement-dependent clearance of apoptotic cells by human macrophages
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644974
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Functional identification of SLC5A8, a tumor suppressor down-regulated in colon cancer, as a Na(+)-coupled transporter for short-chain fatty acids
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641687
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641688
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641693
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641694
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641691
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641692
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641686
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641685
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644995
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644996
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644997
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644998
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5644999
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645000
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645001
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645002
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645003
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641627
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641629
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641624
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641625
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641616
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641620
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641682
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641681
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641684
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641683
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641678
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641679
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641680
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641674
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641675
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641676
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641677
The Xenopus Wnt effector XTcf-3 interacts with Groucho-related transcriptional repressors
Cleavage site specificity and conformational selection in type I collagen degradation
The two major sites of cbl tyrosine phosphorylation in abl-transformed cells select the crkL SH2 domain
Eph-dependent tyrosine phosphorylation of ephexin1 modulates growth cone collapse
Crystal structure of a coiled-coil domain from human ROCK I
Human platelets contain SNARE proteins and a Sec1p homologue that interacts with syntaxin 4 and is phosphorylated after thrombin activation: implications for platelet secretion
D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain
Molecular and functional identification of sodium ion-dependent, high affinity human carnitine transporter OCTN2
Molecular cloning, expression, and chromosomal localization of two isoforms of the AE3 anion exchanger from human heart
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22591.1
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379745
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_23357.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_212951.2
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631831
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Release of platelet fibronectin (cold-insoluble globulin) from alpha granules induced by thrombin or collagen; lack of requirement for plasma fibronectin in ADP-induced platelet aggregation
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_219055.2
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Mast cell signal transduction from the high-affinity IgE receptor
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_214763.2
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631792
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379760
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_17466.1
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631861
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631859
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_16119.1
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Molecular cloning of a DEG/ENaC sodium channel cDNA from human testis
Biochem. Biophys. Res. Commun. 245:589-93
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=379709
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Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_18191.1
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Human glutamine phosphoribosylpyrophosphate amidotransferase. Kinetic and regulatory properties
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15744.2
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CalDAG-GEFIII activation of Ras, R-ras, and Rap1
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Genetic alterations of the transforming growth factor beta receptor genes in pancreatic and biliary adenocarcinomas
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15932.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_207340.2
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631909
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631910
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631912
Ephrin-B1 regulates axon guidance by reverse signaling through a PDZ-dependent mechanism
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_17148.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15748.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15829.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_15653.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_209900.2
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631851
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5631853
Cloning and expression of the gene involved in Sanfilippo B syndrome (mucopolysaccharidosis III B)
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641669
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641670
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641671
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641672
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641665
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641666
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641667
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641668
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641664
Recycling of the cell adhesion molecule L1 in axonal growth cones
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641663
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641660
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641661
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641658
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641659
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641656
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641657
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641654
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641655
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641647
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641648
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641649
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641650
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641651
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641652
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641653
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641644
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641645
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641646
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641638
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641639
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641634
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641636
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641642
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641643
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641640
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641641
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641631
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641632
Rho-associated coiled-coil-forming kinases (ROCKs): potential targets for the treatment of atherosclerosis and vascular disease
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645888
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Genetic approaches to translation initiation in Saccharomyces cerevisiae.
Translational Control of Gene Expression. N. Sonenberg, J.W. Hershey and M.B. Mathews (eds.)487-502
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D box and KEN box motifs in budding yeast Hsl1p are required for APC-mediated degradation and direct binding to Cdc20p and Cdh1p
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New insights into an old problem: ternary complex (Met-tRNAf.eIF.GTP) formation in animal cells.
Post-transcriptional control of gene expression. J.E. McCarty and M.F.Tuite (eds).521-526
Purification and characterization of membrane-bound phospholipase C specific for phosphoinositides from human platelets
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A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells
Pathway and mechanism of initiation of protein synthesis.
Translational Control of Gene Expression. (Sonenberg, Hershey and Mathews, eds.)33-88
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Coupling RNA polymerase II transcription with pre-mRNA processing.
Protein kinase C is differentially stimulated by Wnt and Frizzled homologs in a G-protein-dependent manner
Stimulation-dependent I kappa B alpha phosphorylation marks the NF-kappa B inhibitor for degradation via the ubiquitin-proteasome pathway
The Protein Biosynthesis Elongation Cycle
Translational Control of Gene Expression89-127
Translocation of cyclin B1 to the nucleus at prophase requires a phosphorylation-dependent nuclear import signal
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Mechanism of tyrosine phosphorylation and activation of phospholipase C-gamma 1. Tyrosine 783 phosphorylation is not sufficient for lipase activation
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TRP channels: sensors and transducers of gasotransmitter signals
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The role of FAST-1 and Smads in transcriptional regulation by activin during early Xenopus embryogenesis
Molecular cloning of a fourth member of the potassium-dependent sodium-calcium exchanger gene family, NCKX4
A Cdc42 activation cycle coordinated by PI 3-kinase during Fc receptor-mediated phagocytosis
An isoform of hPANK2, deficient in pantothenate kinase-associated neurodegeneration, localizes to mitochondria
Elevation of cellular NAD levels by nicotinic acid and involvement of nicotinic acid phosphoribosyltransferase in human cells
Reconstitution of the strand invasion step of double-strand break repair using human Rad51 Rad52 and RPA proteins
Protein kinase C alpha activates RAF-1 by direct phosphorylation
The nucleoside diphosphate kinase D (NM23-H4) binds the inner mitochondrial membrane with high affinity to cardiolipin and couples nucleotide transfer with respiration
Localization of platelet osteonectin at the internal face of the alpha-granule membranes in platelets and megakaryocytes
The sulfur-containing amino acids: an overview
Zinc and its transporter ZIP10 are involved in invasive behavior of breast cancer cells
Intracellular calcium release from human platelets: different messengers for multiple stores
Mutational spectrum of D-bifunctional protein deficiency and structure-based genotype-phenotype analysis
Phosphatidylinositol 3-kinase regulatory alpha subunit
3-phosphoinositide dependent protein kinase-1
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A cell-based reglucosylation assay demonstrates the role of GT1 in the quality control of a maturing glycoprotein
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Stress-activated map kinase interacting protein 1
Target of rapamycin complex 2 subunit MAPKAP1
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Structure of a human Tcf4-beta-catenin complex
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The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant DNA synthesis.
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Atypical functional properties of GluK3-containing kainate receptors
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Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit, alpha isoform
Phosphatidylinositol 3-kinase catalytic subunit, alpha isoform (EC 2.7.1.137) (PI3-kinase p110 subunit alpha) (PtdIns-3-kinase p110) (PI3K)
phospho-Phosphorylated Fibroblast growth factor receptor 2b short
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Signal-induced degradation of I kappa B alpha requires site-specific ubiquitination
RNA polymerase III Transcription Complexes
Transcriptional Regulation, eds. McKnight, S.L., Yamamoto, K.R. 22:247-280
Tyrosine phosphorylation of Vav stimulates IL-6 production in mast cells by a Rac/c-Jun N-terminal kinase-dependent pathway
Human mitochondrial phosphoenolpyruvate carboxykinase 2 gene. Structure, chromosomal localization and tissue-specific expression
Non-vesicular lipid transport by lipid-transfer proteins and beyond
Cloning and expression of a proteoglycan UDP-galactose:beta-xylose beta1,4-galactosyltransferase I. A seventh member of the human beta4-galactosyltransferase gene family
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Localization and identification of Ca2+ATPases in highly purified human platelet plasma and intracellular membranes. Evidence that the monoclonal antibody PL/IM 430 recognizes the SERCA 3 Ca2+ATPase in human platelets
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The role of individual SH2 domains in mediating association of phospholipase C-gamma1 with the activated EGF receptor
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The intrinsic affinity between E2 and the Cys domain of E1 in ubiquitin-like modifications
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Cloning and functional characterization of a sodium-dependent phosphate transporter expressed in human lung and small intestine
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Maturation of collagen Ketoimine cross-links by an alternative mechanism to pyridinoline formation in cartilage
Arylsulphatase B, an exo-sulphatase for chondroitin 4-sulphate tetrasaccharide
Hereditary juvenile cobalamin deficiency caused by mutations in the intrinsic factor gene
Proc. Natl. Acad. Sci. U.S.A. 102:4130-3
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N-glycan antennae elongation in the medial/trans-Golgi
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Netrin signal transduction and the guanine nucleotide exchange factor DOCK180 in attractive signaling
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Mitogen-activated protein kinase 3 (EC 2.7.1.-) (Extracellular signal- regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase 1) (MAPK 1) (p44-ERK1) (ERT2) (p44-MAPK) (Microtubule- associated protein-2 kinase)
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_14295.2
Activation of EGF receptor kinase by L1-mediated homophilic cell interactions
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Dual specificity mitogen-activated protein kinase kinase 1 (EC 2.7.1.-) (MAP kinase kinase 1) (MAPKK 1) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK1)
Dual specificity mitogen-activated protein kinase kinase 1
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Dual specificity mitogen-activated protein kinase kinase 2
Dual specificity mitogen-activated protein kinase kinase 2 (EC 2.7.1.-) (MAP kinase kinase 2) (MAPKK 2) (ERK activator kinase 2) (MAPK/ERK kinase 2) (MEK2)
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NMD factors UPF2 and UPF3 bridge UPF1 to the exon junction complex and stimulate its RNA helicase activity
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_14674.2
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Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
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Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
Phosphodiesterase 1B, calcium/calmodulin-dependent
Phosphodiesterase 1A, calcium/calmodulin-dependent
Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_13949.2
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=266029
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1247934
Mediation of adenylyl cyclase sensitization by PTX-insensitive GalphaoA, Galphai1, Galphai2 or Galphai3
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_13879.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_13874.2
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_14642.2
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Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association
Effector role reversal during evolution: the case of frataxin in Fe-S cluster biosynthesis
Superoxide dismutases: role in redox signaling, vascular function, and diseases
cAMP-dependent protein kinase, alpha-catalytic subunit
cAMP-dependent protein kinase type I-beta regulatory chain
cAMP-dependent protein kinase type I-alpha regulatory chain
Analysis and update of the human solute carrier (SLC) gene superfamily
Ca(2+)/calmodulin activated adenylyl cyclase
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The segment polarity gene porcupine encodes a putative multitransmembrane protein involved in Wingless processing
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646126
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646075
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646071
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646072
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646069
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646070
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646067
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646068
Persistent DNA damage signalling triggers senescence-associated inflammatory cytokine secretion
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646065
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646066
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646057
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646058
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646059
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646060
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646061
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646053
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Cloning and expression of human steroid-sulfatase. Membrane topology, glycosylation, and subcellular distribution in BHK-21 cells
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Leucine-rich repeats and immunoglobulin-like domains protein 1 precursor
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Characterization of UDP-N-acetylglucosamine:alpha-6-d-mannoside beta-1,6-N-acetylglucosaminyltransferase V from a human hepatoma cell line Hep3B
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Proteomic analysis of proteins associated with lipid droplets of basal and lipolytically stimulated 3T3-L1 adipocytes
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The retromer complex - endosomal protein recycling and beyond
The glutamate/GABA-glutamine cycle: aspects of transport, neurotransmitter homeostasis and ammonia transfer
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Ca2+-activated ATPase in microsomes from human liver
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Natural resistance-associated macrophage protein 1
Acetylcholine Neurotransmitter Release Cycle
Crystal structure of the p38 alpha-MAPKAP kinase 2 heterodimer
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Shugoshin collaborates with protein phosphatase 2A to protect cohesin
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Uridine diphosphate glucose pyrophosphorylase. IV. Crystallization and properties of the enzyme from human liver
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Cetuximab monotherapy and cetuximab plus irinotecan in irinotecan-refractory metastatic colorectal cancer
Molecular structure and physiological functions of GABA(B) receptors
Phosphoinositides in constitutive membrane traffic
Identification of an autonomously initiating RNA polymerase III holoenzyme containing a novel factor that is selectively inactivated during protein synthesis inhibition
Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes
CblE type of homocystinuria due to methionine synthase reductase deficiency: clinical and molecular studies and prenatal diagnosis in two families
Phosphatidylinositol transfer proteins: negotiating the regulatory interface between lipid metabolism and lipid signaling in diverse cellular processes
A mediator of Rho-dependent invasion moonlights as a methionine salvage enzyme
Novel recruitment of Shc, Grb2, and Sos by fibroblast growth factor receptor-1 in v-Src-transformed cells
Structural and biochemical aspects of keratan sulphate in the cornea
Insights from mouse models into human retinoblastoma
Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain
The autosomal recessively inherited progressive myoclonus epilepsies and their genes
C-mannosylation and o-fucosylation of thrombospondin type 1 repeats
5-hydroxylysyl-collagen alpha-1(XXVIII) chain
Glu-Gal-Hyl-collagen alpha-1(XXVIII) chain
4-hydroxyprolyl-collagen alpha-1(XXVIII) chain
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXVIII) chain
4-Hyp 5-Hyl-collagen alpha-1(XXVIII) chain
5-Gal-Hyl-collagen alpha-1(XXVIII) chain
4-hydroxyprolyl collagen alpha-1(XXVIII) chain
4-Hyp 5-Gal-Hyl-collagen alpha-1(XXVIII) chain
The Drosophila tweety family: molecular candidates for large-conductance Ca2+-activated Cl- channels
5-hydroxylysyl collagen alpha-2(I) propeptide
5-Gal-Hyl collagen alpha-2(I) propeptide
4-hydroxyprolyl collagen alpha-2(I) propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-2(I) propeptide
4-Hyp 5-Hyl collagen alpha-2(I) propeptide
4-Hyp 5-Gal-Hyl collagen alpha-2(I) propeptide
3,4-hydroxyprolyl collagen alpha-2(I) propeptide
3,4-Hyp Glu-Gal-Hyl collagen alpha-2(I) propeptide
3,4-Hyp 5-Hyl collagen alpha-2(I) propeptide
3,4-Hyp 5-Gal-Hyl collagen alpha-2(I) propeptide
4-hydroxyprolyl collagen alpha-1(I) propeptide
5-hydroxylysl-collagen alpha-1(I) propeptide
3,4-hydroxyprolyl collagen alpha-1(I) propeptide
4-Hyp 5-Gal-Hyl collagen alpha-1(I) propeptide
4-Hyp 5-Hyl collagen alpha-1(I) propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-1(I) propeptide
Glu-Gal-Hyl-collagen alpha-2(I) propeptide
Human lysozyme gene mutations cause hereditary systemic amyloidosis
3,4-Hyp 5-Hyl collagen alpha-1(II) propeptide
3,4-Hyp 5-Gal-Hyl collagen alpha-1(II) propeptide
Glu-Gal-Hyl collagen alpha-1(I) propeptide
3,4-hydroxyprolyl collagen alpha-1(II) propeptide
3,4-Hyp Glu-Gal-Hyl collagen alpha-1(II) propeptide
5-Gal-Hyl collagen alpha-1(I) propeptide
3,4-Hyp Glu-Gal-Hyl collagen alpha-1(I) propeptide
3,4-Hyp 5-Gal-Hyl collagen alpha-1(I) propeptide
3,4-Hyp 5-Hyl collagen alpha-1(I) propeptide
4-Hyp 5-Hyl collagen alpha-1(II) propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-1(II) propeptide
4-hydroxyprolyl collagen alpha-1(II) propeptide
5-Gal-Hyl collagen alpha-1(II) propeptide
4-Hyp 5-Gal-Hyl collagen alpha-1(II) propeptide
3,4-Hyp 5-Gal-Hyl collagen alpha-1(III) propeptide
5-hydroxylysyl collagen alpha-1(II) propeptide
Glu-Gal-Hyl collagen alpha-1(II) propeptide
4-Hyp 5-Hyl collagen alpha-1(III) propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-1(III) propeptide
3,4-hydroxyprolyl collagen alpha-1(III) propeptide
4-Hyp 5-Gal-Hyl collagen alpha-1(III) propeptide
3,4-Hyp 5-Hyl collagen alpha-1(III) propeptide
3,4-Hyp Glu-Gal-Hyl collagen alpha-1(III) propeptide
5-hydroxylysyl collagen alpha-1(III) propeptide
4-hydroxyprolyl collagen alpha-1(III) propeptide
5-Gal-Hyl collagen alpha-1(III) propeptide
SNX3 regulates endosomal function through its PX-domain-mediated interaction with PtdIns(3)P
Tec kinases mediate sustained calcium influx via site-specific tyrosine phosphorylation of the phospholipase Cgamma Src homology 2-Src homology 3 linker
PAR-1 is a Dishevelled-associated kinase and a positive regulator of Wnt signalling
Glu-Gal-Hyl-collagen alpha-1(III) propeptide
3,4-Hyp 5-Gal-Hyl collagen alpha-1(V) propeptide
3,4-Hyp 5-Hyl collagen alpha-1(V) propeptide
3,4-Hyp Glu-Gal-Hyl collagen alpha-1(V) propeptide
3,4-hydroxyprolyl collagen alpha-1(V) propeptide
4-Hyp 5-Gal-Hyl collagen alpha-1(V) propeptide
4-Hyp 5-Hyl collagen alpha-1(V) propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-1(V) propeptide
4-hydroxyprolyl collagen alpha-1(V) propeptide
Structure-function analysis of HKE4, a member of the new LIV-1 subfamily of zinc transporters
The secretory pathway Ca2+/Mn2+-ATPase 2 is a Golgi-localized pump with high affinity for Ca2+ ions
The NOD: a signaling module that regulates apoptosis and host defense against pathogens
Beyond the RING: CBL proteins as multivalent adapters
Identification of a vesicular glutamate transporter that defines a glutamatergic phenotype in neurons
Binding of a novel SMG-1-Upf1-eRF1-eRF3 complex (SURF) to the exon junction complex triggers Upf1 phosphorylation and nonsense-mediated mRNA decay
Dock6, a Dock-C subfamily guanine nucleotide exchanger, has the dual specificity for Rac1 and Cdc42 and regulates neurite outgrowth
5-hydroxylysyl-collagen alpha-1(XXV) chain
Regulation of the bioavailability of thioredoxin in the lens by a specific thioredoxin-binding protein (TBP-2)
Structure and sequence of the human alpha-L-iduronidase gene
3,4-hydroxyprolyl-collagen alpha-1(XXVII) propeptide
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXVII) propeptide
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XXVII) propeptide
3,4-Hyp 5-Hyl-collagen alpha-1(XXVII) propeptide
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXVII) propeptide
4-hydroxyprolyl-collagen alpha-1(XXVII) propeptide
4-Hyp 5-Hyl-collagen alpha-1(XXVII) propeptide
4-Hyp 5-Gal-Hyl-collagen alpha-1(XXVII) propeptide
4-hydroxyprolyl collagen alpha-1(XXVII) propeptide
5-Gal-Hyl-collagen alpha-1(XXVII) propeptide
5-hydroxylysyl-collagen alpha-1(XXVII) propeptide
Glu-Gal-Hyl-collagen alpha-1(XXVII) propeptide
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XXVIII) chain
3,4-hydroxyprolyl-collagen alpha-1(XXVIII) chain
3,4-Hyp 5-Hyl-collagen alpha-1(XXVIII) propeptide
3,4-hydroxyprolyl-collagen alpha-1(XXVIII) propeptide
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXVIII) chain
Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2
Cdc42, Rac1, and Rac2 display distinct patterns of activation during phagocytosis
Genetic evidence that HNF-1alpha-dependent transcriptional control of HNF-4alpha is essential for human pancreatic beta cell function
The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor 5A (eIF5A)
Human sphingosine-1-phosphate lyase: cDNA cloning, functional expression studies and mapping to chromosome 10q22(1)
Dual role of the tyrosine activation motif of the Ig-alpha protein during signal transduction via the B cell antigen receptor
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Translesion synthesis by DNA polymerases bypassing lesion on DNA template
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Evidence of functional modulation of the MEKK/JNK/cJun signaling cascade by the low density lipoprotein receptor-related protein (LRP)
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4-hydroxyprolyl collagen alpha-1(XXV) chain
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4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXV) chain
4-hydroxyprolyl-collagen alpha-1(XXV) chain
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Carbonic anhydrase inhibitors. The mitochondrial isozyme VB as a new target for sulfonamide and sulfamate inhibitors
Extracellular matrix and integrin signalling: the shape of things to come
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Relationship between structures and biological activities of mycoplasmal diacylated lipopeptides and their recognition by toll-like receptors 2 and 6
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Role of the beta subunit in determining the pharmacology of human gamma-aminobutyric acid type A receptors
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FATP1 channels exogenous FA into 1,2,3-triacyl-sn-glycerol and down-regulates sphingomyelin and cholesterol metabolism in growing 293 cells
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Fibroblast growth factor receptors have different signaling and mitogenic potentials
Regulation and cellular roles of phosphoinositide 5-kinases
AMP-activated protein kinase inhibits TREK channels
4-hydroxyprolyl collagen alpha-1(XXI) chain
3,4-hydroxyprolyl-collagen alpha-1(XXIII) chain
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XXIII) chain
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXIII) chain
3,4-Hyp 5-Hyl-collagen alpha-1(XXIII) chain
4-hydroxyprolyl-collagen alpha-1(XXIII) chain
4-Hyp 5-Hyl-collagen alpha-1(XXIII) chain
4-Hyp 5-Gal-Hyl-collagen alpha-1(XXIII) chain
4-hydroxyprolyl collagen alpha-1(XXIII) chain
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXIII) chain
5-hydroxylysyl-collagen alpha-1(XXIII) chain
3,4-Hyp 5-Hyl-collagen alpha-1(XXIV) propeptide
3,4-hydroxyprolyl-collagen alpha-1(XXIV) propeptide
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XXIV) propeptide
Glu-Gal-Hyl-collagen alpha-1(XXIII) chain
4-Hyp 5-Gal-Hyl-collagen alpha-1(XXIV) propeptide
4-hydroxyprolyl-collagen alpha-1(XXIV) propeptide
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXIV) propeptide
Switching of origins to a post-replicative state
4-hydroxyprolyl collagen alpha-1(XIX) chain
4-hydroxyprolyl-collagen alpha-1(XIX) chain
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XIX) chain
5-hydroxylysyl-collagen alpha-1(XIX) chain
3,4-hydroxyprolyl-collagen alpha-1(XIX) chain
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XIX) chain
4-Hyp 5-Gal-Hyl-collagen alpha-1(XIX) chain
5-hydroxylysyl-collagen alpha-1(XXI) chain
4-hydroxyprolyl-collagen alpha-1(XXI) chain
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXI) chain
4-Hyp 5-Gal-Hyl-collagen alpha-1(XXI) chain
3,4-hydroxyprolyl-collagen alpha-1(XXI) chain
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXI) chain
3,4-Hyp 5-Hyl-collagen alpha-1(XXI) chain
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XXI) chain
Purification, molecular cloning, and expression of 2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine pyrophosphate-dependent enzyme that catalyzes the carbon-carbon bond cleavage during alpha-oxidation of 3-methyl-branched fatty acids
3,4-hydroxyprolyl-collagen alpha-1(XXV) chain
Homologues of 3x4Hyp-GalHyl-COL25A1(1-654)
4-Hyp 5-Gal-Hyl-collagen alpha-1(XXV) chain
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXV) chain
Homologues of 3x4Hyp-3Hyp-COL25A1(1-654)
Homologues of 3x4Hyp-GlcGalHyl-COL25A1(1-654)
Homologues of 3x4Hyp-5Hyl-COL25A1(1-654)
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XXV) chain
5-hydroxylysyl-collagen alpha-1(XXIV) propeptide
Glu-Gal-Hyl-collagen alpha-1(XXIV) propeptide
Homologues of 3x4Hyp-3Hyp-GalHyl-COL25A1(1-654)
Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1)
4-Hyp 5-Hyl-collagen alpha-1(XXIV) propeptide
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXIV) propeptide
4-hydroxyprolyl collagen alpha-1(XXIV) propeptide
5-Gal-Hyl-collagen alpha-1(XXIV) propeptide
Kinetic analysis of peptide binding to the TAP transport complex: evidence for structural rearrangements induced by substrate binding
Homologues of 3x4Hyp-3Hyp-GlcGalHyl-COL25A1(1-654)
3,4-Hyp 5-Hyl-collagen alpha-1(XXV) chain
Homologues of 3x4Hyp-3Hyp-5Hyl-COL25A1(1-654)
A genome-wide RNA interference screen uncovers two p24 proteins as regulators of Wingless secretion
Rac-dependent trans-endocytosis of ephrinBs regulates Eph-ephrin contact repulsion
GH-dependent STAT5 signaling plays an important role in hepatic lipid metabolism
Bone morphogenetic protein receptor complexes on the surface of live cells: a new oligomerization mode for serine/threonine kinase receptors
Mammalian nuclei become licensed for DNA replication during late telophase.
Homologues of GlcGalHyl-COL18A1(24-1754)
Pathway leading to correctly folded beta-tubulin
Glu-Gal-Hyl-collagen alpha-1(XVIII) chain
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XIX) chain
3,4-Hyp 5-Hyl-collagen alpha-1(XIX) chain
Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals
Immunoelectron microscopy of type X collagen: supramolecular forms within embryonic chick cartilage
The cyclin-dependent kinase Cdc28p regulates distinct modes of Cdc6p proteolysis during the budding yeast cell cycle.
EphA receptors regulate growth cone dynamics through the novel guanine nucleotide exchange factor ephexin
Rho guanine dissociation inhibitors: pivotal molecules in cellular signalling
5-hydroxylysyl-collagen alpha-1(XV) chain
The Ras branch of small GTPases: Ras family members don't fall far from the tree
Functional analysis of ABCA8, a new drug transporter
Differential activation of recombinant human acetyl-CoA carboxylases 1 and 2 by citrate
Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes
Characterization of voltage-dependent sodium and calcium channels in mouse pancreatic A- and B-cells
Molecular cloning and functional characterization of KCC3, a new K-Cl cotransporter
beta-Catenin mutation is a frequent cause of Wnt pathway activation in gastric cancer
Heme scavenging and the other facets of hemopexin
Loss of expression for the Wnt pathway components adenomatous polyposis coli and glycogen synthase kinase 3-beta in parathyroid carcinomas
Water channel expression in human ADPKD kidneys
DNA chain length dependence of formation and dynamics of hMutSalpha.hMutLalpha.heteroduplex complexes
Synergistic activation of stress-activated protein kinase 1/c-Jun N-terminal kinase (SAPK1/JNK) isoforms by mitogen-activated protein kinase kinase 4 (MKK4) and MKK7
Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1
Aspects on human amyloid forms and their fibril polypeptides
Maintaining cholesterol homeostasis: sterol regulatory element-binding proteins
Na+-dependent purine nucleoside transporter from human kidney: cloning and functional characterization
Am J Physiol Renal Physiol 273:1058-1065
Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways
The stem cell factor receptor/c-Kit as a drug target in cancer
4-Hyp 5-Gal-Hyl-collagen alpha-1(XV) chain
Homologues of 3x4Hyp-GalHyl-COL15A1(28-1388)
3,4-hydroxyprolyl-collagen alpha-1(XV) chain
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XV) chain
Homologues of 3x4Hyp-GlcGalHyl-COL15A1(28-1388)
Homologues of 3x4Hyp-5Hyl-COL15A1(28-1388)
Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes
Analysis of the open region of RNA polymerase II transcription complexes in the early phase of elongation.
Hereditary disorders of connective tissue
Deficient t-PA release and elevated PA inhibitor levels in patients with spontaneous or recurrent deep venous thrombosis
Abcg2/Bcrp1 mediates the polarized transport of antiretroviral nucleosides abacavir and zidovudine
truncated APC mutants destabilize the destruction complex
4-hydroxyprolyl collagen alpha-1(IX) chain
4-Hyp Glu-Gal-Hyl-collagen alpha-1(IX) chain
4-hydroxyprolyl-collagen alpha-1(IX) chain
5-hydroxylysyl-collagen alpha-1(IX) chain
On the specificity of the tricarboxylate carrier system in rat liver mitochondria
3,4-Hyp 5-Hyl-collagen alpha-1(XV) chain
Homologues of 3x4Hyp-3Hyp-GalHyl-COL15A1(28-1388)
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XV) chain
Homologues of 3x4Hyp-3Hyp-5Hyl-COL15A1(28-1388)
The neural cell adhesion molecule N-CAM enhances L1-dependent cell-cell interactions
Homologues of 3x4Hyp-3Hyp-GlcGalHyl-COL15A1(28-1388)
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XV) chain
Homologues of 3x4Hyp-3Hyp-COL15A1(28-1388)
Regulation of human thymidine kinase during the cell cycle
3,4-hydroxyprolyl-collagen alpha-1(IX) chain
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(IX) chain
5-hydroxylysyl-collagen alpha-2(IX) chain
4-Hyp Glu-Gal-Hyl collagen alpha-2(IX) chain
4-hydroxyprolyl collagen alpha-2(IX) chain
Molecular cloning of cDNA and chromosomal assignment of the gene for human phenylethanolamine N-methyltransferase, the enzyme for epinephrine biosynthesis
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(IX) chain
Homologues of 3x4Hyp-3Hyp-GlcGalHyl-COL9A1
3,4-Hyp 5-Hyl-collagen alpha-1(IX) chain
4-Hyp 5-Gal-Hyl-collagen alpha-1(IX) chain
MyD88:Mal cascade initiated on plasma membrane
Heat shock factor 4a (HSF4a) represses HSF2 expression and HSF2-mediated transcriptional activity
Mechanisms of transcription-coupled DNA repair.
Comparative analysis of signaling pathways between mast cell growth factor (c-kit ligand) and granulocyte-macrophage colony-stimulating factor in a human factor-dependent myeloid cell line involves phosphorylation of Raf-1, GTPase-activating protein and mitogen-activated protein kinase
Insulin action on glucose transporters through molecular switches, tracks and tethers
Function and biological roles of the Dickkopf family of Wnt modulators
In vivo binding of active heat shock transcription factor 1 to human chromosome 9 heterochromatin during stress
beta-catenin destruction complex: insights and questions from a structural perspective
Colorectal cancer and genetic alterations in the Wnt pathway
3,4-Hyp 5-Hyl collagen alpha-2(IX) chain
3,4-Hyp Glu-Gal-Hyl collagen alpha-2(IX) chain
3,4-hydroxyprolyl-collagen alpha-2(IX) chain
4-Hyp 5-Gal-Hyl collagen alpha-2(IX) chain
5-hydroxylysyl collagen alpha-3(IX) chain
3,4-Hyp 5-Gal-Hyl collagen alpha-2(IX) chain
4-hydroxyprolyl collagen alpha-3(IX) chain
Local Ca²+ entry via Orai1 regulates plasma membrane recruitment of TRPC1 and controls cytosolic Ca²+ signals required for specific cell functions
Cdk5 regulates EphA4-mediated dendritic spine retraction through an ephexin1-dependent mechanism
Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis
3,4-Hyp 5-Hyl collagen alpha-3(IX) chain
3,4-Hyp 5-Gal-Hyl collagen alpha-3(IX) chain
4-Hyp 5-Gal-Hyl collagen alpha-3(IX) chain
3,4-hydroxyprolyl collagen alpha-3(IX) chain
3,4-Hyp Glu-Gal-Hyl collagen alpha-3(IX) chain
4-Hyp Glu-Gal-Hyl collagen alpha-3(IX) chain
Systematic analysis of myotubularins: heteromeric interactions, subcellular localisation and endosome related functions
4-hydroxyprolyl collagen alpha-1(XI) propeptide
4-hydroxyprolyl-collagen alpha-1(XI) propeptide
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XI) propeptide
5-hydroxylysyl-collagen alpha-1(XI) propeptide
5-Gal-Hyl-collagen alpha-1(XI) propeptide
Glu-Gal-Hyl-collagen alpha-1(XI) propeptide
5-hydroxylysyl-collagen alpha-2(XI) propeptide
5-Gal-Hyl collagen alpha-2(XI) propeptide
3,4-Hyp 5-Hyl-collagen alpha-2(XI) propeptide
3,4-Hyp Glu-Gal-Hyl-collagen alpha-2(XI) propeptide
3,4-Hyp 5-Gal-Hyl-collagen alpha-2(XI) propeptide
4-Hyp 5-Hyl collagen alpha-2(XI) propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-2(XI) propeptide
3,4-hydroxyprolyl collagen alpha-2(XI) propeptide
Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reaction
4-Hyp 5-Gal-Hyl collagen alpha-2(XI) propeptide
Cloning, characterization, and chromosomal mapping of human aquaporin of collecting duct
4-Hyp 5-Hyl-collagen alpha-1(XI) propeptide
Glu-Gal-Hyl collagen alpha-2(XI) propeptide
4-hydroxyprolyl collagen alpha-2(XI) propeptide
3,4-hydroxyprolyl-collagen alpha-1(XI) propeptide
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XI) propeptide
3,4-Hyp 5-Hyl-collagen alpha-1(XI) propeptide
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XI) propeptide
4-Hyp 5-Gal-Hyl-collagen alpha-1(XI) propeptide
A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome
3,4-Hyp 5-Hyl collagen alpha-3(V) propeptide
3,4-Hyp 5-Gal-Hyl collagen alpha-3(V) propeptide
Glu-Gal-Hyl collagen alpha-2(V) propeptide
5-hydroxylysyl collagen alpha-2(V) propeptide
4-hydroxyprolyl collagen alpha-2(V) propeptide
5-Gal-Hyl collagen alpha-2(V) propeptide
4-Hyp 5-Hyl collagen alpha-2(V) propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-2(V) propeptide
Superoxide production and electron transport in mitochondrial oxidation of dihydroorotic acid.
5-hydroxylysyl collagen alpha-3(V) propeptide
Glu-Gal-Hyl collagen alpha-3(V) propeptide
4-Hyp 5-Hyl collagen alpha-3(V) propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-3(V) propeptide
4-hydroxyprolyl collagen alpha-3(V) propeptide
5-Gal-Hyl collagen alpha-3(V) propeptide
3,4-Hyp Glu-Gal-Hyl collagen alpha-3(V) propeptide
3,4-hydroxyprolyl collagen alpha-3(V) propeptide
4-Hyp 5-Gal-Hyl collagen alpha-3(V) propeptide
Activation of Ca-permeable Kainate Receptor
NAGLU mutations underlying Sanfilippo syndrome type B
Phospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk
3,4-Hyp 5-Gal-Hyl collagen alpha-2(V) propeptide
3,4-Hyp 5-Hyl collagen alpha-2(V) propeptide
3,4-Hyp Glu-Gal-Hyl collagen alpha-2(V) propeptide
3,4-hydroxyprolyl collagen alpha-2(V) propeptide
4-Hyp 5-Gal-Hyl collagen alpha-2(V) propeptide
Bi-directional routing of DNA mismatch repair protein human exonuclease 1 to replication foci and DNA double strand breaks
5-Gal-Hyl collagen alpha-1(V) propeptide
5-hydroxylysyl collagen alpha-1(V) propeptide
Glu-Gal-Hyl collagen alpha-1(V) propeptide
Metabolism of water-soluble vitamins and cofactors
Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis
Inhibition of replication initiation of damaged DNA by RB1/E2F1
Essential roles of PI(3)K-p110beta in cell growth, metabolism and tumorigenesis
Isolation and characterization of a human thiamine pyrophosphokinase cDNA
Processing of the lipocalin alpha(1)-microglobulin by hemoglobin induces heme-binding and heme-degradation properties
Expression and characterization of the human 3 beta-hydroxysteroid sulfotransferases (SULT2B1a and SULT2B1b)
Agrin binds alpha-synuclein and modulates alpha-synuclein fibrillation
Molecular cloning of human thiamin pyrophosphokinase
ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization
Proc. Natl. Acad. Sci. U.S.A. 106:8653-8
Central spindle assembly and cytokinesis require a kinesin-like protein/RhoGAP complex with microtubule bundling activity
Human glutamine phosphoribosylpyrophosphate amidotransferase. Two molecular forms interconvertible by purine ribonucleotides and phosphoribosylpyrophosphate
Structure-function analysis of Friedreich's ataxia mutants reveals determinants of frataxin binding and activation of the Fe-S assembly complex
Polycomb mediated epigenetic silencing and replication timing at the INK4a/ARF locus during senescence
Gain-of-function RAF1 mutations cause Noonan and LEOPARD syndromes with hypertrophic cardiomyopathy
Phosphatidylinositol-4-phosphate 5-kinase isozymes catalyze the synthesis of 3-phosphate-containing phosphatidylinositol signaling molecules
Clinical and genetic spectrum of pyruvate dehydrogenase deficiency: dihydrolipoamide acetyltransferase (E2) deficiency
Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism.
hMutSalpha forms an ATP-dependent complex with hMutLalpha and hMutLbeta on DNA
Presentation of cytosolic antigens via MHC class II molecules
Interferon-gamma: an overview of signals, mechanisms and functions
Comparative analysis of the efficacy of A1 adenosine receptor activation of Gi/o alpha G proteins following coexpression of receptor and G protein and expression of A1 adenosine receptor-Gi/o alpha fusion proteins
Ror-family receptor tyrosine kinases in noncanonical Wnt signaling: their implications in developmental morphogenesis and human diseases
Octamer formation and coupling of cardiac sarcomeric mitochondrial creatine kinase are mediated by charged N-terminal residues
Role of cysteine-82 in the catalytic mechanism of human S-adenosylmethionine decarboxylase
Structural basis of mitochondrial tethering by mitofusin complexes
Energy dependent regulation of mTOR by LKB1-AMPK
Neural cell adhesion molecule L1: signaling pathways and growth cone motility
Mutations in TMEM76* cause mucopolysaccharidosis IIIC (Sanfilippo C syndrome)
Loading of the human 9-1-1 checkpoint complex onto DNA by the checkpoint clamp loader hRad17-replication factor C complex in vitro
Mini-review: Specificity and expression of CIITA, the master regulator of MHC class II genes
Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin
Functional characterization and localization of AQP3 in the human colon
The ins and outs of IgE-dependent mast-cell exocytosis
Rocks: multifunctional kinases in cell behaviour
Protein kinase G mediates vascular endothelial growth factor-induced Raf-1 activation and proliferation in human endothelial cells
The role of non-P450 enzymes in drug oxidation
The polo-like kinase Plx1 is required for activation of the phosphatase Cdc25C and cyclin B-Cdc2 in Xenopus oocytes
Mitotic phosphorylation of Golgi reassembly stacking protein 55 by mitogen-activated protein kinase ERK2
A new biochemical subtype of the Sanfilippo syndrome: characterization of the storage material in cultured fibroblasts of Sanfilippo C patients
A novel quality control compartment derived from the endoplasmic reticulum
Bone morphogenetic proteins and their antagonists
Specificity of WNT-receptor interactions
Synbindin, A novel syndecan-2-binding protein in neuronal dendritic spines
Agrin isoforms with distinct amino termini: differential expression, localization, and function
Cold Spring Harb Perspect Biol 3:a004978
Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain
Frataxin and mitochondrial FeS cluster biogenesis
Low-density lipoprotein receptor-related protein-5 binds to Axin and regulates the canonical Wnt signaling pathway
Mutations in the transporter ABCA12 are associated with lamellar ichthyosis type 2
Cytosolic iron-sulfur cluster assembly (CIA) system: factors, mechanism, and relevance to cellular iron regulation
Diverging substrate specificity of pure human thymidine kinases 1 and 2 against antiviral dideoxynucleosides
'ATP [cytosol]' negatively regulates 'PGYM dimer, b form + 2 AMP <=> PGYM b dimer:AMP complex'
'G6P [cytosol]' negatively regulates 'PGYM dimer, b form + 2 AMP <=> PGYM b dimer:AMP complex'
'FMN [cytosol]' negatively regulates 'SLC52A3 transports extracellular RIB to cytosol'
'FAD [cytosol]' negatively regulates 'SLC52A3 transports extracellular RIB to cytosol'
'Mg2+ [cytosol]' is required for 'A phosphoribosyl group is added to nicotinate to form nicotinate mononucleotide (NaMN)'
'Ac-CoA [mitochondrial matrix]' positively regulates 'Pyruvate + CO2 + ATP => ADP + Orthophosphate + Oxaloacetate'
'AMP [cytosol]' negatively regulates 'D-fructose 1,6-bisphosphate + H2O => D-fructose 6-phosphate + orthophosphate'
'G6P [cytosol]' is required for 'Phosphorylated GYS1 catalyzes the polyglucosylation of oligoGlc-GYG1'
'Ca2+ [cytosol]' positively regulates 'glycogen phosphorylase (PYGM) dimer b + 2 ATP => glycogen phosphorylase (PYGM) dimer a + 2 ADP'
'Ca2+ [cytosol]' positively regulates 'glycogen phosphorylase (PYGL) dimer b + 2 ATP => glycogen phosphorylase (PYGL) dimer a + 2 ADP'
'D-Fructose 1,6-bisphosphate [cytosol]' positively regulates 'phosphoenolpyruvate + ADP => pyruvate + ATP'
'ATP [nucleoplasm]' negatively regulates 'phosphoenolpyruvate + ADP => pyruvate + ATP'
'ADP [cytosol]' positively regulates 'D-fructose 6-phosphate + ATP => D-fructose 1,6-bisphosphate + ADP'
'AMP [cytosol]' positively regulates 'D-fructose 6-phosphate + ATP => D-fructose 1,6-bisphosphate + ADP'
'Ac-CoA [cytosol]' negatively regulates 'phosphoenolpyruvate + ADP => pyruvate + ATP'
'cAMP [cytosol]' negatively regulates 'phosphoenolpyruvate + ADP => pyruvate + ATP'
Processing of primary microRNAs by the Microprocessor complex
Dissecting the role of 5'-AMP for allosteric stimulation, activation, and deactivation of AMP-activated protein kinase
The Microprocessor complex mediates the genesis of microRNAs
'D-Fructose 2,6-bisphosphate [cytosol]' positively regulates 'D-fructose 6-phosphate + ATP => D-fructose 1,6-bisphosphate + ADP'
Three-dimensional structure of the anaphase-promoting complex
'CIT [cytosol]' negatively regulates 'D-fructose 6-phosphate + ATP => D-fructose 1,6-bisphosphate + ADP'
'D-Fructose 2,6-bisphosphate [cytosol]' positively regulates 'D-fructose 6-phosphate + ATP => D-fructose 2,6-bisphosphate + ADP'
'ATP [cytosol]' negatively regulates 'D-fructose 6-phosphate + ATP => D-fructose 1,6-bisphosphate + ADP'
On the mechanism of preprotein import by the mitochondrial presequence translocase
'MYO7A [cytosol]' positively regulates 'RPE65 isomero-hydrolyses atREs to 11cROL'
'GUCA:Ca2+ [photoreceptor disc membrane]' negatively regulates 'GUCYs converts GTP to cGMP'
'Ca2+ [cytosol]' positively regulates 'CALM1:Ca2+ binds CNG channel'
Human liver estrogen sulfotransferase: identification by cDNA cloning and expression
Isolation and characterization of the circulating form of human endostatin
'Activated FGFR:p-FRS2:p-SHP2 (name copied from entity in Homo sapiens) [plasma membrane]' positively regulates 'Ras nucleotide exchange by GRB2:SOS1 bound to p-FRS2:activated FGFR'
Inactivation of Chibby affects function of motile airway cilia
'S40L-PAH [cytosol]' negatively regulates 'phenylalanine + tetrahydrobiopterin + O2 => tyrosine + 4a-hydroxytetrahydrobiopterin + H2O'
'L-Phe [cytosol]' negatively regulates 'kynurenine + pyruvate => 4-(2-aminophenyl)-2,4-dioxobutanoic acid + alanine [CCBL1]'
'L-Asp [lysosomal lumen]' negatively regulates 'Beta-glucuronidase (GUSB) hydrolyses glucuronate from the linker chain'
'HS [extracellular region]' is required for 'FGFR3c binds to FGF'
'HS [extracellular region]' is required for 'FGFR4 binds to FGF'
'Activated FGFR:pThr-FRS2alpha (name copied from entity in Homo sapiens) [plasma membrane]' negatively regulates 'Phosphorylation of FRS2-alpha by activated FGFR'
Signal transduction pathways mediated by the interaction of CpG DNA with Toll-like receptor 9
TIR domains, which are conserved among all TLRs. Recent accumulating
'HS [extracellular region]' is required for 'FGFR2c binds to FGF'
'HS [extracellular region]' is required for 'FGFR3b binds to FGF'
'HS [extracellular region]' is required for 'FGFR1c binds to FGF'
'HS [extracellular region]' is required for 'FGFR2b binds to FGF'
'AKT:PIP3:THEM4/TRIB3 (name copied from entity in Homo sapiens) [plasma membrane]' negatively regulates 'TORC2 (mTOR) phosphorylates AKT at S473'
'Ligand-responsive p-6Y-EGFR mutants:CBL (name copied from entity in Homo sapiens) [plasma membrane]' negatively regulates 'Inefficient ubiquitination of ligand-responsive EGFR mutants by phosphorylated CBL'
'PKC phosphorylates GRK2' negatively regulates 'Inhibition of GRK2 by calmodulin'
'p-MEK1 [cytosol]' negatively regulates 'MEK1 phosphorylates ERK-1'
'I(1,4,5)P3 [cytosol]' positively regulates 'Release of calcium from intracellular stores by IP3 receptor activation'
'4xCa2+:CaM (name copied from entity in Homo sapiens) [cytosol]' positively regulates 'Calmodulin activates Cam-PDE 1'
Mechanism of Cu,Zn-superoxide dismutase activation by the human metallochaperone hCCS
Protein ligands to HuR modulate its interaction with target mRNAs in vivo
Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase
Molecular characterization of the family of choline transporter-like proteins and their splice variants
CLIF, a novel cycle-like factor, regulates the circadian oscillation of plasminogen activator inhibitor-1 gene expression
A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNA(Met) is an important translation initiation intermediate in vivo.
Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription.
Active Nercc1 protein kinase concentrates at centrosomes early in mitosis and is necessary for proper spindle assembly
Dephosphorylation of human p34cdc2 kinase on both Thr-14 and Tyr-15 by human cdc25B phosphatase
Carnitine palmitoyltransferase II deficiency: structure of the gene and characterization of two novel disease-causing mutations
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XVI) chain
4-hydroxyprolyl-collagen alpha-1(XVI) chain
4-hydroxyprolyl collagen alpha-1(XVI) chain
3,4-hydroxyprolyl-collagen alpha-1(XVI) chain
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XVI) chain
4-Hyp 5-Gal-Hyl-collagen alpha-1(XVI) chain
Identification and characterization of human mitochondrial tryptophanyl-tRNA synthetase
4-hydroxyprolyl collagen alpha-1(XV) chain
Homologues of 3x4Hyp-3Hyp-GalHyl-COL16A1
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XVI) chain
3,4-Hyp 5-Hyl-collagen alpha-1(XVI) chain
Homologues of 3x4Hyp-3Hyp-GlcGalHyl-COL16A1
Homologues of GlcGalHyl-COL15A1(28-1388)
Structure of a multifunctional protein. Mammalian phosphatidylinositol transfer protein complexed with phosphatidylcholine
4-hydroxyprolyl-collagen alpha-1(XVIII) chain
4-Hyp 5-Hyl-collagen alpha-1(XVIII) chain
Homologues of 3x4Hyp-GlcGalHyl-COL18A1(24-1754)
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XVIII) chain
4-Hyp 5-Gal-Hyl-collagen alpha-1(XVIII) chain
Homologues of 3x4Hyp-5Hyl-COL18A1(24-1754)
Induction of CHOP expression by amino acid limitation requires both ATF4 expression and ATF2 phosphorylation
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XVIII) chain
3,4-hydroxyprolyl-collagen alpha-1(XVIII) chain
A mitogen-activated protein kinase-dependent signaling pathway in the activation of platelet integrin alpha IIbbeta3
Homologues of 3x4Hyp-GalHyl-COL18A1(24-1754)
Homologues of 3x4Hyp-3Hyp-GlcGalHyl-COL18A1(24-1754)
3,4-Hyp 5-Hyl-collagen alpha-1(XVIII) chain
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XVIII) chain
Homologues of 3x4Hyp-3Hyp-5Hyl-COL18A1(24-1754)
Identification of a binding region for human origin recognition complex proteins 1 and 2 that coincides with an origin of DNA replication.
Strict regulation of CAIX(G250/MN) by HIF-1alpha in clear cell renal cell carcinoma
5-hydroxylysyl-collagen alpha-1(XVI) chain
Homologues of 3x4Hyp-3Hyp-GalHyl-COL18A1(24-1754)
Ornithine delta-aminotransferase mutations in gyrate atrophy. Allelic heterogeneity and functional consequences.
Human liver mitochondrial carnitine palmitoyltransferase I: characterization of its cDNA and chromosomal localization and partial analysis of the gene
A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1
From glycosylation disorders to dolichol biosynthesis defects: a new class of metabolic diseases
4-hydroxyprolyl collagen alpha-1(XVIII) chain
Nitric oxide stimulates guanylate cyclase
The Ste20-like kinase Mst2 activates the human large tumor suppressor kinase Lats1
N-glycan trimming and elongation in the cis-Golgi
The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth
Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia
Glucuronidation and the UDP-glucuronosyltransferases in health and disease
MAPKAP kinase 3pK phosphorylates and regulates chromatin association of the polycomb group protein Bmi1
A mutant EGF-receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling
Triggering and amplifying pathways of regulation of insulin secretion by glucose
Shedding of collagen XXIII is mediated by furin and depends on the plasma membrane microenvironment
cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia
Characterization of bovine endothelial nitric oxide synthase as a homodimer with down-regulated uncoupled NADPH oxidase activity: tetrahydrobiopterin binding kinetics and role of haem in dimerization
Structural determinants of water permeation through aquaporin-1
Control of pyrimidine biosynthesis in human lymphocytes. Simultaneous increase in activities of glutamine-utilizing carbamyl phosphate synthetase and aspartate transcarbamylase in phytohemagglutinin-stimulated human peripheral lymphocytes and their enzyme co-purification
Construction of a model for the aggregation and cross-linking region (7S domain) of type IV collagen based upon an evaluation of the primary structure of the alpha 1 and alpha 2 chains in this region
Isoform-specific and exercise intensity-dependent activation of 5'-AMP-activated protein kinase in human skeletal muscle
Biosynthesis of tetrahydrobiopterin. Purification and characterization of 6-pyruvoyl-tetrahydropterin synthase from human liver
Regulation of LIM-kinase 1 and cofilin in thrombin-stimulated platelets
Heat shock factor 1 binds to and transcribes satellite II and III sequences at several pericentromeric regions in heat-shocked cells
Axin-mediated CKI phosphorylation of beta-catenin at Ser 45: a molecular switch for the Wnt pathway
Structure-function analysis of LIV-1, the breast cancer-associated protein that belongs to a new subfamily of zinc transporters
3-Hydroxy-3-methylglutaryl coenzyme A lyase (HL). Cloning of human and chicken liver HL cDNAs and characterization of a mutation causing human HL deficiency.
Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits
Allelic variation in GAD1 (GAD67) is associated with schizophrenia and influences cortical function and gene expression
Spatial expression patterns and biochemical properties distinguish a second myo-inositol monophosphatase IMPA2 from IMPA1
Rev-erbalpha, a heme sensor that coordinates metabolic and circadian pathways
Characterization of the proteins released from activated platelets leads to localization of novel platelet proteins in human atherosclerotic lesions
Isolation and chromosomal localization of a novel FMS-like tyrosine kinase gene
The GPIb thrombin-binding site is essential for thrombin-induced platelet procoagulant activity
Phosphatidylinositol 3-kinase-? inhibitor CAL-101 shows promising preclinical activity in chronic lymphocytic leukemia by antagonizing intrinsic and extrinsic cellular survival signals
Folic acid: nutritional biochemistry, molecular biology, and role in disease processes
The enzymatic formation of sphingomyelin from ceramide and lecithin in mouse liver
Characterization of the mechanisms controlling Greatwall activity
Cloned mammalian neutral sphingomyelinase: functions in sphingolipid signaling?
Specificity in cytokine signal transduction: lessons learned from the IL-3/IL-5/GM-CSF receptor family
Transcriptional map of 170-kb region at chromosome 11p15.5: identification and mutational analysis of the BWR1A gene reveals the presence of mutations in tumor samples
The small GTP-binding protein Cdc42 is required for nerve growth factor withdrawal-induced neuronal death
Transaldolase deficiency: liver cirrhosis associated with a new inborn error in the pentose phosphate pathway.
Two new proteases in the MHC class I processing pathway
The stem-loop binding protein is required for efficient translation of histone mRNA in vivo and in vitro
The dynamic phagosomal proteome and the contribution of the endoplasmic reticulum
Lipid-independent secretion of a Drosophila Wnt protein
Cbl: many adaptations to regulate protein tyrosine kinases
Cdc6 is regulated by E2F and is essential for DNA replication in mammalian cells.
Cloning and characterization of human agmatinase
The hierarchy of exon-junction complex assembly by the spliceosome explains key features of mammalian nonsense-mediated mRNA decay
A double-hexamer archaeal minichromosome maintenance protein is an ATP-dependent DNA helicase.
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The subcellular localization of acetyl-CoA carboxylase 2
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Phosphorylation of serine 256 suppresses transactivation by FKHR (FOXO1) by multiple mechanisms. Direct and indirect effects on nuclear/cytoplasmic shuttling and DNA binding
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Age-related variations in hydroxylation of lysine and proline in collagen
Zonula occludens-1 alters connexin43 gap junction size and organization by influencing channel accretion
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Regulation of Hypoxia-inducible Factor (HIF) by oxygen
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Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities
Calcineurin homologous protein as an essential cofactor for Na+/H+ exchangers
integral component of cytoplasmic side of endoplasmic reticulum membrane
Granulocyte-macrophage progenitors as candidate leukemic stem cells in blast-crisis CML
Molecular identification and characterization of novel human and mouse concentrative Na+-nucleoside cotransporter proteins (hCNT3 and mCNT3) broadly selective for purine and pyrimidine nucleosides (system cib)
GTP:AMP phosphotransferase, mitochondrial
Leucine-rich repeat-containing protein 16A
Histone H3.3 with methylated lysine9 (H3K9)
Determinants of growth hormone receptor down-regulation
A-kinase anchor protein 10, mitochondrial
A-kinase anchor protein 1, mitochondrial
tissue plasminogen activator, heavy chain
tissue plasminogen activator, light chain
The H syndrome is caused by mutations in the nucleoside transporter hENT3
tissue plasminogen activator (one-chain)
26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide
Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2
Matrilysin cleavage of corneal collagen type XVIII NC1 domain and generation of a 28-kDa fragment
Invest. Ophthalmol. Vis. Sci. 42:2517-24
The receptor tyrosine kinase Ror2 is involved in non-canonical Wnt5a/JNK signalling pathway
Intracellular hyaluronan-binding protein 4
Bromodomain and PHD finger-containing protein 3
A quantitative model of human DNA base excision repair. I. Mechanistic insights
SCF(Skp2)-mediated degradation of p27/p21
Endogenous retroviral sequence is fused to FGFR1 kinase in the 8p12 stem-cell myeloproliferative disorder with t(8;19)(p12;q13.3)
CoREST represses the heat shock response mediated by HSF1
Substrate specificity combined with stereopromiscuity in glutathione transferase A4-4-dependent metabolism of 4-hydroxynonenal
mitochondrial fatty acid beta-oxidation of saturated fatty acids
The processivity of multiubiquitination by the APC determines the order of substrate degradation
A third MRX family (MRX68) is the result of mutation in the long chain fatty acid-CoA ligase 4 (FACL4) gene: proposal of a rapid enzymatic assay for screening mentally retarded patients
Cloning and characterization of murine 1-acyl-sn-glycerol 3-phosphate acyltransferases and their regulation by PPARalpha in murine heart
Golgi Cisternae Pericentriolar Stack Reorganization
Syndecan-1 supports integrin alpha2beta1-mediated adhesion to collagen
Primary structure, functional expression, and chromosomal localization of the bumetanide-sensitive Na-K-Cl cotransporter in human colon
Expression of heparan sulphate L-iduronyl 2-O-sulphotransferase in human kidney 293 cells results in increased D-glucuronyl 2-O-sulphation
Netrin signaling leading to directed growth cone steering
Glycogen debranching enzyme: purification, antibody characterization, and immunoblot analyses of type III glycogen storage disease.
Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activating kinase
Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: involvement of host proteins TSG101 and VPS-4
Hematopoietic cytokine receptor signaling
Transcriptional control of megakaryocyte development
Specific association of the beta isoform of the p85 subunit of phosphatidylinositol-3 kinase with the proto-oncogene c-cbl
Hsp47 and cyclophilin B traverse the endoplasmic reticulum with procollagen into pre-Golgi intermediate vesicles. A role for Hsp47 and cyclophilin B in the export of procollagen from the endoplasmic reticulum
Molecular basis of methylmalonyl-CoA mutase apoenzyme defect in 40 European patients affected by mut(o) and mut- forms of methylmalonic acidemia: identification of 29 novel mutations in the MUT gene
Small is beautiful: insulin-like growth factors and their role in growth, development, and cancer
Phosphate transporters: a tale of two solute carrier families
Two cofactors and cytoplasmic chaperonin are required for the folding of alpha- and beta-tubulin
Ligand-induced, receptor-mediated dimerization and activation of EGF receptor
The path to perdition is paved with protons
Isozymes of human phosphofructokinase: identification and subunit structural characterization of a new system
Platelet alpha granule membrane components that are released on degranulation
Genomic organization and expression of the human alpha 1B-adrenergic receptor
The nucleotide transporter MRP4 (ABCC4) is highly expressed in human platelets and present in dense granules, indicating a role in mediator storage
Activation of purified human protein kinase C alpha and beta I isoenzymes in vitro by Ca2+, phosphatidylinositol and phosphatidylinositol 4,5-bisphosphate
Activation of the tumour suppressor kinase LKB1 by the STE20-like pseudokinase STRAD
A structural perspective on copper uptake in eukaryotes
Transcriptional induction of the human asparagine synthetase gene during the unfolded protein response does not require the ATF6 and IRE1/XBP1 arms of the pathway
Indirect recruitment of the signalling adaptor Shc to the fibroblast growth factor receptor 2 (FGFR2)
Guanylate cyclase soluble subunit alpha-3
Guanylate cyclase soluble subunit alpha-2
Guanylate cyclase soluble subunit beta-1
Purification and partial characterization of cellular retinol-binding protein, type two, from human small intestine
Molecular mechanisms of complement evasion: learning from staphylococci and meningococci
Mucopolysaccharidosis type IVA (Morquio A disease): clinical review and current treatment
Lysosome-associated membrane glycoprotein 3
Multidrug resistance-associated protein 4
IAP proteins: blocking the road to death's door
Plasminogen activator inhibitor-1 precursor
Endothelial plasminogen activator inhibitor
The identification of a distinct export step following the biosynthesis of leukotriene C4 by human eosinophils
Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R)
Cellular functions of TC10, a Rho family GTPase: regulation of morphology, signal transduction and cell growth
The canonical retinoid cycle in rods (twilight vision)
Proximal tubular handling of phosphate: A molecular perspective
Biosynthesis of tricarboxylic acids by carbon dioxide fixation; enzymatic mechanisms
Forearm blood flow during body temperature transients produced by leg exercise.
Low nidogen affinity of laminin-5 can be attributed to two serine residues in EGF-like motif gamma 2III4
The SLC31 (Ctr) copper transporter family
Identification and characterization of a sphingolipid delta 4-desaturase family
Activation of phospholipase C-gamma by phosphatidylinositol 3,4,5-trisphosphate
Inhibition of PI3K/mTOR pathways in glioblastoma and implications for combination therapy with temozolomide
Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein
Aldehyde dehydrogenase, a diphosphopyridine nucleotide-linked enzyme
Expression of Human CTP synthetase in Saccharomyces cerevisiae reveals phosphorylation by protein kinase A
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Regulation of commissural axon pathfinding by slit and its Robo receptors
Peroxisome proliferator-activated receptor alpha target genes
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Identification and characterization of a novel monoamine transporter in the human brain
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Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins
The juxtamembrane region of the EGF receptor functions as an activation domain
Receptor-mediated reversible translocation of the G protein betagamma complex from the plasma membrane to the Golgi complex
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APC truncation mutants are not K63 polyubiquitinated
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Biosynthesis of diphosphopyridine nucleotide. II. Enzymatic aspects.
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Armadillo coactivates transcription driven by the product of the Drosophila segment polarity gene dTCF
The diverse functions of histone lysine methylation
An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation
LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription
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Dapper 1 antagonizes Wnt signaling by promoting dishevelled degradation
Transport of glucose and other sugars, bile salts and organic acids, metal ions and amine compounds
Chromosomal replication initiates and terminates at random sequences but at regular intervals in the ribosomal DNA of Xenopus early embryos.
Expression analysis of RSK gene family members: the RSK2 gene, mutated in Coffin-Lowry syndrome, is prominently expressed in brain structures essential for cognitive function and learning
Essential role for Gab2 in the allergic response
Characterization of cytokine differential induction of STAT complexes in primary human T and NK cells
Effect of acute heat shock on gene expression by human peripheral blood mononuclear cells
AMER1 mutants destabilize the destruction complex
Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia
The human glutathione transferase alpha locus: genomic organization of the gene cluster and functional characterization of the genetic polymorphism in the hGSTA1 promoter
Lack of nidogen-1 and -2 prevents basement membrane assembly in skin-organotypic coculture
LIM and senescent cell antigen-like-containing domain protein 1
Isolation and structural identification of a labile intermolecular crosslink in collagen
Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity
Completion of mammalian lagging strand DNA replication using purified proteins.
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A novel sodium bicarbonate cotransporter-like gene in an ancient duplicated region: SLC4A9 at 5q31
Effect of 3-hydroxyproline residues on collagen stability
Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase
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A molecular determinant for submillisecond desensitization in glutamate receptors
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Promoter clearance by RNA polymerase II is an extended, multistep process strongly affected by sequence.
Glu-Gal-Hyl collagen alpha-2(VI) propeptide
5-hydroxylysyl collagen alpha-2(VI) propeptide
5-Gal-Hyl collagen alpha-2(VI) propeptide
E2F-enabled inhibition of pre-replication complex formation
Learning the language of cell-cell communication through connexin channels
Fluorescence correlation spectroscopy and fluorescence cross-correlation spectroscopy reveal the cytoplasmic origination of loaded nuclear RISC in vivo in human cells
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PRAK is essential for ras-induced senescence and tumor suppression
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PKC412 inhibits the zinc finger 198-fibroblast growth factor receptor 1 fusion tyrosine kinase and is active in treatment of stem cell myeloproliferative disorder
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Mitofusin 2 tethers endoplasmic reticulum to mitochondria
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Feedback regulation of EGFR signalling: decision making by early and delayed loops
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A synopsis of the unconjugated acidic transamination metabolites of phenylalanine in phenylketonuria
Protein AMBP component recommendedName: Alpha-1-microglobulin
Regulation of protein kinase C zeta by PI 3-kinase and PDK-1
Human pentraxin 3 binds to the complement regulator c4b-binding protein
Molybdenum cofactor biosynthesis and deficiency
Active site remodelling accompanies thioester bond formation in the SUMO E1
Tissue plasminogen activator: peptide analyses confirm an indirectly derived amino acid sequence, identify the active site serine residue, establish glycosylation sites, and localize variant differences
Anion inhibition of CO2 hydration catalyzed by human carbonic anhydrase II. Mechanistic implications
An electric lobe suppressor for a yeast choline transport mutation belongs to a new family of transporter-like proteins
Anti-apoptotic signaling by the interleukin-2 receptor reveals a function for cytoplasmic tyrosine residues within the common gamma (gamma c) receptor subunit
Vacuolar protein sorting-associated protein 45
The cytoplasmic domain of NrCAM binds to PDZ domains of synapse-associated proteins SAP90/PSD95 and SAP97
Enzymes and reactions at the eukaryotic DNA replication fork.
A direct role for GRASP65 as a mitotically regulated Golgi stacking factor
Transition of galactosyltransferase 1 from trans-Golgi cisterna to the trans-Golgi network is signal mediated
Expression of cAMP-regulated guanine nucleotide exchange factors in pancreatic beta-cells
Human cytosolic thymidine kinase. Purification and physical characterization of the enzyme from HeLa cells
Molecular physiology of cation-coupled Cl- cotransport: the SLC12 family
Trimethylaminuria: the fish-odour syndrome
Recognition and elimination of nonsense mRNA
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Eph receptors at synapses: implications in neurodegenerative diseases
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cDNA cloning of the beta-subunit of the human gastric H,K-ATPase
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The CoA esters of 2-methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and kidney
Kinesin's light chains inhibit the head- and microtubule-binding activity of its tail
Activation and association of the Tec tyrosine kinase with the human prolactin receptor: mapping of a Tec/Vav1-receptor binding site
Molecular cloning and characterization of the human cardiac Na+/Ca2+ exchanger cDNA
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In vivo analysis of growth hormone receptor signaling domains and their associated transcripts
Low levels of miR-92b/96 induce PRMT5 translation and H3R8/H4R3 methylation in mantle cell lymphoma
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Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe/S cluster biosynthesis
PI 3-kinase and cancer: changing accents
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Human choline acetyltransferase (CHAT): partial gene sequence and potential control regions
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Expression and regulation of GPAT isoforms in cultured human keratinocytes and rodent epidermis
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RNA Polymerase III Abortive And Retractive Initiation
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Localized unfolding of collagen explains collagenase cleavage near imino-poor sites
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Molecular cloning and characterization of a novel muscle adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal cells
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XVII) chain
3,4-hydroxyprolyl-collagen alpha-1(XVII) chain
Homologues of 3x4Hyp-3Hyp-GalHyl-COL17A1(1-1497)
A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line
3,4-Hyp 5-Hyl-collagen alpha-1(XVII) chain
In vitro processing of the human alkyl-dihydroxyacetonephosphate synthase precursor
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XVII) chain
Homologues of 3x4Hyp-3Hyp-GlcGalHyl-COL17A1(1-1497)
Developmental rearrangements of cortical glutamate-NMDA receptor binding sites in late human gestation
Regulation of human hepatic hydroxysteroid sulfotransferase gene expression by the peroxisome proliferator-activated receptor alpha transcription factor
Homologues of 3x4Hyp-3Hyp-5Hyl-COL17A1(1-1497)
4-hydroxyprolyl-collagen alpha-1(XVII) chain
4-Hyp 5-Gal-Hyl-collagen alpha-1(XVII) chain
Homologues of 3x4Hyp-GalHyl-COL17A1(1-1497)
Homologues of 3x4Hyp-3Hyp-COL17A1(1-1497)
Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion
Hyperpolarization-activated cyclic nucleotide-gated channel 1 is a molecular determinant of the cardiac pacemaker current I(f)
Purification of phosphate-dependent glutaminase from isolated mitochondria of Ehrlich ascites-tumour cells
Regulation of Ca2+ signaling in mast cells by tyrosine-phosphorylated and unphosphorylated non-T cell activation linker
The mucopolysaccharidoses: inborn errors of glycosaminoglycan catabolism
Human adenine phosphoribosyltransferase. Affinity purification, subunit structure, amino acid composition, and peptide mapping.
The p46 subunit of eukaryotic initiation factor (eIF)-4F exchanges with eIF-4A.
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Association of licensing factors with the pre-replicative complex
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A single amino acid in the second transmembrane domain of GABA rho receptors regulates channel conductance
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Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1
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Serum galactosyl hydroxylysine as a biochemical marker of bone resorption
Cloning, characterization, and chromosomal localization of a gene frequently deleted in human liver cancer (DLC-1) homologous to rat RhoGAP
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Human liver glucokinase gene: cloning and sequence determination of two alternatively spliced cDNAs
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Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites
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Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity
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Phosphatidylinositol 3-kinase in bovine photoreceptor rod outer segments
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Lysosomal degradation of Asn-linked glycoproteins
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10'-apo-beta-carotenal [ChEBI:53153]
The three isoenzymes of human inositol-1,4,5-trisphosphate 3-kinase show specific intracellular localization but comparable Ca2+ responses on transfection in COS-7 cells
A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases
The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells
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The role of GRASP55 in Golgi fragmentation and entry of cells into mitosis
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3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XIII) chain
3,4-hydroxyprolyl-collagen alpha-1(XIII) chain
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XIII) chain
3,4-Hyp 5-Hyl-collagen alpha-1(XIII) chain
4-Hyp 5-Gal-Hyl-collagen alpha-1(XIII) chain
4-hydroxyprolyl-collagen alpha-1(XIII) chain
4-Hyp 5-Hyl-collagen alpha-1(XIII) chain
Induction of ceruloplasmin synthesis by IFN-gamma in human monocytic cells
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IL-7 Dependence in human B lymphopoiesis increases during progression of ontogeny from cord blood to bone marrow
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4-Hyp Glu-Gal-Hyl-collagen alpha-1(XIII) chain
4-hydroxyprolyl collagen alpha-1(XIII) chain
5-hydroxylysyl-collagen alpha-1(XIII) chain
Glu-Gal-Hyl-collagen alpha-1(XIII) chain
Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
Mammalian exocyst complex is required for the docking step of insulin vesicle exocytosis
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XV)
G(1) to S transition: more than a cell cycle engine switch.
Genetic basis of mitochondrial HMG-CoA synthase deficiency
The ubiquitously expressed Syp phosphatase interacts with c-kit and Grb2 in hematopoietic cells
Regulation of lipid binding underlies the activation mechanism of class IA PI3-kinases
The quality control of MHC class I peptide loading
Molecular cloning and functional characterization of a novel mammalian sphingosine kinase type 2 isoform
Morquio A syndrome: cloning, sequence, and structure of the human N-acetylgalactosamine 6-sulfatase (GALNS) gene
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Neurotransmitter uptake and Metabolism In Glial Cells
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Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS
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Interaction of alphaPIX (ARHGEF6) with beta-parvin (PARVB) suggests an involvement of alphaPIX in integrin-mediated signaling
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Signal transduction by the neurotrophin receptors
Glu-Gal-Hyl-collagen alpha-1(XVII) chain
(GlcN)1 (Ino(acyl)-P)1 (Man)2 (EtN)1 (P)1
6-O-{alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(1->6)-2-O-[(2-aminoethyl)phosphoryl]-alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl}-O-acyl-1-phosphatidyl-1D-myo-inositol [ChEBI:53059]
6-O-[alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl]-O-acyl-1-phosphatidyl-1D-myo-inositol [ChEBI:53056]
Diversification of Neu differentiation factor and epidermal growth factor signaling by combinatorial receptor interactions
Galpha Gbetagamma dissociation may be due to retraction of a buried lysine and disruption of an aromatic cluster by a GTP-sensing Arg Trp pair
Regulation of deoxyadenosine and nucleoside analog phosphorylation by human placental adenosine kinase
5-hydroxylysyl-collagen alpha-1(XVII) chain
Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation
ChEBI:53020 (Glc)2 (GlcNAc)2 (Man)9 (PP-Dol)1
ChEBI:53019 (Glc)3 (GlcNAc)2 (Man)9 (PP-Dol)1
Cdc25A stability is controlled by the ubiquitin-proteasome pathway during cell cycle progression and terminal differentiation
5-hydroxylysyl-collagen alpha-1(XVIII) chain
FACL4, encoding fatty acid-CoA ligase 4, is mutated in nonspecific X-linked mental retardation
Novel interleukin-2 receptor subunit detected by cross-linking under high-affinity conditions
Y14 and hUpf3b form an NMD-activating complex
Gene identification for the cblD defect of vitamin B12 metabolism
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Advanced glycation endproduct (AGE) receptor 1 is a negative regulator of the inflammatory response to AGE in mesangial cells
Activation of FAK and Src are receptor-proximal events required for netrin signaling
Focal adhesion kinase in netrin-1 signaling
Roles of aquaporin-3 water channels in volume-regulatory water flow in a human epithelial cell line
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Characterization of the mitogen-activated protein kinase kinase 4 (MKK4)/c-Jun NH2-terminal kinase 1 and MKK3/p38 pathways regulated by MEK kinases 2 and 3. MEK kinase 3 activates MKK3 but does not cause activation of p38 kinase in vivo.
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Vascular endothelial growth factor signaling to endothelial nitric oxide synthase: more than a FLeeTing moment
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DNA replication initiates at multiple sites on plasmid DNA in Xenopus egg extracts.
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integral component of lumenal side of endoplasmic reticulum membrane
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4-Hyp 5-Hyl-collagen alpha-1(XVII) chain
Homologues of 3x4Hyp-5Hyl-COL17A1(1-1497)
Activation of adenylyl cyclases, regulation of insulin status, and cell survival by G(alpha)olf in pancreatic beta-cells
Am J Physiol Regul Integr Comp Physiol 282:R870-80
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XVII) chain
Homologues of 3x4Hyp-GlcGalHyl-COL17A1(1-1497)
Connections with connexins: the molecular basis of direct intercellular signaling
Differential expression and regulation of toll-like receptors (TLR) in human leukocytes: selective expression of TLR3 in dendritic cells
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Angiogenesis is regulated by a novel mechanism: pro- and antiangiogenic proteins are organized into separate platelet alpha granules and differentially released
SOST is a ligand for LRP5/LRP6 and a Wnt signaling inhibitor
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Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution.
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Sequencing and expression of a cDNA for human glutathione synthetase
Isolation and characterization of a cDNA clone encoding human aromatic L-amino acid decarboxylase
4-hydroxyprolyl collagen alpha-1(XVII) chain
The unfolded protein response is an important regulator of inflammatory genes in endothelial cells
Cloning and functional expression of a human kidney Na+:HCO3- cotransporter
Mutational analysis of a patient with mucopolysaccharidosis type VII, and identification of pseudogenes
miRNAs on the move: miRNA biogenesis and the RNAi machinery
Transcriptional regulation of HMG-CoA synthase and HMG-CoA reductase genes by human ACBP
Wingless secretion requires endosome-to-Golgi retrieval of Wntless/Evi/Sprinter by the retromer complex
Wingless secretion promotes and requires retromer-dependent cycling of Wntless
N-retinylidene-phosphatidylethanolamine is the preferred retinoid substrate for the photoreceptor-specific ABC transporter ABCA4 (ABCR)
Identification and characterization of PS-GAP as a novel regulator of caspase-activated PAK-2
Cytochromes P450 with bisallylic hydroxylation activity on arachidonic and linoleic acids studied with human recombinant enzymes and with human and rat liver microsomes
Potential role of protein kinase B in insulin-induced glucose transport, glycogen synthesis, and protein synthesis
The human zinc transporter SLC39A8 (Zip8) is critical in zinc-mediated cytoprotection in lung epithelia
Am J Physiol Lung Cell Mol Physiol 294:L1127-36
Ubiquitin ligase Nedd4L targets activated Smad2/3 to limit TGF-beta signaling
Novel 5 alpha-steroid reductase (SRD5A3, type-3) is overexpressed in hormone-refractory prostate cancer
Cellular circadian pacemaking and the role of cytosolic rhythms
The E3 ubiquitin ligase TRIM21 negatively regulates the innate immune response to intracellular double-stranded DNA
Dynamic, site-specific interaction of hypoxia-inducible factor-1alpha with the von Hippel-Lindau tumor suppressor protein
New functional roles for non-collagenous domains of basement membrane collagens
Somatic mutations in p85alpha promote tumorigenesis through class IA PI3K activation
Identification of shc as the primary protein binding to the tyrosine-phosphorylated beta 3 subunit of alpha IIbbeta 3 during outside-in integrin platelet signaling
Cloning of the human equilibrative, nitrobenzylmercaptopurine riboside (NBMPR)-insensitive nucleoside transporter ei by functional expression in a transport-deficient cell line
Fractional Ca(2+) current through human neuronal alpha7 nicotinic acetylcholine receptors
Architecture of the human origin recognition complex.
NRAGE, a p75 neurotrophin receptor-interacting protein, induces caspase activation and cell death through a JNK-dependent mitochondrial pathway
The structure of importin-beta bound to SREBP-2: nuclear import of a transcription factor
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NMNAT2 (Mg2+) (name copied from entity in Homo sapiens)
NADSYN1 hexamer (name copied from entity in Homo sapiens)
Btn-ACACB:2Mn2+ (name copied from entity in Homo sapiens)
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Intracellular retention, degradation, and signaling of glycosylation-deficient FGFR2 and craniosynostosis syndrome-associated FGFR2C278F
Highly conserved mouse and human brain sulfotransferases: molecular cloning, expression, and functional characterization
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110720
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3541.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110693
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4471.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110680
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4429.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110668
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3368.2
MOCOS:PXLP (name copied from entity in Homo sapiens)
GPHN:Mg2+ (name copied from entity in Homo sapiens)
3xGPHN:3xMg2+ (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636663
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110731
SMAD7:NEDD4L (name copied from entity in Homo sapiens)
p-2S-SMAD2/3:SMAD4 (name copied from entity in Homo sapiens)
SMAD7:SMURF/NEDD4L (name copied from entity in Homo sapiens)
Ub-SMAD3 (name copied from entity in Homo sapiens)
p-2S-SMAD2/3:MTMR4 (name copied from entity in Homo sapiens)
Ub-SMAD2 (name copied from entity in Homo sapiens)
SMAD3:STUB1 (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4564.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5419.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110732
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_236390.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110638
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_241112.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636576
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636575
2xMTHFD1 (name copied from entity in Homo sapiens)
2xNAPRT1 (name copied from entity in Homo sapiens)
2xMTHFR (name copied from entity in Homo sapiens)
Proximal signaling events in Fc epsilon RI-mediated mast cell activation
J. Allergy Clin. Immunol. 119:544-52; quiz 553-4
4xSHMT1 (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2983.2
MOCS3:Zn2+ (red.) (name copied from entity in Homo sapiens)
holo-MOCS1 (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5595.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110652
MOCS3-S-S(1-):Zn2+ (name copied from entity in Homo sapiens)
2xNFS1:2xPXLP (name copied from entity in Homo sapiens)
MOCS3:Zn2+ (ox.) (name copied from entity in Homo sapiens)
2xMOCS2-CO-S(1-):2xMOCS2B (name copied from entity in Homo sapiens)
2xMOCS2A:2xMOCS2B (name copied from entity in Homo sapiens)
2-Hydroxy-1,2,3-propanetricarboxylic acid
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636568
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2857.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110660
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2310.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110711
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4768.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110685
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110672
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636567
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_209169.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623738
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2490.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_227095.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621783
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621781
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_217444.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_260184.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620456
Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_250134.1
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RNA Polymerase III Transcription Termination
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623733
Members of the human glyceraldehyde-3-phosphate dehydrogenase-related gene family map to dispersed chromosomal locations.
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4986.2
ChEBI:30725 aflatoxin B1 exo-8,9-epoxide
starch (amylose) (name copied from entity in Homo sapiens)
starch (amylopectin) (name copied from entity in Homo sapiens)
GSTO2 homodimer (name copied from entity in Homo sapiens)
CYB5A:ferriheme (name copied from entity in Homo sapiens)
CYB5R3:FAD (name copied from entity in Homo sapiens)
2xENPP1 (name copied from entity in Homo sapiens)
2xTRAP (name copied from entity in Homo sapiens)
2xTPK1:Mg2+ (name copied from entity in Homo sapiens)
RFK:Mg2+ (name copied from entity in Homo sapiens)
CYB5A:heme (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648650
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_151593.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648155
phosphoribosyl pyrophosphate synthetase holoenzyme
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648159
phosphoribosyl pyrophosphate synthetase 1 holoenzyme (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2395883
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_150797.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2395817
2xPNPO:2xFMN (name copied from entity in Homo sapiens)
2xAOX1:cofactors (name copied from entity in Homo sapiens)
AOX1:cofactors (name copied from entity in Homo sapiens)
MMACHC:cob(II)alamin (name copied from entity in Homo sapiens)
MMACHC:MMADHC:cob(II)alamin (name copied from entity in Homo sapiens)
MMACHC:MMADHC (name copied from entity in Homo sapiens)
MTRR:MTR (name copied from entity in Homo sapiens)
MTR:Zn2+ (name copied from entity in Homo sapiens)
3xPPCDC:3xFMN (name copied from entity in Homo sapiens)
2xPDXK:2xZn2+ (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2395880
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_223025.2
2xPPCS (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648157
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_203212.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2395877
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_151268.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_150635.1
2xMUT (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648647
3xMMAB (name copied from entity in Homo sapiens)
2xMMAA:2xMUT (name copied from entity in Homo sapiens)
MTRR:MTR(cob(I)alamin) (name copied from entity in Homo sapiens)
Human aquaporin adipose (AQPap) gene. Genomic structure, promoter analysis and functional mutation
MTR:Zn2+:cob(I)alamin (name copied from entity in Homo sapiens)
MTRR:MTR(MeCbl) (name copied from entity in Homo sapiens)
MTR:Zn2+:MeCbl (name copied from entity in Homo sapiens)
MTRR:MTR(cob(II)alamin) (name copied from entity in Homo sapiens)
MTR:Zn2+:cob(II)alamin (name copied from entity in Homo sapiens)
MTRR:FMN:FAD (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2509836
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_151581.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648643
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648644
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648646
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_221351.2
4x(Btn-PC:Mn2+) (name copied from entity in Homo sapiens)
6xMCCC1:6xMCCC2 (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_220313.2
PCCA:PCCB (name copied from entity in Homo sapiens)
6x(Btn-PCCA:PCCB) (name copied from entity in Homo sapiens)
Btn-PCCA:PCCB (name copied from entity in Homo sapiens)
4x(PC:Mn2+) (name copied from entity in Homo sapiens)
Uninterrupted MCM2-7 function required for DNA replication fork progression.
2xMMAA (name copied from entity in Homo sapiens)
2xMMAA:2xMUT:AdoCbl (name copied from entity in Homo sapiens)
2xMUT:AdoCbl (name copied from entity in Homo sapiens)
6x(PCCA:PCCB) (name copied from entity in Homo sapiens)
Identification of cytochrome P450 isoforms involved in the metabolism of loperamide in human liver microsomes
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_212708.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648653
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_152050.1
EGF receptor gene mutations are common in lung cancers from "never smokers" and are associated with sensitivity of tumors to gefitinib and erlotinib
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_150529.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648649
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2509848
glycogen-GYG1:GYS1-a tetramer (name copied from entity in Homo sapiens)
PPP1R3C:glycogen-GYG2:GYS2-a tetramer (name copied from entity in Homo sapiens)
PPP1R3C:glycogen-GYG1:GYS1-a tetramer (name copied from entity in Homo sapiens)
glycogen-GYG2:GYS2-a tetramer (name copied from entity in Homo sapiens)
glycogen-GYG1:GYS1-b tetramer (name copied from entity in Homo sapiens)
Src-family kinases in B-cell development and signaling
oligoGlc-GYG2:GYS2-b tetramer (name copied from entity in Homo sapiens)
Me2K37-replicative histone H3, MeK5-replicative histone H3
polyGlc-GYG1:GYS1-a tetramer (name copied from entity in Homo sapiens)
MeK5-replicative histone H3, Replicative histone H3
oligoGlc-GYG2:GYS2-a tetramer (name copied from entity in Homo sapiens)
Me2K5 replicative histone H3, MeK5-replicative histone H3
GYG2:GYS2-b tetramer (name copied from entity in Homo sapiens)
Phosphoglucomutase 1: a gene with two promoters and a duplicated first exon
polyGlc-GYG1:GYS1-b tetramer (name copied from entity in Homo sapiens)
polyGlc-GYG2:GYS2-a tetramer (name copied from entity in Homo sapiens)
G(q) alpha subunit (pancreatic beta cell)
PGYM dimer a form (name copied from entity in Homo sapiens)
PGYM dimer, b form (name copied from entity in Homo sapiens)
Characterization of RasGRP2, a plasma membrane-targeted, dual specificity Ras/Rap exchange factor
PGYL dimer a form (name copied from entity in Homo sapiens)
PGYL dimer b form (name copied from entity in Homo sapiens)
PGYB b dimer:AMP (name copied from entity in Homo sapiens)
phosphorylase kinase complex (PHKL) (name copied from entity in Homo sapiens)
PPP1R3C:phosphoglycogen-GYG1:GYS1-a tetramer (name copied from entity in Homo sapiens)
PPP1R3C:phosphoglycogen-GYG2:GYS2-a tetramer (name copied from entity in Homo sapiens)
PGYB dimer b form (name copied from entity in Homo sapiens)
PGYB dimer a form (name copied from entity in Homo sapiens)
phosphorylase kinase complex (PHKM) (name copied from entity in Homo sapiens)
poly((1,4)-alpha-glucosyl) glycogenin dimer
Delta, epsilon, gamma subunits of acetylcholine receptor
((1,6)-alpha-glucosyl)poly((1,4)-alpha-glucosyl)GYG2 dimer (name copied from entity in Homo sapiens)
((1,6)-alpha-glucosyl)poly((1,4)-alpha-glucosyl)GYG1 dimer (name copied from entity in Homo sapiens)
((1,6)-alpha-glucosyl)poly((1,4)-alpha-glucosyl) glycogenin dimer
((1,6)-alpha-glucosyl)poly((1,4)-alpha-glucosyl)GYG dimer
limit dextrin-glycogenin-2 dimer (name copied from entity in Homo sapiens)
glycogen-glycogenin-2 dimer (name copied from entity in Homo sapiens)
limit dextrin-glycogenin-1 dimer (name copied from entity in Homo sapiens)
PGYM b dimer:AMP (name copied from entity in Homo sapiens)
glycogen-glycogenin-1 dimer (name copied from entity in Homo sapiens)
Molecular cloning of a human cDNA encoding a trifunctional enzyme of carbamoyl-phosphate synthetase-aspartate transcarbamoylase-dihydroorotase in de Novo pyrimidine synthesis
PGD dimer (name copied from entity in Homo sapiens)
MeK37-replicative histone H3, Replicative histone H3
G6PD tetramer (name copied from entity in Homo sapiens)
Me3K10 replicative histone H3, Me2K10-replicative histone H3
transketolase dimer (name copied from entity in Homo sapiens)
Me2K10 replicative histone H3, MeK10-replicative histone H3
RPE dimer (name copied from entity in Homo sapiens)
Me3K5 replicative histone H3, Me2K5-replicative histone H3
GALE dimer (name copied from entity in Homo sapiens)
GYG2 dimer (name copied from entity in Homo sapiens)
G6PD dimer (name copied from entity in Homo sapiens)
Me3K28 replicative histone H3, Me2K28-replicative histone H3
Me2K28 replicative histone H3, MeK28-replicative histone H3
poly((1,4)-alpha-glucosyl)GYG1 dimer (name copied from entity in Homo sapiens)
poly((1,4)-alpha-glucosyl)GYG2 dimer (name copied from entity in Homo sapiens)
Me2sR9-replicative histone H3, MeR9-replicative histone H3
GYG1 dimer (name copied from entity in Homo sapiens)
Mutations in antiquitin in individuals with pyridoxine-dependent seizures
DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs.
The cytochrome P450 superfamily: biochemistry, evolution and drug metabolism in humans
Mutations in INPP5E, encoding inositol polyphosphate-5-phosphatase E, link phosphatidyl inositol signaling to the ciliopathies
6x(Btn-MCCC1:MCCC2) (name copied from entity in Homo sapiens)
Btn-ACACA:2Mn2+ (name copied from entity in Homo sapiens)
ACACA:2Mn2+ (name copied from entity in Homo sapiens)
ACACB:2Mn2+ (name copied from entity in Homo sapiens)
Potassium channels: newly found players in synaptic plasticity
Functional characterization of an isoform-selective inhibitor of PI3K-p110? as a potential anticancer agent
Integrating the VEGF signals leading to actin-based motility in vascular endothelial cells
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623722
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_225020.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623720
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621775
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621776
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623717
Somatic mutations of the protein kinase gene family in human lung cancer
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623715
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_241140.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623716
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623701
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623713
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623702
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623710
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623706
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623712
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623711
Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein
Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells
The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation
Cell-cell signaling via Eph receptors and ephrins
Citrate lyase homotetramer (name copied from entity in Homo sapiens)
phosphorylated HSL dimer (name copied from entity in Homo sapiens)
NPC1L1:ezetimibe complex (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621766
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621767
FAS dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110095
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2972.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621762
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110093
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5210.2
GPD1 dimer (name copied from entity in Homo sapiens)
AMPK heterotrimer (active) (name copied from entity in Homo sapiens)
ACADVL dimer (name copied from entity in Homo sapiens)
GPD1L dimer (name copied from entity in Homo sapiens)
DGAT1 tetramer (name copied from entity in Homo sapiens)
NUDT3:Mg2+ (name copied from entity in Homo sapiens)
DNA with RNA Polymerase III Type 1 Closed Promoter
DNA with RNA Polymerase III Type 2 Closed Promoter
NUDT10:Mg2+/Mn2+ (name copied from entity in Homo sapiens)
Polymerase III gene DNA with a termination site
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_234010.1
IMPA1:Mg2+ (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621761
IMPA1 dimer (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_206329.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622587
elongating pre-mRNA Pol III transcript plus 1 nucleotide
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621623
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621625
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621621
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621622
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621617
Polymerase III gene DNA with transcription bubble (single-stranded region)
IMPA2 dimer (name copied from entity in Homo sapiens)
IMPA2:Mg2+ (name copied from entity in Homo sapiens)
elongating pre-mRNA Pol III oligonucleotide
ISYNA1:NAD+ (name copied from entity in Homo sapiens)
DNA with RNA Polymerase III Type 1 Open Promoter
dimerized CEL:bile salt complex (name copied from entity in Homo sapiens)
DNA with RNA Polymerase III Type 2 Open Promoter
CEL:bile salt complex (name copied from entity in Homo sapiens)
released pre-mRNA Pol III oligonucleotide
PLCH1:Ca2+ (name copied from entity in Homo sapiens)
PLCG2:Ca2+ (name copied from entity in Homo sapiens)
PLCG1:Ca2+ (name copied from entity in Homo sapiens)
PLCD3:Ca2+ (name copied from entity in Homo sapiens)
Sarco/endoplasmic reticulum Ca2+ ATPases (SERCAs)
PLCE1:Ca2+ (name copied from entity in Homo sapiens)
PLCD1:Ca2+ (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636682
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_216269.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623693
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623689
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623694
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623697
Sarco/endoplasmic reticulum Ca2+ ATPases
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5725.2
Sef is a spatial regulator for Ras/MAP kinase signaling
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111736
ITPKB:Ca2+:CALM1 (name copied from entity in Homo sapiens)
NUDT4:Mg2+/Mn2+ (name copied from entity in Homo sapiens)
PLCH2:Ca2+ (name copied from entity in Homo sapiens)
PLCD4:Ca2+ (name copied from entity in Homo sapiens)
WLS:retromer (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_239300.1
PLCB2:Ca2+ (name copied from entity in Homo sapiens)
Identification of the non-lysosomal glucosylceramidase as beta-glucosidase 2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636679
PLCB1:Ca2+ (name copied from entity in Homo sapiens)
WLS:WNT (name copied from entity in Homo sapiens)
VPS35:VPS29:VPS26 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622588
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_249310.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621769
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_257111.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621788
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621790
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621787
Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636680
Probable phospholipid-transporting ATPases
Peroxisome proliferator activated receptors and lipoprotein metabolism
PLCB3:Ca2+ (name copied from entity in Homo sapiens)
PLCB4:Ca2+ (name copied from entity in Homo sapiens)
PLCZ1:Ca2+ (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_232181.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623588
Molecular cloning and transient expression in COS7 cells of a novel human PDE4B cAMP-specific phosphodiesterase, HSPDE4B3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621828
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110092
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_247164.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623591
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_248217.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623590
PORCN:LGK974 (name copied from entity in Homo sapiens)
TNKS1/2:XAV939 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110090
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623584
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_240813.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622162
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622160
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622159
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5622155
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4457.2
Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components
Deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_235901.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621612
Collagen XXIII, novel ligand for integrin alpha2beta1 in the epidermis
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4046.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110091
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110094
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621613
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2815.2
The PI-3 kinase/Akt pathway and T cell activation: pleiotropic pathways downstream of PIP3
Vav1: a key signal transducer downstream of the TCR
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621833
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621829
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4501.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621838
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621836
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5621835
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623581
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_232986.1
Small conductance Ca2+ activated potassium channel subunits
DVL:CUL3:KLHL12:RBX1 (name copied from entity in Homo sapiens)
CUL3:KLHL12:RBX1 (name copied from entity in Homo sapiens)
XPO1:YWHAZ:p-S20-CBY1:CTNNB1 (name copied from entity in Homo sapiens)
CTNNB1:CHD8 (name copied from entity in Homo sapiens)
DVL:CCDC88C (name copied from entity in Homo sapiens)
RYK:WNTs (name copied from entity in Homo sapiens)
ub-DVL1:HECW1 (name copied from entity in Homo sapiens)
WIF1:WNT (name copied from entity in Homo sapiens)
ub-DVL:CUL3:KLHL12:RBX1 (name copied from entity in Homo sapiens)
DVL1:HECW1 (name copied from entity in Homo sapiens)
Inhibition of Mcm4,6,7 helicase activity by phosphorylation with cyclin A/Cdk2.
pS45-beta-catenin:p-Axin:GSK3 del304-316:CK1alpha:APC:PP2A:AMER1 complex (name copied from entity in Homo sapiens)
p-AXIN:GSK3 del304-316:CK1alpha:APC:PP2A:AMER1 complex (name copied from entity in Homo sapiens)
CSNK2A1 dimer (name copied from entity in Homo sapiens)
CSNK2A2 dimer (name copied from entity in Homo sapiens)
Casein kinase II (name copied from entity in Homo sapiens)
CTNNB1:AXIN:GSK3:CK1alpha:ub-APC:PP2A:AMER1 complex (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111783
TCF/LEF:TLE:HDAC1 (name copied from entity in Homo sapiens)
CSNK2A1:CSNK2A2 (name copied from entity in Homo sapiens)
ppDVL:PIP5K1B (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111814
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5432.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623723
Binding of MET-TRNAf and GTP to homogeneous initiation factor MP.
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623724
pS37,T41,S45-CTNNB1 S33 mutants:Axin:GSK3:CK1alpha:APC:PP2A:AMER1 complex (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111349
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4307.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111809
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3101.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623721
TLE:HDAC1 (name copied from entity in Homo sapiens)
TCF/LEF:CTNNB1 (name copied from entity in Homo sapiens)
TCF/LEF:CTNNB1:CBP/p300 (name copied from entity in Homo sapiens)
TCF/LEF:CTNNB1:PAF1-like complex (name copied from entity in Homo sapiens)
TCF/LEF:CTNNB1:RUVBL1:TRRAP:KAT5 (name copied from entity in Homo sapiens)
TCF/LEF:CTNNB1:APC:CTBP:BTRC (name copied from entity in Homo sapiens)
APC:CTBP:CTNNB1:BTRC (name copied from entity in Homo sapiens)
YWHAZ:p-S20-CBY:CTNNB1 (name copied from entity in Homo sapiens)
pS20-CBY1:CTNNB1 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623728
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111793
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5731.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5623725
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4892.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111786
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5414.2
Steroid hydroxylation by human fetal CYP3A7 and human NADPH-cytochrome P450 reductase coexpressed in insect cells using baculovirus
Res Commun Mol Pathol Pharmacol 100:15-28
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111784
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4262.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111785
TLE3 tetramer (name copied from entity in Homo sapiens)
TLE2 tetramer (name copied from entity in Homo sapiens)
TLE1 tetramer (name copied from entity in Homo sapiens)
p-AXIN:CK1alpha:GSK3B:phospho-APC (20 aa repeat region):PP2A:AMER1 complex (name copied from entity in Homo sapiens)
ubiquitinated phospho-beta-catenin:RBX1:SCF(beta-TrCP1) complex (name copied from entity in Homo sapiens)
RBX1:SKP1:CUL1:beta-TrCP1:phosphorylated beta-catenin complex (name copied from entity in Homo sapiens)
SCF beta-TrCP complex (name copied from entity in Homo sapiens)
p-S33,S37,T41,S45-beta-catenin:p-AXIN:CK1alpha:GSK3B:phospho-ub-APC (20 aa repeat region):PP2A:AMER1 complex (name copied from entity in Homo sapiens)
p-S37,T41,S45-beta-catenin:p-AXIN:GSK3:CK1alpha:ub-APC:PP2A:AMER1 complex (name copied from entity in Homo sapiens)
p-S33,S37,T41,S45-beta-catenin:p-AXIN:GSK3:CK1alpha:ub-APC:PP2A:AMER1 complex (name copied from entity in Homo sapiens)
CTNNB1 S45 mutants:AXIN:GSK3:CK1alpha:APC:PP2A:AMER1 complex (name copied from entity in Homo sapiens)
TCF7L2/TCF7L1:CTBPs (name copied from entity in Homo sapiens)
pT41,S45-CTNNB1 S37 mutants:Axin:GSK3:CK1alpha:APC:PP2A:AMER1 complex (name copied from entity in Homo sapiens)
pS45-CTNNB1 T41 mutants:Axin:GSK3:CK1alpha:APC:PP2A:AMER1 complex (name copied from entity in Homo sapiens)
TLE3:HDAC1 (name copied from entity in Homo sapiens)
TLE2:HDAC1 (name copied from entity in Homo sapiens)
TLE:AES (name copied from entity in Homo sapiens)
TLE4:HDAC1 (name copied from entity in Homo sapiens)
Purified Wnt5a protein activates or inhibits beta-catenin-TCF signaling depending on receptor context
TLE1:HDAC1 (name copied from entity in Homo sapiens)
TLE4 tetramer (name copied from entity in Homo sapiens)
Ub-SMAD7 (name copied from entity in Homo sapiens)
SMAD7:RNF111 (name copied from entity in Homo sapiens)
Ub-SMAD4 (name copied from entity in Homo sapiens)
p-SMAD2/3:SMAD4:RBL1:E2F4/5:DP1/2 (name copied from entity in Homo sapiens)
template DNA:9 nucleotide transcript hybrid
RBL1:E2F4/5:DP1/2 (name copied from entity in Homo sapiens)
template DNA:11 nucleotide transcript hybrid
CDK8:CCNC (name copied from entity in Homo sapiens)
p-T,2S-SMAD2/3:SMAD4 (name copied from entity in Homo sapiens)
P-TEFb complex (name copied from entity in Homo sapiens)
Elongating transcript prior to separation
PAR-SMAD2/3:PAR-SMAD4 (name copied from entity in Homo sapiens)
Open DNA -10 to +2 containing RNA Polymerase II promoter
p-AXIN:GSK3:CK1alpha:ub-APC:PP2A:AMER1 complex (name copied from entity in Homo sapiens)
p-2S-SMAD2/3:SMAD4:PPM1A (name copied from entity in Homo sapiens)
beta-catenin:p-AXIN:GSK3:CK1alpha:ub-APC:PP2A:AMER1 complex (name copied from entity in Homo sapiens)
PP2A (name copied from entity in Homo sapiens)
template DNA:4-9 nucleotide transcript hybrid
p-T41,S45-beta-catenin:p-AXIN:GSK3:CK1alpha:ub-APC:PP2A:AMER1 complex (name copied from entity in Homo sapiens)
Elongating transcript in processive Pol II mediated elongation
pS45-beta-catenin:p-Axin:GSK3:CK1alpha:ub-APC:PP2A:AMER1 complex (name copied from entity in Homo sapiens)
Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20
Ub-SMAD4:USP9X (name copied from entity in Homo sapiens)
template DNA with first transcript dinucleotide, opened to +8 position
p-T-2S-SMAD2/3:SMAD4:NEDDL4 (name copied from entity in Homo sapiens)
Template DNA hybrid with phosphodiester-PPi intermediate
Ub-p-T-2S-SMAD2/3:SMAD4 (name copied from entity in Homo sapiens)
template DNA:4 nucleotide transcript hybrid
p-2S-SMAD2/3:SMAD4:PARP1 (name copied from entity in Homo sapiens)
template DNA:3 nucleotide transcript hybrid
template DNA opened from -10 to +2, with first nucleotide base-paired at 5'-end
DNA containing RNA Polymerase II promoter
Management of cellular energy by the AMP-activated protein kinase system
Mammalian G proteins and their cell type specific functions
Genetics of mammalian meiosis: regulation, dynamics and impact on fertility
Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
Biochemistry of signal transduction and regulation
Collagen biosynthesis and modifying enzymes
The heteromeric cyclic nucleotide-gated channel adopts a 3A:1B stoichiometry
Heparan sulfate/heparin (HS-GAG) metabolism
Cellular localization of the vesicular inhibitory amino acid transporter in the mouse and human retina
NCAM-mediated adhesion of transfected cells to agrin
Nuclear translocation of plk1 mediated by its bipartite nuclear localization signal
Stimulation of the human CTP:phosphoethanolamine cytidylyltransferase gene by early growth response protein 1
The adapter protein APS associates with the multifunctional docking sites Tyr-568 and Tyr-936 in c-Kit
Regulation of gene expression in endocrine-committed (NEUROG3+) progenitor cells
Dickkopf-1 is a member of a new family of secreted proteins and functions in head induction
PLA2G2D:Ca2+ (name copied from entity in Homo sapiens)
Interleukin 3 and erythropoietin induce association of Vav with Tec kinase through Tec homology domain
STIM1 converts TRPC1 from a receptor-operated to a store-operated channel: moving TRPC1 in and out of lipid rafts
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_27529.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=936706
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_117597.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=977329
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638643
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638646
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638644
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_212006.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_205852.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637661
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619602
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619600
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619599
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26092.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=893598
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_235859.1
PI:PITPNB (name copied from entity in Homo sapiens)
CHPT1:Mg2+/Mn2+ (name copied from entity in Homo sapiens)
PCYT1B dimer (name copied from entity in Homo sapiens)
CEPT1:Mg2+/Mn2+ (name copied from entity in Homo sapiens)
EPT1:Mg2+/Mn2+ (name copied from entity in Homo sapiens)
Novel variants in human Aquaporin-4 reduce cellular water permeability
LPIN3:Mg2+ (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619593
PCYT1A dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619598
PISD:Pyruvoyl (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619597
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619588
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619587
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619589
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619585
LPIN2:Mg2+ (name copied from entity in Homo sapiens)
LPIN1:Mg2+ (name copied from entity in Homo sapiens)
PLA2G2E:Ca2+ (name copied from entity in Homo sapiens)
PLA2G2F:Ca2+ (name copied from entity in Homo sapiens)
PLA2G5:Ca2+ (name copied from entity in Homo sapiens)
PLA2G10:Ca2+ (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619583
CHKA:CHKA (name copied from entity in Homo sapiens)
CHKB:CHKB (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619581
CHKA:CHKB (name copied from entity in Homo sapiens)
PCYT2 dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619579
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4410.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113522
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_255650.1
PIP4K2A:PIP4K2B (name copied from entity in Homo sapiens)
PIP4K2B:PIP4K2B (name copied from entity in Homo sapiens)
PIK3C2B:Ca2+/Mg2+/Mn2+ (name copied from entity in Homo sapiens)
PIP4K2A:PIP4K2A (name copied from entity in Homo sapiens)
Characterization of fibroblast growth factor receptor 2 overexpression in the human breast cancer cell line SUM-52PE
PIK3CA:PIK3R3 (name copied from entity in Homo sapiens)
PIK3CA:PIK3R2 (name copied from entity in Homo sapiens)
PIK3CA:PIK3R1 (name copied from entity in Homo sapiens)
PIKFYVE:VAC14:FIG4 (name copied from entity in Homo sapiens)
PIK3C2A:Ca2+/Mg2+ (name copied from entity in Homo sapiens)
PIK3C3:Mn2+ (name copied from entity in Homo sapiens)
ARF1/3:GTP:PI4KB (name copied from entity in Homo sapiens)
PIK3C3:Mn2+:PIK3R4:Mn2+ (name copied from entity in Homo sapiens)
PIK3R4:Mn2+ (name copied from entity in Homo sapiens)
The shed ectodomain of type XIII collagen associates with the fibrillar fibronectin matrix and may interfere with its assembly in vitro
HADH octamer (name copied from entity in Homo sapiens)
CDIPT:Mg2+/Mn2+ (name copied from entity in Homo sapiens)
ARF1:GTP (name copied from entity in Homo sapiens)
PC:PITPNB (name copied from entity in Homo sapiens)
CDS1:Mg2+ (name copied from entity in Homo sapiens)
COQ6:FAD (name copied from entity in Homo sapiens)
COQ7:Fe2+ (name copied from entity in Homo sapiens)
active STS dimer (name copied from entity in Homo sapiens)
G(q) alpha 11,14,15,Q:GDP:G beta:G gamma (name copied from entity in Homo sapiens)
G(q) alpha 11,14,15,Q:GDP (name copied from entity in Homo sapiens)
Alpha-2 adrenoceptor:Catecholamine (name copied from entity in Homo sapiens)
Muscarinic Acetylcholine Receptor M3:Acetylcholine Complex (name copied from entity in Homo sapiens)
ASAH1 (name copied from entity in Homo sapiens)
Active N-SMase:Mg2+ (name copied from entity in Homo sapiens)
Kinesin-5 regulates the growth of the axon by acting as a brake on its microtubule array
GLA dimer (name copied from entity in Homo sapiens)
SPTLC1:SPTLC3 (name copied from entity in Homo sapiens)
LTA4H:Zn2+ (name copied from entity in Homo sapiens)
GGT1 (name copied from entity in Homo sapiens)
GGT5 (name copied from entity in Homo sapiens)
SPTLC1:SPTLC2 (name copied from entity in Homo sapiens)
ACSL1 (name copied from entity in Homo sapiens)
HPGDS dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=30102
ECHS1 hexamer (name copied from entity in Homo sapiens)
HADH dimer (name copied from entity in Homo sapiens)
Trifunctional Protein (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3974.2
ACADL tetramer (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_254462.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3962.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29588
The synthesis of inositol hexakisphosphate. Characterization of human inositol 1,3,4,5,6-pentakisphosphate 2-kinase
ACAT1 tetramer (name copied from entity in Homo sapiens)
DECR1 tetramer (name copied from entity in Homo sapiens)
ACADM tetramer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29702
NF-Y (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2965.2
SREBP1A,2:NF-Y:HMGCR gene (name copied from entity in Homo sapiens)
OXCT1 dimer (name copied from entity in Homo sapiens)
Oxidation of aflatoxin B1 by bacterial recombinant human cytochrome P450 enzymes
HMGCL dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=70846
SREBP1A,2 dimer (name copied from entity in Homo sapiens)
SREBP1A,1C,2:NF-Y:FDPS gene (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5337.2
SREBP1A,1C,2 dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=70721
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3652.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=70701
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619684
HACL1 tetramer (name copied from entity in Homo sapiens)
PHYH:Fe++ (name copied from entity in Homo sapiens)
ACOX2:FAD (name copied from entity in Homo sapiens)
HACL1 holoenzyme monomer (name copied from entity in Homo sapiens)
HSD17B4 dimer (name copied from entity in Homo sapiens)
ACOX3:FAD (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4872.2
ACOX1 dimer (name copied from entity in Homo sapiens)
ABCD1 homodimer (name copied from entity in Homo sapiens)
Inborn errors of ketogenesis and ketone body utilization
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638636
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638639
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638637
ACOX1:FAD complex (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_209550.2
GNPAT:AGPS complex (name copied from entity in Homo sapiens)
AGPS:FAD (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638622
FDPS:3Mg2+ (name copied from entity in Homo sapiens)
2(FDPS:3Mg2+) (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638624
IDI1 or 2 (name copied from entity in Homo sapiens)
MVD dimer (name copied from entity in Homo sapiens)
MVK dimer (name copied from entity in Homo sapiens)
HMGCR dimer (name copied from entity in Homo sapiens)
IDH1 dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638628
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638626
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_204520.2
SREBP1A,1C,2:SCAP (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638632
Molecular cloning and expression of human hepatocyte growth factor
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638629
Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins
SREBP1A,1C,2:SCAP:Cop II Coat (name copied from entity in Homo sapiens)
SCAP tetramer (name copied from entity in Homo sapiens)
3' -UTR-mediated translational regulation
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652512
Ran-GTP (name copied from entity in Homo sapiens)
SREBP1A,1C,2:Importin beta-1 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653339
SREBP1A,2:NF-Y:SP1:IDI1 gene (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_183293.3
Importin-beta:Ran GTP complex (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113576
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5174.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113584
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2393.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619706
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619708
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619653
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619702
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619704
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619705
SREBP1A,1C:NF-Y:GPAM gene (name copied from entity in Homo sapiens)
CH25H (Fe2+ cofactor) (name copied from entity in Homo sapiens)
SREBP1A,1C,2:ELOVL6 gene (name copied from entity in Homo sapiens)
SREBP1A,1C:NF-Y:SP1:FASN gene (name copied from entity in Homo sapiens)
PLA2G2A:Ca2+ (name copied from entity in Homo sapiens)
Coupling of tandem Smad ubiquitination regulatory factor (Smurf) WW domains modulates target specificity
SREBP1A,1C dimer (name copied from entity in Homo sapiens)
SREBP1A,2:LSS gene (name copied from entity in Homo sapiens)
SREBP1A,1C:ACACA gene (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=70715
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636762
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_227015.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_254278.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=70718
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5465.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5091.2
ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid synthesis
Identification of Vangl2 and Scrb1 as planar polarity genes in mammals
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619685
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619690
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619695
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619696
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619697
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619699
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_239181.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636763
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113580
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4213.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_206028.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113540
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2426.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113537
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4106.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4718.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619700
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Stimulation of the cell death response by PAK-2p34
VEGFs and receptors involved in angiogenesis versus lymphangiogenesis
Interaction of plexin-B1 with PDZ domain-containing Rho guanine nucleotide exchange factors
The E3 ubiquitin ligase ITCH negatively regulates canonical Wnt signaling by targeting dishevelled protein
Characterization of the human fumarylacetoacetate hydrolase gene and identification of a missense mutation abolishing enzymatic activity.
A novel class II phosphoinositide 3-kinase predominantly expressed in the liver and its enhanced expression during liver regeneration
Complement protein C1q directs macrophage polarization and limits inflammasome activity during the uptake of apoptotic cells
p53-Independent G1/S DNA damage checkpoint
The SIRP family of receptors and immune regulation
Molecular cloning of human 5-hydroxytryptamine3 receptor: heterogeneity in distribution and function among species
De novo mutations of the gene encoding the histone acetyltransferase KAT6B in two patients with Say-Barber/Biesecker/Young-Simpson syndrome
Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors
The Rac1 guanine nucleotide exchange factor Tiam1 mediates EphB receptor-dependent dendritic spine development
Proc. Natl. Acad. Sci. U.S.A. 104:7265-70
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Cyclin E associated events during G1/S transition
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Hyperpolarization-activated cation channels: from genes to function
Cloning and identification of a new member of water channel (AQP10) as an aquaglyceroporin
Human gastric (H+ + K+)-ATPase gene. Similarity to (Na+ + K+)-ATPase genes in exon/intron organization but difference in control region
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Exome and whole-genome sequencing of esophageal adenocarcinoma identifies recurrent driver events and mutational complexity
Voltage-gated Calcium Channels (pancreatic beta cell)
PP2A-ABdeltaC complex (name copied from entity in Homo sapiens)
Activated AMPK heterotrimer (name copied from entity in Homo sapiens)
AMPK gamma2:AMP (name copied from entity in Homo sapiens)
AMPK heterotrimer:AMP (name copied from entity in Homo sapiens)
AMPK heterotrimer (inactive) (name copied from entity in Homo sapiens)
Gs-activated adenylate cyclase (name copied from entity in Homo sapiens)
Voltage-gated Calcium Channel, R-type 2.3 (name copied from entity in Homo sapiens)
Voltage-gated Calcium Channel, P,Q-type 2.1 (name copied from entity in Homo sapiens)
Voltage-gated Calcium Channel, L-type, 1.3 (name copied from entity in Homo sapiens)
Voltage-gated Calcium Channel, L-type 1.2 (name copied from entity in Homo sapiens)
Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies
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PLC beta1,2,3:G(q) alpha:GTP (name copied from entity in Homo sapiens)
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G(q) alpha 11,14,15,Q:G beta:G gamma (name copied from entity in Homo sapiens)
G(q) alpha:GTP (pancreatic beta cell) (name copied from entity in Homo sapiens)
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Adenylate cyclase: G-protein alpha (s): GTP Complex (name copied from entity in Homo sapiens)
G-protein alpha (s):GTP (name copied from entity in Homo sapiens)
Protein Kinase C, alpha type: DAG (name copied from entity in Homo sapiens)
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IP3-gated Ca-channel type 3 (name copied from entity in Homo sapiens)
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IP3-gated Ca-channel type 2 (name copied from entity in Homo sapiens)
ITPR1 tetramer (name copied from entity in Homo sapiens)
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IP3-gated Ca-channel type 1 (open) (name copied from entity in Homo sapiens)
SNX3 controls Wingless/Wnt secretion through regulating retromer-dependent recycling of Wntless
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IP3-gated Ca-channel type 2 (open) (name copied from entity in Homo sapiens)
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RAPGEF4:cAMP Complex (name copied from entity in Homo sapiens)
RAPGEF3:cAMP complex (name copied from entity in Homo sapiens)
Rap1-GTP (name copied from entity in Homo sapiens)
Rap1-GDP (name copied from entity in Homo sapiens)
Adenine nucleotide translocator homodimer
ADP/ATP translocase 2 homodimer (name copied from entity in Homo sapiens)
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ADP/ATP translocase 1 homodimer (name copied from entity in Homo sapiens)
Role of leptin in the pancreatic ?-cell: effects and signaling pathways
IP3-gated Ca-channel type 3 (open) (name copied from entity in Homo sapiens)
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Sensing of viral infection and activation of innate immunity by toll-like receptor 3
Mutation in the 4a-carbinolamine dehydratase gene leads to mild hyperphenylalaninemia with defective cofactor metabolism.
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Structure-Function analysis of the CTLA-4 interaction with PP2A
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Identification and partial purification of PAPS translocase
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Expression and regulation by interferon of a double-stranded-RNA-specific adenosine deaminase from human cells: evidence for two forms of the deaminase.
Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase
The FGFR4 Y367C mutant is a dominant oncogene in MDA-MB453 breast cancer cells
ChEBI:27403 3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA
Investigation of the ABC transporter MRP1 in selected patients with presumed defects in vitamin B12 absorption
Mapping of binding sites for nidogens, fibulin-2, fibronectin and heparin to different IG modules of perlecan
Mutation of the fumarase gene in two siblings with progressive encephalopathy and fumarase deficiency
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Dishevelled phosphorylation, subcellular localization and multimerization regulate its role in early embryogenesis
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Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis
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Hydroxylation of HIF-1: oxygen sensing at the molecular level
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Casein kinase I{gamma}2 down-regulates trafficking of ceramide in the synthesis of sphingomyelin
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The hippo signaling pathway in development and cancer
Regulation of TCF3 by Wnt-dependent phosphorylation during vertebrate axis specification
Degradation of cysteine and homocysteine
Comparison of the metabolism of alpha-linolenic acid and its delta 6 desaturation product, stearidonic acid, in cultured NIH-3T3 cells
Chromatin organization in the mammalian nucleus
The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro
The cellular response to neuregulins is governed by complex interactions of the erbB receptor family
Stimulation of phosphatidylglycerolphosphate phosphatase activity by unsaturated fatty acids in rat heart
A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase
Wnt signaling gradients establish planar cell polarity by inducing Vangl2 phosphorylation through Ror2
ArfGAP1 dynamics and its role in COPI coat assembly on Golgi membranes of living cells
Stat recruitment by tyrosine-phosphorylated cytokine receptors: an ordered reversible affinity-driven process
Ca2+/calmodulin-dependent protein kinase IIdelta and protein kinase D overexpression reinforce the histone deacetylase 5 redistribution in heart failure
Leukotriene A4 hydrolase in human leukocytes. Purification and properties
Mechanism of selectivity in aquaporins and aquaglyceroporins
Replication of UV-damaged DNA: new insights into links between DNA polymerases, mutagenesis and human disease.
di-retinoid-pyridinium-ethanolamine [ChEBI:71980]
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Discovery of the ergothioneine transporter
TGF-? signalling is mediated by two autonomously functioning T?RI:T?RII pairs
3,4-Hyp 5-Hyl-collagen alpha-1(XXVIII) chain
Metabolic characteristics and importance of the universal methionine salvage pathway recycling methionine from 5'-methylthioadenosine
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The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II
Homologues of 3x4Hyp-3Hyp-COL18A1(24-1754)
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Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
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Molecular basis for methionine synthase reductase deficiency in patients belonging to the cblE complementation group of disorders in folate/cobalamin metabolism
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Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1
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Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors
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Regulation of cadherin-mediated adhesion in morphogenesis
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Cloning of the sulphamidase gene and identification of mutations in Sanfilippo A syndrome
Role of the cAMP sensor Epac as a determinant of KATP channel ATP sensitivity in human pancreatic beta-cells and rat INS-1 cells
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Procollagen trafficking, processing and fibrillogenesis
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Molecular structure of the collagen triple helix
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Regulation of small GTPases at epithelial cell-cell junctions
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Fatty acid elongases in mammals: their regulation and roles in metabolism
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Structure and regulation of MAPK phosphatases
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Defective T cell differentiation in the absence of Jnk1
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Direct activation of protein kinases by unanchored polyubiquitin chains
PI and PC transport between ER and Golgi membranes
Signaling mechanisms utilized by antigen receptors and integrins: common intermediates, different outcomes?
Functionally defective high-density lipoprotein: a new therapeutic target at the crossroads of dyslipidemia, inflammation, and atherosclerosis
Phosphorylation of the CARMA1 linker controls NF-kappaB activation
Lack of collagen XV impairs peripheral nerve maturation and, when combined with laminin-411 deficiency, leads to basement membrane abnormalities and sensorimotor dysfunction
Activation of p75NTR by proBDNF facilitates hippocampal long-term depression
A novel and evolutionarily conserved PtdIns(3,4,5)P3-binding domain is necessary for DOCK180 signalling
No effects of Smad2 (madh2) null mutation on malignant progression of intestinal polyps in Apc(delta716) knockout mice
DNA double strand break repair, chromosome synapsis and transcriptional silencing in meiosis
The multiple actions of GLP-1 on the process of glucose-stimulated insulin secretion
Fcgamma receptor (FCGR) dependent phagocytosis
Unblocking of NMDA receptor, glutamate binding and activation
Components of the collagen prolyl 3-hydroxylation complex are crucial for normal bone development
Regulation of the insulin gene by glucose and fatty acids
The asymmetry of chloride transport at 38 degrees C in human red blood cell membranes
Mutation spectrum and genotype-phenotype analyses in Cowden disease and Bannayan-Zonana syndrome, two hamartoma syndromes with germline PTEN mutation
Molecular physiology and pathophysiology of electroneutral cation-chloride cotransporters
Transcriptional regulation and the role of diverse coactivators in animal cells
Healing and hurting: molecular mechanisms, functions, and pathologies of cellular senescence
Genetic disorders of mitochondrial fatty acid oxidation.
Transformation and Stat activation by derivatives of FGFR1, FGFR3, and FGFR4
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Peroxisomal straight-chain Acyl-CoA oxidase and D-bifunctional protein are essential for the retroconversion step in docosahexaenoic acid synthesis
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Biosynthesis of the linkage region of glycosaminoglycans: cloning and activity of galactosyltransferase II, the sixth member of the beta 1,3-galactosyltransferase family (beta 3GalT6)
The family of glycogen phosphorylases: structure and function
The TMEM16 protein family: a new class of chloride channels?
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Deleted in colorectal cancer binding netrin-1 mediates cell substrate adhesion and recruits Cdc42, Rac1, Pak1, and N-WASP into an intracellular signaling complex that promotes growth cone expansion
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Mitotic inhibition of GRASP65 organelle tethering involves Polo-like kinase 1 (PLK1) phosphorylation proximate to an internal PDZ ligand
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Genetic basis of hemolytic anemia caused by pyrimidine 5' nucleotidase deficiency
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Molybdenum cofactors, enzymes and pathways
Function and biogenesis of iron-sulphur proteins
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Activation of gene expression by SREBF (SREBP)
Prostaglandin and leukotriene omega-hydroxylases
Prostaglandins Other Lipid Mediat 68:345-62
Perifosine, a novel alkylphospholipid, inhibits protein kinase B activation
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Identification of the global transcriptomic response of the hypothalamic arcuate nucleus to fasting and leptin
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Serine 228 is essential for catalytic activities of 85-kDa cytosolic phospholipase A2
Constitutive activating mutation of the FGFR3b in oral squamous cell carcinomas
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Studies on the substrate specificity of a carboxyl ester hydrolase from human pancreatic juice. II. Action on cholesterol esters and lipid-soluble vitamin esters.
Studies on the substrate specificity of a carboxyl ester hydrolase from human pancreatic juice. I. Action on carboxyl esters, glycerides and phospholipids.
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cDNA cloning and chromosome mapping of human dihydropyrimidine dehydrogenase, an enzyme associated with 5-fluorouracil toxicity and congenital thymine uraciluria
Biochemical purification of a mammalian slit protein as a positive regulator of sensory axon elongation and branching
Slit proteins bind Robo receptors and have an evolutionarily conserved role in repulsive axon guidance
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ABCG5 and ABCG8 are obligate heterodimers for protein trafficking and biliary cholesterol excretion
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In vivo uptake of chylomicron [3H]retinyl ester by rat liver: evidence for retinol transfer from parenchymal to nonparenchymal cells
Proc. Natl. Acad. Sci. U.S.A. 79:7326-30
Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor
Leptin-cytokine crosstalk in breast cancer
CDK-mediated phosphorylation and removal of Cdc6
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Formation of a rate-limiting intermediate in 5S RNA gene transcription
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The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth
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Human copper-containing superoxide dismutase of high molecular weight
Nitric oxide, tetrahydrobiopterin, oxidative stress, and endothelial dysfunction in hypertension
Elongation factor Tu, a GTPase triggered by codon recognition on the ribosome: mechanism and GTP consumption
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The basis for selective E1-E2 interactions in the ISG15 conjugation system
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Two erbA homologs encoding proteins with different T3 binding capacities are transcribed from opposite DNA strands of the same genetic locus
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HSF4, a new member of the human heat shock factor family which lacks properties of a transcriptional activator
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Targeting the oncogene and kinome chaperone CDC37
CD28/CTLA-4 and CD80/CD86 families: signaling and function
Simultaneous blockade of NFkappaB, JNK, and p38 MAPK by a kinase-inactive mutant of the protein kinase TAK1 sensitizes cells to apoptosis and affects a distinct spectrum of tumor necrosis factor [corrected] target genes
The collagen substrate specificity of human neutrophil collagenase
Agrin: an extracellular matrix heparan sulfate proteoglycan involved in cell interactions and synaptogenesis
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Promoting neurotrophic effects by GPCR ligands
Novartis Found Symp 276:181-9; discussion 18
Arkadia activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation
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Presynaptic nicotinic acetylcholine receptors
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Leber congenital amaurosis: clinical correlations with genotypes, gene therapy trials update, and future directions
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Integration of DAG signaling systems mediated by PKC-dependent phosphorylation of RasGRP3
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A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene causes carbohydrate-deficient glycoprotein syndrome type-Ic
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Keratan sulfate: structure, biosynthesis, and function
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benzo[a]pyrene diol epoxide I [ChEBI:30614]
(+/-)-Benzo(a)pyrene-7,8-diol-9,10-epoxide, anti-
SUMOylation and deSUMOylation at a glance
Mechanisms of Cables 1 gene inactivation in human ovarian cancer development
Human and rat peroxisome proliferator activated receptors (PPARs) demonstrate similar tissue distribution but different responsiveness to PPAR activators
Identification of novel phosphorylation sites required for activation of MAPKAP kinase-2
Protein kinase C theta is expressed in mast cells and is functionally involved in Fcepsilon receptor I signaling
The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase
Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPs
Molecular cloning and expression of the gene for a human D1 dopamine receptor
Rapid and reversible relocalization of heat shock factor 1 within seconds to nuclear stress granules
Proc. Natl. Acad. Sci. U.S.A. 96:6769-74
Structural basis for inhibition of the epidermal growth factor receptor by cetuximab
Bone morphogenetic protein-1 (BMP-1) mediates C-terminal processing of procollagen V homotrimer
Mechanisms of monocyte recruitment in vascular repair after injury
SIRP-alpha-CD47 system functions as an intercellular signal in the renal glomerulus
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Expression and characterization of recombinant human and rat liver 6-pyruvoyl tetrahydropterin synthase. Modified cysteine residues inhibit the enzyme activity
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New insights into the mechanism of Wnt signaling pathway activation
Perilipin A is essential for the translocation of hormone-sensitive lipase during lipolytic activation
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Role of the SCFSkp2 ubiquitin ligase in the degradation of p21Cip1 in S phase
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Molecular basis of hepatic carnitine palmitoyltransferase I deficiency
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Mutations in the liver glycogen synthase gene in children with hypoglycemia due to glycogen storage disease type 0
A "slow" homotetrameric kinesin-related motor protein purified from Drosophila embryos
Interactions of active-site residues and catalytic activity of human carbonic anhydrase III
Identification of a mammalian H(+)-myo-inositol symporter expressed predominantly in the brain
Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry
Neutral amino acid transporter ASCT2 displays substrate-induced Na+ exchange and a substrate-gated anion conductance
Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding
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MOZ and MORF, two large MYSTic HATs in normal and cancer stem cells
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The PI3K-PDK1 connection: more than just a road to PKB
Purification, cDNA cloning and heterologous expression of human phosphomannose isomerase
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Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin
Proc. Natl. Acad. Sci. U.S.A. 102:8501-6
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Involvement of fibroblast growth factor receptor 2 isoform switching in mammary oncogenesis
Cloning of a human type II phosphatidylinositol 4-kinase reveals a novel lipid kinase family
Calcium release-activated calcium channel protein 1
Phosphorylated RasGRP1 and phosphorylated RasGRP3
Molecular cloning and characterization of a novel (Na+,K+)/H+ exchanger localized to the trans-Golgi network
CHIR-258, a novel, multitargeted tyrosine kinase inhibitor for the potential treatment of t(4;14) multiple myeloma
Band 3 Memphis variant II. Altered stilbene disulfonate binding and the Diego (Dia) blood group antigen are associated with the human erythrocyte band 3 mutation Pro854-->Leu
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Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules
Prolyl hydroxylase PHD3 activates oxygen-dependent protein aggregation
Cloning, Golgi localization, and enzyme activity of the full-length heparin/heparan sulfate-glucuronic acid C5-epimerase
Ryk: a novel Wnt receptor regulating axon pathfinding
Bartter's syndrome, hypokalaemic alkalosis with hypercalciuria, is caused by mutations in the Na-K-2Cl cotransporter NKCC2
The fourth immunoglobulin-like domain of NCAM contains a carbohydrate recognition domain for oligomannosidic glycans implicated in association with L1 and neurite outgrowth
Antigen processing: Ubiquitination & Proteasome degradation
Identification of the nuclear factor HMG2 as an activator for DFF nuclease activity
Cholesterol sulfate in human physiology: what's it all about?
Gustin from human parotid saliva is carbonic anhydrase VI
FGFR3 as a therapeutic target of the small molecule inhibitor PKC412 in hematopoietic malignancies
A dominant negative mutation of transforming growth factor-beta receptor type II gene in microsatellite stable oesophageal carcinoma
Purification and properties of steroid sulfatase from human placenta
PIG-B, a membrane protein of the endoplasmic reticulum with a large lumenal domain, is involved in transferring the third mannose of the GPI anchor
Cloning, expression, and properties of the regulatory subunit of bovine pyruvate dehydrogenase phosphatase
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Dynamics of the full length and mutated heat shock factor 1 in human cells
Functional dissection of eukaryotic initiation factor 4F: the 4A subunit and the central domain of the 4G subunit are sufficient to mediate internal entry of 43S preinitiation complexes.
Graded activation of fibroblast growth factor receptor 3 by mutations causing achondroplasia and thanatophoric dysplasia
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Protein kinase G dynamically modulates TASK1-mediated leak K+ currents in cholinergic neurons of the basal forebrain
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Role for NudC, a dynein-associated nuclear movement protein, in mitosis and cytokinesis
Interaction of the Ski oncoprotein with Smad3 regulates TGF-beta signaling
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Sema4D induced cell migration and growth-cone collapse
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Expression of the HsOrc1 gene, a human ORC1 homolog, is regulated by cell proliferation via the E2F transcription factor
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Substrate binding is the rate-limiting step in thromboxane synthase catalysis
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The WIF domain of the human and Drosophila Wif-1 secreted factors confers specificity for Wnt or Hedgehog
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Heregulin-dependent delay in mitotic progression requires HER4 and BRCA1
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Molecular Mechanisms of Phagocytosis (Book): 97-116
From molecular action to physiological outputs: peroxisome proliferator-activated receptors are nuclear receptors at the crossroads of key cellular functions
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Activation of the AP-1 family of transcription factors
Molecular analysis of the epidermal growth factor-like short consensus repeat domain-mediated protein-protein interactions: dissection of the CD97-CD55 complex
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Functional requirements for the lysosomal thiol reductase GILT in MHC class II-restricted antigen processing
Synergy between Ca2+ and protein kinase C is the major factor in determining the level of secretion from human platelets
Myotubularin phosphatases: policing 3-phosphoinositides
Mammalian cells express two VPS4 proteins both of which are involved in intracellular protein trafficking
Overview of retinoid metabolism and function
Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase
Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core
Identification of OCT6 as a novel organic cation transporter preferentially expressed in hematopoietic cells and leukemias
Regulation of human cystathionine beta-synthase by S-adenosyl-L-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region
Identification of tyrosine phosphorylation sites in human Gab-1 protein by EGF receptor kinase in vitro
Expression cloning of a novel scavenger receptor from human endothelial cells
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Asparagine-proline sequence within membrane-spanning segment of SREBP triggers intramembrane cleavage by site-2 protease
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Localization of human Cdc25C is regulated both by nuclear export and 14-3-3 protein binding.
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Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors
G(z) signaling: emerging divergence from G(i) signaling
p38 and extracellular signal-regulated kinases regulate the myogenic program at multiple steps
Haploid loss of the tumor suppressor Smad4/Dpc4 initiates gastric polyposis and cancer in mice
RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?
Abortive initiation by RNA polymerase II in vitro at the adenovirus 2 major late promoter.
Can type VII collagen injections cure dystrophic epidermolysis bullosa?
Human serotonin 1D receptor is encoded by a subfamily of two distinct genes: 5-HT1D alpha and 5-HT1D beta
cDNA cloning of the human retinal rod Na-Ca + K exchanger: comparison with a revised bovine sequence
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Mechanisms of inhibition of insulin release
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Cell-free synthesis of procollagen: L-929 fibroblasts as a cellular model for dermatosparaxis
Proc. Natl. Acad. Sci. U.S.A. 70:1378-82
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The monocytic leukemia zinc finger protein MOZ is a histone acetyltransferase
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7alpha,12alpha-Dihydroxy-5beta-cholestan-3-one [ChEBI:2288]
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Cloning, expression, and characterization of a human 4'-phosphopantetheinyl transferase with broad substrate specificity
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Tyrosine-protein kinase transmembrane receptor ROR2 precursor
Fyn associates with Cbl and phosphorylates tyrosine 731 in Cbl, a binding site for phosphatidylinositol 3-kinase
Plasma membrane adaptor AP-2 50 kDa protein
7alpha-Hydroxy-5beta-cholestan-3-one [ChEBI:2290]
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Adapter-related protein complex 2 beta 1 subunit
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Adaptor protein complex AP-2 alpha-2 subunit
Adaptor protein complex AP-2 alpha-1 subunit
Tyrosine phosphorylation of Sprouty2 enhances its interaction with c-Cbl and is crucial for its function
Plasma membrane adaptor AP-2 17 kDa protein
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Regulation of intracellular localization and transcriptional activity of FOXO4 by protein kinase B through phosphorylation at the motif sites conserved among the FOXO family
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S-adenosylmethionine: nothing goes to waste
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Identification of the gene responsible for Best macular dystrophy
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Biochemical properties of human pantothenate kinase 2 isoforms and mutations linked to pantothenate kinase-associated neurodegeneration
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Kinetic mechanism of AKT/PKB enzyme family
Normal T-cell development and immune functions in TRIM-deficient mice
Cross-presentation: avoiding trafficking chaos?
Rho guanine nucleotide exchange factor 1 (p115-RhoGEF)
PRAK, a novel protein kinase regulated by the p38 MAP kinase
Guanine nucleotide-binding protein, alpha-12 subunit
Occurrence of surface IgM, IgD, and free light chains of human lymphocytes
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Guanine nucleotide-binding protein G alpha (o)
Calcineurin, testis-specific catalytic subunit
Calmodulin-dependent calcineurin A subunit, gamma isoform
Serine/threonine protein phosphatase 2B catalytic subunit, gamma isoform
Serine/threonine protein phosphatase 2B catalytic subunit, alpha isoform
Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
Functional characterization and mutation analysis of human ATP:Cob(I)alamin adenosyltransferase
Characterization of rhoGAP. A GTPase-activating protein for rho-related small GTPases.
S-adenosylmethionine synthesis: molecular mechanisms and clinical implications
Metabolism of alpha-linolenic acid in humans
Prostaglandins Leukot Essent Fatty Acids 75:161-8
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Identification of galectin-3 as a high-affinity binding protein for advanced glycation end products (AGE): a new member of the AGE-receptor complex
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Function of eukaryotic initiation factor 5 in the formation of an 80 S ribosomal polypeptide chain initiation complex.
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_90571.4
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Effect of TBCD and its regulatory interactor Arl2 on tubulin and microtubule integrity
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XTRPC1-dependent chemotropic guidance of neuronal growth cones
DCC regulates cell adhesion in human colon cancer derived HT-29 cells and associates with ezrin
Altered aquaporin 9 expression and localization in human hepatocellular carcinoma
Protein phosphatase 3 regulatory subunit B alpha isoform 1
Protein phosphatase 2B regulatory subunit 1
Myotubularin regulates the function of the late endosome through the gram domain-phosphatidylinositol 3,5-bisphosphate interaction
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Skp2-mediated degradation of p27 regulates progression into mitosis
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Molecular cloning, expression, and chromosomal localization of a human brain-specific Na(+)-dependent inorganic phosphate cotransporter
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MCD4 encodes a conserved endoplasmic reticulum membrane protein essential for glycosylphosphatidylinositol anchor synthesis in yeast
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Synthesis of (Pro-Hyp-Gly) n of defined molecular weights. Evidence for the stabilization of collagen triple helix by hydroxypyroline
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Cooperation of translocase complexes in mitochondrial protein import
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641038
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641037
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Activation of peripheral NMDA receptors contributes to human pain and rat afferent discharges evoked by injection of glutamate into the masseter muscle
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Four Na+/H+ exchanger isoforms are distributed to Golgi and post-Golgi compartments and are involved in organelle pH regulation
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5641851
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Amyloid beta A4 precursor protein-binding family B member 1- interacting protein
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Signal transduction induced by opioids in immune cells: a review
Silencing of TGF-beta signalling by the pseudoreceptor BAMBI
Profound ligand-independent kinase activation of fibroblast growth factor receptor 3 by the activation loop mutation responsible for a lethal skeletal dysplasia, thanatophoric dysplasia type II
DNA polymerase alpha:primase (name copied from entity in Homo sapiens)
E2F1:TFDP1 (name copied from entity in Homo sapiens)
DNA polymerase epsilon (name copied from entity in Homo sapiens)
DNA polymerase epsilon:origin complex (name copied from entity in Homo sapiens)
RNA primer-DNA primer:origin duplex (name copied from entity in Homo sapiens)
DNA polymerase alpha:primase:DNA polymerase alpha:origin complex (name copied from entity in Homo sapiens)
RNA primer-DNA primer:origin duplex with DNA damage (name copied from entity in Homo sapiens)
RNA primer:origin duplex:DNA polymerase alpha:primase complex (name copied from entity in Homo sapiens)
CAK (name copied from entity in Homo sapiens)
RFC Heteropentamer:RNA primer-DNA primer:origin duplex (name copied from entity in Homo sapiens)
RFC Heteropentamer (name copied from entity in Homo sapiens)
Unwinding complex at replication fork (name copied from entity in Homo sapiens)
GINS complex (name copied from entity in Homo sapiens)
Mcm4,6,7 complex (name copied from entity in Homo sapiens)
Mcm2-7 complex (name copied from entity in Homo sapiens)
ubiquitinated Cdc6 (name copied from entity in Homo sapiens)
CDK (name copied from entity in Homo sapiens)
ubiquitinated Orc1 (name copied from entity in Homo sapiens)
Cyclin B:Cdk1 complex (name copied from entity in Homo sapiens)
Cyclin B1:phospho-Cdc2 ( Thr 14) (name copied from entity in Homo sapiens)
Cyclin B1:phospho-Cdc2(Thr 161, Thr 14, Tyr 15) (name copied from entity in Homo sapiens)
phospho(T286)-Cyclin D1:Cdk4 (name copied from entity in Homo sapiens)
Cyclin D1:Cdk4 (name copied from entity in Homo sapiens)
multi-ubiquitinated phospho-(T286) Cyclin D1 (name copied from entity in Homo sapiens)
PCNA homotrimer (name copied from entity in Homo sapiens)
RNA primer-DNA primer:origin duplex:PCNA (name copied from entity in Homo sapiens)
RFC Heteropentamer:RNA primer-DNA primer:origin duplex:PCNA homotrimer (name copied from entity in Homo sapiens)
Identification of a switch in neurotrophin signaling by selective tyrosine phosphorylation
CCNB1:p-T14-CDK1 (name copied from entity in Homo sapiens)
CCNB1:p-T14,Y15,T161-CDK1 (name copied from entity in Homo sapiens)
phospho-cyclin B1(CRS):phosph-Cdc2(Thr 161) (name copied from entity in Homo sapiens)
CCNB1:p-T161-CDK1 (name copied from entity in Homo sapiens)
p-4S-CCNB1:p-T161-CDK1 (name copied from entity in Homo sapiens)
CCNB1:p-T14,T161-CDK1 (name copied from entity in Homo sapiens)
Cyclin B2:phospho-Cdc2(Thr 14, Thr 161) (name copied from entity in Homo sapiens)
CCNB2:p-T161-CDK1 (name copied from entity in Homo sapiens)
Phosphorylated Myosin Phosphatase (name copied from entity in Homo sapiens)
p-T216,S274,S373-GORASP1:p-S37-GOLGA2:p-RAB1:GTP:PLK1 (name copied from entity in Homo sapiens)
p-T216,S274,S373-GORASP1:p-S37-GOLGA2:p-RAB1:GTP (name copied from entity in Homo sapiens)
p-RAB1:GTP (name copied from entity in Homo sapiens)
p-T216,S189,S274,S373-GORASP1:p-S37-GOLGA2:p-RAB1:GTP:PLK1 (name copied from entity in Homo sapiens)
GORASP2:BLZF1:RAB2A:GTP (name copied from entity in Homo sapiens)
RAB2A:GTP (name copied from entity in Homo sapiens)
p-T222,225-GORASP2:BLZF1:RAB2A:GTP (name copied from entity in Homo sapiens)
p-Y204-MAPK3-3/p-T185,Y187-MAPK1 homodimer
Hepatitis C virus induces epithelial-mesenchymal transition in primary human hepatocytes
p-3S,2T-NEK9 (name copied from entity in Homo sapiens)
p-T333-NEK9 (name copied from entity in Homo sapiens)
p-3S,T-NEK9 (name copied from entity in Homo sapiens)
p-Y204-MAPK3-3 homodimer (name copied from entity in Homo sapiens)
phospho-ERK-2 dimer (name copied from entity in Homo sapiens)
CTDNEP1:CNEP1R1 (name copied from entity in Homo sapiens)
DAG:active PKC:Ca+2 (name copied from entity in Homo sapiens)
p-3S,2T-NEK9:NEK6/NEK7 (name copied from entity in Homo sapiens)
p-3S,2T-NEK9: p-S206-NEK6/ p-S195-NEK7 (name copied from entity in Homo sapiens)
Sister Chromosomal Arms:p-STAG2,RAD21-Ac-Cohesin:PDS5:p-CDCA5:WAPAL (name copied from entity in Homo sapiens)
p-STAG2,RAD21-Ac-Cohesin:PDS5:p-CDCA5:WAPAL (name copied from entity in Homo sapiens)
p-STAG2,RAD21-Ac-Cohesin (name copied from entity in Homo sapiens)
ESPL1 Autocleaved (name copied from entity in Homo sapiens)
Sister Chromosomal Arms:Ac-Cohesin:PDS5:p-CDCA5:WAPAL (name copied from entity in Homo sapiens)
Ac-Cohesin:PDS5:p-CDCA5:WAPAL (name copied from entity in Homo sapiens)
Ac-Cohesin Complex (name copied from entity in Homo sapiens)
ANKLE2:VRK1/VRK2 (name copied from entity in Homo sapiens)
p-T2,T3,S4-BANF1 (name copied from entity in Homo sapiens)
BANF1 (name copied from entity in Homo sapiens)
DNA polymerase alpha:primase:DNA polymerase alpha:G-strand extended telomere end (name copied from entity in Homo sapiens)
V-ATPase (name copied from entity in Homo sapiens)
SPO11:double stand break (name copied from entity in Homo sapiens)
SPO11 Dimer (name copied from entity in Homo sapiens)
RNA primer-DNA primer:G-strand extended telomere:PCNA (name copied from entity in Homo sapiens)
RFC Heteropentamer:RNA primer-DNA primer:G-strand extended telomere end duplex:PCNA homotrimer (name copied from entity in Homo sapiens)
RFC Heteropentamer:RNA primer-DNA primer:G-strand extended telomere end (name copied from entity in Homo sapiens)
RNA primer-DNA primer:G-strand extended telomere (name copied from entity in Homo sapiens)
RNA primer:G-strand extended telomere end:DNA polymerase alpha:primase complex (name copied from entity in Homo sapiens)
DNA polymerase epsilon:G-strand extended telomere end (name copied from entity in Homo sapiens)
SCF-associated multiubiquitinated Emi1complexes (name copied from entity in Homo sapiens)
Nephrin--a unique structural and signaling protein of the kidney filter
SCF-beta-TrCP1 complex (name copied from entity in Homo sapiens)
Cohesin:PDS5:WAPAL:NIPBL:MAU2:Centromere (name copied from entity in Homo sapiens)
SCF-beta-TrCP:phospho-Emi1 complexes (name copied from entity in Homo sapiens)
Cohesin:PDS5:WAPAL:NIPBL:MAU2:Chromosomal Arm (name copied from entity in Homo sapiens)
Cohesin Complex (name copied from entity in Homo sapiens)
PP2A (Aalpha:B55alpha:Calpha) (name copied from entity in Homo sapiens)
NIPBL:MAU2 (name copied from entity in Homo sapiens)
Cohesin:PDS5:WAPAL (name copied from entity in Homo sapiens)
RED2, a brain-specific member of the RNA-specific adenosine deaminase family.
ATP6V1 (name copied from entity in Homo sapiens)
ATP6V1B trimer (name copied from entity in Homo sapiens)
ATP6V1A trimer (name copied from entity in Homo sapiens)
ATP6V1G dimer (name copied from entity in Homo sapiens)
ATP6V0C hexamer (name copied from entity in Homo sapiens)
Direct proteasome-independent cross-presentation of viral antigen by plasmacytoid dendritic cells on major histocompatibility complex class I
ATP6V0 (name copied from entity in Homo sapiens)
ATP6V0A (name copied from entity in Homo sapiens)
ATP6V0D (name copied from entity in Homo sapiens)
ADAM:Zn2+ (name copied from entity in Homo sapiens)
ATP6V0E (name copied from entity in Homo sapiens)
Organization and sequence of the gene for the human mitochondrial dicarboxylate carrier: evolution of the carrier family
Mutation of BSND causes Bartter syndrome with sensorineural deafness and kidney failure
Collagen fibrillogenesis in tendon development: current models and regulation of fibril assembly
Birth Defects Res. C Embryo Today 84:228-44
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_247581.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_255738.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_243128.1
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Molecular mechanisms of the decision between life and death: regulation of apoptosis by apoptosis signal-regulating kinase 1
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PTEN restoration and PIK3CB knockdown synergistically suppress glioblastoma growth in vitro and in xenografts
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_259140.1
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5647666
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_256605.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_197715.3
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_252789.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_232470.1
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Troponin C, slow skeletal and cardiac muscles
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_256179.1
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A telomeric sequence in the RNA of Tetrahymena telomerase required for telomere repeat synthesis
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_234111.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20947.2
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638612
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_239399.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_225239.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=162768
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5638609
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4171.2
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EGF:p-6Y-EGFR:p-Y371-CBL (name copied from entity in Homo sapiens)
EGF:p-6Y-EGFR:CBL (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652524
EGF:p-5Y-EGFR:GRB2:p-5Y-GAB1:SHP2 (name copied from entity in Homo sapiens)
EGF:p-6Y-EGFR:GRB2:p-5Y-GAB1:SHP2 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624650
EGF:Phospho-EGFR (- Y992) (name copied from entity in Homo sapiens)
EGF:Phospho-EGFR (-Y992) dimer (name copied from entity in Homo sapiens)
PHLPP (Mn2+ cofactor) (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=162856
PTEN:Mg2+ (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4602.2
EGF:p-6Y-EGFR:GRB2:GAB1 (name copied from entity in Homo sapiens)
PDPK1:PIP2 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624648
Glucose transporter isoforms GLUT1 and GLUT3 transport dehydroascorbic acid
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_238453.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3639.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=30158
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619821
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=162793
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619823
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624653
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_262593.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_249814.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=175992
p-S-AKT:PDPK1:PIP3 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624651
AKT:PIP3:THEM4/TRIB3 (name copied from entity in Homo sapiens)
TORC2 complex (name copied from entity in Homo sapiens)
p-S-AKT:PIP3 (name copied from entity in Homo sapiens)
PDPK1:PIP3 (name copied from entity in Homo sapiens)
AKT:PIP3 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=162777
PIK3R1:p-ERBB4cyt1 (name copied from entity in Homo sapiens)
PI3K:p-ERBB4cyt1 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=162803
Cloning, tissue distribution, and intrarenal localization of ClC chloride channels in human kidney
EGF:p-6Y-EGFR:p-6Y-ERBB2 (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3657.3
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3849.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_244004.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619832
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4347.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113556
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_230458.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619830
EGF:p-EGFR:p-ERBB2:GRB2:GAB1:PI3K (name copied from entity in Homo sapiens)
beta-NGF homodimer (name copied from entity in Homo sapiens)
EGF:p-EGFR:p-ERBB2:GRB2:GAB1 (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2701.2
EGF:p-EGFR:p-ERBB2:GRB2:GAB1:PIK3R1 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=162843
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21673.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2468.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624658
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=508531
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624660
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624661
Activated FGFR:p-FRS2alpha:p-SHP2:GRB2:GAB1:PI3KR1 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624663
Activated FGFR:p-FRS2alpha:p-SHP2:GRB2:GAB1:PI3K (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_235755.1
PI3K:p-KIT:sSCF dimer:p-KIT (name copied from entity in Homo sapiens)
Activated FGFR:p-FRS2-alpha:p-SHP2 (name copied from entity in Homo sapiens)
p-7Y-KIT:sSCF dimer:p-7Y-KIT (name copied from entity in Homo sapiens)
PI3K alpha (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3737.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29444
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=30176
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_243412.1
Activated FGFR3c homodimer (name copied from entity in Homo sapiens)
Activated FGFR3b homodimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=162681
Activated FGFR2c short homodimer bound to FGF (name copied from entity in Homo sapiens)
Activated FGFR2c long homodimer (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3229.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=162872
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3693.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619827
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5855.4
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619828
Activated FGFR4 homodimer (name copied from entity in Homo sapiens)
Activated FGFR1c homodimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624664
Activated FGFR2b short homodimer bound to FGF (name copied from entity in Homo sapiens)
Porphyrin accumulation in mitochondria is mediated by 2-oxoglutarate carrier
Activated FGFR2b long homodimer (name copied from entity in Homo sapiens)
Molecular cloning and functional characterization of a human 5-HT1B serotonin receptor: a homologue of the rat 5-HT1B receptor with 5-HT1D-like pharmacological specificity
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629137
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629138
EGF:p-6Y-EGFR:p-Y349,350-SHC1:GRB2:SOS1 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=204628
EGF:p-6Y-EGFR:GRB2:GAB1:PIK3R1 (name copied from entity in Homo sapiens)
GRB2:Phospho-GAB1 (name copied from entity in Homo sapiens)
EGF:p-6Y-EGFR:GRB2:GAB1:PIK3 (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_12734.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629124
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629123
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629126
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629125
Activated FGFR:p-FRS2alpha (name copied from entity in Homo sapiens)
Activated FGFR1b homodimer (name copied from entity in Homo sapiens)
Activated FGFR:p-FRS2alpha:GRB2:GAB1:PI3K (name copied from entity in Homo sapiens)
Activated FGFR:p-FRS2alpha:GRB2:GAB1:PI3KR1 (name copied from entity in Homo sapiens)
GRB2:GAB1:PIK3R1 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629148
MEK1:ERK-1 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629147
phospho-ERK-1:MEK1 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629146
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629145
Activated RAF1 complex:MEK2 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629143
Neuron-glia cell adhesion molecule interacts with neurons and astroglia via different binding mechanisms
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_195406.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629140
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_195417.3
EGF:p-6Y-EGFR:p-Y349,350-SHC1 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629141
Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1
EGF:p-6Y-EGFR:SHC1 (name copied from entity in Homo sapiens)
MEK2:ERK-2 (name copied from entity in Homo sapiens)
phospho-ERK-2:MEK2 (name copied from entity in Homo sapiens)
phospho-ERK-1 dimer (name copied from entity in Homo sapiens)
active PKC (alpha, gamma, delta) (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629154
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629157
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629155
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653085
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_195390.3
GRB2:SOS1 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653086
EGF:p-6Y-EGFR:GRB2:SOS1 (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_183782.3
p21 RAS:GDP (name copied from entity in Homo sapiens)
p21 RAS:GTP (name copied from entity in Homo sapiens)
p-Raf1(S259,S621):14-3-3 protein beta/alpha (name copied from entity in Homo sapiens)
RAS:RAF (name copied from entity in Homo sapiens)
RAS:RAF:14-3-3 (name copied from entity in Homo sapiens)
Activated RAF1 complex (name copied from entity in Homo sapiens)
Activated RAF1 complex:MEK (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629150
Metabolism of carcinogenic heterocyclic and aromatic amines by recombinant human cytochrome P450 enzymes
Activated RAF1 complex:MEK1 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629149
Adenylate cyclase (Mg2+ cofactor) (name copied from entity in Homo sapiens)
4xCa2+:CaM (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2861.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=162839
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4739.2
PKA tetramer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624676
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5624674
Cam-PDE 1A homodimer (name copied from entity in Homo sapiens)
cAMP:PKA regulatory subunit (name copied from entity in Homo sapiens)
phospho-CREB dimer (name copied from entity in Homo sapiens)
active Cam-PDE 1 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=162341
GRK2:calmodulin (name copied from entity in Homo sapiens)
Cam-PDE 1B homodimer (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_183784.3
Cam-PDE 1C homodimer (name copied from entity in Homo sapiens)
IP3 receptor:IP3 complex (name copied from entity in Homo sapiens)
IP3 receptor homotetramer (name copied from entity in Homo sapiens)
EGF:p-6Y-EGFR:p-Y472,771,783,1254-PLCG1 (name copied from entity in Homo sapiens)
EGF:p-6Y-EGFR:PLCG1 (name copied from entity in Homo sapiens)
EGF:Phospho-EGFR (name copied from entity in Homo sapiens)
EGF:p-6Y-EGFR (name copied from entity in Homo sapiens)
EGF:EGFR dimer (name copied from entity in Homo sapiens)
EGF:EGFR (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620015
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620018
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620016
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636777
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_263019.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_206460.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3119.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=30337
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=71160
Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620001
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620000
Syndecans in wound healing, inflammation and vascular biology
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_217747.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=31365
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_250567.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620003
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2627.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629128
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629129
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629130
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629131
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629132
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629133
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629121
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629116
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5629122
Structure of human adenosine kinase at 1.5 A resolution.
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=71045
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630611
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5630613
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_216630.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=70955
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2558.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619979
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_179901.3
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2814.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=70951
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619837
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619839
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619836
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113577
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5045.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_246086.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620007
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620008
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620010
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=71129
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4011.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_25923.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637656
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_201932.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=893599
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652525
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_256071.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_238922.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619983
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619984
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3284.1
The vitelliform macular dystrophy protein defines a new family of chloride channels
Proc. Natl. Acad. Sci. U.S.A. 99:4008-13
Identification of the substrate binding region of vesicular monoamine transporter-2 (VMAT-2) using iodoaminoflisopolol as a novel photoprobe
Hormone-sensitive lipase: control of intracellular tri-(di-)acylglycerol and cholesteryl ester hydrolysis
Atomic structure of GTP cyclohydrolase I
Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors
The angiopoietins and Tie2/Tek: adding to the complexity of cardiovascular development
SCF-beta-TrCP mediated degradation of Emi1
Regulatory Mechanisms of Striated Muscle Contraction
Advances in Experimental Medicine and Biology 592:
Rac1-mediated endocytosis during ephrin-A2- and semaphorin 3A-induced growth cone collapse
Human Mcm proteins at a replication origin during the G1 to S phase transition.
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632322
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_203249.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632329
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_207468.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_203865.2
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Mice with a homozygous deletion of the Mgat2 gene encoding UDP-N-acetylglucosamine:alpha-6-D-mannoside beta1,2-N-acetylglucosaminyltransferase II: a model for congenital disorder of glycosylation type IIa
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_220915.2
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632371
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632316
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632311
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632315
Phospho-CBL:GRB2 (name copied from entity in Homo sapiens)
CDC42:GTP (name copied from entity in Homo sapiens)
CBL:Beta-Pix (name copied from entity in Homo sapiens)
CBL:Beta-Pix:CDC42:GTP (name copied from entity in Homo sapiens)
CBL:GRB2 (name copied from entity in Homo sapiens)
EGF:p-6Y-EGFR:CBL:GRB2 (name copied from entity in Homo sapiens)
EGF:p-6Y-EGFR:p-Y371-CBL:GRB2 (name copied from entity in Homo sapiens)
EGF:Ub-p-6Y-EGFR:p-Y371-CBL:GRB2 (name copied from entity in Homo sapiens)
EGF:p-6Y-EGFR:CBL:CIN85 (name copied from entity in Homo sapiens)
EGF:Ub-p-6Y-EGFR:p-Y371-CBL (name copied from entity in Homo sapiens)
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_262808.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_182973.3
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_177234.3
Which DNA polymerases are used for DNA-repair in eukaryotes?
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4798.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=70799
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_211278.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636764
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_255193.1
Activated FGFR:p-FRS2:SHP2 (name copied from entity in Homo sapiens)
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Activated FGFR:p-FRS2:GRB2:SOS1 (name copied from entity in Homo sapiens)
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Activated FGFR:p-FRS2:p-SHP2 (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_174247.3
Activated FGFR bound to activated PLC gamma (name copied from entity in Homo sapiens)
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Activated FGFR bound to PLC gamma (name copied from entity in Homo sapiens)
Activated FGFR:p-SHC1 (name copied from entity in Homo sapiens)
Activated FGFR:SHC1 (name copied from entity in Homo sapiens)
Activated FGFR:p-SHC1:GRB2:SOS1 (name copied from entity in Homo sapiens)
Activated FGFR:p-FRS2alpha:p-CBL:GRB2 (name copied from entity in Homo sapiens)
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_259631.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619738
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653170
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_244138.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619734
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653163
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619715
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619713
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29896
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_250412.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619712
FGFR3c homodimer bound to FGF (name copied from entity in Homo sapiens)
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FGFR3b homodimer (name copied from entity in Homo sapiens)
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632328
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632340
Activated FGFR:FRS2alpha (name copied from entity in Homo sapiens)
FGFR4 homodimer (name copied from entity in Homo sapiens)
FGFR4 homodimer bound to FGF (name copied from entity in Homo sapiens)
FGFR3c homodimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619730
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_182963.3
Activated FGFR:p-FRS2beta (name copied from entity in Homo sapiens)
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Cellular glutathione peroxidase as a predominant scavenger of hydroperoxyeicosatetraenoic acids in rabbit alveolar macrophages
Activated FGFR:pThr-FRS2alpha (name copied from entity in Homo sapiens)
Activated FGFR:FRS2beta (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2670.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632327
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632323
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=70772
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_249994.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3130.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_246025.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632305
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632306
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632302
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632309
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632303
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632310
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_257170.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653167
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_233273.1
Overexpressed FGFR1:TKIs (name copied from entity in Homo sapiens)
Activated overexpressed FGFR1c homodimer (name copied from entity in Homo sapiens)
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Activated overexpressed FGFR1 homodimers
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632445
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632446
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_255599.1
Ub-Activated FGFR complex:Ub-p-FRS2alpha (name copied from entity in Homo sapiens)
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_177186.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653162
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632307
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632308
CUX1-FGFR1 fusion mutant dimer (name copied from entity in Homo sapiens)
p-EGFR mutants:p-Y472,771,783,1254-PLCG1 (name copied from entity in Homo sapiens)
Ligand-responsive p-6Y-EGFR mutants:CBL (name copied from entity in Homo sapiens)
Ligand-responsive p-6Y-EGFR mutants:p-Y371-CBL (name copied from entity in Homo sapiens)
Ligand-responsive Ub-p-6Y-EGFR mutants:p-Y371-CBL (name copied from entity in Homo sapiens)
HSP90:Benzoquinoid ansamycins (name copied from entity in Homo sapiens)
Sensitive ligand-responsive EGFR mutants:Non-covalent EGFR TKIs (name copied from entity in Homo sapiens)
Active dimers of ligand-responsive EGFR mutants sensitive to non-covalent TKIs
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632268
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632277
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632250
p-EGFR mutants:GRB2:GAB1:PIK3R1 (name copied from entity in Homo sapiens)
p-EGFR mutants:GRB2:GAB1:PI3K (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632262
p-EGFR mutants:PLCG1 (name copied from entity in Homo sapiens)
Ligand-responsive p-6Y-EGFR mutants:HSP90:CDC37
p-5Y-EGFRvIII mutant dimer (name copied from entity in Homo sapiens)
Phospho-EGFRvIIImut:HSP90:CDC37 (name copied from entity in Homo sapiens)
EGFRvIII mutant:HSP90:CDC37 (name copied from entity in Homo sapiens)
EGFRvIII mutant dimer (name copied from entity in Homo sapiens)
p-EGFR mutants:p-Y349,350-SHC1 (name copied from entity in Homo sapiens)
p-EGFR mutants:p-Y349,350-SHC1:GRB2:SOS1 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632273
p-EGFR mutants:GRB2:SOS1 (name copied from entity in Homo sapiens)
p-EGFR mutants:SHC1 (name copied from entity in Homo sapiens)
Two distinct pathways remove mammalian cohesin from chromosome arms in prophase and from centromeres in anaphase
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632258
Ligand-responsive p-6Y-EGFR mutants resistant to non-covalent TKIs:HSP90:CDC37 (name copied from entity in Homo sapiens)
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Ligand-responsive p-6Y-EGFR mutants sensitive to non-covalent TKIs:HSP90:CDC37 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632369
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632304
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632254
Compound disruption of smad2 accelerates malignant progression of intestinal tumors in apc knockout mice
FGFR3b homodimer bound to FGF (name copied from entity in Homo sapiens)
Functional complexes between YAP2 and ZO-2 are PDZ domain-dependent, and regulate YAP2 nuclear localization and signalling
FGFR2c long homodimer bound to FGF (name copied from entity in Homo sapiens)
FGFR2c long homodimer (name copied from entity in Homo sapiens)
FGFR2c short homodimer bound to FGF (name copied from entity in Homo sapiens)
The human glycine receptor beta subunit: primary structure, functional characterisation and chromosomal localisation of the human and murine genes
FGFR2c short homodimer (name copied from entity in Homo sapiens)
FGFR2b long homodimer bound to FGF (name copied from entity in Homo sapiens)
FGFR2b short homodimer bound to FGF (name copied from entity in Homo sapiens)
FGFR2b short homodimer (name copied from entity in Homo sapiens)
CD28-mediated co-stimulation: a quantitative support for TCR signalling
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Novel D761Y and common secondary T790M mutations in epidermal growth factor receptor-mutant lung adenocarcinomas with acquired resistance to kinase inhibitors
Synthesis of 12-eicosatetraenoic acid derivatives
FGFR1c homodimer bound to FGF (name copied from entity in Homo sapiens)
FGFR1c homodimer (name copied from entity in Homo sapiens)
EGF:EGFR Dimer:Covalent EGFR TKIs (name copied from entity in Homo sapiens)
FGFR1b homodimer bound to FGF (name copied from entity in Homo sapiens)
Dimers of ligand-responsive EGFR mutants resistant to non-covalent TKIs (name copied from entity in Homo sapiens)
Editing of glutamate receptor B subunit ion channel RNAs by four alternatively spliced DRADA2 double-stranded RNA adenosine deaminases.
Resistant ligand-responsive EGFR mutants:Covalent EGFR TKIs (name copied from entity in Homo sapiens)
Resistant ligand-responsive EGFR mutants
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_177144.3
Dimers of EGF:Ligand-responsive EGFR mutants resistant to non-covalent TKIs (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632374
Dimers of EGF:Ligand-responsive EGFR mutants sensitive to non-covalent TKIs (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632368
Dimers of ligand-responsive EGFR mutants sensitive to non-covalent TKIs (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632366
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632349
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5632357
Analysis of proteins binding to the ITAM motif of the beta-subunit of the high-affinity receptor for IgE (FcepsilonRI)
J. Recept. Signal Transduct. Res. 27:67-81
Ub-Beta-Pix:CDC42:GTP (name copied from entity in Homo sapiens)
EGF:p-6Y-EGFR:CBL:Beta-Pix:CDC42:GTP (name copied from entity in Homo sapiens)
Beta-Pix:CDC42:GTP (name copied from entity in Homo sapiens)
EGF:p-6Y-EGFR:p-Y371-CBL:CIN85:Endophilin:Epsin:Eps15R:Eps15 (name copied from entity in Homo sapiens)
Eps15:HGS:STAM (name copied from entity in Homo sapiens)
EGF:p-6Y-EGFR:p-Y371-CBL:GRB2:CIN85:Endophilin (name copied from entity in Homo sapiens)
CIN85:Endophilin (name copied from entity in Homo sapiens)
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_262317.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3521.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=34979
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4310.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=30721
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3169.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29612
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_259480.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652523
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_263448.1
EGF:Ligand-responsive EGFR mutants dimer (name copied from entity in Homo sapiens)
Dimers of ligand-responsive p-6Y-EGFR mutants (name copied from entity in Homo sapiens)
EGF:Ligand-responsive p-6Y-EGFR mutants sensitive to non-covalent TKIs:HSP90:CDC37 (name copied from entity in Homo sapiens)
EGF:Ligand-responsive p-6Y-EGFR mutants resistant to non-covalent TKIs:HSP90:CDC37 (name copied from entity in Homo sapiens)
EGF:Ligand-responsive p-6Y-EGFR mutants:HSP90:CDC37
Dimers of EGF:Ligand-responsive p-6Y-EGFR mutants (name copied from entity in Homo sapiens)
Ligand-responsive p-6Y-EGFR mutant dimers
Active dimers of ligand-responsive EGFR mutants
Ligand-responsive EGFR mutants dimer (name copied from entity in Homo sapiens)
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_261536.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_215405.2
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EGF:Ligand-responsive EGFR mutants resistant to non-covalent TKIs:HSP90:CDC37 (name copied from entity in Homo sapiens)
EGF:Ligand-responsive EGFR mutants sensitive to non-covalent TKIs:HSP90:CDC37 (name copied from entity in Homo sapiens)
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A mutation in the Glut2 glucose transporter gene of a diabetic patient abolishes transport activity
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Ligand-responsive EGFR mutants resistant to non-covalent TKIs:HSP90:CDC37 (name copied from entity in Homo sapiens)
Ligand-responsive EGFR mutants:HSP90:CDC37
EGF:Ligand-responsive EGFR mutants:HSP90:CDC37
Ligand-responsive EGFR mutants sensitive to non-covalent TKIs:HSP90:CDC37 (name copied from entity in Homo sapiens)
CIN85 ubiquitinated:Endophilin (name copied from entity in Homo sapiens)
EGF:p-6Y-EGFR:p-Y371-CBL:Ub-CIN85:Endophilin:Epsin:Eps15R:Eps15 (name copied from entity in Homo sapiens)
CDC37 (name copied from entity in Homo sapiens)
HSP90 (name copied from entity in Homo sapiens)
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EGF:p-6Y-EGFR:CBL:p-Y53/55-SPRY1/2 (name copied from entity in Homo sapiens)
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EGF:p-6Y-EGFR:CBL:Ub-p-Y53/55-SPRY1/2 (name copied from entity in Homo sapiens)
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Ub-p-Y53/55-SPRY1/2 (name copied from entity in Homo sapiens)
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Mapping of the alpha-1,6-fucosyltransferase gene, FUT8, to human chromosome 14q24.3
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The t(8;22) in chronic myeloid leukemia fuses BCR to FGFR1: transforming activity and specific inhibition of FGFR1 fusion proteins
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SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sites
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Targeting exocytosis: ins and outs of the modulation of quantal dopamine release
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Regulation of calmodulin-stimulated cyclic nucleotide phosphodiesterase (PDE1): review
Class C/3 (Metabotropic glutamate/pheromone receptors)
Half-site reactivity in 6-phosphogluconate dehydrogenase from human erythrocytes
Cleavage of Growing Transcript in the Termination Region
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Post-Elongation Processing of the Transcript
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N-retinylidenephosphatidylethanolamine [ChEBI:71063]
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Mechanisms of glycerophospholipid homeostasis in mammalian cells
Expression of CD83 is regulated by HuR via a novel cis-active coding region RNA element
eIF4AIII binds spliced mRNA in the exon junction complex and is essential for nonsense-mediated decay
The mode of bone morphogenetic protein (BMP) receptor oligomerization determines different BMP-2 signaling pathways
Characterization of p87PIKAP, a novel regulatory subunit of phosphoinositide 3-kinase gamma that is highly expressed in heart and interacts with PDE3B
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_263137.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_246330.1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_263288.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_235546.1
Essential and mutually compensatory roles of {alpha}-mannosidase II and {alpha}-mannosidase IIx in N-glycan processing in vivo in mice
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Scavenger receptors: role in innate immunity and microbial pathogenesis
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LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production
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phosphorylated FGFR3c P250R mutant dimer (name copied from entity in Homo sapiens)
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FGFR3 (4;14) translocation mutant dimers
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Activated FGFR3 t(4;14) translocation mutants
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FGFR3 mutant dimers:TKIs (name copied from entity in Homo sapiens)
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FGFR3c P250R mutant dimer (name copied from entity in Homo sapiens)
Activated FGFR3c P250R mutant (name copied from entity in Homo sapiens)
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_241908.1
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=449243
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620105
FGFR4 Y367C mutant dimer (name copied from entity in Homo sapiens)
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Activated FGFR4 Y367C mutant (name copied from entity in Homo sapiens)
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FGFR4 N535K mutant dimer (name copied from entity in Homo sapiens)
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Activated FGFR3 mutants with enhanced kinase activity
Activated FGFR3 G380R mutant (name copied from entity in Homo sapiens)
FGFR3 K650E mutant dimer (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_195213.3
FGFR3b G697C mutant dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635849
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635847
FGFR3 G382D mutant dimer (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22784.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=449298
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2656.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=36027
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_195046.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620098
FGFR3c P250R mutant dimer bound to FGF (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635754
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620101
Activated FGFR3 795fs*139STOP mutant (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620099
Activated FGFR3b G967C (name copied from entity in Homo sapiens)
Activated FGFR3 G382D mutant (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_235034.1
Activated FGFR3 K650E mutant (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_240976.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=449315
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22524.1
FGFR3 S371C mutant dimer (name copied from entity in Homo sapiens)
FGFR3 Y373C mutant dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635758
Activated FGFR3 R248C mutant dimer (name copied from entity in Homo sapiens)
Activated FGFR3b S249C mutant (name copied from entity in Homo sapiens)
Activated FGFR3 G370C mutant (name copied from entity in Homo sapiens)
Activated FGFR3 S371C mutant dimer (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_238970.1
Activated FGFR3 Y373C mutant dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620115
FGFR3 point mutant dimers with enhanced kinase activity
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_23080.4
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620113
FGFR3 G380R mutant dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=449229
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620112
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22890.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=449311
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113546
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2361.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3641.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=35139
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=449312
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635766
phosphorylated FGFR2b C3 variant dimer (name copied from entity in Homo sapiens)
FGFR2b C3 variant dimer (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22967.1
Overexpressed FGFR2 homodimers:GP369 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635760
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_229612.1
Activated overexpressed FGFR2 (name copied from entity in Homo sapiens)
Overexpressed FGFR2:TKIs (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619609
FGFR3 G370C mutant dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635768
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619607
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_195158.3
Positive newborn screen for methylmalonic aciduria identifies the first mutation in TCblR/CD320, the gene for cellular uptake of transcobalamin-bound vitamin B(12)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652520
FGFR3 R248C mutant dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635767
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_256362.1
FGFR3b S249C mutant dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635761
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2266.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29498
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5017.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620137
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635861
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_195310.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620135
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635862
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620136
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635859
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=449365
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22683.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635801
Claudins in occluding junctions of humans and flies
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620133
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620131
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_234422.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=31369
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4905.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5613.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=31503
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=31311
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620123
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4362.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_251580.1
Purification, sequencing, and molecular identification of a mammalian PP-InsP5 kinase that is activated when cells are exposed to hyperosmotic stress
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11683.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=200351
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5739.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29916
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_229624.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652555
Activated FGFR mutants:p-FRS2alpha:GRB2:GAB1:PI3K (name copied from entity in Homo sapiens)
Activated FGFR mutants:p-FRS2alpha:GRB2:GAB1:PIK3R1 (name copied from entity in Homo sapiens)
FGFR mutants:p-FRS2alpha:GRB2:SOS1 (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620144
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620146
activated FGFR4 N535K mutant (name copied from entity in Homo sapiens)
FGFR4 V550E mutant dimer (name copied from entity in Homo sapiens)
Activated FGFR mutants:p-FRS2alpha (name copied from entity in Homo sapiens)
Activated FGFR mutants:FRS2alpha (name copied from entity in Homo sapiens)
FGFR4 mutant dimers with enhanced kinase activity:PD173074 (name copied from entity in Homo sapiens)
activated FGFR4 V550E mutant (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4432.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=30235
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620143
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_207075.2
Insights into the recruitment of the NMD machinery from the crystal structure of a core EJC-UPF3b complex
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5838.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29434
Close encounters: regulation of vertebrate skeletal myogenesis by cell-cell contact
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628158
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628162
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628166
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628167
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628153
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_250180.1
Openers of SKCa and IKCa channels enhance agonist-evoked endothelial nitric oxide synthesis and arteriolar vasodilation
p-FGFR1 fusion mutant dimers:PIK3R1 (name copied from entity in Homo sapiens)
p-FGFR1 mutant fusions:PI3K (name copied from entity in Homo sapiens)
Activated FGFR1 fusion mutants:PLC-gamma (name copied from entity in Homo sapiens)
Activated FGFR1 fusion mutants:p-PLCgamma (name copied from entity in Homo sapiens)
CUX1-p-FGFR1 fusion mutant dimer (name copied from entity in Homo sapiens)
FGFR1 fusion mutant dimers:TKIs (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628147
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628143
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628150
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628151
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628148
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628149
Regulation of apoptosis: the ubiquitous way
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628139
Association of Fyn and Lyn with the proline-rich domain of glycoprotein VI regulates intracellular signaling
The actin-binding protein UNC-115/abLIM controls formation of lamellipodia and filopodia and neuronal morphogenesis in Caenorhabditis elegans
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_183021.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=532214
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_23358.2
Crystal structure of human homogentisate dioxygenase.
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635884
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635882
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653259
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_194213.3
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_236719.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652980
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_208530.2
Distinct roles of the phosphatidylinositol 3-kinase and STAT5 pathways in IL-7-mediated development of human thymocyte precursors
Specificity of the myotubularin family of phosphatidylinositol-3-phosphatase is determined by the PH/GRAM domain
phosphorylated FGFR2c S252W mutant dimer (name copied from entity in Homo sapiens)
FGFR2 point mutant dimers:TKIs (name copied from entity in Homo sapiens)
Activated FGFR2 N549K mutant (name copied from entity in Homo sapiens)
Activated FGFR2 K660N mutant (name copied from entity in Homo sapiens)
Activated FGFR2 mutants with enhanced kinase activity
FGFR2 N549K mutant dimer (name copied from entity in Homo sapiens)
FGFR2 K660N mutant dimer (name copied from entity in Homo sapiens)
FGFR2 mutant dimers with enhanced kinase activity
phosphorylated FGFR2c A315S mutant dimer (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_256465.1
phosphorylated FGFR2c P253R mutant dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653220
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_231986.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653260
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635853
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635855
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_195177.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635785
phosphorylated FGFR2b mutant dimers with enhanced ligand binding
phosphorylated FGFR2b P253R mutant dimer (name copied from entity in Homo sapiens)
FGFR2c A315S mutant dimer (name copied from entity in Homo sapiens)
FGFR2c P253R mutant dimer (name copied from entity in Homo sapiens)
phosphorylated FGFR2c mutant dimers with enhanced ligand-binding
Activated FGFR2c mutants with enhanced ligand-binding (name copied from entity in Homo sapiens)
FGFR2c mutant dimers with enhanced ligand-binding bound to FGFs (name copied from entity in Homo sapiens)
FGFR2b mutant-binding FGFs:FP-1039 (name copied from entity in Homo sapiens)
FGFR2c S252W mutant dimer (name copied from entity in Homo sapiens)
FGFR2c mutant dimers with enhanced ligand-binding
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635778
phosphorylated FGFR2b S252W mutant dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635782
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635783
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=449222
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22684.2
Characterization of human liver thermostable phenol sulfotransferase (SULT1A1) allozymes with 3,3',5-triiodothyronine as the substrate
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22649.2
FGFR2 S267P mutant dimer (name copied from entity in Homo sapiens)
phosphorylated FGFR1 N546K mutant dimer (name copied from entity in Homo sapiens)
Activated FGFR2c W290G mutant (name copied from entity in Homo sapiens)
Activated FGFR2 S267C mutant (name copied from entity in Homo sapiens)
Activated FGFR2 ligand-independent mutants
FGFR2c W290G mutant dimer (name copied from entity in Homo sapiens)
Activated FGFR2b mutants with enhanced ligand binding (name copied from entity in Homo sapiens)
FGFR2b P253R mutant dimer (name copied from entity in Homo sapiens)
FGFR2b mutant dimers with enhanced ligand-binding
FGFR2b mutant dimers with enhanced ligand-binding bound to FGFs (name copied from entity in Homo sapiens)
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=449293
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_23138.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=449283
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635837
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_195134.3
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_195212.3
FGFR1 P252X mutant dimers bound to FGFs (name copied from entity in Homo sapiens)
FGFR1 P252S mutant dimer (name copied from entity in Homo sapiens)
Activated FGFR1 P252X mutants (name copied from entity in Homo sapiens)
phosphorylated FGFR1 P252X mutant dimers
phosphorylated FGFR1 P252S mutant dimer (name copied from entity in Homo sapiens)
FGFR1 mutant dimers with enhanced kinase activity
phosphorylated FGFR1 P252T mutant dimer (name copied from entity in Homo sapiens)
FGFR1 N546K mutant dimer (name copied from entity in Homo sapiens)
FGFR1 K656E mutant dimer (name copied from entity in Homo sapiens)
phosphorylated FGFR1 K656E mutant dimer (name copied from entity in Homo sapiens)
Activated FGFR1 mutant dimers with enhanced kinase activity
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635870
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_195301.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=449737
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22812.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635841
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635843
Molecular background of leak K+ currents: two-pore domain potassium channels
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_260471.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5647495
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_229540.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648491
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646582
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646581
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646580
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646928
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646926
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648483
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_257331.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648485
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648484
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648481
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648480
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648486
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5648482
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646576
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646577
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646574
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646573
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646572
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646571
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646570
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646569
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646568
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646567
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646575
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646566
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646588
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646587
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646590
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646589
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646584
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646583
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646586
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Molecular cloning of a sixth member of the K+-dependent Na+/Ca2+ exchanger gene family, NCKX6
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Fundamental Immunology (Book): 1077-1104
Oxidative stress and antioxidant defense
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_222591.2
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646930
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646931
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Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature
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Molecular mechanisms involved in the regulation of cytokine production by muramyl dipeptide
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646883
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646882
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646877
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646876
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646879
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646878
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646884
The visual cycle of the cone photoreceptors of the retina
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646899
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646901
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646902
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646903
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646904
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646895
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646896
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646897
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646889
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646890
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646887
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646888
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646893
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646894
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646891
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646892
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646885
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646886
Genomic cloning, heterologous expression and pharmacological characterization of a human histamine H1 receptor
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646923
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646924
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646915
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646916
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646917
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646918
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646914
Functions of replication factor C and proliferating-cell nuclear antigen: functional similarity of DNA polymerase accessory proteins from human cells and bacteriophage T4.
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646913
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646911
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646838
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646909
Differences between the interaction of beta-catenin with non-phosphorylated and single-mimicked phosphorylated 20-amino acid residue repeats of the APC protein
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646907
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646908
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646905
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5646906
pyruvate kinase complex, liver and RBC (name copied from entity in Homo sapiens)
pyruvate carboxylase holoenzyme (name copied from entity in Homo sapiens)
dolichyl D-mannosyl phosphate [ChEBI:15809]
malate dehydrogenase 2 dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620036
malate dehydrogenase 1 dimer (name copied from entity in Homo sapiens)
GOT2 dimer (name copied from entity in Homo sapiens)
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Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2618.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=31175
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635989
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635991
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635990
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_236954.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635993
enolase 1 dimer, (alpha) (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=532204
enolase 2 dimer, (gamma, neuronal) (name copied from entity in Homo sapiens)
pyruvate kinase M1 complex (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_23093.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620032
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_229879.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620029
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620030
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2697.2
ALDOB tetramer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=31135
triosephosphate isomerase dimer (name copied from entity in Homo sapiens)
phosphofructokinase, P2L2 complex (name copied from entity in Homo sapiens)
phosphofructokinase, PL3 complex (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620025
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_194942.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620023
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635748
glyceraldehyde-3-phosphate dehydrogenase tetramer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635746
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_251933.1
phosphoglycerate kinase 1 complex (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635826
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635822
phosphofructokinase, P4 complex (name copied from entity in Homo sapiens)
phosphofructokinase, P3L complex (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635828
phosphofructokinase, L4 complex (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635827
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5741.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620022
The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair.
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635972
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635971
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22935.2
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Excision of an intact intron as a novel lariat structure during pre-mRNA splicing in vitro.
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Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2
Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine
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8xUGP2 (name copied from entity in Homo sapiens)
GYG1:GYS1-a tetramer (name copied from entity in Homo sapiens)
PGM1:Mg++ (name copied from entity in Homo sapiens)
Identification of a novel gene, FGFR1OP2, fused to FGFR1 in 8p11 myeloproliferative syndrome
PGM2:Mg++ (name copied from entity in Homo sapiens)
FBP2 tetramer (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22827.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=449703
FBP1 tetramer (name copied from entity in Homo sapiens)
SLC25A11 homodimer (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_254175.1
GOT1 dimer (name copied from entity in Homo sapiens)
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635976
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635876
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635877
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635809
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635810
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635812
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_195124.3
Nodal signaling: developmental roles and regulation
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=33179
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3188.2
Vitamin B12: unique metalorganic compounds and the most complex vitamins
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_258317.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652521
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_231592.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619645
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619643
NEDL1, a novel ubiquitin-protein isopeptide ligase for dishevelled-1, targets mutant superoxide dismutase-1
Q/R site editing controls kainate receptor inhibition by membrane fatty acids
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619637
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619639
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_246884.1
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Characterisation of Cdc25B localisation and nuclear export during the cell cycle and in response to stress
Similar regulation of human inducible nitric-oxide synthase expression by different isoforms of the RNA-binding protein AUF1
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22559.2
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5619631
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_262017.1
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_233526.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653258
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_183020.3
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620052
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652552
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_258958.1
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Metal transporters in intestine and brain: their involvement in metal-associated neurotoxicities
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_23267.2
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_224579.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_254492.1
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29666
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5636829
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5653.3
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620044
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620046
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620045
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620084
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620086
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_250200.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620092
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620094
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=30487
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3123.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620091
Activated FGFR mutants bound to PLC-gamma (name copied from entity in Homo sapiens)
CCBL1 dimer (name copied from entity in Homo sapiens)
lactate dehydrogenase B4 complex (name copied from entity in Homo sapiens)
Activated FGFR mutants bound to activated PLC gamma (name copied from entity in Homo sapiens)
PAH tetramer (name copied from entity in Homo sapiens)
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_204045.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620083
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620081
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620077
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3577.1
Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620073
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_236280.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637689
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637692
RBP2:atROL (name copied from entity in Homo sapiens)
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RBP1:atROL (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637694
ARSB:Ca2+ (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5637696
B3GAT3 dimer (name copied from entity in Homo sapiens)
cGMP:CNG channel (name copied from entity in Homo sapiens)
CNG channel (name copied from entity in Homo sapiens)
BCO2:Fe2+ (name copied from entity in Homo sapiens)
RBP2:atRAL (name copied from entity in Homo sapiens)
BCMO1:Fe2+ (name copied from entity in Homo sapiens)
Subunit stoichiometry of the CNG channel of rod photoreceptors.
Rod cyclic nucleotide-gated channels have a stoichiometry of three CNGA1 subunits and one CNGB1 subunit.
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620062
GUSB tetramer (name copied from entity in Homo sapiens)
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620066
SLC9A1:p-CHP:Ca2+ (name copied from entity in Homo sapiens)
HA:HAR:HYAL2 (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_259090.1
HA:HAR:HYAL2:SLC9A1:pCHP:Ca2+ (name copied from entity in Homo sapiens)
p-CHP1:Ca2+ (name copied from entity in Homo sapiens)
bHEXB (name copied from entity in Homo sapiens)
B3GAT1 dimer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5620070
B3GAT2 dimer (name copied from entity in Homo sapiens)
HEXA (name copied from entity in Homo sapiens)
PIK3R1:PIK3CA mutants (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5651229
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22689.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=449221
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5651227
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_189358.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5651225
PIK3R1 mutants:PIK3CA (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_172823.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=4419981
PI3K Inhibitors:PI3K (name copied from entity in Homo sapiens)
PDPK1:p-S473-AKT1 E17K mutant:PIP2 (name copied from entity in Homo sapiens)
p-S473-AKT1 E17K mutant:PIP2 (name copied from entity in Homo sapiens)
AKT1 E17K mutant:PIP2 (name copied from entity in Homo sapiens)
EPM2A:PPP1R3C:phosphoglycogen-GYG1:GYS1-a tetramer (name copied from entity in Homo sapiens)
IDH1 R132H dimer (name copied from entity in Homo sapiens)
AKT inhibitors:AKT (name copied from entity in Homo sapiens)
METAP1:2Co2+ (name copied from entity in Homo sapiens)
METAP2:2Co2+ (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_183451.3
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_189361.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=449299
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_22548.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635795
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5635797
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_195174.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652979
GUCA1A:Ca2+ (name copied from entity in Homo sapiens)
Guanylate cyclase activating proteins:Ca2+
GUCA1C:Ca2+ (name copied from entity in Homo sapiens)
GUCA1B:Ca2+ (name copied from entity in Homo sapiens)
GCAP1:Ca2+ (name copied from entity in Homo sapiens)
GCAP2:Ca2+ (name copied from entity in Homo sapiens)
CALM1:Ca2+:CNG channel (name copied from entity in Homo sapiens)
CALM1:Ca2+ (name copied from entity in Homo sapiens)
glucose 6-phosphate isomerase dimer (name copied from entity in Homo sapiens)
GLUT1:ATP (name copied from entity in Homo sapiens)
GLUT4 tetramer (name copied from entity in Homo sapiens)
PFKFB4 dimer (name copied from entity in Homo sapiens)
PFKFB3 dimer (name copied from entity in Homo sapiens)
PFKFB2 dimer (name copied from entity in Homo sapiens)
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase isoform homodimers
PFKFB1 dimer (name copied from entity in Homo sapiens)
phosphoPFKFB1 dimer (name copied from entity in Homo sapiens)
EPM2A:PPP1R3C:phosphoglycogen-GYG2:GYS2-a tetramer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=4419982
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_172824.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652866
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_253085.1
EPM2A:PPP1R3C:glycogen-GYG1:GYS1-a tetramer (name copied from entity in Homo sapiens)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=4419987
EPM2A:PPP1R3C:glycogen-GYG2:GYS2-a tetramer (name copied from entity in Homo sapiens)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_172825.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5652865
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_254384.1
GLUT2 tetramer (name copied from entity in Homo sapiens)
GLUT3 tetramer (name copied from entity in Homo sapiens)
GLUT1 tetramer (name copied from entity in Homo sapiens)
sucrase-isomaltase (name copied from entity in Homo sapiens)
sucrase-isomaltase dimer (name copied from entity in Homo sapiens)
LCT dimer (name copied from entity in Homo sapiens)
MGAM dimer (name copied from entity in Homo sapiens)
Disturbed Wnt Signalling due to a Mutation in CCDC88C Causes an Autosomal Recessive Non-Syndromic Hydrocephalus with Medial Diverticulum
Cloning and characterization of a novel mammalian zinc transporter, zinc transporter 5, abundantly expressed in pancreatic beta cells
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5647029
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PTEN loss in the continuum of common cancers, rare syndromes and mouse models
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The role of calmodulin recruitment in Ca2+ stimulation of adenylyl cyclase type 8
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Regulation of the Ras signaling pathway by GTPase-activating protein in PC12 cells
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Prostaglandins, thromboxanes, leukotrienes, and cytochrome P-450 metabolites of arachidonic acid
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Analysis of protein-protein interactions involved in the activation of the Shc/Grb-2 pathway by the ErbB-2 kinase
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Membrane-bound enzymes of cholesterol synthesis from lanosterol
Cholesterol, hydroxycholesterols, and bile acids
Functional properties of four splice variants of a human pancreatic tandem-pore K+ channel, TALK-1
Dimerization of sterol regulatory element-binding protein 2 via the helix-loop-helix-leucine zipper domain is a prerequisite for its nuclear localization mediated by importin beta
Insertion of residues 429 to 822 at 340 from UniProt:P11362 FGFR1 (in Homo sapiens)
GYG1:GYS1-b tetramer (name copied from entity in Homo sapiens)
oligoGlc-GYG1:GYS1-a tetramer (name copied from entity in Homo sapiens)
GYG2:GYS2-a tetramer (name copied from entity in Homo sapiens)
oligoGlc-GYG1:GYS1-b tetramer (name copied from entity in Homo sapiens)
cAMP sensor Epac as a determinant of ATP-sensitive potassium channel activity in human pancreatic beta cells and rat INS-1 cells
Lysosomes in iron metabolism, ageing and apoptosis
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Regulation of phosphoinositide-specific phospholipase C
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Synthesis and function of 3-phosphorylated inositol lipids
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Human cataract lens membrane at subnanometer resolution
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Antigen processing and presentation by the class I major histocompatibility complex
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Mapping iron binding sites on human frataxin: implications for cluster assembly on the ISU Fe-S cluster scaffold protein
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The proline-rich region of Vav binds to Grb2 and Grb3-3
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Cloning and sequencing of the cDNA encoding human P5
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5-Heptenoic acid, 7-[3,5-dihydroxy-2-(3-hydroxy-1-octenyl)cyclopentyl]-
7-[3, 5-dihydroxy-2-(3-hydroxy-1-octenyl) cyclopentyl]-5-heptenoic acid
Trans-synaptic transmission of vesicular Wnt signals through Evi/Wntless
Characterization and partial amino acid sequencing of a 107-kDa procollagen I N-proteinase purified by affinity chromatography on immobilized type XIV collagen
(5Z,13E)-(15S)-9alpha,15-Dihydroxy-11-oxoprosta-5,13-dienoate [ChEBI:246]
An insight into the mechanism of human cysteine dioxygenase. Key roles of the thioether-bonded tyrosine-cysteine cofactor
The microsomal cardiolipin remodeling enzyme acyl-CoA lysocardiolipin acyltransferase is an acyltransferase of multiple anionic lysophospholipids
The regulation of AP-1 activity by mitogen-activated protein kinases
Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases
Specific phosphorylation and activation of ERK1c by MEK1b: a unique route in the ERK cascade
Mouse, but not Human STING, Binds and Signals in Response to the Vascular Disrupting Agent 5,6-Dimethylxanthenone-4-Acetic Acid
Kinetic analysis of Smad nucleocytoplasmic shuttling reveals a mechanism for transforming growth factor beta-dependent nuclear accumulation of Smads
Peroxisomal fatty acid oxidation disorders and 58 kDa sterol carrier protein X (SCPx). Activity measurements in liver and fibroblasts using a newly developed method.
Multiple phosphoinositide 3-kinase-dependent steps in activation of protein kinase B
(13E)-(15S)-11alpha,15-Dihydroxy-9-oxoprost-13-enoate [ChEBI:142]
The isolation and characterization of a cDNA encoding phospholipid-specific inositol polyphosphate 5-phosphatase
Functional characterization of an organic cation transporter (hOCT1) in a transiently transfected human cell line (HeLa)
RNA Polymerase II Transcription Elongation
Potassium voltage-gated channel subfamily KQT member 2
Characterization and tRNA recognition of mammalian mitochondrial seryl-tRNA synthetase
Neuronal cell adhesion molecule precursor
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GABAA receptors: properties and trafficking
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Cloning and characterization of a 72-kDa inositol-polyphosphate 5-phosphatase localized to the Golgi network
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Pharmacology of AMPA/kainate receptor ligands and their therapeutic potential in neurological and psychiatric disorders
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Ephrin type-B receptor 3 ecNumber2.7.10.1/ecNumber
Ephrin type-B receptor 4 ecNumber2.7.10.1/ecNumber
The narrow substrate specificity of human tyrosine aminotransferase--the enzyme deficient in tyrosinemia type II
Ephrin type-B receptor 1 ecNumber2.7.10.1/ecNumber
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G protein betagamma subunits: central mediators of G protein-coupled receptor signaling
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The Ca2+ Sensor STIM1 is Necessary and Sufficient for the Store-Operated Ca2+ Entry Function of TRPCs in Endothelial Cells
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Phosphorylation inhibits guanine nucleotide exchange on eukaryotic initiation factor 2.
Smad6 inhibits BMP/Smad1 signaling by specifically competing with the Smad4 tumor suppressor
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Mutations in the APC gene and their implications for protein structure and function
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Structure and transcription of a human gene for H1 RNA, the RNA component of human RNase P
Piccolo, a Ca2+ sensor in pancreatic beta-cells. Involvement of cAMP-GEFII.Rim2.Piccolo complex in cAMP-dependent exocytosis
Neural cell adhesion molecule L1-like protein
Mechanisms of p75-mediated death of hippocampal neurons. Role of caspases
Cloning of cDNAs encoding the human gamma-aminobutyric acid type A receptor alpha 6 subunit and characterization of the pharmacology of alpha 6-containing receptors
Newly administered [3H]retinol is transferred from hepatocytes to stellate cells in liver for storage
Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2
Synthesis and recycling of tetrahydrobiopterin in endothelial function and vascular disease
Ca2+ entry, efflux and release in smooth muscle
Genetic heterogeneity and clinical variability in the Sanfilippo syndrome (types A, B, and C)
Characterization of Stat5a and Stat5b homodimers and heterodimers and their association with the glucocortiocoid receptor in mammary cells
Nerve growth factor activates extracellular signal-regulated kinase and p38 mitogen-activated protein kinase pathways to stimulate CREB serine 133 phosphorylation
The Netrin family of guidance factors: emphasis on Netrin-1 signalling
Ten years on: mediation of cell death by the common neurotrophin receptor p75(NTR)
(5Z,8Z,10E,14Z)-(12S)-12-Hydroperoxyeicosa-5,8,10,14-tetraenoate [ChEBI:250]
(5Z,9alpha,11alpha,13E,15S)-9,11-Epoxy-15-hydroxythromboxa-5,13-dien-1-oic acid
(5-Deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt
Tissue factor pathway inhibitor and the revised theory of coagulation
Initiating DNA synthesis: from recruiting to activating the MCM complex.
Structural basis of the interaction between integrin alpha6beta4 and plectin at the hemidesmosomes
xanthosine 5'-monophosphate [ChEBI:15652]
The DNA damage response: sensing and signaling
5-Hydroperoxy-6-trans-8,11,14-cis-eicosatetraenoate [ChEBI:2061]
RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways
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Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2
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Phosphatidylinositol transfer protein alpha isoform
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Uses for JNK: the many and varied substrates of the c-Jun N-terminal kinases
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Phospholipase Cgamma activates Ras on the Golgi apparatus by means of RasGRP1
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Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases
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Dihydropyrimidinase-related protein 1 (CRMP-1)
Vitamins B6 activation to pyridoxal phosphate
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The late endosomal ClC-6 mediates proton/chloride countertransport in heterologous plasma membrane expression
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TRPM4 is a Ca2+-activated nonselective cation channel mediating cell membrane depolarization
Fragmentation and dispersal of the pericentriolar Golgi complex is required for entry into mitosis in mammalian cells
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Proto-oncogene tyrosine-protein kinase ABL1
Head inducer Dickkopf-1 is a ligand for Wnt coreceptor LRP6
Insights into lysosomal cobalamin trafficking: lessons learned from cblF disease
A novel mechanism of JNK1 activation. Nuclear translocation and activation of JNK1 during ischemia and reperfusion.
Identification of protein kinase C (PKC) phosphorylation sites on human lamin B. Potential role of PKC in nuclear lamina structural dynamics
Regulation of pyruvate dehydrogenase activity through phosphorylation at multiple sites
NCAM-induced intracellular signaling revisited
Purification and properties of two DNA ligases from human placenta
The intermediate-conductance Ca2+ -activated K+ channel (KCa3.1) in vascular disease
Cardiovasc Hematol Agents Med Chem 7:1-11
A theory of marginotomy. The incomplete copying of template margin in enzymic synthesis of polynucleotides and biological significance of the phenomenon.
Eph receptor-ephrin bidirectional signals that target Ras and Rho proteins
(R)-4'-Phosphopantothenoyl-L-cysteine [ChEBI:328]
3,4-Dihydroxy-L-phenylalanine [ChEBI:1377]
Nicotinate D-ribonucleotide [ChEBI:7561]
3-Hydroxy-N6,N6,N6-trimethyl-L-lysine [ChEBI:15786]
N-Acetyl-D-glucosamine 6-phosphate [ChEBI:7127]
Genetic and biochemical approach to early prenatal diagnosis in a family with mut methylmalonic aciduria
DNA replication control through interaction of E2F-RB and the origin recognition complex.
The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments
The cell-cycle regulatory protein Cks1 is required for SCF(Skp2)-mediated ubiquitinylation of p27
Congenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase
2-Aminomuconate semialdehyde [ChEBI:15745]
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Triggering of TLR7 and TLR8 expressed by human lung cancer cells induces cell survival and chemoresistance
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Cloning and characterization of a pH-sensing regulatory factor that modulates transport activity of the human H+/peptide cotransporter, PEPT1
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Recent advances in understanding leptin signaling and leptin resistance
Am. J. Physiol. Endocrinol. Metab. 297:E1247-59
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Gene expression networks: competing mRNA decay pathways in mammalian cells
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Leukocyte chemotactic factor 2: A novel renal amyloid protein
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IRAK2 mediated activation of TAK1 complex
spectrin alpha chain, brain/alpha II fodrin
Regulation of human separase by securin binding and autocleavage
Receptor-type tyrosine-protein phosphatase alpha
SHP2 associates directly with tyrosine phosphorylated p90 (SNT) protein in FGF-stimulated cells
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Voltage-dependent T-type calcium channel subunit alpha-1G
Voltage-dependent L-type calcium channel subunit alpha-1S
Voltage-dependent T-type calcium channel subunit alpha-1H
Differential recognition by CD28 of its cognate counter receptors CD80 (B7.1) and B70 (B7.2): analysis by site directed mutagenesis
Voltage-dependent T-type calcium channel subunit alpha-1I
Surprising versatility of Na+-glucose cotransporters: SLC5
Neural cell adhesion molecule 1, 140 kDa isoform
RhoGEF and pleckstrin domain-containing protein 2 (FARP2)
Phosphorylated smooth muscle/non-muscle myosin 2 regulatory light chains
Mindbomb 1, an E3 ubiquitin ligase, forms a complex with RYK to activate Wnt/?-catenin signaling
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Platelets and the injured vessel wall-- "rolling into action": focus on glycoprotein Ib/V/IX and the platelet cytoskeleton
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Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins
Protein phosphatase 2Cepsilon is an endoplasmic reticulum integral membrane protein that dephosphorylates the ceramide transport protein CERT to enhance its association with organelle membranes
Characterization of ceramide synthase 2: tissue distribution, substrate specificity, and inhibition by sphingosine 1-phosphate
Beta oxidation of butanoyl-CoA to acetyl-CoA
Human alanine-glyoxylate aminotransferase 2 lowers asymmetric dimethylarginine and protects from inhibition of nitric oxide production
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Dolichyl beta-D-glucosyl phosphate [ChEBI:4689]
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Dolichyl phosphate D-mannose [ChEBI:4694]
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Neuronal voltage-gated K+ (Kv) channels function in macromolecular complexes
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Structural changes in the calcium pump accompanying the dissociation of calcium
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A molecular perspective of CTLA-4 function
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Comprehending the complex connection between PKCbeta, TAK1, and IKK in BCR signaling
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Docosahexaenoic acid synthesis in human skin fibroblasts involves peroxisomal retroconversion of tetracosahexaenoic acid
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Structural and kinetic features of amyloid beta-protein fibrillogenesis
Tuberculosis: what we don't know can, and does, hurt us
Adapters in the organization of mast cell signaling
Homophilic NCAM interactions interfere with L1 stimulated neurite outgrowth
Molecular and evolutionary basis of the cellular stress response
K63polyUb-Phosphatidylinositol 3-kinase regulatory alpha subunit
Myosin regulatory light chain 2-B, smooth muscle isoform
Smooth muscle/non-muscle myosin 2 regulatory light chains
Identification of a putative gamma-aminobutyric acid (GABA) receptor subunit rho2 cDNA and colocalization of the genes encoding rho2 (GABRR2) and rho1 (GABRR1) to human chromosome 6q14-q21 and mouse chromosome 4
Characterization of the proteins of isolated human platelet alpha-granules. Evidence for a separate alpha-granule-pool of the glycoproteins IIb and IIIa.
Eukaryotic translation initiation factor 4 gamma 3
Eukaryotic translation initiation factor 4E type 2
Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15
Molecular mechanisms of conduction and selectivity in aquaporin water channels
A human homolog of the Schizosaccharomyces pombe rad9+ checkpoint control gene
The enzymes, regulation, and genetics of bile acid synthesis
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Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation
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Construction and expression of human aldolase A and B expression plasmids in Escherichia coli host
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Analysis of a shortened form of human carbonic anhydrase VII expressed in vitro compared to the full-length enzyme
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3-(4-Hydroxyphenyl)pyruvate [ChEBI:1431]
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Molecular characterization of the human peroxisomal branched-chain acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and evidence for the absence of the protein in Zellweger syndrome
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SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion
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Buffer enhancement of proton transfer in catalysis by human carbonic anhydrase III
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Identification of HsORC4, a member of the human origin of replication recognition complex.
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Normal human chromosomes have long G-rich telomeric overhangs at one end
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Promoter escape by RNA polymerase II. Formation of an escape-competent transcriptional intermediate is a prerequisite for exit of polymerase from the promoter.
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Agrin binds to the nerve-muscle basal lamina via laminin
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Structure of human cytidine deaminase bound to a potent inhibitor
Pyrimidine nucleotidases from human erythrocyte possess phosphotransferase activities specific for pyrimidine nucleotides
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From birth to death: the complex lives of eukaryotic mRNAs
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Lessons from photoreceptors: turning off G-protein signaling in living cells
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Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction
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Role of the CLOCK protein in the mammalian circadian mechanism
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Determination of the organisation of coding sequences within the iduronate sulphate sulphatase (IDS) gene
Amino acid synthesis and interconversion (transamination)
APC truncation mutants have impaired AXIN binding
Biosynthesis of chondroitin/dermatan sulfate
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4-Hyp Glu-Gal-Hyl collagen alpha-2(VI) propeptide
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4-Hyp 5-Hyl collagen alpha-2(VI) propeptide
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4-hydroxyprolyl collagen alpha-2(VI) propeptide
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3,4-Hyp Glu-Gal-Hyl collagen alpha-2(VI) propeptide
3,4-Hyp 5-Hyl collagen alpha-2(VI) propeptide
4-Hyp 5-Gal-Hyl collagen alpha-2(VI) propeptide
3,4-hydroxyprolyl collagen alpha-2(VI) propeptide
Glu-Gal-Hyl collagen alpha-1(VI) propeptide
3,4-Hyp 5-Gal-Hyl collagen alpha-2(VI) propeptide
activated TAK1 mediates p38 MAPK activation
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Metabolism of carotenoids and retinoids related to vision
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Free fatty acid receptors and drug discovery
Rod and cone visual pigments and phototransduction through pharmacological, genetic, and physiological approaches
The phosphotyrosine phosphatase SHP2 is a critical mediator of transformation induced by the oncogenic fibroblast growth factor receptor 3
5-hydroxylysyl collagen alpha-1(VI) propeptide
5-Gal-Hyl collagen alpha-1(VI) propeptide
A ubiquitin-interacting motif (UIM) is essential for Eps15 and Eps15R ubiquitination
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Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease
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Structure of mitogen-activated protein kinase-activated protein (MAPKAP) kinase 2 suggests a bifunctional switch that couples kinase activation with nuclear export
3,4-Hyp 5-Gal-Hyl collagen alpha-1(VI) propeptide
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3,4-Hyp 5-Hyl collagen alpha-1(VI) propeptide
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A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis
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N-acetyl-D-glucosaminylphosphatidylinositol [ChEBI:15935]
Molecular mechanism of hypoxia-inducible factor 1alpha -p300 interaction. A leucine-rich interface regulated by a single cysteine
4-Hyp 5-Hyl collagen alpha-1(VI) propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-1(VI) propeptide
4-hydroxyprolyl collagen alpha-1(VI) propeptide
4-Hyp 5-Gal-Hyl collagen alpha-1(VI) propeptide
The Akt kinase signals directly to endothelial nitric oxide synthase
Messenger RNA capping enzymes from eukaryotic cells.
3,4-Hyp Glu-Gal-Hyl collagen alpha-1(VI) propeptide
Homologues of 3x4Hyp-3Hyp-GlcGalHyl-COL6A1
3,4-hydroxyprolyl collagen alpha-1(VI) propeptide
The interleukin 2 receptor. Functional consequences of its bimolecular structure
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Distinct regions of the interleukin-7 receptor regulate different Bcl2 family members
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GTP cyclohydrolase feedback regulatory protein controls cofactor 6-tetrahydrobiopterin synthesis in the cytosol and in the nucleus of epidermal keratinocytes and melanocytes
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Loss of the candidate tumor suppressor BTG3 triggers acute cellular senescence via the ERK-JMJD3-p16(INK4a) signaling axis
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4-Hyp Glu-Gal-Hyl collagen alpha-2(IV) propeptide
4-hydroxyprolyl collagen alpha-2(IV) propeptide
5-Gal-Hyl collagen alpha-2(IV) propeptide
5-hydroxylysyl collagen alpha-2(IV) propeptide
Glu-Gal-Hyl-collagen alpha-2(IV) propeptide
Regulation of myosin II dynamics by phosphorylation and dephosphorylation of its light chain in epithelial cells
Identification of a novel domain in two mammalian inositol-polyphosphate 5-phosphatases that mediates membrane ruffle localization. The inositol 5-phosphatase skip localizes to the endoplasmic reticulum and translocates to membrane ruffles following epidermal growth factor stimulation
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Purification and characterization of homogeneous initiation factor M2A from rabbit reticulocytes.
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Making heads or tails of phospholipids in mitochondria
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Differential expression of aquaporin 8 in human colonic epithelial cells and colorectal tumors
Activation of the MAPK signal cascade by the neural cell adhesion molecule L1 requires L1 internalization
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The crystal structure of human phosphoglucose isomerase at 1.6 A resolution: implications for catalytic mechanism, cytokine activity and haemolytic anaemia
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Activation of Rac GTPase by p75 is necessary for c-jun N-terminal kinase-mediated apoptosis
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Activin signaling and its role in regulation of cell proliferation, apoptosis, and carcinogenesis
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Ectodomain cleavage of ErbB-4: characterization of the cleavage site and m80 fragment
Getting to the end: telomerase access in yeast and humans
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Disruption of ClC-3, a chloride channel expressed on synaptic vesicles, leads to a loss of the hippocampus
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Structural and functional properties of two mutants of lecithin-cholesterol acyltransferase (T123I and N228K)
CREB is a regulatory target for the protein kinase Akt/PKB
The Orc4p and Orc5p subunits of the Xenopus and human origin recognition complex are related to Orc1p and Cdc6p.
Bidirectional water fluxes and specificity for small hydrophilic molecules in aquaporins 0-5
Dominant-negative mutants of importin-beta block multiple pathways of import and export through the nuclear pore complex
Overexpression of human alanine:glyoxylate aminotransferase in Escherichia coli: renaturation from guanidine-HCl and affinity for pyridoxal phosphate co-factor
Activation of HER4 by heparin-binding EGF-like growth factor stimulates chemotaxis but not proliferation
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Recognition of bacterial products by toll-like receptors
Identification of 14 novel GLB1 mutations, including five deletions, in 19 patients with GM1 gangliosidosis from South America
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Crystal structure of human ABAD/HSD10 with a bound inhibitor: implications for design of Alzheimer's disease therapeutics
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Mutations in the MMAA gene in patients with the cblA disorder of vitamin B12 metabolism
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Carbonic anhydrase activators: the first activation study of the human secretory isoform VI with amino acids and amines
3,4-hydroxyprolyl collagen alpha-2(IV) propeptide
4-Hyp 5-Gal-Hyl collagen alpha-2(IV) propeptide
Homologues of 3x4Hyp-GalHyl-COL4A2(26-1712)
Homologues of 3x4Hyp-5Hyl-COL4A2(26-1712)
4-Hyp 5-Hyl collagen alpha-2(IV) propeptide
Homologues of 3x4Hyp-GlcGalHyl-COL4A2(26-1712)
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Eukaryotic mRNA cap binding protein: purification by affinity chromatography on sepharose-coupled m7GDP.
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3,4-Hyp 5-Gal-Hyl collagen alpha-2(IV) propeptide
Homologues of 3x4Hyp-3Hyp-GalHyl-COL4A2(26-1712)
Homologues of 3x4Hyp-3Hyp-GlcGalHyl-COL4A2(26-1712)
3,4-Hyp 5-Hyl collagen alpha-2(IV) propeptide
Homologues of 3x4Hyp-3Hyp-5Hyl-COL4A2(26-1712)
Homologues of 3x4Hyp-3Hyp-COL4A2(26-1712)
3,4-Hyp Glu-Gal-Hyl collagen alpha-2(IV) propeptide
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Identification of bacterial muramyl dipeptide as activator of the NALP3/cryopyrin inflammasome
The many faces and functions of ?-catenin
Purification and kinetic properties of human erythrocyte Mg2+-dependent inorganic pyrophosphatase
Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution.
Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution.
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
Cloning and characterization of two distinct human extracellular signal-regulated kinase activator kinases, MEK1 and MEK2.
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
Human RFT1 deficiency leads to a disorder of N-linked glycosylation
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Bicarbonate transport in cell physiology and disease
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The glucose-lactic acid cycle and gluconeogenesis
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Identification of a family of animal sphingomyelin synthases
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Adipocyte-specific transcription factor ARF6 is a heterodimeric complex of two nuclear hormone receptors, PPAR gamma and RXR alpha
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Peroxisome proliferator-activated receptor gamma
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Aberrant receptor internalization and enhanced FRS2-dependent signaling contribute to the transforming activity of the fibroblast growth factor receptor 2 IIIb C3 isoform
Site-directed mutagenesis of diphosphoinositol polyphosphate phosphohydrolase, a dual specificity NUDT enzyme that attacks diadenosine polyphosphates and diphosphoinositol polyphosphates
Niemann-Pick C1 Like 1 protein is critical for intestinal cholesterol absorption
Mechanism of two classes of cancer mutations in the phosphoinositide 3-kinase catalytic subunit
Regulation of cell migration by the C2 domain of the tumor suppressor PTEN
Role of lipid rafts in the interaction between hTRPC1, Orai1 and STIM1
Subunit structures and stoichiometries of human DNA fragmentation factor proteins before and after induction of apoptosis
HDL as a target in the treatment of atherosclerotic cardiovascular disease
Molecular mechanism of an oncogenic mutation that alters membrane targeting: Glu17Lys modifies the PIP lipid specificity of the AKT1 PH domain
IFI16 is an innate immune sensor for intracellular DNA
Mode of proviral activation of a putative mammary oncogene (int-1) on mouse chromosome 15
Class I MHC mediated antigen processing & presentation
Beta-catenin hits chromatin: regulation of Wnt target gene activation
Elimination of cholesterol as cholestenoic acid in human lung by sterol 27-hydroxylase: evidence that most of this steroid in the circulation is of pulmonary origin
NIPBL, encoding a homolog of fungal Scc2-type sister chromatid cohesion proteins and fly Nipped-B, is mutated in Cornelia de Lange syndrome
ZNF198-FGFR1 transforming activity depends on a novel proline-rich ZNF198 oligomerization domain
Structure of the synthetase domain of human CTP synthetase, a target for anticancer therapy
Acta Crystallogr Sect F Struct Biol Cryst Commun 62:613-7
Collagenous Alzheimer amyloid plaque component assembles amyloid fibrils into protease resistant aggregates
Specific inhibition of pyruvate transport in rat liver mitochondria and human erythrocytes by alpha-cyano-4-hydroxycinnamate
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Control of mitosis by changes in the subcellular location of cyclin-B1-Cdk1 and Cdc25C
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Biosynthetic studies of A2E, a major fluorophore of retinal pigment epithelial lipofuscin
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Selective RNA binding by a single CCCH zinc-binding domain from Nup475 (Tristetraprolin)
Synthesis of Leukotrienes (LT) and Eoxins (EX)
Adjacent asparagines in the NR2-subunit of the NMDA receptor channel control the voltage-dependent block by extracellular Mg2+
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Peptide binding and antigen presentation by class II histocompatibility glycoproteins
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The plasma membrane of erythrocytes plays a fundamental role in the transport of oxygen, carbon dioxide and nitric oxide and in the maintenance of the reduced state of the heme iron
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The molecular basis of insulin-stimulated glucose uptake: signalling, trafficking and potential drug targets
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Recruitment of repair and signaling proteins to double-strand breaks
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Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns
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The helicase DDX41 senses intracellular DNA mediated by the adaptor STING in dendritic cells
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The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch
Roles of AUF1 isoforms, HuR and BRF1 in ARE-dependent mRNA turnover studied by RNA interference
Comparison of human B cell antigen receptor complexes: membrane-expressed forms of immunoglobulin (Ig)M, IgD, and IgG are associated with structurally related heterodimers
DNA topology and a minimal set of basal factors for transcription by RNA polymerase II.
Nedd4 mediates ErbB4 JM-a/CYT-1 ICD ubiquitination and degradation in MDCK II cells
Nuclear receptor subfamily 5 group A member 2
Antigen Presentation: Folding, assembly and peptide loading of class I MHC
Norepinephrine Neurotransmitter Release Cycle
AES/GRG5: more than just a dominant-negative TLE/GRG family member
Vilse, a conserved Rac/Cdc42 GAP mediating Robo repulsion in tracheal cells and axons
Pontin52, an interaction partner of beta-catenin, binds to the TATA box binding protein
Proc. Natl. Acad. Sci. U.S.A. 95:14787-92
Species-specific recognition of single-stranded RNA via toll-like receptor 7 and 8
Neuregulin-3 (NRG3): a novel neural tissue-enriched protein that binds and activates ErbB4
Homologues of p-Y1252,Y1336,Y1474-GRIN2B
Human diseases: clues to cracking the connexin code?
Regulation of ASIC activity by ASIC4--new insights into ASIC channel function revealed by a yeast two-hybrid assay
Stem-loop binding protein facilitates 3'-end formation by stabilizing U7 snRNP binding to histone pre-mRNA.
AT-AC pre-mRNA splicing mechanisms and conservation of minor introns in voltage-gated ion channel genes.
Heparan sulfate proteoglycan core protein
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Plexins: axon guidance and signal transduction
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5-hydroxylysyl collagen alpha-1(V) chain
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4-hydroxyprolyl collagen alpha-1(V) chain
4-Hyp Glu-Gal-Hyl collagen alpha-1(V) chain
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5-hydroxylysyl collagen alpha-2(V) chain
3,4-Hyp 5-Gal-Hyl collagen alpha-1(V) chain
3,4-hydroxyprolyl collagen alpha-1(V) chain
3,4-Hyp Glu-Gal-Hyl collagen alpha-1(V) chain
4-Hyp 5-Gal-Hyl collagen alpha-1(V) chain
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Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2/3 complex
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Variable mutation frequencies in coding repeats of TCF-4 and other target genes in colon, gastric and endometrial carcinoma showing microsatellite instability
Stimulation of cloned human glucagon-like peptide 1 receptor expressed in HEK 293 cells induces cAMP-dependent activation of calcium-induced calcium release
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3,4-hydroxyprolyl collagen alpha-2(V) chain
3,4-Hyp Glu-Gal-Hyl collagen alpha-2(V) chain
3,4-Hyp 5-Gal-Hyl collagen alpha-2(V) chain
4-hydroxyprolyl collagen alpha-2(V) chain
4-Hyp Glu-Gal-Hyl collagen alpha-2(V) chain
4-Hyp 5-Gal-Hyl collagen alpha-2(V) chain
Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin.
Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O-fucosylation
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Molecular characterization of the HLA-linked steroid 21-hydroxylase B gene from an individual with congenital adrenal hyperplasia
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Structural basis for a direct interaction between FGFR1 and NCAM and evidence for a regulatory role of ATP
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Formation and activation by phosphorylation of activin receptor complexes
Nuclear cyclin D1/CDK4 kinase regulates CUL4 expression and triggers neoplastic growth via activation of the PRMT5 methyltransferase
Prophase destruction of Emi1 by the SCF(betaTrCP/Slimb) ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase
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Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells
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Origins and Mechanisms of miRNAs and siRNAs
Sanfilippo syndrome type C: mutation spectrum in the heparan sulfate acetyl-CoA: alpha-glucosaminide N-acetyltransferase (HGSNAT) gene
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XCtBP is a XTcf-3 co-repressor with roles throughout Xenopus development
Chondroitin sulfate synthase-3. Molecular cloning and characterization
Structure-function analysis of the bestrophin family of anion channels
Evidence for protein-tyrosine-phosphatase catalysis proceeding via a cysteine-phosphate intermediate
Selective degradation of AU-rich mRNAs promoted by the p37 AUF1 protein isoform
Docosahexaenoic Acid Induces Proteasome-dependent Degradation of {beta}-catenin, Down-regulation of Survivin and Apoptosis in Human Colorectal Cancer Cells not expressing COX-2
5-Phosphoribose 1-diphosphate biosynthesis
Synthesis of cytosolic 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) from D-ribose 5-phosphate
Identification of a novel guanine nucleotide exchange factor for the Rho GTPase
Cytosolic and membrane-associated proteins involved in the recruitment of AP-1 adaptors onto the trans-Golgi network
Kid, a novel kinesin-like DNA binding protein, is localized to chromosomes and the mitotic spindle
Interactions between Src homology (SH) 2/SH3 adapter proteins and the guanylnucleotide exchange factor SOS are differentially regulated by insulin and epidermal growth factor.
Constitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasia
Insights into COPI coat assembly and function in living cells
Diseases associated with visual transduction
Wnt stabilization of ?-catenin reveals principles for morphogen receptor-scaffold assemblies
4-Hyp 5-Hyl-collagen alpha-1(XXVII) -N propeptide
4-hydroxyprolyl collagen alpha-1(XXVII) -N propeptide
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXVII) -N propeptide
5-hydroxylysyl-collagen alpha-1(XXVII) -N propeptide
5-Gal-Hyl-collagen alpha-1(XXVII) -N propeptide
Glu-Gal-Hyl-collagen alpha-1(XXVII) -N propeptide
3,4-Hyp 5-Gal-Hyl collagen alpha-2(I) chain
Sulfotransferases in the bioactivation of xenobiotics
4-Hyp 5-Gal-Hyl collagen alpha-2(I) chain
3,4-hydroxyprolyl collagen alpha-2(I) chain
3,4-Hyp Glu-Gal-Hyl collagen alpha-2(I) chain
4-hydroxyprolyl collagen alpha-2(I) chain
4-Hyp Glu-Gal-Hyl collagen alpha-2(I) chain
5-hydroxylysyl collagen alpha-2(I) chain
5-hydroxylysyl collagen alpha-1(II) chain
3,4-Hyp 5-Gal-Hyl collagen alpha-1(III) chain
3,4-Hyp 5-Hyl collagen alpha-1(III) chain
4-Hyp Glu-Gal-Hyl collagen alpha-1(II) chain
4-hydroxyprolyl collagen alpha-1(II) chain
Synthesis of Prostaglandins (PG) and Thromboxanes (TX)
5-hydroxylysyl collagen alpha-1(III) chain
4-Hyp Glu-Gal-Hyl collagen alpha-1(III) chain
4-hydroxyprolyl collagen alpha-1(III) chain
4-Hyp 5-Gal-Hyl collagen alpha-1(III) chain
4-Hyp 5-Hyl collagen alpha-1(III) -N propeptide
3,4-Hyp Glu-Gal-Hyl collagen alpha-1(III) chain
3,4-hydroxyprolyl collagen alpha-1(III) chain
3,4-hydroxyprolyl collagen alpha-1(I) chain
4-Hyp 5-Gal-Hyl collagen alpha-1(I) chain
4-Hyp Glu-Gal-Hyl collagen alpha-1(I) chain
3,4-Hyp 5-Gal-Hyl collagen alpha-1(I) chain
3,4-Hyp Glu-Gal-Hyl collagen alpha-1(I) chain
Targeting the Wnt/?-catenin signaling pathway in human cancers
4-hydroxyprolyl collagen alpha-1(I) chain
3,4-hydroxyprolyl collagen alpha-1(II) chain
4-Hyp 5-Gal-Hyl collagen alpha-1(II) chain
3,4-Hyp 5-Hyl collagen alpha-1(II) chain
3,4-Hyp Glu-Gal-Hyl collagen alpha-1(II) chain
3,4-Hyp 5-Gal-Hyl collagen alpha-1(II) chain
Gamma linolenic acid: an antiinflammatory omega-6 fatty acid
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3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XI) -N propeptide
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XI) -N propeptide
3,4-Hyp 5-Hyl-collagen alpha-1(XI) -N propeptide
3,4-hydroxyprolyl-collagen alpha-1(XI) -N propeptide
4-hydroxyprolyl collagen alpha-3(V) -N propeptide
5-hydroxylysyl collagen alpha-3(V) -N propeptide
5-Gal-Hyl collagen alpha-3(V) -N propeptide
Facilitative Na+-independent glucose transporters
Glu-Gal-Hyl collagen alpha-3(V) -N propeptide
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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11283.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628319
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=200640
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5628341
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4-Hyp 5-Gal-Hyl collagen alpha-3(V) -N propeptide
3,4-hydroxyprolyl collagen alpha-3(V) -N propeptide
3,4-Hyp Glu-Gal-Hyl collagen alpha-3(V) -N propeptide
3,4-Hyp 5-Hyl collagen alpha-3(V) -N propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-3(V) -N propeptide
4-Hyp 5-Hyl collagen alpha-3(V) -N propeptide
3,4-Hyp 5-Gal-Hyl collagen alpha-3(V) -N propeptide
Glu-Gal-Hyl collagen alpha-1(V) -N propeptide
Collagen alpha-2(XI) chain N-term fragment
5-hydroxylysyl-collagen alpha-2(XI) chain N-term fragment
Glu-Gal-Hyl collagen alpha-2(XI) chain N-term fragment
4-Hyp 5-Hyl collagen alpha-2(XI) -N propeptide
4-Hyp 5-Gal-Hyl collagen alpha-2(XI) chain C-term fragment
5-Gal-Hyl collagen alpha-2(XI) -N propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-2(XI) -N propeptide
3,4-Hyp 5-Hyl-collagen alpha-2(XI) chain C-term fragment
3,4-hydroxyprolyl collagen alpha-2(XI) -N propeptide
3,4-Hyp Glu-Gal-Hyl-collagen alpha-2(XI) chain C-term fragment
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3,4-Hyp 5-Gal-Hyl-collagen alpha-2(XI) -N propeptide
Glu-Gal-Hyl-collagen alpha-1(XI) -N propeptide
5-hydroxylysyl-collagen alpha-1(XI) -N propeptide
5-Gal-Hyl-collagen alpha-1(XI) -N propeptide
Assignment of the human and mouse prion protein genes to homologous chromosomes
4-hydroxyprolyl collagen alpha-1(XI) -N propeptide
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4-Hyp Glu-Gal-Hyl-collagen alpha-1(XI) -N propeptide
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4-Hyp 5-Hyl-collagen alpha-1(XI) -N propeptide
4-Hyp 5-Gal-Hyl-collagen alpha-1(XI) -N propeptide
Glu-Gal-Hyl-collagen alpha-1(XXIV) -N propeptide
4-hydroxyprolyl collagen alpha-1(XXIV) -N propeptide
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XXVII) -N propeptide
3,4-Hyp 5-Hyl-collagen alpha-1(XXVII) -N propeptide
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXVII) -N propeptide
3,4-hydroxyprolyl-collagen alpha-1(XXVII) -N propeptide
4-Hyp 5-Gal-Hyl-collagen alpha-1(XXVII) -N propeptide
Armadillo nuclear import is regulated by cytoplasmic anchor Axin and nuclear anchor dTCF/Pan
5-hydroxylysyl-collagen alpha-1(XXIV) -N propeptide
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XXIV) -N propeptide
p21-activated kinase regulates mast cell degranulation via effects on calcium mobilization and cytoskeletal dynamics
3,4-Hyp 5-Hyl-collagen alpha-1(XXIV) -N propeptide
4-hydroxyprolyl collagen alpha-2(XI) chain N-term fragment
4-Hyp 5-Gal-Hyl-collagen alpha-1(XXIV) -N propeptide
4-Hyp 5-Hyl-collagen alpha-1(XXIV) -N propeptide
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXIV) -N propeptide
cAMP-dependent mobilization of intracellular Ca2+ stores by activation of ryanodine receptors in pancreatic beta-cells. A Ca2+ signaling system stimulated by the insulinotropic hormone glucagon-like peptide-1-(7-37)
3,4-hydroxyprolyl-collagen alpha-1(XXIV) -N propeptide
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXIV) -N propeptide
5-Gal-Hyl-collagen alpha-1(XXIV) -N propeptide
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Protein synthesis and protein phosphorylation during heat stress, recovery, and adaptation
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Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors
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Chromokinesins: multitalented players in mitosis
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Identification of two tyrosine phosphoproteins, pp70 and pp68, which interact with phospholipase Cgamma, Grb2, and Vav after B cell antigen receptor activation
Structural models of amyloid-like fibrils
The Role of Gbetagamma Subunits in the Organization, Assembly, and Function of GPCR Signaling Complexes
Expression cloning of a human cDNA encoding folylpoly(gamma-glutamate) synthetase and determination of its primary structure
Molecular mechanisms of megakaryocyte differentiation
Consistent fusion of ZNF198 to the fibroblast growth factor receptor-1 in the t(8;13)(p11;q12) myeloproliferative syndrome
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Temporal differences in the activation of three classes of non-transmembrane protein tyrosine kinases following B-cell antigen receptor surface engagement
Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2
C1q differentially modulates phagocytosis and cytokine responses during ingestion of apoptotic cells by human monocytes, macrophages, and dendritic cells
3,4-Hyp 5-Gal-Hyl collagen alpha-1(III) -N propeptide
3,4-Hyp 5-Hyl collagen alpha-1(III) -N propeptide
3,4-Hyp Glu-Gal-Hyl collagen alpha-1(III) -N propeptide
3,4-hydroxyprolyl collagen alpha-1(III) -N propeptide
5-hydroxylysyl collagen alpha-1(II) -N propeptide
Glu-Gal-Hyl collagen alpha-1(II) -N propeptide
4-Hyp 5-Gal-Hyl collagen alpha-1(III) -N propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-1(III) -N propeptide
Activation of the apoptotic endonuclease DFF40 (caspase-activated DNase or nuclease). Oligomerization and direct interaction with histone H1
3,4-Hyp 5-Gal-Hyl collagen alpha-2(V) -N propeptide
3,4-Hyp 5-Hyl collagen alpha-2(V) -N propeptide
Glu-Gal-Hyl-collagen alpha-1(III) -N propeptide
5-hydroxylysyl collagen alpha-1(III) -N propeptide
4-hydroxyprolyl collagen alpha-1(III) -N propeptide
5-Gal-Hyl collagen alpha-1(III) -N propeptide
3,4-Hyp Glu-Gal-Hyl collagen alpha-2(V) -N propeptide
3,4-hydroxyprolyl collagen alpha-2(V) -N propeptide
4-Hyp 5-Gal-Hyl collagen alpha-2(V) -N propeptide
Cyclic GMP phosphodiesterase-5: target of sildenafil
4-Hyp 5-Hyl collagen alpha-2(V) -N propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-2(V) -N propeptide
4-hydroxyprolyl collagen alpha-2(V) -N propeptide
5-Gal-Hyl collagen alpha-2(V) -N propeptide
5-hydroxylysyl collagen alpha-2(V) -N propeptide
Glu-Gal-Hyl collagen alpha-2(V) -N propeptide
3,4-Hyp 5-Hyl collagen alpha-1(V) -N propeptide
COPII-mediated vesicle formation at a glance
3,4-Hyp Glu-Gal-Hyl collagen alpha-1(V) -N propeptide
3,4-Hyp 5-Gal-Hyl collagen alpha-1(V) -N propeptide
4-Hyp 5-Hyl collagen alpha-1(V) -N propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-1(V) -N propeptide
3,4-hydroxyprolyl collagen alpha-1(V) -N propeptide
4-Hyp 5-Gal-Hyl collagen alpha-1(V) -N propeptide
5-hydroxylysyl collagen alpha-1(V) -N propeptide
4-hydroxyprolyl collagen alpha-1(V) -N propeptide
5-Gal-Hyl collagen alpha-1(V) -N propeptide
4-Hyp 5-Hyl collagen alpha-1(II) -N propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-1(II) -N propeptide
4-hydroxyprolyl collagen alpha-1(II) -N propeptide
5-Gal-Hyl collagen alpha-1(II) -N propeptide
3,4-Hyp 5-Hyl collagen alpha-1(II) -N propeptide
3,4-Hyp Glu-Gal-Hyl collagen alpha-1(II) -N propeptide
3,4-hydroxyprolyl collagen alpha-1(II) -N propeptide
4-Hyp 5-Gal-Hyl collagen alpha-1(II) -N propeptide
Formation of novel TRPC channels by complex subunit interactions in embryonic brain
Butyrate Response Factor 1 (BRF1) destabilizes mRNA
Molecular cloning, tissue distribution, and functional expression of the human Na(+)/H(+) exchanger NHE2
5-Gal-Hyl collagen alpha-1(I) -N propeptide
3,4-Hyp 5-Gal-Hyl collagen alpha-1(I) -N propeptide
3,4-Hyp Glu-Gal-Hyl collagen alpha-1(I) -N propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-1(I) -N propeptide
3,4-Hyp 5-Hyl collagen alpha-1(I) -N propeptide
4-Hyp 5-Hyl collagen alpha-1(I) -N propeptide
4-Hyp 5-Gal-Hyl collagen alpha-1(I) -N propeptide
3,4-hydroxyprolyl collagen alpha-1(I) -N propeptide
5-hydroxylysl-collagen alpha-1(I) -N propeptide
Glu-Gal-Hyl collagen alpha-1(I) -N propeptide
3,4-hydroxyprolyl collagen alpha-2(I) -N propeptide
4-Hyp 5-Hyl collagen alpha-2(I) -N propeptide
4-Hyp 5-Gal-Hyl collagen alpha-2(I) -N propeptide
4-Hyp Glu-Gal-Hyl collagen alpha-2(I) -N propeptide
4-hydroxyprolyl collagen alpha-2(I)-N propeptide
5-Gal-Hyl collagen alpha-2(I) -N propeptide
5-hydroxylysyl collagen alpha-2(I) -N propeptide
Glu-Gal-Hyl-collagen alpha-2(I) -N propeptide
4-hydroxyprolyl collagen alpha-1(I) -N propeptide
3,4-Hyp Glu-Gal-Hyl collagen alpha-2(I) -N propeptide
3,4-Hyp 5-Gal-Hyl collagen alpha-2(I) -N propeptide
3,4-Hyp 5-Hyl collagen alpha-2(I) -N propeptide
The p110? and p110? isoforms of PI3K play divergent roles in mammary gland development and tumorigenesis
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TIP49 regulates beta-catenin-mediated neoplastic transformation and T-cell factor target gene induction via effects on chromatin remodeling
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Cleavage preferences of the apoptotic endonuclease DFF40 (caspase-activated DNase or nuclease) on naked DNA and chromatin substrates
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Molecular mechanisms leading to three different phenotypes in the cblD defect of intracellular cobalamin metabolism
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The role of CDP-diacylglycerol synthetase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content
Helical model of nucleation and propagation to account for the growth of type I collagen fibrils from symmetrical pointed tips: a special example of self-assembly of rod-like monomers
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53BP1 and NFBD1/MDC1-Nbs1 function in parallel interacting pathways activating ataxia-telangiectasia mutated (ATM) in response to DNA damage.
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GTPase signaling: bridging the GAP between ARF and Rho
Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
Presenilin-dependent ErbB4 nuclear signaling regulates the timing of astrogenesis in the developing brain
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Regulation of actin dynamics by stress-activated protein kinase 2 (SAPK2)-dependent phosphorylation of heat-shock protein of 27 kDa (Hsp27)
The isolation and characterization of cDNA encoding human and rat brain inositol polyphosphate 4-phosphatase
Nomenclature of the GLUT/SLC2A family of sugar/polyol transport facilitators.
Am J Physiol Endocrinol Metab 282:E974-6
Distinct recognition of collagen subtypes by alpha(1)beta(1) and alpha(2)beta(1) integrins. Alpha(1)beta(1) mediates cell adhesion to type XIII collagen
Replication protein A stimulates proliferating cell nuclear antigen-dependent repair of abasic sites in DNA by human cell extracts.
ABCA6, a novel a subclass ABC transporter
Cytochrome P450 - arranged by substrate type
Persistent initiation of DNA replication and chromatin-bound MCM proteins during the cell cycle in cdc6 mutants.
Cooperative inhibition of bone morphogenetic protein signaling by Smurf1 and inhibitory Smads
p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27
Mutations of OCTN2, an organic cation/carnitine transporter, lead to deficient cellular carnitine uptake in primary carnitine deficiency
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Mutations in the gene for the IL-7 receptor result in T(-)B(+)NK(+) severe combined immunodeficiency disease
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Sequence position of 3-hydroxyproline in basement membrane collagen. Isolation of glycyl-3-hydroxyprolyl-4-hydroxyproline from swine kidney
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Dual-specificity histone demethylase KIAA1718 (KDM7A) regulates neural differentiation through FGF4
Tek/Tie2 signaling: new and old partners
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T cell antigen-receptor signal transduction
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The WASP-WAVE protein network: connecting the membrane to the cytoskeleton
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Measurement of muscle striations in stretch and contraction
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MicroRNA genes are transcribed by RNA polymerase II
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Histone demethylation by a family of JmjC domain-containing proteins
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Interaction of one-chain and two-chain tissue plasminogen activator with intact and plasmin-degraded fibrin
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Properties of an affinity-column-purified human deoxycytidylate deaminase
Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations
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LSD1 demethylates histone and non-histone proteins
hZip2 and hZip3 zinc transporters are down regulated in human prostate adenocarcinomatous glands
An essential role for RasGRP1 in mast cell function and IgE-mediated allergic response
ATM mediated response to DNA double-strand break
The Mammalian synaptonemal complex: a scaffold and beyond
Target selection of heparan sulfate hexuronic acid 2-O-sulfotransferase
DNA mismatch repair in eukaryotes and bacteria
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The Sec6/8 complex in mammalian cells: characterization of mammalian Sec3, subunit interactions, and expression of subunits in polarized cells
Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine
The role of leptin in the control of insulin-glucose axis
Comparative analysis of human masculinity
Pancreatic islet GLUT2 glucose transporter mRNA and protein expression in humans with and without NIDDM
DNA damage recognition during nucleotide excision repair in mammalian cells.
Probable ATP-dependent RNA helicase DDX41
Ubiquitin-like modifier-activating enzyme 7
Probable E3 ubiquitin-protein ligase HERC5
Ubiquitin/ISG15-conjugating enzyme E2 L6
Interferon-induced 17 kDa protein component recommendedName: Ubiquitin cross-reactive protein
Probable ubiquitin carboxyl-terminal hydrolase CYLD
Protein kinase C substrate 60.1 kDa protein heavy chain
Oligosaccharyl transferase 48 kDa subunit
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
Mitochondrial energy-linked nicotinamide nucleotide transhydrogenase. Membrane topography of the bovine enzyme
AZD2171 shows potent antitumor activity against gastric cancer over-expressing fibroblast growth factor receptor 2/keratinocyte growth factor receptor
The Drosha-DGCR8 complex in primary microRNA processing
Human sprouty 4, a new ras antagonist on 5q31, interacts with the dual specificity kinase TESK1
Substrate specificity of phospholipase B from guinea pig intestine. A glycerol ester lipase with broad specificity
Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin
Dishevelled activates JNK and discriminates between JNK pathways in planar polarity and wingless signaling
The intracellular interactions of the L1 family of cell adhesion molecules
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The rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens
Efflux and compartmentalization of zinc by members of the SLC30 family of solute carriers
The sodium/glucose cotransport family SLC5
The SLC36 family: proton-coupled transporters for the absorption of selected amino acids from extracellular and intracellular proteolysis
The SLC39 family of metal ion transporters
Cloning and functional expression of the human GlcNAc-1-P transferase, the enzyme for the committed step of the dolichol cycle, by heterologous complementation in Saccharomyces cerevisiae
Receptor-activated single channels in intact human platelets
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Suppression of c-ras transformation by GTPase-activating protein
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The human homologue of yeast ArgRIII protein is an inositol phosphate multikinase with predominantly nuclear localization
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Homologues of 3x4Hyp-GlcGalHyl-COL17A1(1-?)
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Mutation eliminating mitochondrial leader sequence of methylmalonyl-CoA mutase causes muto methylmalonic acidemia
Proc. Natl. Acad. Sci. U.S.A. 87:3147-50
Heparan sulfate 3-O-sulfotransferase isoform 5 generates both an antithrombin-binding site and an entry receptor for herpes simplex virus, type 1
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Phosphorylation of carbovir enantiomers by cellular enzymes determines the stereoselectivity of antiviral activity
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The structural basis of the activation of Ras by Sos
Sulfation and sulfotransferases 1: Sulfotransferase molecular biology: cDNAs and genes
Resistance to thromboembolism in PI3Kgamma-deficient mice
Biochemical characterization of Wnt-frizzled interactions using a soluble, biologically active vertebrate Wnt protein
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Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells
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Homologues of 3x4Hyp-3Hyp-GlcGalHyl-COL17A1(1-?)
Thrombospondin cooperates with CD36 and the vitronectin receptor in macrophage recognition of neutrophils undergoing apoptosis
Protection and reactivation of human methylmalonyl-CoA mutase by MMAA protein
Biochem. Biophys. Res. Commun. 404:443-7
Phospholipase C gamma1 and Phospholipase C gamma2
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2
Homologues of 3x4Hyp-GalHyl-COL17A1(1-?)
Leucine-rich repeat flightless-interacting protein 1
The single minichromosome maintenance protein of Methanobacterium thermoautotrophicum DeltaH contains DNA helicase activity.
Molecular characterization of human Argonaute-containing ribonucleoprotein complexes and their bound target mRNAs
The P2Y1 receptor mediates ADP-induced p38 kinase-activating factor generation in human platelets
Proton magnetic resonance studies of carbonic anhydrase. II. Group controlling catalytic activity
Gastric hyperplasia in mice lacking the putative Cdc42 effector IQGAP1
Grb2 mediates negative regulation of stem cell factor receptor/c-Kit signaling by recruitment of Cbl
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Dissection of the mitochondrial import and assembly pathway for human Tom40
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Inhibition of collagen fibrillogenesis by cells expressing soluble extracellular domains of DDR1 and DDR2
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Functions and mechanisms of RNA editing.
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The netrin-1 receptor DCC promotes filopodia formation and cell spreading by activating Cdc42 and Rac1
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RNA Polymerase III Transcription Initiation From Type 2 Promoter
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A common variant in methionine synthase reductase combined with low cobalamin (vitamin B12) increases risk for spina bifida
5-Gal-Hyl-collagen alpha-1(XIII) chain ectodomain
5-hydroxylysyl-collagen alpha-1(XIII) chain ectodomain
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XIII) chain ectodomain
4-hydroxyprolyl collagen alpha-1(XIII) chain ectodomain
4-Hyp 5-Gal-Hyl-collagen alpha-1(XIII) chain ectodomain
4-Hyp 5-Hyl-collagen alpha-1(XIII) chain ectodomain
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XIII) chain ectodomain
3,4-hydroxyprolyl-collagen alpha-1(XIII) chain ectodomain
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3,4-Hyp 5-Hyl-collagen alpha-1(XIII) chain ectodomain
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Processing of Capped Intronless Pre-mRNA
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3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XIII) chain ectodomain
Homologues of 3x4Hyp-3Hyp-GalHyl-COL17A1(1-?)
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Identification and characterization of SMPD1 mutations causing Niemann-Pick types A and B in Spanish patients
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Glu-Gal-Hyl-collagen alpha-1(XIII) chain ectodomain
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Collagen alpha-1(XIII) chain N-term transmembrane regions
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Homologues of 3x4Hyp-3Hyp-5Hyl-COL17A1(1-?)
Colocalization of the homophilic binding site and the neuritogenic activity of the cell adhesion molecule L1 to its second Ig-like domain
Leptin and the central nervous system control of glucose metabolism
Transcriptional networks controlling pancreatic development and beta cell function
Signal-induced proliferation-associated protein 1
cGMP-dependent protein kinase 1, alpha isozyme
Active cyclin B1-Cdk1 first appears on centrosomes in prophase
Base-free sugar-phosphate removal via the single-nucleotide replacement pathway
Di- and triphosphopyridine nucleotide isocitric dehydrogenases in yeast
Signal transduction via platelet-derived growth factor receptors
Collagen alpha-1(XVIII) endostatin-like fragment
Bleeding due to disruption of a cargo-specific ER-to-Golgi transport complex
5-hydroxylysyl-collagen alpha-1(XVIII) endostatin-like fragment
Adrenodoxin: structure, stability, and electron transfer properties
5-Gal-Hyl-collagen alpha-1(XVIII) endostatin-like fragment
Fabry disease: identification of 50 novel alpha-galactosidase A mutations causing the classic phenotype and three-dimensional structural analysis of 29 missense mutations
Gamma-interferon-inducible lysosomal thiol reductase
4-hydroxyprolyl collagen alpha-1(XVIII) endostatin-like fragment
Isolation and characterization of human Nramp cDNA
Traffic control: regulation of kinesin motors
3,4-hydroxyprolyl-collagen alpha-1(XVIII) endostatin-like fragment
Cathepsin D component recommendedName: Cathepsin D light chain /component component recommendedName: Cathepsin D heavy chain /component
SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate remodeling of the mRNA surveillance complex during nonsense-mediated mRNA decay
Wnt proteins are lipid-modified and can act as stem cell growth factors
beta4GalT-II is a key regulator of glycosylation of the proteins involved in neuronal development
Glu-Gal-Hyl-collagen alpha-1(XVIII) endostatin-like fragment
Homologues of 3x4Hyp-3Hyp-COL18A1(?-1754)
Subtype-specific stimulation of [35S]GTPgammaS binding by recombinant alpha2-adrenoceptors
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Functional structure and composition of the extracellular matrix
The Wnt/calcium pathway activates NF-AT and promotes ventral cell fate in Xenopus embryos
Preclinical studies of fibroblast growth factor receptor 3 as a therapeutic target in multiple myeloma
Identification of a cDNA encoding an isoform of human CTP synthetase
Proteasome and peptidase function in MHC-class-I-mediated antigen presentation
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Human deoxythymidine kinase. I. Purification and general properties of the cytoplasmic and mitochondrial isozymes derived from blast cells of acute myelocytic leukemia
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C/EBP?'s role in determining Ras-induced senescence or transformation
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Analysis of cytochrome P450 metabolites of arachidonic and linoleic acids by liquid chromatography-mass spectrometry with ion trap MS
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4-Hyp Glu-Gal-Hyl-collagen alpha-1(XVIII) endostatin-like fragment
4-Hyp 5-Hyl-collagen alpha-1(XVIII) endostatin-like fragment
Homologues of 3x4Hyp-GlcGalHyl-COL18A1(?-1754)
4-Hyp 5-Gal-Hyl-collagen alpha-1(XVIII) endostatin-like fragment
Homologues of 3x4Hyp-5Hyl-COL18A1(?-1754)
Homologues of 3x4Hyp-GalHyl-COL18A1(?-1754)
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XVIII) endostatin-like fragment
Homologues of 3x4Hyp-3Hyp-GlcGalHyl-COL18A1(?-1754)
3,4-Hyp 5-Hyl-collagen alpha-1(XVIII) endostatin-like fragment
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XVIII) endostatin-like fragment
Homologues of 3x4Hyp-3Hyp-5Hyl-COL18A1(?-1754)
'Mg2+ [cytosol]' is required for 'ribose phosphate diphosphokinase activity of phosphoribosyl pyrophosphate synthetase 1 holoenzyme (name copied from entity in Homo sapiens) [cytosol]'
'Ca2+ [cytosol]' positively regulates 'phosphorylase kinase activity of phosphorylase kinase complex (PHKL) (name copied from entity in Homo sapiens) [cytosol]'
'Ca2+ [cytosol]' positively regulates 'phosphorylase kinase activity of phosphorylase kinase complex (PHKM) (name copied from entity in Homo sapiens) [cytosol]'
'GUCA1A [cytosol]' positively regulates 'guanylate cyclase activity of GUCYs [photoreceptor disc membrane]'
'GUCA1B [cytosol]' positively regulates 'guanylate cyclase activity of GUCYs [photoreceptor disc membrane]'
'GCAP1:Ca2+ (name copied from entity in Homo sapiens) [cytosol]' negatively regulates 'guanylate cyclase activity of GUCYs [photoreceptor disc membrane]'
'GCAP2:Ca2+ (name copied from entity in Homo sapiens) [cytosol]' negatively regulates 'guanylate cyclase activity of GUCYs [photoreceptor disc membrane]'
The structure of apo human glutamate dehydrogenase details subunit communication and allostery
4-hydroxyprolyl collagen alpha-1(XV) endostatin-XV
Homologues of 3x4Hyp-3Hyp-GalHyl-COL18A1(?-1754)
The endo-8,9-epoxide of aflatoxin B1: a new metabolite
5-hydroxylysyl-collagen alpha-1(XV) endostatin-XV
Homologues of GlcGalHyl-COL15A1(1212-1388)
Glu-Gal-Hyl-collagen alpha-1(XV) endostatin-XV
Class II MHC peptide loading by the professionals
5-Gal-Hyl-collagen alpha-1(XV) endostatin-XV
Pancreatic-duodenal homeobox 1 regulates expression of liver receptor homolog 1 during pancreas development
Insig-mediated degradation of HMG CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol
The ERBB4/HER4 intracellular domain 4ICD is a BH3-only protein promoting apoptosis of breast cancer cells
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XV) endostatin-XV
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Postsynaptic nicotinic acetylcholine receptors
Homologues of 3x4Hyp-GlcGalHyl-COL15A1(1212-1388)
4-Hyp 5-Hyl-collagen alpha-1(XV) endostatin-XV
Homologues of 3x4Hyp-GalHyl-COL15A1(1212-1388)
3,4-hydroxyprolyl-collagen alpha-1(XV) endostatin-XV
4-Hyp 5-Gal-Hyl-collagen alpha-1(XV) endostatin-XV
Mechanism of GTP hydrolysis by G-protein alpha subunits
Characterization of human platelet GTPase activating protein for the Ral GTP-binding protein
Homologues of 3x4Hyp-5Hyl-COL15A1(1212-1388)
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XV) endostatin-XV
Homologues of 3x4Hyp-3Hyp-COL15A1(1212-1388)
4a-hydroxytetrahydrobiopterin [ChEBI:15374]
Peroxidasin forms sulfilimine chemical bonds using hypohalous acids in tissue genesis
'4xCa2+:CaM (name copied from entity in Homo sapiens) [cytosol]' positively regulates 'calcium- and calmodulin-responsive adenylate cyclase activity of Adenylate cyclase (Mg2+ cofactor) (name copied from entity in Homo sapiens) [plasma membrane]'
The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease
Cloning and sequencing of the cDNA for the light subunit of human liver gamma-glutamylcysteine synthetase and relative mRNA levels for heavy and light subunits in human normal tissues
Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains
Phosphorylation of Nephrin Triggers Ca2+ Signaling by Recruitment and Activation of Phospholipase C-{gamma}1
HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets
High-throughput immunoblotting. Ubiquitiin-like protein ISG15 modifies key regulators of signal transduction
Distinct missense mutations of the FGFR3 lys650 codon modulate receptor kinase activation and the severity of the skeletal dysplasia phenotype
Acidosis, acid-sensing ion channels, and neuronal cell death
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NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein
Proc. Natl. Acad. Sci. U.S.A. 97:599-604
Enzymatic reduction of disulfide bonds in lysosomes: characterization of a gamma-interferon-inducible lysosomal thiol reductase (GILT)
Phospholipase C-gamma: diverse roles in receptor-mediated calcium signaling
Molecular cloning and characterization of a novel human beta1,3-glucosyltransferase, which is localized at the endoplasmic reticulum and glucosylates O-linked fucosylglycan on thrombospondin type 1 repeat domain
Molecular cloning and characterization of a novel isoform of the human UDP-galactose transporter, and of related complementary DNAs belonging to the nucleotide-sugar transporter gene family
Biochemical analysis of pathogenic ligand-dependent FGFR2 mutations suggests distinct pathophysiological mechanisms for craniofacial and limb abnormalities
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Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes
Mammalian CARMIL inhibits actin filament capping by capping protein
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TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver
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Krüppel-like transcription factor KLF5 is a key regulator of adipocyte differentiation
AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism
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DPC4, a candidate tumor suppressor gene at human chromosome 18q21.1
Human BAMBI cooperates with Smad7 to inhibit transforming growth factor-beta signaling
Functional characterization of human duodenal cytochrome b (Cybrd1): Redox properties in relation to iron and ascorbate metabolism
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XV) endostatin-XV
Homologues of 3x4Hyp-3Hyp-GalHyl-COL15A1(1212-1388)
Receptor-type protein-tyrosine phosphatase S precursor
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3,4-Hyp 5-Hyl-collagen alpha-1(XV) endostatin-XV
Membrane transport: retromer to the rescue
Homologues of 3x4Hyp-3Hyp-GlcGalHyl-COL15A1(1212-1388)
Homologues of 3x4Hyp-3Hyp-5Hyl-COL15A1(1212-1388)
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Biochemical properties of mammalian neutral sphingomyelinase 2 and its role in sphingolipid metabolism
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Diversity of the mammalian sodium/proton exchanger SLC9 gene family
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Regulation of phosphatidylinositol kinases and metabolism by Wnt3a and Dvl
Glu-Gal-Hyl-collagen alpha-1(XXVII) chain
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXVII) chain
3,4-Hyp 5-Hyl-collagen alpha-1(XXVII) chain
4-hydroxyprolyl collagen alpha-1(XXVII) chain
5-hydroxylysyl-collagen alpha-1(XXVII) chain
4-Hyp 5-Gal-Hyl-collagen alpha-1(XXVII) chain
Molecular analysis of collagen binding by the human discoidin domain receptors, DDR1 and DDR2. Identification of collagen binding sites in DDR2
3,4-hydroxyprolyl-collagen alpha-1(XXVII) chain
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XXVII) chain
4-Hyp 5-Hyl-collagen alpha-1(XXVII) chain
Trafficking protein particle complex subunit 4
Co-operative Cdc42 and Rho signalling mediates ephrinB-triggered endothelial cell retraction
Epithelial discoidin domain-containing receptor 1
Secretory protein trafficking and organelle dynamics in living cells
4-Hyp Glu-Gal-Hyl-collagen alpha-1(XI) chain
4-Hyp 5-Gal-Hyl-collagen alpha-1(XI) chain
3,4-Hyp Glu-Gal-Hyl-collagen alpha-1(XI) chain
3,4-hydroxyprolyl-collagen alpha-1(XI) chain
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XI) chain
3,4-Hyp 5-Hyl-collagen alpha-1(XI) chain
4-hydroxyprolyl collagen alpha-2(XI) chain
Cloning and recombinant expression of a structurally novel human secreted phospholipase A2
4-Hyp Glu-Gal-Hyl collagen alpha-2(XI) chain
5-hydroxylysyl-collagen alpha-2(XI) chain
3,4-Hyp Glu-Gal-Hyl-collagen alpha-2(XI) chain
3,4-hydroxyprolyl collagen alpha-2(XI) chain
4-Hyp 5-Gal-Hyl collagen alpha-2(XI) chain
3,4-Hyp 5-Gal-Hyl-collagen alpha-2(XI) chain
3,4-Hyp 5-Hyl-collagen alpha-2(XI) chain
The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism
3,4-Hyp 5-Gal-Hyl-collagen alpha-1(XXVII) chain
4-hydroxyprolyl collagen alpha-1(XI) chain
5-hydroxylysyl-collagen alpha-1(XI) chain
MyD88 cascade initiated on plasma membrane
Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase
The role of cytoplasmic serine residues of the cell adhesion molecule L1 in neurite outgrowth, endocytosis, and cell migration
3alpha,7alpha-Dihydroxy-5beta-cholestanoyl-CoA [ChEBI:1709]
4,8,12-Trimethyltridecanoyl-CoA [ChEBI:1757]
(2S,3S)-3-Hydroxy-2-methylbutanoyl-CoA [ChEBI:15449]
Characterization of 5-oxo-L-prolinase in normal and tumor tissues of humans and rats: a potential new target for biochemical modulation of glutathione
Diseases caused by defects in the visual cycle: retinoids as potential therapeutic agents
Annu. Rev. Pharmacol. Toxicol. 47:469-512
Differential recruitment of Dishevelled provides signaling specificity in the planar cell polarity and Wingless signaling pathways
(S)-3-Hydroxy-3-methylglutaryl-CoA [ChEBI:15467]
(S)-2-Methyl-3-oxopropanoyl-CoA [ChEBI:15466]
(R)-2-Methyl-3-oxopropanoyl-CoA [ChEBI:15465]
The DIX domain of Dishevelled confers Wnt signaling by dynamic polymerization
1D-myo-inositol 1,3,4,5-tetrakisphosphate
phosphatidylinositol 1,3,4,5-tetrakisphosphate
1D-myo-Inositol 1,3,4,5,6-pentakisphosphate
myo-inositol 1,3,4,5,6-pentakisphosphate
1D-myo-inositol 1,3,4,6-tetrakisphosphate
Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations
1-phosphatidyl-1D-myo-inositol 4-phosphates
RNF mutants show enhanced WNT signaling and proliferation
Endosomal Sorting Complex Required For Transport (ESCRT)
A module of negative feedback regulators defines growth factor signaling
Subcellular localization of 3-methylcrotonyl-coenzyme A carboxylase in bovine kidney
The molecular dissection of Fc gamma receptor mediated phagocytosis
Sequence differences between human muscle and liver cDNAs for UDPglucose pyrophosphorylase and kinetic properties of the recombinant enzymes expressed in Escherichia coli.
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Conformational transition associated with E1-E2 interaction in small ubiquitin-like modifications
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Interleukin-2 stimulation induces tyrosine phosphorylation of p120-Cbl and CrkL and formation of multimolecular signaling complexes in T lymphocytes and natural killer cells
Preferential alternative splicing in cancer generates a K-sam messenger RNA with higher transforming activity
Cellular signalling mechanisms of neural cell adhesion molecules
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Mutations in the transmembrane domain of FGFR3 cause the most common genetic form of dwarfism, achondroplasia
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The ARE-dependent mRNA-destabilizing activity of BRF1 is regulated by protein kinase B
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The human UDP-N-acetylglucosamine: alpha-6-D-mannoside-beta-1,2- N-acetylglucosaminyltransferase II gene (MGAT2). Cloning of genomic DNA, localization to chromosome 14q21, expression in insect cells and purification of the recombinant protein
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Components and dynamics of DNA replication complexes in S. cerevisiae: redistribution of MCM proteins and Cdc45p during S phase.
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LSD1 and the chemistry of histone demethylation
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Molecular cloning of a novel member of the eukaryotic polypeptide chain-releasing factors (eRF). Its identification as eRF3 interacting with eRF1.
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Dermatan sulphate-rich proteoglycan associates with rat tail-tendon collagen at the d band in the gap region
Serum and glucocorticoid-induced kinase (SGK) 1 and the epithelial sodium channel are regulated by multiple with no lysine (WNK) family members
Migfilin interacts with vasodilator-stimulated phosphoprotein (VASP) and regulates VASP localization to cell-matrix adhesions and migration
Aquaporins in the hepatobiliary tract. Which, where and what they do in health and disease
Structural relationships and the classification of aminoacyl-tRNA synthetases
Cross GTPase-activating protein (CrossGAP)/Vilse links the Roundabout receptor to Rac to regulate midline repulsion
Excitatory amino acid transporter 5, a retinal glutamate transporter coupled to a chloride conductance
HYAL2, a human gene expressed in many cells, encodes a lysosomal hyaluronidase with a novel type of specificity
Molecular cloning, sequencing and expression studies of the human breast cancer cell glutaminase
Octameric structure of the human bifunctional enzyme PAICS in purine biosynthesis
Phosphate incorporation during glycogen synthesis and Lafora disease
Many cuts to ruin: a comprehensive update of caspase substrates
Phosphorylation of Gz in human platelets. Selectivity and site of modification
Reviews in molecular biology and biotechnology: transmembrane signaling by G protein-coupled receptors
Glucose-sensing mechanisms in pancreatic beta-cells
Philos Trans R Soc Lond B Biol Sci 360:2211-25
(R)-2-Hydroxy-3-(phosphonooxy)-1-monoanhydridewith phosphoric propanoic acid
Amino acid transport across the plasma membrane
Transcriptional regulation of a metastasis suppressor gene by Tip60 and beta-catenin complexes
Nodal enhances the activity of FoxO3a and its synergistic interaction with Smads to regulate cyclin G2 transcription in ovarian cancer cells
Gitelman's variant of Bartter's syndrome, inherited hypokalaemic alkalosis, is caused by mutations in the thiazide-sensitive Na-Cl cotransporter
Argonaute proteins: mediators of RNA silencing
Profiling of promoter occupancy by PPAR{alpha} in human hepatoma cells via ChIP-chip analysis
Abortive initiation is increased only for the weakest members of a set of down mutants of the adenovirus 2 major late promoter.
Enzymatic, metabolic and secretory patterns in human islets of type 2 (non-insulin-dependent) diabetic patients
Chicken FK506-binding protein, FKBP65, a member of the FKBP family of peptidylprolyl cis-trans isomerases, is only partially inhibited by FK506
The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper
Ras effectors and their role in mitogenesis and oncogenesis
Structure and sequence of the human sulphamidase gene
Phosphorylation of serine 230 promotes inducible transcriptional activity of heat shock factor 1
Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG)
ATP-dependent interaction of human mismatch repair proteins and dual role of PCNA in mismatch repair
Insulin signalling and the regulation of glucose and lipid metabolism
KDM3B is the H3K9 demethylase involved in transcriptional activation of lmo2 in leukemia
Comp Biochem Physiol A Mol Integr Physiol 157:193-7
Release and trafficking of lipid-linked morphogens
The lipocalin alpha(1)-microglobulin binds heme in different species
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An integrated genomic analysis of human glioblastoma multiforme
Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta signalling
A critical role for beta cell M3 muscarinic acetylcholine receptors in regulating insulin release and blood glucose homeostasis in vivo
Phosphoinositides in cell regulation and membrane dynamics
Viral evasion and subversion of pattern-recognition receptor signalling
Highly calcium permeable postsynaptic nicotinic acetylcholine receptors
4-(2-aminophenyl)-2,4-dioxobutanoic acid
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Functional variant of CYP4A11 20-hydroxyeicosatetraenoic acid synthase is associated with essential hypertension
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Molecular characterization and chromosomal localization of a third alpha-class hypoxia inducible factor subunit, HIF3alpha
NCAM140 interacts with the focal adhesion kinase p125(fak) and the SRC-related tyrosine kinase p59(fyn)
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Effects of cyclic GMP on smooth muscle relaxation
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Solute carrier family 52, riboflavin transporter, member 3
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Transport of Mature mRNA derived from an Intron-Containing Transcript
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TBP, a universal eukaryotic transcription factor?
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phosphoribosyl pyrophosphate synthetase 1
Phosphoribosyl pyrophosphate synthetase I
Ribose-phosphate pyrophosphokinase I (EC 2.7.6.1) (Phosphoribosyl pyrophosphate synthetase I) (PPRibP) (PRS-I)
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6-phosphogluconate dehydrogenase, decarboxylating
The t(6;8)(q27;p11) translocation in a stem cell myeloproliferative disorder fuses a novel gene, FOP, to fibroblast growth factor receptor 1
Purification and properties of phosphoribosyl pyrophosphate synthetase from rat liver
Human cystinuria-related transporter: localization and functional characterization
Evidence for procollagen, a biosynthetic precursors of collagen
p38-dependent phosphorylation of the mRNA decay-promoting factor KSRP controls the stability of select myogenic transcripts
Decyanation of vitamin B12 by a trafficking chaperone
Proc. Natl. Acad. Sci. U.S.A. 105:14551-4
Molecular cloning of a third member of the potassium-dependent sodium-calcium exchanger gene family, NCKX3
Wnt inhibitory factor 1 is epigenetically silenced in human osteosarcoma, and targeted disruption accelerates osteosarcomagenesis in mice
Expression of human alpha-l-fucosyltransferase gene homologs in monkey kidney COS cells and modification of potential fucosyltransferase acceptor substrates by an endogenous glycosidase
Aldo-keto reductases from the AKR1B subfamily: retinoid specificity and control of cellular retinoic acid levels
Identification of tyrosine residues in constitutively activated fibroblast growth factor receptor 3 involved in mitogenesis, Stat activation, and phosphatidylinositol 3-kinase activation
Wnt3a-mediated formation of phosphatidylinositol 4,5-bisphosphate regulates LRP6 phosphorylation
Synthesis of bile acids and bile salts via 24-hydroxycholesterol
Anomalous megakaryocytopoiesis in mice with mutations in the c-Myb gene
Cloning of the NCX2 isoform of the plasma membrane Na(+)-Ca2+ exchanger
Active Wnt proteins are secreted on exosomes
Destruction of cytochrome P-450 by ethylene. Structure of the resulting prosthetic heme adduct.
DNA primase from KB cells. Characterization of a primase activity tightly associated with immunoaffinity-purified DNA polymerase-alpha.
Cloning and identification of amino acid residues of human phospholipase C delta 1 essential for catalysis
Characterization of human FAST-1, a TGF beta and activin signal transducer
Characterization of a human lysophosphatidic acid acyltransferase that is encoded by a gene located in the class III region of the human major histocompatibility complex
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Heterotrimeric G protein activation by G-protein-coupled receptors
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Subunit composition of mammalian transient receptor potential channels in living cells
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Purification and properties of carnitine acetyltransferase from human liver
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Tyrosine phosphorylation and activation of Bruton tyrosine kinase upon Fc epsilon RI cross-linking
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Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor
Epidermal growth factor receptors harboring kinase domain mutations associate with the heat shock protein 90 chaperone and are destabilized following exposure to geldanamycins
Purification and some properties of inorganic pyrophosphatase from human erythrocytes
Transforming growth factor-beta induces nuclear import of Smad3 in an importin-beta1 and Ran-dependent manner
A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex.
CLAC: a novel Alzheimer amyloid plaque component derived from a transmembrane precursor, CLAC-P/collagen type XXV
6Z,9Z,12Z,15Z,18Z-tetracosapentaenoyl-CoA (TPA-CoA)
9Z,12Z,15Z,18Z-Tetracosatetraenoyl-CoA (TTA-CoA)
Crystal structure of a beta-catenin/APC complex reveals a critical role for APC phosphorylation in APC function
Retinoic acid activation of peroxisome proliferation-activated receptor delta represses obesity and insulin resistance
Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation
Dynamic assembly of TRPC1-STIM1-Orai1 ternary complex is involved in store-operated calcium influx. Evidence for similarities in store-operated and calcium release-activated calcium channel components
(S)-Hydroperoxy-6-trans-8,11,14-cis-eicosatetraenoic acid
A histone H3 lysine 27 demethylase regulates animal posterior development
6Z,9Z,12Z,15Z,18Z,21Z-tetracosahexaenoyl-CoA (THA-CoA)
9Z,12Z,15Z,18Z,21Z-tetracosapentaenoyl-CoA (TPA-CoA)
8Z,11Z,14Z,17Z-Eicosatetraenoyl-CoA (ETA-CoA)
(4Z,7Z,10Z,13Z,16Z,19Z)-Docosahexaenoic acid
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
The MRN complex: coordinating and mediating the response to broken chromosomes.
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphates
1-phosphatidyl-1D-myo-inositol 5-phosphate
1-phosphatidyl-1D-myo-inositol 3-phosphate
Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding
1-phosphatidyl-1D-myo-inositol 4-phosphate
The quaternary structure of bovine brain kinesin
ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response
Lysophospholipid acyltransferases and arachidonate recycling in human neutrophils
Molecular cloning and functional expression of the human Golgi UDP-N-acetylglucosamine transporter
Species-specific detection of the antiviral small-molecule compound CMA by STING
Fatty acid metabolism in health and disease: the role of delta-6-desaturase
Am J Clin Nutr 57:732S-736S; discussion 736S-737S
Expression of GFP-tagged neuronal glutamate transporters in cerebellar Purkinje neurons
Identification, retinoid binding, and x-ray analysis of a human retinol-binding protein
Visualization of eukaryotic DNA mismatch repair reveals distinct recognition and repair intermediates
Cell biology of IL-7, a key lymphotrophin
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645407
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645406
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_197627.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645403
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645401
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645410
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645409
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645411
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645420
A Toll-like receptor recognizes bacterial DNA
A hyaluronidase activity of the sperm plasma membrane protein PH-20 enables sperm to penetrate the cumulus cell layer surrounding the egg
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645415
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_194672.3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645814
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645812
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645413
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645412
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645419
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645418
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645820
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645821
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645423
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645421
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645425
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645424
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645427
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645426
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645818
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645819
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645431
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645432
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645429
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_232095.1
Complete amino acid sequence of the neurone-specific gamma isozyme of enolase (NSE) from human brain and comparison with the non-neuronal alpha form (NNE)
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645822
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_227570.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645800
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645798
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645797
Cloning of a human cDNA for CTP-phosphoethanolamine cytidylyltransferase by complementation in vivo of a yeast mutant
TAZ controls Smad nucleocytoplasmic shuttling and regulates human embryonic stem-cell self-renewal
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645336
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645354
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_225402.2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_123676.2
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645334
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645335
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645316
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2022890
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645328
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645329
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645326
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645327
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645323
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645324
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645321
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645322
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645318
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645320
Crystal structure of the nucleosome core particle at 2.8 A resolution
Rate-equilibria relationships in intramolecular proton transfer in human carbonic anhydrase III
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_203602.2
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645383
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645384
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645385
Clinical, biochemical and molecular genetic correlations in adenylosuccinate lyase deficiency
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=742343
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_23317.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645338
Phosphoproteomics reveals new ERK MAP kinase targets and links ERK to nucleoporin-mediated nuclear transport
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645399
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645393
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645386
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645387
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645391
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645392
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645389
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645390
Recombinant domain IV of perlecan binds to nidogens, laminin-nidogen complex, fibronectin, fibulin-2 and heparin
[Receptors for cholecystokinin and gastrin]
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645304
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645308
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645307
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645310
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645309
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645313
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645312
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645315
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645314
Signal transduction by fibroblast growth factor receptor-4 (FGFR-4). Comparison with FGFR-1
Platelet alpha2-macroglobulin and alpha1-antitrypsin
Succinate dehydrogenase deficiency in human
Location of type XV collagen in human tissues and its accumulation in the interstitial matrix of the fibrotic kidney
The role of semaphorins and their receptors in gliomas
A new secreted protein that binds to Wnt proteins and inhibits their activities
Signal transduction via the stem cell factor receptor/c-Kit
Domains and maturation processes that regulate the activity of ADAMTS-2, a metalloproteinase cleaving the aminopropeptide of fibrillar procollagens types I-III and V
The human sef-a isoform utilizes different mechanisms to regulate receptor tyrosine kinase signaling pathways and subsequent cell fate
Human geranylgeranyl diphosphate synthase: isolation of the cDNA, chromosomal mapping and tissue expression
The Sec61 complex is located in both the ER and the ER-Golgi intermediate compartment
Functional expression and characterisation of a new human phosphatidylinositol 4-kinase PI4K230
Kinetic analysis of the binding of monomeric and dimeric ephrins to Eph receptors: correlation to function in a growth cone collapse assay
Trace amines: identification of a family of mammalian G protein-coupled receptors
Molecular characterization of human UDP-glucuronic acid/UDP-N-acetylgalactosamine transporter, a novel nucleotide sugar transporter with dual substrate specificity
clathrin-coated endocytic vesicle membrane
ATP bound to the origin recognition complex is important for preRC formation.
Regulation of HSF1-mediated heat shock response
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645437
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645433
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645434
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645440
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645438
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645439
DNA damage signaling triggers degradation of histone methyltransferases through APC/C(Cdh1) in senescent cells
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642363
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642367
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642366
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642369
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642368
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642375
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642374
The architecture of the human Rad54-DNA complex provides evidence for protein translocation along DNA.
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Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642623
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645508
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645507
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642622
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642621
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645504
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645503
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645506
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645505
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5653300
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_183206.3
Glutamate accelerates RPE cell proliferation through ERK1/2 activation via distinct receptor-specific mechanisms
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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645510
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645509
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642631
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642630
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642629
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642628
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642627
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5642626
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645483
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645484
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645485
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645486
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645487
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645488
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645489
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645490
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645491
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645492
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645494
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645495
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645493
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645498
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645499
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645496
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645497
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645502
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645500
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645501
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645463
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645464
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645465
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645466
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645471
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=5645472
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Mechanisms for the role of tetrahydrobiopterin in endothelial function and vascular disease
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Aflatoxin B1-induced hepatocellular carcinoma in developing countries: Geographical distribution, mechanism of action and prevention
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Characterization of the COQ5 gene from Saccharomyces cerevisiae. Evidence for a C-methyltransferase in ubiquinone biosynthesis
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Failure of blood-island formation and vasculogenesis in Flk-1-deficient mice
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A novel mechanism for GABA synthesis and packaging into synaptic vesicles
A novel interleukin-17 receptor-like protein identified in human umbilical vein endothelial cells antagonizes basic fibroblast growth factor-induced signaling
Electrostatics of aquaporin and aquaglyceroporin channels correlates with their transport selectivity
International Union of Basic and Clinical Pharmacology. LXXXV: calcium-activated chloride channels
Kinetics and inhibition of recombinant human cystathionine gamma-lyase. Toward the rational control of transsulfuration
RGS17, an overexpressed gene in human lung and prostate cancer, induces tumor cell proliferation through the cyclic AMP-PKA-CREB pathway
The mitochondrial ornithine transporter. Bacterial expression, reconstitution, functional characterization, and tissue distribution of two human isoforms
Ror receptor tyrosine kinases: orphans no more
Low levels of glucose transporters and K+ATP channels in human pancreatic beta cells early in development
Kit signaling through PI 3-kinase and Src kinase pathways: an essential role for Rac1 and JNK activation in mast cell proliferation
CpG-DNA-specific activation of antigen-presenting cells requires stress kinase activity and is preceded by non-specific endocytosis and endosomal maturation
Fc receptor-mediated phagocytosis requires CDC42 and Rac1
A novel member of a zinc transporter family is defective in acrodermatitis enteropathica
5beta-cholesten-7alpha, 12alpha-diol-3-one
25(R) 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA
25(S) 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA
Expression of the SNT-1/FRS2 phosphotyrosine binding domain inhibits activation of MAP kinase and PI3-kinase pathways and antiestrogen resistant growth induced by FGF-1 in human breast carcinoma cells
Characterization of the D-glucuronyl C5-epimerase involved in the biosynthesis of heparin and heparan sulfate
25(S) 3alpha,7alpha-dihydroxy-5beta-cholestanoyl-CoA
(24R, 25R) 3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA
25(S) 3alpha,7alpha-dihydroxy-5beta-cholest-24-enoyl-CoA
(24R, 25R) 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA
Stop codon FGFR3 mutations in thanatophoric dwarfism type 1
1-Hydroxypropane-1,2,3-tricarboxylic acid
The ratio between tetrahydrobiopterin and oxidized tetrahydrobiopterin analogues controls superoxide release from endothelial nitric oxide synthase: an EPR spin trapping study
Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB
Molecular cloning of human Syk. A B cell protein-tyrosine kinase associated with the surface immunoglobulin M-B cell receptor complex
Transcriptional regulation and binding of heat shock factor 1 and heat shock factor 2 to 32 human heat shock genes during thermal stress and differentiation
Structure of human holocarboxylase synthetase gene and mutation spectrum of holocarboxylase synthetase deficiency
Glycosaminoglycans. A biochemical and clinical review
25(R) 3alpha,7alpha,24(S)-trihydroxy-5beta-cholestanoyl-CoA
25(R) 3alpha,7alpha,12alpha,24(S)-tetrahydroxy-5beta-cholestanoyl-CoA
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Specificity, promiscuity and localization of ARF protein interactions with NCS-1 and phosphatidylinositol-4 kinase-III beta
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Regulation of Smurf2 ubiquitin ligase activity by anchoring the E2 to the HECT domain
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Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1
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cDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase
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The hyaluronate receptor is a member of the CD44 (H-CAM) family of cell surface glycoproteins
Btk is a positive regulator in the TREM-1/DAP12 signaling pathway
The crystal structure of yeast thiamin pyrophosphokinase
Identification, characterization, and crystal structure of the Omega class glutathione transferases
Isolation and sequence of the human farnesyl pyrophosphate synthetase cDNA. Coordinate regulation of the mRNAs for farnesyl pyrophosphate synthetase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and 3-hydroxy-3-methylglutaryl coenzyme A synthase by phorbol ester
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Genomic screening of fibroblast growth-factor receptor 2 reveals a wide spectrum of mutations in patients with syndromic craniosynostosis
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Human pancreatic islets express mRNA species encoding two distinct catalytically active isoforms of group VI phospholipase A2 (iPLA2) that arise from an exon-skipping mechanism of alternative splicing of the transcript from the iPLA2 gene on chromosome 22q13.1
Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate acyltransferase, a key enzyme in de novo triacylglycerol synthesis
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The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase
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Chromosomal localization of the gene for human glucosamine-6-sulphatase to 12q14
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The in vitro replication of DNA containing the SV40 origin.
Human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A synthase: expression, purification, and characterization of recombinant wild-type and Cys129 mutant enzymes
Thematic Review Series: Proteomics. An integrated omics analysis of eicosanoid biology
cDNA cloning of mouse and human cholesterol 25-hydroxylases, polytopic membrane proteins that synthesize a potent oxysterol regulator of lipid metabolism
ATP binding/hydrolysis by and phosphorylation of peroxisomal ATP-binding cassette proteins PMP70 (ABCD3) and adrenoleukodystrophy protein (ABCD1)
MutLalpha and proliferating cell nuclear antigen share binding sites on MutSbeta
Large-scale proteomic analysis of the human spliceosome.
hMSH3 and hMSH6 interact with PCNA and colocalize with it to replication foci
Control of hippocampal dendritic spine morphology through ephrin-A3/EphA4 signaling
WW domain-containing protein YAP associates with ErbB-4 and acts as a co-transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that translocates to the nucleus
Ligand regulates epidermal growth factor receptor kinase specificity: activation increases preference for GAB1 and SHC versus autophosphorylation sites
beta-Hydroxy-beta-methylglutaryl coenzyme A
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Na+/Ca2+-K+ exchangers (NCKX): functional properties and physiological roles
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DPC4/SMAD4 gene alterations in human cancer, and their functional implications
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Cytoplasmic chaperonin containing TCP-1: structural and functional characterization
The lipid phosphatase activity of PTEN is critical for its tumor supressor function
Cloning and analysis of unique human glutaminase isoforms generated by tissue-specific alternative splicing
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The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses
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Identification of peroxisomal acyl-CoA thioesterases in yeast and humans
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Pygopus and Legless target Armadillo/beta-catenin to the nucleus to enable its transcriptional co-activator function
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Subcellular localization and physiological role of alpha-methylacyl-CoA racemase
N (epsilon)-(carboxymethyl)lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction
Collagen cross-linking: lysyl oxidase dependent synthesis of pyridinoline in vitro: confirmation that pyridinoline is derived from collagen
Biochem. Biophys. Res. Commun. 108:1546-50
Mitochondrial and peroxisomal targeting of 2-methylacyl-CoA racemase in humans
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Fibroblast Growth Factor Receptor (FGFR) signaling
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Mutational spectrum of beta-catenin, AXIN1, and AXIN2 in hepatocellular carcinomas and hepatoblastomas
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The 10+4 microfibril structure of thin cartilage fibrils
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Transport of Mature Transcript to Cytoplasm
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The human ATP-binding cassette (ABC) transporter superfamily
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Glucokinase and molecular aspects of liver glycogen metabolism
Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase
Cloning and expression of a cDNA encoding human sterol carrier protein 2
Structure, function, and control of phosphoinositide-specific phospholipase C
5-Acetamido-3,5-dideoxy-D-glycero-D-galacto-2-nonulosonic acid
A novel skeletal dysplasia with developmental delay and acanthosis nigricans is caused by a Lys650Met mutation in the fibroblast growth factor receptor 3 gene
Molecular enzymology of carnitine transfer and transport
Extracellular Protein Interactions Mediated by the Neural Cell Adhesion Molecule, NCAM: Heterophilic Interactions Between NCAM and Cell Adhesion Molecules, Extracellular Matrix Proteins, and Viruses
The expanding role of mitochondria in apoptosis.
1-acylglycerol-3-phosphate O-acyltransferase 9
1-acylglycerol-3-phosphate O-acyltransferase 8
A role for the malonyl-CoA/long-chain acyl-CoA pathway of lipid signaling in the regulation of insulin secretion in response to both fuel and nonfuel stimuli
Aquaporin-11: a channel protein lacking apparent transport function expressed in brain
Lysophosphatidic acid acyltransferase-alpha
1-acylglycerol-3-phosphate O- acyltransferase 1
1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
Lysophosphatidic acid acyltransferase-beta
1-acylglycerol-3-phosphate O- acyltransferase 2
1-acyl-sn-glycerol-3-phosphate acyltransferase beta
1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
1-acylglycerol-3-phosphate O-acyltransferase 5
Lysophosphatidic acid acyltransferase-epsilon
Nicotinamide N-methyltransferase knockdown protects against diet-induced obesity
solute carrier family 25 (carnitine/acylcarnitine translocase), member 20
carnitine palmitoyltransferase 1B (muscle)
Growth of collagen fibril seeds from embryonic tendon: fractured fibril ends nucleate new tip growth
The human AQP4 gene: definition of the locus encoding two water channel polypeptides in brain
carnitine palmitoyltransferase 1A (liver)
Elongation of very long chain fatty acids protein 6
acyl-CoA synthetase long-chain family member 5
Elongation of very long chain fatty acids protein 3
acyl-CoA synthetase long-chain family member 1
A protein interaction framework for human mRNA degradation
Identification of a human heme exporter that is essential for erythropoiesis
1-acylglycerol-3-phosphate O-acyltransferase 6
Glycerol-3-phosphate acyltransferase, mitochondrial
Glycerol-3-phosphate dehydrogenase 1-like protein
Glycerol-3-phosphate dehydrogenase (NAD+), cytoplasmic
Serotonin Neurotransmitter Release Cycle
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SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases
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Two forms of collagen XVII in keratinocytes. A full-length transmembrane protein and a soluble ectodomain
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Protein kinase C alpha-dependent phosphorylation of the mRNA-stabilizing factor HuR: implications for posttranscriptional regulation of cyclooxygenase-2
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Regulation and functions of Rho-associated kinase
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Characterization of the novel human serotonin receptor subunits 5-HT3C,5-HT3D, and 5-HT3E
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Enoyl-CoA hydratase, mitochondrial precursor
Long chain 3-hydroxyacyl-CoA dehydrogenase
Trifunctional enzyme alpha subunit, mitochondrial precursor
Acyl-CoA dehydrogenase, long-chain specific, mitochondrial precursor
Large conductance, Ca2+-activated K+ channels (BKCa) and arteriolar myogenic signaling
Differential stimulation of cholesterol and unsaturated fatty acid biosynthesis in cells expressing individual nuclear sterol regulatory element-binding proteins
short chain 3-hydroxyacyl-CoA dehydrogenase monomer
Medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase
Short chain 3-hydroxyacyl-CoA dehydrogenase, mitochondrial precursor
Acyl-CoA dehydrogenase, very-long-chain specific, mitochondrial precursor
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Trifunctional enzyme beta subunit, mitochondrial precursor
Molecular cloning and identification of 3'-phosphoadenosine 5'-phosphosulfate transporter
Free fatty acids regulate insulin secretion
Crystal structure of pyruvate dehydrogenase phosphatase 1 and its functional implications
Coupling of the alpha 2-adrenergic receptor to the inhibitory G-protein Gi and adenylate cyclase in HT29 cells
Close homolog of L1 is an enhancer of integrin-mediated cell migration
Cloning, distribution and functional expression of the human mGlu6 metabotropic glutamate receptor
The MIA system for protein import into the mitochondrial intermembrane space
Differential mechanism of G-protein activation induced by endogenous mu-opioid peptides, endomorphin and beta-endorphin
Modulation of mitochondrial membrane permeability in pathogenesis, autophagy and control of metabolism
5-phospho-alpha-D-ribose 1-diphosphate [ChEBI:17111]
Inhibition of the Wnt signaling pathway by Idax, a novel Dvl-binding protein
Myosin-X induces filopodia by multiple elongation mechanism
Purification, properties, and sequencing of aminoisobutyrate aminotransferases from rat liver
Human Wapl is a cohesin-binding protein that promotes sister-chromatid resolution in mitotic prophase
Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein
Cathepsin S required for normal MHC class II peptide loading and germinal center development
The mRNA for alpha 1(XIX) collagen chain, a new member of FACITs, contains a long unusual 3' untranslated region and displays many unique splicing variants
Inositol polyphosphate 5-phosphatase OCRL-1
Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2
Repression of human heat shock factor 1 activity at control temperature by phosphorylation
The general transcription factors of RNA polymerase II.
Downstream signaling events of B Cell Receptor (BCR)
Amino acid transport across mammalian intestinal and renal epithelia
Acyl-coenzyme A synthetases in metabolic control
Lipin is required for efficient breakdown of the nuclear envelope in Caenorhabditis elegans
Inactivation of the C. elegans lipin homolog leads to ER disorganization and to defects in the breakdown and reassembly of the nuclear envelope
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Cloning and characterization of a mammalian lithium-sensitive bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate
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Demonstration of a specific mitochondrial isovaleryl-CoA dehydrogenase deficiency in fibroblasts from patients with isovaleric acidemia.
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The proline-rich homeodomain protein recruits members of the Groucho/Transducin-like enhancer of split protein family to co-repress transcription in hematopoietic cells
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CDG-IL: an infant with a novel mutation in the ALG9 gene and additional phenotypic features
Identification and characterization of a major liver lysophosphatidylcholine acyltransferase
Identification of a colon mucosa gene that is down-regulated in colon adenomas and adenocarcinomas
Haplotype analysis suggests that the two predominant mutations in Japanese patients with holocarboxylase synthetase deficiency are founder mutations
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Biochemistry, physiology, and genetics of GPAT, AGPAT, and lipin enzymes in triglyceride synthesis
Am J Physiol Endocrinol Metab 296:E1195-209
Hexosamine biosynthetic pathway mutations cause neuromuscular transmission defect
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Cancer progression and tumor cell motility are associated with the FGFR4 Arg(388) allele
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Functional characterization of NBC4: a new electrogenic sodium-bicarbonate cotransporter
ribose 1-phosphate, deoxyribose 1-phosphate
Germ-layer specification and control of cell growth by Ectodermin, a Smad4 ubiquitin ligase
Cloning and characterization a novel human 1-acyl-sn-glycerol-3-phosphate acyltransferase gene AGPAT7
The RNA polymerase II elongation complex.
Distinct transcriptional control and action of fibroblast growth factor receptor 4 in differentiating skeletal muscle cells
Diacylglycerol metabolism and arachidonic acid release in human fetal membranes and decidua vera
Purification and subunit structure studies of human placental threonyl-tRNA synthetase
The oxidation of pyruvate in pigeon breast muscle
Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
Alkyldihydroxyacetonephosphate synthase, peroxisomal precursor
Alkyldihydroxyacetonephosphate synthase precursor
Isocitrate dehydrogenase (NADP) cytoplasmic
Acyl- CoA:dihydroxyacetonephosphateacyltransferase
Dihydroxyacetone phosphate acyltransferase
Human heat shock factor 1 is predominantly a nuclear protein before and after heat stress
Identification of cross-linking sites in bovine cartilage type IX collagen reveals an antiparallel type II-type IX molecular relationship and type IX to type IX bonding
Isopentenyl-diphosphate delta-isomerase 1
Sterol regulatory element-binding protein 2
Sterol regulatory element-binding protein 1
Sterol regulatory element-binding protein 1A
Sterol regulatory element-binding protein cleavage-activating protein
Characterization of protein synthesis factors from rabbit reticulocytes
(R,R)-3,3'-thiobis-(2-aminopropanoic acid)
(R,R)-2,6-diamino-4-thiaheptanedioic acid
Elongation factor 1 beta of artemia: localization of functional sites and homology to elongation factor 1 delta
Complementation of Saccharomyces cerevisiae coq7 mutants by mitochondrial targeting of the Escherichia coli UbiF polypeptide: two functions of yeast Coq7 polypeptide in coenzyme Q biosynthesis
An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
Bile acid-CoA:amino acid N-acetyltransferase
ATP-binding cassette sub-family B member 11
Phosphorylation of the protein kinase C-theta activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-kappaB induction
Sterol regulatory element-binding protein 1C
Patatin-like phospholipase domain-containing protein 2
Calcium-dependent phospholipase A2 precursor
Calcium-independent phospholipase A2-epsilon
Patatin-like phospholipase domain-containing protein 3
A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery
A unified nomenclature for protein subunits of mediator complexes linking transcriptional regulators to RNA polymerase II
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Non-pancreatic secretory phospholipase A2
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glycerol-3-phosphate acyltransferase 2, mitochondrial
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Cloning and characterization of a functional human gamma-aminobutyric acid (GABA) transporter, human GAT-2
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(deoxy)cytidine, thymidine, (deoxy)uridine
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Cell signaling by receptor tyrosine kinases
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Monoamine metabolism and behavioral responses to ethanol in mitochondrial aldehyde dehydrogenase knockout mice
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Variant apolipoprotein AI as a major constituent of a human hereditary amyloid
Formation of the Early Elongation Complex
Sequence, tissue distribution, and chromosomal localization of mRNA encoding a human glucose transporter-like protein
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Structural basis of guanine nucleotide exchange mediated by the T-cell essential Vav1
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Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates
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Molecular cloning of a human, hemicholinium-3-sensitive choline transporter
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Syndecan signaling: when, where and why?
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Immunolocalization of AQP9 in liver, epididymis, testis, spleen, and brain
Cyclic AMP raises intracellular Ca(2+) in human megakaryocytes independent of protein kinase A
FRS2 family docking proteins with overlapping roles in activation of MAP kinase have distinct spatial-temporal patterns of expression of their transcripts
Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs
Am J Physiol Endocrinol Metab 284:E855-62
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The granulocyte-macrophage colony-stimulating factor receptor: linking its structure to cell signaling and its role in disease
Molecular cloning of the cDNA encoding a human renal sodium phosphate transport protein and its assignment to chromosome 6p21.3-p23
Next generation sequencing in a family with autosomal recessive Kahrizi syndrome (OMIM 612713) reveals a homozygous frameshift mutation in SRD5A3
Determinants of function and substrate specificity in human UDP-galactose 4'-epimerase
Intracellular signaling by the neural cell adhesion molecule
C1q binds directly and specifically to surface blebs of apoptotic human keratinocytes: complement deficiency and systemic lupus erythematosus revisited
2,4-dienoyl-CoA reductase, mitochondrial precursor
Acyl-CoA dehydrogenase, medium-chain specific, mitochondrial precursor
Hydroxymethylglutaryl-CoA lyase, mitochondrial (EC 4.1.3.4) (HMG-CoA lyase) (HL) (3-hydroxy-3-methylglutarate-CoA lyase)
Hydroxymethylglutaryl-CoA synthase, mitochondrial precursor
3-hydroxy-3-methylglutaryl coenzyme A synthase
Succinyl-CoA:3-ketoacid-coenzyme A transferase, mitochondrial precursor
Acetyl-CoA acetyltransferase, mitochondrial
Human Scc4 is required for cohesin binding to chromatin, sister-chromatid cohesion, and mitotic progression
A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
The nonsense-mediated decay RNA surveillance pathway
Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure
A model organism approach: defining the role of Neph proteins as regulators of neuron and kidney morphogenesis
Molecular cloning of AMP deaminase isoform L. Sequence and bacterial expression of human AMPD2 cDNA
Long-chain fatty acid transport protein 1
3-hydroxy-3-methylglutaryl-coenzyme A reductase-1
Nuclear transcription factor Y subunit gamma
ATP-binding cassette sub-family A member 1
A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes
Peroxisomal multifunctional enzyme type 2
hydroxysteroid (17-beta) dehydrogenase 4
Biotinidase deficiency: "if you have to have an inherited metabolic disease, this is the one to have"
Peroxisome proliferator-activated receptor alpha
Ral guanine nucleotide dissociation stimulator-like 1
Global defects in collagen secretion in a Mia3/TANGO1 knockout mouse
Thioredoxin reductase, cytoplasmic precursor
Thioredoxin reductase, cytoplasmic precursor (EC 1.8.1.9) (TR)
T-lymphoma invasion and metastasis-inducing protein 2
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Cloning, expression and characterization of the pig liver GDP-mannose pyrophosphorylase. Evidence that GDP-mannose and GDP-Glc pyrophosphorylases are different proteins
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Isolation and initial characterization of the single polypeptide that synthesizes uridine 5'-monophosphate from orotate in Ehrlich ascites carcinoma. Purification by tandem affinity chromatography of uridine-5'-monophosphate synthase
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Molecular and cellular mechanisms of altered GAD1/GAD67 expression in schizophrenia and related disorders
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Replication factors required for SV40 DNA replication in vitro. II. Switching of DNA polymerase alpha and delta during initiation of leading and lagging strand synthesis.
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Vertebrate shugoshin links sister centromere cohesion and kinetochore microtubule stability in mitosis
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WW domain-containing proteins, WWOX and YAP, compete for interaction with ErbB-4 and modulate its transcriptional function
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Inactivation of menin, a Smad3-interacting protein, blocks transforming growth factor type beta signaling
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NaPO(4) cotransport type III (PiT1) expression in human embryonic kidney cells and regulation by PTH
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Retinaldehyde is a substrate for human aldo-keto reductases of the 1C subfamily
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Interactions between UPF1, eRFs, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathways
WGEF activates Rho in the Wnt-PCP pathway and controls convergent extension in Xenopus gastrulation
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negative regulation of TCF-dependent signaling by DVL-interacting proteins
A new human hereditary amyloidosis: the result of a stop-codon mutation in the apolipoprotein AII gene
Spectrum of mutations in MMACHC, allelic expression, and evidence for genotype-phenotype correlations
Identification of an endocytosis motif in an intracellular loop of Wntless protein, essential for its recycling and the control of Wnt protein signaling
Human acid ceramidase gene: novel mutations in Farber disease
Pathways of DNA double-strand break repair during the mammalian cell cycle.
Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade
Signal transduction, cell cycle regulatory, and anti-apoptotic pathways regulated by IL-3 in hematopoietic cells: possible sites for intervention with anti-neoplastic drugs
Characterization of the gene encoding human peroxisomal 3-oxoacyl-CoA thiolase (ACAA). No large DNA rearrangement in a thiolase-deficient patient
Studies on the metabolic fate of n-3 polyunsaturated fatty acids
Mothers against decapentaplegic homolog 4
Mothers against decapentaplegic homolog 3
Mothers against decapentaplegic homolog 2
Histone demethylase JMJD3 contributes to epigenetic control of INK4a/ARF by oncogenic RAS
PP2A -56 kDa regulatory subunit B epsilon isoform
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4A-ARF locus in response to oncogene- and stress-induced senescence
Wnt-Ryk signalling mediates medial-lateral retinotectal topographic mapping
Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway
Probable ubiquitin carboxyl-terminal hydrolase FAF-X
Homologues of 2xADPRib-p-S423,S425-SMAD3
Glutathione-S-transferase P1 is a critical regulator of Cdk5 kinase activity
Rad51 recombinase and recombination mediators.
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform
PP2A- 56 kDa regulatory subunit, alpha isoform
Epac-selective cAMP analog 8-pCPT-2'-O-Me-cAMP as a stimulus for Ca2+-induced Ca2+ release and exocytosis in pancreatic beta-cells
2-acyl-sn-glycero-3-phospho-D-myo-inositol [ChEBI:62746]
1-acyl-sn-glycero-3-phosphoglycerol [ChEBI:62747]
Affixin interacts with alpha-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell-substrate interaction
NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest
HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia
Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
Linking colorectal cancer to Wnt signaling
Hepatocyte nuclear factor-1alpha recruits the transcriptional co-activator p300 on the GLUT2 gene promoter
Hepatic and neuromuscular forms of glycogen storage disease type IV caused by mutations in the same glycogen-branching enzyme gene.
Purification and partial amino acid sequence of human aconitase
The kinetics of aflatoxin B1 oxidation by human cDNA-expressed and human liver microsomal cytochromes P450 1A2 and 3A4
Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent
Cloning and characterization of a mammalian fatty acyl-CoA elongase as a lipogenic enzyme regulated by SREBPs
Role of second messengers in netrin-1 signaling
A drug targeting only p110? can block phosphoinositide 3-kinase signalling and tumour growth in certain cell types
Structural analysis and detection of biological inositol pyrophosphates reveal that the family of VIP/diphosphoinositol pentakisphosphate kinases are 1/3-kinases
SLC34A3 mutations in patients with hereditary hypophosphatemic rickets with hypercalciuria predict a key role for the sodium-phosphate cotransporter NaPi-IIc in maintaining phosphate homeostasis
Pyruvate carboxylase, mitochondrial precursor
methylcrotonyl-CoA carboxylase beta chain
methylcrotonyl-CoA carboxylase alpha chain
Movement of tRNA but not the nascent peptide during peptide bond formation on ribosomes
Biotin--protein ligase ecNumber6.3.4.-/ecNumber
Propanoyl-CoA:carbon dioxide ligase beta subunit
Propionyl-CoA carboxylase beta chain, mitochondrial precursor
Propanoyl-CoA:carbon dioxide ligase alpha subunit
propionyl-CoA carboxylase alpha chain, apoprotein
Propionyl-CoA carboxylase alpha chain, mitochondrial precursor
GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking
Multidrug resistance-associated protein 1
Aldehyde oxidase ecNumber1.2.3.1/ecNumber
Rapid secretion of interleukin-1beta by microvesicle shedding
Methylmalonic aciduria and homocystinuria type C protein
Methylmalonic aciduria and homocystinuria type D protein, mitochondrial
Methylmalonic aciduria type A protein, mitochondrial ecNumber3.6.-.-/ecNumber
Methylmalonyl-CoA mutase, mitochondrial precursor
Phosphopantothenoylcysteine decarboxylase
alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase
FAD1 flavin adenine dinucleotide synthetase homolog
Ectonucleotide pyrophosphatase/phosphodiesterase 1
Tartrate-resistant acid phosphatase type 5
Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis
Nicotinamide mononucleotide adenylyltransferase 2
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Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
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Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells
4-hydroxy-17beta-estradiol [ChEBI:62845]
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A conserved cyclin-binding domain determines functional interplay between anaphase-promoting complex-Cdh1 and cyclin A-Cdk2 during cell cycle progression
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Mitochondrial Cu,Zn-superoxide dismutase mediates pulmonary fibrosis by augmenting H2O2 generation
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Human interleukin-1 receptor-associated kinase-2 is essential for Toll-like receptor-mediated transcriptional and post-transcriptional regulation of tumor necrosis factor alpha
Comprehensive genomic characterization defines human glioblastoma genes and core pathways
The collagen fibril: the almost crystalline structure
BMAL1:CLOCK,NPAS2 activates circadian gene expression
Oligopeptide biases in protein sequences and their use in predicting protein coding regions in nucleotide sequences
Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides
Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA
IL-1beta induces stabilization of IL-8 mRNA in malignant breast cancer cells via the 3' untranslated region: Involvement of divergent RNA-binding factors HuR, KSRP and TIAR
1-diphospho-1D-myo-inositol (2,3,4,5,6)pentakisphosphate [ChEBI:62919]
1-diphospho-1D-myo-inositol (2,3,4,5,6)pentakisphosphate
Mechanisms of action of glucagon-like peptide 1 in the pancreas
Activation of Cyclin B/Cdk1 by Cdc25a (string) protein
Phosphorylation of Cyclin E2:Cdk2 complexes by Myt1
Dephosphorylation of Cyclin E:Cdk2 complexes by Cdc25A
Degradation of ubiquitinated p27/p21 by the 26S proteasome
Phosphorylation of Cyclin E1:Cdk2 complexes by Myt1
DNA polymerase epsilon binds at the origin
Human mismatch repair: reconstitution of a nick-directed bidirectional reaction
Detection of damage during initiation of DNA synthesis in S-phase
CAK-mediated phosphorylation of Cyclin E:Cdk2
DNA polymerase alpha:primase binds at the origin
Association of Cks1 with SCF(Skp2) complex
Translocation of Cyclin E:Cdk2 complex to the nucleus
p107 (RBL1) in complex with E2F4:DP1/2 binds to cyclin E/A:CDK2
p130 (RBL2) in complex with E2F4/5:DP1/2 binds to cyclin E/A:CDK2
Dephosphorylation of p107 (RBL1) by PP2A
Dephosphorylation of p130 (RBL2) by PP2A
Phosphorylated p130 (RBL2) binds SCF(Skp2):Cks1 complex
Ubiquitination of p130 (RBL2) by SCF (Skp2)
Translocation of active Cdc25C to the nucleus
Relocalization of nuclearly localized Cyclin D1 to the cytoplasm
Proteasome mediated degradation of Cyclin D1
Phosphorylation of Cyclin D1 at T286 by glycogen synthase kinase-3 beta
Relocalization of nuclearly localized phospho-(T286):cyclin D1:Cdk4 to cytoplasm
Polo-like kinase is required for the fragmentation of pericentriolar Golgi stacks during mitosis
RFC dissociates after sliding clamp formation
Loading of PCNA - Sliding Clamp Formation
Multiple proteins are localized at replication fork
Phosphorylated Cdc6 is exported from the nucleus
Ubiquitinated Cdc6 is degraded by the proteasome
Mcm4,6,7 trimer forms and associates with the replication fork
Rearrangement and mobilization of Mcm2-7
Phosphorylated Orc1 is ubiquitinated while still associated with chromatin
Ubiquitinated Orc1 is degraded by the proteasome
Critical role for the docking-protein FRS2 alpha in FGF receptor-mediated signal transduction pathways
The primase component of DNA polymerase:primase synthesizes a 6-10 nucleotide RNA primer at the origin
The polymerase component of DNA polymerase alpha:primase synthesizes a 20-nucleotide primer at the origin
Dab2 is recruited to the junctional plaques
Dynamin is recruited to the gap junction plaque
Phospholipases and phagocytosis: the role of phospholipid-derived second messengers in phagocytosis
trans-Golgi Network Lysosomal Vesicle Scission
Vamp2 associated secretory vesicle to plasma membrane transport
Vamp8 associated secretory vesicle to plasma membrane transport
Lysyl hydroxylase-2b directs collagen cross-linking pathways in MC3T3-E1 cells
Sculpting and pinching-off of Golgi vessicle
Coatomer:Arf1-GTP:GAP lattice formation on golgi membrane
Diffusion of inactive Arf1-GDP from membrane
Human alpha-galactosidase A: nucleotide sequence of a cDNA clone encoding the mature enzyme
Transcription of E2F targets under negative control by DREAM complex
Inactivation of APC/C via CDC20 sequestration
Phosphorylation of Cdc25C at Ser 216 by Chk1
Recruitment of the Rad9-Hus1-Rad1 complex to DNA
Myt-1 mediated phosphorylation of Cyclin B:Cdc2 complexes
Retention of phospho-Cdc25C:14-3-3 complexes within the cytoplasm
Proteolytic degradation of ubiquitinated-Cdc25A
Phosphorylation and activation of Chk1 by ATM
Phosphorylation of Cdc25A at Ser-123 by Chk1
Phosphorylation and activation of CHK2 by ATM
GLUT4 vesicle fuses with the plasma membrane
Translocation of GLUT4 Vesicle translocates and docks at the plasma membrane
Phosphorylation of Cdc25A at Ser-123 by Chk2
Phosphorylation of Cdc25A at Ser-123 in response to DNA damage
A novel inhibitor of beta-glucuronidase: L-aspartic acid
The third 20 amino acid repeat is the tightest binding site of APC for beta-catenin
Nuclear-cytoplasmic shuttling of Chibby controls beta-catenin signaling
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 1
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 2
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 3
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 4
Polyamines are oxidized to amines, aldehydes and H2O2 by PAOs
1,5-bisdiphosphoinositol-1D-myo-inositol (3,4,6)trisphosphate
1,5-bisdiphosphoinositol-1D-myo-inositol (3,4,6)trisphosphate [ChEBI:62931]