Once biotinylated, three halocarboxylases (hCBXs) are localised to the mitochondrial matrix. The mechanism of transfer is still unclear. Pyruvate carboxylase (PC) is required for gluconeogenesis, lipogenesis, neurotransmitter synthesis and insulin secretion; Methylcrotonyl-CoA carboxylase (MCC) is required for amino acid metabolism; propionyl-CoA carboxylase (PCC) is required for odd-chain fatty acid oxidation (Ingaramo & Beckett 2012, Hiratsuka et al. 1998, Bailey et al. 2010).
Biotin (Btn) acts as a coenzyme to 4 carboxylases which exist in their inactive apo forms. In the cytosol, these apo carboxylases are biotinylated to their active halo forms by the activity of biotin-protein ligase (HCLS) (Ingaramo & Beckett 2012, Hiratsuka et al. 1998, Bailey et al. 2010). Defects in HLCS causes holocarboxylase synthetase deficiency (HLCS deficiency aka biotin-responsive multiple carboxylase deficiency; MIM:253270). HLCS deficiency is an autosomal recessive disorder whereby deficient HLCS activity results in reduced activity of multiple carboxylases. Symptoms include metabolic acidosis, organic aciduria, lethargy, hypotonia, convulsions and dermatitis (Suzuki et al. 2005). Acetyl-CoA carboxylases 1 and 2 (ACACA and ACACB) bind 2 Mn2+ and 1 Btn per subunit (Colbert et al. 2010). They can exist as either monomers, homodimers or homotetramers (latter two not shown in this reaction) (Magnard et al. 2002, Moreau et al. 2006). Unlike the other carboxylases acted upon by HCLS, ACACA and B are located in the cytosol (shown here) as well as the mitochondrial membrane. The exact order in which this complex is constructed is unknown.
Biotin (Btn) acts as a coenzyme to 4 carboxylases which exist in their inactive apo forms. In the cytosol, these apo carboxylases are biotinylated to their active halo forms by the activity of biotin-protein ligase (HCLS) (Ingaramo & Beckett 2012, Hiratsuka et al. 1998, Bailey et al. 2010). Defects in HLCS causes holocarboxylase synthetase deficiency (HLCS deficiency aka biotin-responsive multiple carboxylase deficiency; MIM:253270). HLCS deficiency is an autosomal recessive disorder whereby deficient HLCS activity results in reduced activity of multiple carboxylases. Symptoms include metabolic acidosis, organic aciduria, lethargy, hypotonia, convulsions and dermatitis (Suzuki et al. 2005). Methylcrotonoyl-CoA carboxylase is most likely functional as a dodecamer, composed of 6 Btn-containing alpha subunits (MCCC1) and six beta subunits (MCCC2). The exact order in which this complex is constructed is unknown.
The enzyme, nicotinate nucleotide pyrophosphorylase, is specific for quinolinate. Its activity is strictly dependent on Mg2+ ions being present. A phosphoribosyl group is transferred to quinolinate to form nicotinate D-ribonucleotide. This reaction represents another rate-limiting step of the pathway from tryptophan to NAD+.
NMNAT1 catalyzes the reaction of nicotinate D-ribonucleotide and ATP to form deamino-NAD+ (nicotinate adenine dinucleotide) and pyrophosphate (Schweiger et al. 2001). The active form of the enzyme in vitro is a hexamer (Zhou et al. 2002), and its activity is substantially greater in the presence of Zn++ than of Mg++ (Sorci et al. 2007). The predicted amino acid sequence of the enzyme contains a nuclear localization domain and the protein is observed to localize to the nucleus (Schweiger et al. 2001; Berger et al. 2005).
Human biotinidase (BTD) (Cole et al. 1994) is a secreted enzyme that catalyzes the hydrolysis of biocytin (BCTN), the product of biotin-dependent carboxylase degradation, to biotin (Btn) and lysine. BTD deficiency, an autosomal recessive disorder, results in a secondary Btn deficiency that leads to late-onset multiple carboxylase deficiency (MIM:253260) (Wolf et al. 1983).
Biotin (Btn) is an essential cofactor in a variety of carboxylation reactions (Zempleni et al. 2009). Humans cannot synthesize Btn but it is abundant in the human diet and can be taken up from the intestinal lumen by the SLC5A6 transporter. Its uptake, intracellular translocation, covalent conjugation to apoenzymes, and salvage are described here.
NAD synthase catalyzes the final step in the biosynthesis of NAD+, both in the de novo synthesis and in the salvage pathways. The enzyme makes use of glutamine as an amide donor in the reaction. NAD synthase exists as a homohexamer in the cytosol. There are two forms of NAD synthase in humans, NADsyn1 and NADsyn2. The major difference between the two forms is that NADsyn1 appears to be glutamine-dependent whereas NADsyn2 is strictly ammonia-dependent.
NMNAT2 catalyzes the reaction of nicotinate D-ribonucleotide and ATP to form deamino-NAD+ (nicotinate adenine dinucleotide) and pyrophosphate (Sorci et al. 2007). The active form of the enzyme is a monomer in vitro (Raffaelli et al. 2002). Although the predicted amino acid sequence of the enzyme lacks an obvious signal sequence or transmembrane domain (Yalowitz et al. 2004), recombinant FLAG-tagged protein expressed in HeLa cells localizes predominantly to the Golgi apparatus (Berger et al. 2005). Its localization within the Golgi apparatus is unknown and the annotation here is based on the plausible but speculative assumption that the enzyme is associated with the Gogi membrane and accessible from the cytosol. Immunostaining studies indicate that the protein is abundant in Islets of Langerhans and in several regions of the brain (Yalowitz et al. 2004).
NMNAT3 catalyzes the reaction of nicotinate D-ribonucleotide and ATP to form deamino-NAD+ (nicotinate adenine dinucleotide) and pyrophosphate (Sorci et al. 2007). The active form of the enzyme is a tetramer in vitro (Zhang et al. 2003). Recombinant FLAG-tagged protein expressed in HeLa cells localizes both to the cytosol and to mitochondria (Berger et al. 2005). The cytosolic protein is annotated here.
Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations
Cloning and molecular analysis of the human citrate synthase gene
SLC25A32 protein in the inner mitochondrial membrane mediates the reversible transport of tetrahydrofolate between the cytosol and the mitochondrial matrix. Retention of tetrahydrofolate within the mitochondrial matrix is dependent on mitochondrial polyglutamate addition (Titus and Moran 2000; Chen et al. 1996).
NAD+ kinase catalyzes the transfer of a phosphate group from ATP to NAD+, forming NADP+. This is the only way to generate NADP+ in all living organisms. The enzyme requires a divalent metal to be effective. Zn2+ is the best metal for this purpose.
Cytosolic nicotinate phosphoribosyltransferase (NaPRT) catalyzes the Mg++-dependent reaction of nicotinate and phosphoribosyl pyrophosphate to form nicotinate mononucleotide (NaMN, nicotinate D-ribonucleotide) and pyrophosphate. The active form of the enzyme is a homodimer (Preiss and Handler 1958; Niedel and Dietrich 1973; Hara et al. 2007).
Nicotinamide levels are modulated by the action of three enzymes involved in nicotinamide salvaging. They are nicotinamide deaminase, nicotinamide phosphoribosyltransferase and nicotinate phosphoribosyltransferase. These enzymes are poorly characterized in humans, depsite their importance in nicotinamide utilization.
Nicotinate (niacin) and nicotinamide are precursors of the coenzymes nicotinamide-adenine dinucleotide (NAD+) and nicotinamide-adenine dinucleotide phosphate (NADP+). When NAD+ and NADP+ are interchanged in a reaction with their reduced forms, NADH and NADPH respectively, they are important cofactors in several hundred redox reactions. Nicotinate is synthesized from 2-amino-3-carboxymuconate semialdehyde, an intermediate in the catabolism of the essential amino acid tryptophan.
SLC19A1 protein, associated with the plasma membrane, mediates the uptake of extracellular 5-methyltetrahydrofolate and other reduced folates (Williams and Flintoff 1995; Ferguson and Flintoff 1999).
Cytosolic dihydrofolate reductase catalyzes the reaction of folate, NADPH, and H+ to form dihydrofolate and NADP+ (Chen et al. 1984; Davies et al. 1990).
Cytosolic dihydrofolate reductase catalyzes the reaction of dihydrofolate, NADPH, and H+ to form tetrahydrofolate (THF) and NADP+ (Chen et al. 1984; Davies et al. 1990).
Cytosolic folylpolyglutamate synthase catalyzes the reaction of THF-glutamate(n), L-glutamate, and ATP to form THF-glutamate(n+1), ADP, and orthophosphate. (The first glutamate residue is attached to the glutamate moiety of THF itself; for convenience the process is annotated here as if it proceeded in a single concerted step.) The extent of conjugation is variable, but the commonest cytosolic form of THF has five added glutamate residues. Although its properties as a donor of one-carbon units are not affected by glutamate addition, THF that lacks added glutamate residues cannot be retained in the cytosol so this reaction is needed for normal THF function under physiological conditions (Garrow et al. 1992; Chen et al. 1996).
Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI
Cytosolic folylpolyglutamate synthase catalyzes the reaction of 5-methylTHF-glutamate(n), L-glutamate, and ATP to form 5-methylTHF-glutamate(n+1), ADP, and orthophosphate. (The first glutamate residue is attached to the glutamate moiety of 5-methylTHF itself; for convenience the process is annotated here as if it proceeded in a single concerted step.) The extent of conjugation is variable, but the commonest cytosolic form of 5-methylTHF has five added glutamate residues. Although its properties as a donor of one-carbon units are not affected by glutamate addition, 5-methylTHF that lacks added glutamate residues cannot be retained in the cytosol so this reaction is needed for normal 5-methylTHF function under physiological conditions (Garrow et al. 1992; Chen et al. 1996).
Isolation of inositol 1,3,4-trisphosphate 5/6-kinase, cDNA cloning and expression of the recombinant enzyme
Sulfur transfer onto MOCS2A is closely preceded by its adenylylation and deadenylylation. After release of MOCS2A-CO-S(1-), two cysteines on MOCS3 form a disulfide bridge. This means that MOCS3 has to be reduced to be able to participate in the next round. The reducing agent is not known (Marelja et al, 2008).
In order to get a sulfur atom for subsequent sulfuration reactions, cysteine is first desulfurated by NFS1 which transfers it onto a cysteine of MOCS3, yielding a protein persulfide (Marelja et al, 2008).
The methenyltetrahydrofolate cyclohydrolase activity of the trifunctional MTHFD1 enzyme catalyzes the reversible reaction of 5,10-methenylTHF polyglutamate and H2O to form 10-formylTHF polyglutamate. MTHFD1 is cytosolic and occurs as a dimer. The human enzyme has been identified and partially characterized biochemically (Hum et al. 1988); additional reaction details can be inferred from the properties of the well-studied homologous rabbit enzyme (Villar et al. 1985).
Folates are essential cofactors that provide one-carbon moieties in various states of reduction for biosynthetic reactions. Processes annotated here include transport reactions by which folates are taken up by cells and moved intracellularly, folate conjugation with glutamate (required for folate retention within a cell), and some of the key reactions in the generation of reduced folates and one-carbon derivatives of folate.
Cytosolic MTHFR dimer catalyzes the reaction of 5,10-methyleneTHF polyglutamate, NADPH, and H+ to form 5-methylTHF polyglutamate and NADP+. The specificity and importance of this reaction in vivo have been established through the study of patients deficient in the enzyme (Goyette et al. 1995).
The methylenetetrahydrofolate dehydrogenase activity of the trifunctional MTHFD1 enzyme catalyzes the reversible reaction of 5,10-methyleneTHF polyglutamate and NADP+ to form 5,10-methenylTHF polyglutamate, NADPH, and H+. MTHFD1 is cytosolic and occurs as a dimer. The human enzyme has been identified and partially characterized biochemically (Hum et al. 1988); additional reaction details can be inferred from the properties of the well-studied homologous rabbit enzyme (Villar et al. 1985).
The methenyltetrahydrofolate cyclohydrolase activity of the trifunctional MTHFD1 enzyme catalyzes the reversible reaction of 10-formylTHF polyglutamate to form 5,10-methenylTHF polyglutamate and H2O. MTHFD1 is cytosolic and occurs as a dimer. The human enzyme has been identified and partially characterized biochemically (Hum et al. 1988); additional reaction details can be inferred from the properties of the well-studied homologous rabbit enzyme (Villar et al. 1985).
The methylenetetrahydrofolate dehydrogenase activity of the trifunctional MTHFD1 enzyme catalyzes the reversible reaction of 5,10-methenylTHF polyglutamate, NADPH, and H+ to form 5,10-methyleneTHF polyglutamate and NADP+. MTHFD1 is cytosolic and occurs as a dimer. The human enzyme has been identified and partially characterized biochemically (Hum et al. 1988); additional reaction details can be inferred from the properties of the well-studied homologous rabbit enzyme (Villar et al. 1985).
Mitochondrial folylpolyglutamate synthase catalyzes the reaction of THF-glutamate(n), L-glutamate, and ATP to form THF-glutamate(n+1), ADP, and orthophosphate. (The first glutamate residue is attached to the glutamate moiety of THF itself; for convenience the process is annotated here as if it proceeded in a single concerted step.) The extent of conjugation is variable, but the commonest mitochondrial form of THF has six added glutamate residues. Although its properties as a donor of one-carbon units are not affected by glutamate addition, THF that lacks added glutamate residues cannot be retained in the mitochondrial matrix so this reaction is needed for normal THF function under physiological conditions. The mitochondrial and cytosolic forms of folylpolyglutamate synthase are encoded by the same gene - alternative splicing generates mRNA with or without an initial exon encoding a mitochondrial targeting sequence (Garrow et al. 1992; Chen et al. 1996).
The formate-tetrahydrofolate ligase activity of the trifunctional MTHFD1 enzyme catalyzes the reaction of THF polyglutamate, formate, and ATP to form 10-formylTHF polyglutamate, ADP, and orthophosphate. MTHFD1 is cytosolic and occurs as a dimer. The human enzyme has been identified and partially characterized biochemically (Hum et al. 1988); additional reaction details can be inferred from the properties of the well-studied homologous rabbit enzyme (Villar et al. 1985).
GTP cyclizes in a reaction involving radicals of S-adenosylmethionine, catalyzed by the iron-sulfur cluster dimeric MOCS1. The intermediate result is called precursor Z (Hanzelmann et al, 2002; Hanzelmann et al, 2004).
A tandemly repeated sequence at the termini of the extrachromosomal ribosomal RNA genes in Tetrahymena
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. Water-soluble vitamins include ascorbate (vitamin C) and the members of the B group: thiamin (vitamin B1), riboflavin (B2), niacin (B3), pantothenate (B5), pyridoxine (B6), biotin (B7), folate (B9), and cobalamin (B12). Metabolic processes annotated here include the synthesis of thiamin pyrophosphate (TPP) from thiamin (B1), the synthesis of FMN and FAD from riboflavin (B2), the synthesis of nicotinic acid (niacin - B3) from tryptophan, the synthesis of Coenzyme A from pantothenate (B5), and features of the metabolism of folate (B9).
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.
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.
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.
After the MOCS2A dimer is loaded with two sulfur atoms, their sequential deposition on the precursor Z molecule, with ring cleavage, is catalyzed by the MOCS2B half of the MOCS2 tetramer (Leimkuhler et al, 2003; Wuebbens & Rajagopalan, 2002).
Gephyrin, which stabilizes receptors on neuronal membranes, also catalyzes the transfer of a molybdenum ion onto the cofactor. The mechanism was elucidated in plants but, as the pathway is highly conserved, human gephyrin can complement missing plant proteins. Doubts remain about the actual molybdenum donor, probably molybdate, and whether a copper ion is possibly bound and removed (Stallmeyer et al, 1999).
While the biosynthesis of the molybdenum cofactor for sulfite oxidase is finished after molybdenum ion insertion, human xanthine oxidase and aldehyde oxidase will only show activity with this cofactor when one of the oxygens bound to molybdenum is replaced with sulfur. The exchange is catalyzed by the MOCOS cysteine desulfurase (Ichida et al, 2001).
Molybdenum cofactor (MoCo) is needed by three enzymes in humans: sulfite oxidase, xanthine oxidase and aldehyde oxidase. The pathway of its synthesis is so conserved that plants and bacteria can readily use human enzymes. Bacteria, however, diverge after the first three steps from this path and their final MoCo differs from that of the eukaryotes. Plants and animals have also developed a refinement of their MoCo which is needed for the function of their xanthine and aldehyde oxidases. This means, in humans we find sulfurated instead of desulfurated molybdenum cofactor on these two enzymes (Schwarz 2005; Schwarz, Mendel, Ribbe 2009).
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).
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 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).
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).
Vitamin C (ascorbate) is an antioxidant and a cofactor in reactions catalyzed by Cu+-dependent monooxygenases and Fe++-dependent dioxygenases. Many mammals can synthesize ascorbate de novo; humans and other primates cannot due to an evolutionarily recent mutation in the gene catalyzing the last step of the biosynthetic pathway. Reactions annotated here mediate the uptake of ascorbate and its fully oxidized form, dehydroascorbate (DHA) by cells, and the reduction of DHA and monodehydroascorbate to regenerate ascorbate (Linster and Van Schaftingen 2007).
The uptake of extracellular dehydroascorbate into the cytosol is mediated by GLUT1 and GLUT3 associated with the plasma membrane (Rumsey et al. 1997, 2000). This process may play a significant role in ascorbate utilization in the central nervous system (Agus et al. 1997). The process is efficiently competitively inhibited by glucose, leading to the suggestion that inhibited dehydroascorbate uptake may contribute to the pathology of diabetes (Liang et al. 2001; Rumsey et al. 2000).
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".
Constitutive activation of fibroblast growth factor receptor 3 by mutations responsible for the lethal skeletal dysplasia thanatophoric dysplasia type I
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.
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).
Riboflavin (vitamin B2, E101) is an essential component for the cofactors FAD (flavin-adenine dinucleotide) and FMN (flavin mononucleotide). Together with NAD+ and NADP+, FAD and FMN are important hydrogen carriers and take part in more than 100 redox reactions involved in energy metabolism. Riboflavin is present in many vegetables and meat and during digestion, various flavoproteins from food are degraded and riboflavin is resorbed. The major degradation and excretion product in humans is riboflavin (Rivlin 1970).
Phosphatase action on flavin adenine dinucleotide (FAD) can reform flavin mononucleotide (FMN). The enzyme performing the reaction is nucleotide pyrophosphatase (ENPP1) and it exists as a homodimer on the plasma membrane.
The decarboxylation of phosphopantothenoylcysteine (PPC) to 4'-phosphopantetheine (PPANT) is carried out by phosphopantothenoylcysteine decarboxylase (PPCDC). PPCDC is cytosolic and exists as a homotrimer, binding one FMN cofactor per subunit. While a second isoform has been inferred from large-scale sequnceing studies, it lacks the protein's FMN-binding domain and would thus appear to be nonfunctional if it is expressed.
The conjugation of cysteine (Cys) and 4'- phosphopantothenate (PPanK) to form 4-phosphopantothenoylcysteine (PPC) , coupled to the conversion of ATP to AMP and pyrophosphate, is catalyzed by cytosolic phosphopantothenate-cysteine ligase (PPCS aka Phosphopantothenoylcysteine synthase or PPC synthase). Mammalian PPCS prefers ATP to CTP, unlike the E. coli ortholog (Daughtery et al. 2002; Manoj et al. 2003).
The kinase activity of CoA synthase (COASY) catalyzes the phosphorylation of dephospho-CoA to form Coenzyme A (CoA-SH). The enzyme is located in the mitochondrial outer membrane (Daugherty et al. 2002; Zhyvoloup et al. 2003).
The adenylyl transferase activity of bifunctional coenzyme A synthase (COASY) catalyzes the transfer of an adenylyl group from ATP to pantetheinephosphate (PPANT) to form dephospho-Coenzyme A (DP-CoA) (Daugherty et al. 2002). The enzyme is associated with the mitochondrial outer membrane (Zhyvoloup et al. 2003).
Enzyme-substrate intermediate formation at lysine 329 of human deoxyhypusine synthase
Cytosolic thiamin pyrophosphokinase (TPK1) catalyzes the reaction of thiamin (THMN) and ATP to form thiamin diphosphate (ThDP aka thiamin pyrophosphate) and ADP. ThDP is an active cofactor for transketolase, pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase, enzymes involved in glycolysis and energy production. The gene encoding the human enzyme has been cloned and its protein product has been shown to have TPK1 activity (Nosaka et al. 2001; Zhao et al. 2001). Its homodomeric structure and association with Mg2+ are inferred from properties of the homologous yeast enzyme (Baker et al. 2001).
Two transport proteins, SLC19A2 (THTR1) and SLC19A3 (THTR2), associated with the plasma membrane, are each able to mediate the transport of extracellular thiamin into the cytosol. In the body, both transporters are widely distributed, and both are abundant in kidney and intestinal epithelia, consistent with their involvement in thiamin uptake under physiological conditions (Ashokkumar et al. 2006; Said et al. 2004; Subramanian et al. 2006 - J Biol Chem). The observation that mutations in SLC19A2 (THTR1) cause a progressive disorder that can be partially reversed by treatment with high doses of thiamin likewise suggests a role for this protein in thiamin uptake under normal conditions (Diaz et al. 1999; Fleming et al. 1999; Labay et al. 1999). Two features of this transport process remain incompletely understood, however. First, mutations in SLC19A3 cause a progressive disorder that is responsive to biotin treatment (Zhou et al. 2005), although studies of cultured cells indicate that the protein has no affinity for biotin (Subramanian et al. 2006 - Am J Physiol). Also, studies to date provide little information about the mechanism by which thiamin, once taken up by epithelial cells in the intestine and kidney, is released from these cells into the blood.
7,8-dihydro-7-hydroxy-8S-glutathionylbenzo[a]pyrene [ChEBI:34479]
FMN can be phosphorylated and adenylated to produce the second cofactor from riboflavin origins, flavin adenine dinucleotide (FAD). The enzyme responsible , FMN adenylyltransferase (FLAD1 aka FAD synthase), is cytosolic and transfers a phosphate and an adenyl group from ATP to form FAD.
Vitamin B1 (thiamin) is found naturally in certain foodstuffs such as green peas, spinach, liver, bananas, whole grains and legumes. Human diseases associated with thiamin deficiency include beriberi, due to a thiamin-deficient diet, TMRA, due to defects in the SLC19A2 transport protein, and Wernicke-Korsakoff Syndrome, associated with thiamin deficiency in alcoholism (Haas 1988). Thiamin is water-soluble so is not stored in the body. When pyrophosphorylated, thiamin is converted into the coenzyme thiamin pyrophosphate (ThPP, codecarboxylase) which plays an essential role in oxidative decarboxylation and group transfer reactions.
Subcellular localization of 3-methylcrotonyl-coenzyme A carboxylase in bovine kidney
The probable lysosomal cobalamin transporter (LMBRD1) is the most likely candidate to transport cobalamin (Cbl) from inside the lysosome to the cytosol (Rutsch et al. 2009). From here, Cbl can either be used to synthesise the essential cofactors for methionine synthase in the cytosol or methylmalonyl-CoA mutase in the mitochondria or, it can transported out of the cell to tissues that require Cbl. Defects in LMBRD1 cause methylmalonic aciduria and homocystinuria type cblF (MMAHCF; MIM:277380), characterised biochemically by decreased levels of the coenzymes adenosylcobalamin (AdoCbl) and methylcobalamin (MetCbl) (Rutsch et al. 2009, Gailus et al. 2010).
Animals cannot synthesize pyridoxal 5'-phosphate (PLP) which is a ligand in aminotransferases and other enzymes. PLP's accessible derivatives pyridoxine, pyridoxal, and pyridoxamine are traditionally called vitamins B6. They are taken up nutritionally from bacteria and plants, but also created from PLP in the body. The pathways used to recycle PLP from these three compounds can therefore be called vitamin B6 activation as well as PLP salvage. Because of the close similarity of the molecules, only two enzymes are needed for the task (McCormick & Chen, 1999).
Pyridoxine-5'-phosphate oxidase (PNPO) is able to oxidize pyridoxine phosphate (PDXP) to pyridoxal 5'-phosphate (PXLP) (Kang et al. 2004).
Pyridoxine-5'-phosphate oxidase (PNPO) is able to oxidize pyridoxamine phosphate (PXAP) to pyridoxal 5'-phosphate (PXLP) (Kang et al. 2004).
Pyridoxal kinase (PDXK) catalyzes the ATP-dependent phosphorylation of pyridoxine (PDX) to form pyridoxine phosphate (PDXP) (Lee et al. 2000, di Salvo et al. 2004).
Pyridoxal kinase (PDXK) catalyzes the ATP-dependent phosphorylation of pyridoxamine (PXA) to form pyridoxamine phosphate (PXAP) (Lee et al. 2000, di Salvo et al. 2004).
Pyridoxal kinase (PDXK) catalyzes the ATP-dependent phosphorylation of pyridoxal (PXL) to form pyridoxal 5'-phosphate (PXLP) (Lee et al. 2000, di Salvo et al. 2004).
Panthothenate (vitamin B5) is the precursor of coenzyme A (Robishaw and Neely 1985) and is the prosthetic group of acyl carrier protein (ACP) (Joshi et al. 2003). Its name is derived from the Greek pantothen meaning "from everywhere" and small quantities of pantothenic acid are found in nearly every foodstuff.
Coenzyme A (CoA) is a ubiquitous cofactor that functions as an acyl group carrier in diverse processes including fatty acid metabolism and the TCA cycle (Lipmann 1953). It is synthesized from the vitamin pantothenate in a sequence of five reactions (Daugherty et al. 2002; Leonardi et al. 2005; Robishaw and Neely 1985). These reactions all occur in the cytosol or the mitochondrial intermembrane space (Leonardi et al. 2005). A recently described transport protein appears to mediate the uptake of Coenzyme A into the mitochondrial matrix (Prohl et al. 2001).
Graves disease carrier protein (SLC25A16), associated with the inner mitochondrial membrane, mediates the transport of cytosolic coenzyme A (CoA-SH) into the mitochondrial matrix. Evidence for this event is indirect. The protein has the sequence motifs expected for a transport protein, and yeast cells deficient in its homologue, Leu5p, fail to accumulate mitochondrial CoA-SH and can be rescued by expression of SLC25A16. At the same time, neither the yeast nor the human protein has been shown directly to function as a transporter (Prohl et al. 2001, Leonardi et al. 2007).
The molecular dissection of Fc gamma receptor mediated phagocytosis
Cloning and expression of a human ATP-citrate lyase cDNA
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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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Multidrug resistance-associated protein 1 (ABCC1, MRP1) can specifically mediate the ATP-dependant export of free cobalamin (Cbl aka vitamin B12) from small intestine cells to the portal vein (Shah et al. 2011).
Methylmalonyl-CoA mutase (MUT aka MCM) (Jansen et al. 1989) utilises adenosylcobalamin (AdoCbl) as a cofactor and transfers an adenosyl group from AdoCbl to methymalonyl-CoA to form succinyl-CoA, a precursor for the citric acid cycle. MUT has a homodimeric structure and is located in the mitochondrial matrix. Defects in MUT cause methylmalonic aciduria type mut (MMAM; MIM:251000), an often fatal disorder of organic acid metabolism (Worgan et al. 2006). Methylmalonic aciduria type A protein (MMAA) (Dobson et al. 2002) is thought to act as a chaperone to MUT and is suggested to play a dual role with regards to MUT protection and reactivation. Defects in MMAA cause methylmalonic aciduria type cblA (MMAA aka methylmalonic aciduria type A or vitamin B12-responsive methylmalonicaciduria of cblA complementation type; MIM:251100). Affected individuals accumulate methylmalonic acid in the blood and urine and are prone to potentially life threatening acidotic crises in infancy or early childhood (Dobson et al. 2002, Lerner-Ellis et al. 2004).
Biotin (Btn) acts as a coenzyme to 4 carboxylases which exist in their inactive apo forms. In the cytosol, these apo carboxylases are biotinylated to their active halo forms by the activity of biotin-protein ligase (HCLS) (Ingaramo & Beckett 2012, Hiratsuka et al. 1998, Bailey et al. 2010). Defects in HLCS causes holocarboxylase synthetase deficiency (HLCS deficiency aka biotin-responsive multiple carboxylase deficiency; MIM:253270). HLCS deficiency is an autosomal recessive disorder whereby deficient HLCS activity results in reduced activity of multiple carboxylases. Symptoms include metabolic acidosis, organic aciduria, lethargy, hypotonia, convulsions and dermatitis (Suzuki et al. 2005). Propionyl-CoA carboxylase is most likely functional as a dodecamer, composed of six Btn-containing alpha subunits (PCCA) and six beta subunits (PCCB). The exact order in which this complex is constructed is unknown.
Vitamin B12 (cobalamin, Cbl) is a water-soluble vitamin with a key role in blood formation and normal functioning of the brain and nervous system. Cbl consists of a planar corrin ring coordinating with a cobalt atom through four nitrogen atoms. A 5,6-dimethylbenzamidizole base coordinates with the cobalt atom in the lower axial position while a number of different species can coordinate with the cobalt atom in the upper axial position. It is the cobalt-corrin ring complex that gives all Cbls a deep red colour. Only bacteria and archaea are able to synthesize Cbl thus humans need a dietary intake to prevent deficiency (Green 2010, Quadros 2010, Watkins & Rosenblatt 2011). A common semi-synthetic form of the vitamin, cyanocobalamin (CNCbl, where a cyanide group is in the upper axial position), is produced from bacterial hydroxocobalamin and used in many pharmaceuticals, supplements and as a food additive. In mammalian cells, Cbl or CNCbl is converted to two active coenzyme derivatives; methylcobalamin (MetCbl) and adenosylcobalamin (AdoCbl). MetCbl is required for activity of the cytoplasmic enzyme methionine synthase, which converts homocysteine to methionine. AdoCbl is required for activity of the mitochondrial enzyme methylmalonyl CoA mutase, which converts L-methylmalonyl-CoA to succinyl-CoA (Seetharam 1999). This pathway outlines the intake, transport and metabolism of Cbl and is assumed to be equally applicable to CNCbl.
A methyl group from methylcobalamin (MeCbl) is transferred to homocysteine (HCYS), forming methionine (L-Met) (Leclerc et al. 1996). MTR is now in an inactive state as its cofactor state, B12r (cob(II)alamin), requires reduction to B12s (cob(I)alamin) to reactivate the enzyme. This is performed by methionine synthase reducatse (MTRR).
Methionine synthase (MTR) catalyses the transfer of a methyl group from 5-methyltetrahydrofolate (MTHF) to homocysteine (HCYS) to then form methionine (L-Met). In the first step, MTR mediates the transfer of a methyl group from 5-methyltetrahydrofolate (MTHF) to B12s (bound to the enzyme MTR) to form the cofactor methylcobalamin (MeCbl), the form that activates MTR (Leclerc et al. 1996). Defects in MTR cause methylcobalamin deficiency type G (cblG; MIM:250940), an autosomal recessive inherited disease that causes mental retardation, macrocytic anemia, and homocystinuria. Mutations causing cblG include P1173L, Ile881, H920D, R585*, E1204* and A1204P (Leclerc et al. 1996, Gulati et al. 1996, Watkins et al. 2002).
Mitochondrial cob(I)yrinic acid a,c-diamide adenosyltransferase (MMAB) is a dual purpose enzyme involved in the reduction and adenosylation of cobalamin. In the second step, MMAB transfers an adenosyl group from ATP to cob(I)alamin (B12s) to form adenosylcabalamin (AdoCbl) (Fan & Bobik 2008, Leal et al. 2003). Defects in MMAB cause methylmalonic aciduria type cblB (MMAB aka methylmalonic aciduria type B or vitamin B12-responsive methylmalonicaciduria of cblB complementation type; MIM:251110). Affected individuals have methylmalonic aciduria and metabolic ketoacidosis, despite a functional methylmalonyl-CoA mutase. In severe cases, newborns are lethargic, prone to vomiting and fail to thrive (Dobson et al. 2002).
Mitochondrial cob(I)yrinic acid a,c-diamide adenosyltransferase (MMAB) is a dual purpose enzyme involved in the reduction and adenosylation of cobalamin. In the first step, MMAB reduces cob(II)alamin (B12r) to cob(I)alamin (B12s) (Fan & Bobik 2008, Leal et al. 2003). Defects in MMAB cause methylmalonic aciduria type cblB (MMAB aka methylmalonic aciduria type B or vitamin B12-responsive methylmalonicaciduria of cblB complementation type; MIM:251110). Affected individuals have methylmalonic aciduria and metabolic ketoacidosis, despite a functional methylmalonyl-CoA mutase. In severe cases, newborns are lethargic, prone to vomiting and fail to thrive (Dobson et al. 2002).
Methionine synthase reductase (MTRR) is involved in reducing B12r (cob(II)alamin) to B12s (cob(I)alamin), the cofactor form used by methionine synthase (MTR) to become functional. Regeneration of functional MTR requires reductive methylation via a reaction catalyzed by MTRR in which S-adenosylmethionine (SAM) is used as a methyl donor. MTRR requires 1 FMN and 1 FAD per subunit for activity (Wolthers et al. 2007). MTRR exists a stable complex with MTR, bound through their FMN-binding and C-terminal activation domains respectively (Wolthers & Scrutton 2007, Wolthers & Scrutton 2009). Defects in MTRR cause methylcobalamin deficiency type E (cblE; MIM:236270) (Wilson et al. 1999). Patients with cblE exhibit megaloblastic anemia and hyperhomocysteinemia. SAM is used as a methyl donor in many biological reactions and demethylation of methionine produces homocysteine. Remethylation is carried out by MTR but in cblE patients, MTR cannot be reduced by defective MTRR to form a functional enzyme thus homocysteine accumulates. Mutations in MTRR that cause cblE include Leu576del (Leclerc et al. 1998), S454L (Zavadakova et al. 2005) and the compound heterozygote G487R/M569Ifs*9 (Zavadakova et al. 2002). Wilson et al. showed that a 66A-G polymorphism, resulting in an Ile22Met (I22M) substitution, is associated with susceptibility to folate-sensitive neural tube defects (FS-NTD; MIM:601634) (Wilson et al. 1999b, Doolin et al. 2002). Serum deficiency of vitamin B12 increased the effect.
Methionine synthase reductase (MTRR) is involved in reducing B12r (cob(II)alamin) to B12s (cob(I)alamin), the cofactor form used by methionine synthase (MTR) to become functional. MTRR requires 1 FMN and 1 FAD per subunit for activity (Wolthers et al. 2007). MTRR exists a stable complex with MTR, bound through their FMN-binding and C-terminal activation domains respectively (Wolthers & Scrutton 2007, Wolthers & Scrutton 2009).
AASS tetramer (name copied from entity in Homo sapiens)
PAK bound to Rac1 and Cdc42 (name copied from entity in Homo sapiens)
PIP3:PDK1:active AKT (name copied from entity in Homo sapiens)
Aldose reductase is a major reductase for isocaproaldehyde, a product of side-chain cleavage of cholesterol, in human and animal adrenal glands
AADAT dimer (name copied from entity in Homo sapiens)
CDC42:GTP (name copied from entity in Homo sapiens)
ALDH7A1 tetramer (name copied from entity in Homo sapiens)
RAC1-GTP (name copied from entity in Homo sapiens)
HPD dimer (name copied from entity in Homo sapiens)
TAT dimer (name copied from entity in Homo sapiens)
HGD hexamer (name copied from entity in Homo sapiens)
PAH tetramer (name copied from entity in Homo sapiens)
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GCDH tetramer (name copied from entity in Homo sapiens)
QDPR dimer (name copied from entity in Homo sapiens)
PCBD1 tetramer (name copied from entity in Homo sapiens)
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Conformational transition associated with E1-E2 interaction in small ubiquitin-like modifications
PAK homodimer (name copied from entity in Homo sapiens)
p-S-AKT:PDPK1:PIP3 (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)
AKT:PIP3 (name copied from entity in Homo sapiens)
PDPK1:PIP3 (name copied from entity in Homo sapiens)
branched-chain alpha-ketoacid dehydrogenase E1 complex (name copied from entity in Homo sapiens)
PDK1:PIP2,PIP3 (name copied from entity in Homo sapiens)
branched-chain alpha-ketoacid dehydrogenase complex (name copied from entity in Homo sapiens)
PKC-theta (open): DAG (name copied from entity in Homo sapiens)
p-Y90-PKC-theta:DAG (name copied from entity in Homo sapiens)
Active PKC theta bound to DAG (name copied from entity in Homo sapiens)
FTCD octamer (name copied from entity in Homo sapiens)
urocanate hydratase (name copied from entity in Homo sapiens)
HIBADH tetramer (name copied from entity in Homo sapiens)
ACAD8 tetramer (name copied from entity in Homo sapiens)
HSD17B10 tetramer (name copied from entity in Homo sapiens)
ACADSB tetramer (name copied from entity in Homo sapiens)
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AUH hexamer (name copied from entity in Homo sapiens)
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IVD tetramer (name copied from entity in Homo sapiens)
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The SUMO-specific protease SENP5 is required for cell division
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Crystal structure of the human monoacylglycerol lipase, a key actor in endocannabinoid signaling
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Activated PLC gamma1 bound to PIP2 (name copied from entity in Homo sapiens)
VAMP2:STX4:SNAP23 (name copied from entity in Homo sapiens)
PTEN:Mg2+ (name copied from entity in Homo sapiens)
RAC1:GTP (name copied from entity in Homo sapiens)
TC10:GTP (name copied from entity in Homo sapiens)
GLUT4:TUG (name copied from entity in Homo sapiens)
Structure, pharmacology and therapeutic prospects of family C G-protein coupled receptors
STX4:STXBP3 (MUNC18C) (name copied from entity in Homo sapiens)
Translocon (name copied from entity in Homo sapiens)
TAP (name copied from entity in Homo sapiens)
ARD:Fe++ (name copied from entity in Homo sapiens)
Cytosolic dihydropyrimidinase tetramer catalyzes the reaction of 5,6-dihydrothymine and water to yield 3-ureidoisobutyrate (Hamajima et al. 1998).
Particulate Ag:DC receptors (name copied from entity in Homo sapiens)
DIO1 homodimer (name copied from entity in Homo sapiens)
Rap1-GTP (name copied from entity in Homo sapiens)
TH:Fe2+ (name copied from entity in Homo sapiens)
DAO dimer (name copied from entity in Homo sapiens)
Rap1 cAMP-GEFs:cAMP (name copied from entity in Homo sapiens)
TPH:Fe++ (name copied from entity in Homo sapiens)
Rap1-GDP (name copied from entity in Homo sapiens)
AGXT dimer (name copied from entity in Homo sapiens)
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).
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D-amino-acid oxidase:FAD complex (name copied from entity in Homo sapiens)
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).
MAT I homotetramer (name copied from entity in Homo sapiens)
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 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 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).
MAT I/III (Mg, K cofactors) (name copied from entity in Homo sapiens)
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.
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.
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).
Isolation and functional expression of human COQ2, a gene encoding a polyprenyl transferase involved in the synthesis of CoQ
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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.
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).
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Structural analysis of the GLUT1 facilitative glucose transporter (review).
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ChEBI:28540 5beta-cholestane-3alpha,7alpha,26-triol
26S proteasome (name copied from entity in Homo sapiens)
E3:K48-polyubiquitinated substrate (name copied from entity in Homo sapiens)
Ub:substrate (name copied from entity in Homo sapiens)
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).
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).
p21 RAS:GDP (name copied from entity in Homo sapiens)
p21 RAS:GTP (name copied from entity in Homo sapiens)
TDO2 tetramer (name copied from entity in Homo sapiens)
PDPK1:PIP2 (name copied from entity in Homo sapiens)
ALDH4A1 dimer (name copied from entity in Homo sapiens)
E1 bound ubiquitin (name copied from entity in Homo sapiens)
FAH dimer (name copied from entity in Homo sapiens)
Ubiquitin:E2 conjugating enzymes (name copied from entity in Homo sapiens)
GSTZ1 dimer (name copied from entity in Homo sapiens)
E3:Ub:substrate (name copied from entity in Homo sapiens)
ACMSD dimer (name copied from entity in Homo sapiens)
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.
HAAO (name copied from entity in Homo sapiens)
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).
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KYNU dimer (name copied from entity in Homo sapiens)
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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CCBL2 dimer (name copied from entity in Homo sapiens)
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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Cytosolic glutathione reductase catalyzes the reaction of glutathione (oxidized) and NADPH + H+ to form two molecules of glutathione (reduced) and NADP+ (Loos et al. 1976).
Comparison of messenger RNA distribution for 60 proteins in fat cells vs the nonfat cells of human omental adipose tissue
In this reaction, 1 molecule of 'thioredoxin, oxidized' is translocated from nucleoplasm to cytosol. This movement of the molecule occurs through the 'nuclear pore'.
E1:Mg++ (name copied from entity in Homo sapiens)
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.
Differential regulation of zinc efflux transporters ZnT-1, ZnT-5 and ZnT-7 gene expression by zinc levels: a real-time RT-PCR study
APIP:Zn++ (name copied from entity in Homo sapiens)
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.
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_9855.2
Targeting purine and pyrimidine metabolism in human apicomplexan parasites
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_86357.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_9593.2
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=191409
PP2A (name copied from entity in Homo sapiens)
PDK1:AKT:PIP3 (name copied from entity in Homo sapiens)
Activated PKC beta (name copied from entity in Homo sapiens)
Active Calmodulin (name copied from entity in Homo sapiens)
p-RasGRP1,3:DAG (name copied from entity in Homo sapiens)
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ESCRT-III (name copied from entity in Homo sapiens)
Vamp7:SNAP23:Syn4 Plasma membrane vesicle docking and fusion complex (name copied from entity in Homo sapiens)
ESCRT-II/Cargo Complex (name copied from entity in Homo sapiens)
Arf1-GDP (name copied from entity in Homo sapiens)
Vamp2:SNAP23:Syn4 Secretory granule docking and fusion complex (name copied from entity in Homo sapiens)
Coatomer:Arf1-GTP Complex (name copied from entity in Homo sapiens)
Coatomer:Arf1-GTP:GAP Complex (name copied from entity in Homo sapiens)
Arf1-GTP (name copied from entity in Homo sapiens)
Coatomer (name copied from entity in Homo sapiens)
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ESCRT-II (name copied from entity in Homo sapiens)
Ubiquinated and PIP3 Endosmal Membrane Bound Cargo (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_96115.9
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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=191385
ChEBI:28533 3alpha,7alpha-dihydroxy-24-oxo-5beta-cholestanoyl-CoA
The ARE-dependent mRNA-destabilizing activity of BRF1 is regulated by protein kinase B
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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_97704.9
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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=3644454
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_9707.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=191265
RALA:GTP:MYO1C:Exocyst (name copied from entity in Homo sapiens)
RALA:GTP (name copied from entity in Homo sapiens)
MYO1C:CALM1 (name copied from entity in Homo sapiens)
RAB8A/10/13/14:GTP (name copied from entity in Homo sapiens)
RGC1:RGC2 (name copied from entity in Homo sapiens)
p-S237-TBC1D1:14-3-3 (name copied from entity in Homo sapiens)
RAB8A/10/13/14:GDP (name copied from entity in Homo sapiens)
Exocyst Complex (name copied from entity in Homo sapiens)
RALA:GTP:MYO1C:Calmodulin:F-actin (name copied from entity in Homo sapiens)
RGC1:p-486,696-T715-RGC2 (name copied from entity in Homo sapiens)
p-S1652-MYO5A:F-actin (name copied from entity in Homo sapiens)
Cyclin A- and cyclin E-Cdk complexes shuttle between the nucleus and the cytoplasm
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Receptor-mediated endocytosis of cobalamin (vitamin B12)
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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_30428.10
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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=191309
Components and dynamics of DNA replication complexes in S. cerevisiae: redistribution of MCM proteins and Cdc45p during S phase.
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_9771.2
AMPK gamma:AMP (name copied from entity in Homo sapiens)
AMPK-alpha2:AMPK-beta:AMPK-gamma:AMP (name copied from entity in Homo sapiens)
ESCRT-III/Cargo 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=3641149
Vps/Vta1 (name copied from entity in Homo sapiens)
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AS160:IRAP (name copied from entity in Homo sapiens)
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Phospho AS160:IRAP (name copied from entity in Homo sapiens)
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YWHAE dimer (name copied from entity in Homo sapiens)
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Phospho AS160:14-3-3:IRAP (name copied from entity in Homo sapiens)
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Phospho AS160:14-3-3 (name copied from entity in Homo sapiens)
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Nucleocytoplasmic shuttling modulates activity and ubiquitination-dependent turnover of SUMO-specific protease 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_4227.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643379
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_80457.9
Database identifier. Use 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=3643383
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641257
D-2-hydroxyglutaric acidaemia: identification of a new enzyme, D-2-hydroxyglutarate dehydrogenase, localized in mitochondria
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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=3641278
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641265
FDX1L (reduced) (name copied from entity in Homo sapiens)
FXN:NFS1:ISD11:ISCU:2Fe-2S Cluster (name copied from entity in Homo sapiens)
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CIAPIN1:4Fe-4S:2Fe-2S oxidized (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_124901.1
NDOR1:CIAPIN1 oxidized (name copied from entity in Homo sapiens)
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NDOR1:CIAPIN1 reduced (name copied from entity in Homo sapiens)
NDOR1:FAD:FMN (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=2161177
NUBP1:4Fe-4S (name copied from entity in Homo sapiens)
CIAPIN1:4Fe-4S:2Fe-2S reduced (name copied from entity in Homo sapiens)
NARFL:CIAO1:FAM96B:MMS19 (name copied from entity in Homo sapiens)
NUBP2:4Fe-4S:NUBP1 (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=3643870
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_126149.5
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_153975.3
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=3652008
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650801
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_155860.3
Conservation of the Caenorhabditis elegans timing gene clk-1 from yeast to human: a gene required for ubiquinone biosynthesis with potential implications for aging
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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=3643868
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643867
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_99549.9
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Regulation of origin recognition complex conformation and ATPase activity: differential effects of single-stranded and double-stranded DNA binding.
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Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets
D-Fructose 2,6-bisphosphate [ChEBI:28602]
holo-POLD1 (name copied from entity in Homo sapiens)
Identification of two mammalian reductases involved in the two-carbon fatty acyl elongation cascade
NARFL:4Fe-4S (name copied from entity in Homo sapiens)
Exosome 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=3642166
PAK-2p34:RHG10 complex (name copied from entity in Homo sapiens)
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holo-BRIP1 (holo-FANCJ) (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=3644385
holo-XPD (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_92365.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644387
Deadenylated mRNA:Lsm1-7 Complex (name copied from entity in Homo sapiens)
Lsm1-7 Complex (name copied from entity in Homo sapiens)
Exosome Ring Hexamer (name copied from entity in Homo sapiens)
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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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Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_126689.5
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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=3651832
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_110710.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21911.1
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_114037.8
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=500260
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643874
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=194634
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21428.1
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_160024.3
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_10504.2
The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone
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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_91998.9
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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=3641231
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651792
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_98650.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642176
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_99990.9
Reactome stable identifier. Use this 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
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_87607.9
Identification of human PMP34 as a peroxisomal ATP transporter
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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_112378.8
Database identifier. Use 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=3651962
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_84468.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643406
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643407
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651956
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641014
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_98868.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651955
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_31913.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641239
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641227
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641302
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641266
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641223
Reactome stable identifier. Use this 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
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_99614.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643410
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_109853.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643392
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643391
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643408
ISG15:RIG-I conjugate (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=3641243
AGE adducts:Peptide:AGER-1,2,3 (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=3641251
dsRNA bound to RIG-I (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=3642874
Association of the human SUMO-1 protease SENP2 with the nuclear pore
Human beta-galactosidase gene mutations in GM1-gangliosidosis: a common mutation among Japanese adult/chronic cases
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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=3641252
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642854
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640112
Constitutive PI3K/AKT Signaling in Cancer
CNDP2 (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=3640106
CDO1:Fe2+ (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=3640105
SQR: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=3640108
ETHE1:2Zn++ (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=3640107
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_156609.3
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=3643493
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640109
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640111
DDX41:DDX41 ligand (name copied from entity in Homo sapiens)
dsRNA:MDA5 (name copied from entity in Homo sapiens)
MAT II heterotetramer (name copied from entity in Homo sapiens)
MDA5:DAK (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=3642916
MAT II homodimer (name copied from entity in Homo sapiens)
ISG15:UBEIL/UbcH8:CEB1 (name copied from entity in Homo sapiens)
4x(AHCY:NAD+) (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=3641235
HsRPC8:HsRPC9 (name copied from entity in Homo sapiens)
AHCY:NAD+ (name copied from entity in Homo sapiens)
HsRPC4:HsRPC5 (name copied from entity in Homo sapiens)
CBS 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=3641024
HsRPC6:HsRPC3:HsRPC7 (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_153683.3
CTH tetramer:PXLP (name copied from entity in Homo sapiens)
RNA Polymerase III Holoenzyme (name copied from entity in Homo sapiens)
DHX9:CpG (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=3641055
CDC42-GDP (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=3642075
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641045
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642071
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641032
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641056
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642893
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640103
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640104
2xPPO: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_31789.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651711
2xUROD (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_93981.9
2xCPO (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=3651957
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640099
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640102
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640101
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640100
ALAS1 homodimer (pyridoxal phosphate 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=3642042
holo-SUOX (name copied from entity in Homo sapiens)
8xALAD:Pb2+:Zn2+ (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=3641036
HMBS:DIPY (name copied from entity in Homo sapiens)
ALAS2 homodimer (pyridoxal phosphate 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=3641028
8x(ALAD:Zn2+) (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=3651456
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651447
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641181
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641189
Protein interactions in the human methionine synthase-methionine synthase reductase complex and implications for the mechanism of enzyme reactivation
2xGSTP1 (name copied from entity in Homo sapiens)
2xGSTT1 (name copied from entity in Homo sapiens)
GSS (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=3641185
2xGSTA1 (name copied from entity in Homo sapiens)
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Negative regulation of MDA5- but not RIG-I-mediated innate antiviral signaling by the dihydroxyacetone kinase
2xGSTA3 (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=3648380
2x(FECH:2Fe-2S cluster) (name copied from entity in Homo sapiens)
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FMO1 (FAD cofactor) (name copied from entity in Homo sapiens)
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Mutations in COX15 produce a defect in the mitochondrial heme biosynthetic pathway, causing early-onset fatal hypertrophic cardiomyopathy
FMO2 (FAD, Mg2+ cofactors) (name copied from entity in Homo sapiens)
FMO3 (FAD 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=3651502
2xGSTT2B (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=3647501
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641058
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641220
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641221
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647517
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640154
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640152
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640151
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640147
FDX1L (oxidized) (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=3640142
FDXR: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=3641057
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_159684.3
FDXR:FADH2 (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=3640118
2 Iron:FXN:NFS1:ISD11:ISCU (name copied from entity in Homo sapiens)
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2 Iron:FXN (name copied from entity in Homo sapiens)
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FXN:ISD11:NFS1:ISCU (name copied from entity in Homo sapiens)
NFS1:pyridoxal phosphate (name copied from entity in Homo sapiens)
2xGSTZ1 (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=3641018
2xHPGDS (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=3641168
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648188
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641173
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648044
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641159
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648647
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641160
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641203
Aquaporins in the hepatobiliary tract. Which, where and what they do in health and 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=3648177
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644082
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641177
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648727
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641194
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648721
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641155
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648736
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641202
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3823.2
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=111584
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_80364.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641993
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_102501.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641992
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641990
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641989
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641164
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641172
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642275
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647546
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647580
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647525
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647551
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647556
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641983
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641985
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642752
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_108131.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=35141
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5442.2
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=3642935
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642934
Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5122.1
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Structural relationships and the classification of aminoacyl-tRNA synthetases
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Enzymatic activities of the human AGPAT isoform 3 and isoform 5: localization of AGPAT5 to mitochondria
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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).
Cytosolic 3-ureidopropionase catalyzes the reaction of 3-ureidopropionate and water to form beta-alanine, CO2, and NH3 (van Kuilenberg et al. 2004).
Amino acid transport across the plasma membrane
Cytosolic dihydropyrimidinase tetramer catalyzes the reaction of 5,6-dihydrouracil and water to form 3-ureidopropionate (Hamajima et al. 1998).
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).
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).
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).
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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Wnt family proteins are secreted and associated with the cell surface
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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 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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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.
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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).
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 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.
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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 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 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 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).
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).
Localization of MCM2-7, Cdc45, and GINS to the site of DNA unwinding during eukaryotic DNA replication
PMP70, the 70-kDa peroxisomal membrane protein: a member of the ATP-binding cassette transporters
Reverse transcriptase motifs in the catalytic subunit of telomerase
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Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules
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Role for the class A macrophage scavenger receptor in the phagocytosis of apoptotic thymocytes in vitro
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Electron Transport from NADPH to Ferredoxin
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A novel PtdIns3P and PtdIns(3,5)P2 phosphatase with an inactivating variant in centronuclear myopathy
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Molecular basis of signaling specificity of insulin and IGF receptors: neglected corners and recent advances
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Biosynthesis of delta-aminolevulinic acid and the regulation of heme formation by immature erythroid cells in man
Many cuts to ruin: a comprehensive update of caspase substrates
Phosphorylation of Gz in human platelets. Selectivity and site of modification
Geometry of a complex formed by double strand break repair proteins at a single DNA end: recruitment of DNA-PKcs induces inward translocation of Ku protein.
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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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Reviews in molecular biology and biotechnology: transmembrane signaling by G protein-coupled receptors
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Tyrosines can be iodinated in thyroglobulin to produce precursors for thyroid hormone synthesis.
Mono- and di-iodinated tyrosine can combine to form tri-iodothyronine (T3). The hormone thyrotropin can stimulate the production of T3 and T4.
Insulin-responsive human adipocytes express two glucose transporter isoforms and target them to different vesicles
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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)
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:
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)
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)
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.
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).
Melatonin in the skin: synthesis, metabolism and functions
Identification and characterization of human glucose transporter-like protein-9 (GLUT9): alternative splicing alters trafficking
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).
Glucose-sensing mechanisms in pancreatic beta-cells
Philos Trans R Soc Lond B Biol Sci 360:2211-25
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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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Iodothyronine deiodinases 1 and 2 (DIO1/2) are the vertebrate enzymes responsible for the deiodination of the prohormone thyroxine (T4; 3,5,3',5'-tetraiodothyronine) into the biologically active hormone T3 (3,5,3'-triiodothyronine). DIO1/2 activity is critical for appropriate T3 levels in the brain during development.
The iodothyronine deiodinases (DIO) are dimeric, membrane-bound enzymes that regulate the activity of thyroid hormone by removal of specific iodines from the precursor T4. There are three types of DIOs in humans; types I, II and III (D1, D2 and D3 respectively) which are proteins of about 250 residues that contain a selenocysteine at their active site. Signaling by thyroid hormone can change in individual tissues by this activation or inactivation process, even when serum concentrations of the hormone remain normal. Generally, cell types express just one type of DIO at any one time. The exception is the pituitary gland which expresses all three.
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.
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).
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.
Catecholamines and thyroxine are synthesized from tyrosine, and serotonin and melatonin from tryptophan.
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).
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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Genomic basis of mucopolysaccharidosis type IIID (MIM 252940) revealed by sequencing of GNS encoding N-acetylglucosamine-6-sulfatase
Cytosolic kynurenine 3-monooxygenase catalyzes the reaction of L-kynurenine, NADPH + H+, and O2 to form 3-hydroxy-L-kynurenine, NADP+, and H2O.
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.
CCBL1 (KAT 1) catalyzes the reaction of kynurenine and pyruvate to form 4-(2-aminophenyl)-2,4-dioxobutanoate 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). The pH optimum observed for CCBL1 in vitro is 9.5 - 10.0, so its role in kynurenine metabolism in vivo is not clear (Baran et al. 1994). Biochemical studies of CCBL1 activity in vitro (e.g., Baren et al. 1994) invariably measure kynurenic acid as the reaction product, not 4-(2-aminophenyl)-2,4-dioxobutanoate, the product to be expected from transamination of kynurenine. The condensation of 4-(2-aminophenyl)-2,4-dioxobutanoate and elimination of a water molecule to form kynurenic acid has not been demonstrated directly. As noted by Miller et al. (1953), discussing their characterization of a bacterial form of the enzyme, "The keto acid assumed to be formed prior to ring closure in the conversion of kynurenine to kynurenic acid has not yet been detected. In principle, such detection should be possible, since it is sufficiently stable to have been synthesized. It also remains to be established whether ring closure is spontaneous, enzymatic, or both. The formation of kynurenic acid from L-kynurenine by the L-amino acid oxidase of Neurospora suggests, however, that ring closure can be spontaneous, unless the somewhat improbable assumption is made that Neurospora filtrate contained the ring-closing enzyme."
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).
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).
Purification, characterization, and cDNA cloning of an AU-rich element RNA-binding protein, AUF1
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).
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AADAT dimer localized in the mitochondrial matrix catalyzes the reaction of kynurenine and 2-oxoglutarate to form 4-(2-aminophenyl)-2,4-dioxobutanoate and glutamate (Han et al. 2008). Biochemical studies of kynurenine transamination in vitro invariably measure kynurenic acid, not 4-(2-aminophenyl)-2,4-dioxobutanoate, the expected transamination product. As noted by Miller et al. (1953), "The keto acid assumed to be formed prior to ring closure in the conversion of kynurenine to kynurenic acid has not yet been detected. In principle, such detection should be possible, since it is sufficiently stable to have been synthesized. It also remains to be established whether ring closure is spontaneous, enzymatic, or both. The formation of kynurenic acid from L-kynurenine by the L-amino acid oxidase of Neurospora suggests, however, that ring closure can be spontaneous, unless the somewhat improbable assumption is made that Neurospora filtrate contained the ring-closing enzyme."
Targeting, import, and dimerization of a mammalian mitochondrial ATP binding cassette (ABC) transporter, ABCB10 (ABC-me)
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'.
Cytosolic 3-hydroxyanthranilate oxygenase catalyzes the reaction of 3-hydroxyanthranilate and O2 to form 2-amino-3-carboxymuconate semialdehyde.
Cytosolic kynureninase catalyzes the hydrolysis of 3-hydroxy-L-kynurenine to form L-alanine and 3-hydroxyanthranilate.
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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.
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.
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)
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.
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).
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).
Mitochondrial N acetylglutamate synthetase (NAGS) catalyzes the reaction of glutamate and acetyl-CoA to form N-acetylglutamate and CoA. NAGS is activated by arginine and the N-acetylglutamate produced in the reaction in turn is required to activate carbamoyl synthetase I. Consistent with this regulatory role in urea synthesis, NAGS mutations in humans are associated with hyperammonemia (Caldovic et al. 2002; Morizono et al. 2004).
Endoplasmic reticulum-bound ribosomes reside in stable association with the translocon following termination of protein synthesis
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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.
The functional human dihydrofolate reductase gene
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)
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Kynurenine/alpha-aminoadipate aminotransferase (AADAT) catalyzes the reversible reaction of alpha-ketoadipate and glutamate to form alpha-aminoadipate and alpha-ketoglutarate. Crystallographic studies have demonstrated that active AADAT enzyme is a homodimer with a pyridoxal phosphate moiety covalently attached to each monomer (Han et al. 2008; Rossi et al. 2008). The enzyme is inferred to be located within the mitochondrion because of a mitochondrial localization sequence motif at the aminoterminal end of the AADAT polypeptide (Goh et al. 2002).
Kynurenine/alpha-aminoadipate aminotransferase (AADAT) catalyzes the reversible reaction of alpha-aminoadipate and alpha-ketoglutarate to form alpha-ketoadipate and glutamate. Crystallographic studies have demonstrated that active AADAT enzyme is a homodimer with a pyridoxal phosphate moiety covalently attached to each monomer (Han et al. 2008; Rossi et al. 2008). The enzyme is inferred to be located within the mitochondrion because of a mitochondrial localization sequence motif at the aminoterminal end of the AADAT polypeptide (Goh et al. 2002).
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).
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).
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).
Cytosolic phenylalanine hydroxylase (PAH) catalyzes the reaction of phenylalanine, molecular oxygen and tetrahydrobiopterin to form tyrosine, water, and 4 alpha-hydroxytetrahydrobiopterin. The active form of the enzyme is a homotetramer (Fusetti et al. 1998).
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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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).
Anoctamins are a family of Ca2+ activated Cl- channels
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).
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).
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.
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).
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.
Cytosolic fumarylacetoacetase catalyzes the hydrolysis of 4-fumarylacetoacetate to form fumarate and acetoacetate (Labelle et al. 1993).
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.
p(S27)-G protein alpha (z):GTP (name copied from entity in Homo sapiens)
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).
Heterotrimeric G-protein Gi (active) (name copied from entity in Homo sapiens)
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).
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RhoA,B,C:GDP (name copied from entity in Homo sapiens)
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).
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G-protein alpha (z):GDP (name copied from entity in Homo sapiens)
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).
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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.
Mitochondrial ethylglutaconyl-CoA hydratase (AUH) catalyzes the hydrolysis of beta-methylglutaconyl-CoA to yield beta-hydroxy-beta-methylglutaryl-CoA (IJlst et al. 2002; Narisawa et al. 1986). Crystallographic studies have shown the active enzyme to be a hexamer of AUH polypeptides whose aminoterminal 67 residues, a mitochondrial targeting sequence, have been removed ((Kurimoto et al. 2001).
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 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).
Argonaute proteins: mediators of RNA silencing
Ligand:GPCR complexes that activate Gi:Heterotrimeric G-protein Gi (inactive) (name copied from entity in Homo sapiens)
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).
G-protein alpha (z):GTP (name copied from entity in Homo sapiens)
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).
G-protein alpha (i):GDP (name copied from entity in Homo sapiens)
Heterotrimeric G-protein Gi (inactive) (name copied from entity in Homo sapiens)
Ligand:GPCR complexes that activate Gi:Heterotrimeric G-protein Gi (active) (name copied from entity in Homo sapiens)
G-protein beta-gamma complex (name copied from entity in Homo sapiens)
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RhoGTPase:GDP (name copied from entity in Homo sapiens)
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).
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Inactivated RhoGTPase:GDP:GDI complex (name copied from entity in Homo sapiens)
RhoGTPase:GTP (name copied from entity in Homo sapiens)
Cytosolic formimidoyltransferase-cyclodeaminase (FTCD) catalyzes the reaction of N-formiminoglutamate and tetrahydrofolate to form glutamate and 5-formiminotetrahydrofolate. The gene encoding the human enzyme has beeen cloned and its sequence can encode a protein homologous the the biochemically characterized porcine protein (Solans et al. 2000; Murley et al. 1993). The function of FTCD in vivo was established by identification of missense mutations that reduce enzyme activity in patients with glutamate formiminotransferase deficiency (Hilton et al. 2003). Human FTCD is inferred to be an octamer by homology to the porcine enzyme (Murley et al. 1993).
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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.
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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 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).
In vivo disposal of phenylalanine in phenylketonuria: a study of two siblings
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).
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G-protein alpha (z):GTP:Adenylate cyclase (name copied from entity in Homo sapiens)
Cytosolic histidine ammonia lyase (HAL) catalyzes the reaction of histidine to form urocanate and NH4+ (Kawai et al. 2005).
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PIP3:PDK1 complex (name copied from entity in Homo sapiens)
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 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).
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.
Ub-RNF41 (name copied from entity in Homo sapiens)
PIP3:RhoA (name copied from entity in Homo sapiens)
RAC1:GDP (name copied from entity in Homo sapiens)
PIP3:AKT2 complex (name copied from entity in Homo sapiens)
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p-AMPK heterotrimer:AMP (name copied from entity in Homo sapiens)
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).
p-AMPK heterotrimer (name copied from entity in Homo sapiens)
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.
Association of folding intermediates of glycoproteins with calnexin during protein maturation
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.
Activated mTORC1 (name copied from entity in Homo sapiens)
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).
Rheb:GTP (name copied from entity in Homo sapiens)
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).
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eIF4E:4E-BP1-P (name copied from entity in Homo sapiens)
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).
eIF4E:4E-BP (name copied from entity in Homo sapiens)
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).
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UPF1:eRF3 Complex on Translated mRNA (name copied from entity in Homo sapiens)
mRNA Complex with a Premature Termination Codon Not Preceding an Exon Junction (name copied from entity in Homo sapiens)
Rheb:GDP (name copied from entity in Homo sapiens)
Slo3 Channel (name copied from entity in Homo sapiens)
hCTR1: a human gene for copper uptake identified by complementation in yeast
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 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).
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Substrate specificity and phosphorylation of antiviral and anticancer nucleoside analogues by human deoxyribonucleoside kinases and ribonucleoside kinases
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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).
Translated mRNA Complex with Premature Termination Codon Not Preceding Exon Junction (name copied from entity in Homo sapiens)
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.
Mechanism of metal activation of human hematopoietic prostaglandin D synthase
SMG1:Phosphorylated UPF1:EJC:Translated mRNP (name copied from entity in Homo sapiens)
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)
SMG1:SMG8:SMG9 Complex (name copied from entity in Homo sapiens)
Dephosphorylation of O-phospho-L-serine to L-serine proceeds through a phospho-enzyme intermediate of the catalysing phosphatase PSP (Collet et al. 1997).
Magoh-Y14 complex (name copied from entity in Homo sapiens)
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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Core Exon Junction Complex (Core EJC) (name copied from entity in Homo sapiens)
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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Exon Junction:UPF2:UPF3 Complex (name copied from entity in Homo sapiens)
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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GDP bound eRF3 (name copied from entity in Homo sapiens)
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).
40S ribosomal complex (name copied from entity in Homo sapiens)
60S ribosomal complex (name copied from entity in Homo sapiens)
80S ribosome (name copied from entity in Homo sapiens)
Serine biosynthesis starts from 3-phosphoglycerate, a glycolysis intermediate. Its dehydrogenation is catalysed by tetrameric phosphoglycerate dehydrogenase PHGDH. (Tabatabaie et al. 2009).
long-chain fatty acid anion [ChEBI:57560]
RNA Polymerase III Transcription Initiation
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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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Profiling of promoter occupancy by PPAR{alpha} in human hepatoma cells via ChIP-chip analysis
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BRF1:mRNA Complex (name copied from entity in Homo sapiens)
Phosphorylated BRF1 (Ser92, Ser203):mRNA Complex (name copied from entity in Homo sapiens)
TTP:mRNA Complex (name copied from entity in Homo sapiens)
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HuR with phosphoserine221 and phosphoserine158:mRNA Complex (name copied from entity in Homo sapiens)
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HuR with phosphoserine221 and phosphoserine318:mRNA Complex (name copied from entity in Homo sapiens)
HuR with Unknown Phosphorylation: mRNA Complex (name copied from entity in Homo sapiens)
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(GlcN)1 (Ino(acyl)-P)1 (Man)4 (EtN)3 (P)3
SMG1:UPF1:EJC:Translated mRNP (name copied from entity in Homo sapiens)
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Translated mRNA Complex with Premature Termination Codon Preceding Exon Junction (name copied from entity in Homo sapiens)
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mRNA Complex with a Premature Termination Codon Preceding an Exon Junction (name copied from entity in Homo sapiens)
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(ethanolamineP) mannose (a1-2) mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI
Cap Binding Complex (CBC) (name copied from entity in Homo sapiens)
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Ubiquitinated AUF1 Tetramer (name copied from entity in Homo sapiens)
Decapped mRNA:LSM1-7 Complex (name copied from entity in Homo sapiens)
Phosphorylated AUF1 p40 Dimer (name copied from entity in Homo sapiens)
AUF1 Tetramer: Destabilized mRNA Complex (name copied from entity in Homo sapiens)
AUF1 p37 Dimer (name copied from entity in Homo sapiens)
Phosphorylated AUF1 p40 Tetramer (name copied from entity in Homo sapiens)
Ubiquitinated AUF1 Tetramer: Destabilized mRNA Complex (name copied from entity in Homo sapiens)
AUF1 p37 Tetramer (name copied from entity in Homo sapiens)
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Enzymatic, metabolic and secretory patterns in human islets of type 2 (non-insulin-dependent) diabetic patients
InsP3-mediated intracellular calcium signalling is altered by expression of synaptojanin-1
1-phosphatidyl-1D-myo-inositol [ChEBI:16749]
Purification, cDNA cloning and expression of 15-oxoprostaglandin 13-reductase from pig lung
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dolichyl D-mannosyl phosphate [ChEBI:15809]
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Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities.
Propanoyl-CoA:carbon dioxide ligase alpha subunit
Note: the coordinates are copied over from Homo sapiens.
propionyl-CoA carboxylase alpha chain, apoprotein
Propionyl-CoA carboxylase alpha chain, mitochondrial precursor
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Propanoyl-CoA:carbon dioxide ligase beta subunit
Propionyl-CoA carboxylase beta chain, mitochondrial precursor
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methylcrotonyl-CoA carboxylase alpha chain
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Structure and sequence of the human sulphamidase gene
Biotin--protein ligase ecNumber6.3.4.-/ecNumber
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Immunoglobulin G-mediated phagocytosis activates a calcium-independent, phosphatidylethanolamine-specific phospholipase
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Phosphopantothenoylcysteine decarboxylase
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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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Probable lysosomal cobalamin transporter
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Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway.
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The Ca-calmodulin-dependent protein kinase cascade
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non-metastatic cells 1, protein (NM23A) expressed in
Tumor metastatic process-associated protein
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Nucleoside diphosphate kinase, mitochondrial
non-metastatic cells 4, protein expressed in
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FAD1 flavin adenine dinucleotide synthetase homolog
Ectonucleotide pyrophosphatase/phosphodiesterase 1
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ATP6V0A (name copied from entity in Homo sapiens)
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Inhibition of replication initiation of damaged DNA by RB1/E2F1
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FGFR1 fusion mutant dimers:TKIs (name copied from entity in Homo sapiens)
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Activated FGFR1 fusion mutants:PLC-gamma (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_3793.1
Activated FGFR1 fusion mutants:p-PLCgamma (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=111345
L-amino acid oxidase (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=3644866
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_78229.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642693
CUX1-FGFR1 fusion mutant dimer (name copied from entity in Homo sapiens)
CUX1-p-FGFR1 fusion mutant dimer (name copied from entity in Homo sapiens)
AKT1 E17K mutant:PIP2 (name copied from entity in Homo sapiens)
PDPK1:p-S473-AKT1 E17K mutant: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=3644535
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5463.1
Insulin signalling and the regulation of glucose and lipid metabolism
p-S473-AKT1 E17K mutant: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=3642691
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644562
Reactome stable identifier. Use this 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=3642690
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_93667.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111344
Paused processive elongation 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=3642687
Elongin 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_5617.1
Functional properties and genomics of glucose transporters
FACT 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
P-TEFb 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=3642688
IDH1 R132H dimer (name copied from entity in Homo sapiens)
DSIF complex (name copied from entity in Homo sapiens)
AKT inhibitors:AKT (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=3648318
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3646487
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_33657.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113571
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3796.2
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=3642686
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3646448
Database identifier. Use 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
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649428
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5587.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649436
RhoA/B/C:GTP (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=3646435
G protein alpha:GTP complex (name copied from entity in Homo sapiens)
G-protein alpha:GDP (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=3645775
Activated PLC beta 1/4 (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=113550
PP2B catalytic (Fe3+, Zn2+) (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=3642684
PP2B catalytic (Fe3+, Zn2+):Active Calmodulin (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_5790.1
METAP1:2Co2+ (name copied from entity in Homo sapiens)
METAP2:2Co2+ (name copied from entity in Homo sapiens)
Guanylate cyclase activating proteins:Ca2+
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5621.1
Crystal structures of human glutaryl-CoA dehydrogenase with and without an alternate substrate: structural bases of dehydrogenation and decarboxylation reactions
ER-mediated phagocytosis: a new membrane for new functions
Database identifier. Use 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
Reactome stable identifier. Use this 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=3649543
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29428
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3913.3
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=3649566
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642682
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642683
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649574
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_108007.9
Database identifier. Use 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
GUCA1C: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=3645913
UBA2:SAE1 (name copied from entity in Homo sapiens)
GUCA1A:Ca2+ (name copied from entity in Homo sapiens)
GUCA1B: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=3645916
ATP6V0 (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_5885.1
ATP6V0E (name copied from entity in Homo sapiens)
Primary structure of human triosephosphate isomerase
SUMO1 S-glycyl-cys173 UBA2:SAE1 (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=3642680
V-ATPase (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=3641972
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4670.1
ATP6V0D (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=29892
ATP6V0C hexamer (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=29604
Characterization of the human mitochondrial methionyl-tRNA synthetase
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2773.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=30187
Purification and properties of uroporphyrinogen I synthase from human erythrocytes. Identification of stable enzyme-substrate intermediates.
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642497
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642498
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642499
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651880
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642501
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_87638.9
Succinate Dehydrogenase complex subunit A
Succinate dehydrogenase (ubiquinone) flavoprotein subunit, 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=3651793
Succinate dehydrogenase (ubiquinone) iron-sulfur protein, mitochondrial
Succinate Dehydrogenase complex subunit B
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_156642.3
Succinate Dehydrogenase complex subunit C
Succinate-ubiquinone oxidoreductase cytochrome B large subunit
Succinate dehydrogenase cytochrome b560 subunit, mitochondrial precursor
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641292
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641291
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641294
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_159441.3
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=3641283
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641293
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641295
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_156963.3
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=3640124
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_82354.9
Electron Transfer Flavoprotein 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_3468.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651783
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113518
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_142444.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644290
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640157
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640156
Is the mammalian serine palmitoyltransferase a high-molecular-mass complex?
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640155
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_154776.3
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=3641793
Database identifier. Use 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
Isocitrate dehydrogenase (NAD) subunit alpha, mitochondrial precursor
Reactome stable identifier. Use this 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
Isocitrate dehydrogenase (NAD) subunit gamma, mitochondrial precursor
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_89432.9
Aconitate hydratase, mitochondrial precursor
Isocitrate dehydrogenase (NAD) subunit beta, mitochondrial precursor
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641794
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial precursor
70 kDa mitochondrial autoantigen of primary biliary cirrhosis
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641800
Citrate synthase, mitochondrial precursor
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651878
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650947
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_155796.3
Mechanism of porphobilinogen synthase. Requirement of Zn2+ for enzyme 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=3642731
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_156055.3
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=3642729
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648149
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642730
Crystal structure of human protein tyrosine phosphatase 1B
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649230
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642728
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_159131.3
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=3651879
Reactome stable identifier. Use this 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
2-oxoglutarate dehydrogenase E1 component, mitochondrial precursor
alpha-ketoglutarate dehydrogenase E1 apoenzyme
Database identifier. Use 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
nicotinamide nucleotide transhydrogenase
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642187
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642189
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_77127.9
N-glycan trimming in the ER and Calnexin/Calreticulin cycle
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642186
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651201
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642665
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651143
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642681
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_32256.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651286
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642666
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_83429.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2529016
Cytochrome P450 and arachidonic acid bioactivation. Molecular and functional properties of the arachidonate monooxygenase
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651865
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=77601
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4094.2
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=3642727
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644073
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642194
Reactome stable identifier. Use this 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
pyruvate dehydrogenase E1 alpha apoprotein
Pyruvate dehydrogenase E1 component alpha subunit, somatic form, mitochondrial precursor
Database identifier. Use 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
Dihydrolipoamide dehydrogenase, 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=3642193
Pyruvate dehydrogenase protein X component, mitochondrial precursor
Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex
pyruvate dehydrogenase complex X component (E3 binding protein)
The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci
Pyruvate dehydrogenase E1 component beta subunit, mitochondrial precursor
pyruvate dehydrogenase E1 beta apoprotein
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2530.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113535
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113575
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642196
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_30688.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640931
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640936
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642685
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640997
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642692
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640998
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=72085
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3987.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642689
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_93299.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642696
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_114145.8
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642697
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643439
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651165
Reactome stable identifier. Use this 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=113569
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5022.2
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_22071.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=500739
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=500742
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651943
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_155022.3
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=3651944
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21695.1
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_159430.3
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=3641904
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641903
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641906
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_105551.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643881
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_107492.9
Glutathione reductase, mitochondrial precursor
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651697
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_101076.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651696
deoxythymidylate kinase (thymidylate 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=500759
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_30611.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651772
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_76954.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2843.2
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_21421.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=500761
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_28980.10
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21676.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643271
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641843
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641842
uridine monophosphate synthetase (orotate phosphoribosyl transferase and orotidine-5'-decarboxylase)
Uridine 5'-monophosphate synthase (UMP synthase) (Includes: Orotate phosphoribosyltransferase (EC 2.4.2.10) (OPRtase); Orotidine 5'- phosphate decarboxylase (EC 4.1.1.23) (OMPdecase))
Adenylate kinase isoenzyme 2, mitochondrial
Adenylate kinase isoenzyme 2, mitochondrial (EC 2.7.4.3) (ATP-AMP transphosphorylase)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_152952.3
Guanylate kinase (EC 2.7.4.8) (GMP 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=3643276
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643277
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651942
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_114637.8
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643274
Thymidine kinase, cytosolic (EC 2.7.1.21)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643275
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641798
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_32516.10
AMP deaminase 3 (EC 3.5.4.6) (AMP deaminase isoform E) (Erythrocyte AMP deaminase)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641796
AMP deaminase 2 (EC 3.5.4.6) (AMP deaminase isoform L)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=76632
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=68422
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_96047.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_107132.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4914.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=76630
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=68424
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2531.1
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_3288.1
Hypoxanthine-guanine phosphoribosyltransferase
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3639820
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5211.1
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_3748.1
Removal of licensing factors from origins
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113656
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640046
carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase
CAD protein (Includes: Glutamine-dependent carbamoyl-phosphate synthase (EC 6.3.5.5); Aspartate carbamoyltransferase (EC 2.1.3.2); Dihydroorotase (EC 3.5.2.3))
Glutamine-dependent carbamoyl-phosphate synthase
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113499
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=111629
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641301
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641300
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641299
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641274
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641270
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_86723.9
Bifunctional purine biosynthesis protein PURH (Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) (AICAR transformylase); IMP cyclohydrolase (EC 3.5.4.10) (Inosinicase) (IMP synthetase) (ATIC))
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase
Bifunctional purine biosynthesis protein PURH
Phosphoribosylaminoimidazolecarboxamide formyltransferase
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641787
Phosphoribosylformylglycinamidine synthase
Formylglycinamide ribotide amidotransferase
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_81573.9
phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase
Trifunctional purine biosynthetic protein adenosine-3 (Includes: Phosphoribosylamine--glycine ligase (EC 6.3.4.13) (GARS) (Glycinamide ribonucleotide synthetase) (Phosphoribosylglycinamide synthetase); Phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) (AIRS) (Phosphoribosyl-aminoimidazole synthetase) (AIR synthase); Phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) (GART) (GAR transformylase) (5'-phosphoribosylglycinamide transformylase))
Trifunctional purine biosynthetic protein adenosine-3
5'-phosphoribosylglycinamide transformylase
Phosphoribosylformylglycinamidine cyclo-ligase
Phosphoribosylglycinamide formyltransferase
Phosphoribosyl-aminoimidazole synthetase
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641789
Glutamine phosphoribosylpyrophosphate amidotransferase
Amidophosphoribosyltransferase precursor (EC 2.4.2.14) (Glutamine phosphoribosylpyrophosphate amidotransferase) (ATASE) (GPAT)
Amidophosphoribosyltransferase precursor
phosphoribosyl pyrophosphate amidotransferase
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641785
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641287
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641784
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651707
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3215.1
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_103160.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643273
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3639854
IMP (inosine monophosphate) dehydrogenase 1
Inosine-5'-monophosphate dehydrogenase 1 (EC 1.1.1.205) (IMP dehydrogenase 1) (IMPDH-I) (IMPD 1)
Inosine-5'-monophosphate dehydrogenase 1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648087
AMP deaminase 1 (EC 3.5.4.6) (Myoadenylate deaminase) (AMP deaminase isoform M)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648088
Adenylosuccinate synthetase (EC 6.3.4.4) (IMP--aspartate ligase) (AdSS) (AMPSase)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648089
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_83562.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652215
Requirement of the DEAD-Box protein ded1p for messenger RNA translation.
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641860
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_108769.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641862
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_109094.9
Activation of DNA-binding activity in an apparently cytoplasmic precursor of the NF-kappa B transcription factor
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644495
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=109379
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644496
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3054.2
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=3644498
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=500829
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_78952.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21803.1
Database identifier. Use 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
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=109383
Reactome stable identifier. Use this 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=3644500
Database identifier. Use 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
Reactome stable identifier. Use this 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
An integrated genomic analysis of human glioblastoma multiforme
Database identifier. Use 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
Phosphoinositides in cell regulation and membrane dynamics
Reactome stable identifier. Use this 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
Reactome stable identifier. Use this 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
Database identifier. Use 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
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644507
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_31955.10
Database identifier. Use 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_2801.1
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, 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).
Database identifier. Use 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_5528.1
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, 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, 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).
Downstream Signaling Events Of B Cell Receptor (BCR)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=73584
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 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 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).
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Regulation of the Fanconi anemia pathway
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Isolation and characterization of the human pyruvate kinase M gene
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).
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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).
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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, 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-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 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 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 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 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 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).
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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, 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-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-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, 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 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).
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).
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).
Viral evasion and subversion of pattern-recognition receptor signalling
The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2.
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).
Initial-rate kinetics of human NMN-adenylyltransferases: substrate and metal ion specificity, inhibition by products and multisubstrate analogues, and isozyme contributions to NAD+ biosynthesis
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-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 3,5-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 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 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).
The human and rat forms of multiple inositol polyphosphate phosphatase: functional homology with a histidine acid phosphatase up-regulated during endochondral ossification
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).
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.
Human spermidine synthase gene: structure and chromosomal localization
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).
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).
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).
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).
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).
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).
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.
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.
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.
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).
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).
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).
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).
Molecular identification and characterization of two medium-chain acyl-CoA synthetases, MACS1 and the Sa gene product
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).
Aldo-keto reductase family 1 member C3 (AKR1C3) aka PGFS is the enzyme involved in NADPH-dependent prostaglandin D2 11-keto reductase activity of reducing prostaglandin D2 (PGD2) to 11-epi-Prostaglandin F2alpha (11-epi-PGF2a) (Liston & Roberts 1985, Koda et al. 2004).
Prostaglandin reductase 1 (PTGR1) aka LTB4DH is a 13-prostaglandin reductase which metabolises eicosanoids by catalysing NADH/NADPH-dependant double bond reduction in 15-keto-prostaglandin E2 (15k-PGE2) and F2alpha (15k-PGF2a) to produce 13,14-dihydro-15-keto-prostaglandin E2 (dhk-PGE2) and F2alpha (dhk-PGF2a) respectively (Yokomizo 1996). This has been inferred from the reaction event in mice involving prostaglandin reductase 2 (Ptgr2) (Chou et al. 2007).
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).
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).
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).
Aldo-keto reductase family 1 member C3 (AKR1C3) aka PGFS is responsible for the reduction of prostaglandin H2 (PGH2) to prostaglandin F2alpha (PGF2a) (Suzuki-Yamamoto et al. 1999, Komoto et al. 2004, Komoto et al. 2006). There is an additional way of achieving this reaction involving the prostamide/prostaglandin F synthase, FAM213B and thioredoxin (TRX).
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.
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).
Prostaglandin reductase 1 (PTGR1) aka LTB4DH metabolizes eicosanoids by catalysing the oxidation of leukotriene B4 (LTB4) to form 12-oxo-Leukotriene B4 (12-oxoLTB4) aka 12-Keto-LTB4. The gene was originally cloned as leukotriene B4 12-hydroxydehydrogenase (LTB4DH) but was later discovered to have dual functionality as a prostaglandin reductase (Yokomizo et al. 1996). This reaction has been inferred from a reaction in pigs (Yokomizo et al. 1993, Ensor et al. 1998).
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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.
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pol II open pre-initiation complex (name copied from entity in Homo sapiens)
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Aborted elongation complex after arrest (name copied from entity in Homo sapiens)
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pol II promoter:TFIID:TFIIA:TFIIB complex (name copied from entity in Homo sapiens)
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pol II promoter:TFIID complex (name copied from entity in Homo sapiens)
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pol II promoter:TFIID:TFIIA:TFIIB:Pol II:TFIIF:TFIIE complex (name copied from entity in Homo sapiens)
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Pol II initiation complex (name copied from entity in Homo sapiens)
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TFIIA (name copied from entity in Homo sapiens)
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TFIIE (name copied from entity in Homo sapiens)
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pol II closed pre-initiation complex (name copied from entity in Homo sapiens)
pol II promoter:TFIID:TFIIA:TFIIB:Pol II:TFIIF complex (name copied from entity in Homo sapiens)
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Functional variant of CYP4A11 20-hydroxyeicosatetraenoic acid synthase is associated with essential hypertension
TFIID (name copied from entity in Homo sapiens)
Regulation of PKC-? function by phosphorylation in T cell receptor signaling
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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
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RNA Pol II (hypophosphorylated):capped pre-mRNA complex (name copied from entity in Homo sapiens)
RNA Polymerase II holoenzyme complex (hypophosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
DSIF:NELF:early elongation complex (name copied from entity in Homo sapiens)
RNA Pol II (hypophosphorylated) complex bound to DSIF protein (name copied from entity in Homo sapiens)
RNA Polymerase II holoenzyme complex (hyperphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
Processive elongation complex (name copied from entity in Homo sapiens)
Elongin B:C complex (name copied from entity in Homo sapiens)
NELF complex (name copied from entity in Homo sapiens)
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The PTEN-regulating microRNA miR-26a is amplified in high-grade glioma and facilitates gliomagenesis in vivo
Active RNA Polymerase I (name copied from entity in Homo sapiens)
Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding, and angiogenesis activity
RNA Polymerase III:TFIIIB:TFIIIC:Type 2 Open Promoter Complex (name copied from entity in Homo sapiens)
TFIIIC (name copied from entity in Homo sapiens)
The porphobilinogen synthase catalyzed reaction mechanism
Production of phosphatidylinositol 5-phosphate by the phosphoinositide 3-phosphatase myotubularin in mammalian cells
Elongation complex prior to separation (name copied from entity in Homo sapiens)
Elongation complex with separated and uncleaved transcript (name copied from entity in Homo sapiens)
RNA Polymerase I Holoenzyme (name copied from entity in Homo sapiens)
Effects of cyclic GMP on smooth muscle relaxation
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RNA Polymearse II:NTP:TFIIF complex (name copied from entity in Homo sapiens)
pol II transcription complex containing 9 nucleotide long transcript (name copied from entity in Homo sapiens)
pol II transcription complex containing 11 nucleotide long transcript (name copied from entity in Homo sapiens)
pol II transcription complex containing 3 Nucleotide long transcript (name copied from entity in Homo sapiens)
pol II transcription complex containing 4 nucleotide long transcript (name copied from entity in Homo sapiens)
Early elongation complex with hyperphosphorylated Pol II CTD (name copied from entity in Homo sapiens)
Elongation complex (name copied from entity in Homo sapiens)
Pol II transcription complex containing extruded transcript to +30 (name copied from entity in Homo sapiens)
Pol II transcription complex with (ser5) phosphorylated CTD containing extruded transcript to +30 (name copied from entity in Homo sapiens)
Pol II Initiation complex with phosphodiester-PPi intermediate (name copied from entity in Homo sapiens)
Immature dendritic cells phagocytose apoptotic cells via alphavbeta5 and CD36, and cross-present antigens to cytotoxic T lymphocytes
pol II transcription complex (name copied from entity in Homo sapiens)
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40S:eIF3:eIF1A (name copied from entity in Homo sapiens)
ternary complex (name copied from entity in Homo sapiens)
43S complex (name copied from entity in Homo sapiens)
eIF3 subunits complex (name copied from entity in Homo sapiens)
eIF2:GTP (name copied from entity in Homo sapiens)
eIF5B:GTP (name copied from entity in Homo sapiens)
The product of the MLD gene is a member of the membrane fatty acid desaturase family: overexpression of MLD inhibits EGF receptor biosynthesis
eIF4F (name copied from entity in Homo sapiens)
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48S complex (name copied from entity in Homo sapiens)
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Human cytidine deaminase: purification of enzyme, cloning, and expression of its complementary DNA
80S:Met-tRNAi:mRNA:eIF5B:GTP (name copied from entity in Homo sapiens)
eIF4A subunits complex (name copied from entity in Homo sapiens)
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Retinoids for treatment of retinal diseases
Mechanisms, regulation and consequences of protein SUMOylation
TFIIIB:TFIIIC:Type 2 Promoter Complex (name copied from entity in Homo sapiens)
RNA Polymerase III:TFIIIB:TFIIIC:Type 2 Promoter Complex (name copied from entity in Homo sapiens)
Elongating RNA Polymerase III Transcription Complex (name copied from entity in Homo sapiens)
TFIIIB-Type 1 and 2 Promoter Selective Complex (name copied from entity in Homo sapiens)
eIF2 subunit complex (name copied from entity in Homo sapiens)
Maternal genetic effects, exerted by genes involved in homocysteine remethylation, influence the risk of spina bifida
multiubiquitinated Cyclin A associated with MCC:APC/C complex (name copied from entity in Homo sapiens)
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Cdc2:Cyclin A:MCC:APC/C complex (name copied from entity in Homo sapiens)
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Cyclin A:phospho-Cdc2(Thr 161) complex (name copied from entity in Homo sapiens)
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Paused RNA Polymerase III Transcription Complex (name copied from entity in Homo sapiens)
TFIIIC:Type 2 Promoter 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=193728
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193829
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10863.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193813
Signal Recognition Particle (name copied from entity in Homo sapiens)
SRP receptor (name copied from entity in Homo sapiens)
SRP:polypeptide+signal:ribosome (name copied from entity in Homo sapiens)
Translocon:TRAP (name copied from entity in Homo sapiens)
SRP receptor:SRP:ribosome:polypeptide+signal (name copied from entity in Homo sapiens)
TRAP Complex (name copied from entity in Homo sapiens)
membrane-bound ribosome:mRNA:polypeptide+signal (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_112535.8
polypeptide+signal:Translocon (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_144124.5
cleaved polypeptide:Translocon (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=3652042
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_13314.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644546
Regulation of PLK1 Activity at G2/M Transition
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644515
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644516
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10201.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193830
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644550
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644512
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644513
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644514
80S:Met-tRNAi:mRNA (name copied from entity in Homo sapiens)
eIF5B:GDP (name copied from entity in Homo sapiens)
eIF2:GDP: eIF2B (name copied from entity in Homo sapiens)
eIF2:GDP (name copied from entity in Homo sapiens)
eIF2B subunits complex (name copied from entity in Homo sapiens)
40S:Met-tRNAi:mRNA (name copied from entity in Homo sapiens)
ribosome:mRNA:polypeptide+signal (name copied from entity in Homo sapiens)
Purification and characterization of human Syk produced using a baculovirus expression system
phospho-L13a associated wth the 3' UTR GAIT element of ceruloplasmin mRNA within the translation initiation 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=193835
Antigen processing and presentation: TAPping into ABC transporters
43S: Ceruloplasmin mRNA:eIF4F:eIF4B:eIF4H:PABP (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_10821.1
60s ribosomal complex lacking L13a subunit (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_10380.2
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=3644549
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_118242.7
eRF3-GDP:eRF1:80S Ribosome:mRNA:tRNA Complex (name copied from entity in Homo sapiens)
Calmodulin:CaMK IV (name copied from entity in Homo sapiens)
Prefoldin (name copied from entity in Homo sapiens)
membrane-bound ribosome:mRNA:cleaved polypeptide (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_89387.9
PAK1 dimer (name copied from entity in Homo sapiens)
Signal Peptidase (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=3652046
RAC1/CDC42:PAK dimer (name copied from entity in Homo sapiens)
80S:Met-tRNAi:mRNA:aminoacyl-tRNA (name copied from entity in Homo sapiens)
RAC1/CDC42:p-S144,T423-PAK (name copied from entity in Homo sapiens)
80S Ribosome:mRNA:peptidyl-tRNA with elongating peptide (name copied from entity in Homo sapiens)
Active LIMK1 (name copied from entity in Homo sapiens)
eEF2:GTP (name copied from entity in Homo sapiens)
pCofilin: Active LIMK-1 (name copied from entity in Homo sapiens)
GTP bound eRF3 (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_10552.2
Adenylate cyclase (Mg2+ cofactor) (name copied from entity in Homo sapiens)
eRF3-GTP:eRF1:80S Ribosome:mRNA:peptidyl-tRNA 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=193103
PKA tetramer (name copied from entity in Homo sapiens)
eRF3-GDP:eRF1:80S Ribosome:mRNA:peptidyl-tRNA Complex (name copied from entity in Homo sapiens)
cAMP:PKA regulatory subunit (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=193124
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29368
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5251.2
Mother filament:branching complex:daughter filament (name copied from entity in Homo sapiens)
CCT/TriC(ADP):Sphingosine kinase 1 (name copied from entity in Homo sapiens)
Mother filament:ARP2/3:actin:GDP (name copied from entity in Homo sapiens)
Actin:ADP (name copied from entity in Homo sapiens)
CCT/TriC(ADP)-associated non-native tubulin (name copied from entity in Homo sapiens)
ARP3:ATP (name copied from entity in Homo sapiens)
CCT/TriC(ATP):unfolded tubulin complex (name copied from entity in Homo sapiens)
ARP2:ATP (name copied from entity in Homo sapiens)
CCT/TriC(ADP) (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_10773.2
CDC42-GTP:WASP/N-WASP (name copied from entity in Homo sapiens)
actin/tubulin-bound CCT/TriC(ADP) (name copied from entity in Homo sapiens)
ARP2/3 complex (ATP bound) (name copied from entity in Homo sapiens)
CCT/TriC(ATP)-associated actin (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=3644862
Activated WAVE2 and WASP/N-WASP:ARP2/3 complex:G-actin (name copied from entity in Homo sapiens)
CCT/TriC(ATP) (name copied from entity in Homo sapiens)
Mother filament:branching complex (name copied from entity in Homo sapiens)
tubulin-GTP folding intermediate (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=3644863
G-actin (name copied from entity in Homo sapiens)
CCT/TriC (ADP) associated actin (name copied from entity in Homo sapiens)
CDC42-GTP:p-WASP/p-N-WASP:WIP:SH3 proteins (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=3644864
Gap-filling DNA repair synthesis and ligation in GG-NER
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644865
The t(6;8)(q27;p11) translocation in a stem cell myeloproliferative disorder fuses a novel gene, FOP, to fibroblast growth factor receptor 1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644867
Prefoldin-associated actin/tubulin (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_107357.9
Purification and properties of phosphoribosyl pyrophosphate synthetase from rat liver
ISG15:UBE1L (name copied from entity in Homo sapiens)
pPLCgamma:PIP2 (name copied from entity in Homo sapiens)
pPAK1:Rac1-GTP (name copied from entity in Homo sapiens)
CaN catalytic alpha/beta:Zn++:Fe3+:CaM:Ca2+ (name copied from entity in Homo sapiens)
CaN catalytic alpha/beta:Zn++:Fe3+ (name copied from entity in Homo sapiens)
RasGRPs:DAG:Ca2+ (name copied from entity in Homo sapiens)
p-5Y-PKC-theta:DAG (name copied from entity in Homo sapiens)
NFAT:CaN:CaM (name copied from entity in Homo sapiens)
CaN alpha regulatory:Ca2+ (name copied from entity in Homo sapiens)
CaN:CaM:Ca2+ (name copied from entity in Homo sapiens)
Identification and characterization of human PMP34, a protein closely related to the peroxisomal integral membrane protein PMP47 of Candida boidinii
A GDP dissociation inhibitor that serves as a GTPase inhibitor for the Ras-like protein CDC42Hs
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644509
PPP3CA/B:Calmodulin (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=3644510
Calcineurin:Calmodulin (CaN:CaM) (name copied from entity in Homo sapiens)
Calcineurin alpha regulatory subunit:Calcium (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_10659.1
Calcineurin (CaN) (name copied from entity in Homo sapiens)
PPP3CA/B:Fe3+:Zn2+ (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=3644508
phospho-CaMK IV:Calmodulin (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=3644511
Beta-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors
CK2 Phosphorylated Condensin I (name copied from entity in Homo sapiens)
5-Phosphoribose 1-diphosphate biosynthesis
Synthesis of cytosolic 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) from D-ribose 5-phosphate
Condensin I (name copied from entity in Homo sapiens)
CDK1 Phosphorylated Condensin I (name copied from entity in Homo sapiens)
Casein kinase II (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_114241.8
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate [ChEBI:16618]
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=112158
ESPL1 Autocleaved (name copied from entity in Homo sapiens)
Ribose-5-phosphate isomerase deficiency: new inborn error in the pentose phosphate pathway associated with a slowly progressive leukoencephalopathy
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640091
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640092
Human intestinal glucose transporter expression and localization of GLUT5
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_86611.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651702
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_33489.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651703
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_105564.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4386.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=68452
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=69172
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642720
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642719
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642718
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5389.1
Ac-Cohesin:PDS5:p-CDCA5:WAPAL (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_30065.10
CCNB:p-T161-CDK1 (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=3642722
Sister Chromosomal Arms:p-STAG2,RAD21-Ac-Cohesin:PDS5:p-CDCA5:WAPAL (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=3642721
p-STAG2,RAD21-Ac-Cohesin:PDS5:p-CDCA5:WAPAL (name copied from entity in Homo sapiens)
Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_112667.8
p-STAG2,RAD21-Ac-Cohesin (name copied from entity in Homo sapiens)
Ac-Cohesin:PDS5:CDCA5:WAPAL (name copied from entity in Homo sapiens)
Sister Chromosomal Arms:Ac-Cohesin:PDS5:CDCA5:WAPAL (name copied from entity in Homo sapiens)
p-T161-CDK1:CCNB1 (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)
Sister Chromosomal Arms:Ac-Cohesin:PDS5:p-CDCA5:WAPAL (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_85243.9
Ac-Cohesin 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=3640072
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640083
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_34250.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640081
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640082
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_31925.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651873
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640090
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640089
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640088
EVH1/WH1 domains of VASP and WASP proteins belong to a large family including Ran-binding domains of the RanBP1 family
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2672.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=110756
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642709
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642714
p-T216,S274,S373-GORASP1:p-S37-GOLGA2:p-RAB1:GTP (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=3642713
p-RAB1:GTP (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_106369.9
GLUT4 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=3642715
p-T216,S274,S373-GORASP1:p-S37-GOLGA2:p-RAB1:GTP:PLK1 (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=29364
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=70106
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4941.2
DNA polymerase alpha:primase (name copied from entity in Homo sapiens)
Cdc45:CDK:DDK:Mcm10:pre-replicative complex (name copied from entity in Homo sapiens)
SLC11 family of H+-coupled metal-ion transporters NRAMP1 and DMT1
DNA polymerase epsilon:origin complex (name copied from entity in Homo sapiens)
ADP,ATP carrier protein, heart/skeletal muscle isoform T1
Ubiquinone biosynthesis protein COQ7 homolog
2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial ecNumber2.1.1.201/ecNumber
Hexaprenyldihydroxybenzoate methyltransferase, mitochondrial ecNumber2.1.1.114/ecNumber
Ubiquinone biosynthesis monooxygenase COQ6 ecNumber1.14.13.-/ecNumber
Para-hydroxybenzoate--polyprenyltransferase, mitochondrial
DDK (name copied from entity in Homo sapiens)
Decaprenyl-diphosphate synthase subunit 2 ecNumber2.5.1.91/ecNumber
Mcm10:active pre-replicative complex (name copied from entity in Homo sapiens)
Decaprenyl-diphosphate synthase subunit 1 ecNumber2.5.1.91/ecNumber
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=196066
active pre-replicative complex (name copied from entity in Homo sapiens)
CDK (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_4609.3
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=29366
CDT1:CDC6:ORC:origin complex (name copied from entity in Homo sapiens)
pre-replicative 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_2991.3
CDK:DDK:Mcm10:pre-replicative 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=3651877
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_103492.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651874
Mcm2-7 complex (name copied from entity in Homo sapiens)
CDC6:ORC:origin complex (name copied from entity in Homo sapiens)
Orc2 associated with MCM8 (name copied from entity in Homo sapiens)
ORC:origin (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_90700.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651704
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_94764.9
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Vertebrates have conserved capping protein alpha isoforms with specific expression patterns
Ectonucleotide pyrophosphatase/phosphodiesterase family member 7
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Orc1:Orc4:Orc5:Orc3:Orc2:origin (name copied from entity in Homo sapiens)
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ORC complex bound to origin (name copied from entity in Homo sapiens)
Orc5:Orc3:Orc2:origin (name copied from entity in Homo sapiens)
Orc4:Orc5:Orc3:Orc2:origin (name copied from entity in Homo sapiens)
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Orc2:origin (name copied from entity in Homo sapiens)
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Orc3:Orc2:origin (name copied from entity in Homo sapiens)
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Non-erythroid Rh glycoproteins: a putative new family of mammalian ammonium transporters
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Current knowledge of the large RhoGAP family of proteins
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Protein kinase C phosphorylates G12 alpha and inhibits its interaction with G beta gamma
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Activation of NMDA receptor upon glutamate binding and postsynaptic events
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Anomalous megakaryocytopoiesis in mice with mutations in the c-Myb gene
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Purification and partial characterization of aldehyde dehydrogenase from human erythrocytes.
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The unfolded protein response: a pathway that links insulin demand with beta-cell failure and diabetes
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Porcupine-mediated lipidation is required for Wnt recognition by Wls
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Acetylation of Smc3 by Eco1 is required for S phase sister chromatid cohesion in both human and yeast
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Active Wnt proteins are secreted on exosomes
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Destruction of cytochrome P-450 by ethylene. Structure of the resulting prosthetic heme adduct.
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DNA primase from KB cells. Characterization of a primase activity tightly associated with immunoaffinity-purified DNA polymerase-alpha.
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Transport of inorganic cations/anions and amino acids/oligopeptides
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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'.
At the end of this reaction, 1 molecule of 'Acetyl-CoA carboxylase 2 ' is present. This reaction takes place in the 'nucleus'.
At the end of this reaction, 1 molecule of 'citrate lyase monomer' is present. This reaction takes place in the 'nucleus'.
DNA polymerase zeta: new insight into eukaryotic mutagenesis and mammalian embryonic development.
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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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In the first of two salvage steps to maintain BH4 levels in the cell, sepiapterin is taken up by the cell and reduced by sepiapterin reductase (SRP) to form BH2 (Sawabe et al. 2008).
Sepiapterin reductase (SPR) (Ichinose et al. 1991) reduces DHNTP to tetrahydrobiopterin (BH4).
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).
Crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site
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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).
Isolation and partial characterization of SAA-an amyloid-related protein from human serum
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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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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Accurate cleavage and polyadenylation of exogenous RNA substrate.
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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.
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).
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).
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 (Thöny et al. 2000, Crabtree & Channon 2011, Schulz et al. 2008, Schmidt & 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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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).
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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).
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).
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.
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).
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Negative regulation of the wee1 protein kinase by direct action of the nim1/cdr1 mitotic inducer
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ChEBI:28477 7alpha,12alpha-dihydroxycholest-4-en-3-one
Mitochondrial COQ3 is an O-methyltransferase required in the reaction to convert 3-demethylubiquinol-10 (DeMQ10H2) to ubiquinol-10 (Q10H2) (Jonassen & Clarke 2000).
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).
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.
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.
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.
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).
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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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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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.
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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.
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Bestrophin and TMEM16-Ca(2+) activated Cl(-) channels with different functions
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Alcohol dehydrogenases, aldehyde dehydrogenases, and related enzymes
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.)
Cloning and identification of amino acid residues of human phospholipase C delta 1 essential for catalysis
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).
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
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).
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.
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.
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.
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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 '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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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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ISG15 Arg151 and the ISG15-conjugating enzyme UbE1L are important for innate immune control of Sindbis virus
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Purification and properties of human cytosolic folylpoly-gamma-glutamate synthetase and organization, localization, and differential splicing of its gene
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Mitochondrial phosphatase PTPMT1 is essential for cardiolipin biosynthesis
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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).
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).
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).
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 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).
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).
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).
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.
TIRAP/Mal, TRIF and TRAM. Differential utilization of these TIR
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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 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 APRT dimer catalyzes the reaction of adenine and 5-phospho-alpha-D-ribose 1-diphosphate to form AMP and pyrophosphate (Holden et al. 1979).
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).
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).
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).
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).
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 guanine deaminase (GDA) catalyzes the reaction of guanine and water to form xanthine and ammonia (Yuan et al. 1999). The active enzyme is a homodimer (Murphy et al. 2009).
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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)).
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).
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.
Identification of the human sphingolipid C4-hydroxylase, hDES2, and its up-regulation during keratinocyte differentiation
Regulation of the cyclin E gene by transcription factor E2F1
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).
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).
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).
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).
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).
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.
Bile salt and organic anion SLC transporters
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.
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.
Cytosolic AMP, GMP, and IMP stimulate the association of phosphoribosyl pyrophosphate amidotransferase (PPAT) dimers to form tetramers (Holmes et al. 1973a,b).
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.
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.
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.
ETF-ubiquinone oxidoreductase (ETF-QO), catalyzes the re-oxidation of reduced ETF, with ubiquinone as the electron acceptor.
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.
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Molecular scanning of insulin-responsive glucose transporter (GLUT4) gene in NIDDM subjects
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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Constitutive receptor activation by Crouzon syndrome mutations in fibroblast growth factor receptor (FGFR)2 and FGFR2/Neu chimeras
Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product
RNA Polymerase II holoenzyme complex (phosphorylated) (name copied from entity in Homo sapiens)
TFIIF (name copied from entity in Homo sapiens)
CAK (name copied from entity in Homo sapiens)
TFIIH (name copied from entity in Homo sapiens)
DNA polymerase alpha:primase:DNA polymerase alpha:origin complex (name copied from entity in Homo sapiens)
DNA polymerase epsilon (name copied from entity in Homo sapiens)
RNA polymerase II (phosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
CE:Pol II CTD:Spt5 complex (name copied from entity in Homo sapiens)
Capping complex (initial) (name copied from entity in Homo sapiens)
Capping complex (hydrolyzed) (name copied from entity in Homo sapiens)
Capping complex (intermediate) (name copied from entity in Homo sapiens)
Requirement of PIG-F and PIG-O for transferring phosphoethanolamine to the third mannose in glycosylphosphatidylinositol
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Cell signalling diversity of the Gqalpha family of heterotrimeric G proteins
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Stem-looped mRNA:ACF complex (name copied from entity in Homo sapiens)
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RNA Pol II with phosphorylated CTD: CE complex (name copied from entity in Homo sapiens)
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capped pre-mRNA:CBC:RNA Pol II (phosphorylated) complex (name copied from entity in Homo sapiens)
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RNA Polymerase II (phosphorylated):TFIIF:capped pre-mRNA (name copied from entity in Homo sapiens)
Capping complex (with freed 5'- GMP) (name copied from entity in Homo sapiens)
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Capping complex (GpppN..) (name copied from entity in Homo sapiens)
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Covalent CE:GMP intermediate complex (name copied from entity in Homo sapiens)
Cleavage and Polyadenylation Complex (name copied from entity in Homo sapiens)
Coenzyme Q biosynthesis: Coq6 is required for the C5-hydroxylation reaction and substrate analogs rescue Coq6 deficiency
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Synthesis of glycosylphosphatidylinositol (GPI)
Identification and expression of a cDNA for human hydroxypyruvate/glyoxylate reductase
Enzymic properties of different types of human erythrocyte glucose-6-phosphate dehydrogenase, with characterization of two new genetic variants
Choline-phosphate cytidylyltransferase B
Choline-phosphate cytidylyltransferase A
Phosphatidylethanolamine N-methyltransferase
Putative glycerophosphocholine phosphodiesterase GPCPD1
Glycerophosphodiester phosphodiesterase 5
15-Keto-prostaglandin F2alpha [ChEBI:760]
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Diacylglycerol cholinephosphotransferase 1
Phosphatidylinositol transfer proteins: from closed for transport to open for exchange
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(5Z,8Z,11Z,14Z)-20-Hydroxyicosa-5,8,11,14-tetraenoic 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=109395
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4841.2
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=3649820
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649821
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649823
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_143208.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1500581
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_124951.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641306
6xSLC35D1 (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_5157.1
Aquaporin-8 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=72073
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641253
Porcupine homolog is required for canonical Wnt signaling and gastrulation in mouse embryos
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GLUT1 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=3641208
GLUT3 tetramer (name copied from entity in Homo sapiens)
GLUT1:ATP (name copied from entity in Homo sapiens)
CYP2U1, a novel human thymus- and brain-specific cytochrome P450, catalyzes omega- and (omega-1)-hydroxylation of fatty acids
GLUT2 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=3641305
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641303
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641304
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641154
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641112
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641204
ABC7 dimer (name copied from entity in Homo sapiens)
GTP hydrolysis and joining of the 60S ribosomal subunit
MTABC3 dimer (name copied from entity in Homo sapiens)
ABCG5:ABCG8 heterodimer (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=3641107
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641096
ABCD2:ABCD3 (name copied from entity in Homo sapiens)
Execution of nonsense-mediated mRNA decay: what defines a substrate?
ABCD1:ABCD3 (name copied from entity in Homo sapiens)
ABCD1:ABCD2 (name copied from entity in Homo sapiens)
Contributions of proteomics to understanding phagosome maturation
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641212
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641214
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641215
Capped Intronless Histone pre-mRNA:CBP80:CBP20:SLBP (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=3641007
capped intronless pre-mRNA:CBC complex (name copied from entity in Homo sapiens)
CPSF:capped intronless pre-mRNA:CBC complex (name copied from entity in Homo sapiens)
CstF:CPSF:capped intronless pre-mRNA:CBC complex (name copied from entity in Homo sapiens)
HSD11B1 dimer (name copied from entity in Homo sapiens)
HSD17B1 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=3641087
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4848.1
ABCD1 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=72051
Role of gastrin peptides in carcinogenesis
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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=3641121
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641116
Purification of deoxyribonucleic acid polymerase delta from calf thymus: partial characterization of physical properties.
Capped Intronless Histone pre-mRNA:CBC 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=3641079
post exon ligation complex (name copied from entity in Homo sapiens)
U6 ATAC snRNP (name copied from entity in Homo sapiens)
U4 ATAC snRNP (name copied from entity in Homo sapiens)
U4 ATAC:U5:U6 ATAC Complex (name copied from entity in Homo sapiens)
U4 ATAC snRNP:U6 ATAC snRNP (name copied from entity in Homo sapiens)
U12 snRNP (name copied from entity in Homo sapiens)
ATAC B 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=3641093
ATAC A 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=3641111
U11 snRNP (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=3641146
ATAC C Complex (name copied from entity in Homo sapiens)
1-phosphatidylinositol-3-phosphate 5-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=3641138
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641088
hnRNP proteins (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=3641008
Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA
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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=3641059
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3989.1
RAD51:RAD52:DNA double strand break end complex (name copied from entity in Homo sapiens)
Functional expression of the human hZIP2 zinc transporter
RAD52:DNA double-strand break (name copied from entity in Homo sapiens)
FEN1:PCNA 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=3641148
Pol zeta 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=3641081
Pol zeta:damaged DNA template 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_4072.1
RAD50:MRE11 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=72039
LIG3:XRRC1-bound DNA strand containing the ligated residue (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=3641068
POL Beta: APE1-bound 5' incised DNA strand break containing first resynthesized base (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=3641063
APE1:DNA ligase I complex (name copied from entity in Homo sapiens)
APE1:FEN1 complex (name copied from entity in Homo sapiens)
Identification of TTP mRNA targets in human dendritic cells reveals TTP as a critical regulator of dendritic cell maturation
The predicted ATP-binding domains in the hexose transporter GLUT1 critically affect transporter activity.
Evolution, structure, and activation mechanism of family 3/C G-protein-coupled 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_3970.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641106
LIG3:XRCC1:POL Beta:DNA strand break containing replaced unligated residue (name copied from entity in Homo sapiens)
LIG3:XRCC1:POL Beta complex at site of base repair (name copied from entity in Homo sapiens)
LIG3:XRRC1 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=3641142
POL Beta: APE1-bound DNA strand break containing incision 5' to AP site (name copied from entity in Homo sapiens)
POL Beta-bound DNA strand break containing gap left by excised residue (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=71916
DNA containing an APE1-bound AP site (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=3641006
APE1-bound DNA strand break containing an incision 5' to an AP site (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=3641108
hNTH1 glycosylase:thymine glycol 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=3641083
DNA containing a hNTH1-bound apurinic/apyrimidinic site (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_5767.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=72046
hNTH1 glycosylase: foramidopyrimidine complex (name copied from entity in Homo sapiens)
Structural insights into the dehydroascorbate reductase activity of human omega-class glutathione transferases
From hematopoietic stem cells to platelets
DNA containing an hOGG1-bound apurinic/apyrimidinic site (name copied from entity in Homo sapiens)
DNA containing an MYH-bound apurinic/apyrimidinic site (name copied from entity in Homo sapiens)
hNTH1 glycosylase:dihydrouracil complex (name copied from entity in Homo sapiens)
hNTH1 glycosylase:cytosine glycol 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=3641077
Intramolecular disulfide bond is a critical check point determining degradative fates of ATP-binding cassette (ABC) transporter ABCG2 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_2529.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=72056
GABAB receptor:GABA (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=3641080
G-protein alpha (i): GTP (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=3641095
G-protein alpha (i):GTP:Adenylate cyclase (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_4415.1
MYH glycosylase:adenine 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=72055
hOGG1 glycosylase:8-oxo guanine 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=3641101
hOGG1 glycosylase: formamidopyrimidine 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=72052
COPII (Coat Protein 2) Mediated Vesicle Transport
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643862
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643863
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643860
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643879
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_157163.3
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=3643864
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_156087.3
Homodimer of 4 aminobutyrate aminotransferase (name copied from entity in Homo sapiens)
ATP6V1G dimer (name copied from entity in Homo sapiens)
GABAB receptor (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=3641072
ABCG2 dimer (name copied from entity in Homo sapiens)
Rho GTPases have diverse effects on the organization of the actin filament system
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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=3641105
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641129
ATP6V1B trimer (name copied from entity in Homo sapiens)
H2S biogenesis by human cystathionine gamma-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia
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ATP6V1A trimer (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=3641009
ATP6V1 (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=3641147
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641110
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643878
Phosphatidylinositol-4-phosphate 5-kinase type-1 alpha
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643880
Phosphatidylinositol-4-phosphate 5-kinase type-1 beta
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649713
Cloning, sequencing and expression of a cDNA encoding mammalian valyl-tRNA synthetase
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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=3649714
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643857
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649715
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643853
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649716
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643854
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649718
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_130731.5
Human Myt1 is a cell cycle-regulated kinase that inhibits Cdc2 but not Cdk2 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_123472.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1524083
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_124336.1
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).
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.
The polyprenyl diphosphate synthase consists of a tetramer comprising two units of decaprenyl-diphosphate synthase subunit 1 (PDSS1) and two units of decaprenyl-diphosphate synthase subunit 2 (PDSS2). It catalyses the combination of 2-trans,6-trans-farnesyl diphosphate (FPP) with isopentenyl diphosphate (IPPP) to form the polyisoprenoid tail all-trans-decaprenyl diphosphate (all-E-10PrP2) (Saiki et al. 2005, Tekle et al. 2008).
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).
Regulation and dysregulation of aquaporins in water balance disorders
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).
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).
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ChEBI:53020 (Glc)2 (GlcNAc)2 (Man)9 (PP-Dol)1
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CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1 ecNumber3.1.3.27/ecNumber
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ChEBI:53019 (Glc)3 (GlcNAc)2 (Man)9 (PP-Dol)1
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Human autoantibodies against the 54 kDa protein of the signal recognition particle block function at multiple stages
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).
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).
Neutral ceramidase (ASAH2) is an enzyme localised to the plasma membrane that catalyses the hydrolysis of ceramide to sphingosine and free fatty acid (Hwang et al. 2005, Galadari et al. 2006).
The steps involved in the synthesis of glycosphingolipids (sphingolipids with one or more sugars attached) are annotated here (Gault et al. 2010).
The main steps involved in de novo sphingolipid synthesis are annotated here (Merrill 2002, Gault et al. 2010).
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).
Beta-galactosidase can hydrolyse a galactose moeity from globosides to form cerebrosides. Here, lactosylceramide is hydrolysed to glucosylceramide (Asp et al. 1969).
Vitamin C: biosynthesis, recycling and degradation in mammals
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).
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).
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).
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).
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Lysophosphatidylinositol acyltransferase
Membrane-bound O-acyltransferase domain-containing protein 7
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Phosphatidylinositol transfer protein beta isoform
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CDP-diacylglycerol--inositol 3-phosphatidyltransferase
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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).
SGPP1 and 2 (sphingosine-1-phosphate phosphatase 1 and 2) enzymes associated with the endoplasmic reticulum membrane catalyze the hydrolysis of cytosolic sphingosine 1-phosphate to form sphingosine and orthophosphate (Johnson et al. 2003; Ogawa et al. 2003).
CDC6 association with the ORC:origin complex
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).
The structure of human mitochondrial branched-chain aminotransferase.
Acta Crystallogr D Biol Crystallogr 57:506-15
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SGPP1 and 2 (sphingosine-1-phosphate phosphatase 1 and 2) enzymes associated with the endoplasmic reticulum membrane catalyze the hydrolysis of cytosolic sphinganine 1-phosphate to form sphinganine (dihydrosphingosine) and orthophosphate (Johnson et al. 2003; Ogawa et al. 2003).
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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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).
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ACER3 (alkaline ceramidase 3) catalyzes the hydrolysis of phytoceramide to yield a free fatty acid (annotated here as stearate) and phytosphingosine. ACER3 mRNA is widely expressed in the body, although most abundant in placenta. Immunofluoresence studies of cultured cells over-expressing GFP-tagged protein suggest its localization to membranes of the endoplasmic reticulum (annotated here) and also the Golgi apparatus (Mao et al. 2001).
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).
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.
KDSR (3-ketodihydrosphingosine reductase) enzyme associated with the cytosolic face of the endoplasmic reticulum membrane catalyzes the reduction of 3-ketosphinganine by NADPH to form sphinganine (dihydrosphingosine) (Kihara and Igarashi 2004).
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Three-dimensional structure of 6-pyruvoyl tetrahydropterin synthase, an enzyme involved in tetrahydrobiopterin biosynthesis
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Cloning and in vitro expression of the human selenoprotein, type I iodothyronine deiodinase
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 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).
Mutation in cystatin C gene causes hereditary brain haemorrhage
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).
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).
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).
Prostaglandin reductase 1 (PTGR1) aka LTB4DH, a 15-oxoprostaglandin 13-reductase (Yokomizo et al. 1996), metabolises 15-oxo lipoxin A4 aka 15-keto-LXA4 (15k-LXA4) to produce 13,14-dihydro-15-keto-Lipoxin A4 (dhk-LXA4). This reaction has been inferred from a reaction in pig (Clish et al. 2000).
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).
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).
Lipoxins A4 (LXA4) and B4 (LXB4), structurally characterized from human neutrophils incubated with 15-hydroperoxy-eicosatetraenoic acid (15-HpETE), each contain three hydroxyl moieties and a conjugated tetraene. The third hydroxyl of LXA4 is positioned at C-6, and of LXB4 at C-14. The action of arachidonate 5-lipoxygenase (ALOX5), in concert with an arachidonate 12-lipoxygenase (ALOX12) or arachidonate 15-lipoxygenase (ALOX15) activity, has been shown to produce lipoxins by three distinct pathways. Neutrophil ALOX5 can produce and secrete leukotriene A4 (LTA4) that is taken up by platelets, where it is acted upon by ALOX12 to form lipoxins. Likewise, ALOX15s can generate either 15-hydroperoxy-eicosatetraenoic acid (15-HpETE) or 15-hydro-eicosatetraenoic acid (15-HETE) that can be taken up by monocytes and neutrophils, where highly expressed ALOX5 uses it to generate lipoxins. Finally, aspirin acetylated prostaglandin G/H synthase 2 (PTGS2), rendered unable to synthesize prostaglandins, can act as a 15-lipoxygenase. This leads to the formation of 15R-HETE and culminates in creation of epi-lipoxins, which have altered stereochemistry at the C-15 hydroxyl but similar biological potency (Chiang et al. 2006, Buczynski et al. 2009, Vance & Vance 2008).
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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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The role of aminoacyl-tRNA synthetases in genetic diseases
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Oligomeric structure of the multifunctional protein CAD that initiates pyrimidine biosynthesis in mammalian cells
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Purification and some properties of inorganic pyrophosphatase from human erythrocytes
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The mucopolysaccharidoses: a success of molecular medicine
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Spliceosomal Intermediate C Complex (name copied from entity in Homo sapiens)
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U1 snRNP (name copied from entity in Homo sapiens)
RNA Polymerase II holoenzyme complex (unphosphorylated) (name copied from entity in Homo sapiens)
RNA Polymerase II (unphosphorylated):TFIIF complex (name copied from entity in Homo sapiens)
capped, methylated pre-mRNA:CBC Complex (name copied from entity in Homo sapiens)
Spliceosomal E Complex (name copied from entity in Homo sapiens)
SF3A (name copied from entity in Homo sapiens)
SF3B (name copied from entity in Homo sapiens)
U2 snRNP (name copied from entity in Homo sapiens)
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Spliceosomal A Complex (name copied from entity in Homo sapiens)
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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]
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(GlcN)1 (Ino(acyl)-P)1 (Man)2 (EtN)1 (P)1
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6-O-[alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl]-O-acyl-1-phosphatidyl-1D-myo-inositol [ChEBI:53056]
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Receptor-to-effector signaling through G proteins: roles for beta gamma dimers as well as alpha subunits
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U6 snRNP (name copied from entity in Homo sapiens)
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U4 snRNP:U6 snRNP complex (name copied from entity in Homo sapiens)
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U4 snRNP (name copied from entity in Homo sapiens)
Spliceosomal B Complex (name copied from entity in Homo sapiens)
CPSF (name copied from entity in Homo sapiens)
snRNP Sm core complex (name copied from entity in Homo sapiens)
U5 snRNP (name copied from entity in Homo sapiens)
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CF I (name copied from entity in Homo sapiens)
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CstF (name copied from entity in Homo sapiens)
CF II (name copied from entity in Homo sapiens)
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A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex.
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Dock180 and ELMO1 proteins cooperate to promote evolutionarily conserved Rac-dependent cell migration
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Functional properties of a Drosophila homolog of the E2F1 gene
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The pathway "Signaling by EGFR in Cancer" shows "Signaling by constitutively active EGFR" in parallel with "Signaling by EGFR". This allows users to compare signaling by constitutively active EGFR cancer mutants with the wild-type EGFR protein. Red lines emphasize cancer related events and physical entities, while wild-type entities and events are shaded. Please refer to "Signaling by constitutively active EGFR" and "Signaling by EGFR" for detailed pathway summations.
Infection by Mycobacterium tuberculosis (Mtb) is soon countered by the host's immune system, the organism is however almost never eradicated; ten per cent of infections will develop into "open tuberculosis", while the other ninety per cent become "latent", a state that can persist for decades until loss of immune control. A third of the world's population is estimated to harbour latent tuberculosis. Latent infection involves the bacterium being internalized by macrophages where it stops and counters the innate immune answer (Russell 2011, Russell et al. 2010). When a status-quo is reached, Mtb enters a non-replicating persistent state (Barry et al. 2009, Boshoff & Barry 2005).
Alveolar macrophages normally develop their phagosome along the endolysosomal pathway. However, after having internalized Mtb, this development is arrested at an early stage and only includes acidification, nitric oxide and superoxide production, as well as the use of a few other proteins that can be gained from other endosomes which still can interact with the phagosome (Flannagan et al. 2009).
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).
After ligand-independent dimerization, FGFR1 fusions are trans-autophosphorylated on tyrosine residues (see for instance Popovici, 1998; Ollendorff, 1999; Guasch, 2000). Although the sites of tyrosine phosphorylation have not been mapped in the context of the fusion proteins, at least some of the same residues appear to be phosphorylated as in full length FGFR1. For instance, phospho-specific antibodies have demonstrated that TRIM24 is phosphorylated on Y653 and Y654, the activation loop tyrosines of FGFR1 (Belloni, 2005). Likewise, FGFR1 fusions with ZMYM2, BCR, FGFR1OP and TRIM24 all result in recruitment and phosphorylation of PLCgamma, and where mutational studies have been performed, mutation of the PLCgamma binding site Y766 has been shown to abrogate this signaling (Roumiantsev, 2004, Lelievre, 2008, Chase, 2007). In the case of BCR-FGFR1, the BCR moiety of the fusion protein has also been shown to be phosphorylated on at least one tyrosine residue, Y177, which results in the recruitment of GRB2 (Roumiantsev, 2004).
8p11 myeloproliferative syndrome (EMS) is a myeloproliferative disorder that rapidly progresses to acute myeloid leukemia if not treated (reviewed in Jackson, 2010, Knights and Cook, 2010). A characteristic feature of EMS is the presence of fusion proteins that contain the kinase domain of FGFR1 and the oligomerization domain of an unrelated protein. This is believed to promote the ligand independent dimerization and activation of the kinase domain. To date, there are 11 identified partners that form fusion proteins with FGFR1 in EMS: ZMYM2 (Xiao, 1998; Popovici, 1998; Reiter, 1998; Ollendorff, 1999; Xiao, 2000), FGFR1OP1 (Popovici, 1999), CNTRL (Guasch, 2000), BCR (Demiroglu, 2001), FGFR1OP2 (Grand, 2004), TRIM24 (Belloni, 2005), CUX1 (Wasag, 2011), MYO18A (Walz, 2005), CPSF6 (Hidalgo-Curtis, 2008), HERV-K (Guasch, 2003) and LRRFIP1 (Soler, 2009).
Amyloid is a term used to describe typically extracellular deposits of aggregated proteins, sometimes known as plaques. Abnormal accumulation of amyloid is amyloidosis, a term associated with diseased organs and tissues, particularly neurodegenerative diseases such as Alzheimer's, Parkinson's and Huntingdon's. Amyloid deposits consist predominantly of amyloid fibrils, rigid, non-branching structures that form ordered assemblies, characteristically with a cross beta-sheet structure where the sheets run parallel to the direction of the fibril (Sawaya et al. 2007). Often the fibril has a left-handed twist (Nelson & Eisenberg 2006). At least 27 human proteins form amyloid fibrils (Sipe et al. 2010). Many of these proteins have non-pathological functions; the trigger that leads to abnormal aggregations differs between proteins and is not well understood but in many cases the peptides are abnormal fragments or mutant forms arising from polymorphisms, suggesting that the initial event may be aggregation of misfolded or unfolded peptides. Early studies of Amyloid-Beta assembly led to a widely accepted model that assembly was a nucleation-dependent polymerization reaction (Teplow 1998) but it is now understood to be more complex, with multiple 'off-pathway' events leading to a variety of oligomeric structures in addition to fibrils (Roychaudhuri et al. 2008). An increasing body of evidence suggests that these oligomeric forms are primarily responsible for the neurotoxic effects of Amyloid-beta (Roychaudhuri et al. 2008), alpha-synuclein (Winner et al. 2011) and tau (Dance & Strobel 2009, Meraz-Rios et al. 2010). Amyloid oligomers are believed to have a common structural motif that is independent of the protein involved and not present in fibrils (Kayed et al. 2003). Conformation dependent, aggregation specific antibodies suggest that there are 3 general classes of amyloid oligomer structures (Glabe 2009) including annular structures which may be responsible for the widely reported membrane permeabilization effect of amyloid oligomers. Toxicity of amyloid oligomers preceeds the appearance of plaques in mouse models (Ferretti et al. 2011). Fibrils are often associated with other molecules, notably heparan sulfate proteoglycans and Serum Amyloid P-component, which are universally associated and seem to stabilize fibrils, possibly by protecting them from degradation.
Amyloid fibril formation is associated with a wide range of diseases (Chiti & Dobson 2006), thoughthe accumulation and deposition of fibrillar material does not correlate well with disease pathogenesis and it is now widely believed that oligomeric amyloid forms are largely responsible for the cytotoxic effects of amyloid (Glabe 2009). Fibrils have been described as more like crystalline polymer structures than the protein monomers they are derived from (Wetzel et al. 2007). Fibril formation is usually preceded by the association of monomers into oligomeric structures (Kodali & Wetzel 2007). For Beta-amyloid, these are spherical structures with around 12 units (Bernstein et al. 2005). Larger structures called protofibrils are also observed, non-spherical filamentous structures lacking a periodic substructure (Goldsbury 2005).
FGFR1 fusions with ZMYM2, BCR, FGFR1OP and TRIM24 all result in recruitment and phosphorylation of PLCgamma, and where mutational studies have been performed, mutation of the PLCgamma binding site Y766 has been shown to abrogate this signaling (Guasch, 2001; Roumiantsev, 2004, Lelievre, 2008, Chase, 2007). In the case of BCR-FGFR1 and ZMYM2-FGFR1, mutation of the PLCgamma binding site significantly decreased the transformative phenotype of the FGFR1 fusion (Roumiantsev, 2004).
In a murine mouse model of ZNF198-FGFR1-induced EMS, treatment with the FGFR-inhibitor Midostaurin (PKC412) resulted in prolonged survival (Chen, 2004). Similarly, growth of ZNF-198-FGFR1-, FGFR1OP2-FGFR1-, and BCR-FGFR1-expressing lines is blocked by treatment with FGFR-inhibitors (Demiroglu, 2001; Gu, 2006; Chase, 2007; Zhen, 2007; Wasag, 2011).
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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.
The UBA2:SAE1 complex catalyzes the formation of a thioester bond between SUMO3 and cysteine-173 of UBA2 (Tatham et al. 2001, Werner et al. 2009). ATP reacts with the C-terminal glycine residue of SUMO3 to yield pyrophosphate and a transient intermediate, SUMO3 adenylate, which then reacts with the thiol group of the cysteine residue on UBA2.
The UBA2:SAE1 complex catalyzes the formation of a thioester bond between SUMO2 and cysteine-173 of UBA2 (Tatham et al. 2001, Werner et al. 2009). ATP reacts with the C-terminal glycine residue of SUMO2 to yield pyrophosphate and a transient intermediate, SUMO2 adenylate, which then reacts with the thiol group of the cysteine residue on UBA2.
SUMO3 is transferred from cysteine-173 of UBA2 to cysteine-93 of UBC9 (UBE2I) in a transthiolation reaction (Tatham et al. 2001, Werner et al. 2009).
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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).
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SUMO2 is transferred from cysteine-173 of UBA2 to cysteine-93 of UBC9 (UBE2I) in a transthiolation reaction (Tatham et al. 2001, Werner et al. 2009).
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),
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).
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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.
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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.
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Ankyrin repeat domain-containing protein 1
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ATP-binding cassette sub-family A member 1
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Mucopolysaccharidosis IV A (MPS IVA, MPS4A, Morquio's syndrome, Morquio's; MIM:253000) is a rare, autosomal recessive mucopolysaccharide storage disease, first described simultaneously in 1929 by L Morquio (Morquio L, Sur une forme de distrophie familiale, Bull Soc Pediat, Paris, 27, 1929, 145-152) and JF Brailsford (Brailsford, JF, Chondro-osteo-dystrophy: roentgenographic and clinical features of child with dislocation of vertebrae, Am j Surg, 7, 1929, 404-410). MPSIVA is caused by a deficiency in N-acetylgalactosamine 6-sulfatase (GALNS; MIM:612222) which normally hydrolyses 6-sulfate groups of N-acetylgalactosamine 6-sulfate units of chondroitin sulfate (CS) and of galactose 6-sulfate units of keratan sulfate (KS) (Matalon et al. 1974). The result is accumulation of KS/DS in cells and overexcretion in urine. Severe osteochondrodysplasia is a commonly seen phenotype for this disease. The severity of the disease is variable but severe cases limits lifespan to their 20's or 30's (Prat et al. 2008, Tomatsu et al. 2011). The gene coding for human GALNS was mapped to chromosome 16q24.3 (Masuno et al. 1993) and its structure described at the same time by two independent groups as comprising 14 exons and spanning approximately 40-50 kb (Nakashima et al.1994, Morris et al.1994).
Mucopolysaccharidosis III (Sanfilippo syndrome) was described in 1963 by a pediatrician named Sylvester Sanfilippo (J. Pediat. 63: 837-838, 1963, no reference). Mucopolysaccharidosis type IIID (MPS IIID, Sanfilippo syndrome D, MIM:252940) is an autosomal recessive genetic disorder due to the loss of N-acetyl-D-glucosamine 6-sulfatase (GNS; MIM:607664), that hydrolyses the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of the glycosaminoglycans (GAGs) heparan sulfate and keratan sulfate. GNS is localized to chromosome 12q14 and has 14 exons spanning 46 kb (Robertson et al. 1988, Mok et al. 2003). Loss of enzyme activity leads to lysosomal accumulation and urinary excretion of heparan sulfate and N-acetylglucosamine 6-sulfate residues (Mok et al. 2003). Keratan sulphate does not accumulate in MPS IIID, as beta-linked N-acetyl-D-glucosamine 6-sulphate can be cleaved by beta-hexosaminidase A (Kresse et al. 1980). This disorder is characterized by progressive mental deterioration but only moderate physical abnormalities and death duing the second or third decade of life, presenting a phenotype similar to MPSIIIA (Jones et al. 1997, de Ruijter et al. 2011).
Mucopolysaccharidosis III (Sanfilippo syndrome) was described in 1963 by a pediatrician named Sylvester Sanfilippo (J. Pediat. 63: 837838, 1963, no reference). Mucopolysaccharidosis type IIIC (MPS IIIC, Sanfilippo syndrome C; MIM:252930) is an autosomal recessive genetic disorder due to the loss of heparan alpha-glucosaminide N-acetyltransferase (HGSNAT; MIM:610453) that normally acetylates the non-reducing terminal alpha-glucosamine residue of heparan sulfate. The molecular defects underlying MPS IIIC remained unknown for almost three decades due to the low tissue content and instability of HGSNAT. But, during the last decade, the gene was cloned in parallel by two different groups and shown to contain 18 exons and span approximately 62Kb (Fan et al. 2006, Hrebicek et al. 2006). Loss of HGSNAT results in build up of this glycosaminglycan (GAG) in cells and tissues and is characterized by severe central nervous system degeneration but only with mild somatic disease and death occurs typically during the second or third decade of life (Kresse et al. 1978, Klein et al. 1978, Feldhammer et al. 2009, de Ruijter et al. 2011).
Mucopolysaccharidosis III (Sanfilippo syndrome) was described in 1963 by a pediatrician named Sylvester Sanfilippo (J. Pediat. 63: 837838, 1963, no reference). MPS IIIB (Mucopolysaccharidosis type IIIB, MPS IIIB, Sanfilippo syndrome type B; MIM:252920) is an autosomal recessive genetic disorder due to loss of function of alpha-N-acetylglucosaminidase (NAGLU; MIM:609701), involved in the hydrolysis of terminal non-reducing N-acetylglucosamine residues in heparan sulfate (HS) The gene encoding NAGLU was cloned in 1996 by Zhao and colleagues. It contains 6 exons and spans 8.3 kb on chromosome 17q21 (Zhao et al. 1996). MPSIIIB is characterized by severe CNS retardation but only mild somatic disease and death usually occurs in the second or third decade of life (Zhao et al. 1996, Yogalingam & Hopwood 2001, de Ruijter et al. 2011). MPS IIIB shows extensive molecular heterogeneity (Schmidtchen et al. 1998).
Mucopolysaccharidosis III (MPS III, Sanfilippo syndrome) was described in 1963 by a pediatrician named Sylvester Sanfilippo (J. Pediat. 63: 837-838, 1963, no reference). Mucopolysaccharidosis IIIA (MPS IIIA, Sanfilippo syndrome A, MIM:252900) is a rare, autosomal recessive lysosomal storage disease characterised by severe CNS degeneration in early childhood leading to death between 10 and 20 years of age. A deficiency of the enzyme N-sulphoglucosamine sulphohydrolase (SGSH, MIM:605270), which normally hydrolyses the sulfate group from the terminal N-sulphoglucosamine residue of heparan sulfate (HS), leads to the build-up of HS in cells and tissues and its presence in urine (van de Kamp et al. 1981, Yogalingam & Hopwood 2001, de Ruijter et al. 2011). The gene encoding N-sulfoglucosamine sulfohydrolase, SGSH, was cloned in 1995 (Scott et al.1995) and, later, shown to contain 8 exons spanning approximately 11 kb (Karageorgos et al. 1996).
Mucopolysaccharidosis II (MPS II, Hunter syndrome, MIM:309900) is an X-linked, recessive genetic disorder which therefore primarily affects males. MPS II was first described in 1917, by Major Charles Hunter (Hunter 1917) and is caused by a deficiency (or absence) of iduronate-2-sulfatase (IDS, MIM:300823), which would normally hydrolyse the 2-sulfate groups of the L-iduronate 2-sulfate units of dermatan sulfate, heparan sulfate and heparin. Without IDS, these GAGs accumulate in the body and are excessively excreted in urine. Although the disease was known since the early 1970s, being the first MPS to be defined clinically in humans, it wasnt until the 1990s that IDS was cloned. It is now known to be localized to Xq28 (Wilson et al. 1991) and contain 9 exons (Flomen et al. 1993) spanning approximately 24 kb (Wilson et al. 1993). Build up can occur in the liver and spleen as well as in the walls and valves of the heart (reduced hepatic and cardiac function, liver/spleen hepatosplenomegaly), airways (leading to obstructive airway disease), all major joints and bones (joint stiffness and skeletal deformities) and in brain (severe mental retardation). The rate of progression and degree of severity of the disorder can be different for each person with MPS II. Severe forms of the disorder can result in death in childhood whereas those with a "milder" form can expect to live to their 20's or 30's. Some patients even survive into their fifth and sixth decades of life (Wraith et al. 2008, Beck 2011).
Molecular basis of mitochondrial fatty acid oxidation defects.
Mucopolysaccharidosis type IX (MPS IX, Natowicz syndrome, Hyaluronidase deficiency, MIM:601492) is a rare lysosomal storage disease characterized by high hyaluronan (HA) concentration in the serum resulting from deficiency in hyaluronidase 1 (HYAL1, MIM:607071) which normally hydrolyses 1-4 linkages between N-acetylglucosamine (GlcNAc) and D-glucuronate (GlcA) residues. Symptoms of MPS IX are periodically painful soft tissue masses around the joints, acquired short stature and erosion of the hip joint, although joint movement and intelligence are normal (Natowicz et al. 1996, Triggs-Raine et al. 1999).
Mucopolysaccharidosis type VII (MPS VII, Sly syndrome, beta-glucuronidase deficiency; MIM:253220) is an autosomal recessive lysosomal storage disease characterized by a deficiency of the enzyme beta-glucuronidase (GUSB; MIM:611499) which would normally cleave glucuronide residues from dematan sulphate, keratan sulphate and chondroitin sulphate, resulting in build up of these GAGs in cells and tissues (Sly et al. 1973). The gene encoding GUSB is 21 kb long, contains 12 exons and gives rise to two different types of cDNAs, through an alternate splicing mechanism (Miller et al. 1990). It maps to 7q11.21-q11.22 (Speleman et al. 1996). The phenotype is highly variable, ranging from severe causing death, non-immune hydrops fetalis (Vervoort et al. 1996) to mild forms with survival into adulthood (Storch et al. 2003). Most patients with the intermediate phenotype show hepatomegaly, skeletal anomalies, coarse facies, and variable degrees of mental impairment (Shipley et al. 1993, Tomatsu et al. 2009).
Mucopolysaccharidosis type VI (MPS VI, Maroteaux-Lamy syndrome, polydystrophic dwarfism; MIM:253200) is an autosomal recessive lysosomal storage disorder caused by a deficiency in arylsulfatase B (ARSB, N-acetyl-galactosamine 4-sulfatase; MIM:611542). It is named after two French physicians, Pierre Maroteaux and Maurice Emil Joseph Lamy. Maroteaux first described this disorder as a novel dysostosis associated with increased urinary excretion of chondroitin sulfate (CS; Maroteaux et al. 1963). The gene encoding ARSB is mapped to chromosome 5q11-q13 (Fidzianska et al. 1984) and contains 8 exons spanning about 206 kb (Karangeorgos et al. 2007). Defective ARSB results in build up of dermatan sulfate (DS) and chondroitin sulfate (CS) in soft tissues causing compression and blockages in blood vessels, nerves, trachea, corneal clouding and disrupting normal bone development. Symptoms are similar to MPS I but with normal intelligence generally (Rapini et al. 2007, Valayannopoulos et al. 2010).
Defects in beta-galactosidase (GLB1; MIM:611458) can result in GM1 gangliosidosis (GM1; MIM:230500) (Nishimoto et al. 1991) (not described here), with several phenotypes indicating mental deterioration, as well as in mucopolysaccharidosis IVB, a characteristic mucopolysaccharidosis with no neurological symptoms (Callahan 1999). Mucopolysaccharidosis IVB (MPS IVB, Morquio's syndrome B; MIM:253010) is a rare, autosomal recessive mucopolysaccharide storage disease characterized by intracellular accumulation of keratan sulfate (KS), skeletal dysplasia and corneal clouding. There is no central nervous system involvement, intelligence is normal and there is increased KS excretion in urine (Suzuki et al. "Beta-galactosidase deficiency (beta-galactosidosis): GM1 gangliosidosis and Morquio B disease", p3775-3809 in Stryer et al. 2001). MPSIVB is caused by a defect in betagalactosidase (GLB1), which normally cleaves terminal galactosyl residues from glycosaminoglycans, gangliosides and glycoproteins. The GLB1 gene spans 62.5 kb and contains 16 exons (Oshima et al.1988, Santamaria et al. 2007) and maps to chromosome 3p21.33 (Takano & Yamanouchi 1993).
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Mechanistic studies on phosphopantothenoylcysteine decarboxylase: trapping of an enethiolate intermediate with a mechanism-based inactivating agent
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8p11 myeloproliferative syndrome (EMS) is an aggressive disorder that is associated with a translocation event at the FGFR1 gene on chromosome 8p11. Typical symptoms upon diagnosis include eosinophilia and associated T-cell lymphoblastic lymphoma; the disease rapidly advances to acute leukemia, usually of myeloid lineage. At present the only effective treatment is allogenic stem cell transplantation (reviewed in Jackson, 2010). At the molecular level, EMS appears to be caused by translocation events on chromosome 8 that create gene fusions between the intracellular domain of FGFR1 and an N-terminal partner gene that encodes a dimerization domain. The resulting fusion protein dimerizes in a ligand-independent fashion based the N-terminal domain provided by the partner protein and stimulates constititutive downstream FGFR1 signaling without altering the intrisic kinase activity of the receptor. To date, 11 partner genes have been identified: ZMYM2, FGFR1OP, FGFR1OP2, HERVK, TRIM24, CUX1, BCR, CEP110, LRRFIP1, MYO18A and CPSF6, although not all have been functionally characterized (reviewed in Jackson, 2010, Turner and Grose, 2010; Wesche, 2011). Where examined, cell lines carrying FGFR1 fusion genes have been shown to be transforming and to support IL3-independent proliferation through anti-apoptotic, prosurvival pathways(Lelièvre, 2008; Ollendorff, 1999; Chase, 2007; Guasch, 2001; Wasag 2011; Roumiantsev, 2004; Demiroglu, 2001; Smedley, 1999). Signaling appears to occur predominantly through PLCgamma, PI3K and STAT signaling, with a more minor contribution from MAPK activation. Because the fusion proteins lack the FRS2-binding site, the mechanism of MAPK activation is unclear. Recruitment of GRB2:SOS1 through recruitment of SHC is one possibility (Guasch, 2001).
Dissociation from the activated receptor quickly follows phosphorylation of PLC-gamma. Phosphorylated PLC-gamma catalyzes the hydrolysis of phosphatidylinositol(4, 5)bisphosphate to generate two second messengers, diacylglycerol and inositol (1,4,5) triphosphate.
A number of skeletal and developmental diseases have been shown to arise as a result of mutations in the FGFR1, 2 and 3 genes. These include dwarfism syndromes (achondroplasia, hypochondroplasia and the neonatal lethal disorders thanatophoric dysplasia I and II), as well as craniosynostosis disorders such as Pfeiffer, Apert, Crouzon, Jackson-Weiss and Muenke syndromes (reviewed in Webster and Donoghue 1997; Burke, 1998, Cunningham, 2009; Harada, 2009). These mutations fall into four general regions of the receptor: a) the immunoglobulin (Ig)-like domain II-III linker region, b) the alternatively spliced second half of the Ig III domain, c) the transmembrane domain and d) the tyrosine kinase domain (reviewed in Webster and Donoghue, 1997). With the exception of mutations in class b), which affect only the relevant splice variant, these mutations may be present in either the 'b' or 'c' isoforms. These activating mutations affect FGFR function by altering or expanding the ligand-binding range of the receptors (see for instance Ibrahimi, 2004a), by promoting ligand-independent dimerization (for instance, Galvin,1996; Neilson and Friesel, 1996; d'Avis,1998) or by increasing the activity of the kinase domain (for instance, Webster, 1996; Naski, 1996; Tavormina, 1999; Bellus, 2000). Thus, a number of the point mutations found in FGFR receptors alter their activity without altering their intrinsic kinase activity. Many of the mutations that promote constitutive dimerization do so by creating or removing cysteine residues; the presence of an unpaired cysteine in the receptor is believed to promote dimerization through the formation of intramolecular disulphide bonds (Galvin, 1996; Robertson, 1998). Paralogous mutations at equivalent positions have been identified in more than one FGF receptor, sometimes giving rise to different diseases. For instance, mutation of the highly conserved FGFR2 Ser252-Pro253 dipeptide in the region between the second and third Ig domain is responsible for virtually all cases of Apert Syndrome (Wilkie, 1995), while paralogous mutations in FGFR1 (S252R) and FGFR3 (P250R) are associated with Pfeiffer and Crouzon syndromes, respectively (Bellus, 1996). FGFR4 is unique in that mutations of this gene are not known to be associated with any developmental disorders. Recently, many of the same activating mutations in the FGFR genes that have been characterized in skeletal and developmental disorders have begun to be identified in a range of cancers (reviewed in Turner and Gross, 2010; Greulich and Pollock, 2011; Wesche, 2011). The best established link between a somatic mutation of an FGFR and the development of cancer is in the case of FGFR3, where 50% of bladder cancers have mutations in the FGFR3 coding sequence. Of these mutations, which largely match the activating mutations seen in thanatophoric dysplasias, over half occur at a single residue (S249C) (Cappellen, 1999; van Rhijn, 2002). Activating mutations have also been identified in the coding sequences of FGFR1, 2 and 4 (for review, see Wesche, 2011) In addition to activating point mutations, the FGFR1, 2 and 3 genes are subject to misregulation in cancer through gene amplification and translocation events, which are thought to lead to overexpression and ligand-independent dimerization (Weiss, 2010; Turner, 2010; Kunii, 2008; Takeda, 2007; Chesi, 1997; Avet-Loiseau, 1998; Ronchetti, 2001). It is important to note, however, that in each of these cases, the amplification or translocation involve large genomic regions encompassing additional genes, and the definitive roles of the FGFR genes in promoting oncogenesis has not been totally established. In the case of FGFR1, translocation events also give rise to FGFR1 fusion proteins that contain the intracellular kinase domain of the receptor fused to a dimerization domain from the partner gene. These fusions, which are expressed in a pre-leukemic myeloproliferative syndrome, dimerize constitutively based on the dimerization domain provided by the fusion partner and are constitutively active (reviewed in Jackson, 2010).
The FGFR1 gene has been shown to be subject to activating mutations, chromosomal rearrangements and gene amplification leading to a variety of proliferative and developmental disorders depending on whether these events occur in the germline or arise somatically (reviewed in Webster and Donoghue, 1997; Burke, 1998; Cunningham, 2007; Wesche, 2011; Greulich and Pollock, 2011). Activating mutation P252R in FGFR1 is associated with the development of Pfeiffer syndrome, characterized by craniosynostosis (premature fusion of several sutures in the skull) and broadened thumbs and toes (Muenke, 1994; reviewed in Cunningham, 2007). This residue falls in a highly conserved Pro-Ser dipeptide between the second and third Ig domains of the extracellular region of the receptor. The mutation is thought to increase the number of hydrogen bonds formed with the ligand and to thereby increase ligand-binding affinity (Ibrahimi, 2004a). Unlike other FGF receptors, few activating point mutations in the FGFR1 coding sequence have been identified in cancer. Point mutations in the Ig II-III linker analagous to the P252R Pfeiffer syndrome mutation have been identified in lung cancer and melanoma (Ruhe, 2007; Davies, 2005), and two kinase-domain mutations in FGFR1 have been identified in glioblastoma (Rand, 2005, Network TCGA, 2008). In contrast, FGFR1 is a target of chromosomal rearrangements in a number of cancers. FGFR1 has been shown to be recurrently translocated in the 8p11 myeloproliferative syndrome (EMS), a pre-leukemic condition also known as stem cell leukemia/lymphoma (SCLL) that rapidly progresses to leukemia. This translocation fuses the kinase domain of FGFR1 with the dimerization domain of one of 10 identified fusion partners, resulting in the constitutive dimerization and activation of the kinase (reviewed in Jackson, 2010). Amplification of the FGFR1 gene has been implicated as a oncogenic factor in a range of cancers, including breast, ovarian, bladder, lung, oral squamous carcinomas, and rhabdomyosarcoma (reviewed in Turner and Grose, 2010; Wesche, 2011; Greulich and Pollock, 2011), although there are other candidate genes in the amplified region and the definitive role of FGFR1 has not been fully established.
PLCgamma is phosphorylated by activated FGFR, resulting in PLCgamma activation, stimulation of phosphatidyl inositol hydrolysis and generation of two second messengers, diacylglycerol and inositol (1,4,5) P3.
Mucopolysaccharidosis type I (MPS I, Hurler syndrome, Hurler's disease, gargoylism, Scheie, Hirler-Scheie syndrome; MIM:607014, 607015 and 607016) is an autosomal recessive genetic disorder where there is a deficiency of alpha-L iduronidase (IDUA, MIM:252800), a glycosidase that removes non-reducing terminal alpha-L-iduronide residues during the lysosomal degradation of the glycosaminoglycans heparan sulphate and dermatan sulphate (McKusick 1959). In 1992, Scott and colleagues were able to clone and purify the gene that encodes this enzyme, IDUA, demonstrating that it spans approximately 19 kb and contains 14 exons (Scott et al. 1992). Hurler syndrome is named after a German paediatrician Gertrud Hurler (1919, no reference available). The result is build up of heparan sulfate and dermatan sulfate in the body and increased urinary excretion of these GAGs. Symptoms and signs include hepatosplenomegaly, dwarfism, unique facial features, corneal clouding, retinopathy, progressive mental retardation appears during childhood and early death can occur due to organ damage (Campos & Monaga 2012). MPS I is divided into three subtypes, ranging from severe to mild phenotypes; Mucopolysaccharidosis type IH (MPSIH, Hurler syndrome, MIM:607014), mucopolysaccharidosis type IH/S (MPSIH/S, HurlerScheie syndrome, MIM: 607015) and mucopolysaccharidosis type IS (MPSIS, Scheie syndrome, MIM: 607016) respectively (McKusick 1972).
Extracellular IL4I1 catalyzes the reaction of phenylalanine, water, and molecular oxygen to form keto-phenylpyruvate, ammonia, and hydrogen peroxide. IL4I1, inferred to form a complex with FAD, has L-amino acid oxidase activity and with a strong preference for phenylalanine. The enzyme, found both in lysosomes and secreted into the extracellular space, is produced in the body by myeloid and dedritic cells (Boulland et al. 2007).
The pathway 'Signaling by FGFR in disease' shows 'Signaling by FGFR mutants' in parallel with the wild-type pathway 'Signaling by FGFR', allowing users to compare disease and normal events. FGFR mutants and events associated with germline diseases and cancer are highlighted in red. The wild-type pathway is shaded in the background. For detailed pathway summations, please see 'Signaling by FGFR mutants' and 'Signaling by FGFR'.
Phenylalanine hydroxylase (PAH) catalyzes the conversion of phenylalanine to tyrosine. In the absence of functional PAH, phenylalanine accumulates to high levels in the blood (Mitchell and Scriver 2010) and is converted to phenylpyruvate and phenyllactate (Clemens et al. 1990; Langenbeck et al. 1992). The extent of these conversions is modulated by genetic factors distinct from PAH, as siblings with the identical PAH defect can produce different amounts of them (Treacy et al. 1996). Both L-amino acid oxidase (Boulland et al. 2004) and Kynurenine--oxoglutarate transaminase 3 (Han et al. 2004) can catalyze the conversion of phenylalanine to phenylpyruvate and lactate dehydrogenase can catalyze the conversion of the latter molecule to phenyllactate (Meister 1951). Elevated levels of phenylalanine, phenylpyruvate, and phenyllactate are all thought to contribute to the symptoms of phenylketonuria. One possible target is the metabolism of kynurenine.
CCBL1 (KAT1) catalyzes the reaction of phenylalanine and oxaloacetate to form keto-phenylpyruvate and aspartate. The active form of CCBL1 is a homodimer with one molecule of pyridoxal phosphate bound to each monomer (Rossi et al. 2004). CCBL1 (KAT1) acts on phenylalanine and kynurenine with comparable efficiencies (Han et al. 2004), consistent with the idea that when phenylalanine levels are elevated CCBL1 (KAT1) activity could be a major source of phenylpyruvate. Oxaloacetate is one of several 2-oxoacids that function efficiently in CCBL1-mediated transamination (Han et al. 2004). Notably, neither tyrosine aminotransferase (Sivaraman and Kirsch 2006) nor glutamate-oxaloacetate aminotransferase (Cammarata and Cohen 1951) acts on phenylalanine.
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Biotinylation of biotinidase following incubation with biocytin
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Selective inhibition of 2-AG hydrolysis enhances endocannabinoid signaling in hippocampus
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Dopamine- and cAMP-regulated phosphoprotein, Mr 32 kDa (DARPP-32), was identified as a major target for dopamine and protein kinase A (PKA) in striatum. Recent advances now indicate that regulation DARPP-32 phosphorylation provides a mechanism for integrating information arriving at dopaminoceptive neurons, in multiple brain regions, via a variety of neurotransmitters, neuromodulators, neuropeptides, and steroid hormones. Activation of PKA or PKG stimulates DARPP-32 phosphorylation at Thr34, converting DARPP-32 into a potent inhibitor of protein phosphatase-1 (PP-1). DARPP-32 is also phosphorylated at Thr75 by Cdk5, converting DARPP-32 into an inhibitor of PKA. Thus, DARPP-32 has the unique property of being a dual-function protein, acting either as an inhibitor of PP-1 or of PKA.
Opioids are chemical substances similar to opiates, the active substances found in opium (morphine, codeine etc.). Opioid action is mediated by the receptors for endogenous opioids; peptides such as the enkephalins, the endorphins or the dynorphins. Opioids possess powerful analgesic and sedative effects, and are widely used as pain-killers. Their main side-effect is the rapid establishment of a strong addiction. Opioids receptors are G-protein coupled receptors (GPCR). There are four classes of receptors: mu (MOR), kappa (KOR) and delta (DOR), and the nociceptin receptor (NOP).
When dissociated Galpha-GTP and Gbeta-gamma can activate or inhibit different signalling cascades and effector proteins. The precise pathways depends on the identity of the alpha and beta/gamma subtypes.
PP2B (calcineurin) is a calcium-dependent, calmodulin-stimulated protein phosphatase. It comprises of two components; a catalytic subunit and a regulatory subunit which confers calcium sensitivity to the complex. PP2B is in equilibrium between active and inactive forms. Because the affinity of calmodulin for the active form is higher than for the inactive form, it stabilises PP2B.
G protein-coupled receptors (GPCRs; 7TM receptors; seven transmembrane domain receptors; heptahelical receptors; G protein-linked receptors [GPLR]) are the largest family of transmembrane receptors in humans, accounting for more than 1% of the protein-coding capacity of the human genome. All known GPCRs share a common architecture of seven membrane-spanning helices connected by intra- and extracellular loops. The extracellular loops contain two highly-conserved cysteine residues that form disulphide bonds to stabilize the structure of the receptor. They recognize diverse messengers such as light, odorants, small molecules, hormones and neurotransmitters. Most GPCRs act as guanine nucleotide exchange factors; activated by ligand binding, they promote GDP-GTP exchange on associated heterotrimeric guanine nucleotide-binding (G) proteins. There are two models for GPCR-G Protein interactions: 1) ligand-GPCR binding first, then binding to G Proteins; 2) "Pre-coupling" of GPCRs and G Proteins before ligand binding (review Oldham WM and Hamm HE, 2008). These in turn activate effector enzymes or ion channels. GPCRs are involved in a range of physiological roles which include the visual sense, smell, behavioural regulation, functions of the autonomic nervous system and regulation of the immune system and inflammation. GPCRs are divided into 6 classes based on sequence homology and functional similarity; the main mammalian families are classes A/1-C/3; Class A/1 (Rhodopsin-like) Class B/2 (Secretin receptor family) Class C/3 (Metabotropic glutamate/pheromones) Class D/4 (fungal mating pheromone receptors) Class E/5 (cAMP receptors) Class F/6 (Frizzled/Smoothened) Here, those Class A/1 (Rhodopsin-like) receptors that bind peptide ligands have been annotated. The binding events mediated by other classes of receptors, as well as the downstream events triggered by receptor-ligand interactions will be annotated in future releases of Reactome.
The MRN complex: coordinating and mediating the response to broken chromosomes.
All WNT ligands are predicted to be highly glycosylated. By similarity with WNT ligands in mouse, human WNTs are believed to undergo N-linked glycosylation at multiple asparagine residues and this glycosylation is critical for their secretion (Smolich et al, 1993; Willert et al, 2003, Komekado et al, 2006; Kurayoshi et al, 2007). The mechanism of N-linked glycosylation is not shown here. For a more detailed description, please refer to pathway "Asparagine N-linked glycosylation".
Gastrin, through the action of diacylglycerol produced from downstream G alpha (q) events, transactivates EGFR via a PKC-mediated pathway by activation of MMP3 (Matrix Metalloproteinase 3) which allows formation of mature HBEGF (heparin-binding epidermal growth factor) by cleaving pro-HBEGF. Mature HBEGF is then free to bind the EGFR, resulting in EGFR activation (Dufresne et al. 2006, Liebmann 2011).
Gastrin is a hormone whose main function is to stimulate secretion of hydrochloric acid by the gastric mucosa, which results in gastrin formation inhibition. This hormone also acts as a mitogenic factor for gastrointestinal epithelial cells. Gastrin has two biologically active peptide forms, G34 and G17.Gastrin gene expression is upregulated in both a number of pre-malignant conditions and in established cancer through a variety of mechanisms. Depending on the tissue where it is expressed and the level of expression, differential processing of the polypeptide product leads to the production of different biologically active peptides. In turn, acting through the classical gastrin cholecystokinin B receptor CCK-BR, its isoforms and alternative receptors, these peptides trigger signalling pathways which influence the expression of downstream genes that affect cell survival, angiogenesis and invasion (Wank 1995, de Weerth et al. 1999, Grabowska & Watson 2007)
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19 WNT proteins have been identified in human cells. The WNTs are members of a conserved metazoan family of secreted morphogens that activate several signaling pathways in the responding cell: the canonical (beta-catenin) WNT signaling cascade and several non-canonical pathways, including the planar cell polarity (PCP), the regulation of intracellular calcium signaling and activation of JNK kinases. WNT proteins exist in a gradient outside the secreting cell and are able to act over both short and long ranges to promote proliferation, changes in cell migration and polarity and tissue homeostasis, among others (reviewed in Saito-Diaz et al, 2012; Willert and Nusse, 2012). The WNTs are ~40kDa proteins with 23 conserved cysteine residues in the N-terminal that may form intramolecular disulphide bonds. They also contain an N-terminal signal sequence and a number of N-linked glycosylation sites (Janda et al, 2012). In addition to being glycosylated, WNTs are also lipid-modified in the endoplasmic reticulum by a WNT-specific O-acyl-transferase, Porcupine (PORCN), contributing to their characteristic hydrophobicity. PORCN-dependent palmitoylation is required for the secretion of WNT as well as its signaling activity, as either depletion of PORCN or mutation of the conserved serine acylation site results in the intracellular accumulation of WNT ligand (Takada et al, 2006; Barrott et al, 2011; Biechele et al, 2011; reviewed in Willert and Nusse, 2012). Secretion of WNT requires a number of other dedicated factors including the sorting receptor Wntless (WLS) (also knownas Evi, Sprinter, and GPR177), which binds WNT and escorts it to the cell surface (Bänziger et al, 2006; Bartscherer et al, 2006; Goodman et al, 2006). A WNT-specific retromer containing SNX3 is subsequently required for the recycling of WLS back to the Golgi (reviewed in Herr et al, 2012; Johannes and Wunder, 2011). Once at the cell surface, WNT makes extensive contacts with components of the extracellular matrix such as heparan sulphate proteoglycans (HSPGs) and may be bound by any of a number of regulatory proteins, including WIFs and SFRPs. The diffusion of the WNT ligand may be aided by its packing either into WNT multimers, exosomes or onto lipoprotein particles to shield the hydrophobic lipid adducts from the aqueous extracellular environment (Gross et al, 2012; Luga et al, 2012, Korkut et al, 2009; reviewed in Willert and Nusse, 2012).
This black box event represents the non-WNT-specific ER-to-Golgi trafficking step of protein secretion (reviewed in Dancourt and Barlowe, 2010; Lippincott Schwatz et al, 2000; for more details, please refer to the pathway "ER to Golgi transport"). Two recent screens in Drosophila have identified members of the p24 family as WNT-specific regulators of ER-to-Golgi transport, although the details have not been elucidated (Port et al, 2011; Buechling et al, 2011; reviewed in Strating and Martens, 2009). Depletion of the Drosophila p24 protein Opossum causes accumulation of WNT ligand in the ER, suggesting a role for Opm in ER-to-Golgi transport of WNTs. WNT-dependent reporter activity was reduced in HEK293 cells that were depleted for the human p24 homologue TMED5, supporting a conserved role for these proteins in WNT signaling (Buechling et al, 2011; reviewed in Palmer et al, 2012).
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PI3K gamma (PI3KG) is a heterodimer consisting of a p110 catalytic subunit associated with a regulatory p101 or p84 subunit. PI3KG is most highly expressed in neutrophils, where the p101 form predominates (approximately 95%). G beta:gamma recruits PI3KG to the plasma membrane, both activating PI3KG and providing access to its substrate PIP2, which is converted to PIP3.
The classical role of the G-protein beta/gamma dimer was believed to be the inactivation of the alpha subunit, Gbeta/gamma was viewed as a negative regulator of Galpha signalling. It is now known that Gbeta/gamma subunits can directly modulate many effectors, including some also regulated by G alpha.
G protein-coupled receptors (GPCRs) are classically defined as the receptor, G-protein and downstream effectors, the alpha subunit of the G-protein being the primary signaling molecule. However, it has become clear that this greatly oversimplifies the complexities of GPCR signaling (see Gurevich & Gurevich, 2008). The beta:gamma G-protein dimer is also involved in downstream signaling (Smrcka, 2008), and some receptors form part of metastable complexes of receptor and accessory proteins such as the arrestins. GPCRs are involved in many diverse signaling events (Kristiansen 2004), using a variety of pathways that include modulation of adenylyl cyclase, phospholipase C, the mitogen activated protein kinases (MAPKs), extracellular signal regulated kinase (ERK) c-Jun-NH2-terminal kinase (JNK) and p38 MAPK.
Slow intrisinc GTPase activity results in an inactivation of the alpha-i subunit by hydrolyzing GTP to GDP.
Enzymatic hydration of leukotriene A4. Purification and characterization of a novel epoxide hydrolase from human erythrocytes
Receptor activated heterotrimeric G proteins consist of the Galpha and the tightly associated Gbeta-gamma subunits. When a ligand binds to a G protein-coupled receptor, it stabilises a conformation with an high affinity for the G-protein bound to GDP. GDP is then exchanged for GTP on the Galpha subunit. This exchange triggers the dissociation of the Galpha subunit from the Gbeta-gamma dimer and the receptor. Galpha-GTP and Gbeta-gamma, can then modulate different signalling cascades and effector proteins, while the receptor is able to activate another G protein, resulting in an amplification cascade. The Galpha subunit will eventually hydrolyze the attached GTP to GDP by its inherent enzymatic activity, allowing it to reassociate with Gbeta-gamma and start a new cycle.
The active form of G protein alpha subunit q (Gq-alpha) was found to activate phospholipase C beta-1 (PLC-beta1), in investigations using bovine membranes. Subsequently, all 4 human isoforms have been shown to be activated by Gq, though activation of PLCbeta-4 is limited. In recombinant assays, several activated rat G alpha q family members were found to stimulate human PLC-beta isoforms with the same rank order of decreasing potency. PLC-beta1 stimulation was slightly more than for PLC-beta3; PLC-beta3 stimulation was 10-fold greater than for beta-2. PLC-beta2 is expressed specifically in hematopoietic cells. PLC-beta acts directly on Gq to accelerate hydrolysis of bound GTP, thus PLC-betas are GTPase activating proteins (GAPs). The crystal structure of the C-terminal region from Turkey PLC-beta, revealed a novel fold composed almost entirely of three long helices forming a coiled-coil that dimerizes along its long axis in an antiparallel orientation. The extent of the dimer interface and gel exclusion chromatography data suggest that PLC-betas are functionally dimeric.
The phospholipase C (PLC) family of enzymes is both diverse and complex. The isoforms beta, gamma and delta (each have subtypes) make up the members of this family. One type, PLC-beta1, hydrolyzes phosphatidylinositol bisphosphate (PIP2) into two second messengers, inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). IP3 mobilizes intracellular calcium stores while DAG activates protein kinase C isoforms which are involved in regulatory functions.
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Calcium, as the ion Ca2+, is essential in many biological processes. The majority of Ca2+ in many organisms is bound to phosphates which form skeletal structures and also buffer Ca2+ levels in extracellular fluids (typically 1 millimolar). Intracellular free Ca2+, by contrast, is 10,000 times lower than the outside of the cell (typically 10 micromolar). This concentration gradient is used to import Ca2+ into cells where it acts as a second messenger.
PLC-beta1 is a GTPase-activating protein (GAP) for Gq-alpha, exchanging GTP for GDP and releasing the alpha subunit to cycle back to the membrane and reassociate with the beta-gamma subunits. Between itself and the receptor, they regulate the amplitude of the PLC signal and the rates of signal initiation and termination.
The phospholipase C (PLC) family of enzymes is both diverse and complex. The isoforms beta, gamma and delta (each have subtypes) make up the members of this family. PLC hydrolyzes phosphatidylinositol bisphosphate (PIP2) into two second messengers, inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). IP3 mobilizes intracellular calcium stores while DAG activates protein kinase C isoforms which are involved in regulatory functions.
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The SUMO3 precursor has 11 extra residues at the C-terminus which can be removed endoproteolytically by SENP1, SENP2, or SENP5 (Zheng and Au, 2005, Gong and Yeh 2006, Mikolajczyk et al. 2007). The order of processing activity is: SENP1 greater than SENP2 greater than SENP5 (Mikolajczyk et al. 2007). Overall, processing of SUMO3 is the lowest of any SUMO (Mikolajczyk et al. 2007). SENP1 and SENP2 shuttle between the nucleus and cytosol and are predominantly nuclear (Bailey and O'Hare 2004, Kim et al. 2005, Zhang et al. 2002, Hang and Dasso 2002, Itahana et al. 2006). SENP5 is located in the nucleolus (Di Bacco et al. 2006, Gong and Yeh 2006).
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).
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).
The SUMO2 precursor has 2 extra residues at the C-terminus which can be removed endoproteolytically by SENP1, SENP2, or SENP5 (Zheng and Au, 2005, Gong and Yeh 2006, Mikolajczyk et al. 2007). The order of processing activity is: SENP1 greater than SENP2 greater than SENP5 (Mikolajczyk et al. 2007). SENP2 and SENP5 have highest activity on SUMO2, however the processing activity of SENP1 is higher overall (Mikolajczyk et al. 2007). SENP1 and SENP2 shuttle between the nucleus and cytosol and are predominantly nuclear (Bailey and O'Hare 2004, Kim et al. 2005, Zhang et al. 2002, Hang and Dasso 2002, Itahana et al. 2006). SENP5 is located in the nucleolus (Di Bacco et al. 2006, Gong and Yeh 2006).
Signal transduction is a process in which extracellular signals elicit changes in cell state and activity. Transmembrane receptors sense changes in the cellular environment by binding ligands, such as hormones and growth factors, or reacting to other types of stimuli, such as light. Stimulation of transmembrane receptors leads to their conformational change which propagates the signal to the intracellular environment by activating downstream signaling cascades. Depending on the cellular context, this may impact cellular proliferation, differentiation, and survival. On the organism level, signal transduction regulates overall growth and behavior. Receptor tyrosine kinases (RTKs) transmit extracellular signals by phosphorylating their protein partners on conserved tyrosine residues. Some of the best studied RTKs are EGFR (reviewed in Avraham and Yarden, 2011), FGFR (reviewed in Eswarakumar et al, 2005), insulin receptor (reviewed in Saltiel and Kahn, 2001), NGF (reviewed in Reichardt, 2006), PDGF (reviewed in Andrae et al, 2008) and VEGF (reviewed in Xie et al, 2004). RTKs frequently activate downstream signaling through RAF/MAP kinases (reviewed in McKay and Morrison, 2007 and Wellbrock et al 2004), AKT (reviewed in Manning and Cantley, 2007) and PLC- gamma (reviewed in Patterson et al), which ultimately results in changes in gene expression and cellular metabolism. Receptor serine/threonine kinases of the TGF-beta family, such as TGF-beta receptors (reviewed in Kang et al. 2009) and BMP receptors (reviewed in Miyazono et al. 2009), transmit extracellular signals by phosphorylating regulatory SMAD proteins on conserved serine and threonine residues. This leads to formation of complexes of regulatory SMADs and SMAD4, which translocate to the nucleus where they act as transcription factors. WNT receptors transmit their signal through beta-catenin. In the absence of ligand, beta-catenin is constitutively degraded in a ubiquitin-dependent manner. WNT receptor stimulation releases beta-catenin from the destruction complex, allowing it to translocate to the nucleus where it acts as a transcriptional regulator (reviewed in MacDonald et al, 2009 and Angers and Moon, 2009). WNT receptors were originally classified as G-protein coupled receptors (GPCRs). Although they are structurally related, GPCRs primarily transmit their signals through G-proteins, which are trimers of alpha, beta and gamma subunits. When a GPCR is activated, it acts as a guanine nucleotide exchange factor, catalyzing GDP to GTP exchange on the G-alpha subunit of the G protein and its dissociation from the gamma-beta heterodimer. The G-alpha subunit regulates the activity of adenylate cyclase, while the gamma-beta heterodimer can activate AKT and PLC signaling (reviewed in Rosenbaum et al. 2009, Oldham and Hamm 2008, Ritter and Hall 2009). NOTCH receptors are activated by transmembrane ligands expressed on neighboring cells, which results in cleavage of NOTCH receptor and release of its intracellular domain. NOTCH intracellular domain translocates to the nucleus where it acts as a transcription factor (reviewed in Kopan and Ilagan, 2009). Integrins are activated by extracellular matrix components, such as fibronectin and collagen, leading to conformational change and clustering of integrins on the cell surface. This results in activation of integrin-linked kinase and other cytosolic kinases and, in co-operation with RTK signaling, regulates survival, proliferation and cell shape and adhesion (reviewed in Hehlgans et al, 2007) . Besides inducing changes in gene expression and cellular metabolism, extracellular signals that trigger the activation of Rho GTP-ases can trigger changes in the organization of cytoskeleton, thereby regulating cell polarity and cell-cell junctions (reviewed in Citi et al, 2011).
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).
The visual pigment (rhodopsin in rods) consists of an 11-cis-retinal (11cRAL) chromophore covalently attached to a GPCR opsin family member via a Schiff base linkage. Upon photon absorption, 11cRAL isomerizes to all trans retinal (atRAL), changing the conformation of opsin to a form that can activate the regulatory G protein transducin (Gt). The alpha subunit of Gt activates phosphodiesterase which hydrolyses cGMP to 5'-GMP. A high level of cGMP keeps cGMP-gated cation channels open, so lower cGMP levels close these channels and hyperpolarize the cell. The hyperpolarization spreads passively to the synapse located at the opposite end of the rod, where it subsequently closes voltage-gated calcium channels. Vesicular release of the neurotransmitter glutamate subsides as the intracellular calcium levels drop. This diminution of neurotransmitter release relays the light signal to postsynaptic neurons. The events below describe activation, inactivation, recovery and regulation of the phototransduction cascade in rods (Burns & Pugh 2010, Korenbrot 2012, Smith 2010).
Visual phototransduction is the process by which photon absorption by visual pigment molecules in photoreceptor cells is converted to an electrical cellular response. The events in this process are photochemical, biochemical and electrophysiological and are highly conserved across many species. This process occurs in two types of photoreceptors in the retina, rods and cones. Each type consists of two parts, the outer segment which detects a photon signal and the inner segment which contains the necessary machinery for cell metabolism. Each type of cell functions differently. Rods are very light sensitive but their flash response is slow so they work best in twilight conditions but are not good at detecting objects moving quickly. Cones are less light-sensitive and have a fast flash response so they work best in daylight conditions and are better at detecting fast moving objects than rods. The visual pigment consists of a chromophore (11-cis-retinal, 11cRAL, A1) covalently attached to a GPCR opsin family member. The linkage is via a Schiff base forming retinylidene protein. Upon photon absorption, 11cRAL isomerises to all-trans retinal (atRAL), changing the conformation of opsin to an activated form which can activate the regulatory G protein transducin (Gt). The alpha subunit of Gt activates phosphodiesterase which hydrolyses cGMP to 5'-GMP. As high level of cGMP keep cGMP-gated sodium channels open, the lowering of cGMP levels closes these channels which causes hyperpolarization of the cell and subsequently, closure of voltage-gated calcium channels. As calcium levels drop, the level of the neurotransmitter glutamate also drops causing depolarization of the cell. This effectively relays the light signal to postsynaptic neurons as electrical signal (Burns & Pugh 2010, Korenbrot 2012, Pugh & Lamb 1993). 11cRAL cannot be synthesised in vertebrates. Vitamin A from many dietary sources is the precursor for 11cRAL. It is taken from food in the form of esters such as retinyl acetate or palmitate or one of four caretenoids (alpha-carotene, beta-carotene, gamma-carotene and beta-cryptoxanthin). Retinoids are transported from the gut to be stored in liver, until required by target organs such as the eye (Harrison & Hussain 2001, Harrison 2005). In the eye, in the form 11cRAL, it is used in the retinoid (visual) cycle to initiate phototransduction and for visual pigment regeneration to ready the photoreceptor for the next phototransduction event (von Lintig 2012, Blomhoff & Blomhoff 2006, von Lintig et al. 2010, D'Ambrosio et al. 2011, Wang & Kefalov 2011, Kefalov 2012, Wolf 2004).
The activity of guanylyl cyclases is regulated by Ca2+-binding, guanylyl cyclase-activating proteins (GCAPs). This regulation is the most important negative feedback mechanism triggered by Ca2+ in light. There are three GCAPs in humans; GUCA1A (Subbaraya et al. 1994), GUCA1B (Surguchov et al. 1997) and GUCA1C (Haeseleer et al. 1999). In darkness, when intracellular Ca2+ is relatively high, GCAPs suppress guanylate cyclase activity. But the light-induced fall in Ca2+ prompts Ca2+ to dissociate from GCAPs and be replaced by Mg2+, allowing the GCAPs to stimulate guanylate cyclase activity by an order of magnitude. Different GCAPs have different affinities for Ca2+. Defects in GCAP1 give rise to cone dystrophy and Lebers congenital amaurosis (https://sph.uth.edu/retnet/).
To terminate the single photon response and restore the system to its basal state, the three activated intermediates in phototransduction, rhodopsin (MII), transducin alpha subunit with GTP bound (GNAT1-GTP) and phosphodiesterase 6 (PDE6) all need to be efficiently deactivated. In addition, the cGMP concentrations must be restored to support reopening of the CNG channels. This section describes the inactivation and recovery events of the activated intermediates involved in phototransduction (Burns & Pugh 2010, Korenbrot 2012).
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Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
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Regulation of growth cone actin dynamics by ADF/cofilin
Bovine studies (Beharry et al. 2004) have indicated NRPE to be the preferred substrate for ABCA4 (ABCR, rim protein, RmP) (Azarian et al. 1998), which acts an inward-directed retinoid flippase and facilitates the transfer of NRPE to the cytoplasmic side of the disc membrane. This transfer is essential to avoid build up of potentially toxic retinoid intermediates which are implicated in many retinal degenerative diseases (see review Tsybovsky et al. 2010). Defective ABCA4 cannot perform this function leading to impaired vision and blindness disorders such as Stargardt disease (MIM:248200).
The reversible, NADP(H)-dependent reduction of all-trans-retinal (atRAL) to all-trans-retinol (atROL) occurs in both rod and cone photoreceptor cells where multiple retinol dehydrogenases (RHDs) are located. RHDs belong to the short-chain dehydrogenase/reductase (SDR) superfamily. RDH8 (located in photoreceptor outer segments) is partially responsible, together with other RDHs, for mediating this reaction. The activity for human RDH8 is inferred from a bovine experiment (Rattner et al. 2000).
The retinoid cycle (also referred to as the visual cycle) is the process by which the visual chromophore 11-cis-retinal (11cRAL) is released from light-activated opsins in the form all-trans-retinal and isomerized back to its 11-cis isomer ready for another photoisomerization reaction. This process involves oxidation, reduction and isomerization reactions and take place in the retinal pigment epithelium (RPE) and photoreceptor segments of the eye (von Lintig 2012, Blomhoff & Blomhoff 2006, von Lintig et al. 2010, D'Ambrosio et al. 2011). This section describes the retinoid cycle in rods during dark/twilight conditions.
All eukaryotic proteins synthesized in the cytosol are initiated by methionine (Met). For the maturation of many proteins, the removal of N-terminal Met is essential and is mediated by methionine-aminopeptidases (METAPs). In human, there are two forms, METAP1 and 2 (Arfin et al. 1995). These enzymes utilise 2 cobalt ions (Co2+) as cofactors (Addlagatta et al. 2005, Hu et al. 2006, Marino et al. 2007).
The extracellular matrix (ECM) is a network of macro-molecules that underlies all epithelia and endothelia and that surrounds all connective tissue cells. This matrix provides the mechanical strength and also influences the behavior and differentiation state of cells in contact with it. The ECM are diverse in composition, but they generally comprise a mixture of fibrillar proteins, polysaccharides synthesized, secreted and organized by neighboring cells. Collagens, fibronectin, and laminins are the principal components involved in cell matrix interactions; other components, such as vitronectin, thrombospondin, and osteopontin, although less abundant, are also important adhesive molecules. Integrins are the receptors that mediate cell adhesion to ECM. Integrins consists of one alpha and one beta subunit forming a noncovalently bound heterodimer. 18 alpha and 8 beta subunits have been identified in humans that combine to form 24 different receptors. The integrin dimers can be broadly divided into three families consisting of the beta1, beta2/beta7, and beta3/alphaV integrins. beta1 associates with 12 alpha-subunits and can be further divided into RGD-, collagen-, or laminin binding and the related alpha4/alpha9 integrins that recognise both matrix and vascular ligands. beta2/beta7 integrins are restricted to leukocytes and mediate cell-cell rather than cell-matrix interactions, although some recognize fibrinogen. The beta3/alphaV family members are all RGD receptors and comprise aIIbb3, an important receptor on platelets, and the remaining b-subunits, which all associate with alphaV. It is the collagen receptors and leukocyte-specific integrins that contain alpha A-domains.
The phosphorylated type 1 insulin-like growth factor receptor phosphorylates IR1, IRS2, IRS4 and possibly other IRS/DOK family members (reviewed in Pavelic et al. 2007, Chitnis et al. 2008, Maki et al. 2010, Parrella et al. 2010, Siddle et al. 2012). The phosphorylated IRS proteins serve as scaffolds that bind the effector molecules PI3K and GRB2:SOS. PI3K then activates PKB (AKT) signaling while GRB2:SOS activates RAS-RAF-MAPK signaling.
After autophosphorylation the type 1 insulin-like growth factor receptor (IGF1R) binds and phosphorylates scaffold proteins, IRS1/2/4 and SHC1, which in turn bind effectors possessing enzymatic activity (recently reviewed in Pavelic et al. 2007, Chitnis et al. 2008, Maki et al. 2010, Parrella et al. 2010, and Siddle et al. 2012). IRS1/2/4 can bind both PI3K (via the p85 subunit of PI3K) and the GRB2:SOS complex. PI3K activates PKB (AKT, AKT1) signaling. GRB:SOS stimulates RAS to exchange GDP for GTP leading to activation of RAF and MAPK.
Binding of IGF1 (IGF-I) or IGF2 (IGF-II) to the extracellular alpha peptides of the type 1 insulin-like growth factor receptor (IGF1R) triggers the activation of two major signaling pathways: the SOS-RAS-RAF-MAPK (ERK) pathway and the PI3K-PKB (AKT) pathway (recently reviewed in Pavelic et al. 2007, Chitnis et al. 2008, Maki et al. 2010, Parella et al. 2010, Annunziata et al. 2011, Siddle et al. 2012, Holzenberger 2012).
WNT signaling pathways control a wide range of developmental and adult process in metozoans including cell proliferation, cell fate decisions, cell polarity and stem cell maintenance (reviewed in Saito-Diaz et al, 2013; MacDonald et al, 2009). The pathway is named for the WNT ligands, a large family of secreted cysteine-rich glycoproteins. At least 19 WNT members have been identified in humans and mice with distinct expression patterns during development (reviewed in Willert and Nusse, 2012). These ligands can activate at least three different downstream signaling cascades depending on which receptors they engage. In the so-called 'canonical' WNT signaling pathway, WNT ligands bind one of the 10 human Frizzled (FZD) receptors in conjunction with the LRP5/6 co-receptors to activate a transcriptional cascade that controls processes such as cell fate, proliferation and self-renenwal of stem cells. Engagement of the FZD-LRP receptor by WNT ligand results in the stabilization and translocation of cytosolic beta-catenin to the nucleus where it is a co-activator for LEF (lymphoid enhancer-binding factor)- and TCF (T cell factor) -dependent transcription. In the absence of WNT ligand, cytosolic beta-catenin is phosphorylated by a degradation complex consisting of glycogen synthase kinase 3 (GSK3), casein kinase 1 (CK1), Axin and Adenomatous polyposis coli (APC), and subsequently ubiquitinated and degraded by the 26S proteasome (reviewed in Saito-Diaz et al, 2013; Kimmelman and Xu, 2006). In addition to the beta-catenin-dependent transcriptional response, WNT signaling can also activate distinct non-transcriptional pathways that regulate cell migration and polarity. These beta-catenin-independent 'non-canonical' pathways signal through Frizzled receptors independently of LRP5/6, or occur through the tyrosine kinase receptors ROR and RYK (reviewed in Veeman et al, 2003; James et al, 2009). Non-canonical WNT pathways are best studied in Drosophila where the planar cell polarity (PCP) pathway controls the orientation of wing hairs and eye facets, but are also involved in processes such as convergent extension, neural tube closure, inner ear development and hair orientation in vertebrates and mammals(reviewed in Seifert and Mlodzik, 2007; Simons and Mlodzik, 2008). In the PCP pathway, binding of WNT ligand to the FZD receptor leads to activation of small Rho GTPases and JNK, which regulate the cytoskeleton and coordinate cell migration and polarity (reviewed in Lai et al, 2009; Schlessinger et al, 2009). In some cases, a FZD-WNT interaction increases intracellular calcium concentration and activates CaMK II and PKC; this WNT calcium pathway promotes cell migration and inhibits the canonical beta-catenin dependent transcriptional pathway (reviewed in Kuhl et al, 2000; Kohn and Moon, 2005; Rao et al 2010). Binding of WNT to ROR or RYK receptors also regulates cell migration, apparently through activation of JNK or SRC kinases, respectively, however the details of these pathways remain to be worked out (reviewed in Minami et al, 2010). Although the WNT signaling pathways were originally viewed as discrete, linear pathways controlled by defined subsets of 'canonical' or 'non-canonical' ligands and receptors, the emerging evidence is challenging this notion. Instead, the specificity and the downstream response appear to depend on the particular cellular context and vary with species, tissue and stage of development (reviewed in van Amerongen and Nusse, 2009; Rao et al, 2010).
The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity
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After removal of the N-terminal methionine (Met) residue, the enzymes glycylpeptide N-tetradecanoyltransferase 1 and 2 (NMT1 and 2) mediate the transfer of the myristoyl (MYS) group from myristoyl-CoA to the now N-terminal glycine (Gly) residue of transducin's alpha subunit (GNAT1) (Glover et al. 1997, Giang & Cravatt 1998). Myristoylation is thought to aid enzyme function and localization. Evidence from chicken experiments suggest non-myristoylated proteins do not bind to membranes (Kamps et al. 1986).
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Sensing and repairing DNA double-strand breaks
Raf and akt mediate distinct aspects of sensory axon growth
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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
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Lysophospholipid acyltransferases and arachidonate recycling in human neutrophils
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Cancer-associated IDH1 mutations produce 2-hydroxyglutarate
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Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA
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Molecular mechanisms and regulation of insulin exocytosis as a paradigm of endocrine secretion
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Fine-tuning of GPCR activity by receptor-interacting proteins
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Species-specific detection of the antiviral small-molecule compound CMA by STING
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E2F-dependent accumulation of hEmi1 regulates S phase entry by inhibiting APC(Cdh1)
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Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 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=3644429
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_95693.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649430
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=382571
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_16095.2
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=382577
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649711
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_156805.3
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_142211.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645070
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649744
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645068
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649742
Reactome stable identifier. Use this 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
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_16090.2
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=3649741
Reactome stable identifier. Use this 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=3649739
Database identifier. Use 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=3649740
Database identifier. Use 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=3649738
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651754
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_29205.10
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_122526.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1524060
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645094
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_130567.5
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_123890.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645096
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1524071
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=199622
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5336.2
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_11255.2
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=196934
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649798
Antigen Activates B Cell Receptor Leading to Generation of Second Messengers
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11831.2
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=3649800
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652072
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_89239.9
RNA primer:G-strand extended telomere end:DNA polymerase alpha:primase complex (name copied from entity in Homo sapiens)
RNA primer-DNA primer:G-strand extended telomere (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)
Fcgamma receptors: old friends and new family members
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652050
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_78733.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644912
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644910
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644909
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_103618.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644905
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644903
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_101380.9
Transcriptional activation of Acetyl-CoA carboxylase by ChREBP:MLX
Transcriptional activation of GP-acyl transferase gene by ChREBP:MLX
SCF-beta-TrCP1 complex (name copied from entity in Homo sapiens)
Transcriptional activation of Citrate lyase monomer gene by ChREBP:MLX
cell cycle proteins:phospho-APC/C:Cdh1 complex (name copied from entity in Homo sapiens)
SCF-associated multiubiquitinated Emi1complexes (name copied from entity in Homo sapiens)
multiubiquitinated cell cycle protein:APC/C:Cdh1 complex (name copied from entity in Homo sapiens)
Nuclear organization of DNA replication initiation proteins in mammalian cells.
phospho-APC/C:Cdh1 complex (name copied from entity in Homo sapiens)
DNA polymerase epsilon:G-strand extended telomere end (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)
Homologous DNA pairing by human recombination factors Rad51 and Rad54
phospho-Cdh1:phospho-APC/C (name copied from entity in Homo sapiens)
SCF-beta-TrCP:phospho-Emi1 complexes (name copied from entity in Homo sapiens)
phosphorylated anaphase promoting complex (APC/C) (name copied from entity in Homo sapiens)
Cyclin A:phospho-Cdk2(Thr 160):phospho-Cdh1:phospho-APC/C complex (name copied from entity in Homo sapiens)
A highly conserved repetitive DNA sequence, (TTAGGG)n, present at the telomeres of human chromosomes
Crystal structure of human uroporphyrinogen decarboxylase
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644888
Phosphorylation and activation of human cdc25-C by cdc2--cyclin B and its involvement in the self-amplification of MPF at mitosis
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644887
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_104603.9
Morquio's syndrome: deficiency of a chondroitin sulfate N-acetylhexosamine sulfate sulfatase
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644890
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29480
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4009.4
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=3652049
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_107585.9
Cyclin B1:phospho-Cdc2(Thr 161) (name copied from entity in Homo sapiens)
Cdh1:phospho-APC/C complex (name copied from entity in Homo sapiens)
Cyclin A:phospho-Cdk(Thr 160):Cdh1:phosho-APC/C complex (name copied from entity in Homo sapiens)
Cyclin B2:phospho-Cdc2(Thr 161) (name copied from entity in Homo sapiens)
Cyclin B2:phospho-Cdc2(Thr 14, Thr 161) (name copied from entity in Homo sapiens)
Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649665
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=196786
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649671
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11705.2
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_11378.2
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=196834
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644874
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644877
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644875
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649698
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649815
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649793
Oncogenic signaling from the hematopoietic growth factor receptors c-Kit and Flt3
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649675
RFC Heteropentamer:RNA primer-DNA primer:origin duplex (name copied from entity in Homo sapiens)
Cloning of a human cDNA for CTP-phosphoethanolamine cytidylyltransferase by complementation in vivo of a yeast mutant
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649622
RFC Heteropentamer (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=3649730
RFC Heteropentamer:RNA primer-DNA primer:origin duplex:PCNA homotrimer (name copied from entity in Homo sapiens)
PCNA homotrimer (name copied from entity in Homo sapiens)
multi-ubiquitinated phospho-(T286) Cyclin D1 (name copied from entity in Homo sapiens)
RNA primer-DNA primer:origin duplex:PCNA (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=3649630
Cohesin:PDS5:WAPAL:Chromosomal Arm (name copied from entity in Homo sapiens)
Mcm4,6,7 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=3649642
GINS 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=3649634
Unwinding complex at replication fork (name copied from entity in Homo sapiens)
Cyclin A:Cdk2:phosphorylated substrate complex (name copied from entity in Homo sapiens)
Cyclin A:phospho-Cdk2(Thr160) 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=3649616
Cyclin A:Cdk2:substrate 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=3649610
Cyclin A:phospho-Cdk2(Tyr 15) (name copied from entity in Homo sapiens)
ubiquitinated Cdc6 (name copied from entity in Homo sapiens)
ubiquitinated Orc1 (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=3649628
pre-replicative complex (Orc1-minus) (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_133307.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649724
Cyclin A:Cdk2 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=3649722
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652199
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649723
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_144663.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649710
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649719
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_122642.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649721
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649720
phospho-Cyclin B1:phospho-Cdc2(Thr 161) (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=3649743
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649799
phospho-cyclin B1(CRS):phosph-Cdc2(Thr 161) (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=3649765
Cyclin B1:phospho-Cdc2(Thr 161, Thr 14, Tyr 15) (name copied from entity in Homo sapiens)
nuclear Cyclin B1:phospho-Cdc2 ( Thr 14) complexes (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=3649749
Cyclin A:phospho-Cdc2(Thr 161, Thr 14, Tyr 15) (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=3649637
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649748
Cyclin A:phospho-Cdc2(Thr 161) (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_122034.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1524146
Cyclin B1:phospho-Cdc2 ( Thr 14) (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=3649859
Cyclin A:phospho-Cdc2(Thr 14, Thr 161) (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=426639
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649842
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649824
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_123561.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649639
GEF what? Dock180 and related proteins help Rac to polarize cells in new ways
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649840
Cyclin A:phospho-Cdc2(Thr 14) (name copied from entity in Homo sapiens)
Immunohistochemical localisation of thrombospondin in human megakaryocytes and platelets
phospho-Cdc2(Thr 14):Cyclin A (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=3649685
Cyclin A:Cdc2 (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=3649822
Ac-Cohesin:PDS5:WAPAL:Centromere (name copied from entity in Homo sapiens)
Cohesin:PDS5:WAPAL:Centromere (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=3649717
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649843
Ac-Cohesin:PDS5:WAPAL:Chromosomal Arm (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_137856.5
Ac-Cohesin:PDS5:WAPAL (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=3652306
Cohesin:PDS5:WAPAL (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=3649809
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_93154.9
Cohesin 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=3649750
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_147492.5
Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_130791.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649751
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649826
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649825
Peroxisomal multifunctional enzyme type 2
hydroxysteroid (17-beta) dehydrogenase 4
Acyl- CoA:dihydroxyacetonephosphateacyltransferase
Dihydroxyacetone phosphate acyltransferase
Alkyldihydroxyacetonephosphate synthase, peroxisomal precursor
Alkyldihydroxyacetonephosphate synthase precursor
Isocitrate dehydrogenase (NADP) cytoplasmic
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3646477
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3646481
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3646485
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Stalled Pol II in TC-NER (name copied from entity in Homo sapiens)
Active Pol II complex with repaired DNA template:mRNA hybrid (name copied from entity in Homo sapiens)
Transcription-coupled (TC) repair complex (name copied from entity in Homo sapiens)
hBUBR1:hBUB3:MAD2*:CDC20 complex (name copied from entity in Homo sapiens)
Nek2A:MCC:APC/C complex (name copied from entity in Homo sapiens)
The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
MCC:APC/C complex (name copied from entity in Homo sapiens)
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Ubiquitinated Phospho-Cdc25A (name copied from entity in Homo sapiens)
N-glycan trimming and elongation in the cis-Golgi
Multiubiquitinated Nek2A (name copied from entity in Homo sapiens)
ubiquitinated phospho-COP1(ser-387) (name copied from entity in Homo sapiens)
Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport
3-hydroxy-3-methylglutaryl-coenzyme A reductase-1
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Isolation of two cDNAs encoding functional human cytoplasmic cysteinyl-tRNA synthetase
RAD51:resected ends of DNA double-strand break (name copied from entity in Homo sapiens)
Ku70:Ku80 heterodimer (name copied from entity in Homo sapiens)
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Ku:DNA double-strand break ends (name copied from entity in Homo sapiens)
Mdm2 promotes the rapid degradation of p53.
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DNA-PK:DNA complex (name copied from entity in Homo sapiens)
DNA-PK synaptic complex (name copied from entity in Homo sapiens)
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XPC:HR23B complex (name copied from entity in Homo sapiens)
XPC:HR23B:damaged DNA complex (name copied from entity in Homo sapiens)
ERCC1:XPF complex (name copied from entity in Homo sapiens)
RNA Polymerase II holoenzyme complex (hyperphosphorylated) (name copied from entity in Homo sapiens)
Active Pol II transcription complex with damaged DNA hybrid (name copied from entity in Homo sapiens)
There are more than 800 G-protein coupled receptor (GPCRs) in the human genome, making it the largest receptor superfamily. GPCRs are also the largest class of drug targets, involved in virtually all physiological processes (Frederiksson 2003). GPCRs are receptors for a diverse range of ligands from large proteins to photons (Kristiansen et al. 2004) and have an equal diversity of ligand-binding mechanisms (Gether et al. 2002). Classical GPCR signaling involves signal transduction via heterotrimeric G-proteins, however many G-protein independent mechanisms have been reported.
Farnesyl-diphosphate farnesyltransferase
The activation of adenylyl (adenylate) cyclase (AC) results in the production of adenosine-3',5'-monophosphate i.e. cyclic AMP. Humans have 9 genes encoding membrane-associated AC and one encoding a soluble AC. Two of the classes of heterotrimeric G-proteins are named according to their effect on AC; Gs stimulates all membrane-bound ACs (the s in Gs denotes AC stimulatory); the Gi class inhibits some AC isoforms, particularly 5 and 6. Beta-gamma subunits of heterotrimeric G-proteins can also regulate AC. Ca2+/Calmodulin activates some AC isoforms (1, 8 and 3) but is inhibitory to others (5 and 6).
The Rho family of small guanine nucleotide binding proteins is one of five generally recognized branches of the Ras superfamily. Like most Ras superfamily members, typical Rho proteins function as binary switches controlling a variety of biological processes. They perform this function by cycling between active GTP-bound and inactive GDP-bound conformations. Mammalian Rho GTPases include RhoA, RhoB and RhoC (Rho proteins), Rac1 3 (Rac proteins), Cdc42, TC10, TCL, Wrch1, Chp/Wrch2, RhoD and RhoG, to name some. The family also includes RhoH and Rnd1-3, which lack GTPase activity and are predicted to exist in a constitutively active state. Members of the Rho family have been identified in all eukaryotes. Including the atypical RHOBTB1-3 and RHOT1-2 proteins, 24 Rho family members have been identified in mammals (Jaffe and Hall, 2005; Bernards, 2005; Ridley, 2006). Among Rho GTPases, RhoA, Rac1 and Cdc42 have been most extensively studied. These proteins are best known for their ability to induce dynamic rearrangements of the plasma membrane-associated actin cytoskeleton (Aspenstrom et al, 2004; Murphy et al, 1999; Govek et al, 2005). Beyond this function, Rho GTPases also regulate actomyosin contractility and microtubule dynamics. Rho mediated effects on transcription and membrane trafficking are believed to be secondary to these functions. At the more macroscopic level, Rho GTPases have been implicated in many important cell biological processes, including cell growth control, cytokinesis, cell motility, cell cell and cell extracellular matrix adhesion, cell transformation and invasion, and development (Govek et al., 2005). The illustration below lists Rho GTPase effectors implicated in actin and microtubule dynamics (courtesy: Govek et al., 2005, Genes and Development, CSHL Press). Detailed annotations of various biological processes regulated by Rho GTPases will be available in future releases.
The class C G-protein-coupled receptors are a class of G-protein coupled receptors that include the metabotropic glutamate receptors and several additional receptors (Bräuner-Osborne H et al, 2007). Family C GPCRs have a large extracellular N-terminus which binds the orthosteric (endogenous) ligand. The shape of this domain is often likened to a clam. Several allosteric ligands to these receptors have been identified and these bind within the seven transmembrane region.
The general function of the G alpha (s) subunit (Gs) is to activate adenylate cyclase, which in turn produces cAMP, leading to the activation of cAMP-dependent protein kinases (often referred to collectively as Protein Kinase A). The signal from the ligand-stimulated GPCR is amplified because the receptor can activate several Gs heterotrimers before it is inactivated.
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Cyclin E:phospho-Cdk2 Complex (name copied from entity in Homo sapiens)
Isopentenyl-diphosphate delta-isomerase 1
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[Receptors for cholecystokinin and gastrin]
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RNA primer-DNA primer:origin duplex with DNA damage
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Cyclin B:Cdk1 complex (name copied from entity in Homo sapiens)
RNA primer-DNA primer:origin duplex (name copied from entity in Homo sapiens)
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RNA primer:origin duplex:DNA polymerase alpha:primase complex (name copied from entity in Homo sapiens)
Cyclin E2:Cdk2 complex (name copied from entity in Homo sapiens)
Cyclin E2:phospho-Cdk2 complex (name copied from entity in Homo sapiens)
Cyclin E1:Cdk2 complex (name copied from entity in Homo sapiens)
Cyclin E1:phospho-Cdk2 complex (name copied from entity in Homo sapiens)
Guanine nucleotide exchange factors (GEFs) activate GTPases by enhancing the exchange of bound GDP for GTP. Much evidence points to GEFs being critical mediators of Rho GTPase activation (Schmidt and Hall, 2002). Many GEFs are known to be highly specific for a particular GTPase, e.g. Fgd1/Cdc42 and p115RhoGEF/Rho (Hart et al., 1996, Zheng et al., 1996). Others have a broader spectrum and activate several GTPases, e.g. Vav1 for Rac, Rho, and Cdc42 (Hart et al, 1994).
The cycling of Rho GTPases is tightly controlled by three classes of protein. These are (1) guanine nucleotide dissociation inhibitors or GDIs, which maintain Rho proteins in an inactive state in the cytoplasm, (2) guanine nucleotide exchange factors or GEFs, which destabilize the interaction between Rho proteins and their bound nucleotide, the net result of which is the exchange of bound GDP for the more abundant GTP, and (3) GTPase Activating Proteins or GAPs, which stimulate the low intrinsic GTP hydrolysis activity of Rho family members, thus promoting their inactivation. GDIs, GEFs, and GAPs are themselves subject to tight regulation, and the overall level of Rho activity reflects the balance of their activities. In their active GTP-bound state, Rho family members have the ability to interact with a large variety of so-called effector proteins. By changing the subcellular localization of effectors, by altering their enzymatic properties, or by directing the formation of specific effector complexes, members of the Rho family mediate their various effects. This Rho GTPase cycle is diagrammed in the figure below. External or internal cues promote the release of Rho GTPases from the inhibitory complex (1) which allows them to associate with the plasma membrane (2) where they are activated by GEFs (3) and can signal to effector proteins. Then, GAPs inactivate the GTPases by accelerating the intrinsic GTPase activity, leading to the GDP bound form (4). Once again, the GDI molecules stabilize the inactive GDP bound form in the cytoplasm, waiting for further instructions (5). (Figure and text from Tcherkezian and Lamarche Vane, 2007).
GDIs sequester the inactive GTPases, preventing the dissociation of GDP and interactions with regulatory and effector molecules. They maintain Rho GTPases as soluble cytosolic proteins by forming high affinity complexes. In these complexes, the geranylgeranyl membrane targeting moiety present at the C terminus of the Rho GTPases is shielded from the solvent by its insertion into the hydrophobic pocket formed by the immunoglobulin like beta sandwich of the GDI (DerMardirossian and Bokoch, 2005). Rho proteins, when released from the sequestering cytosolic GDIs, insert into the lipid bilayer of the plasma membrane with their isoprenylated C termini. The membrane bound GEFs activate these free RhoGTPases and thereby trigger the downstream signaling events via respective effector proteins on the membrane (Robbe et al., 2003). Detailed annotation of the activities of farnesyltransferase / geranylgeranyltransferases on prenylation of Rho GTPases thereby enabling their subsequent localization to plasma membrane will be available in future releases.
GDP dissociation inhibitors or GDIs confer an additional but important layer of Rho GTPase regulation along with GEFs and GAPs. GDIs mainly inhibit the dissociation of bound guanine nucleotide (usually GDP) from their partner GTPases. So far, three human GDIs with proven biological functions have been found: RhoGDI/GDIalpha/GDI1, hematopoietic cell selective Ly/D4GDI/GDIbeta/GDI2, and Rho GDIgamma/GDI3 (DerMardirossian and Bokoch, 2005). Three specific biochemical functions of GDIs have been established: inhibiting the dissociation of GDP from Rho proteins, maintaining the GTPases in an inactive form, and preventing GTPase activation by GEFs (Olofsson, 1999). Detailed annotations of GDIs will be available in future releases.
ORC:origin:cyclin B:cdk1 complex (name copied from entity in Homo sapiens)
The human genome includes approximately 70 genes that are predicted to encode Rho-specific GTPase Activating Proteins (RhoGAPs). As in the case of GEFs, some RhoGAPs are believed to be highly specific, whereas others are more promiscuous with respect to their target GTPases. Increasing evidence suggests that GAPs are also regulated by external cues in addition to being signal terminators leading to Rho GTPase inactivation. These proteins play important role in many Rho mediated signaling pathways. Some known GAPs include p190 A, cdGAP, ARAP3, MgcRacGAP, Chimaerin, Nadrin, TCGAP, DLC 1, 2, ArhGAP6, Myosin IXA. These and other GAPs have been implicated in many processes, such as exocytosis, endocytosis, cytokinesis, cell differentiation, migration, neuronal morphogenesis, angiogenesis and tumor suppression. Detailed annotations of the biological role of GAPs in Rho mediated signaling will be available in future releases.
The heterotrimeric G protein Gz, is a member of the Gi family. Unlike other Gi family members it lacks an ADP ribosylation site cysteine four residues from the carboxyl terminus and is thus pertussis toxin-insensitive. It inhibits adenylyl cyclase types I, V and VI. G alpha (z) interacts with the Rap1 GTPase activating protein (Rap1GAP) to attenuate Rap1 signaling. Like all G-proteins Gz has an intrinsic GTPase activity, but this activity tends to be lower for the pertussis toxin insensitive G-proteins, most strikingly so for Gz, whose kcat value for GTP hydrolysis is 200-fold lower than those of Gs or Gi (Grazziano et al. 1989). Gz knockout mice have disrupted platelet aggregation at physiological concentrations of epinephrine and responses to several neuroactive drugs are altered (Yang et al. 2000).
The classic signalling route for G alpha (q) is activation of phospholipase C beta thereby triggering phosphoinositide hydrolysis, calcium mobilization and protein kinase C activation. This provides a path to calcium-regulated kinases and phosphatases, GEFs, MAP kinase cassettes and other proteins that mediate cellular responses ranging from granule secretion, integrin activation, and aggregation in platelets. Gq participates in many other signalling events including direct interaction with RhoGEFs that stimulate RhoA activity and inhibition of PI3K. Both in vitro and in vivo, the G-protein Gq seems to be the predominant mediator of the activation of platelets.
The G12/13 family is probably the least well characterized subtype, partly because G12/13 coupling is difficult to determine when compared with the other subtypes which predominantly rely on assay technologies that measure intracellular calcium. The G12/13 family are best known for their involvement in the processes of cell proliferation and morphology, such as stress fiber and focal adhesion formation. Interactions with Rho guanine nucleotide exchange factors (RhoGEFs) are thought to mediate many of these processes. (Buhl et al.1995, Sugimoto et al. 2003). Activation of Rho or the regulation of events through Rho is often taken as evidence of G12/13 signaling. Receptors that are coupled with G12/13 invariably couple with one or more other G protein subtypes, usually Gq.
sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
Cyclin B:phospho-Cdc2(Thr 14) (name copied from entity in Homo sapiens)
Mad1:kinetochore complex (name copied from entity in Homo sapiens)
Kinetochore:Mad1:MAD2 Complex (name copied from entity in Homo sapiens)
MAD2*CDC20 complex (name copied from entity in Homo sapiens)
Mutations in phosphoinositide metabolizing enzymes and human disease
phospho-Cdc25C:14-3-3 protein complex (name copied from entity in Homo sapiens)
Cyclin B1:phospho-Cdc2 (Thr 14, Thr 161) (name copied from entity in Homo sapiens)
Cyclin B:Cdc2 complex (name copied from entity in Homo sapiens)
When a ligand activates a G protein-coupled receptor, it induces a conformational change in the receptor (a change in shape) that allows the receptor to function as a guanine nucleotide exchange factor (GEF), stimulating the exchange of GDP for GTP on the G alpha subunit. In the traditional view of heterotrimeric protein activation, this exchange triggers the dissociation of the now active G alpha subunit from the beta:gamma dimer, initiating downstream signalling events. The G alpha subunit has intrinsic GTPase activity and will eventually hydrolyze the attached GTP to GDP, allowing reassociation with G beta:gamma. Additional GTPase-activating proteins (GAPs) stimulate the GTPase activity of G alpha, leading to more rapid termination of the transduced signal. In some cases the downstream effector may have GAP activity, helping to deactivate the pathway. This is the case for phospholipase C beta, which possesses GAP activity within its C-terminal region.
The liganded receptor undergoes a conformational change, generating a signal that is propagated in a manner that is not completely understood to the the G-protein. This stimulates the exchange of GDP for GTP in the G-protein alpha subunit, activating the G-protein.
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. Experimental data for this reaction was obtained in vitro using rat G alpha (i) and dog Adenylate Cyclase.
Cyclin E:Cdk2 complex (name copied from entity in Homo sapiens)
The classical signalling mechanism for G alpha (i) is inhibition of the cAMP dependent pathway through inhibition of adenylate cyclase. Decreased production of cAMP from ATP results in decreased activity of cAMP-dependent protein kinases.
Cyclin E:Cdk2 complexes (name copied from entity in Homo sapiens)
G alpha z (Lounsbury et al. 1991) and G alpha 12 (Kozasa & Gilman, 1996) are excellent in vitro substrates for all three subtypes of protein kinase C (PKC). Activation of PKC in intact platelets by agents such as thrombin, thromboxane A2 (TXA2) analogues and phorbol esters leads to rapid and near-stoichiometric phosphorylation of G alpha z (Carlson et al. 1989). The primary site of G alpha z phosphorylation is Ser-27 (Lounsbury et al. 1993). This phosphorylation blocks the interaction of G alpha z with Gbeta:gamma suggesting that it is a regulatory mechanism for attenuating signalling by preventing subunit reassociation.
1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
1-acylglycerol-3-phosphate O-acyltransferase 5
Lysophosphatidic acid acyltransferase-epsilon
Pol II mediated transcription of microRNA genes
Ethanolamine-phosphate cytidylyltransferase
Choline/ethanolaminephosphotransferase 1
Upf1 senses 3'UTR length to potentiate mRNA decay
Expression of SRPRB (SRP Receptor subunit beta)
Expression of SRPR (SRP Receptor subunit alpha)
Platelet alpha2-macroglobulin and alpha1-antitrypsin
Spontaneous autophosphorylation of Lyn tyrosine kinase at both its activation segment and C-terminal tail confers altered substrate specificity
Nramp2 expression is associated with pH-dependent iron uptake across the apical membrane of human intestinal Caco-2 cells
Succinate dehydrogenase deficiency in human
Phosphatidylserine decarboxylase proenzyme Chain A
Expression of BIP (78 kDa Glucose-regulated protein, GRP78, HSPA5)
Phosphatidylserine decarboxylase proenzyme Chain B
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.
Regulation and mechanisms of mammalian double-strand break repair.
Stem cell factor and its receptor c-Kit as targets for inflammatory diseases
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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Enzymes of fatty acid metabolism. II. Properties of crystalline crotonase.
The biochemical and structural basis for trans-to-cis isomerization of retinoids in the chemistry of vision
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Cold Spring Harb Perspect Biol 4:a007864
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6-phosphogluconate dehydrogenase, decarboxylating
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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.
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.
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.
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.
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Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase
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.
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Joining of the 60S subunit to form the 80S ribosome is catalyzed by the presence of GTP-bound eIF5B.
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.
Purification and properties of isoleucyl ribonucleic acid synthetase from Escherichia coli
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.
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UTP-glucose-1-phosphate uridylyltransferase
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The genetics of mammalian circadian order and disorder: implications for physiology and disease
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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.
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.
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.
eIF4E gets released from the inactive eIF4E:4EBP complex.
Signal transduction via the stem cell factor receptor/c-Kit
Rape et al. have recently demonstrated that the order in which APC/C targeted proteins are degraded is determined by the processivity of multiubiquitination of these substrates. Processive substrates acquire a polyubiquitin chain upon binding to the APC/C once and are degraded. Distributive substrates bind, dissociate and reassociate with the APC/C multiple times before acquiring an ubiquitin chain of sufficient length to insure degradation. In addition, distributive substrates that dissociate from the APC/C with short ubiquitin chains are targeted for deubiquitination (Rape et al., 2006). Paradoxically, although the multiubiquitination of cyclin A is distributive and later substrates of APC-Cdc20 such as Securin are processive (Rape et al., 2006), Cyclin A is degraded prior to Securin and Cyclin B. The mechanisms insuring this order have not yet be determined.
Cyclin A is believed to be recognized by the APC/C:Cdc20 complex through its D-box sequence, which is 10-20 residues longer than the D-box of cyclin B (Geley et al., 2001).
Cyclin A, functions in mitosis as well as DNA replication and is degraded in the interim by the APC/C to permit normal chromosome segregation, cell division, and the onset of S phase (see Lukas and Bartek, 2004). Cyclin A is initially degraded early in mitosis by APC/C:Cdc20 when the spindle checkpoint is still active and degradation of securin and cyclin B is inhibited.
Following multiubiquitination, Cyclin A is targeted for destruction by the 26S proteasome.
mitochondrial aspartate glutamate carrier
Aspartate aminotransferase, mitochondrial precursor
aspartate aminotransferase, mitochondrial, apoenzyme monomer
D-fructose-1,6-bisphosphate 1-phosphohydrolase
D-fructose-1,6- bisphosphate 1-phosphohydrolase
Phosphoenolpyruvate carboxykinase (GTP), mitochondrial
The influence of bound GDP on the kinetics of guanine nucleotide binding to G 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.
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.
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. ÃÂ
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In this module, the processes by which calcium binding triggers actin - myosin interactions and force generation in smooth and striated muscle tissues are annotated.
Purification to homogeneity of mitochondrial acyl coa:glycine n-acyltransferase from human liver
Transcription by RNA Polymerase I, RNA Polymerase III and transcription from mitochondrial promoters.
Layers of smooth muscle cells can be found in the walls of numerous organs and tissues within the body. Smooth muscle tissue lacks the striated banding pattern characteristic of skeletal and cardiac muscle. Smooth muscle is triggered to contract by the autonomic nervous system, hormones, autocrine/paracrine agents, local chemical signals, and changes in load or length. Actin:myosin cross bridging is used to develop force with the influx of calcium ions (Ca2+) initiating contraction. Two separate protein pathways, both triggered by calcium influx contribute to contraction, a calmodulin driven kinase pathway, and a caldesmon driven pathway. Recent evidence suggests that actin, myosin, and intermediate filaments may be far more volatile then previously suspected, and that changes in these cytoskeletal elements along with alterations of the focal adhesions that anchor these proteins may contribute to the contractile cycle. Contraction in smooth muscle generally uses a variant of the same sliding filament model found in striated muscle, except in smooth muscle the actin and myosin filaments are anchored to focal adhesions, and dense bodies, spread over the surface of the smooth muscle cell. When actin and myosin move across one another focal adhesions are drawn towards dense bodies, effectively squeezing the cell into a smaller conformation. The sliding is triggered by calcium:caldesmon binding, caldesmon acting in an analogous fashion to troponin in striated muscle. Phosphorylation of myosin light chains also is involved in the initiation of an effective contraction.
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).
Pol III initiation complexes open the promoter spontaneously similar to the mechanism employed in archaeal and bacterial transcription.
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Insulin effects increased synthesis of Xylulose-5-Phosphate
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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.
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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 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 .
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.
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.
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Localization of p21-activated kinase 1 (PAK1) to pseudopodia, membrane ruffles, and phagocytic cups in activated human neutrophils
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The roles of anabolic and catabolic reactions in the synthesis and recycling of polyunsaturated fatty acids
Prostaglandins Leukot Essent Fatty Acids 67:79-83
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).
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]
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.
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'.
After the assembly of the RNA Polymerase I Holoenzyme, Rrn3 binding occurs.
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.
At the beginning of this reaction, 1 molecule of 'DNA-directed RNA polymerases I, II, and III 17.1 kDa polypeptide ', 1 molecule of 'DNA-directed RNA polymerase I 135 kDa polypeptide ', 1 molecule of 'DNA-directed RNA polymerases I, II, and III 7.0 kDa polypeptide ', 1 molecule of 'DNA-directed RNA polymerase I 16 kDa polypeptide ', 1 molecule of 'DNA-directed RNA polymerase I 40 kDa polypeptide ', and 1 molecule of 'DNA-directed RNA polymerase I largest subunit ' are present. At the end of this reaction, 1 molecule of 'RNA Polymerase I Holoenzyme (Human)' is present. This reaction takes place in the 'nucleolus'.
Translational silencing of ceruloplasmin requires the essential elements of mRNA circularization: poly(A) tail, poly(A)-binding protein, and eukaryotic translation initiation factor 4G
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.
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Human geranylgeranyl diphosphate synthase: isolation of the cDNA, chromosomal mapping and tissue expression
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The Sec61 complex is located in both the ER and the ER-Golgi intermediate compartment
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alpha-linolenic (omega3) and linoleic (omega6) acid metabolism
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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.
RNA Polymerase II promoter escape occurs after the first phosphodiester bond has been created.
Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate
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'.
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.
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.
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).
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.
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.
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Characterization of CDw92 as a member of the choline transporter-like protein family regulated specifically on dendritic cells
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1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 4
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1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 3
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 2
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1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 1
Functional expression and characterisation of a new human phosphatidylinositol 4-kinase PI4K230
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ADP signalling through P2Y purinoceptor 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_26765.2
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=3652299
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=965146
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650518
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648832
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649629
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26021.2
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=3650472
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650561
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650557
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650563
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650512
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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=3649641
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_142720.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644881
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_88373.9
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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_11629.2
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_26354.2
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PAK and other Rho-associated kinases--effectors with surprisingly diverse mechanisms of regulation
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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_106013.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_78197.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644892
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=196778
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650526
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Molecular characterization of human UDP-glucuronic acid/UDP-N-acetylgalactosamine transporter, a novel nucleotide sugar transporter with dual substrate specificity
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SnapShot: motor proteins in spindle assembly
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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_134402.5
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_94324.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1524028
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652047
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_122985.1
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_85842.9
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CHIP28 water channels are localized in constitutively water-permeable segments of the nephron
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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=3645078
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643630
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642376
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645742
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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=3644092
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_160672.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3149479
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651610
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_168435.1
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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=3649783
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_164047.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3149496
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_142916.5
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_124009.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1483256
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644096
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_123040.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651657
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649631
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_166042.1
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_84441.9
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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=3644087
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644088
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651656
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644095
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1498737
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648842
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649623
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648839
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649621
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648838
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_136857.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649676
Synthesis and interconversion of nucleotide di- and triphosphates
ATP bound to the origin recognition complex is important for preRC 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_137172.5
Releasing cohesin from chromosome arms in early mitosis: opposing actions of Wapl-Pds5 and Sgo1
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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=1498733
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3714.1
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_122617.1
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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_126386.5
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_127539.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3000241
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_165195.1
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_123470.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649729
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_164390.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649728
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_126383.5
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Neural recognition molecules of the immunoglobulin superfamily: signaling transducers of axon guidance and neuronal migration
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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_83704.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652260
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_140077.5
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_129597.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3000239
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=426955
Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases
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Human gamma-aminobutyric acid type B receptors are differentially expressed and regulate inwardly rectifying K+ channels
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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=3646739
Activation of ErbB4 by the bifunctional epidermal growth factor family hormone epiregulin is regulated by ErbB2
The architecture of the human Rad54-DNA complex provides evidence for protein translocation along DNA.
Interaction between citrate synthase and malate dehydrogenase. Substrate channeling of oxaloacetate
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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=3644296
Human DNA polymerase beta initiates DNA synthesis during long-patch repair of reduced AP sites in DNA.
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11451.2
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=200665
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3149508
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651641
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651639
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_166561.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651638
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648905
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3646755
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3646514
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3646508
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_160641.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645175
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642394
2xMMAA (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=3642461
2xMUT:AdoCbl (name copied from entity in Homo sapiens)
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2xMUT (name copied from entity in Homo sapiens)
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2xMMAA:2xMUT (name copied from entity in Homo sapiens)
ECHS1 hexamer (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)
2xMMAA:2xMUT:AdoCbl (name copied from entity in Homo sapiens)
Btn-ACACA:2Mn2+ (name copied from entity in Homo sapiens)
AMPK heterotrimer (active) (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=3642445
DGAT1 tetramer (name copied from entity in Homo sapiens)
Citrate lyase homotetramer (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=3645247
NPC1L1:ezetimibe complex (name copied from entity in Homo sapiens)
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ISYNA1:NAD+ (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=3648093
acetaminophen glutathione conjugate [ChEBI:32639]
IMPA2: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=3648130
Folding of A+U-rich RNA elements modulates AUF1 binding. Potential roles in regulation of mRNA turnover
IMPA1:Mg2+ (name copied from entity in Homo sapiens)
IMPA2 dimer (name copied from entity in Homo sapiens)
IMPA1 dimer (name copied from entity in Homo sapiens)
ITPK1:Mg2+ (name copied from entity in Homo sapiens)
PLCG1: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=3642155
The role of transient receptor potential cation channels in Ca2+ signaling
Cold Spring Harb Perspect Biol 2:a003962
PLCD3:Ca2+ (name copied from entity in Homo sapiens)
PLCH1: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=3642054
PLCG2:Ca2+ (name copied from entity in Homo sapiens)
PLCD4:Ca2+ (name copied from entity in Homo sapiens)
PLCH2: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=3642148
PLCZ1: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=3640492
PLCD1:Ca2+ (name copied from entity in Homo sapiens)
PLCE1:Ca2+ (name copied from entity in Homo sapiens)
PLCB1:Ca2+ (name copied from entity in Homo sapiens)
bHEXA (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=3640675
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=3640662
PLCB4:Ca2+ (name copied from entity in Homo sapiens)
PLCB3: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=3640656
PLCB2:Ca2+ (name copied from entity in Homo sapiens)
Mechanisms for the role of tetrahydrobiopterin in endothelial function and vascular disease
beta-Nicotinamide adenine dinucleotide phosphate
Nicotinamide adenine dinucleotide phosphate
The protein that binds the 3' end of histone mRNA: a novel RNA-binding protein required for histone pre-mRNA processing.
RPE dimer (name copied from entity in Homo sapiens)
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=3642703
PGD dimer (name copied from entity in Homo sapiens)
8xUGP2 (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=193079
PGM2:Mg++ (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=193092
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10517.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644538
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_155506.3
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'.
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 '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'.
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'.
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).
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).
Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2
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).
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).
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=193055
G6PD dimer (name copied from entity in Homo sapiens)
G6PD tetramer (name copied from entity in Homo sapiens)
Structural basis of GLUT1 inhibition by cytoplasmic ATP
GALE dimer (name copied from entity in Homo sapiens)
Characterization of the COQ5 gene from Saccharomyces cerevisiae. Evidence for a C-methyltransferase in ubiquinone biosynthesis
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_10590.2
PGYM dimer, b form (name copied from entity in Homo sapiens)
PGYM b dimer:AMP (name copied from entity in Homo sapiens)
PGYB dimer b form (name copied from entity in Homo sapiens)
PGYB b dimer:AMP (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=193132
phosphoglycerate mutase 2 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_10667.2
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=193066
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.
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.
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.
Protein kinase C and a calcium-independent phospholipase are required for IgG-mediated phagocytosis by Mono-Mac-6 cells
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.
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'.
FBP2 tetramer (name copied from entity in Homo sapiens)
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'.
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 ââ¬Åfullââ¬Â open complex formation. This reaction is sensitive to inhibition by single-stranded oligonucleotides.
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'.
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_98944.9
GOT2 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=3652037
GOT1 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_157319.3
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=3644539
FBP1 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_10325.1
pyruvate kinase M1 complex (name copied from entity in Homo sapiens)
pyruvate kinase complex, liver and RBC (name copied from entity in Homo sapiens)
malate dehydrogenase 1 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=3644555
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644559
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644560
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644561
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644563
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_103191.9
A portion of PDPK1 (PDK1) is anchored to the plasma membrane in the absence of PI3K activity through PIP2 binding (Currie et al. 1999). This PIP2-bound PDPK1 is able to bind and phosphorylate PIP2-bound AKT E17K mutants (Carpten et al. 2007, Landgraf et al. 2008) phosphorylated on serine residue S473.
PIP2-bound AKT1 E17K mutant is constitutively phosphorylated on threonine residue T308 (Carpten et al. 2007, Landgraf et al. 2008), presumably by PIP2-bound PDPK1 (Currie et al. 1999).
Substitution of glutamic acid with lysine at position 17 of AKT1 results in constitutive plasma membrane localization of AKT1, independent of PI3K activity and PIP3 generation (Carpten et al. 2007). This constitutive plasma membrane targeting of AKT1 E17K mutant is due to an increased affinity for PIP2 (Landgraf et al. 2008).
PIP2-binding AKT1 E17K mutants are anchored to the plasma membrane in the absence of PI3K activity and are constitutively phosphorylated on serine S473, presumably by the TORC2 complex (Carpten et al. 2007, Landgraf et al. 2008).
The process of vision involves two stages; the retinoid cycle which supplies and regenerates the visual chromophore required for vision and phototransduction which propagates the light signal. Defects in the genes involved in the retinoid cycle cause degenerative retinal diseases. These defective genes are described here (for reviews see Travis et al. 2007, Palczewski 2010, Fletcher et al. 2011, den Hollander et al. 2008).
One of the functions of PTEN is to act as a phosphoinositide phosphatase that catalyzes dephosphorylation of PIP3 into PIP2. PTEN thus reduces the amount of available PIP3, counteracting PI3K activity and downregulating AKT signaling. PTEN is frequently targeted by loss of function mutations in cancer and in familial cancer syndromes known as PTHS (PTEN hamartoma tumor syndromes, a collection of diseases including Cowden syndrome, Bannayan-Riley-Ruvalcaba syndrome, and Lhermitte-Duclos disease). Some PTEN loss-of-function variants are also found in autism spectrum disorder patients. For a recent review of PTEN involvement in cancer, please refer to Hollander et al. 2011. The majority of missense mutations that impair phosphoinositide phosphatase activity of PTEN cluster in exon 5 of PTEN gene and result in substitution of amino acid residues in the catalytic cleft of the phosphatase domain. Arginine at position 130 is the most frequently substituted PTEN residue in cancer. R130 of human PTEN is the last arginine residue in the conserved H-C-K/R-A-G-K-G-R sequence (corresponding to HCXXGXXR motif of protein tyrosine phosphatases) in the catalytic cleft of the PTEN phosphatase domain and is essential for catalysis (Barford et al. 1994, Lee et al. 1999). PTEN R130 substitution mutants show markedly decreased phosphoinositide phosphatase activity (Han et al. 2000, Koul et al. 2002) and are frequently found in endometrial carcinoma (Kong et al. 1997, Konopka et al. 2007). The cysteine residue at position 124 (C124) of human PTEN, in the conserved H-C-K/R-A-G-K-G-R sequence, 'attacks' the phosphate group of a substrate and forms a thio-phosphate intermediate during the dephosphorylation reaction (Guan and Dixon 1991, Barford et al. 1994, Lee et al. 1999). Therefore, substitution of this critical C124 abolishes PTEN phosphatase activity (Han et al. 2000, Koul et al. 2002). Substitution of histidine H123 in the conserved H-C-K/R-A-G-K-G-R sequence also impairs PTEN phosphatase activity (Lee et al. 1999). Missense mutations also target amino acid residues in the N-terminal phosphatase domain that are outside the catalytic cleft. Substitution of histidine at position 93 affects the conserved WPD loop of the phosphatase domain of PTEN, and PTEN H93 mutants show low phosphoinositide phosphatase activity (Lee et al. 1999). Serine residue S170 and histidine residue H173 participate in the formation of hydrogen bonds between the N-terminal phosphatase domain of PTEN and the C-terminal membrane-binding C2 domain (Lee et al. 1999). H173, and to a lesser extent S170, are targeted by missense mutations in cancer, and substitution mutants have impaired phosphoinositide phosphatase activity (Han et al. 2000). Missense mutations also occur in the C2 domain of PTEN. The C2 domain is implicated in membrane binding and localization of PTEN, but also in PTEN roles unrelated to its phosphoinositide phosphatase function (Raftopoulou et al. 2004). Since the roles of these C2 domain PTEN mutants in cancer have not been clarified, these variants will be annotated when more information becomes available. Besides missense mutations, nonsense mutations that result in PTEN protein truncation are also frequently found in cancer samples. The three residues most frequently targeted by nonsense mutations are R130, R233 and R335. While R130* mutation directly affects the phosphatase domain of PTEN, R233* and R335* affect the C2 domain. It is has not yet been elucidated whether R233* and R335* affect PTEN membrane localization or impair PTEN function in some other way. In cancer, PTEN is also frequently inactivated by genomic deletions and loss of heterozygosity (LOH) affecting chromosome band 10q23 or by epigenetic silencing (reviewed by Hollander et al. 2011).
The gene defects which cause diseases related to the retinoid cycle are described here (Travis et al. 2007, Palczewski 2010, Fletcher et al. 2011, den Hollander et al. 2008).
Lipofuscin is a yellow-brown pigment grain composed mainly of lipids but also sugars and certain metals. Accumulation of lipofuscin is associated with degenerative diseases such as Alzheimer's disease, Parkinson's disease, chronic obstructive pulmonary disease and retinal macular degeneration. A prominent component of lipofuscin in retinal pigment epithelial (RPE) cells is the bisretinoid A2E (di-retinoid-pyridinium-ethanolamine), the end-product of the condensation of 2 molecules of all-trans-retinal (atRAL) and phosphatidylethanolamine (PE) in photoreceptor outer disc membranes. Once formed, A2E is phagocytosed, together with outer segments (Kevany & Palczewski 2010), to RPE where it accumulates. There is no evidence as yet to indicate that A2E can be catabolised (Sparrow et al. 2012, Sparrow et al. 2010). A simplified biosynthetic pathway for A2E is described here.
The outer segment of photoreceptor cells is shed every 10-14 days to be completely replaced. The shed material is phagocytosed and transferred to the retinal pigment epithelium (RPE). Diretinoid-pyridinium-phosphatidylethanolamine (A2PE) can be hydrolysed to diretinoid-pyridinium-ethanolamine (A2E), a prominent constituent of lipofuscin (the material deposited in retinal tissue which accumulates over time and is implicated in macular degeneration). Evidence suggests this happens before transfer to RPE cells as part of the phagocytosed outer segment. A2E has been detected in outer segments (Ben-Shabat et al. 2002) and an N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D (NAPEPLD) activity detected in rat, mouse and human proteins (Okamoto et al. 2004, Ueda et al. 2005, Wang et al. 2006). This activity has been shown to hydrolyse A2PE to A2E in bovine outer segments before phagocytosis and transfer to RPE cells, suggesting A2PE is hydrolysed to A2E in photoreceptor outer segment membranes (Sparrow et al. 2003, Salvador & Giusto 1998).
The mucopolysaccharidoses (MPS) are a group of rare, inherited lysosomal storage disorders caused by deficiencies of enzymes catalyzing the stepwise degradation of glycosaminoglycans (GAGs, originally called mucopolysaccharides) (Neufeld & Muenzer in Scriver et al. 2001). Catabolism of the GAGs dermatan sulfate, heparan sulfate, heparin, keratan sulfate, chondroitin sulfate or hyaluronan may be blocked at one or more steps, resulting in lysosomal accumulation of GAG fragments of varying size. Over time these collect in the cells, blood and connective tissues ultimately resulting in progressive irreversible cellular damage which affects appearance, physical abilities, organ and system function, vision, and usually mental development (Lehman et al. 2011, Ashworth et al. 2006). Life expectancy is also reduced. There are 11 known enzyme deficiencies that give rise to 7 distinct MPS. These disorders are biochemically characterized by elevated levels of partially or undegraded GAGs in lysosomes, blood, urine and cerebro-spinal fluid (Muenzer 2011, Coutinho et al. 2012). The MPS are part of the lysosomal storage disease family, a group of about 50 genetic disorders caused by deficient lysosomal proteins (Ballabio & Gieselmann 2009).
phosphoglycerate mutase 1 dimer (name copied from entity in Homo sapiens)
Biotin-responsive basal ganglia disease-linked mutations inhibit thiamine transport via hTHTR2: biotin is not a substrate for hTHTR2
ALDOB tetramer (name copied from entity in Homo sapiens)
The Xenopus Xmus101 protein is required for the recruitment of Cdc45 to origins of DNA replication.
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)
glyceraldehyde-3-phosphate dehydrogenase, testis-specific, tetramer (name copied from entity in Homo sapiens)
phosphoglycerate kinase 1 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_10200.2
glyceraldehyde-3-phosphate dehydrogenase tetramer
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=194035
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=176626
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29510
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3097.2
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_156507.3
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_7166.3
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=3644537
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'.
This pathway describes how normal signaling by PI3K/AKT, presented in the contained module 'PIP3 Activates AKT Signaling' and recently reviewed by Manning and Cantley in 2007, is perturbed in cancer, as described in the contained module 'Constitutive Signaling by PI3K/AKT'. Please refer to Liu et al. 2009 and Hollander et al. 2011 for recent reviews.
Mutant forms of IDH1 in which the arginine residue at position 132 has been replaced by histidine, cystine, leucine, or serine catalyze the reaction of 2-oxoglutarate and NADPH + H+ to form (R)-2-hydroxyglutarate and NADP+. Like normal IDH1, the mutant enzyme forms a dimer located in the cytosol (Dang et al. 2009). Such mutations occur frequently as a somatic event in human glioblastomas (Parsons et al. 2008). Cells expressing the mutant protein accumulate elevated levels of 2-hydroxyglutarate, probably in the cytosol as IDH1 is a cytosolic enzyme. The fate of the 2-hydroxyglutarate is unclear, but the high frequency with which the mutation is found in surveys of primary tumors is consistent with the possibility that it is advantageous to the tumor cells (Dang et al. 2009).
Somatic mutations affecting arginine residue 132 of IDH1 (isocitrate dehydrogenase 1, a cytosolic enzyme that normally catalyzes the NADP+-dependent conversion of isocitrate to 2-oxoglutarate), are very commonly found in human glioblastomas (Parsons et al. 2008). These mutant proteins efficiently catalyze the NADPH-dependent reduction of 2-oxoglutarate to form 2-hydroxyglutarate. Cells expressing the mutant protein accumulate elevated levels of 2-hydroxyglutarate, probably in the cytosol as IDH1 is a cytosolic enzyme. The fate of the 2-hydroxyglutarate is unclear, but the high frequency with which the mutation is found in surveys of primary tumors is consistent with the possibility that it is advantageous to the tumor cells (Dang et al 2009).
Biological processes are captured in Reactome by identifying the molecules (DNA, RNA, protein, small molecules) involved in them and describing the details of their interactions. From this molecular viewpoint, human disease pathways have three mechanistic causes: the inclusion of microbially-expressed proteins, altered functions of human proteins, or changed expression levels of otherwise functionally normal human proteins. The first group encompasses the infectious diseases such as influenza, tuberculosis and HIV infection. The second group involves human proteins modified either by a mutation or by an abnormal post-translational event that produces an aberrant protein with a novel function. Examples include somatic mutations of EGFR and FGFR (epidermal and fibroblast growth factor receptor) genes, which encode constitutively active receptors that signal even in the absence of their ligands, or the somatic mutation of IDH1 (isocitrate dehydrogenase 1) that leads to an enzyme active on 2-oxoglutarate rather than isocitrate, or the abnormal protein aggregations of amyloidosis which lead to diseases such as Alzheimer's. Infectious diseases are represented in Reactome as microbial-human protein interactions and the consequent events. The existence of variant proteins and their association with disease-specific biological processes is represented by inclusion of the modified protein in a new or variant reaction, an extension to the 'normal' pathway. Diseases which result from proteins performing their normal functions but at abnormal rates can also be captured, though less directly. Many mutant alleles encode proteins that retain their normal functions but have abnormal stabilities or catalytic efficiencies, leading to normal reactions that proceed to abnormal extents. The phenotypes of such diseases can be revealed when pathway annotations are combined with expression or rate data from other sources.
AKT1 E17K gain-of-function mutant is expected to phosphorylate ribosomal protein S6 kinase beta-2, like the wild-type AKT (Koh et al. 1999), but this has not been experimentally tested.
phosphofructokinase, L4 complex (name copied from entity in Homo sapiens)
AKT1 E17K gain-of-function mutant is expected to translocate to the nucleus, like the wild-type AKT (Borgatti et al. 2003), but this has not been directly experimentally tested.
phosphofructokinase, P4 complex (name copied from entity in Homo sapiens)
Class IA PI3K is a heterodimer of a p85 regulatory subunit (encoded by PIK3R1, PIK3R2 or PIK3R3) and a p110 catalytic subunit (encoded by PIK3CA, PIK3CB or PIK3CD). In the absence of activating signals, the regulatory subunit stabilizes the catalytic subunit while inhibiting its activity. The complex becomes activated when extracellular signals stimulate the phosphorylation of the cytoplasmic domains of transmembrane receptors or receptor-associated proteins. The p85 regulatory subunit binds phosphorylated motifs of activator proteins, which induces a conformational change that relieves p85-mediated inhibition of the p110 catalytic subunit and enables PI3K to phosphorylate PIP2 to form PIP3. The phosphoinositide kinase activity of PI3K is opposed by the phosphoinositide phosphatase activity of PTEN. PIP3 acts as a messenger that recruits PDPK1 (PDK1) and AKT (AKT1, AKT2 or AKT3) to the plasma membrane. PDPK1 also possesses a low affinity for PIP2, so small amounts of PDPK1 are always present at the membrane. Binding of AKT to PIP3 induces a conformational change that enables TORC2 complex to phosphorylate AKT at a conserved serine residue (S473 in AKT1). Phosphorylation at the serine residue enables AKT to bind to PDPK1 and exposes a conserved threonine residue (T308) that is phosphorylated by PDPK1. AKT phosphorylated at both serine and threonine residues dissociates from the plasma membrane and acts as a serine/threonine kinase that phosphorylates a number of cytosolic and nuclear targets involved in regulation of cell metabolism, survival and gene expression. For a recent review, please refer to Manning and Cantley, 2007. Signaling by PI3K/AKT is frequently constitutively activated in cancer. This activation can be via gain-of-function mutations in PI3KCA (encoding catalytic subunit p110alpha), PIK3R1 (encoding regulatory subunit p85alpha) and AKT1. The PI3K/AKT pathway can also be constitutively activated by loss-of-function mutations in tumor suppressor genes such as PTEN. Gain-of-function mutations activate PI3K signaling by diverse mechanisms. Mutations affecting the helical domain of PIK3CA and mutations affecting nSH2 and iSH2 domains of PIK3R1 impair inhibitory interactions between these two subunits while preserving their association. Mutations in the catalytic domain of PIK3CA enable the kinase to achieve an active conformation. PI3K complexes with gain-of-function mutations therefore produce PIP3 and activate downstream AKT in the absence of growth factors (Huang et al. 2007, Zhao et al. 2005, Miled et al. 2007, Horn et al. 2008, Sun et al. 2010, Jaiswal et al. 2009, Zhao and Vogt 2010, Urick et al. 2011). While AKT1 gene copy number, expression level and phosphorylation are often increased in cancer, only one low frequency point mutation has been repeatedly reported in cancer and functionally studied. This mutation represents a substitution of a glutamic acid residue with lysine at position 17 of AKT1, and acts by enabling AKT1 to bind PIP2. PIP2-bound AKT1 is phosphorylated by TORC2 complex and by PDPK1 that is always present at the plasma membrane, due to low affinity for PIP2. Therefore, E17K substitution abrogates the need for PI3K in AKT1 activation (Carpten et al. 2007, Landgraf et al. 2008). Loss-of-function mutations affecting the phosphatase domain of PTEN are frequently found in sporadic cancers (Kong et al. 1997, Lee et al. 1999, Han et al. 2000), as well as in PTEN hamartoma tumor syndromes (PHTS) (Marsh et al. 1998). PTEN can also be inactivated by gene deletion or epigenetic silencing, or indirectly by overexpression of microRNAs that target PTEN mRNA (Huse et al. 2009). Cells with deficient PTEN function have increased levels of PIP3, and therefore increased AKT activity. For a recent review, please refer to Hollander et al. 2011. Because of their clear involvement in human cancers, PI3K and AKT are targets of considerable interest in the development of small molecule inhibitors. Although none of the currently available inhibitors display preference for mutant variants of PIK3CA or AKT, several inhibitors targeting the wild-type kinases are undergoing clinical trials. These include dual PI3K/mTOR inhibitors, class I PI3K inhibitors, pan-PI3K inhibitors, and pan-AKT inhibitors. While none have yet been approved for clinical use, these agents show promise for future therapeutics. In addition, isoform-specific PI3K and AKT inhibitors are currently being developed, and may provide more specific treatments along with reduced side-effects. For a recent review, please refer to Liu et al. 2009.
phosphofructokinase, P3L complex (name copied from entity in Homo sapiens)
AKT inhibitors bind AKT and prevent its association with the membrane, thereby blocking AKT activation (Kondapaka et al. 2003, Yap et al. 2011, Berndt et al. 2010). AKT inhibitors annotated here target all AKT isoforms (AKT1, AKT2 and AKT3). None of the annotated inhibitors are AKT E17K mutant specific and none of them have been approved for clinical use. For a recent review, please refer to Liu et al. 2009.
AKT1 E17K gain-of-function mutant preserves the ability to phosphorylate GSK3 (Malanga et al. 2008). AKT-mediated phosphorylation inactivates GSK3 and enables WNT-independent stabilization of beta-catenin (CTNNB1) (Haq et al. 2003). AKT-mediated inactivation of GSK3 also triggers changes in glucose metabolism (Ueki et al. 1997).
KIF18A dimer (name copied from entity in Homo sapiens)
Kinesin-14 (name copied from entity in Homo sapiens)
Kinesins:microtubule (name copied from entity in Homo sapiens)
PPA1 dimer (name copied from entity in Homo sapiens)
A novel mechanism for GABA synthesis and packaging into synaptic vesicles
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PPA2 dimer (name copied from entity in Homo sapiens)
The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes.
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glucose 6-phosphate isomerase dimer (name copied from entity in Homo sapiens)
Expression, purification, and characterization of human and rat acetyl coenzyme A carboxylase (ACC) isozymes
Enoyl-CoA hydratase, mitochondrial precursor
Identification of a vertebrate sister-chromatid separation inhibitor involved in transformation and tumorigenesis
Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase
1-acylglycerol-3-phosphate O-acyltransferase 9
KIF4A homodimer (name copied from entity in Homo sapiens)
Kinesin-10 (name copied from entity in Homo sapiens)
DOCK-GEFs:RAC1, CDC42 (name copied from entity in Homo sapiens)
F-actin capping protein:f-actin (name copied from entity in Homo sapiens)
LRRC16A:F-actin capping protein (name copied from entity in Homo sapiens)
CENP-E dimer (name copied from entity in Homo sapiens)
Centralspindlin (name copied from entity in Homo sapiens)
Kinesin-5 homotetramer (name copied from entity in Homo sapiens)
KIF4B homodimer (name copied from entity in Homo sapiens)
Succinyl-CoA:3-ketoacid-coenzyme A transferase, 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
Acetyl-CoA acetyltransferase, mitochondrial
Methylmalonic aciduria type A protein, mitochondrial ecNumber3.6.-.-/ecNumber
Methylmalonyl-CoA mutase, mitochondrial precursor
PIP3:PDK1:AKT:PKC zeta (name copied from entity in Homo sapiens)
RNA primer-DNA primer:G-strand extended telomere:PCNA (name copied from entity in Homo sapiens)
CalDAG-GEFs:DAG:Ca2+ (name copied from entity in Homo sapiens)
PIP3:PDK1:AKT:p(T410)-PKC zeta (name copied from entity in Homo sapiens)
Preferential cleavage of chromatin-bound cohesin after targeted phosphorylation by Polo-like kinase
RFC Heteropentamer:RNA primer-DNA primer:G-strand extended telomere end duplex:PCNA homotrimer (name copied from entity in Homo sapiens)
F-actin capping protein (name copied from entity in Homo sapiens)
Protein kinase C, novel isoforms:DAG (name copied from entity in Homo sapiens)
Activated PKC gamma (name copied from entity in Homo sapiens)
Activated PKC alpha (name copied from entity in Homo sapiens)
acyl-CoA synthetase long-chain family member 1
acyl-CoA synthetase long-chain family member 5
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1-acyl-sn-glycerol-3-phosphate acyltransferase delta
1-acylglycerol-3-phosphate O- acyltransferase 4
Lysophosphatidic acid acyltransferase-delta
Lysophosphatidic acid acyltransferase-gamma
1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
1-acylglycerol-3-phosphate O- acyltransferase 3
Lysophosphatidic acid acyltransferase-beta
1-acylglycerol-3-phosphate O- acyltransferase 2
1-acyl-sn-glycerol-3-phosphate acyltransferase beta
Lysophosphatidic acid acyltransferase-alpha
1-acylglycerol-3-phosphate O- acyltransferase 1
1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
Molecular cloning and functional expression of cDNAs encoding a human Na+-nucleoside cotransporter (hCNT1)
1-acylglycerol-3-phosphate O-acyltransferase 8
di-retinoid-pyridinium-ethanolamine [ChEBI:71980]
1-acylglycerol-3-phosphate O-acyltransferase 6
Nitric oxide stimulates guanylate cyclase
Proactivator polypeptide (Contains: Saposin-A)
Maintaining copper homeostasis: regulation of copper-trafficking proteins in response to copper deficiency or overload
Identification and functional characterization of adipose-specific phospholipase A2 (AdPLA)
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Electrostatics of aquaporin and aquaglyceroporin channels correlates with their transport selectivity
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Deoxyhypusine hydroxylase is a Fe(II)-dependent, HEAT-repeat enzyme. Identification of amino acid residues critical for Fe(II) binding and catalysis [corrected].
International Union of Basic and Clinical Pharmacology. LXXXV: calcium-activated chloride channels
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Control of mRNA decay by phosphorylation of tristetraprolin
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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
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The mitochondrial ornithine transporter. Bacterial expression, reconstitution, functional characterization, and tissue distribution of two human isoforms
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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).
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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).
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).
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.
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).
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).
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).
Crystal structure of Spot 14, a modulator of fatty acid synthesis
Proc. Natl. Acad. Sci. U.S.A. 107:18820-5
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)
Leucine-rich repeat-containing protein 16A
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Structures and mechanisms of Nudix hydrolases
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Structural basis for activation of calcineurin by calmodulin
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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).
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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).
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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).
Megakaryocyte development and platelet production
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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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).
A cytosolic, non-specific peptidase can hydrolyze cysteinylglycine to release cysteine and glycine (Tuefel et al, 2003).
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.
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.
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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Bromodomain and PHD finger-containing protein 3
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Low levels of glucose transporters and K+ATP channels in human pancreatic beta cells early in development
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.
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).
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.
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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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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.
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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.
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Fc receptor-mediated phagocytosis requires CDC42 and Rac1
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.
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NMD: multitasking between mRNA surveillance and modulation of gene expression
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.
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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.
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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).
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The committed step for porphyrin synthesis is the formation of 5-aminolevulinate (ALA) by condensation of glycine (from the general amino acid pool) and succinyl-CoA (from the TCA cycle), in the mitochondrial matrix. The reaction is catalyzed by two different ALA synthases, one expressed ubiquitously (ALAS1) and the other only expressed in erythroid precursors (ALAS2). Both enzymes are expressed as homodimers and require pyridoxal 5-phosphate as a cofactor. No disease-causing mutations of ALAS1 have been recognised in humans. Mutations in ALAS2 cause X-linked sideroblastic anaemia (XLSA), characterised by a microcytic hypochromic anaemia.
5-Aminolevulinic acid dehydratase (ALAD aka porphobilinogen synthase, PBGS), catalyzes the asymmetric condensation of two molecules of ALA to form porphobilinogen (PBG). The substrate that becomes the acetyl side chain-containing half of PBG is called A-side ALA; the half that becomes the propionyl side chains and the pyrrole nitrogen is called P-ALA (Jaffe 2004). PBG is the first pyrrole formed, the precursor to all tetrapyrrole pigments such as heme and chlorophyll. There are at least eight bonds that are made or broken during this reaction. The active form of the ALAD enzyme is an octamer complexed with eight Zn2+ ions, four that are strongly bound and four that are weakly bound. The four weakly bound ones are dispensible for enzyme activity in vitro (Bevan et al. 1980; Mitchell et al. 2001). Deficiencies of ALAD enzyme in vivo are associated with 5-aminolevulinate dehydratase-deficient porphyria (e.g., Akagi et al. 2000).
Lead binds to ALAD enzyme displacing half the zinc ions essential for its catalytic activity and inactivating it. Lead is a major environmental toxin and this enzyme is one of its principal molecular targets (Jaffe et al. 2001).
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Cytosolic uroporphyrinogen decarboxylase (UROD) catalyzes the sequntial removal of four carboxylic groups from the acetic acid side chains of uroporphyrinogen III (URO3) to form coproporphyrinogen III (COPRO3) (de Verneuil et al. 1983). Human UROD is a dimer (Whitby et al. 1998). Heterogenous and homogenous deficiencies of UROD are associated with porphyria cutanea tarda and hepatoerythropoietic porphyria respectively in vivo (Moran-Jiminez et al. 1996).
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Cytosolic porphobilinogen deaminase catalyzes the polymerization of four molecules of porphobilinogen (PBG) to generate hydroxymethylbilane (HMB), an unstable tetrapyrrole. This reaction is the first step in the formation of the tetrapyrrole macrocycle. Two isoforms of porphobilinogen deaminase are generated by alternative splicing, one expresssed in erythroid tissues and one ubiquitously expressed in the body. Deficiencies of both forms of PBG deaminase are associated with acute intermittent porphyria.
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O2-dependent coproporpyrinogen oxidase (CPO) catalyzes the conversion of coproporphyrinogen III (COPRO3) to protoporphyrinogen IX (PPGEN9). The localization of the human enzyme to the mitochondrial intermembrane space is inferred from studies of the homologous rat enzyme (Elder and Evans 1978). The human enzyme functions as a homodimer (Lee et al. 2005). Enzyme deficiency is associated with hereditary coproporphyria in vivo.
Cytosolic uroporphyrinogen decarboxylase (UROD) catalyzes the sequential removal of four carboxylic groups from the acetic acid side chains of uroporphyrinogen I (URO1) to form coproporphyrinogen I (COPRO1). UROD catalyzes this reaction less efficiently than the decarboxylation of uroporphyrinogen III (de Verneuil et al. 1983).
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Ferrochelatase (FECH) catalyzes the insertion of ferrous iron into protoporphyrin IX (PRIN9) to form heme. FECH is localized on the matrix surface of the inner mitochondrial membrane and this reaction takes place within the mitochondrial matrix. The enzyme functions as a homodimer with each monomer containing a nitric oxide-sensitive 2Fe-2S cluster. Enzyme deficiency is associated with erythropoietic protoporphyria in vivo, and inhibition of ferrochelatase activity is a clinically important consequence of lead poisoning (Piomelli et al. 1987).
Six electrons are oxidized in protophorphyrinogen IX (PPGEN9) to form the planar macrocycle protoporphyrin IX (PRIN9). This reaction is performed by the enzyme protoporphyrinogen oxidase (PPO). PPO functions as a homodimer containing one non-covalently-bound FAD. The protein resides on the outer surface of the inner mitochondrial membrane. PPO deficiency is associated with variegate porphyria in vivo.
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3-(2-Aminoethyl)-1H-indol-5-ol [ChEBI:28790]
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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.
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 '.
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.
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.
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Benzoic acid, widely used as a food preservative, is converted to hippuric acid by activation and conjugation with glycine. This was one of the first detoxification pathways discovered, and was formerly exploited clinically as an alternative means of nitrogen excretion in patients with urea cycle defects (Brusilow and Horwich 2001).
Benzoate and ATP react with coenzyme A to form benzoyl CoA, AMP, and pyrophosphate (Vessey et al. 1999, 2003). Two human CoA ligases have been characterized that catalyze this reaction efficiently in vitro: acyl-CoA synthetase medium-chain family member 1 (BUCS1) (Fujino et al. 2001) and xenobiotic/medium-chain fatty acid:CoA ligase (Vessey et al. 2003). Their relative contributions to benzoate metabolism in vivo are unknown.
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.
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.
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).
A novel member of a zinc transporter family is defective in acrodermatitis enteropathica
In the second step in the formation of glutathione, gamma-glutamylcysteine ligates with glycine to form glutathione (Gali and Board, 1995; ).
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Relationship between interferon-gamma, indoleamine 2,3-dioxygenase, and tryptophan catabolism
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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).
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.
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.
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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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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.
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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.
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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.
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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.
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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.
ACSS1 (acyl-CoA synthetase short-chain family member 1) in the mitochondrial matrix catalyzes the reaction of acetate, coenzyme A, and ATP to form acetyl-CoA, AMP, and pyrophosphate (Schwer et al. 2006).
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.
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The Rhesus blood group type A glycoprotein (RhAG) passively transports carbon dioxide (CO2) across the plasma membrane according to the concentration gradient (Endeward et al. 2006, Endeward et al. 2008, Musa-Aziz et al. 2009).
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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.
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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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.
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.
Evaluation of the "scanning model" for initiation of protein synthesis in eucaryotes.
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).
Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue monophosphates.
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).
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 and Mitoferrin-2. (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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Phospholipid synthesis in a membrane fraction associated with mitochondria
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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.
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Xenobiotics that contain either a carboxylic group or an aromatic hydroxylamine group are possible substrates for amino acid conjugation. Xenobiotics with a carboxylic group conjugate with an amino group of amino acids such as glycine, taurine and glutamine. The hydroxylamine group conjugates with the carboxylic group of amino acids such as proline and serine. The amino acid is first activated by an aminoacyl-tRNA-synthetase which then reacts with the hydroxylamine group to form a reactive N-ester. N-esters can degrade to form electrophilic nitrenium (R-N+-R') and carbonium (R-C+H2) ions. The pyrolysis product of tryptophan, an N-hydroxy intermediate, can potentially form these reactive electrophilic ions.
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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.
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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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Phenylacetate and ATP react with coenzyme A to form phenylacetyl CoA, AMP, and pyrophosphate (Vessey et al. 1999). Two human CoA ligases have been characterized that catalyze this reaction efficiently in vitro: acyl-CoA synthetase medium-chain family member 1 (BUCS1) (Fujino et al. 2001) and xenobiotic/medium-chain fatty acid:CoA ligase (Vessey et al. 2003). Their relative contributions to phenylacetate metabolism in vivo are unknown.
In the body, aspirin (acetylsalicylic acid) is hydrolyzed to salicylic acid. Salicylic acid (2-hydroxybenzoic acid) can then be hydroxylated to yield gentisic acid, conjugated with glucuronate, or conjugated with glycine to yield molecules that are excreted by the kidneys. The third of these conjugation processes is annotated here, and proceeds in two steps. First, salicylate and ATP react with coenzyme A to form salicylate CoA, AMP, and pyrophosphate in a reaction catalyzed by xenobiotic/medium-chain fatty acid:CoA ligase (Vessey et al. 2003). Second, salicylate CoA and glycine react to form salicyluric acid and Coenzyme A (Mawal and Qureshi 1994).
Xenobiotics and endogenous compounds containing carboxylate groups can be activated with coenzyme A to produce acyl-CoA thioesters and then conjugated with the amino groups of glycine or glutamine to form amide-linked conjugates. Clinically important substrates include benzoic acid, phenylacetic acid, and salicylic acid.
Phenylacetate metabolism is of clinical importance because its conjugation with glutamine to form phenylacetylglutamine, which can be excreted in the urine, provides an alternative pathway for nitrogen excretion in patients with urea cycle defects (James et al. 1972; Batshaw et al. 2001; Brusilow and Horwich 2001). This conjugation proceeds in two steps. First, phenylacetate and ATP react with coenzyme A to form phenylacetyl CoA, AMP, and pyrophosphate (Vessey et al. 1999). Two human CoA ligases have been characterized that catalyze this reaction efficiently in vitro: acyl-CoA synthetase medium-chain family member 1 (BUCS1) (Fujino et al. 2001) and xenobiotic/medium-chain fatty acid:CoA ligase (Vessey et al. 2003). Their relative contributions to phenylacetate metabolism in vivo are unknown. Second, phenylacetyl CoA and glutamine react to form phenyacetyl glutamine and Coenzyme A. The enzyme that catalyzes this reaction has been purified from human liver mitochondria and shown to be a distinct polypeptide species from glycine-N-acyltransferase (Webster et al. 1976). This human glutamine-N-acyltransferase activity has not been characterized by sequence analysis at the protein or DNA level, however, and thus cannot be associated with a known human protein in the annotation of phenylacetate conjugation.
Salicylate and ATP react with coenzyme A to form salicylate CoA, AMP, and pyrophosphate in a reaction catalyzed by xenobiotic/medium-chain fatty acid:CoA ligase (Vessey et al. 2003).
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Inactive PAK-2 can be partially autophosphorylated in the regulatory region without being activated (Gatti et al. 1999).
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In response to stress signals, the p21-activated protein kinase PAK-2 stimulates a cell death response characterized by increased cell rounding and apoptotic chromatin condensation (see Jakobi et al., 2003). PAK-2 is proteolytically cleaved by caspase-3 producing a constitutively active fragment, PAK-2p34. Following cleavage, PAK-2p34 is autophosphorylated at Thr 402 and transported to the nucleus where it accumulates due to the loss of its nuclear export signal motif (Jakobi et al., 2003). The activity of PAK-2p34 appears to be regulated both by proteosomal degradation (Jakobi et al., 2003) and by association with the GTPase-activating protein PS-GAP/ RHG-10. This interaction inhibits the kinase activity of PAK-2p34 and changes the localization of PAK-2p34 from the nucleus to the perinuclear region (Koeppel et al., 2004). PAK-2p34 may function in the down-regulation of translation initiation in apoptosis through phosphorylation of Mnk1 (Orton et al.,2004).
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Apoptotic factors released from the mitochondria promote apoptosis through several different mechanisms. Cytochrome C participates in Apoptosome driven effector caspase activation while SMAC relieves IAP mediated caspase inhibition.
The intrinsic (Bcl-2 inhibitable or mitochondrial) pathway of apoptosis functions in response to various types of intracellular stress including growth factor withdrawal, DNA damage, unfolding stresses in the endoplasmic reticulum and death receptor stimulation. Following the reception of stress signals, proapoptotic BCL-2 family proteins are activated and subsequently interact with and inactivate antiapoptotic BCL-2 proteins. This interaction leads to the destabilization of the mitochondrial membrane and release of apoptotic factors. These factors induce the caspase proteolytic cascade, chromatin condensation, and DNA fragmentation, ultimately leading to cell death. The key players in the Intrinsic pathway are the Bcl-2 family of proteins that are critical death regulators residing immediately upstream of mitochondria. The Bcl-2 family consists of both anti- and proapoptotic members that possess conserved alpha-helices with sequence conservation clustered in BCL-2 Homology (BH) domains. Proapoptotic members are organized as follows: 1. "Multidomain" BAX family proteins such as BAX, BAK etc. that display sequence conservation in their BH1-3 regions. These proteins act downstream in mitochondrial disruption. 2. "BH3-only" proteins such as BID,BAD, NOXA, PUMA,BIM, and BMF have only the short BH3 motif. These act upstream in the pathway, detecting developmental death cues or intracellular damage. Anti-apoptotic members like Bcl-2, Bcl-XL and their relatives exhibit homology in all segments BH1-4. One of the critical functions of BCL-2/BCL-XL proteins is to maintain the integrity of the mitochondrial outer membrane.
Activation of PAK-2p34 coincides with autophosphorylation of Thr 402 in the the catalytic domain (Walter et al., 1998).
The subcellular localization of PAK-2 is controlled by nuclear localization and nuclear export signal motifs (Jakobi et al.,2003). The regulatory domain contains a nuclear export signal motif that prevents the nuclear accumulation of full-length PAK-2. The activating proteolytic cleavage disrupts the nuclear export signal in PAK-2 and removes most its regulatory domain. The resulting activated PAK-2p34 fragment contains a nuclear localization signal and translocates to and is retained in the nucleus (Jakobi et al.,2003).
A complex of four proteins termed CIA targeting complex is involved in the delivery of the NUBP1-NUBP2-bound Fe/S cluster to specific target apoproteins. NARFL (IOP1, Nar1 in yeast) is similar in sequence to iron-only hydrogenases and binds two [4Fe-4S] clusters. These cofactors are essential for biogenesis but their molecular function is unknown. The WD40 domain protein CIAO1 (Cia1 in yeast) forms a propeller-like structure which may serve as a docking site for the other members of the CIA targeting complex. The role of FAM96B (YHR122W, CIA2 in yeast) and MMS19 is still unclear, but they show some specificity for the delivery of Fe/S clusters into certain target apoproteins. They directly interact with numerous Fe/S target proteins including many proteins involved in nuclear DNA integrity and maintenance such as DNA polymerases (POLD1), helicases of the DNA repair pathway (XPD or FANCJ) or of telomere maintenance (RTEL1), and primases. Cells with mutated MMS19 are hypersensitive to DNA damage and have elongated telomeres therefore these target proteins are relevant to various cancer-related diseases and aging.
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 Mühlenhoff 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.
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.
Permeabilization of the outer mitochondrial membrane by pro-apoptotic BCL2 family proteins, such as BAK and BAX, allows cytochrome c eflux from the mitochondrial intermembrane space into the cytosol (Arnoult et al. 2003).
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A [4Fe-4S] cluster is assembled on a scaffold composed of the P-loop NTPases NUBP2 (CFD1 in yeast) and NUBP1 (Nbp35 in yeast) in a nucleotide-dependent fashion. The two proteins form a heterotetramer which transiently binds the [4Fe-4S] cluster in a bridged form between two subunits of the complex. The Fe/S cluster is bound to two highly conserved Cys residues in the C-termini of each of these proteins. NUBP1 contains an additional, stably associated [4Fe-4S] cluster at its N-terminus which is essential for function. Mitochondria play a crucial role in cytosolic and nuclear Fe/S protein biogenesis. They export via a mitochondrial ABC transporter (yeast ATM1, human ABCB7) a still unknown, sulfur-containing compound which is essential for Fe/S cluster assembly in the cytosol. The general cytosolic iron donor, the multi-domain monothiol glutaredoxin (human GRX3 or PICOT, yeast Grx3-Grx4) plays a crucial role in cytosolic-nuclear Fe/S protein biogenesis. The precise molecular function of the glutaredoxin is still unclear.
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.
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.
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).
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).
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 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).
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).
ATP-binding cassette sub-family G member 2 (ABCG2), associated with the plasma membrane, mediates the ATP-dependent efflux of abacavir (Doyle et al. 1998). The active form of ABCG2 is a homodimer stabilized by an interchain disulfide bond (Wakabayashi et al. 2007). The abacavir specificity of the human ABCG2 transporter is inferred from studies of the corresponding mouse protein (Pan et al. 2007).
Chaperonins: The hunt for the Group II mechanism
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Molecular cloning of human Syk. A B cell protein-tyrosine kinase associated with the surface immunoglobulin M-B cell receptor complex
Mechanisms of phagocytosis in macrophages
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Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding
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Assembly and protection of the radical enzyme, methylmalonyl-CoA mutase, by its chaperone
Immunodeficiency in protein kinase cbeta-deficient mice
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Identification of three cationic amino acid transporters in placental trophoblast: cloning, expression, and characterization of hCAT-1
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RNA Polymerase II Pre-transcription Events
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G alpha 12 and G alpha 13 stimulate Rho-dependent stress fiber formation and focal adhesion assembly
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alpha-ketoglutarate dehydrogenase E1 homodimer (name copied from entity in Homo sapiens)
alpha-ketoglutarate dehydrogenase E1 holoenzyme (name copied from entity in Homo sapiens)
Succinyl-CoA synthetase heterodimer (GDP-forming) (name copied from entity in Homo sapiens)
Succinyl-CoA synthetase heterodimer (ADP-forming) (name copied from entity in Homo sapiens)
Succinate dehydrogenase complex (oxidised) (name copied from entity in Homo sapiens)
Succinate dehydrogenase Iron Sulphur (subunit B) (name copied from entity in Homo sapiens)
Specificity, promiscuity and localization of ARF protein interactions with NCS-1 and phosphatidylinositol-4 kinase-III beta
Succinate dehydrogenase flavoprotein (subunit A), oxidised (name copied from entity in Homo sapiens)
Succinate dehydrogenase complex (reduced) (name copied from entity in Homo sapiens)
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fumarate hydratase tetramer (name copied from entity in Homo sapiens)
Succinate dehydrogenase flavoprotein (subunit A) (name copied from entity in Homo sapiens)
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alpha-keto acid dehydrogenase E3 holoenzyme (name copied from entity in Homo sapiens)
pyruvate dehydrogenase E1 complex (name copied from entity in Homo sapiens)
pyruvate dehydrogenase complex (name copied from entity in Homo sapiens)
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alpha-keto acid dehydrogenase E3 homodimer (name copied from entity in Homo sapiens)
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NNT dimer (name copied from entity in Homo sapiens)
IDH3 complex (name copied from entity in Homo sapiens)
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Citrate Synthase Holoenzyme (name copied from entity in Homo sapiens)
pyruvate dehydrogenase E2 trimer (name copied from entity in Homo sapiens)
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alpha-ketoglutarate dehydrogenase E2 holoenzyme (name copied from entity in Homo sapiens)
alpha-ketoglutarate dehydrogenase complex (name copied from entity in Homo sapiens)
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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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Alteration of decreased plasma NO metabolites and platelet NO synthase activity by paroxetine in depressed patients
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The mitochondrial ADP/ATP carrier: structural, physiological and
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Regulation of nitric oxide-sensitive guanylyl cyclase
Glycosaminoglycan storage disorders: a review
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The crystal structure of yeast thiamin pyrophosphokinase
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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=3650537
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Reversible ATP-dependent transition between two forms of human cytosolic thymidine kinase with different enzymatic properties
Identification, characterization, and crystal structure of the Omega class glutathione transferases
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SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs
The joys of HexNAc. The synthesis and function of N- and O-glycan branches
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GGPS1:3Mg++ (name copied from entity in Homo sapiens)
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holo-GGPS1 hexamer (name copied from entity in Homo sapiens)
FDPS:3Mg++ (name copied from entity in Homo sapiens)
holo-FDPS 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=3642791
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642790
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_31569.10
FDFT (Mg2+ cofactor) (name copied from entity in Homo sapiens)
HMGCR dimer (name copied from entity in Homo sapiens)
IDI1 or 2 (name copied from entity in Homo sapiens)
MVD dimer (name copied from entity in Homo sapiens)
2'-Deoxyinosine 5'-phosphate [ChEBI:28806]
MVK dimer (name copied from entity in Homo sapiens)
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
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_81157.9
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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_106431.9
HSD17B4 dimer (name copied from entity in Homo sapiens)
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HACL1 holoenzyme monomer (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=3642799
GNPAT:AGPS complex (name copied from entity in Homo sapiens)
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IDH1 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_28562.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651896
HMGCL dimer (name copied from entity in Homo sapiens)
ACAT1 tetramer (name copied from entity in Homo sapiens)
HACL1 tetramer (name copied from entity in Homo sapiens)
OXCT1 dimer (name copied from entity in Homo sapiens)
RNA interference suggests a primary role for monoacylglycerol lipase in the degradation of the endocannabinoid 2-arachidonoylglycerol
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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_3448.1
Metabolism of highly unsaturated n-3 and n-6 fatty acids
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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_81358.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=109966
CDIPT:Mg2+/Mn2+ (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_4318.1
PC:PITPNB (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_3852.2
MHC class I endosomal and lysosomal trafficking coincides with exogenous antigen loading in dendritic cells
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)
PCYT1A dimer (name copied from entity in Homo sapiens)
PISD:Pyruvoyl (name copied from entity in Homo sapiens)
Inorganic pyrophosphatase 2, mitochondrial
Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K
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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_107448.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642806
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_100673.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_3022.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642803
LPIN3:Mg2+ (name copied from entity in Homo sapiens)
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EPT1:Mg2+/Mn2+ (name copied from entity in Homo sapiens)
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CEPT1:Mg2+/Mn2+ (name copied from entity in Homo sapiens)
PCYT2 dimer (name copied from entity in Homo sapiens)
LPIN2: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=110291
LPIN1:Mg2+ (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=3650539
MGLL dimer (name copied from entity in Homo sapiens)
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SQLE:FAD (name copied from entity in Homo sapiens)
glyceraldehyde-3-phosphate dehydrogenase, testis-specific, monomer
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Glyceraldehyde 3-phosphate dehydrogenase, liver
glyceraldehyde-3-phosphate dehydrogenase monomer
glyceraldehyde 3-phosphate dehydrogenase, muscle
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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=3650524
A common mutation in the fibroblast growth factor receptor 1 gene in Pfeiffer syndrome
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Prolactin and ErbB4/HER4 signaling interact via Janus kinase 2 to induce mammary epithelial cell gene expression differentiation
The amino acid sequence of cytosolic aspartate aminotransferase from human liver
HPGDS dimer (name copied from entity in Homo sapiens)
LTA4H:Zn2+ (name copied from entity in Homo sapiens)
PIKFYVE:VAC14:FIG4 (name copied from entity in Homo sapiens)
ACSL1 (name copied from entity in Homo sapiens)
SPTLC1:SPTLC3 (name copied from entity in Homo sapiens)
SPTLC1:SPTLC2 (name copied from entity in Homo sapiens)
bHEXB (name copied from entity in Homo sapiens)
The E3 ligase Aip4/Itch ubiquitinates and targets ErbB-4 for degradation
5'-Phosphoribosyl-5-aminoimidazole [ChEBI:28843]
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
ARF1:GTP (name copied from entity in Homo sapiens)
Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate acyltransferase, a key enzyme in de novo triacylglycerol synthesis
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)
PIK3C3:Mn2+ (name copied from entity in Homo sapiens)
PIP4K2A:PIP4K2A (name copied from entity in Homo sapiens)
PIP4K2A:PIP4K2B (name copied from entity in Homo sapiens)
PIP4K2B:PIP4K2B (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=75165
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_88846.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5340.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642474
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642470
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642475
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642476
3'-End processing of pre-mRNA in eukaryotes.
The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase
DHFR dimer (name copied from entity in Homo sapiens)
p-PTPS hexamer (name copied from entity in Homo sapiens)
p-SPR dimer (name copied from entity in Homo sapiens)
GCH1 decamer (name copied from entity in Homo sapiens)
GCH1 dimer (name copied from entity in Homo sapiens)
AMPK gamma2:AMP (name copied from entity in Homo sapiens)
Activated AMPK heterotrimer (name copied from entity in Homo sapiens)
Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains
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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_34677.10
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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=3642505
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_112298.8
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_114215.8
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642503
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642477
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642478
AMPK heterotrimer:AMP (name copied from entity in Homo sapiens)
Functional characterization of human aquaporin 9 as a facilitative glycerol carrier
AMPK heterotrimer (inactive) (name copied from entity in Homo sapiens)
Inactive PP2A-ABdeltaC complex (name copied from entity in Homo sapiens)
COQ6 mutations in human patients produce nephrotic syndrome with sensorineural deafness
RAPGEF3:cAMP complex (name copied from entity in Homo sapiens)
RAPGEF4:cAMP Complex (name copied from entity in Homo sapiens)
ADP/ATP translocase 1 homodimer (name copied from entity in Homo sapiens)
PDSS1: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)
Protein Kinase C, alpha type: DAG (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_115285.8
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642481
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_78453.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651859
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Chromosomal localization of the gene for human glucosamine-6-sulphatase to 12q14
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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_79781.9
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PDSS1/2 tetramer (name copied from entity in Homo sapiens)
GLA 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_38459.10
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_83244.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652051
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644916
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RNA metabolism consists of both mRNA degradative pathways and non-coding RNA metabolism. Non-coding RNA metabolism includes the processing and packaging of the small nuclear ribonucleoproteins (snRNPs).
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Cdc6 is an unstable protein whose de novo synthesis in G1 is important for the onset of S phase and for preventing a 'reductional' anaphase in the budding yeast Saccharomyces cerevisiae.
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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.
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.
Once synthesized mRNA can be utilized until degraded. Degradation itself is the final mode of gene expression regulation.
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.
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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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).
ERK1c regulates Golgi fragmentation during mitosis
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.
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.
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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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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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.
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Protein Kinase C, unconventional isoforms
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Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex
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.
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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.
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Protein kinase C alpha (PKCalpha) phosphorylates HuR (ELAVL1) on serine221 and serine 158.
Protein kinase C delta (PKCdelta) phosphorylates HuR (ELAVL1) at serine 221 and serine 318.
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. 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).
Deregulated FGFR3 mutants in multiple myeloma cell lines with t(4;14): comparative analysis of Y373C, K650E and the novel G384D mutations
Butyrate response factor 1 (BRF1) binds AU-rich elements in the 3' untranslated region of mRNAs.
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.
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.
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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.
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.
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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.
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High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
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(APC/C:Cdh1)-targeted cell cycle proteins
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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.
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.
Beta-amino acids: mammalian metabolism and utility as alpha-amino acid analogues
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.
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
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).
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.
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.
PS-GAP (RGH10) interacts specifically with caspase-activated PAK-2p34 reducing the ability of PAK-2p34 to induce cell death. This interaction Â inhibits the kinase activity of Â PAK-2p34 and changes the localization of PAK-2p34 from the nucleus to the perinuclear region (Koeppel et al., 2004). Â
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Following caspase mediated cleavage, PAK-2p34 translocates to the nucleus (Jakobi et al., 2003). The interaction with PS-GAP changes the localization of PAK-2p34 from the nucleus to the perinuclear region (Koeppel et al.,2004).
Apoptosis is a distinct form of cell death that is functionally and morphologically different from necrosis. Nuclear chromatin condensation, cytoplasmic shrinking, dilated endoplasmic reticulum, and membrane blebbing characterize apoptosis in general. Mitochondria remain morphologically unchanged. In 1972 Kerr et al introduced the concept of apoptosis as a distinct form of "cell-death", and the mechanisms of various apoptotic pathways are still being revealed today. The two principal pathways of apoptosis are (1) the Bcl-2 inhibitable or intrinsic pathway induced by various forms of stress like intracellular damage, developmental cues, and external stimuli and (2) the caspase 8/10 dependent or extrinsic pathway initiated by the engagement of death receptors The caspase 8/10 dependent or extrinsic pathway is a death receptor mediated mechanism that results in the activation of caspase-8 and caspase-10. Activation of death receptors like Fas/CD95, TNFR1, and the TRAIL receptor is promoted by the TNF family of ligands including FASL (APO1L OR CD95L), TNF, LT-alpha, LT-beta, CD40L, LIGHT, RANKL, BLYS/BAFF, and APO2L/TRAIL. These ligands are released in response to microbial infection, or as part of the cellular, humoral immunity responses during the formation of lymphoid organs, activation of dendritic cells, stimulation or survival of T, B, and natural killer (NK) cells, cytotoxic response to viral infection or oncogenic transformation. The Bcl-2 inhibitable or intrinsic pathway of apoptosis is a stress-inducible process, and acts through the activation of caspase-9 via Apaf-1 and cytochrome c. The rupture of the mitochondrial membrane, a rapid process involving some of the Bcl-2 family proteins, releases these molecules into the cytoplasm. Examples of cellular processes that may induce the intrinsic pathway in response to various damage signals include: auto reactivity in lymphocytes, cytokine deprivation, calcium flux or cellular damage by cytotoxic drugs like taxol, deprivation of nutrients like glucose and growth factors like EGF, anoikis, transactivation of target genes by tumor suppressors including p53. In many non-immune cells, death signals initiated by the extrinsic pathway are amplified by connections to the intrinsic pathway. The connecting link appears to be the truncated BID (tBID) protein a proteolytic cleavage product mediated by caspase-8 or other enzymes.
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A regulated balance between cell survival and apoptosis is essential for normal development and homeostasis of multicellular organisms (see Matsuzawa, 2001). Defects in control of this balance may contribute to autoimmune disease, neurodegeneration and cancer. Protein ubiquitination and degradation is one of the major mechanisms that regulate apoptotic cell death (reviewed in Yang and Yu 2003).
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Adenoviral expression of the BAP31 cleavage product, p20 causes early release of Ca2+ from the ER, concomitant uptake of Ca2+ into mitochondria, and recruitment of Drp1 to the mitochondria (Breckenridge et al., 2003) . Drp1 mediates scission of the outer mitochondrial membrane, resulting in dramatic fragmentation and fission of the mitochondrial network .
Proteolytic cleavage of the COOH-terminal domain of Mst3 by caspases promotes nuclear translocation of the catalytic domain (Huang et al., 2002).
Activity and genomic organization of human glucose transporter 9 (GLUT9), a novel member of the family of sugar-transport facilitators predominantly expressed in brain and leucocytes
In the execution phase of apoptosis, effector caspases cleave vital cellular proteins leading to the morphological changes that characterize apoptosis. These changes include destruction of the nucleus and other organelles, DNA fragmentation, chromatin condensation, cell shrinkage and cell detachment and membrane blebbing (reviewed in Fischer et al., 2003).
Proteolytically activated PAK-2p34, but not full-length PAK-2, is degraded rapidly by the proteasome (Jakobi et al., 2003). Here, degradation of PAK-2p34 is described as occurring in the cytosol. However, to date it is not known whether this occurs in the nucleus or in the cytoplasm.
Stimulation of cell death by PAK-2 requires the generation and stabilization of the caspase-activated form, PAK-2p34 (Walter et al., 1998;Jakobi et al., 2003). Levels of proteolytically activated PAK-2p34 protein are controlled by ubiquitin-mediated proteolysis. PAK-2p34 but not full-length PAK-2 is degraded by the 26 S proteasome (Jakobi et al., 2003). It is not known whether ubiquitination and degradation of PAK-2p34 occurs in the cytoplasm or in the nucleus.
Murine PS-GAP interacts specifically with caspase-activated PAK-2p34, but not active or inactive full-length PAK-2, through a region between the GAP and SH3 domains (Koeppel et al.,2004). Evidence for this reaction comes from experiments using both mouse and rabbit proteins.
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IMP (inosine monophosphate) dehydrogenase 1 tetramer (name copied from entity in Homo sapiens)
PPAT tetramer (name copied from entity in Homo sapiens)
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.
ATIC dimer (name copied from entity in Homo sapiens)
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).
adenylosuccinate synthetase holoenzyme dimer (name copied from entity in Homo sapiens)
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.
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.
adenylosuccinate synthetase like 1 holoenzyme dimer (name copied from entity in Homo sapiens)
Release of phospho-IRS from the insulin receptor triggers a cascade of signalling events via PI3K, SOS, RAF and the MAP kinases.
adenylosuccinate synthetase like 1 holoenzyme (name copied from entity in Homo sapiens)
The in vitro replication of DNA containing the SV40 origin.
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]'.
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'.
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.
ETF (reduced) (name copied from entity in Homo sapiens)
PPAT dimer (name copied from entity in Homo sapiens)
ETF (name copied from entity in Homo sapiens)
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M-phase inducer phosphatase 2 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25B)
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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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Human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A synthase: expression, purification, and characterization of recombinant wild-type and Cys129 mutant enzymes
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AMPD2 tetramer (name copied from entity in Homo sapiens)
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.
AMPD3 tetramer (name copied from entity in Homo sapiens)
ADAL:Zn (name copied from entity in Homo sapiens)
APRT homodimer (name copied from entity in Homo sapiens)
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.
HGPRT homotetramer (name copied from entity in Homo sapiens)
NT5C2 tetramer (name copied from entity in Homo sapiens)
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.
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).
At the beginning of this reaction, 2 molecules of 'ATP', and 1 molecule of 'eIF4E:4E-BP' are present. At the end of this reaction, 1 molecule of 'eIF4E:4E-BP1-P', and 2 molecules of 'ADP' are present. This reaction is mediated by the 'kinase activity' of 'Activated mTORC1'.
Raptor recruits mTOR to non-phosphorylated 4E-BP1 bound to eIF4E and positively modulates phosphorylation of 4E-BP1 by mTOR. 4E-BP1 is further phosphorylated on multiple sites by other unknown kinases, also contributing to the dissociation of 4E-BP1 from eIF4E. Thus mTORC1 relieves the inhibitory effect of 4E-BP1 on eIF4E dependent translation initiation (PMIDs 15755954, 10872469, 11297505, 12150926 and 15809305).
At the beginning of this reaction, 1 molecule of 'eIF4E:4E-BP1-P' is present. At the end of this reaction, 1 molecule of '4E-BP1-P', and 1 molecule of 'eIF4E' are present. This reaction takes place in the 'cytosol'.
adenylosuccinate synthetase holoenzyme (name copied from entity in Homo sapiens)
adenosine kinase holoenzyme (name copied from entity in Homo sapiens)
AMPD1 tetramer (name copied from entity in Homo sapiens)
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M-phase inducer phosphatase 3 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25C)
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Thematic Review Series: Proteomics. An integrated omics analysis of eicosanoid biology
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S6K1 contains a TOS motif. mTORC1 requires an intact TOS motif to bind and phosphorylate S6K1 (PMID 15809305).
mTOR forms a functional protein complex with at least two proteins: Raptor (Regulated Associated Protein of mTOR) and mLst8. This complex is called mammalian TOR complex 1 (mTORC1). Raptor serves as a scaffolding protein to bridge the interaction between mTOR and its substrates. mLst8 enhances the association of mTOR with Raptor. [Rheb:GTP] binds and activates mTORC1. Besides binding directly to mTOR, Rheb can also bind to Raptor and mLst8 (PMIDs 15854902, 15755954 and 12150926).
Rheb is a GTP binding protein that exhibits GTPase activity. GDP is exchanged for GTP in the [Rheb:GDP] complex to form [Rheb:GTP], which binds and activates the mTORC1 complex. This exchange is catalysed by an as yet unidentified guanine exchange factor (GEF) (PMIDs 15951850 and 15755954).
The 22 members of the fibroblast growth factor (FGF) family of growth factors mediate their cellular responses by binding to and activating the different isoforms encoded by the four receptor tyrosine kinases (RTKs) designated FGFR1, FGFR2, FGFR3 and FGFR4. These receptors are key regulators of several developmental processes in which cell fate and differentiation to various tissue lineages are determined. Unlike other growth factors, FGFs act in concert with heparin or heparan sulfate proteoglycan (HSPG) to activate FGFRs and to induce the pleiotropic responses that lead to the variety of cellular responses induced by this large family of growth factors. An alternative, FGF-independent, source of FGFR activation originates from the interaction with cell adhesion molecules, typically in the context of interactions on neural cell membranes and is crucial for neuronal survival and development. Upon ligand binding, receptor dimers are formed and their intrinsic tyrosine kinase is activated causing phosphorylation of multiple tyrosine residues on the receptors. These then serve as docking sites for the recruitment of SH2 (src homology-2) or PTB (phosphotyrosine binding) domains of adaptors, docking proteins or signaling enzymes. Signaling complexes are assembled and recruited to the active receptors resulting in a cascade of phosphorylation events. This leads to stimulation of intracellular signaling pathways that control cell proliferation, cell differentiation, cell migration, cell survival and cell shape, depending on the cell type or stage of maturation.
Quantitating protein synthesis, degradation, and endogenous antigen processing
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).
Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase: the importance of potassium and chloride ions for its structure and function
Signaling via FGFRs is mediated via direct recruitment of signaling proteins that bind to tyrosine auto-phosphorylation sites on the activated receptor and via closely linked docking proteins that become tyrosine phosphorylated in response to FGF-stimulation and form a complex with additional complement of signaling proteins. The activation loop in the catalytic domain of FGFR maintains the PTK domain in an inactive or low activity state. The activation-loop of FGFR1, for instance, contains two tyrosine residues that must be autophosphorylated for maintaining the catalytic domain in an active state. In the autoinhibited configuration, a kinase invariant proline residue at the C-terminal end of the activation loop interferes with substrate binding while allowing access to ATP in the nucleotide binding site. In addition to the catalytic PTK core, the cytoplasmic domain of FGFR contains several regulatory sequences. The juxtamembrane domain of FGFRs is considerably longer than that of other receptor tyrosine kinases. This region contains a highly conserved sequence that serves as a binding site for the phosphotyrosine binding (PTB) domain of FRS2. A variety of signaling proteins are phosphorylated in response to FGF stimulation, including Shc, phospholipase-C gamma and FRS2 leading to stimulation of intracellular signaling pathways that control cell proliferation, cell differentiation, cell migration, cell survival and cell shape.
The ability of growth factors to protect from apoptosis is primarily due to the activation of the AKT survival pathway. P-I-3-kinase dependent activation of PDK leads to the activation of AKT which in turn affects the activity or expression of pro-apoptotic factors, which contribute to protection from apoptosis. AKT activation also blocks the activity of GSK-3b which could lead to additional antiapoptotic signals.
Phospholipase C-gamma (PLC-gamma) is a substrate of the fibroblast growth factor receptor (FGFR) and other receptors with tyrosine kinase activity. It is known that the src homology region 2 (SH2 domain) of PLC-gamma and of other signaling molecules (such as GTPase-activating protein and phosphatidylinositol 3-kinase-associated p85) direct their binding toward autophosphorylated tyrosine residues of the FGFR. Recruitment of PLC-gamma results in its phosphorylation and activation by the receptor. Activated PLC-gamma hydrolyzes phosphatidyl inositol[4,5] P2 to form the second messengers diacylglycerol (DAG) and Ins [1,4,5]P3, which stimulate calcium release and activation of calcium/calmodulin dependent kinases.
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Sister chromatid cohesion protein PDS5 homolog A
Sister chromatid cohesion protein PDS5 homolog B
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Structural maintenance of chromosomes protein 3
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Slo3 represents a new and unique type of potassium channel regulated by intracellular pH. Slo3 is sperm specific and controls membrane potential. Incapacitated murine spermatozoa hyperpolarize to approximately 60 mV during capacitation, an effect attributed to an increase in K+ permeability. KSper (potassium transport in sperm) is the dominant, if not the only, K+ selective channel in mouse epididymal spermatozoa.
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At the center of the mammalian circadian clock is a negative transcription/translation-based feedback loop: The BMAL1:CLOCK/NPAS2 heterodimer transactivates CRY and PER genes by binding E-box elements in their promoters; the CRY and PER proteins then inhibit transactivation by BMAL1:CLOCK/NPAS2. BMAL1:CLOCK/NPAS2 activates transcription of CRY, PER, and several other genes in the morning. Levels of PER and CRY proteins rise during the day and inhibit expression of CRY, PER, and other BMAL1:CLOCK/NPAS2-activated genes in the afternoon and evening. During the night CRY and PER proteins are targeted for degradation by phosphorylation and polyubiquitination, allowing the cycle to commence again in the morning. Transcription of the BMAL1 (ARNTL) gene is controlled by ROR-alpha and REV-ERBA, both of which are targets of BMAL1:CLOCK/NPAS2 in mice and both of which compete for the same element (RORE) in the BMAL1 promoter. ROR-alpha activates transcription of BMAL1; REV-ERBA represses transcription of BMAL1. This mutual control forms a secondary, reinforcing loop of the circadian clock. REV-ERBA shows strong circadian rhythmicity and confers circadian expression on BMAL1. BMAL1 can form heterodimers with either CLOCK or NPAS2, which act redundantly but show different tissue specificity. The BMAL1:CLOCK and BMAL1:NPAS2 heterodimers activate a set of genes that possess E-box elements (consensus CACGTG) in their promoters. This confers circadian expression on the genes. The PER genes (PER1, PER2, PER3) and CRY genes (CRY1, CRY2) are among those activated by BMAL1:CLOCK and BMAL1:NPAS2. PER and CRY mRNA accumulates during the morning and the proteins accumulate during the afternoon. PER and CRY proteins form complexes in the cytosol and these are bound by either CSNK1D or CSNK1E kinases which phosphorylate PER and CRY. The phosphorylated PER:CRY:kinase complex is translocated into the nucleus due to the nuclear localization signal of PER and CRY. Within the nucleus the PER:CRY complexes bind BMAL1:CLOCK and BMAL1:NPAS2, inhibiting their transactivation activity and their phosphorylation. This reduces expression of the target genes of BMAL1:CLOCK and BMAL1:NPAS2 during the afternoon and evening. PER:CRY complexes also traffic out of the nucleus into the cytosol due to the nuclear export signal of PER. During the night PER:CRY complexes are polyubiquitinated and degraded, allowing the cycle to begin again. Phosphorylated PER is bound by Beta-TrCP1, a cytosolic F-box type component of some SCF E3 ubiquitin ligases. CRY is bound by FBXL3, a nucleoplasmic F-box type component of some SCF E3 ubiquitin ligases. Phosphorylation of CRY1 by Adenosine monophosphate-activated kinase (AMPK) enhances degradation of CRY1. PER and CRY are subsequently polyubiquitinated and proteolyzed by the 26S proteasome. The circadian clock is cell-autonomous and some, but not all cells of the body exhibit circadian rhythms in metabolism, cell division, and gene transcription. The suprachiasmatic nucleus (SCN) in the hypothalamus is the major clock in the body and receives its major input from light (via retinal neurons) and a minor input from nutrient intake. The SCN and other brain tissues determine waking and feeding cycles and influence the clocks in other tissues by hormone secretion and nervous stimulation. Independently of the SCN, other tissues such as liver receive inputs from signals from the brain and from nutrients.
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Mammalian fertilization comprises sperm migration through the female reproductive tract, biochemical and morphological changes to sperm, and sperm-egg interaction in the oviduct. Although the broad concepts of fertilization are well defined, our understanding of the biochemical mechanisms underlying sperm-egg binding is limited.
A series of receptor signaling pathways potentially govern chemical communication between sperm and egg, chemotactically guiding incoming sperm towards the oocyte. Though several substances are confirmed as sperm chemoattractant, progesterone (P) seems to be the best chemoattractant candidate for human sperm. Ion channels control the sperm ability to fertilize the egg by regulating sperm maturation in the female reproductive tract and by triggering key sperm physiological responses required for successful fertilization such as hyperactivated motility, chemotaxis, and the acrosome reaction. CatSper, a pH regulated, calcium selective ion channel, potassium channel KSper (Slo3), and Hv1, the voltage gated proton channel are involved in regulation of sperm hyperactivated motility. While progesterone, secreted by ovulated cumulus oophorus, may act as a chemoattractant for sperm cells over the short distances, a major determinant of sperm guidance over long distances in the mammalian female reproductive tract is rheotaxis.
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ATP binding/hydrolysis by and phosphorylation of peroxisomal ATP-binding cassette proteins PMP70 (ABCD3) and adrenoleukodystrophy protein (ABCD1)
Activated epidermal growth factor receptors (EGFR) can stimulate phosphatidylinositol (PI) turnover. Activated EGFR can activate phospholipase C-gamma1 (PLC-gamma1, i.e. PLCG1) which hydrolyses phosphatidylinositol 4,5-bisphosphate (PIP2) to inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG). IP3 is instrumental in the release of calcium from intracellular stores and DAG is involved in protein kinase C activation.
Human reproduction mixes the genomes of two individuals creating a new organism. The offspring individuals produced by sexual reproduction differ from their parents and from their siblings. Reproduction includes the reproductive system, sperm and egg production (haploid cells), fertilization, and the early stages embryo development.
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The epidermal growth factor receptor (EGFR) is one member of the ERBB family of transmembrane glycoprotein tyrosine receptor kinases (RTK). Binding of EGFR to its ligands induces conformational change that unmasks the dimerization interface in the extracellular domain of EGFR, leading to receptor homo- or heterodimerization at the cell surface. Dimerization of the extracellular regions of EGFR triggers additional conformational change of the cytoplasmic EGFR regions, enabling the kinase domains of two EGFR molecules to achieve the catalytically active conformation. Ligand activated EGFR dimers trans-autophosphorylate on tyrosine residues in the cytoplasmic tail of the receptor. Phosphorylated tyrosines serve as binding sites for the recruitment of signal transducers and activators of intracellular substrates, which then stimulate intracellular signal transduction cascades that are involved in regulating cellular proliferation, differentiation, and survival. Recruitment of complexes containing GRB2 and SOS1 to phosphorylated EGFR dimers either directly, through phosphotyrosine residues that serve as GRB2 docking sites, or indirectly, through SHC1 recruitment, promotes GDP to GTP exchange on RAS, resulting in the activation of RAF/MAP kinase cascade. Binding of complexes of GRB2 and GAB1 to phosphorylated EGFR dimers leads to formation of the active PI3K complex, conversion of PIP2 into PIP3, and activation of AKT signaling. Phospholipase C-gamma1 (PLCG1) can also be recruited directly, through EGFR phosphotyrosine residues that serve as PLCG1 docking sites, which leads to PLCG1 phosphorylation by EGFR and activation of DAG and IP3 signaling. EGFR signaling is downregulated by the action of ubiquitin ligase CBL. CBL binds directly to the phosphorylated EGFR dimer through the phosphotyrosine Y1045 in the C-tail of EGFR, and after CBL is phosphorylated by EGFR, it becomes active and ubiquitinates phosphorylated EGFR dimers, targeting them for degradation. For a recent review of EGFR signaling, please refer to Avraham and Yarden, 2011.
GAB1 is recruited to the activated EGFR indirectly, through GRB2. GAB1 acts as an adaptor protein that enables formation of an active PIK3, through recruitment of PIK3 regulatory subunit PIK3R1 (also known as PI3Kp85), which subsequently recruits PIK3 catalytic subunit PIK3CA (also known as PI3Kp110). PIK3, in complex with EGFR, GRB2 and GAB1, catalyzes phosphorylation of PIP2 and its conversion to PIP3, which leads to the activation of the AKT signaling.
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MHC molecules and microbial antigen processing in phagosomes
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Glucose and cAMP regulate the L-type pyruvate kinase gene by phosphorylation/dephosphorylation of the carbohydrate response element binding protein
As inferred from mouse, BMAL1:CLOCK and BMAL1:NPAS2 heterodimers bind to sequence elements (E boxes) in the promoters of target genes and enhance transcription (Gekakis et al. 1998, reviewed in Munoz and Baler 2003).
The NOCTURNIN gene is transcribed to yield mRNA and the mRNA is translated to yield protein. The NOCTURNIN gene shows circadian expression because the BMAL1:CLOCK heterodimer binds an E-box element in the NOCTURNIN promoter and activates transcription.
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Purification and properties of beta-hydroxyisobutyric dehydrogenase
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Mitochondrial ATP-binding cassette proteins
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AU binding proteins recruit the exosome to degrade ARE-containing mRNAs
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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.
Large-scale proteomic analysis of the human spliceosome.
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.
Stem cell factor (SCF) is a growth factor with membrane bound and soluble forms. It is expressed by fibroblasts and endothelial cells throughout the body, promoting proliferation, migration, survival and differentiation of hematopoetic progenitors, melanocytes and germ cells.(Linnekin 1999, Rönnstrand 2004, Lennartsson and Rönnstrand 2006). The receptor for SCF is KIT, a tyrosine kinase receptor (RTK) closely related to the receptors for platelet derived growth factor receptor, colony stimulating factor 1 (Linnekin 1999) and Flt3 (Rosnet et al. 1991). Four isoforms of c-Kit have been identified in humans. Alternative splicing results in isoforms of KIT differing in the presence or absence of four residues (GNNK) in the extracellular region. This occurs due to the use of an alternate 5' splice donor site. These GNNK+ and GNNK- variants are co-expressed in most tissues; the GNNK- form predominates and was more strongly tyrosine-phosphorylated and more rapidly internalized (Rönnstrand 2004). There are also splice variants that arise from alternative usage of splice acceptor site resulting in the presence or absence of a serine residue (Crosier et al., 1993). Finally, there is an alternative shorter transcript of KIT expressed in postmeiotic germ cells in the testis which encodes a truncated KIT consisting only of the second part of the kinase domain and thus lackig the extracellular and transmembrane domains as well as the first part of the kinase domain (Rossi et al. 1991). Binding of SCF homodimers to KIT results in KIT homodimerization followed by activation of its intrinsic tyrosine kinase activity. KIT stimulation activates a wide array of signalling pathways including MAPK, PI3K and JAK/STAT (Reber et al. 2006, Rönnstrand 2004). Defects of KIT in humans are associated with different genetic diseases and also in several types of cancers like mast cell leukaemia, germ cell tumours, certain subtypes of malignant melanoma and gastrointestinal tumours.
ERBB2:ERBB3 and ERBB2:ERBB4cyt1 heterodimers activate PI3K signaling by direct binding of PI3K regulatory subunit p85 (Yang et al. 2007, Cohen et al. 1996, Kaushansky et al. 2008) to phosphorylated tyrosine residues in the C-tail of ERBB3 (Y1054, Y1197, Y1222, Y1224, Y1276 and Y1289) and ERBB4 CYT1 isoforms (Y1056 in JM-A CYT1 isoform and Y1046 in JM-B CYT1 isoform). Regulatory subunit p85 subsequently recruits catalytic subunit p110 of PI3K, resulting in the formation of active PI3K, conversion of PIP2 to PIP3, and PIP3-mediated activation of AKT signaling (Junttila et al. 2009, Kainulainen et al. 2000). Heterodimers of ERBB2 and EGFR recruit PI3K indirectly, through GRB2:GAB1 complex (Jackson et al. 2004), which again leads to PIP3-mediated activation of AKT signaling.
Activation of PLCG1 signaling is observed only in the presence of ERBB2:EGFR heterodimers, with PLCG1 binding to phosphorylated tyrosine Y992 and Y1173 in the C-tail of EGFR (Chattopadhyay et al. 1999), and potentially Y1023 in the C-tail of ERBB2 (Fazioli et al. 1991, Cohen et al. 1996).
RNF41 is able to self-ubiquitinate, which keeps its levels low when ERBB3 is unstimulated.
Level of plasma membrane ERBB3 is regulated by E3 ubiquitin ligase RNF41 (also known as NRDP1), which binds and ubiquitinates both inactive and activated ERBB3, targeting it for degradation (Cao et al. 2007). RNF41 is subject to self-ubiquitination which keeps its levels low when ERBB3 is not stimulated, and preserves ERBB3 expression on the cell surface (Qiu et al. 2002). Self-ubiquitination of RNF41 is reversible, through the action of ubiquitin protease USP8, an enzyme stabilized by AKT-mediated phosphorylation. Therefore, activation of AKT by ERBB2:ERBB3 signaling leads to phosphorylation of USP8 (Cao et al. 2007), which increases level of RNF41 through deubiquitination, and results in degradation of activated ERBB3 (Cao et al. 2007) - a negative feedback loop of ERBB3 signaling. Downregulation of EGFR and ERBB4 signaling is explained in pathways Signaling by EGFR and Signaling by ERBB4.
ERBB2, also known as HER2 or NEU, is a receptor tyrosine kinase (RTK) belonging to the EGFR family. ERBB2 possesses an extracellular domain that does not bind any known ligand, contrary to other EGFR family members, a single transmembrane domain, and an intracellular domain consisting of an active kinase and a C-tail with multiple tyrosine phosphorylation sites. Inactive ERBB2 is associated with a chaperone heat shock protein 90 (HSP90) and its co-chaperone CDC37 (Xu et al. 2001, Citri et al. 2004, Xu et al. 2005). In addition, ERBB2 is associated with ERBB2IP (also known as ERBIN or LAP2), a protein responsible for proper localization of ERBB2. In epithelial cells, ERBB2IP restricts expression of ERBB2 to basolateral plasma membrane regions (Borg et al. 2000). ERBB2 becomes activated by forming a heterodimer with another ligand-activated EGFR family member, either EGFR, ERBB3 or ERBB4, which is accompanied by dissociation of chaperoning proteins HSP90 and CDC37 (Citri et al. 2004), as well as ERBB2IP (Borg et al. 2000) from ERBB2. ERBB2 heterodimers function to promote cell proliferation, cell survival and differentiation, depending on the cellular context. ERBB2 can also be activated by homodimerization when it is overexpressed, in cancer for example. In cells expressing both ERBB2 and EGFR, EGF stimulation of EGFR leads to formation of both ERBB2:EGFR heterodimers (Wada et al. 1990, Karunagaran et al. 1996) and EGFR homodimers. Heterodimers of ERBB2 and EGFR trans-autophosphorylate on twelve tyrosine residues, six in the C-tail of EGFR and six in the C-tail of ERBB2 - Y1023, Y1139, Y1196, Y1221, Y1222 and Y1248 (Margolis et al. 1989, Hazan et al. 1990,Walton et al. 1990, Helin et al. 1991, Ricci et al. 1995, Pinkas-Kramarski 1996). Phosphorylated tyrosine residues in the C-tail of EGFR and ERBB2 serve as docking sites for downstream signaling molecules. Three key signaling pathways activated by ERBB2:EGFR heterodimers are RAF/MAP kinase cascade, PI3K-induced AKT signaling, and signaling by phospholipase C gamma (PLCG1). Downregulation of EGFR signaling is mediated by ubiquitin ligase CBL, and is shown under Signaling by EGFR. In cells expressing ERBB2 and ERBB3, ERBB3 activated by neuregulin NRG1 or NRG2 binding (Tzahar et al. 1994) forms a heterodimer with ERBB2 (Pinkas-Kramarski et al. 1996, Citri et al. 2004). ERBB3 is the only EGFR family member with no kinase activity, and can only function in heterodimers, with ERBB2 being its preferred heterodimerization partner. After heterodimerization, ERBB2 phosphorylates ten tyrosine residues in the C-tail of ERBB3, Y1054, Y1197, Y1199, Y1222, Y1224, Y1260, Y1262, Y1276, Y1289 and Y1328 (Prigent et al. 1994, Pinkas-Kramarski et al. 1996, Vijapurkar et al. 2003, Li et al. 2007) that subsequently serve as docking sites for downstream signaling molecules, resulting in activation of PI3K-induced AKT signaling and RAF/MAP kinase cascade. Signaling by ERBB3 is downregulated by the action of RNF41 ubiquitin ligase, also known as NRDP1. In cells expressing ERBB2 and ERBB4, ligand stimulated ERBB4 can either homodimerize or form heterodimers with ERBB2 (Li et al. 2007), resulting in trans-autophosphorylation of ERBB2 and ERBB4 on C-tail tyrosine residues that will subsequently serve as docking sites for downstream signaling molecules, leading to activation of RAF/MAP kinase cascade and, in the case of ERBB4 CYT1 isoforms, PI3K-induced AKT signaling (Hazan et al. 1990, Cohen et al. 1996, Li et al. 2007, Kaushansky et al. 2008). Signaling by ERBB4 is downregulated by the action of WWP1 and ITCH ubiquitin ligases, and is shown under Signaling by ERBB4.
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The CYT1 isoforms of ERBB4 possess a C-tail tyrosine residue that, upon trans-autophosphorylation, serves as a docking site for the p85 alpha subunit of PI3K - PIK3R1 (Kaushansky et al. 2008, Cohen et al. 1996). Binding of PIK3R1 to CYT1 isoforms of ERBB4 is followed by recruitment of the p110 catalytic subunit of PI3K (PIK3CA), leading to assembly of an active PI3K complex that converts PIP2 to PIP3 and activates AKT signaling (Kainulainen et al. 2000).
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ERBB4, also known as HER4, belongs to the ERBB family of receptors, which also includes ERBB1 (EGFR i.e. HER1), ERBB2 (HER2 i.e. NEU) and ERBB3 (HER3). Similar to EGFR, ERBB4 has an extracellular ligand binding domain, a single transmembrane domain and a cytoplasmic domain which contains an active tyrosine kinase and a C-tail with multiple phosphorylation sites. At least three and possibly four splicing isoforms of ERBB4 exist that differ in their C-tail and/or the extracellular juxtamembrane regions: ERBB4 JM-A CYT1, ERBB4 JM-A CYT2 and ERBB4 JM-B CYT1 (the existence of ERBB4 JM-B CYT2 has not been confirmed). ERBB4 becomes activated by binding one of its seven ligands, three of which, HB-EGF, epiregulin EPR and betacellulin BTC, are EGF-like (Elenius et al. 1997, Riese et al. 1998), while four, NRG1, NRG2, NRG3 and NRG4, belong to the neuregulin family (Tzahar et al. 1994, Carraway et al. 1997, Zhang et al. 1997, Hayes et al. 2007). Upon ligand binding, ERBB4 forms homodimers (Sweeney et al. 2000) or it heterodimerizes with ERBB2 (Li et al. 2007). Dimers of ERBB4 undergo trans-autophosphorylation on tyrosine residues in the C-tail (Cohen et al. 1996, Kaushansky et al. 2008, Hazan et al. 1990, Li et al. 2007), triggering downstream signaling cascades. The pathway Signaling by ERBB4 only shows signaling by ERBB4 homodimers. Signaling by heterodimers of ERBB4 and ERBB2 is shown in the pathway Signaling by ERBB2. Ligand-stimulated ERBB4 is also able to form heterodimers with ligand-stimulated EGFR (Cohen et al. 1996) and ligand-stimulated ERBB3 (Riese et al. 1995). Dimers of ERBB4 with EGFR and dimers of ERBB4 with ERBB3 were demonstrated in mouse cell lines in which human ERBB4 and EGFR or ERBB3 were exogenously expressed. These heterodimers undergo trans-autophosphorylation, but their downstream signaling and physiological significance have not been studied. All splicing isoforms of ERBB4 possess two tyrosine residues in the C-tail that serve as docking sites for SHC1 (Kaushansky et al. 2008, Pinkas-Kramarski et al. 1996, Cohen et al. 1996). Once bound to ERBB4, SHC1 becomes phosphorylated on tyrosine residues by the tyrosine kinase activity of ERBB4, which enables it to recruit the complex of GRB2 and SOS1, resulting in the guanyl-nucleotide exchange on RAS and activation of RAF and MAP kinase cascade (Kainulainen et al. 2000). The CYT1 isoforms of ERBB4 also possess a C-tail tyrosine residue that, upon trans-autophosphorylation, serves as a docking site for the p85 alpha subunit of PI3K (Kaushansky et al. 2008, Cohen et al. 1996), leading to assembly of an active PI3K complex that converts PIP2 to PIP3 and activates AKT signaling (Kainulainen et al. 2000). Besides signaling as a transmembrane receptor, ligand activated homodimers of ERBB4 JM-A isoforms (ERBB4 JM-A CYT1 and ERBB4 JM-A CYT2) undergo proteolytic cleavage by ADAM17 (TACE) in the juxtamembrane region, resulting in shedding of the extracellular domain and formation of an 80 kDa membrane bound ERBB4 fragment known as ERBB4 m80 (Rio et al. 2000, Cheng et al. 2003). ERBB4 m80 undergoes further proteolytic cleavage, mediated by the gamma-secretase complex, which releases the soluble 80 kDa ERBB4 intracellular domain, known as ERBB4 s80 or E4ICD, into the cytosol (Ni et al. 2001). ERBB4 s80 is able to translocate to the nucleus, promote nuclear translocation of various transcription factors, and act as a transcription co-factor. In neuronal precursors, ERBB4 s80 binds the complex of TAB and NCOR1, helps to move the complex into the nucleus, and is a co-factor of TAB:NCOR1-mediated inhibition of expression of astrocyte differentiation genes GFAP and S100B (Sardi et al. 2006). In mammary cells, ERBB4 s80 recruits STAT5A transcription factor in the cytosol, shuttles it to the nucleus, and acts as the STAT5A co-factor in binding to and promoting transcription from the beta-casein (CSN2) promoter, and may be involved in the regulation of other lactation-related genes (Williams et al. 2004, Muraoka-Cook et al. 2008). ERBB4 s80 was also shown to bind activated estrogen receptor in the nucleus and act as its transcriptional co-factor in promoting transcription of some estrogen-regulated genes, such as progesterone receptor gene NR3C3 and CXCL12 i.e. SDF1 (Zhu et al. 2006). The C-tail of ERBB4 possesses several WW-domain binding motifs (three in CYT1 isoform and two in CYT2 isoform), which enable interaction of ERBB4 with WW-domain containing proteins. ERBB4 s80, through WW-domain binding motifs, interacts with YAP1 transcription factor, a known proto-oncogene, and may be a co-regulator of YAP1-mediated transcription (Komuro et al. 2003, Omerovic et al. 2004). The tumor suppressor WWOX, another WW-domain containing protein, competes with YAP1 in binding to ERBB4 s80 and prevents translocation of ERBB4 s80 to the nucleus (Aqeilan et al. 2005). ERBB4 s80 is also able to translocate to the mitochondrial matrix, presumably when its nuclear translocation is inhibited. Once in the mitochondrion, the BH3 domain of ERBB4, characteristic of BCL2 family members, may enable it to act as a pro-apoptotic factor (Naresh et al. 2006). Activation of ERBB4 in breast cancer cell lines leads to JNK-dependent increase in BRCA1 mRNA level and mitotic cell cycle delay, but the exact mechanism has not been elucidated (Muraoka-Cook et al. 2006). WW-domain binding motifs in the C-tail of ERBB4 play an important role in the downregulation of ERBB4 receptor signaling, enabling the interaction of intact ERBB4, ERBB4 m80 and ERBB4 s80 with NEDD4 family of E3 ubiquitin ligases WWP1 and ITCH. The interaction of WWP1 and ITCH with intact ERBB4 is independent of receptor activation and autophosphorylation. Binding of WWP1 and ITCH ubiquitin ligases leads to ubiquitination of ERBB4 and its cleavage products, and subsequent degradation through both proteasomal and lysosomal routes (Omerovic et al. 2007, Feng et al. 2009). In addition, the s80 cleavage product of ERBB4 JM-A CYT-1 isoform is the target of NEDD4 ubiquitin ligase. NEDD4 binds ERBB4 JM-A CYT-1 s80 (ERBB4jmAcyt1s80) through its PIK3R1 interaction site and mediates ERBB4jmAcyt1s80 ubiquitination, thereby decreasing the amount of ERBB4jmAcyt1s80 that reaches the nucleus (Zeng et al. 2009).
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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 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.
Following NGF binding, p75NTR activates the RAC (Ras-related C3 botulinum toxin substrate) GTPase.
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.
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.
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.
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.
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.
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.
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.
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.
Exon-intron organization and chromosomal localization of the mouse monoglyceride lipase gene
Frequent translocation t(4;14)(p16.3;q32.3) in multiple myeloma is associated with increased expression and activating mutations of fibroblast growth factor receptor 3
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
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Activity of TKI258 against primary cells and cell lines with FGFR1 fusion genes associated with the 8p11 myeloproliferative syndrome
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Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
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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_104075.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_11817.2
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=197969
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644956
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_79824.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644958
The NLRP3 inflammasome: a sensor of immune danger signals
Multidrug resistance-associated protein 4
Molecular basis of hereditary fructose intolerance: mutations and polymorphisms in the human aldolase B gene
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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_7545.3
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=3645235
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_78397.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=200671
f-actin (ADP) (name copied from entity in Homo sapiens)
Beta-oxidation of very long 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=3646968
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644276
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
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Coatomer:Arf1-GTP:GAP Lattice (name copied from entity in Homo sapiens)
Coatomer:GAP Lattice (name copied from entity in Homo sapiens)
Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control
Coatomer:ARFGAP1 lattice (name copied from entity in Homo sapiens)
Coatomer:Arf1-GDP:GAP Lattice (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=3640117
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=75808
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640140
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_96434.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651831
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_81637.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651898
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_100297.9
The Polo-like kinase Plx1 interacts with and inhibits Myt1 after fertilization of Xenopus eggs
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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=3642831
Chromosome condensation by a human condensin complex in Xenopus egg extracts
LASS5 is a bona fide dihydroceramide synthase that selectively utilizes palmitoyl-CoA as acyl donor
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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_33715.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3639821
Na+/Ca2+-K+ exchangers (NCKX): functional properties and physiological roles
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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=3640047
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643832
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643830
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651195
Transcriptional Regulation of White Adipocyte Differentiation
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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=3640123
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644034
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3639865
Phosphorylation of cofilin by LIM-kinase is necessary for semaphorin 3A-induced growth cone collapse
'RAB8A/10/13/14:GTP (name copied from entity in Homo sapiens) [cytoplasmic vesicle membrane]' positively regulates 'Translocation of GLUT4 Vesicle and Docking at the Plasma Membrane'
'RAC1:GTP (name copied from entity in Homo sapiens) [plasma membrane]' positively regulates 'Translocation of GLUT4 Vesicle and Docking at the Plasma Membrane'
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A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP
'TBC1D4 [cytoplasmic vesicle membrane]' positively regulates 'RAB8A/10/13/14 Hydrolyze GTP'
'TC10:GTP (name copied from entity in Homo sapiens) [plasma membrane]' positively regulates 'Translocation of GLUT4 Vesicle and Docking at the Plasma Membrane'
'TBC1D1 [cytoplasmic vesicle membrane]' positively regulates 'RAB8A/10/13/14 Hydrolyze GTP'
Molecular mechanisms regulating hormone-sensitive lipase and lipolysis
'DAGs [plasma membrane]' positively regulates 'DAG stimulates protein kinase C-delta'
'Ca2+ [cytosol]' positively regulates 'ANOs transport cytosolic Cl- to extracellular region'
'DHX58 [cytosol]' negatively regulates 'dsRNA binds to RIG-I'
'ISG15:RIG-I conjugate (name copied from entity in Homo sapiens) [cytosol]' negatively regulates 'dsRNA binds to RIG-I'
Cytoplasmic chaperonin containing TCP-1: structural and functional characterization
Multimerin is found in the alpha-granules of resting platelets and is synthesized by a megakaryocytic cell line
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The neurotransmitter receptor-anchoring protein gephyrin reconstitutes molybdenum cofactor biosynthesis in bacteria, plants, and mammalian cells
AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy
The lipid phosphatase activity of PTEN is critical for its tumor supressor function
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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=3643998
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643921
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643908
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643913
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643901
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647227
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649105
All three IkappaB isoforms and most Rel family members are stably associated with the IkappaB kinase 1/2 complex
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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=3649107
A novel diacylglycerol acyltransferase (DGAT2) is decreased in human psoriatic skin and increased in diabetic mice
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3646918
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647403
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647071
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647086
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643331
6x(PCCA:PCCB) (name copied from entity in Homo sapiens)
3xMMAB (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=3645692
MTR:Zn2+:MeCbl (name copied from entity in Homo sapiens)
MTRR:MTR(MeCbl) (name copied from entity in Homo sapiens)
MTR:Zn2+:B12s (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=3640271
MTRR:MTR(B12s) (name copied from entity in Homo sapiens)
MTR:Zn2+:B12r (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=3640324
MTRR:MTR(B12r) (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=3645698
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_29888.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645697
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_92734.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_85623.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645695
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645693
PCCA:PCCB (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=3645694
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652105
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640193
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640278
The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral 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=3640291
3xPPCDC:3xFMN (name copied from entity in Homo sapiens)
2xPPCS (name copied from entity in Homo sapiens)
2xPNPO:2xFMN (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_157290.3
4-[(1R)-1-Hydroxy-2-(methylamino)ethyl]-1,2-benzenediol [ChEBI:1942]
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=3652106
NUDT5 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=3640303
2xENPP1 (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=3644303
Human pyridoxal kinase: overexpression and properties of the recombinant enzyme
1-acyl-sn-glycero-3-phospho-D-myo-inositol [ChEBI:28914]
2xTPK1: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_30698.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640122
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640126
MTR:Zn2+ (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_160053.3
MTRR:MTR (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=3652107
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_33731.10
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=3652108
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647768
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640917
Dihydropyriminidase-Zn complex (name copied from entity in Homo sapiens)
DPYD dimer (name copied from entity in Homo sapiens)
CTPS2 tetramer (name copied from entity in Homo sapiens)
CTPS tetramer (name copied from entity in Homo sapiens)
deoxythymidylate kinase (thymidylate kinase) holoenzyme (name copied from entity in Homo sapiens)
3-ureidopropionase-Zn complex (name copied from entity in Homo sapiens)
ITPA dimer (name copied from entity in Homo sapiens)
N (epsilon)-(carboxymethyl)lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction
NME4 hexamer (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=3643396
nucleoside diphosphate kinase 1A:5B heterohexamer (name copied from entity in Homo sapiens)
glutathione reductase 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=3643390
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643405
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644015
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643404
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644273
Heparan sulfate/heparin (HS-GAG) metabolism
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644272
An updated overview on Wnt signaling pathways: a prelude for more
Guanine deaminase 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=3640370
2-acyl-sn-glycero-3-phosphoethanolamine [ChEBI:28936]
catalase holoenzyme monomer (name copied from entity in Homo sapiens)
CAT tetramer (name copied from entity in Homo sapiens)
UMPS dimer (name copied from entity in Homo sapiens)
CAD hexamer (name copied from entity in Homo sapiens)
UCK1 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=3644274
DUT trimer (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_113098.8
TK1 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=3644275
UCK2 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=3644277
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_104340.9
CDA 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=3644278
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_112317.8
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652026
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_90126.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640899
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640858
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645026
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644002
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644009
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644008
BCAT1 dimer (name copied from entity in Homo sapiens)
BCAT2 dimer (name copied from entity in Homo sapiens)
PSAT1 dimer (name copied from entity in Homo sapiens)
PSPH:Mg++ dimer (name copied from entity in Homo sapiens)
CCBL1 dimer (name copied from entity in Homo sapiens)
PHGHD tetramer (name copied from entity in Homo sapiens)
GLUD1 hexamer (name copied from entity in Homo sapiens)
ASNS dimer (name copied from entity in Homo sapiens)
OAT hexamer (name copied from entity in Homo sapiens)
GPT2 dimer (name copied from entity in Homo sapiens)
Identification of novel PPARgamma target genes in primary human adipocytes
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644010
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644006
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644013
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644000
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644012
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644007
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644005
GPHN:Mg2+ (name copied from entity in Homo sapiens)
MOCOS:PXLP (name copied from entity in Homo sapiens)
GPT dimer (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)
3xGPHN:3xMg2+ (name copied from entity in Homo sapiens)
MOCS3:Zn2+ (red.) (name copied from entity in Homo sapiens)
2xNFS1:2xPXLP (name copied from entity in Homo sapiens)
MOCS3-S-S(1-):Zn2+ (name copied from entity in Homo sapiens)
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Checkpoint inhibition of the APC/C in HeLa cells is mediated by a complex of BUBR1, BUB3, CDC20, and MAD2
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NADSYN1 homohexamer (name copied from entity in Homo sapiens)
4xNADK:Zn2+ (name copied from entity in Homo sapiens)
NMNAT2 (Mg2+) (name copied from entity in Homo sapiens)
4xNMNAT3:4xMg2+ (name copied from entity in Homo sapiens)
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
2xMTHFR (name copied from entity in Homo sapiens)
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holo-MOCS1 (name copied from entity in Homo sapiens)
2xNAPRT1 (name copied from entity in Homo sapiens)
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2xMTHFD1 (name copied from entity in Homo sapiens)
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6xNMNAT1:6xZn2+ (name copied from entity in Homo sapiens)
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Btn-ACACB:2Mn2+ (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_95762.9
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The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis.
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1-chloro-2,4-dinitrobenzene [ChEBI:34718]
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Role of subunit diversity in signaling by heterotrimeric G proteins
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6xMCCC1:6xMCCC2 (name copied from entity in Homo sapiens)
6x(Btn-MCCC1:MCCC2) (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)
Neurotrophins and their receptors: a convergence point for many signalling pathways
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L1 and NCAM adhesion molecules as signaling coreceptors in neuronal migration and process outgrowth
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A structural model for the membrane-integral domain of succinate: quinone
Regulation of telomerase by telomeric proteins
RNA Polymerase III Abortive And Retractive Initiation
A critical review of the origin and control of adrenal androgens
Baillieres Clin Obstet Gynaecol 11:229-48
The molecular mechanics of eukaryotic translation
Prefoldin mediated transfer of substrate to CCT/TriC
Iron-sulfur proteins in health and disease
Accumulation of cyclin B1 requires E2F and cyclin-A-dependent rearrangement of the anaphase-promoting complex
The human ATP-binding cassette (ABC) transporter superfamily
Isozymes of glyceraldehyde-3-phosphate dehydrogenase in man and other mammals.
The control of glycogen metabolism in the liver
The equilibrative nucleoside transporter family, SLC29
AU-rich element-mediated translational control: complexity and multiple activities of trans-activating factors
Import of palmitoyl-CoA into the mitochondrial matrix
Tumor necrosis factor-alpha-converting enzyme is required for cleavage of erbB4/HER4
alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-beta-D-glucosylceramide [ChEBI:18313]
Identification of Xenopus SMC protein complexes required for sister chromatid cohesion
The ABCs of solute carriers: physiological, pathological and therapeutic implications of human membrane transport proteinsIntroduction
Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase
O-(4-Hydroxy-3,5-diidophenyl)-3,5-diiodo-L-tyrosine [ChEBI:7663]
Targeting the phosphoinositide 3-kinase pathway in cancer
N,N'-Diacetylchitobiosyldiphosphodolichol [ChEBI:7069]
5-phosphoribosylglycinamide [ChEBI:18349]
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ChEBI:18348 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
4-[(1R)-2-Amino-1-hydroxyethyl]-1,2-benzenediol [ChEBI:1]
A novel skeletal dysplasia with developmental delay and acanthosis nigricans is caused by a Lys650Met mutation in the fibroblast growth factor receptor 3 gene
Potential role of TBC1D4 in enhanced post-exercise insulin action in human skeletal muscle
Basic Medical Biochemistry: A Clinical Approach, 2nd ed (Book): 527
Molecular enzymology of carnitine transfer and transport
D-glucosyl-N-acylsphingosine [ChEBI:18368]
6-(L-erythro-1,2-Dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
7,8-dihydroneopterin 3'-triphosphate [ChEBI:18372]
2-Amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
AKT phosphorylates targets in the nucleus
The expanding role of mitochondria in apoptosis.
Biochemical Pathways - An Atlas of Biochemistry and Molecular Biology
Lehninger - Principles of Biochemistry 4th Edn.
beta-D-Mannosyldiacetylchitobiosyldiphosphodolichol [ChEBI:10408]
Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant
Enterohepatic bile salt transporters in normal physiology and liver disease
Human isopentenyl diphosphate: dimethylallyl diphosphate isomerase: overproduction, purification, and characterization
Exportin-5 mediates the nuclear export of pre-microRNAs and short hairpin RNAs
ChEBI:18381 5'-phosphoribosyl-5-formaminoimidazole-4-carboxamide
Expression patterns of two human genes coding for different rab GDP-dissociation inhibitors (GDIs), extremely conserved proteins involved in cellular transport
Aquaporin-11: a channel protein lacking apparent transport function expressed in brain
D-myo-Inositol 1,3,4,6-tetrakisphosphate
1D-myo-Inositol 1,3,4,6-tetrakisphosphate [ChEBI:809]
1D-myo-Inositol 1,3,4,6-tetrakisphosphate
ChEBI:16152 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphates
ChEBI:16152 ChEBI:16152 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphates
Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism
Biochemistry - The Chemical Reactions of Living Cells 2nd Edn.
The human calcium-independent phospholipase A2 gene multiple enzymes with distinct properties from a single gene
The human AQP4 gene: definition of the locus encoding two water channel polypeptides in brain
2'-deoxyadenosine 5'-diphosphate [ChEBI:16174]
7alpha,12alpha-Dihydroxy-5beta-cholestan-3-one [ChEBI:2288]
7alpha-Hydroxy-5beta-cholestan-3-one [ChEBI:2290]
A protein interaction framework for human mRNA degradation
Oxygen and carbon dioxide transport in vertebrate erythrocytes: an evolutionary change in the role of membrane transport
A mannosyltransferase gene at 11q23 is disrupted by a translocation breakpoint that co-segregates with bipolar affective disorder in a small family
The canonical retinoid cycle in rods (twilight vision)
A proposed nomenclature system for the cytosolic sulfotransferase (SULT) superfamily
SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases
Cloning and sequencing of cDNA encoding human sepiapterin reductase--an enzyme involved in tetrahydrobiopterin biosynthesis
Human GTP cyclohydrolase I: only one out of three cDNA isoforms gives rise to the active enzyme
Protein kinase C alpha-dependent phosphorylation of the mRNA-stabilizing factor HuR: implications for posttranscriptional regulation of cyclooxygenase-2
Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate
The role for endoplasmic reticulum stress in diabetes mellitus
Signaling through PI3Kgamma: a common platform for leukocyte, platelet and cardiovascular stress sensing
Condensation of Prometaphase Chromosomes
Thioredoxin-interacting protein links oxidative stress to inflammasome activation
Post-translational modification: synthesis of GPI-anchored proteins
Phagocytic processing of bacterial antigens for class I MHC presentation to T cells
Topological journey of parasite-derived antigens for presentation by MHC class I molecules
1,2-diacyl-sn-glycero-3-phosphocholine [ChEBI:16110]
Dihydroxyacetone phosphate [ChEBI:16108]
Relative CO2/NH3 selectivities of AQP1, AQP4, AQP5, AmtB, and RhAG
Human skeletal-muscle aldolase: N-terminal sequence analysis of CNBr- and o-iodosobenzoic acid-cleavage fragments
Metabolism of steroid hormones and vitamin D
The cell biology of cross-presentation and the role of dendritic cell subsets
Gz-mediated hormonal inhibition of cyclic AMP accumulation
Crystal structures of human GAR Tfase at low and high pH and with substrate beta-GAR
Conservation of the human telomere sequence (TTAGGG)n among vertebrates
Close homolog of L1 is an enhancer of integrin-mediated cell migration
NODs: intracellular proteins involved in inflammation and apoptosis
Interaction between the functional polymorphisms of the alcohol-metabolism genes in protection against alcoholism.
A gene encoding a putative FAD-dependent L-2-hydroxyglutarate dehydrogenase is mutated in L-2-hydroxyglutaric aciduria
1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide [ChEBI:18406]
5'-Phospho-ribosyl-5-amino-4-imidazole carboxamide
PIKKing on PKB: regulation of PKB activity by phosphorylation
a-(5,6-Dimethylbenzimidazolyl)cobamide coenzyme
(5,6-dimethylbenzimidazolyl)cobamide coenzyme
5'-Phosphoribosylformylglycinamidine [ChEBI:18413]
Identification of a novel aquaporin, AQP12, expressed in pancreatic acinar cells
Dual phosphorylation controls Cdc25 phosphatases and mitotic entry
Presentation of antigens by MHC class II molecules: getting the most out of them
Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide exchange factor expressed predominantly in lymphocytes
System-wide investigation of ErbB4 reveals 19 sites of Tyr phosphorylation that are unusually selective in their recruitment properties
Endosomal proteolysis of internalized proteins.
Understanding specificity in metabolic pathways--structural biology of human nucleotide metabolism
Modulation of mitochondrial membrane permeability in pathogenesis, autophagy and control of metabolism
Differential mechanism of G-protein activation induced by endogenous mu-opioid peptides, endomorphin and beta-endorphin
The rate of bulk flow from the endoplasmic reticulum to the cell surface
cDNA cloning, expression, and mutagenesis study of leukotriene B4 12-hydroxydehydrogenase
Biosynthesis and bioproduction of coenzyme Q10 by yeasts and other organisms
57 varieties: the human cytochromes P450
Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin
Physiological functions of the pentose phosphate pathway
Hereditary orotic aciduria and other disorders of pyrimidine metabolism
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 2663-2704
Integration of inositol phosphate signaling pathways via human ITPK1
Neurotrophin signal transduction in the nervous system
Purification, properties, and sequencing of aminoisobutyrate aminotransferases from rat liver
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
Regulation of the type I IFN induction: a current view
Human Wapl is a cohesin-binding protein that promotes sister-chromatid resolution in mitotic prophase
Compartmentalization of aquaporins in the human intestine
Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein
Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism
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Structure, function and evolution of the signal recognition particle
Decarboxylases involved in polyamine biosynthesis and their inactivation by nitric oxide
UDP-N-acetyl-D-glucosamine [ChEBI:16264]
Human ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways
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NAADP mobilizes calcium from acidic organelles through two-pore channels
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Cathepsin S required for normal MHC class II peptide loading and germinal center development
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Structural organization and complete nucleotide sequence of the gene encoding human acid sphingomyelinase (SMPD1)
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Activation of the FGF receptor underlies neurite outgrowth stimulated by L1, N-CAM, and N-cadherin
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Na+:HCO(3-) cotransporters (NBC): cloning and characterization
Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase. Basis for the dual substrate specificity and activation of the oncolytic agent tiazofurin.
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Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones
The Cdc6 nucleotide-binding site regulates its activity in DNA replication in human cells.
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The general transcription factors of RNA polymerase II.
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Reciprocal cross-talk between P2Y1 and P2Y12 receptors at the level of calcium signaling in human platelets
PKC-beta controls I kappa B kinase lipid raft recruitment and activation in response to BCR signaling
ChEBI:16290 5alpha-cholesta-7,24-dien-3beta-ol
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Amino acid transport across mammalian intestinal and renal epithelia
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Synthesis of bile acids and bile salts via 24-hydroxycholesterol
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Caspase-activated PAK-2 is regulated by subcellular targeting and proteasomal degradation
Acyl-coenzyme A synthetases in metabolic control
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Total enzymic synthesis of cholesterol from lanosterol. Cytochrome b5-dependence of 4-methyl sterol oxidase.
Structure-function relationships in dihydrolipoamide acyltransferases.
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Functional impairment of lens aquaporin in two families with dominantly inherited cataracts
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Metabolic activation of carcinogenic heterocyclic aromatic amines by human liver and colon
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Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinase
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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.
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Activation of human mitochondrial pantothenate kinase 2 by palmitoylcarnitine
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Cloning and characterization of a mammalian lithium-sensitive bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate
Etherphospholipid biosynthesis and dihydroxyactetone-phosphate acyltransferase: resolution of the genomic organization of the human gnpat gene and its use in the identification of novel mutations
Molecular characterization of a new urea transporter in the human kidney
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The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition
Demonstration of a specific mitochondrial isovaleryl-CoA dehydrogenase deficiency in fibroblasts from patients with isovaleric acidemia.
Involvement of Rac/Cdc42/PAK pathway in cytoskeletal rearrangements
CDG-IL: an infant with a novel mutation in the ALG9 gene and additional phenotypic features
Biochemical and genetic aspects of mevalonate kinase and its deficiency
Molecular characterization of cytosolic phospholipase A2-beta
Complementation analysis in PtdInsP kinase-deficient yeast mutants demonstrates that Schizosaccharomyces pombe and murine Fab1p homologues are phosphatidylinositol 3-phosphate 5-kinases
Defective copper-induced trafficking and localization of the Menkes protein in patients with mild and copper-treated classical Menkes disease
Glutathione metabolism and its selective modification
An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing
PTEN1 is frequently mutated in primary endometrial carcinomas
Association of alternative complement pathway components with human blood platelets: secretion and localization of factor D and beta 1H Globulin
Identification and characterization of a major liver lysophosphatidylcholine acyltransferase
The faciogenital dysplasia gene product FGD1 functions as a Cdc42Hs-specific guanine-nucleotide exchange factor
Please note that this reaction was inferred from experiments performed using Saccharomyces cerevisiae.
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.
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.
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'.
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
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.
During the synthesis of actin and tubulin, the nascent ribosome-associated chains bind to the heteromeric chaperone protein, prefoldin (PFD) (Hansen et al., 1999).
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).
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.
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.
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.
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 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 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.
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.
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 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.
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.
Yeast kinesin-8 depolymerizes microtubules in a length-dependent manner
Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase.
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
The cAMP signalling pathway activates CREB through PKA, p38 and MSK1 in NIH 3T3 cells
Characterization of myotubularin-related protein 7 and its binding partner, myotubularin-related protein 9
ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles
Cloning and expression of cDNA of human delta 4-3-oxosteroid 5 beta-reductase and substrate specificity of the expressed enzyme
Phosphoglycerate mutase isozyme marker for tissue differentiation in man
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.
Metabolism of arachidonic acid to 20-hydroxy-5,8,11, 14-eicosatetraenoic acid by P450 enzymes in human liver: involvement of CYP4F2 and CYP4A11
The phosphorylation of a dolichol residue of the ER membrane is a starting step in the N-glycan biosynthesis pathway (Fernandez F et al, 2002). Defects in DOLK are the cause of congenital disorder of glycosylation type 1M (CDG1M), also known as dolichol kinase deficiency (Kranz C et al, 2007).
Most human GPI anchors have ethanolamine phosphate groups attached to their first and third mannose residues, but GPI anchors with ethanolamine phosphates attached to all three mannose residues have also been identified. Addition of the third ethanolamine phosphate can be catalyzed by a complex of PIG-F and a newly described human protein, GPI7. The donor of the ethanolamine phosphate for this reaction is unknown (Shishioh et al. 2005).
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.
Glucosamine-fructose 6-phosphate aminotransferase (GFAT) is the first and rate-limiting enzyme in the hexosamine synthesis pathway, and thus formation of hexosamines like N-acetylglucosamine (GlcNAc). This enzyme probably plays a role in limiting the availability of substrates for the N- and O- linked glycosylation of proteins. Two isoforms, GFAT 1 and 2, have been identified (McKnight GL et al, 1992; Oki T et al, 1999). GFAT is required normal functioning of neuromuscular synaptic transmission. Defects in the gene expressing this protein leads to altered muscle fiber morphology and impaired neuromuscular junction development (Senderek et al, 2011).
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).
In the last step of the N-glycan precursor biosynthesis pathway, the mature N-glycan (Glc3Man9GlcNAc2) is removed from the dolichyl diphosphate molecule upon which it has been synthesized, and attached to a nascent protein. In this process, a dolichyl diphosphate molecule is released and once de-phosphorylated by dolichyl diphosphatase 1 (DOLPP1) to obtain dolichyl phosphate, it can be used as a substrate for the synthesis of another N-glycan oligosaccharide (Wedgwood JF and Strominger JL, 1980).
Dolichol is a polyisoprenol lipid comprised of five-carbon isoprene units linked linearly in a head-to-tail fashion. In the N-glycan biosynthesis pathway, dolichyl phosphate is used as an anchor for the N-glycan sugar to the ER membrane, and as an initiation point for the synthesis. Dolichyl phosphate can be obtained either from direct phosphorylation of dolichol or from de-phosphorylation of dolichyl diphosphate, released at the end of the N-glycan biosynthesis pathway.
Prolactin-derived amyloid in the aging pituitary gland
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.
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).
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.
Cytosolic GDP-mannose reacts with dolichyl phosphate in the endoplasmic reticulum membrane to form dolichyl phosphate D-mannose. The reaction is catalyzed by dolichyl-phosphate mannosyltransferase, a heterotrimeric protein embedded in the endoplasmic reticulum membrane. The first subunit of the heterotrimer appears to be the actual catalyst, and the other two subunits appear to stabilize it (Maeda et al. 2000).
Dolichyl-phosphate-mannose (DPM) is the donor of mannose groups in the synthesis of the dolichyl pyrophosphate-linked precursor oligosaccharide in asparagine-linked glycosylation, in the synthesis of the glycosyl phosphatidylinositol (GPI) anchor precursor, in protein O-mannosylation and in protein C-mannosylation. Its synthesis proceeds in two steps. First, cytosolic GDP-mannose reacts with dolichyl phosphate exposed on the cytosolic face of the endoplasmic reticulum membrane to form DPM with its mannose moiety oriented toward the cytosol. The DPM molecule then flips in the endoplasmic reticulum membrane, so that its mannose moiety is in the endoplasmic reticulum lumen, accessible to the enzymes that catalyze its transfer to growing glycolipids and glycoproteins (Kinoshita and Inoue, 2000; Maeda et al, 2000).
The first step of GPI synthesis is the transfer of N-acetylglucosamine from cytosolic UDP-N-acetylglucosamine to phosphatidyl inositol (PI) in the endoplasmic reticulum membrane. The reaction is catalyzed by a multimeric enzyme, also localized to the endoplasmic reticulum membrane, six components of which have been identified to date by mutagenesis studies in cultured cells and by co-recipitation studies in vitro (Watanabe et al. 1996, 1998, 2000).
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 eighth reaction of GPI synthesis, a third mannose residue is added, catalyzed by PIG-B (Takahashi et al. 1996).
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).
The final step in the main pathway for the synthesis of GPI moieties in human cells is the addition of an ethanolamine phosphate to the third mannose residue of the glycolipid, donated by phosphatidylethanolamine. This reaction has been experimentally characterized in the mouse, where studies with mutated cell lines defective in GPI biosynthesis have established the role of two proteins, PIG-F and PIG-O, in this reaction (Hong et al. 2000). While a human PIG-F protein has been identified and shown to be involved in this event (Inoue et al. 1993), the human event has not been fully characterized and is therefore annotated here as inferred from studies of the mouse event.
Metabolism of retinoids and arachidonic acid by human and mouse cytochrome P450 1b1
Protease-activated receptors in hemostasis, thrombosis and vascular biology
Alpha and beta tubulin folding intermediates are formed through ATPâdependent 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).
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).
Beta-tubulin folding intermediates generated via ATP-dependent interaction with TriC/CCT are captured by cofactors A and D (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.
Factor A:beta tubulin complex act as a reservoir capable of accepting or delivering its target tubulin protein to cofactor D (Tian et al., 1997). In the reverse reaction, Cofactor A may displace cofactor D in a cofactor D:beta tubulin complex.
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%â20% 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).
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).
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).
Nucleotide sequence for a cDNA encoding the alpha subunit of retinal transducin (GNAT1) isolated from the human eye
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).
Human dolichol-phosphate-mannose synthase consists of three subunits, DPM1, DPM2 and DPM3
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.
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.
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).
Unfolded actins and tubulins bound to prefoldin are transferred to CCT via a docking mechanism (McCormack and Willison, 2001).
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).
CCT/TRiC facilitates folding of newly translated SK1 into its mature active form (Zebol et al., 2008)
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).
GPVI and integrin alphaIIb beta3 signaling in platelets
Cloning and functional characterization of the human GLUT7 isoform SLC2A7 from the small intestine
Am J Physiol Gastrointest Liver Physiol 287:G236-42
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Cloning and characterization a novel human 1-acyl-sn-glycerol-3-phosphate acyltransferase gene AGPAT7
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Trk receptors: roles in neuronal signal transduction
The RNA polymerase II elongation complex.
Plk1 regulates activation of the anaphase promoting complex by phosphorylating and triggering SCFbetaTrCP-dependent destruction of the APC Inhibitor Emi1
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
Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7
AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain
Biosynthesis of thyroid hormone: basic and clinical aspects
Mechanisms of caspase-1 activation by P2X7 receptor-mediated K+ release
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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
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La proteins from Drosophila melanogaster and Saccharomyces cerevisiae: a yeast homolog of the La autoantigen is dispensable for growth.
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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
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Hyaluronan: from extracellular glue to pericellular cue
Insulin degradation: mechanisms, products, and significance.
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Cytochrome P450s and cholesterol homeostasis
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Chromatin recruitment of DNA repair proteins: lessons from the fanconi anemia and double-strand break repair pathways
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Structural basis of hereditary coproporphyria
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).
Removal of the second mannose on the alpha 1,3 branch (Frenzel Z et al, 2003).
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).
7alpha,26-dihydroxy-5beta-cholestan-3-one [ChEBI:48778]
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 B position (Gonzalez et al, 1999: Hirao et al, 2006).
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.
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).
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.
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 CM et al, 2000; Völker C et al, 2002).
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.
ZnT-3, a putative transporter of zinc into synaptic vesicles
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)
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.
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.
Proteins that are released from the CNX or CRT complex with folding defects accumulate in a compartment of the ER called ERQC (Kamhi-Nesher S 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 the 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 V 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 GZ, 2009 and Määttänen P et al, 2010.
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).
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).
Cell signaling by receptor tyrosine kinases
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 C et al, 2003). Defects in ALG2 are the cause of CDG1I (Thiel C et al, 2003).
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
Exportin complex translocates pre-miRNA to cytosol
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).
Exportin-5 recognizes 3' overhang of pre-miRNA
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.
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).
Phosphomannomutase 1 and 2 (PMM1 and PMM2) catalyze the isomerization of Mannose 6-phosphate to Mannose 1-phosphate (Wada Y and Sakamoto M et al, 1997; Matthijs G et al, February 1997). Mutations in the PMM2 gene are one of the causes of Jaeken syndrome. a disease of glycosylation, type CDGIa. (Matthijs G et al, May 1997).
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 M et al, 2004; Kranz C et al, 2004; Grubenmann CE 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).
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 S 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.
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.
serine + tRNA(Ser) + ATP => Ser-tRNA(Ser) + AMP + pyrophosphate
proline + tRNA(Pro) + ATP => Pro-tRNA(Pro) + AMP + pyrophosphate
tryptophan + tRNA(Trp) + ATP => Trp-tRNA(Trp) + AMP + pyrophosphate
Mannose-6-phosphate isomerase (MPI) converts Fructose 6-phosphate to Mannose 6-phosphate (Proudfoot AE 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 E et al, 2000).
threonine + tRNA(Thr) + ATP => Thr-tRNA(Thr) + AMP + pyrophosphate
valine + tRNA(Val) + ATP => Val-tRNA(Val) + AMP + pyrophosphate
tyrosine + tRNA(Tyr) + ATP => Tyr-tRNA(Tyr) + AMP + pyrophosphate
methionine + tRNA(Met) + ATP => Met-tRNA(Met) + AMP + pyrophosphate
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 D-mannose) than the previous steps. It has been proposed that ALG3, along with all the mannosyl- and glucosyl transferases in the N-glycan biosynthesis pathway that use dolichyl phosphate D-mannose or dolichyl phosphate D-glucose as donor, derive from duplications of a common ancestral enzyme (Oriol R et al, 2002). Defects in ALG3 are associated with Congenital Disorder of Glycosylation 1D (CDG1D) (Sun L et al, 2005).
lysine + tRNA(Lys) + ATP => Lys-tRNA(Lys) + AMP + pyrophosphate
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 MA et al, 2008).
leucine + tRNA(Leu) + ATP => Leu-tRNA(Leu) + AMP + pyrophosphate
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).
isoleucine + tRNA(Ile) + ATP => Ile-tRNA(Ile) + AMP + pyrophosphate
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).
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 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 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.
phenylalanine + tRNA(Phe) + ATP => Phe-tRNA(Phe) + AMP + pyrophosphate
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).
cysteine + tRNA(Cys) + ATP => Cys-tRNA(Cys) + AMP + pyrophosphate
histidine + tRNA(His) + ATP => His-tRNA(His) + AMP + pyrophosphate
Variant apolipoprotein AI as a major constituent of a human hereditary amyloid
Transition state model and mechanism of nucleophilic aromatic substitution reactions catalyzed by human glutathione S-transferase M1a-1a
glycine + tRNA(Gly) + ATP => Gly-tRNA(Gly) + AMP + pyrophosphate
glutamine + tRNA(Glu) + ATP => Glu-tRNA(Glu) + AMP + pyrophosphate
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. There are no known associations between ALG11 and CDG disorders to date.
glutamate + tRNA(Glu) + ATP => Glu-tRNA(Glu) + AMP + pyrophosphate
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).
Sequence, tissue distribution, and chromosomal localization of mRNA encoding a human glucose transporter-like protein
asparagine + tRNA(Asn) + ATP => Asn-tRNA(Asn) + AMP + pyrophosphate
aspartate + tRNA(Asp) + ATP => Asp-tRNA(Asp) + AMP + pyrophosphate
tyrosine + tRNA(Tyr) + ATP =>Tyr-tRNA(Tyr) + AMP + pyrophosphate
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
arginine + tRNA(Arg) + ATP => Arg-tRNA(Arg) + AMP + pyrophosphate
Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
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
Molecular components of the mammalian circadian clock
Addition of galactose to the Tn antigen via an alpha-1,3 linkage forms a Core 8 glycoprotein
A role for PtdIns(4,5)P2 and PIP5Kalpha in regulating stress-induced apoptosis
Addition of GalNAc to the Tn antigen via an alpha-1,6 linkage forms a Core 7 glycoprotein
Regulation of the anaphase-promoting complex by the dual specificity phosphatase human Cdc14a
The NRAMP family of metal-ion transporters
ADP Binding by Phosphorylated IRE1 Homodimer
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Type II phosphoinositide 5-phosphatases have unique sensitivities towards fatty acid composition and head group phosphorylation
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Assignment of the gene for human arylsulfatase B, ARSB, to chromosome region 5p11----5qter
Substrate preferences of a lysophosphatidylcholine acyltransferase highlight its role in phospholipid remodeling
ABCA10, a novel cholesterol-regulated ABCA6-like ABC transporter
The Calreticulin gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The BIP (HSPA5) gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
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.
The ADD1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
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.
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.
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.
Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the International Society of Amyloidosis
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.
The Endoplasmin (HSP90B1) gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
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 methylation of phosphatidylethanolamine
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.
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).
An unknown N-acetylglucosaminyltransferase mediates the transfer of GlcNAc to Tn antigens via an beta-1,6 linkage to create Core 6 mucins (Brockhausen et al. 2009).
An unknown N-acetylgalactosaminyltransferase mediates the transfer of GalNAc is transferred to Tn antigens via an alpha-1,6 linkage to create Core 7 mucins (Brockhausen et al. 2009).
An unknown galactosyltransferase mediates the transfer of galactose is transferred to Tn antigens via an alpha-1,3 linkage to create Core 8 mucins (Brockhausen et al. 2009).
Mucins are a family of high molecular weight, heavily glycosylated proteins (glycoconjugates) produced by epithelial tissues in most metazoa. Mucins' key characteristic is their ability to form gels; therefore they are a key component in most gel-like secretions, serving functions from lubrication to cell signalling to forming chemical barriers. To date, there are approximately 20 genes that express mucins. Mature mucins are composed of two distinct regions: (1) The amino- and carboxy-terminal regions are very lightly glycosylated, but rich in cysteines. The cysteine residues participate in establishing disulfide linkages within and among mucin monomers. (2) A large central region rich in serine, threonine and proline residues called the variable number of tandem repeat (VNTR) region which can become heavily O-glycosylated with hundreds of O-GalNAc glycans. N-acetyl-galactosamine (GalNAc) is the first glycan to be attached, forming the simplest mucin O-glycan. After this, several different pathways are possible generating "core" structures. Four core structures are commonly formed, several others are possible but infrequent. O-linked glycans are often capped by the addition of a sialic acid residue, terminating the addition of any more O-glycans (Brockhausen et al, 2009; Tarp and Clausen, 2008).
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).
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; Martínez-Menárguez et al, 1999). The other is mediated by LMAN1/MCFD2, mannose-binding lectins that recognize a glycan signal (Zhang B et al, 2003).
N-linked glycosylation is the most important form of post-translational modification for proteins synthesized and folded in the Endoplasmic Reticulum (Stanley P 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 R 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 D and Levy Y, 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 GZ, 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 P 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 SE et al, 2003), and classified as CDG type I for the genes in the LLO synthesis pathway, and CDG type II for the others.
An unknown N-acetylglucosaminyltransferase mediates the transfer of GlcNAc to Tn antigens via an alpha-1,3 linkage to create Core 5 mucins (Brockhausen et al. 2009).
The HYOU1 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 SRPR 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 KDELR3 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 TATDN2 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 TPP1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The C19orf10 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.
The DCTN1 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 DNAJB11 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 GAP 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 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.
Immunolocalization of AQP9 in liver, epididymis, testis, spleen, and brain
Translational control mechanisms often involve interactions between the 3' - or 5' -untranslated regions (UTRs) of mRNA and RNA-binding proteins. One such mechanism requires circularization of the mRNA molecule involving protein-protein interactions between the mRNA termini (Mazumder et al., 2001). While the 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.
Eight SLC gene families are involved in the transport of amino acids and oligopeptides.
Protein metabolism comprises the pathways of translation, post-translational modification and protein folding.
Five SLC gene families encode proteins that mediate transport of amines (neurotransmitters, biogenic amines, ammonium and choline). They are SLC6, SLC14, SLC18, SLC42. The fifth family, SLC22, will appear in a later release (He L et al, 2009).
PERK 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.
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) leads to phosphorylation of the translation initiation factor eIF2alpha and global down-regulation of protein synthesis. These three regulatory pathways are annotated here.
ATF4 is a transcription factor and activates expression of IL-8, MCP1, IGFBP-1, CHOP, HERP1 and ATF3.
Myotubularin lipid phosphatase binds the hVPS15/hVPS34 lipid kinase complex on endosomes
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)
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).
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).
The WIPI1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Temporal and spatial regulation of the phosphatidate phosphatases lipin 1 and 2
The YIF1A 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.
The TSPYL2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The Talin-1 (TLN1) gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Once dissociated from BiP, PERK monomers form homodimers, the active form of the protein.
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.
The Aspariagine Synthetase (ASNS) gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The C-terminal domain of PERK has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1.
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).
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).
CARS2 (mitochondrial cysteinyl tRNA synthetase) catalyzes the reaction of cysteine, mitochondrial tRNA(Cys), and ATP to form Cys-tRNA(Cys), AMP, and pyrophosphate. The CARS2 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).
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).
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).
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).
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).
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).
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).
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).
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).
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).
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).
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).
Purine ribonucleoside monophosphate biosynthesis
Characterization of the CoA ligases of human liver mitochondria catalyzing the activation of short- and medium-chain fatty acids and xenobiotic carboxylic acids
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).
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).
Chaperonin-mediated folding of vertebrate actin-related protein and gamma-tubulin
Synaptojanin 2, a novel Rac1 effector that regulates clathrin-mediated endocytosis
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).
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).
Catecholamine biosynthesis and physiological regulation in neuroendocrine cells
The human ZIP1 transporter mediates zinc uptake in human K562 erythroleukemia cells
4-(2-Aminoethyl)-1,2-benzenediol [ChEBI:18243]
Identification of genetic mutations in Japanese patients with fructose-1,6-bisphosphatase deficiency
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Fibroblast growth factor receptors: lessons from the genes
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Determinants of function and substrate specificity in human UDP-galactose 4'-epimerase
1D-myo-Inositol 1,3,4-trisphosphate [ChEBI:810]
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Resolution of D-loop structures through Holliday junction intermediates
Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositide-dependent protein kinase-1
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An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
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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
Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein.
Beta glucuronidase deficiency: report of clinical, radiologic, and biochemical features of a new mucopolysaccharidosis
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)
Human plasma epidermal growth factor/beta-urogastrone is associated with blood platelets
The nonsense-mediated decay RNA surveillance pathway
Role of LAT2/NTAL/LAB on calcium mobilization
Primary structure and tissue distribution of human 4-aminobutyrate aminotransferase
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p53-Dependent G1/S DNA damage checkpoint
The Src, Syk, and Tec family kinases: distinct types of molecular switches
Molecular cloning of AMP deaminase isoform L. Sequence and bacterial expression of human AMPD2 cDNA
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Gbetagammas and the Ras binding domain of p110gamma are both important regulators of PI(3)Kgamma signalling in neutrophils
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Mutations in the 4-hydroxyphenylpyruvate dioxygenase gene (HPD) in patients with tyrosinemia type III
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ChEBI:60125 N-epsilon-(1-(1-carboxy)ethyl)lysine
1D-myo-Inositol 1,4,5,6-tetrakisphosphate
1D-myo-Inositol 1,4,5,6-tetrakisphosphate [ChEBI:811]
D-myo-Inositol 1,4,5,6-tetrakisphosphate
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Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity
Frizzled/PCP signalling: a conserved mechanism regulating cell polarity and directed motility
Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216.
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Biochemical analysis of the intrinsic Mcm4-Mcm6-mcm7 DNA helicase activity.
MMS19 assembles iron-sulfur proteins required for DNA metabolism and genomic integrity
MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA metabolism
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L13a-mediated translational silencing of Ceruloplasmin expression
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Identification of natural resistance-associated macrophage protein in peripheral blood lymphocytes
adenosine 5'-monophosphate [ChEBI:16027]
Genetic Analysis of Coenzyme Q Biosynthesis
Coenzyme Q: Molecular Mechanisms in Health and Disease (Book): 185-208
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Translesion synthesis by DNA polymerases bypassing lesion on DNA template
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5'-Phosphoribosyl-N-formylglycinamide [ChEBI:18272]
ChEBI:18278 N-acetyl-D-glucosaminyldiphosphodolichol
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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
3-Phospho-D-glyceroyl phosphate [ChEBI:16001]
(R)-2-Hydroxy-3-(phosphonooxy)-1-monoanhydridewith phosphoric propanoic acid
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
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).
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).
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).
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).
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).
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).
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.
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.
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.
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).
The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency.
Cloning, expression and characterization of the pig liver GDP-mannose pyrophosphorylase. Evidence that GDP-mannose and GDP-Glc pyrophosphorylases are different proteins
Exportin-5 binds pre-microRNAs having 2-nucleotide overhangs at the 3' end. Binding is independent of sequence and depends on GTP.
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, however only Argonaute2 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 Argonaute2, 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.
Nuclear Export by Exportin-5. The pre-microRNA is bound by the Exportin-5:RanGTP complex in the nucleus and the complex is translocated through the nuclear pore into the cytoplasm. In the process GTP is hydrolyzed to GDP.
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.
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.
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
The protein deficient in Lowe syndrome is a phosphatidylinositol-4,5-bisphosphate 5-phosphatase
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.
Vertebrate shugoshin links sister centromere cohesion and kinetochore microtubule stability in mitosis
Coupling of rotation and catalysis in F(1)-ATPase revealed by single-molecule imaging and manipulation
Enzymatic activities in cultured human lymphocytes that dephosphorylate dolichyl pyrophosphate and dolichyl phosphate
WW domain-containing proteins, WWOX and YAP, compete for interaction with ErbB-4 and modulate its transcriptional function
Presence of three distinct molecular species of Gi protein alpha subunit. Structure of rat cDNAs and human genomic DNAs
Structure-function analysis of human [corrected] phosphatidylinositol transfer protein alpha bound to phosphatidylinositol
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
Interactions between UPF1, eRFs, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathways
Aminoacyl tRNA synthetases and their connections to disease
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
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Human phosphoglycerate kinase. I. Crystallization and characterization of normal enzyme
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Cytosolic aldehyde dehydrogenase (ALDH1) variants found in alcohol flushers
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Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate
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A new human hereditary amyloidosis: the result of a stop-codon mutation in the apolipoprotein AII gene
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Purification, molecular cloning, and sequencing of phospholipase C-beta 4
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EJC-independent degradation of nonsense immunoglobulin-mu mRNA depends on 3' UTR length
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Pathways of DNA double-strand break repair during the mammalian cell cycle.
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Properties and functions of diacylglycerol kinases
Assembly of the RAD51-ssDNA nucleoprotein complex
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Autophosphorylation of the catalytic subunit of the DNA-dependent protein kinase is required for efficient end processing during DNA double-strand break repair.
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ChEBI:11805 3-hydroxy-2-methylpropanoate
Assembly of the RAD50-MRE11-NBS1 complex at DNA double-strand breaks
Characterization of the gene encoding human peroxisomal 3-oxoacyl-CoA thiolase (ACAA). No large DNA rearrangement in a thiolase-deficient patient
Mutations and polymorphisms in GUSB gene in mucopolysaccharidosis VII (Sly Syndrome)
Studies on the metabolic fate of n-3 polyunsaturated fatty acids
The G473D mutation impairs dimerization and catalysis in human sulfite oxidase
Solute carrier family 2, facilitated glucose transporter member 4
Activation of Chaperone Genes by ATF6-alpha
Ras-related C3 botulinum toxin substrate 1
3-phosphoinositide dependent protein kinase-1
Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase PTEN
Glucose transporter type 4, insulin-responsive
Solute carrier family 2, facilitated glucose transporter, member 4
Trimethylamine N-oxide synthesis: a human variant
Kinetic evaluation of human cloned coproporphyrinogen oxidase using a ring isomer of the natural substrate
Apical GLUT2: a major pathway of intestinal sugar absorption
Wnt/Fz signaling and the cytoskeleton: potential roles in tumorigenesis
Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha
Endoplasmic reticulum (ER) chaperone regulation and survival of cells compensating for deficiency in the ER stress response kinase, PERK
Multidrug resistance protein 4 (MRP4/ABCC4): a versatile efflux transporter for drugs and signalling molecules
Determinants for activation of the atypical AGC kinase Greatwall during M phase entry
ABC transporters and cholesterol metabolism
The TREM receptor family and signal integration
A unique phosphorylation-dependent mechanism for the activation of Ca2+/calmodulin-dependent protein kinase type IV/GR
Glutathione-S-transferase P1 is a critical regulator of Cdk5 kinase activity
Telomeres shorten during ageing of human fibroblasts
The family of ubiquitin-conjugating enzymes (E2s): deciding between life and death of proteins
Prostaglandin F2alpha formation from prostaglandin H2 by prostaglandin F synthase (PGFS): crystal structure of PGFS containing bimatoprost
Rad51 recombinase and recombination mediators.
ABCA3 gene mutations in newborns with fatal surfactant deficiency
Salt wasting and deafness resulting from mutations in two chloride channels
Epac-selective cAMP analog 8-pCPT-2'-O-Me-cAMP as a stimulus for Ca2+-induced Ca2+ release and exocytosis in pancreatic beta-cells
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5-triphospho-1D-myo-inositol (1,2,3,4,6)pentakisphosphate
5-triphospho-1D-myo-inositol (1,2,3,4,6)pentakisphosphate [ChEBI:62985]
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
Renal physiology of SLC26 anion exchangers
The molecular mechanism of nitrogen-containing bisphosphonates as antiosteoporosis drugs
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.
1,5-bisdiphosphoinositol-1D-myo-inositol (2,3,4,6)tetrakisphosphate
1,5-bisdiphosphoinositol-1D-myo-inositol (2,3,4,6)tetrakisphosphate [ChEBI:62923]
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1-diphospho-1D-myo-inositol (3,4,5,6)tetrakisphosphate
1-diphospho-1D-myo-inositol (3,4,5,6)tetrakisphosphate [ChEBI:62926]
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Sequence of the human iduronate 2-sulfatase (IDS) gene
1-diphospho-1D-myo-inositol (2,3,4,5,6)pentakisphosphate [ChEBI:62919]
1-diphospho-1D-myo-inositol (2,3,4,5,6)pentakisphosphate
1D-myo-Inositol 3,4,6-trisphosphate [ChEBI:62918]
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1,5-bisdiphosphoinositol-1D-myo-inositol (3,4,6)trisphosphate
1,5-bisdiphosphoinositol-1D-myo-inositol (3,4,6)trisphosphate [ChEBI:62931]
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AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase
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Precise binding of single-stranded DNA termini by human RAD52 protein.
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5-diphospho-1D-myo-inositol (1,3,4,6)tetrakisphosphate
5-diphospho-1D-myo-inositol (1,3,4,6)tetrakisphosphate [ChEBI:62928]
Heteroduplex formation by human Rad51 protein: effects of DNA end-structure, hRP-A and hRad52.
Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex
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Processing of Capped Intronless Pre-mRNA
NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest
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Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
Class I MHC mediated antigen processing & presentation
Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
Identification of mammalian microRNA host genes and transcription units
Crystal structure of human kynurenine aminotransferase I
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Characterization of phospholipase D activity in bovine photoreceptor membranes
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Functional characterization of human sphingosine kinase-1
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Destabilization of mRNA by Butyrate Response Factor 1 (BRF1)
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Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities
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Hepatocyte nuclear factor-1alpha recruits the transcriptional co-activator p300 on the GLUT2 gene promoter
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Pharmacokinetics of salicylate elimination in man
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Human platelets contain SNARE proteins and a Sec1p homologue that interacts with syntaxin 4 and is phosphorylated after thrombin activation: implications for platelet secretion
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Purification and partial amino acid sequence of human aconitase
Intracellular localization of human Ins(1,3,4,5,6)P5 2-kinase
Multicatalytic endopeptidase complex subunit C5
Multicatalytic endopeptidase complex subunit C9
Activator of multicatalytic protease subunit 3
Activator of multicatalytic protease subunit 2
Probable 26S protease regulatory subunit 8
Multicatalytic endopeptidase complex subunit C8
26S proteasome non-ATPase regulatory subunit 1
Multicatalytic endopeptidase complex chain Z
Proteasome subunit beta type 7 precursor
Multicatalytic endopeptidase complex epsilon chain
Proteasome subunit beta type 5 precursor
Structural analysis and detection of biological inositol pyrophosphates reveal that the family of VIP/diphosphoinositol pentakisphosphate kinases are 1/3-kinases
Inositol polyphosphates: a new frontier for regulating gene expression
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
Ubiquitin-like modifier-activating enzyme 5
Ubiquitin-like modifier-activating enzyme 7
NEDD8-activating enzyme E1 catalytic subunit
Phospholipases D1 and D2 coordinately regulate macrophage phagocytosis
Mast cell signal transduction from the high-affinity IgE receptor
The stem cell marker Bcrp/ABCG2 enhances hypoxic cell survival through interactions with heme
Ubiquitin-like modifier-activating enzyme 6
Ubiquitin-like modifier-activating enzyme 1
DEx/H-box helicases activate type I IFN and inflammatory cytokines production
Synthesis of prostaglandin F ethanolamide by prostaglandin F synthase and identification of Bimatoprost as a potent inhibitor of the enzyme: new enzyme assay method using LC/ESI/MS
Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum
GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking
The LZT proteins; the LIV-1 subfamily of zinc transporters
Human glutamine phosphoribosylpyrophosphate amidotransferase. Kinetic and regulatory properties
Human thymidylate kinase. Purification, characterization, and kinetic behavior of the thymidylate kinase derived from chronic myelocytic leukemia
Involvement of human MCM8 in prereplication complex assembly by recruiting hcdc6 to chromatin
Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1
Multicatalytic endopeptidase complex delta chain
Proteasome subunit beta type 6 precursor
Multicatalytic endopeptidase complex subunit C2
Dynamics of transitional endoplasmic reticulum sites in vertebrate cells
CalDAG-GEFIII activation of Ras, R-ras, and Rap1
26S proteasome non-ATPase regulatory subunit 7
Multicatalytic endopeptidase complex subunit C7-I
Multicatalytic endopeptidase complex iota chain
26S proteasome non-ATPase regulatory subunit 11
26S proteasome non-ATPase regulatory subunit 3
26S proteasome non-ATPase regulatory subunit 9
Sequence survey of receptor tyrosine kinases reveals mutations in glioblastomas
Multicatalytic endopeptidase complex beta chain
Proteasome subunit beta type 4 precursor
StAR protein and the regulation of steroid hormone biosynthesis
Multicatalytic endopeptidase complex subunit MECl-1
Proteasome subunit beta type 10 precursor
Tumor necrosis factor type 1 receptor associated protein 2
26S proteasome non-ATPase regulatory subunit 2
26S proteasome non-ATPase regulatory subunit 8
Multicatalytic endopeptidase complex subunit C13
Proteasome subunit beta type 8 precursor
Multicatalytic endopeptidase complex zeta chain
26S proteasome non-ATPase regulatory subunit 10
Activator of multicatalytic protease subunit 1
Interferon gamma up-regulated I-5111 protein
Multicatalytic endopeptidase complex subunit C3
26S proteasome non-ATPase regulatory subunit 4
26S proteasome non-ATPase regulatory subunit 12
Multicatalytic endopeptidase complex chain 7
Proteasome subunit beta type 9 precursor
26S proteasome non-ATPase regulatory subunit 13
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform
PP2A -56 kDa regulatory subunit B epsilon isoform
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform
PP2A- 56 kDa regulatory subunit, alpha isoform
Caspase activation of mammalian sterile 20-like kinase 3 (Mst3). Nuclear translocation and induction of apoptosis
Phosphorylated RasGRP1 and phosphorylated RasGRP3
Cloning and expression of the gene involved in Sanfilippo B syndrome (mucopolysaccharidosis III B)
Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis
Phosphoinositides as regulators of membrane trafficking in health and disease
Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
Fructose transporter in human spermatozoa and small intestine is GLUT5
The characterization of gene mutations for human glucose phosphate isomerase deficiency associated with chronic hemolytic anemia
Tumor necrosis factor alpha-induced phosphorylation of I kappa B alpha is a signal for its degradation but not dissociation from NF-kappa B
From structure to disease: the evolving tale of aquaporin biology
Tristetraprolin recruits functional mRNA decay complexes to ARE sequences
Signal transduction by immunoglobulin is mediated through Ig alpha and Ig beta
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Catalytic activity is required for calcium/calmodulin-dependent protein kinase IV to enter the nucleus
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De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-glycinamide ribonucleotide transformylase by functional complementation in E. coli
Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture
Loss of signaling through the G protein, Gz, results in abnormal platelet activation and altered responses to psychoactive drugs
D box and KEN box motifs in budding yeast Hsl1p are required for APC-mediated degradation and direct binding to Cdc20p and Cdh1p
Evidence that negative elongation factor represses transcription elongation through binding to a DRB sensitivity-inducing factor/RNA polymerase II complex and RNA.
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Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism.
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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
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Aquaporin-1, nothing but a water channel
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A novel disorder caused by defective biosynthesis of N-linked oligosaccharides due to glucosidase I deficiency
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Regulation of cell growth-dependent expression of mammalian CDC6 gene by the cell cycle transcription factor E2F.
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Differential expression of aquaporin 7 in adipose tissue of lean and obese high fat consumers
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Purification of human platelet-derived growth factor
Coupling RNA polymerase II transcription with pre-mRNA processing.
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Stimulation-dependent I kappa B alpha phosphorylation marks the NF-kappa B inhibitor for degradation via the ubiquitin-proteasome pathway
The role of a group III AQP, AQP11 in intracellular organelle homeostasis
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Translocation of cyclin B1 to the nucleus at prophase requires a phosphorylation-dependent nuclear import signal
A conserved cyclin-binding domain determines functional interplay between anaphase-promoting complex-Cdh1 and cyclin A-Cdk2 during cell cycle progression
Mechanism of tyrosine phosphorylation and activation of phospholipase C-gamma 1. Tyrosine 783 phosphorylation is not sufficient for lipase 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_153540.3
TRP channels: sensors and transducers of gasotransmitter signals
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The mannose receptor is a pattern recognition receptor involved in host 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_95016.9
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Comprehensive genomic characterization defines human glioblastoma genes and core pathways
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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_82716.9
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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=113527
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4600.2
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Cathepsin D component recommendedName: Cathepsin D light chain /component component recommendedName: Cathepsin D heavy chain /component
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Aquaporins: translating bench research to human disease
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Characterization of FIM-FGFR1, the fusion product of the myeloproliferative disorder-associated t(8;13) translocation
A Cdc42 activation cycle coordinated by PI 3-kinase during Fc receptor-mediated phagocytosis
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Intracellular transport and kinesin superfamily proteins, KIFs: structure, function, and dynamics
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A mammalian cell cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia-telangiectasia.
90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1
Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA
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Heterodimerization is required for the formation of a functional GABA(B) receptor
Telomere C-strand (Lagging Strand) Synthesis
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Mechanisms of action of glucagon-like peptide 1 in the pancreas
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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_134862.5
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Signal-induced proliferation-associated protein 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_141782.5
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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_133784.5
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The mitochondrial electron transport and oxidative phosphorylation system
PIKfyve, a mammalian ortholog of yeast Fab1p lipid kinase, synthesizes 5-phosphoinositides. Effect of insulin
DNA-directed RNA polymerase III subunit RPC10
DNA-directed RNA polymerases I, II, and III 17.1 kDa polypeptide
DNA-directed RNA polymerase III subunit 127.6 kDa polypeptide
Elevation of cellular NAD levels by nicotinic acid and involvement of nicotinic acid phosphoribosyltransferase in human cells
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)
The C. elegans heterochronic gene lin-4 encodes small RNAs with antisense complementarity to lin-14
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DNA-directed RNA polymerases I and III subunit RPAC1
DNA-directed RNA polymerase I and III 40 kDa polypeptide
DNA-directed RNA polymerases III 39 kDa polypeptide
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DNA-directed RNA polymerase III subunit RPC3
DNA-directed RNA polymerase III subunit C
DNA-directed RNA polymerases I, II, and III 7.0 kDa polypeptide
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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_25934.1
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_26586.1
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The autonomous activity of calcium/calmodulin-dependent protein kinase IV is required for its role in transcription
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Probable ATP-dependent RNA helicase DDX41
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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
CREB phosphorylation through the activation of Adenylate Cyclase
Polo-like kinase is required for the fragmentation of pericentriolar Golgi stacks during mitosis
Interferon-induced helicase C domain-containing protein 1
Oligosaccharyl transferase 48 kDa subunit
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
Protein kinase C substrate 60.1 kDa protein heavy chain
Interferon-induced 17 kDa protein component recommendedName: Ubiquitin cross-reactive protein
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Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase
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Probable ATP-dependent RNA helicase DHX58
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Reconstitution of the strand invasion step of double-strand break repair using human Rad51 Rad52 and RPA proteins
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Phospholipase C-beta 1 is a GTPase-activating protein for Gq/11, its physiologic regulator
Functional characterization of human 1-acylglycerol-3-phosphate acyltransferase isoform 8: cloning, tissue distribution, gene structure, and enzymatic activity
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Hyaluronan export by the ABC transporter MRP5 and its modulation by intracellular cGMP
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The primary structure of mitochondrial aspartate aminotransferase from human heart
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A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function
Phospholipases and phagocytosis: the role of phospholipid-derived second messengers in phagocytosis
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Phosphate bond hydrolysis by NUDT proteins
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The nucleoside diphosphate kinase D (NM23-H4) binds the inner mitochondrial membrane with high affinity to cardiolipin and couples nucleotide transfer with respiration
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Human alpha-galactosidase A: nucleotide sequence of a cDNA clone encoding the mature enzyme
N-glycan antennae elongation in the medial/trans-Golgi
The sulfur-containing amino acids: an overview
Localization of platelet osteonectin at the internal face of the alpha-granule membranes in platelets and megakaryocytes
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cAMP-dependent protein kinase, alpha-catalytic subunit
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Rap guanine nucleotide exchange factor 3
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Signalling via integrins: implications for cell survival and anticancer strategies
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Rap guanine nucleotide exchange factor 4
Each conserved active site tyr in the three subunits of human isocitrate dehydrogenase has a different function
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Running with RNA polymerase: eukaryotic transcript elongation.
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Mutational spectrum of D-bifunctional protein deficiency and structure-based genotype-phenotype analysis
The AU-rich element mRNA decay-promoting activity of BRF1 is regulated by mitogen-activated protein kinase-activated protein kinase 2
NUDT16 and ITPA play a dual protective role in maintaining chromosome stability and cell growth by eliminating dIDP/IDP and dITP/ITP from nucleotide pools in mammals
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Overexpression of the normal phosphoribosylpyrophosphate synthetase 1 isoform undelies catalytic superactivity of human phosphoribosylpyrophosphate synthetase
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A cell-based reglucosylation assay demonstrates the role of GT1 in the quality control of a maturing glycoprotein
Dual regulation of the anaphase promoting complex in human cells by cyclin A-Cdk2 and cyclin A-Cdk1 complexes
The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant DNA synthesis.
Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis
Epidermal growth factor receptor: elements of intracellular communication
Protein transport protein Sec61 subunit alpha isoform 1
Regulation of actin filament assembly by Arp2/3 complex and formins
Annu Rev Biophys Biomol Struct 36:451-77
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Signal-induced degradation of I kappa B alpha requires site-specific ubiquitination
Fat and beyond: the diverse biology of PPARgamma
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The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1857-1895
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Human mitochondrial phosphoenolpyruvate carboxykinase 2 gene. Structure, chromosomal localization and tissue-specific expression
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Non-vesicular lipid transport by lipid-transfer proteins and beyond
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The LKB1 tumor suppressor kinase in human disease
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Maple syrup urine disease (branched-chain ketoaciduria)
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1971-2005
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The SLC40 basolateral iron transporter family (IREG1/ferroportin/MTP1)
Complex genomic rearrangements lead to novel primate gene function
Why calcium-stimulated adenylyl cyclases?
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Mechanisms involved in the intestinal digestion and absorption of dietary vitamin A
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The intrinsic affinity between E2 and the Cys domain of E1 in ubiquitin-like modifications
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Myosin phosphatase-targeting subunit 1 regulates mitosis by antagonizing polo-like kinase 1
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Cytochrome P450 oxidations in the generation of reactive electrophiles: epoxidation and related reactions
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G protein activation by G protein coupled receptors: ternary complex formation or catalyzed reaction?
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2-acyl-sn-glycero-3-phospho-D-myo-inositol [ChEBI:62746]
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Ether lipid biosynthesis: alkyl-dihydroxyacetonephosphate synthase protein deficiency leads to reduced dihydroxyacetonephosphate acyltransferase activities
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Absorption of chlorophyll phytol in normal man and in patients with Refsum's disease
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 2125-2163
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AUF1, the regulator of tumor necrosis factor alpha messenger RNA decay, is targeted by autoantibodies of patients with systemic rheumatic diseases
Identification of active flavin-containing monooxygenase isoform 2 in human lung and characterization of expressed protein
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ATP-dependent RNA helicase A (Nuclear DNA helicase II) (NDH II) (DEAD-box protein 9)
DNA-directed RNA polymerase III subunit 22.9 kDa polypeptide
DNA-directed RNA polymerase I and III 16 kDa polypeptide
DNA-directed RNA polymerases I and III subunit RPAC2
DNA-directed RNA polymerase III largest subunit
DNA-directed RNA polymerase II 23 kDa polypeptide (EC 2.7.7.6) (RPB25) (XAP4) (RPB5)
DNA-directed RNA polymerase II 23 kDa polypeptide
DNA-directed RNA polymerases III 80 kDa polypeptide
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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
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Phosphorylation of CAP-G is required for its chromosomal DNA localization during mitosis
Biochem. Biophys. Res. Commun. 377:1007-11
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The Bcl10-Malt1 complex segregates Fc epsilon RI-mediated nuclear factor kappa B activation and cytokine production from mast cell degranulation
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Frequent activating mutations of FGFR3 in human bladder and cervix carcinomas
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Phosphoglycerate mutase BB isoenzyme deficiency in a patient with non-spherocytic anemia: familial and metabolic studies
The control of mammalian DNA replication: a brief history of space and timing.
AMPK inhibits chREBP transcriptional activation activity
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Cytochrome P450 - arranged by substrate type
Hot-spot mutations in p110alpha of phosphatidylinositol 3-kinase (pI3K): differential interactions with the regulatory subunit p85 and with RAS
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Molecular cloning and characterization of a human multisubstrate specific nucleotide-sugar transporter homologous to Drosophila fringe connection
Ca(2+)/calmodulin activated adenylyl cyclase
Human cationic amino acid transporters hCAT-1, hCAT-2A, and hCAT-2B: three related carriers with distinct transport properties
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Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function.
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Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association
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Signaling by target of rapamycin proteins in cell growth control
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Inositol hexakisphosphate kinase products contain diphosphate and triphosphate groups
A UAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway
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Effector role reversal during evolution: the case of frataxin in Fe-S cluster biosynthesis
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WAS/WASL-interacting protein family member 3
WAS/WASL-interacting protein family member 2
Rad52 and Ku bind to different DNA structures produced early in double-strand break repair.
Cloning and functional expression of a urea transporter from human bone marrow cells
Analysis and update of the human solute carrier (SLC) gene superfamily
First-in-man clinical trial of the oral pan-AKT inhibitor MK-2206 in patients with advanced solid tumors
Molecular cloning, sequencing and expression of the cDNA of the mitochondrial form of phosphoenolpyruvate carboxykinase from human liver
Deficiency of carbohydrate response element-binding protein (ChREBP) reduces lipogenesis as well as glycolysis
Different functional domains of GLUT2 glucose transporter are required for glucose affinity and substrate specificity
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1777-1805
Cloning and characterization of the major insulin-responsive glucose transporter expressed in human skeletal muscle and other insulin-responsive tissues.
Substrate specificity of MATE1 and MATE2-K, human multidrug and toxin extrusions/H(+)-organic cation antiporters
Proteomic analysis of proteins associated with lipid droplets of basal and lipolytically stimulated 3T3-L1 adipocytes
Disorders of proline and hydroxyproline metabolism
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1821-1838
The glutamate/GABA-glutamine cycle: aspects of transport, neurotransmitter homeostasis and ammonia transfer
Molecular identity and cellular distribution of advanced glycation endproduct receptors: relationship of p60 to OST-48 and p90 to 80K-H membrane proteins
Disorders of tetrahydrobiopterin and related biogenic amines
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1725-1776
Regulation of APC/C activators between G1/S and early anaphase
A cytoplasmic chaperonin that catalyzes beta-actin folding
Architecture of the yeast origin recognition complex bound to origins of DNA replication.
Update on interconversions of vitamin B-6 with its coenzyme
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1909-1963
Shugoshin collaborates with protein phosphatase 2A to protect cohesin
Endoplasmic reticulum stress induction of insulin-like growth factor-binding protein-1 involves ATF4
EGFR interacts with phospholipase C-gamma
Comparative analysis of gene regulation by the transcription factor PPARalpha between mouse and human
Determination of P4501A2 activity in human liver microsomes using [3-14C-methyl]caffeine
4-hydroxy-17beta-estradiol [ChEBI:62845]
Discovery of a lysophospholipid acyltransferase family essential for membrane asymmetry and diversity
Expression of isoforms of the human receptor tyrosine kinase c-kit in leukemic cell lines and acute myeloid leukemia
Uridine diphosphate glucose pyrophosphorylase. IV. Crystallization and properties of the enzyme from human liver
Partial purification of a microsomal sterol 4 -carboxylic acid decarboxylase
Crystallization and properties of human liver ornithine aminotransferase
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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.
Androgens are the determining factors for male development and behaviour in vertebrates (Miller 2002).
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.
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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.
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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).
In female vertebrates, estrogens control reproductive system development and reproductive functions (Payne AH and Hales DB, 2004).
Expression of HSD17B1 which is the main enzyme that catalyzes the hydrogenation of estrone is strongly restricted to placenta, ovaries, endometrium and breast tissue (Moeller and Adamski, 2009).
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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.
Active steroid hormones are produced from the precursor cholesterol.The steps involved in the biosynthesis of the adrenal steroid hormones, corticosterone, cortisol, and aldosterone; and the gonadal steroid hormones, progesterone, estradiol, and testosterone are annotated here. The enzymes that catalyze these reactions fall into two major classes of proteins: the cytochrome P450 heme-containing proteins and the hydroxysteroid dehydrogenases.
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ChREBP activates metabolic gene expression
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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.
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.
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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).
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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).
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Cortisol and NADP+ react to form cortisone, NADPH, and H+. This reaction is catalyzed by 11beta-hydroxysteroid dehydrogenase (11beta-HSD), associated with the endoplasmic reticulum membrane. The conversion of cortisol, an active hormone, into inactive cortisone occurs in many tissues in the body, notably in the liver, and appears to play a role in regulating cortison activity.
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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.
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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).
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.
Processing of mRNA encompasses the capping of mRNA, processing of mRNAs with and without introns, and also modification of mRNA, as in mRNA editing.
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.
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.
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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.
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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'.
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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'.
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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.
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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'.
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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.
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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.
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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 5ââ¬â¢ end of U7 snRNA binds to a sequence 3ââ¬â¢ 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.
Isolation, sequencing, and expression of a cDNA for the HXM-A form of xenobiotic/medium-chain fatty acid:CoA ligase from human liver mitochondria
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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.
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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.
Ligand-regulated association of ErbB-4 to the transcriptional co-activator YAP65 controls transcription at the nuclear level
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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.
Amplification of signal from the kinetochores
Molecular structure and physiological functions of GABA(B) receptors
Phosphoinositides in constitutive membrane traffic
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A1CF protein is cytosolic in origin and is translocated to nucleus where it binds to the target RNA. The order of events in the formation of editosomes, namely, binding of A1CF and APOBEC-1 are not well elucidated in human cells.
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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.
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.
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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.
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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:
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The best characterized case of C to U editing is in the intestinal apolipoprotein B transcript, where the editing event creates a premature translation stop codon and consequently leads to a shorter form of the protein. In the liver, C to U editing is important in the expression of specific isoforms of the apolipoprotein B enzyme. ApoB mRNA editing is a posttranscriptional, nuclear process that can be initiated after splicing, at the time of polyadenylation and is completed by the time pre-mRNA matures fully (reviewed by Blanc and Davidson, 2003). This editing event is a simple hydrolytic cytidine deamination to uridine, and is carried out by the Apobec-1 enzyme, along with the Apobec-1 complementing factor, ACF. The editing of apo-B mRNA involves the site-specific deamination of (C6666 to U), which converts codon 2153 from a glutamine codon, CAA, to a premature stop codon, UAA. As ACF is distributed in a variety of tissues, and these genes contain multiple family members, it is possible that editing events in additional targets will be found. The cis-acting regulatory elements for C to U editing include: 22 nt editing site within ApoB mRNA, 5ââ¬â¢ tripartite motif with an enhancer element adjacent to the target cytidine, a spacer element and mooring sequence both 3ââ¬â¢ to the cytidine (reviewed by Smith et al., 1997). The editing complex can be represented as:
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The editosome for C to U editing in mammals consist of a member of cytidine deaminase family of enzymes, apoB mRNA editig catalytic polypeptide 1 (APOBEC-1) and a complementing specificity factor (ACF) in addition to the target mRNA.
HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin acetylation cycle
Interferons: signaling, antiviral and viral evasion
HNF1A-dependent synthesis of GLUT2 protein
The cap binding complex binds to the methylated GMP cap on the nascent mRNA transcript.
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'.
Nerve growth factor signaling, neuroprotection, and neural repair
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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.
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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)
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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.
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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
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Although, DNA replication occurs in the S phase of the cell cycle, the formation of the DNA replication pre-initiation complex begins during G1 phase.
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Finally, progression out of mitosis and division of the cell into two daughters (cytokinesis) requires the inactivation of Cyclin B - Cdc2 by ubiquitin-dependent proteolysis of Cyclin A and B, which is regulated by a large E3 ubiquitin ligase complex known as the Anaphase Promoting Complex (APC). The detailed annotation of the M/G1 transition will be completed in a later version of GK.
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Identification of an autonomously initiating RNA polymerase III holoenzyme containing a novel factor that is selectively inactivated during protein synthesis inhibition
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In S. cerevisiae, two ORC subunits, Orc1 and Orc5, both bind ATP, and Orc1 in addition has ATPase activity. Both ATP binding and ATP hydrolysis appear to be essential functions in vivo. ATP binding by Orc1 is unaffected by the association of ORC with origin DNA (ARS) sequences, but ATP hydrolysis is ARS-dependent, being suppressed by associated double-stranded DNA and stimulated by associated single-stranded DNA. These data are consistent with the hypothesis that ORC functions as an ATPase switch, hydrolyzing bound ATP and changing state as DNA unwinds at the origin immediately before replication. It is attractive to speculate that ORC likewise functions as a switch as human pre-replicative complexes are activated, but human Orc proteins are not well enough characterized to allow the model to be critically tested. mRNAs encoding human orthologs of all six Orc proteins have been cloned, and ATP-binding amino acid sequence motifs have been identified in Orc1, Orc4, and Orc5. Interactions among proteins expressed from the cloned genes have been characterized, but the ATP-binding and hydrolyzing properties of these proteins and complexes of them have not been determined.
At the beginning of this reaction, 1 molecule of 'origin of replication', and 1 molecule of 'DNA polymerase epsilon' are present. At the end of this reaction, 1 molecule of 'DNA polymerase epsilon:origin complex' is present.
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DNA polymerase alpha:primase is comprised of four subunits, p180, p70, p58, and p49. The two primase subunits, p58 and p49, form a tight complex. The p49 subunit contains the DNA primase activity and one role of p58 appears to be tethering p49 to p180, the DNA polymerase catalytic subunit. The fourth subunit, p70, binds p180 and may tether the DNA polymerase alpha:primase complex to Cdc45.
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Once the Mcm2-7 complex has been assembled onto the origin of replication, the next step is the assembly of Cdc45, an essential replication protein, in late G1. The assembly of Cdc45 onto origins of replication forms a complex distinct from the pre-replicative complex, sometimes called the pre-initiation complex. The assembly of Cdc45 onto origins correlates with the time of initiation. Like the Mcm2-7 proteins, Cdc45 binds specifically to origins in the G1 phase of the cell cycle and then to non-origin DNA during S phase and is therefore thought to travel with the replication fork. Indeed, S. cerevisiae Cdc45 is required for DNA replication elongation as well as replication initiation. Cdc45 is required for the association of alpha DNA polymerase:primase with chromatin. Based on this observation and the observation that in S. cerevisiae, cCdc45 has been found in large complexes with some components of Mcm2-7 complex, it has been suggested that Cdc45 plays a scaffolding role at the replication fork, coupling Pol-alpha:primase to the replication fork through the helicase. Association of Cdc45 with origin DNA is regulated in the cell cycle and its association is dependent on the activity of cyclin-dependent kinases but not the Cdc7/Dbf4 kinase. In Xenopus egg extracts, association of Cdc45 with chromatin is dependent on Xmus101. TopBP1, the human homolog of Xmus1, is essential for DNA replication and interacts with DNA polymerase epsilon, one of the polymerases involved in replicating the genome. TopBP1 homologs have been found in S. cerevisiae and S. pombe. Sld3, an additional protein required for Cdc45 association with chromatin in S. cerevisiae and S. pombe, has no known human homolog.
Genetic studies in S. cerevisiae indicate that wild-type Cdc6 function is required for correctly timed loading of Mcm2-7 onto ORC. Biochemical studies indicate that the human and Xenopus Cdc6 proteins likewise are required for Mcm2-7 loading, and that they are ATPase switches. Specifically, Cdc6 may function as a clamp loader, assembling Mcm2-7 onto DNA in an ATP-dependent reaction. All known Cdc6 proteins have the Walker A and Walker B sequence motifs characteristic of the AAA+ superfamily of ATPases. As expected for an AAA+ protein, human Cdc6 binds and slowly hydrolyzes ATP in vitro. ATP hydrolysis was disrupted by mutations of the Walker B motif, while both binding and hydrolysis were disrupted by Walker A mutations. Microinjection of either mutant protein into HeLa cells blocked their progression through S phase. Both wild-type and mutant proteins can dimerize in vitro, and studies with Xenopus egg extracts suggest that Cdc6 functions in vivo as a dimer or larger multimer. In Xenopus extracts depleted of Cdc6 and reconstituted with either mutant protein, recruitment of Mcm2-7 to chromatin failed.
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DNA replication pre-initiation in eukaryotic cells begins with the formation of the pre-replicative complex (pre-RC) during the late M phase and continues in the G1 phase of the mitotic cell cycle, a process also called DNA replication origin licensing. The association of initiation proteins (ORC, Cdc6, Cdt1, Mcm2-7) with the origin of replication in both S. cerevisiae and humans has been demonstrated by chromatin immunoprecipitation experiments. In S. cerevisiae, pre-replicative complexes are assembled from late M to G1. In mammalian cells as well, pre-replicative complexes are assembled from late M to G1, as shown by biochemical fractionation and immunostaining. There are significant sequence similarities among some of the proteins in the pre-replicative complex. The ORC subunits Orc1, Orc4 and Orc5 are homologous to one another and to Cdc6. The six subunits of the Mcm2-7 complex are homologous to one another. In addition, Orc1, Orc4, Orc5, Cdc6, and the Mcm2-7 subunits, are members of the AAA+ superfamily of ATPases. Since the initial identification of these pre-RC components other factors that participate in this complex have been found, including Cdt1 in human, Xenopus, S. pombe, and S. cerevisiae cells.
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At the beginning of this reaction, 1 molecule of 'ORC:origin', and 1 molecule of 'CDC6' are present. At the end of this reaction, 1 molecule of 'CDC6:ORC:origin complex' is present. This reaction takes place in the 'nucleus'.
CDC6 protein is synthesized under the control of E2F transcription factors
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Cdc6 is a regulator of DNA replication initiation in both yeasts and human cells, but its mechanism of action differs between the two systems. Genetic studies in budding yeast (S. cerevisiae) and fission yeast (S. pombe) indicate that the normal function of Cdc6 protein is required to restrict DNA replication to once per cell cycle. Specifically, Cdc6 may function as an ATPase switch linked to Mcm2-7 association with the Cdt1:Cdc6:ORC:origin complex. In S. cerevisiae, Cdc6 protein is expressed late in the M phase of the cell cycle and, in cells with a prolonged G1 phase, late in G1. This protein has a short half-life, and is destroyed by ubiquitin-mediated proteolysis, mediated by the SCF complex. Human Cdc6 protein levels are reduced early in G1 but otherwise are constant throughout the cell cycle. Some reports have suggested that after cells enter S phase, Cdc6 is phosphorylated, excluded from the nucleus and subject to ubiquitination and degradation. Replenishing Cdc6 protein levels during G1 appears to be regulated by E2F transcription factors.
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The MCM2-7 complex, an essential component of the pre-replication complex, recruits CDC6 and CDT1 proteins to the origin. MCM8, another member of the MCM family has been found to bind to chromatin during early G1 phase. MCM8 interacts specifically with the ORC2 protein.
Induction of Platelet glycoprotein IV (PAS IV, CD36, GPIV) Expression During Adipogenesis
Expression of CD36 (platelet glycoprotein IV, FAT)
At the end of this reaction, 1 molecule of 'Cdc6' is present.
Transcriptional activation of pyruvate kinase gene by ChREBP:MLX
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Expression of Phosphoenolpyruvate carboxykinase 1 (PEPCK-C)
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The docking protein Gab1 is the primary mediator of EGF-stimulated activation of the PI-3K/Akt cell survival pathway
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At the beginning of this reaction, 1 molecule of 'Orc3:Orc2:origin', and 1 molecule of 'Orc5' are present. At the end of this reaction, 1 molecule of 'Orc5:Orc3:Orc2:origin' is present. This reaction takes place in the 'nucleus'.
At the beginning of this reaction, 1 molecule of 'Orc2:origin', and 1 molecule of 'Orc3' are present. At the end of this reaction, 1 molecule of 'Orc3:Orc2:origin' is present. This reaction takes place in the 'nucleus'.
At the beginning of this reaction, 1 molecule of 'Orc4:Orc5:Orc3:Orc2:origin', and 1 molecule of 'Orc1' are present. At the end of this reaction, 1 molecule of 'Orc1:Orc4:Orc5:Orc3:Orc2:origin' is present. This reaction takes place in the 'nucleus'.
At the beginning of this reaction, 1 molecule of 'Orc4', and 1 molecule of 'Orc5:Orc3:Orc2:origin' are present. At the end of this reaction, 1 molecule of 'Orc4:Orc5:Orc3:Orc2:origin' is present. This reaction takes place in the 'nucleus'.
In Saccharomyces cerevisiae, the entire ORC complex is constitutively bound to the origin of replication. However, in mammalian cells, Orc1, and possibly other Orc subunits, dissociate from origins of replication, while Orc2 remains stably associated with chromatin across the cell cycle. The first step in formation of the pre-RC is assembly of the hexameric Origin Recognition Complex (ORC) at the origin of replication. Recent work on human (Hs) ORC has suggested that the heterohexamer assembles in an ordered manner. HsOrc2 appears to be constitutively bound to origins of replication. HsOrc2 and HsOrc3 form a complex that interacts with HsOrc4 and HsOrc5. Recruitment of HsOrc5 into the complex is important for the association of HsOrc1. HsOrc6 is also capable of interacting with the core HsOrc2:3:4:5 complex, but not smaller complexes. Interestingly, HsOrc1 and a subunit of the Mcm2-7 complex (HsMcm2) interact with a histone acetyltransferase, HsHBO1 (Bell & Stillman 1992; Diffley et al. 1994; Lee & Bell 1997; Wenger et al. 1975; Li & DePamphili;s 2001; Dhar et al. 2001; Vashee et al, 2001; Iizuka & Stillman 1999 Burke et al. 2001).
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Binding of Lsm1-7 Complex to Deadenylated mRNA
3' to 5' Exoribonuclease Digestion of mRNA by the Exosome Complex
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
The polo-like kinase PLK1 phosphorylates KIF23 (also known as MKLP1 i.e. mitotic kinesin-like protein 1) on serine residues S904 and S905.
The polo-like kinase PLK1 phosphorylates KIF20A (also known as MKLP2 i.e. mitotic kinesin-like protein 2) on serine residue S528.
BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains
The polo-like kinase PLK1 phosphorylates NUDC on serine residues S274 and S326.
AUF1(hnRNP D0) Dimers Bind AU-rich Element in 3' UTR of Transcripts
In this final phase of mitosis, new membranes are formed around two sets of chromatids and two daughter cells are formed. The chromosomes and the spindle fibers disperse, and the fiber ring around the center of the cell, composed of actin, contracts, pinching the cell into two daughter cells.
5' to 3' Exoribonuclease Digestion of Decapped mRNA
Mitosis, or the M phase, involves nuclear division and cytokinesis, where two identical daughter cells are produced. Mitosis involves prophase, prometaphase, metaphase, anaphase, and telophase. Finally, cytokinesis leads to cell division. The phase between two M phases is called the interphase; it encompasses the G1, S, and G2 phases of the cell cycle.
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While sister chromatids resolve in prometaphase, separating along chromosomal arms, the cohesion of sister centromeres persists until anaphase. At the anaphase onset, the anaphase promoting complex/cyclosome (APC/C) ubiquitinates PTTG1 (securin), targeting it for degradation (Hagting et al. 2002). PTTG1 acts as an inhibitor of ESPL1 (known as separin i.e. separase). Hence, PTTG1 removal initiated by APC/C, enables ESPL1 to become catalytically active (Zou et al. 1999, Waizenegger et al. 2002). ESPL1 undergoes autoleavage (Waizenegger et al. 2002) and also cleaves RAD21 subunit of centromeric cohesin (Hauf et al. 2001). RAD21 cleavage promotes dissociation of cohesin complexes from sister centromeres, leading to separation of sister chromatids. Subsequent movement of sister chromatids to opposite poles of the mitotic spindle segregates replicated chromosomes to two daughter cells (Waizenegger et al. 2000, Hauf et al. 2001, Waizenegger et al. 2002).
After APC/C-mediated degradation of PTTG1 (securin), ESPL1 (separin i.e. separase) is rapidly autocatalytically cleaved after arginine residues at positions 1506 and 1535. The N-terminal and C-terminal fragments remain bound to each other after cleavage. It has not been examined what happens with the short middle fragment of ESPL1, so it is annotated as a part of the autocleaved ESPL1 complex. The autocatalytic cleavage of ESPL1 is not a prerequisite for the subsequent cleavage of the cohesin subunit RAD21 (Waizenegger et al. 2002).
The dissolution of the nuclear membrane marks the beginning of the prometaphase. Kinetochores are created when proteins attach to the centromeres. Microtubules then attach at the kinetochores, and the chromosomes begin to move to the metaphase plate.
The condensin I complex is evolutionarily conserved and consists of five subunits: two SMC (structural maintenance of chromosomes) family subunits, SMC2 and SMC4, and three non-SMC subunits, NCAPD2, NCAPH and NCAPG. The stoichiometry of the complex is 1:1:1:1:1 (Hirano and Mitchinson 1994, Hirano et al. 1997, Kimura et al. 2001). SMC2 and SMC4 subunits, shared between condensin I and condensin II, are DNA-dependent ATPases, and condensins are able to introduce positive supercoils into DNA in an ATP-dependent manner (Kimura and Hirano 1997). Protein levels of condensin subunits are constant during the cell cycle, however condensins are enriched on mitotic chromosomes. Four of the five subunits, SMC4, NCAPD2, NCAPG and NCAPH, are phosphorylated in both mitotic and interphase HeLa cells, but on different sites (Takemoto et al. 2004). CDK1 (CDC2) in complex with CCNB (cyclin B) phosphorylates NCAPD2, NCAPG and NCAPH in mitosis (Kimura et al. 1998, Kimura et al. 2001, Takemoto et al. 2006, Murphy et al. 2008), but other mitotic kinases, such as PLK1 (St-Pierre et al. 2009), and other post-translational modifications, such as acetylation, may also be involved (reviewed by Bazile et al. 2010). Global proteomic analysis of human cell lines has identified N6-acetylation of lysine residues in condensin subunits SMC2, SMC4 and NCAPH (Choudhary et al. 2009). Another high throughput proteomic study showed that condensin I subunits NCAPD2 and NCAPH are phosphorylated upon DNA damage, probably by ATM or ATR kinase (Matsuoka et al. 2007). As condensin I is cytosolic, it gains access to chromosomes only after the nuclear envelope breakdown at the start of prometaphase (Ono et al. 2004). Condensin I, activated by CDK1-mediated phosphorylation, promotes hypercondensation of chromosomes that were condensed in prophase through the action of condensin II (Hirota et al. 2004). AURKB may also regulate association of condensin I complex with chromatin (Lipp et al. 2007). Protein phosphatase PP2A acts independently of its catalytic activity to target condensin II complex to chromatin, but does not interact with condensin I (Takemoto et al. 2009). Full activation of condensin I requires dephosphorylation of sites modified by CK2 during interphase (Takemoto et al. 2006). Besides being essential for chromosome condensation in mitosis, condensin I may also contribute to cohesin removal from chromosome arms in prometaphase, but the exact mechanism is not known (Hirota et al. 2004).
Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197
Nuclear translocation of catalytic domain of Mst3
Metaphase is marked by the formation of the metaphase plate. The metaphase plate is formed when the spindle fibers align the chromosomes along the middle of the cell. Such an organization helps to ensure that later, when the chromosomes are separated, each new nucleus that is formed receives one copy of each chromosome. This pathway has not yet been annotated in Reactome. The metaphase to anaphase transition during mitosis is triggered by the destruction of mitotic cyclins. In anaphase, the paired chromosomes separate at the centromeres, and move to the opposite sides of the cell. The movement of the chromosomes is facilitated by a combination of kinetochore movement along the spindle microtubules and through the physical interaction of polar microtubules.
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Proteasome mediated degradation of PAK-2p34
In anaphase, the paired chromosomes separate at the centromeres, and move to the opposite sides of the cell. The movement of the chromosomes is facilitated by a combination of kinetochore movement along the spindle microtubules and through the physical interaction of polar microtubules.
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carbovir diphosphate + ATP => carbovir triphosphate + ADP
CIA Targeting Complex Transfers 4Fe-4S Cluster to Apoproteins
4Fe-4S Cluster Forms on NUBP2:NUBP1 Scaffold
Autophosphorylation of PAK-2p34 in the activation loop
Inhibitory phosphate groups that were added to condensin I subunits by CK2 during interphase have to be removed for full mitotic activation of condensin I (Takemoto et al. 2006). The responsible phosphatase has not been identified.
Release of Cytochrome c from mitochondria
CDK1 (CDC2) in complex with CCNB (cyclin B) phosphorylates condensin I subunits NCAPD2, NCAPG and NCAPH in mitosis (Kimura et al. 2001, Takemoto et al. 2006), but other mitotic kinases may also be involved. CDK1 phosphorylation sites in NCAPH have not been established. NCAPD2 threonine residues T1339, T1384 and T1389 are inferred to be phosphorylated by CDK1 based on homologues sites in Xenopus laevis Ncapd2 (Kimura et al. 1998). NCAPG threonine residues T308 and T332 are phosphorylated by CDK1 in vitro and functionally important. The functional importance of threonine T931, also phosphorylated by CDK1 in vitro, has not been demonstrated (Murphy et al. 2008). Phosphorylation by CDK1 is required for mitotic activation of condensin I and promotes chromosomal binding, introduction of positive supercoils into DNA, and chromatin condensation (Kimura et al. 1998, Kimura et al. 2001, Takemoto et al. 2006).
The resolution of sister chromatids in mitotic prometaphase involves removal of cohesin complexes from chromosomal arms, with preservation of cohesion at centromeres (Losada et al. 1998, Hauf et al. 2001, Hauf et al. 2005). CDK1-mediated phosphorylation of cohesin-bound CDCA5 (Sororin) at threonine T159 provides a docking site for PLK1, enabling PLK1-mediated phosphorylation of cohesin subunits STAG2 (SA2) and RAD21 (Hauf et al. 2005, Dreier et al. 2011, Zhang et al. 2011). Further phosphorylation of CDCA5 by CDK1 results in dissociation of CDCA5 from cohesin complex, which restores the activity of WAPAL in removing STAG2-phosphorylated cohesin from chromosomal arms (Hauf et al. 2005, Gandhi et al. 2006, Kueng et al. 2006, Shintomi and Hirano 2006, Nishiyama et al. 2010, Zhang et al. 2011). At centromeres, kinetochore proteins shugoshins (SGOL1 and SGOL2) enable PP2A-B56 (also a kinetochore constituent) to dephosphorylate the STAG2 subunit of centromeric cohesin. Dephosphorylation of STAG2 enables maintenance of centromeric cohesion, thus preventing separation of sister chromatids until anaphase (Salic et al. 2004, Kitajima et al. 2004, Kitajima et al. 2005, Kitajima et al. 2006).
Proteolytic PAK-2p34 fragment translocates to the nucleus
Protein levels of condensin subunits are constant during the cell cycle. Four subunits, SMC4, NCAPD2, NCAPG and NCAPH, are phosphorylated in interphase cells (Takemoto et al. 2004) by CK2 i.e. casein kinase II (Takemoto et al. 2006). Except for the phosphorylation of NCAPH subunit on serine residue S570, CK2 phosphorylation sites in condensin I subunits have not been identified. Phosphorylation by CK2 inhibits condensin I-mediated introduction of positive supercoils into DNA and chromatin condensation. Mitotic activation of condensin I involves removal of phosphate groups added by CK2 (Takemoto et al. 2006), but the responsible phosphatase has not been identified.
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beta-Ureidopropionase deficiency: an inborn error of pyrimidine degradation associated with neurological abnormalities
L-2-Hydroxyglutaric aciduria: identification of a mutant gene C14orf160, localized on chromosome 14q22.1
Wapl controls the dynamic association of cohesin with chromatin
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
Retrovirally mediated complementation of the glyB phenotype. Cloning of a human gene encoding the carrier for entry of folates into mitochondria.
Wnts need a p(assport)24 to leave the ER
Essential requirement for two-pore channel 1 in NAADP-mediated calcium signaling
Establishment of Sister Chromatid Cohesion
Structural and biochemical aspects of keratan sulphate in the cornea
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The substrate of Greatwall kinase, Arpp19, controls mitosis by inhibiting protein phosphatase 2A
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Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is essential for mitosis
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The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria
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p24 proteins are required for secretion of Wnt ligands
SLC25A10, the mitochondrial dicarboxylate carrier protein in the inner mitochondrial membrane, mediates the reversible exchange of mitochondrial malate for cytosolic phosphate (Fiermonte et al. 1999).
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).
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).
Sulfate leaves the mitochondrion with the help of the dicarboxylate carrier, via antiport with malate (Crompton et al. 1974, Fiemont et al. 1999)
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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).
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SLC43A2 (LAT4), associated with the plasma membrane, mediates the uptake of isoleucine, leucine, methionine, phenylalanine, and valine in a biphasic and sodium ion-independent transport process. Northern blotting and in situ hybridization experiments indicate gene expression in kidney and intestine (Bodoy et al. 2005).
SLC7A2, isoform B, mediates the uptake of cationic amino acids across the plasma membranes of non-epithelial cells (Broer 2008; Closs et al. 1997; Furesz et al. 2002).
SLC7A3 mediates the uptake of cationic amino acids across the plasma membranes of non-epithelial cells (Vekony et al. 2001).
SLC7A1 mediates the uptake of cationic amino acids across the plasma membranes of non-epithelial cells (Broer 2008; Closs et al. 1997; Furesz et al. 2002; Kamath et al. 1999).
SLC7A2, isoform A, mediates the uptake of cationic amino acids across the plasma membranes of non-epithelial cells (Broer 2008; Closs et al. 1997).
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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 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.
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.
Rhodopsin (RHO) is localised to both the disc membrane and the plasma membrane of rod outer segments (ROS). All-trans-retinal (atRAL) released from rhodopsin during the bleaching process, needs to translocate to the cytosol for reduction to all-trans-retinol (atROL) via all-trans-retinol dehydrogenases. Although atRAL can diffuse through membranes unaided, there exists an ABC transporter on disc membranes which may facilitate the transport of excess atRAL. Retinal-specific ATP-binding cassette transporter (ABCA4, ABCR) is the only ABC transporter which mediates the transport of retinoids (Biswas & Biswas 2000). Studies using bovine ABCA4 demonstrates atRAL transport (Sun et al. 1999). Human ABCR was found to be identical to the ABC transporter linked to Stargardt's disease type 1 (STGD1, MIM:248200), a cause of macular degeneration in childhood (Nasonkin et al. 1998).
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).
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SLC43A1 (LAT3), associated with the plasma membrane, mediates the uptake of isoleucine, leucine, methionine, phenylalanine, and valine in a biphasic and sodium ion-independent transport process. Northern blotting experiments indicate gene expression in liver, pancreas, and skeletal muscle, and at lower levels in many tissues including kidney and intestine (Babu et al. 2003).
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Stimulator of IFN gene is critical for induction of IFN-beta during Chlamydia muridarum infection
ABCG5/8 in the plasma membrane mediates the ATP-dependent export of cytosolic sterols (cholesterol and phytosterols). Mutations affecting the ABCG5/8 proteins are associated with the accumulation of high levels of cholesterol and phytosterols in the body, demonstrating the specificity and physiological importance of this process (Berge et al. 2000). Human ABCG5/8 has not been studied in detail, but the homologous mouse protein complex mediate ATP-dependent sterol export (Wang et al. 2006). The mouse proteins localize to the apical plasma membranes of enterocytes and hepatocytes, consistent with the hypothesis that in vivo ABCG5/8 mediates sterol export into the gut lumen and from hepatocytes into the bile (Graf et al. 2003).
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).
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.
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).
Physiology and pathophysiology of vascular signaling controlled by guanosine 3',5'-cyclic monophosphate-dependent protein kinase [corrected]
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cis-Delta(9,12)-octadecadienoyl-coenzyme A
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The renal plumbing system: aquaporin water channels
The Drosophila tweety family: molecular candidates for large-conductance Ca2+-activated Cl- channels
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Important role of cathepsin S in generating peptides for TAP-independent MHC class I crosspresentation in vivo
Human lysozyme gene mutations cause hereditary systemic amyloidosis
Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5
The Drosophila claret segregation protein is a minus-end directed motor molecule
U5 small nuclear ribonucleoprotein 200 kDa helicase
Small nuclear ribonucleoprotein associated proteins B and B'
U6 snRNA-associated Sm-like protein LSm2
Small nuclear ribonuclear protein D homolog
Lsm1-7-Pat1 complex: A link between 3' and 5'-ends in mRNA decay?
Mammalian Orc1 protein is selectively released from chromatin and ubiquitinated during the S-to-M transition in the cell division cycle.
High Km soluble 5'-nucleotidase from human placenta
Pre-mRNA splicing factor PRP17 (hPRP17) (EH-binding protein 3) (Ehb3)
U4/U6 small nuclear ribonucleoprotein Prp4
116 kDa U5 small nuclear ribonucleoprotein component (U5 snRNP- specific protein, 116 kDa) (U5-116 kDa)
116 kDa U5 small nuclear ribonucleoprotein component
Hypothetical UPF0123 protein BK223H9.2/MGC1346
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)
Pre-mRNA splicing factor SF3b 10 kDa subunit
Regulation of Insulin Secretion by Acetylcholine
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
Hypothetical protein CGI-110 (Protein HSPC175)
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 145 kDa subunit
Splicing factor 3B subunit 2 (Spliceosome associated protein 145) (SAP 145) (SF3b150) (Pre-mRNA splicing factor SF3b 145 kDa subunit)
Actin cytoskeletal dynamics in smooth muscle: a new paradigm for the regulation of smooth muscle contraction
New regulatory mechanisms of TGF-beta receptor function
Studies on the activator 1 protein complex, an accessory factor for proliferating cell nuclear antigen-dependent DNA polymerase delta.
Abnormal conversion of 2-oxoglutarate to 2-hydroxyglutarate
benzoate + Coenzyme A + ATP => benzoyl-CoA + AMP + pyrophosphate
Benzoate and Coenzyme A react to form benzoyl-CoA thioester
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Localization and trafficking of aquaporin 2 in the kidney
Trimethylamine N-oxidised to Trimethylamine-N-oxide
FMO3 N-oxidizes the tertiary amine trimethylamine
acetate + CoA + ATP => acetyl-CoA + AMP + pyrophosphate [mitochondrial]
FMO1 N-oxidizes the anti-cancer drug tamoxifen
FMO2 S-oxidizes the antithyroid drug methimazole
gamma-glutamylcysteine combines with glycine to form glutathione
GST dimers conjugate GSH with cytosolic substrates
Glutathione conjugation of cytosolic substrates
DNA-directed RNA polymerase II 140 kDa polypeptide
Adenosine 3',5'-bisphosphate (PAP) + H2O => AMP + orthophosphate
S-atom dealkylation of 6-methylmercaptopurine
Transcription initiation factor IIF, beta subunit
DNA polymerase epsilon, catalytic subunit A
salicylic acid + Coenzyme A + ATP => salicylate-CoA + AMP + pyrophosphate
Salicylic acid and Coenzyme A react to form salicylate-CoA thioester
phenylacetate + Coenzyme A + ATP => phenylacetyl-CoA + AMP + pyrophosphate
Synthesis of phenylacetyl CoA from phenylacetate and Coenzyme A
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Transcription initiation factor IIF, alpha subunit
DNA-directed RNA polymerase II 33 kDa polypeptide
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DNA-directed RNA polymerase II 14.5 kDa polypeptide
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Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA
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Mitoferrin Transports Iron Across the Mitochondrial Inner Membrane
Transfer of Electrons from NADPH to FDXR
Transfer of Electrons from FDXR to FDX1/1L
FXN:NFS1:ISD11:ISCU Synthesizes Iron-Sulfur Cluster
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
Passive Transport of Carbon Dioxide into the Cell by RhAG
Passive Transport of Carbon Dioxide out of the Cell by RhAG
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
abacavir [cytosol] + ATP + H2O => abacavir[extracellular] + ADP + phosphate
General transcription factor IIH polypeptide 1
TFIIH basal transcription factor complex p62 subunit
Basic transcription factor 62 kDa subunit
DNA-directed RNA polymerase II 19 kDa polypeptide
abacavir monophosphate + H2O => carbovir monophosphate + cyclopropylamine
Deamination of abacavir monophosphate to form carbovir monophosphate
DNA-directed RNA polymerase II 16 kDa polypeptide
DNA-directed RNA polymerase II 13.3 kDa polypeptide
carbovir monophosphate + ATP => carbovir diphosphate + ADP
Phosphorylation of carbovir monophosphate
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carbovir + IMP => carbovir monophosphate + inosine
Conversion of carbovir to carbovir monophosphate
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
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A structural change in the kinesin motor protein that drives motility
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Four PBGs combine through deamination to form hydroxymethylbilane (HMB)
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ALAD octamer associates with Pb++, forming a catalytically inactive complex
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Two molecules of ALA condense to form porphobilinogen (PBG)
Succinyl CoA and glycine condense to form 5-aminolevulinate (ALA)
ALAS condenses SUCC-CoA and Gly to form dALA
Polynucleotide adenylyltransferase alpha
Persulfide sulfur is transferred onto sulfite
Excess cysteine yields lanthionine and H2S
SQR oxidizes sulfide to bound persulfide
Excess homocysteine yields homolanthionine and H2S
80 kDa nuclear cap binding protein (NCBP 80 kDa subunit) (CBP80)
20 kDa nuclear cap binding protein (NCBP 20 kDa subunit) (CBP20) (NCBP interacting protein 1) (NIP1)
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)
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
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)
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
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Ethylene is oxidized to Ethylene oxide by CYP1A1
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Ferrous iron is inserted into protoporphyrin IX to form heme
Cleavage and polyadenylation specificity factor, 160 kDa subunit
High mobility group-like nuclear protein 2 homolog 1
Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism.
Spliceosomal U5 snRNP-specific 15 kDa protein
Thioredoxin-like U5 snRNP protein U5-15kD
Uroporphyrinogen III is decarboxylated to form coproporphyrinogen III
Uroporphyrinogen I is decarboxylated to form coproporphyrinogen I
Conversion of coproporphyrinogen III to protoporphyrinogen IX
Cleavage and polyadenylation specificity factor, 73 kDa subunit
Oxidation of protoporphyrinogen IX to protoporphyrin IX
Cleavage and polyadenylation specificity factor, 100 kDa subunit
Pre-mRNA cleavage complex II protein Clp1
Cleavage stimulation factor, 50 kDa subunit
The NOD: a signaling module that regulates apoptosis and host defense against pathogens
Cleavage stimulation factor, 64 kDa subunit
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PPARs: therapeutic targets for metabolic disease
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Thyroxine is deiodinated to triiodothyronine
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DIT and MIT combine to form triiodothyronine
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Nuclear factor 1 (NF1) affects accurate termination and multiple-round transcription by human RNA polymerase III.
glycine + O2 => glyoxylate + H2O2 + NH4+
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Binding of a novel SMG-1-Upf1-eRF1-eRF3 complex (SURF) to the exon junction complex triggers Upf1 phosphorylation and nonsense-mediated mRNA decay
glyoxylate + NADPH + H+ => glycolate + NADP+
glyoxylate + alanine => glycine + pyruvate [peroxisome]
SAM is sythesized from methionine's reaction with ATP
Cystathionine is formed from homocysteine and serine
Dock6, a Dock-C subfamily guanine nucleotide exchanger, has the dual specificity for Rac1 and Cdc42 and regulates neurite outgrowth
Homocysteine is degraded to oxobutanoate and H2S
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Genomic organization of the human phosphomannose isomerase (MPI) gene and mutation analysis in patients with congenital disorders of glycosylation type Ib (CDG-Ib)
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Structure and sequence of the human alpha-L-iduronidase gene
L-glutamate gamma-semialdehyde + NAD+ => glutamate + NADH + H+
fumarylacetoacetate => fumarate + acetoacetate
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2-amino-3-carboxymuconate semialdehyde => 2-aminomuconate semialdehyde + CO2
3-hydroxyanthranilate + O2 => 2-amino-3-carboxymuconate semialdehyde
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3-hydroxykynurenine + H2O => 3-hydroxyanthranilate + alanine
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kynurenine + O2 + NADPH + H+ => 3-hydroxykynurenine + NADP+ + H2O
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kynurenine + pyruvate => 4-(2-aminophenyl)-2,4-dioxobutanoic acid + alanine [CCBL2]
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kynurenine + pyruvate => 4-(2-aminophenyl)-2,4-dioxobutanoic acid + alanine [CCBL1]
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tryptophan + O2 => N-formylkynurenine [TDO]
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DNA polymerase alpha holoenzyme-associated protein P1
Integrating signals from RTKs to ERK/MAPK
Proteoglycans and Sulfated Glycosaminoglycans
Origin recognition complex subunit Latheo
glutamate + acetyl CoA => N-acetyl glutamate + CoA
kynurenine + 2-oxoglutarate => 4-(2-aminophenyl)-2,4-dioxobutanoic acid + glutamate
S-Adenosyl methionine <=> Decarboxylated-Adenosyl methionine + CO2
ornithine (cytosolic) + citrulline (mitochondrial) => ornithine (mitochondrial) + citrulline (cytosolic)
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Methylthio-ribose-P = Methylthio-ribulose-P
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Putrescine + dc-Adenosyl methionine => Spermidine + 5'-methylthioadenosine
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Methylthio-ribulose-P = Methylthio-ribose-P
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Cell division protein kinase 2 (EC 2.7.1.-)(p33 protein kinase)(CDK2)
Cell division cycle 7-related protein kinase
Cell division cycle 7-related protein kinase (EC 2.7.1.-) (CDC7- related kinase) (HsCdc7) (huCdc7)
Role of the CCAAT enhancer binding proteins (C/EBPs) in adipocyte differentiation
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Point mutations in the aromatic/arginine region in aquaporin 1 allow passage of urea, glycerol, ammonia, and protons
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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).
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).
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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).
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Calcium (Ca2+) can be mobilised from intracellular stores by the presence of nicotinic acid adenine dinucleotide phosphate (NAADP). Two pore calcium channel proteins 1 and 2 (TPCN1 and 2) are expressed on endosomal (not shown here) and lysosomal membranes and mediate the mobilization of Ca2+ from these organelles when activated by NAADP (Brailoiu et al. 2009, Calcraft et al. 2009).
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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).
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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).
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GABA is converted to succinate semialdehyde by 4-aminobutyrate aminotransferase
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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).
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).
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The anaphase-promoting complex: a key factor in the regulation of cell cycle
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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).
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The efflux pump ABCG2 can relieve cells from toxic heme concentrations even against a concentration gradient. It is expressed in placenta, liver, and small intestine (Krishnamurthy et al, 2004; Doyle & Ross, 2003; Zhang et al, 2003).
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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.
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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.
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The human gene ATP7A (MNK) encodes the copper-transporting ATPase 1 (ATP7A, ATPase1, Menkes protein) which is expressed in most tissues except the liver (Vulpe et al, 1993; Chelly et al, 1993). Normally, ATP7A resides on the trans-Golgi membrane (Dierick et al, 1997). When cells are exposed to excessive copper levels, it is rapidly relocalized to the plasma membrane where it functions in copper efflux (Petris and Mercer, 1999). Defects in ATP7A are the cause of Menkes disease (MNKD), an X-linked recessive disorder of copper metabolism characterized by generalized copper deficiency (Ambrosini and Mercer, 1999).
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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).
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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).
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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.
Coexpression of glucose transporters and glucokinase in Xenopus oocytes indicates that both glucose transport and phosphorylation determine glucose utilization
The way Wnt works: Components and mechanism
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Cdc42, Rac1, and Rac2 display distinct patterns of activation during phagocytosis
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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).
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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).
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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.
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.
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.
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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.
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.
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.
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.
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.
The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor 5A (eIF5A)
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Human sphingosine-1-phosphate lyase: cDNA cloning, functional expression studies and mapping to chromosome 10q22(1)
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CaMKIV is activated in a multi-step mechanism in an Ca2+/Calmodulin dependent manner.
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.
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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.
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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.
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.
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.
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.
The Rhesus (Rh) glycoproteins were originally described in human blood cells as potent immunogens. There are three Rh glycoproteins in humans; an erythroid-specific Rh-associated glycoprotein (RhAG) and two non-erythroid Rh glycoproteins, RhBG and RhCG. These proteins are related to ammonium (NH4+) transporters of yeast and bacteria (methylammonium and ammonium permease and ammonium transporter, MEP/Amt) (Nakhoul NL and Hamm LL, 2004; Planelles G, 2007).
The human gene RhCG encodes the Rhesus blood group family type C glycoprotein which is mainly expressed in kidney collecting duct but also found in testis. RhCG is located on the apical membrane and mediates the bi-directional transport of ammonium into and out of renal collecting duct cells in an electroneutral manner, with H+ transported the other way (Liu Z et al, 2000; Marini AM et al, 2000).
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.
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).
N-formiminoglutamate + tetrahydrofolate => glutamate + 5-formiminotetrahydrofolate
lysine + alpha-ketoglutarate +NADPH + H+ => saccharopine + NADP+ + H2O
urocanate + H2O => 4-imidazolone-5-propionate
4-imidazolone-5-propionate + H2O => N-formiminoglutamate + 2H+
Molecular analysis of digenic inheritance in Bartter syndrome with sensorineural deafness
Amyloid beta-protein: monomer structure and early aggregation states of Abeta42 and its Pro19 alloform
Barttin modulates trafficking and function of ClC-K channels
Proc. Natl. Acad. Sci. U.S.A. 103:11411-6
beta-hydroxyisobutyrate + NAD+ <=> methylmalonyl semialdehyde + NADH + H+
beta-hydroxyisobutyryl-CoA + H2O => beta-hydroxyisobutyrate + CoA
isobutyryl-CoA + FAD => methacrylyl-CoA + FADH2
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).
Cloning and expression of a human choline/ethanolaminephosphotransferase: synthesis of phosphatidylcholine and phosphatidylethanolamine
alpha-methyl-acetoacetyl-CoA + CoA => propionyl-CoA + acetyl-CoA
Carrier-mediated urea transport allows rapid urea movement across the cell membrane, which is particularly important in the process of urinary concentration and for rapid urea equilibrium in non-renal tissues. Two carriers exist in humans, HUT2 which is renal-specific (Olives B et al, 1996) and HUT11, which is erythrocyte-specific (Olives B et al, 1994).
The human gene RhAG encodes a Rhesus blood group family type A glycoprotein which is expressed specifically in erythroid cells. It is thought to mediate ammonium export from these cells (Marini AM et al, 2000; Westhoff CM et al, 2002). Defects in RHAG are the cause of regulator type Rh-null hemolytic anemia (RHN) (Rh-deficiency syndrome). RHN is a form of chronic hemolytic anemia (Hyland CA et al, 1998).
The human gene RhBG encodes a Rhesus blood group family type B glycoprotein which is expressed mainly in the kidney but is also found in the liver. The liver and kidney are important tissues for ammonium metabolism and excretion. RhBG is located on the basolateral membrane and mediates the reversible transport of ammonium in and out of renal collecting duct cells in an electroneutral manner, with H+ transported the other way (Ludewig U, 2004; Liu Z et al, 2001).
methylmalonate semialdehyde + NAD+ + CoA => propionyl-CoA + CO2 + NADH + H+
methylmalonyl semialdehyde + NADH + H+ <=> beta-hydroxyisobutyrate + NAD+
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 proteins1â14, 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 1â10, 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)
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).
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).
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).
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alpha-methylbutyryl-CoA + FAD => tiglyl-CoA + FADH2
alpha-methyl-beta-hydroxybutyryl-CoA + NAD+ <=> alpha-methylacetoacetyl-CoA + NADH + H+
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alpha-methylacetoacetyl-CoA + NADH + H+ <=> alpha-methyl-beta-hydroxybutyryl-CoA + NAD+
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.
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Sequence of the human erythrocyte phosphoglycerate mutase by microsequencer and mass spectrometry
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 [BCAT1]
The human gene SLC30A2 encodes zinc transporter ZnT2. Its function is inferred from experiments using rat Znt2 (Palmiter RD et al, 1996).
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
a-ketoisocaproate, a-keto-b-methylvalerate, or a-ketoisovalerate + glutamate <=> leu, ile, or val + alpha-ketoglutarate [BCAT2]
beta-methylcrotonyl-CoA + ATP + CO2 <=> beta-methylglutaconyl-CoA + ADP + orthophosphate + H2O [MCCA]
The human gene SLC30A7 encodes the zinc transporter ZnT7. It is thought to be present in the small intestine and lung in humans (Kirschke CP and Huang L, 2003). Functional properties assigned to ZnT7 are based on studies conducted with mouse experiments.
isovaleryl-CoA + FAD => beta-methylcrotonyl-CoA + FADH2
The human SLC30A8 gene encodes the zinc transporter ZnT8 which is specifically expressed in pancreatic beta cells. 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).
Beta oxidation of octanoyl-CoA to hexanoyl-CoA
beta-methylglutaconyl-CoA + H2O <=> beta-hydroxy-beta-methylglutaryl-CoA
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).
beta-methylglutaconyl-CoA + ADP + orthophosphate + H2O <=> beta-methylcrotonyl-CoA + ATP + CO2 [MCCA]
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.
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.
Mechanisms of human DNA repair: an update.
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 transport of nucleotide sugars such as UDP-GlcNAc and UDP-glucose into the Golgi lumen in exchange for UMP (Suda et al. 2004, Ishida et al. 2005).
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).
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).
maleylacetoacetate => fumarylacetoacetate
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.
homogentisate + O2 => maleylacetoacetate
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 7 TM G-protein-coupled receptor target family
p-hydroxyphenylpyruvate + O2 => homogentisate + CO2
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).
p-hydroxyphenylpyruvate + glutamate <=> tyrosine + alpha-ketoglutarate
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).
tyrosine + alpha-ketoglutarate <=> p-hydroxyphenylpyruvate + glutamate
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).
phenylalanine + pyruvate => 3-(indol-3-yl)pyruvate + alanine
phenylalanine + tetrahydrobiopterin + O2 => tyrosine + 4a-hydroxytetrahydrobiopterin + H2O
4a-hydroxytetrahydrobiopterin => q-dihydrobiopterin + H2O
q-dihydrobiopterin + NADH + H+ => tetrahydrobiopterin + NAD+
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.
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glutaryl-CoA + FAD => crotonyl-CoA + FADH2 + CO2
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).
Dual role of the tyrosine activation motif of the Ig-alpha protein during signal transduction via the B cell antigen receptor
Oxidative decarboxylation of alpha-ketoadipate to glutaryl CoA by alpha-ketoglutarate dehydrogenase
alpha-ketoadipate + CoASH + NAD+ => glutaryl-CoA + CO2 + NADH + H+
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).
2-oxoglutarate [mitochondrial matrix] + 2-oxoadipate [cytosol] <=> 2-oxoglutarate [cytosol] + 2-oxoadipate [mitochondrial matrix]
Exchange of cytosolic 2-oxoadipate for mitochondrial 2-oxoglutarate
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.
alpha-aminoadipic semialdehyde + NAD+ => alpha-aminoadipate + NADH + H+
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.
saccharopine + NAD+ + H2O => alpha-aminoadipic semialdehyde + glutamate + NADH + H+
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.
alpha-ketoadipate + glutamate <=> alpha-aminoadipate + alpha-ketoglutarate
alpha-aminoadipate + alpha-ketoglutarate <=> alpha-ketoadipate + glutamate
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.
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Calmodulin-kinases: modulators of neuronal development and plasticity
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Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution
Conserved initiator proteins in eukaryotes.
The known unknowns of antigen processing and presentation
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Identification and characterization of a novel ABCA subfamily member, ABCA12, located in the lamellar ichthyosis region on 2q34
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Different human TFIIIB activities direct RNA polymerase III transcription from TATA-containing and TATA-less promoters
Glycogen metabolism and glycolytic enzymes
Structural basis for featuring of steroid isomerase activity in alpha class glutathione transferases
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Single eubacterial origin of eukaryotic sulfide:quinone oxidoreductase, a mitochondrial enzyme conserved from the early evolution of eukaryotes during anoxic and sulfidic times
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Resistance exercise and insulin regulate AS160 and interaction with 14-3-3 in human skeletal muscle
Understanding RAGE, the receptor for advanced glycation end products
Constitutive and inducible expression and regulation of vascular endothelial growth factor
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AS160 phosphotyrosine-binding domain constructs inhibit insulin-stimulated GLUT4 vesicle fusion with the plasma membrane
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Mutations in GLUT2, the gene for the liver-type glucose transporter, in patients with Fanconi-Bickel syndrome
STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling
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Regulation and cellular roles of phosphoinositide 5-kinases
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TMEM16A confers receptor-activated calcium-dependent chloride conductance
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Distinct RIG-I and MDA5 signaling by RNA viruses in innate immunity
EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimming
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ATP-dependent positive supercoiling of DNA by 13S condensin: a biochemical implication for chromosome condensation
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Biology, structure and mechanism of P-type ATPases
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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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Mitochondrial association of a plus end-directed microtubule motor expressed during mitosis in Drosophila
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Loading of an Mcm protein onto DNA replication origins is regulated by Cdc6p and CDKs.
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Vav-family proteins in T-cell signalling
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Removal of DNA patch containing abasic residue
Wild-type p53 is a cell cycle checkpoint determinant following irradiation.
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
Molecular cloning, cDNA sequence, and bacterial expression of human glutamine:fructose-6-phosphate amidotransferase
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Chromosome condensation-related SMC-associated protein 1
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Structural maintenance of chromosomes protein 4
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Structural maintenance of chromosomes protein 2
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Phosphoenolpyruvate carboxykinase, cytosolic (GTP)
phosphoenolpyruvate carboxykinase 1 (soluble)
Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing
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Regulation of Lipid Metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha)
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Evidence for a zinc uptake transporter in human prostate cancer cells which is regulated by prolactin and testosterone
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Serine/threonine-protein kinase greatwall
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Kinetic analysis of peptide binding to the TAP transport complex: evidence for structural rearrangements induced by substrate binding
Mitotic Golgi partitioning is driven by the membrane-fissioning protein CtBP3/BARS
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Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein.
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Structural maintenance of chromosome 1-like 1 protein (SMC1alpha protein) (SB1.8/DXS423E protein) (Sb1.8)
Structural maintenance of chromosome 1-like 1 protein
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Multimeric structure of ClC-1 chloride channel revealed by mutations in dominant myotonia congenita (Thomsen)
Double-strand-break repair protein rad21 homolog
Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
A phosphoribosyl group is added to nicotinate to form nicotinate mononucleotide (NaMN)
Serine/threonine protein phosphatase 2B catalytic subunit, alpha isoform
Nicotinate D-ribonucleotide + ATP => deamino-NAD+ + pyrophosphate [NMNAT3]
Nicotinate D-ribonucleotide + ATP => deamino-NAD+ + pyrophosphate [NMNAT1]
Nicotinate D-ribonucleotide + ATP => deamino-NAD+ + pyrophosphate [NMNAT2]
Kinetics of B cell receptor signaling in human B cell subsets mapped by phosphospecific flow cytometry
DHF is reduced to tetrahydrofolate (THF)
Conversion of cytosolic THF to THF-polyglutamate
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Extracellular 5-methyltetrahydrofolate import across the plasma membrane
Phosphorylation of 2',3'-dideoxyinosine by cytosolic 5'-nucleotidase of human lymphoid cells
Folate is reduced to dihydrofolate (DHF)
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Protein phosphatase 3 regulatory subunit B alpha isoform 1
Protein phosphatase 2B regulatory subunit 1
Conversion of mitochondrial THF to THF-polyglutamate
Solute carrier family 2, facilitated glucose transporter, member 2
Diabetes-associated sustained activation of the transcription factor nuclear factor-kappaB
THF polyglutamate + formate + ATP => 10-formylTHF polyglutamate + ADP + orthophosphate
10-formylTHF polyglutamate <=> 5,10-methenylTHF polyglutamate + H2O
5,10-methenylTHF polyglutamate + NADPH + H+ <=> 5,10-methyleneTHF polyglutamate + NADP+
Conversion of cytosolic 5-methyltetrahydrofolate (5-methylTHF) to 5-methylTHF-polyglutamate
Cytosolic tetrahydrofolate import across the inner mitochondrial membrane
Mitochondrial tetrahydrofolate export across the inner mitochondrial membrane
5,10-methyleneTHF polyglutamate + NADPH + H+ => 5-methylTHF polyglutamate + NADP+
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5,10-methyleneTHF polyglutamate + NADP+ <=> 5,10-methenylTHF polyglutamate + NADPH + H+
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5,10-methenylTHF polyglutamate + H2O <=> 10-formylTHF polyglutamate
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Molecular mechanisms and clinical pathophysiology of maturity-onset diabetes of the young
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Transfer of sulfur from MOCS3-S-S onto MOCS2A
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Sulfhydrylation and ring cleavage of precursor Z
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NFS1 transfers sulfur from cysteine onto MOCS3
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alanine + alpha-ketoglutarate <=> pyruvate + glutamate [GPT]
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).
Calcium/calmodulin-dependent protein kinase type IV catalytic chain
Calcium/calmodulin-dependent protein kinase type IV catalytic chain (EC 2.7.1.123) (CAM kinase-GR) (CaMK IV)
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pyruvate + glutamate <=> alanine + alpha-ketoglutarate [GPT]
Molybdenum ion transfer onto molybdopterin
The reversible transport of extracellular fructose into the cytosol is mediated by GLUT5. In the small intestine, GLUT5 is localized on the lumenal surfaces of enterocytes (Davidson et al. 1992) and thus mediates the uptake of dietary fructose, which can be released into the circulation in a separate transport step mediated by basolaterally localized GLUT2. The specificity of GLUT5 has been worked out by studying sugar transport in Xenopus oocytes expressing recombinant human GLUT5 protein (Burant et al. 1992).
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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 Clâ-dependent transport of basic anions [e.g. HCO3â, (CO3)2â] 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 Clâ ion electroneutral symporters (Hebert SC et al, 2004); SLC26 is the trans-epithelial multifunctional anion (e.g. sulfate, oxalate, HCO3â, Clâ) 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)2â 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)â 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.
alanine + alpha-ketoglutarate <=> pyruvate + glutamate [GPT2]
pyruvate + glutamate <=> alanine + alpha-ketoglutarate [GPT2]
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A genome-wide RNA interference screen uncovers two p24 proteins as regulators of Wingless secretion
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The reversible facilitated diffusion of fructose, galactose, and glucose from the cytosol to the extracellular space is mediated by the GLUT2 transporter in the plasma membrane. In the epithelial cells of the small intestine, the basolateral localization of GLUT2 (Thorens et al. 1990) enables hexose sugars derived from the diet and taken up by the action of the SGLT1 and GLUT5 transporters to be released into the circulation. The specificity of the GLUT2 transporter has been established directly through biochemical assays of purified recombinant proteins (Colville et al. 1993; Wu et al. 1998) and indirectly through studies of patients deficient in GLUT2 transporter protein (Santer et al. 1997).
GLUT (glucose transporter) homotetramers associated with the plasma membrane mediate the facilitated diffusion of glucose between the extracellular space and the cytosol. Four human GLUT isoforms have been identified, members of a larger family of transporter proteins (Joost et al. 2002), encoded by the SCLC2A1, 2, 3, and 4 genes. Conserved sequence motifs in the GLUT proteins suggest the existence of shared structural features confirmed by in situ labeling and mutagenesis studies. Each GLUT protein has twelve membrane spanning domains organized to form an aqueous channel. While monomeric protein can form such a channel and transport glucose, kinetic studies suggest that the functional form of the protein is a homotetramer. Different GLUT proteins are expressed in different tissues. GLUT1 is expressed by many cell types, notably endothelial cells, red blood cells and cells of the brain. Its low Km for glucose (~1 mM) relative to normal blood glucose concentration (~5 mM) allows these cells to take up glucose independent of changes in blood glucose levels. Its abundance in red blood cells has allowed it to be purified and biochemically characterized (Hruz and Mueckler 2001; Liu et al. 2001). Cytosolic ATP associates with GLUT1 and inhibits its glucose transporter activity. GLUT2 is expressed on hepatocytes and pancreatic beta cells. Because of its high Km for glucose (~15-20 mM), GLUT2-mediated glucose uptake normally occurs only in the fed state, when its rate is proportional to blood glucose concentration. This feature of the transporter is thought to enable efficient uptake of large amounts of glucose by the liver in the fed state, and to allow it to function as part of a glucose sensor coupled to insulin release in pancreatic beta cells (Thorens 2001). GLUT2 also mediates glucose export from liver cells when gluconeogenesis is underway (Colville et al. 1993; Santer et al. 1997; Wu et al. 1998). GLUT3 is expressed by cells of the brain and possibly other cell types with a high constitutive requirement for glucose. Its low Km for glucose (~1.5 mM) allows these cells to import glucose independent of fluctuations in blood glucose levels (Colville et al. 1993). GLUT4, like GLUT1 and 3, has a high affinity for glucose. GLUT4 is abundant in cells of skeletal muscle and adipose tissue. GLUT4 molecules are translocated from an intracellular store to the cell surface in response to increased insulin levels (Bryant et al. 2002; Fukumoto et al. 1989).
GLUT2 (glucose transporter) homotetramers associated with the plasma membrane mediate the facilitated diffusion of glucose between the cytosol and the extracellular space, so glucose will leave cells when its intracellular concentration exceeds the extracellular one (Colville et al. 1993; Santer et al. 1997; Wu et al. 1998). In the body, such glucose export is a normal feature of liver cells when gluconeogenesis or glycogen breakdown is underway.
Cytosolic ATP reversibly associates with GLUT1. This association inhibits GLUT1 glucose transport (Blodgett et al. 2007).
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oxaloacetate + glutamate <=> aspartate + alpha-ketoglutarate [GOT1]
GLUT1:ATP complexes reversibly dissociate, restoring the glucose transport activity of GLUT1 glucose transport, with the result that depletion of cellular ATP leads to increased glucose uptake (Blodgett et al. 2007).
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Cells take up glucose by facilitated diffusion, via glucose transporters (GLUTs) associated with the plasma membrane, a reversible reaction (Joost and Thorens 2001). Four tissue-specific GLUT isoforms are known. Glucose in the cytosol is phosphorylated by tissue-specific kinases to yield glucose 6-phosphate, which cannot cross the plasma membrane because of its negative charge. In the liver, this reaction is catalyzed by glucokinase which has a low affinity for glucose (Km about 10 mM) but is not inhibited by glucose 6-phosphate. In other tissues, this reaction is catalyzed by isoforms of hexokinase. Hexokinases are feedback-inhibited by glucose 6-phosphate and have a high affinity for glucose (Km about 0.1 mM). Liver cells can thus accumulate large amounts of glucose 6-phosphate but only when blood glucose concentrations are high, while most other tissues can take up glucose even when blood glucose concentrations are low but cannot accumulate much intracellular glucose 6-phosphate. These differences are consistent with the view that that the liver functions to buffer blood glucose concentrations, while most other tissues take up glucose to meet immediate metabolic needs. Glucose 6-phosphatase, expressed in liver and kidney, allows glucose 6-phosphate generated by gluconeogenesis (both tissues) and glycogen breakdown (liver) to leave the cell. The absence of glucose 6-phosphatase from other tissues makes glucose uptake by these tissues essentially irreversible, consistent with the view that cells in these tissues take up glucose for local metabolic use.
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Hexoses, notably fructose, glucose, and galactose, generated in the lumen of the small intestine by breakdown of dietary carbohydrate are taken up by enterocytes lining the microvilli of the small intestine and released from them into the blood. Uptake into enterocytes is mediated by two transporters localized on the lumenal surfaces of the cells, SGLT1 (glucose and galactose, together with sodium ions) and GLUT5 (fructose). GLUT2, localized on the basolateral surfaces of enterocytes, mediates the release of these hexoses into the blood (Wright et al. 2004). GLUT2 may also play a role in hexose uptake from the gut lumen into enterocytes when the lumenal content of monosaccharides is very high (e.g., Kellet and Brot-Laroche, 2005) and GLUT5 mediates fructose uptake from the blood into cells of the body, notably hepatocytes. Cells take up glucose by facilitated diffusion, via glucose transporters (GLUTs) associated with the plasma membrane, a reversible reaction. Four tissue-specific GLUT isoforms are known. Glucose in the cytosol is phosphorylated by tissue-specific kinases to yield glucose 6-phosphate, which cannot cross the plasma membrane because of its negative charge. In the liver, this reaction is catalyzed by glucokinase which has a low affinity for glucose (Km about 10 mM) but is not inhibited by glucose 6-phosphate. In other tissues, this reaction is catalyzed by isoforms of hexokinase. Hexokinases are feedback-inhibited by glucose 6-phosphate and have a high affinity for glucose (Km about 0.1 mM). Liver cells can thus accumulate large amounts of glucose 6-phosphate but only when blood glucose concentrations are high, while most other tissues can take up glucose even when blood glucose concentrations are low but cannot accumulate much intracellular glucose 6-phosphate. These differences are consistent with the view that that the liver functions to buffer blood glucose concentrations, while most other tissues take up glucose to meet immediate metabolic needs. Glucose 6-phosphatase, expressed in liver and kidney, allows glucose 6-phosphate generated by gluconeogenesis (both tissues) and glycogen breakdown (liver) to leave the cell. The absence of glucose 6-phosphatase from other tissues makes glucose uptake by these tissues essentially irreversible, consistent with the view that cells in these tissues take up glucose for local metabolic use.
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aspartate + alpha-ketoglutarate <=> oxaloacetate + glutamate [GOT2]
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ornithine + alpha-ketoglutarate <=> glutamate + L-glutamate gamma-semialdehyde [OAT]
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glutamate + L-glutamate gamma-semialdehyde <=> ornithine + alpha-ketoglutarate [OAT]
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aspartate + glutamine + ATP <=> asparagine + glutamate + AMP + pyrophosphate [ASNS]
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alpha-ketoglutarate + NH4+ + NAD(P)H + H+ <=> glutamate + NAD(P)+ [GLUD1]
Class II facilitative transporters consist of GLUT5, 7, 9 and 11 (Zhao FQ and Keating AF, 2007; Wood IS and Trayhurn P, 2003).
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glutamate + NAD(P)+ => alpha-ketoglutarate + NH4+ + NAD(P)H + H+ [GLUD1]
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).
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glutamine + pyruvate => 2-oxoglutaramate + alanine
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).
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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. GLUT1 was cloned from a HepG2 cell line (Mueckler M et al, 1985). GLUT1 is expressed by SLC2A1 mainly in brain and erythrocytes but is also expressed at lower levels in many other tissues containing endothelial and epithelial barriers. Defects in SLC2A1 are the cause of autosomal dominant GLUT1 deficiency syndrome which results in impaired glucose transport across the brain tissue barrier and is characterized by infantile seizures, delayed development and acquired microcephaly (Klepper J et al, 1999). 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).
3-phosphonooxypyruvic acid + L-glutamate = O-phospho-L-serine + 2-oxoglutarate
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Sanfilippo disease type D: deficiency of N-acetylglucosamine-6-sulfate sulfatase required for heparan sulfate degradation
Tripeptidyl peptidase II is the major peptidase needed to trim long antigenic precursors, but is not required for most MHC class I antigen presentation
The human gene family SLC47 encodes 2 multidrug and toxin extrusion (MATE) proteins. Mammalian MATE-type transporters are responsible for the final step in the excretion of metabolic waste and xenobiotic organic cations in the kidney and liver through electroneutral exchange of H(+). MATE1 is primarily expressed in the kidney and liver, where it is localized to the luminal membranes of the urinary tubules and bile canaliculi. When expressed in HEK293 cells, MATE1 mediates H(+)-coupled electroneutral exchange of various drugs (Otsuka M et al, 2005). MATE2 is a human kidney-specific H+/organic cation antiporter that is responsible for the tubular secretion of cationic drugs across the brush border membranes (Masuda S et al, 2006). Substrates for both MATEs include tetraethylammonium, 1-methyl-4-phenylpyridinium, cimetidine, metformin, creatinine, guanidine and procainamide (Tanihara Y et al, 2007).
Natural resistance-associated macrophage proteins (NRAMPs) regulates macrophage activation for antimicrobial activity against intracellular pathogens. They do this by mediating metal ion transport across macrophage membranes and the subsequent use of these ions in the control of free radical formation. The human gene SLC11A1 encodes NRAMP1 (Kishi F, 2004; Kishi F and Nobumoto M, 1995) which can utilize the protonmotive force to mediate divalent iron (Fe2+), zinc (Zn2+) and manganese (Mn2+) influx to or efflux from phagosomes.
Class III facilitative transporters consist of five members; GLUT6, 8, 10, 12 and HMIT (a H+/myo-inositol transporter). They possess a characteristic glycosylation site on loop 9 (found in loop 1 of classes I and II transporters). Four class III facilitative transporters can transport glucose. SLC2A6 encodes GLUT6, expressed mainly in brain, spleen and leucocytes (Doege H et al, 2000a). In literature, this protein is incorrectly described as GLUT9. SLC2A8 encodes GLUT8 and is expressed in brain, testis and adipose tissue (Doege H et al, 2000b). SLC2A10 (located in the Type 2 diabetes-linked region of human chromosome 20q12-13.1) encodes GLUT10, a transporter with high affinity for glucose (McVie-Wylie AJ et al, 2001) . GLUT10 is highly expressed in liver and pancreas but is present in most tissues in lower levels. Defects in SLC2A10 are the cause of arterial tortuosity syndrome (ATS), an autosomal recessive disorder characterized by tortuosity and elongation of major arteries, often resulting in death at a young age (Coucke PJ et al, 2006). SLC2A12 encodes GLUT12, which is highly expressed in skeletal muscle, heart and prostate, with lower levels in brain, placenta and kidney. It was originally cloned from the human breast cancer cell line MCF-7 (Rogers S et al, 2002).
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).
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leu, ile, or val + alpha-ketoglutarate <=> a-ketoisocaproate, a-keto-b-methylvalerate, or a-ketoisovalerate + glutamate [BCAT1]
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.
The human gene SLC30A1 encodes the zinc transporter ZnT1. It is widely expressed throughout the body and it's expression is regulated by zinc. ZnT1 is the only member of the SLC30 gene family that is located on the plasma membrane and mediates the transport of zinc out of the cell (Devergnas S et al, 2004).
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Mammalian nuclei become licensed for DNA replication during late telophase.
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ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57
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Pathway leading to correctly folded beta-tubulin
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Lead-induced abnormalities of porphyrin metabolism. The relationship with iron deficiency.
cAMP-dependent protein kinase type I-beta regulatory chain
cAMP-dependent protein kinase type I-alpha regulatory chain
Methylation pharmacogenetics: catechol O-methyltransferase, thiopurine methyltransferase, and histamine N-methyltransferase
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LMBRD1 transports lysosomal Cbl to cytosol
PLP from oxidation of pyridoxine phosphate
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MTR transfers CH3 group from MeCbl to HCYS
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MTR transfers CH3 group from MTHF to B12s
PLP from oxidation of pyridoxamine phosphate
Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals
PLP results from phosphorylation of pyridoxal
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Cytoslic carboxylases translocate to mitochondrial matrix
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A phospho-ribosyl group is added to quinolinate
MMAB transfers adenosyl group from ATP to B12s
ABCC1 transports cytosolic Cbl to extracellular region
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The cyclin-dependent kinase Cdc28p regulates distinct modes of Cdc6p proteolysis during the budding yeast cell cycle.
Spectrum of mutations in the major human skeletal muscle chloride channel gene (CLCN1) leading to myotonia
Rho guanine dissociation inhibitors: pivotal molecules in cellular signalling
LSm proteins form heptameric rings that bind to RNA via repeating motifs
Molecular genetics of mucopolysaccharidosis type IIIA and IIIB: Diagnostic, clinical, and biological implications
Molecular mechanisms of MHC class I-antigen processing: redox considerations
'L-Arg [cytosol]' positively regulates 'acetyl-CoA:L-glutamate N-acetyltransferase activity of NAGS(19-534) [mitochondrial matrix]'
'ADP [cytosol]' positively regulates 'glutamate dehydrogenase [NAD(P)+] activity of GLUD1 hexamer (name copied from entity in Homo sapiens) [mitochondrial matrix]'
'ATP [nucleoplasm]' positively regulates 'glutamate dehydrogenase [NAD(P)+] activity of GLUD1 hexamer (name copied from entity in Homo sapiens) [mitochondrial matrix]'
Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing
Glucagon-like peptide-1: regulation of insulin secretion and therapeutic potential
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An overview of sphingolipid metabolism: from synthesis to breakdown
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Cystic fibrosis transmembrane conductance regulator
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ATP-binding cassette sub-family A member 3
Synthesis of PIPs at the plasma membrane
Functional analysis of ABCA8, a new drug transporter
Differential activation of recombinant human acetyl-CoA carboxylases 1 and 2 by citrate
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Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes
Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2
ATP-binding cassette sub-family B member 6, mitochondrial
Multidrug resistance-associated protein 1
ATP-binding cassette sub-family B member 7, mitochondrial
Bone morphogenetic protein receptors and signal transduction
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ATP-binding cassette sub-family D member 2
ATP-binding cassette sub-family D member 3
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Mutations in HYAL1, a member of a tandemly distributed multigene family encoding disparate hyaluronidase activities, cause a newly described lysosomal disorder, mucopolysaccharidosis IX
Proc. Natl. Acad. Sci. U.S.A. 96:6296-300
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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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Identification and expression of a cDNA encoding human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD). A key enzyme for the tryptophan-niacine pathway and "quinolinate hypothesis".
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Water channel expression in human ADPKD kidneys
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Fractionation and properties of glutamic oxalacetic transaminase
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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
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Crystal structures of human TBC1D1 and TBC1D4 (AS160) RabGTPase-activating protein (RabGAP) domains reveal critical elements for GLUT4 translocation
Endoplasmic reticulum-associated degradation of mammalian glycoproteins involves sugar chain trimming to Man6-5GlcNAc2
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Na+-dependent purine nucleoside transporter from human kidney: cloning and functional characterization
Am J Physiol Renal Physiol 273:1058-1065
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Post-Elongation Processing of Intronless pre-mRNA
Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways
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N6-(L-1,3-Dicarboxypropyl)-L-lysine [ChEBI:16927]
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sn-Glycero-3-phosphoethanolamine [ChEBI:10647]
Structural basis for activation of G-protein-coupled receptors
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D-Glucono-1,5-lactone 6-phosphate [ChEBI:16938]
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Leber congenital amaurosis: genes, proteins and disease mechanisms
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Sinauer Associates, Inc., P.O. Box 407 23 Plumtree Road, Sunderland, MA 01375 U.S.A.
The stem cell factor receptor/c-Kit as a drug target in cancer
Critical role of novel Thr-219 autophosphorylation for the cellular function of PKCtheta in T lymphocytes
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The biochemistry and physiology of nucleotides
Detection of the mitochondrial and catalytically active alanine aminotransferase in human tissues and plasma
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ChEBI:16975 1-acyl-sn-glycerol 3-phosphate
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Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex
Human cationic amino acid transporter hCAT-3 is preferentially expressed in peripheral tissues
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Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes
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Analysis of the open region of RNA polymerase II transcription complexes in the early phase of elongation.
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Apoptosis and disease: a life or death decision
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Virus-cell fusion as a trigger of innate immunity dependent on the adaptor STING
Hereditary disorders of connective tissue
Abcg2/Bcrp1 mediates the polarized transport of antiretroviral nucleosides abacavir and zidovudine
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Multidrug resistance-associated protein 3
ATP-binding cassette sub-family C member 3
Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3
Multidrug resistance-associated protein 6
Multidrug resistance-associated protein 5
On the specificity of the tricarboxylate carrier system in rat liver mitochondria
ATP-binding cassette transporter sub-family C member 11
ATP-binding cassette sub-family A member 8
The RSK family of kinases: emerging roles in cellular signalling
Formation of tubulin folding intermediates by CCT/TriC
Dynamic binding of PKA regulatory subunit RI alpha
Retinal-specific ATP-binding cassette transporter
Formation of the Early Elongation Complex
Plk1 docking to GRASP65 phosphorylated by Cdk1 suggests a mechanism for Golgi checkpoint signalling
Large neutral amino acids transporter small subunit 3
Large neutral amino acids transporter small subunit 4
Characterization of a leukotriene C4 export mechanism in human platelets: possible involvement of multidrug resistance-associated protein 1
Mitochondrial dicarboxylate carrier protein
High affinity cationic amino acid transporter 1
Low affinity cationic amino acid transporter 2, isoform B
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The Src homology 2 domain containing inositol 5-phosphatase SHIP2 is recruited to the epidermal growth factor (EGF) receptor and dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-stimulated COS-7 cells
Solute carrier family 2, facilitated glucose transporter member 5
Regulation of human thymidine kinase during the cell cycle
Tyrosine phosphorylation of MB-1, B29, and HS1 proteins in human B cells following receptor crosslinking
Solute carrier family 2, facilitated glucose transporter, member 1
Glucose transporter type 1, erythrocyte/brain
Chapter 3 Activation of TRP Channels in Mammalian Systems
D-Fructose 1,6-bisphosphate [ChEBI:16905]
Post-transcriptional regulation of gene expression by degradation of messenger RNAs
Dephosphorylation and activation of a p34cdc2/cyclin B complex in vitro by human CDC25 protein
Sequence and structure of a human glucose transporter
Frequent and focal FGFR1 amplification associates with therapeutically tractable FGFR1 dependency in squamous cell lung cancer
Mechanisms of accurate translesion synthesis by human DNA polymerase eta.
The presence of reactive oxygen species (ROS) leads to the oxidation of thioredoxin and consequent release of TXNIP (Zhou et al. 2010). The source of the ROS is unclear but they are known to be essential for caspase-1 activation (Cruz et al. 2007) and are produced in response to all known NLRP3 activators (Dostert et al. 2008, Zhou et al. 2010). The freed TXNIP binds NLRP3 and is proposed to activate the NLRP3 inflammasome, explaining how ROS can bring about NLRP3 activation.
The NLRP3 (Cryopyrin) inflammasome is currently the best characterized. It consists of NLRP3, ASC (PYCARD) and procaspase-1; CARD8 (Cardinal) is also suggested to be a component. It is activated by a number of pathogens and bacterial toxins as well as diverse PAMPs, danger-associated molecular patterns (DAMPS) such as hyaluronan and uric acid, and exogenous irritants such as silica and asbestos (see Table S1 Schroder & Tschopp, 2010). Mutations in NLRP3 which lead to constitutive activation are linked to the human diseases Muckle-Wells syndrome, familial cold autoinflammatory syndrome and NOMID (Ting et al. 2006), characterized by skin rashes and other symptoms associated with generalized inflammation. The cause of these symptoms is uncontrolled IL-1 beta production. Multiple studies have shown that activation of the NLRP3 inflammasome by particulate activators (e.g. Hornung et al. 2008) requires phagocytosis, but this is not required for the response to ATP, which is mediated by the P2X7 receptor (Kahlenberg & Dubyak, 2004) and appears to involve the pannexin membrane channel (Pellegrin & Suprenenant 2006). Direct binding of activators to NLRP3 has not been demonstrated and the exact process of activation is unclear, though it is speculated to involve changes in conformation that free the NACHT domain for oligomerization (Inohara & Nunez 2001, 2003).
In contrast to NOD1/2 some NLRPs function as large macromolecular complexes called 'Inflammasomes'. These multiprotein platforms control activation of the cysteinyl aspartate protease caspase-1 and thereby the subsequent cleavage of pro-interleukin 1B (pro-IL1B) into the active proinflammatory cytokine IL1B. Activation of caspase-1 is essential for production of IL1B and IL18, which respectively bind and activate the IL1 receptor (IL1R) and IL18 receptor (IL18R) complexes. IL1R and IL18R activate NFkappaB and other signaling cascades. As the activation of inflammasomes leads to caspase-1 activation, inflammasomes can be considered an upstream step of the IL1R and IL18R signaling cascades, linking intracellular pathogen sensing to immune response pathways mediated by Toll-Like Receptors (TLRs). Monocytes and macrophages do not express pro-IL1B until stimulated, typically by TLRs (Franchi et al. 2009). The resulting pro-IL1B is not converted to IL1B unless a second stimulus activates an inflammasome. This requirement for two distinct stimuli allows tight regulation of IL1B/IL18 production, necessary because excessive IL-1B production is associated with numerous inflammatory diseases such as gout and rheumatoid arthritis (Masters et al. 2009). There are at least four subtypes of the inflammasome, characterized by the NLRP. In addition the protein AIM2 can form an inflammasome. All activate caspase-1. NLRP1 (NALP1), NLRP3 (Cryopyrin, NALP3), IPAF (CARD12, NLRC4) and AIM2 inflammasomes all have clear physiological roles in vivo. NLRP2, NLRP6, NLRP7, NLRP10 and NLRP12 have been demonstrated to modulate caspase-1 activity in vitro but the significance of this is unclear (Mariathasan and Monack, 2007). NLRP3 and AIM2 bind the protein 'apoptosis-associated speck-like protein containing a CARD' (ASC, also called PYCARD), via a PYD-PYD domain interaction. This in turn recruits procaspase-1 through a CARD-CARD interaction. NLRP1 and IPAF contain CARD domains and can bind procaspase-1 directly, though both are stimulated by ASC. Oligomerization of NLRPs is believed to bring procaspases into close proximity, leading to 'induced proximity' auto-activation (Boatright et al. 2003). This leads to formation of the active caspase tetramer. NLRPs are generally considered to be cytoplasmic proteins, but there is evidence for cytoplasmic-nuclear shuttling of the family member CIITA (LeibundGut-Landmann et al. 2004) and tissue/cell dependent NALP1 expression in the nucleus of neurons and lymphocytes (Kummer et al. 2007); the significance of this remains unclear.
The innate immune system is the first line of defense against invading microorganisms, a broad specificity response characterized by the recruitment and activation of phagocytes and the release of anti-bacterial peptides. The receptors involved recognize conserved molecules present in microbes called pathogen-associated molecular patterns (PAMPs), and/or molecules that are produced as a result of tissue injury, the damage associated molecular pattern molecules (DAMPs). PAMPs are essential to the pathogen and therefore unlikely to vary. Examples are lipopolysaccharide (LPS), peptidoglycans (PGNs) and viral RNA. DAMPs include intracellular proteins, such as heat-shock proteins and extracellular matrix proteins released by tissue injury, such as hyaluronan fragments. Non-protein DAMPs include ATP, uric acid, heparin sulfate and dsDNA. The receptors for these factors are referred to collectively as pathogen- or pattern-recognition receptors (PRRs). The best studied of these are the membrane-associated Toll-like receptor family. Less well studied but more numerous are the intracellular nucleotide-binding domain, leucine rich repeat containing receptors (NLRs) also called nucleotide binding oligomerization domain (NOD)-like receptors, a family with over 20 members in humans and over 30 in mice. These recognise PAMPs/DAMPs from phagocytosed microorganisms or from intracellular infections (Kobayashi et al. 2003, Proell et al. 2008, Wilmanski et al. 2008). Some NLRs are involved in process unrelated to pathogen detection such as tissue homeostasis, apoptosis, graft-versus-host disease and early development (Kufer & Sansonetti 2011). Structurally NLRs can be subdivided into the caspase-recruitment domain (CARD)-containing NLRCs (NODs) and the pyrin domain (PYD)-containing NLRPs (NALPs), plus outliers including ice protease (caspase-1) activating factor (IPAF) (Martinon & Tschopp, 2005). In practical terms, NLRs can be divided into the relatively well characterized NOD1/2 which signal via RIP2 primarily to NFkappaB, and the remainder, some of which participate in macromolecular structures called Inflammasomes that activate caspases. Mutations in several members of the NLR protein family have been linked to inflammatory diseases, suggesting these molecules play important roles in maintaining host-pathogen interactions and inflammatory responses. Most NLRs have a tripartite structure consisting of a variable amino-terminal domain, a central nucleotide-binding oligomerization domain (NOD or NACHT) that is believed to mediate the formation of self oligomers, and a carboxy-terminal leucine-rich repeat (LRR) that detects PAMPs/DAMPs. In most cases the amino-terminal domain includes protein-interaction modules, such as CARD or PYD, some harbour baculovirus inhibitor repeat (BIR) or other domains. For most characterised NLRs these domains have been attributed to downstream signaling Under resting conditions, NLRs are thought to be present in an autorepressed form, with the LRR folded back onto the NACHT domain preventing oligomerization. Accessory proteins may help maintain the inactive state. PAMP/DAMP exposure is thought to triggers conformational changes that expose the NACHT domain enabling oligomerization and recruitment of effectors, though it should be noted that due to the lack of availability of structural data, the mechanistic details of NLR activation remain largely elusive. New terminology for NOD-like receptors was adopted by the Human Genome Organization (HUGO) in 2008 to standardize the nomenclature of NLRs. The acronym NLR, once standing for NOD-like receptor, now is an abbreviation of 'nucleotide-binding domain, leucine-rich repeat containing' protein. The term NOD-like receptor is officially outdated and replaced by NLRC where the C refers to the CARD domain. However the official gene symbols for NOD1 and NOD2 still contain NOD and this general term is still widely used.
Toll-like Receptor 4 is a Microbe Associated Molecular Pattern receptor well known for it's sensitivity to Bacterial Lipopolysaccharides (LPS). LPS is assembled within diverse Gram-negative bacteria, many of which are human or plant pathogens. It is a component of the outer membrane of Gram-negative bacteria and consists of lipid A, a core polysaccharide and an O-polysaccharide of variable length (often more than 50 monosaccharide units). LPS is a potent activator of the innate immune response in humans, causing reactions including fever, headache, nausea, diarrhoea, changes in leukocyte and platelet counts, disseminated intravascular coagulation, multiorgan failure, shock and death. All these reactions are induced by cytokines and other endogenous mediators which are produced after interaction of LPS with the humoral and cellular targets of the host. In macrophages and dendritic cells, LPS-mediated activation of TLR4 triggers the biosynthesis of diverse mediators of inflammation, such as TNF-alpha and IL6, and activates the production of co-stimulatory molecules required for the adaptive immune response. In mononuclear and endothelial cells, LPS also stimulates tissue factor production. These events are desirable for clearing local infections, but when these various mediators and clotting factors are overproduced, they can damage small blood vessels and precipitate shock accompanied by disseminated intravascular coagulation and multiple organ failure.
In human, ten members of the Toll-like receptor (TLR) family (TLR1-TLR10) have been identified (TLR11 has been found in mouse, but not in human). All TLRs have a similar Toll/IL-1 receptor (TIR) domain in their cytoplasmic region and an Ig-like domain in the extracellular region, where each is enriched with a varying number of leucine-rich repeats (LRRs). Each TLR can recognize specific microbial pathogen components. The binding pathogenic component to TLR initializes signaling pathways that lead to induction of Interferon alpha/beta and inflammatory cytokines. There are two main signaling pathways. The first is a MyD88-dependent pathway that is common to all TLRs, except TLR3; the second is a TRIF(TICAM1)-dependent pathway that is peculiar to TLR3 and TLR4. TLR4-mediated signaling pathway via TRIF requires adapter molecule TRAM (TRIF-related adapter molecule or TICAM2). TRAM is thought to bridge between the activated TLR4 complex and TRIF.(Takeda & Akira 2004; Akira 2003; Takeda & Akira 2005; Kawai 2005; Heine & Ulmer 2005).
Advanced Glycosylation End- product-specific Receptor (AGER) also known as Receptor for Advanced Glycation End-products (RAGE) is a multi-ligand membrane receptor belonging to the immunoglobulin superfamily. It is considered to be a Pattern Recognition Receptor (Liliensiek et al. 2004). It recognizes a large variety of modified proteins known as advanced glycation/glycosylation endproducts (AGEs), a heterogenous group of structures that are generated by the Maillard reaction, a consequence of long-term incubation of proteins with glucose (Ikeda et al. 1996). Their accumulation is associated with diabetes, atherosclerosis, renal failure and ageing (Schmidt et al. 1999). The most prevalent class of AGE in vivo are N(6)-carboxymethyllysine (NECML) adducts (Kislinger et al. 1991). In addition to AGEs, AGER is a signal transduction receptor for amyloid-beta peptide (Ab) (Yan et al. 1996), mediating Ab neurotoxicity and promoting Ab influx into the brain. AGER also responds to the proinflammatory S100/calgranulins (Hofmann et al. 1999) and High mobility group protein B1 (HMGB1/Amphoterin/DEF), a protein linked to neurite outgrowth and cellular motility (Hori et al. 1995). The major inflammatory pathway stimulated by AGER activation is NFkappaB. Though the signaling cascade is unclear, several pieces of experimental data suggest that activation of AGER leads to sustained activation and upregulation of NFkappaB, measured as NFkappaB translocation to the nucleus, and increased levels of de novo synthesized NFkappaB (Bierhaus et al. 2001). As this is clearly an indirect effect it is represented here as positive regulation of NFkappaB translocation to the nucleus. AGER can bind ERK1/2 and thereby activate the MAPK and JNK cascades (Bierhaus et al. 2005).
In addition to AGER/RAGE, several other proteins have been identified as AGE-binding proteins. AGE binding proteins p60 and p90 (Yang et al. 1991) were subsequently identified as the Oligosaccharyl transferase 48 kDa subunit (Ost-48) and Glucosidease-2 subunit beta (Li et al. 1996). A third member was identified as Galectin-3 (Vlassara et al. 1995). These 3 proteins have been shown to be present on the plasma membrane of many cell types including vascular endothelium (Stitt et al. 1999). They have been designated AGE-R1, -R2 and -R3. Their suggested function is the removal and degradation of AGEs, but AGER-1 was found to negatively regulate AGER/RAGE (Lu et al. 2004), with kinetics that suggested a more complex interaction than simple competition for the same ligand.
MDA5 is the closest relative of RIG-I and contains two CARD-like regions, a DExD/H helicase domain, and a C-terminal region similar to the RD of RIG-I. MDA5 with its C-terminal domain (CTD) preferentially binds dsRNA with blunt ends, but does not associate with dsRNA with either 5' or 3' overhangs. Upon binding dsRNA, MDA5 is presumed to undergo structural alteration and, thereby unmask the CARDs enabling them to recruit downstream signal transducer proteins. Dihydroxyacetone kinase (DAK) binds to the CARD domains of MDA5 and acts as a negative regulator of MAD5. It is released upon the conformational change induced by viral RNA binding, allowing the MDA5 CARD domains to bind to IPS-1 CARD.
RIG-I has two copies of caspase recruitment domain (CARD) in its N-terminus, DExD/H helicase domain with an ATP binding motif in the middle and a repressor domain (RD) in the C-terminus. In the absence of appropriate stimulation, RIG-I is in a 'closed' conformation in which the repressor domain phyically interacts with the helicase domain masking CARD. Upon viral infection the free triphosphate structure at the 5' end of the viral RNAs activate RIG-I by binding to its RNA helicase domain. This provokes change in RIG-I conformation exposing the CARD leading to RIG-I dimerization and allowing it to interact with the mitochondria-bound interferon beta promoter stimulator-1 (IPS-1).
BLNK: molecular scaffolding through 'cis'-mediated organization of signaling proteins
EPACs (exchange proteins directly activated by cAMP) are Rap1 GEFs that are activated by direct binding of cAMP (cyclic adenosine monophosphate). cAMP-GEFI (EPAC1) is widely expressed, while cAMP-GEFII (EPAC2) is enriched in brain and adrenal tissue. Both are selective for Rap1. A role of EPACs has been proposed for Rap1-dependent cell adhesion to laminin in both epithelial and red blood cells, and in the regulation of vascular endothelial barrier function.
Signals from agonist receptors (such as GPVI) trigger the production of PIP3, DAG, cAMP and elevated Ca++ levels. This leads to the activation and translocation of active Rap1-GTP to the plasma membrane. Rap-GEFs stimulate the replacement of GDP for GTP, activating Rap1. Several Rap1 GEFs have been identified enabling Rap1 to respond to diverse stimuli. CalDAG-GEFs activate Rap1 in response to calcium and DAG, downstream of Phospholipase C. EPAC (exchange proteins directly activated by cAMP) GEFs are activated by binding cAMP.
Antigen presenting cells (APCs) such as B cells, dendritic cells (DCs) and monocytes/macrophages express major histocompatibility complex class II molecules (MHC II) at their surface and present exogenous antigenic peptides to CD4+ T helper cells. CD4+ T cells play a central role in immune protection. On their activation they stimulate differentiation of B cells into antibody-producing B-cell blasts and initiate adaptive immune responses. MHC class II molecules are transmembrane glycoprotein heterodimers of alpha and beta subunits. Newly synthesized MHC II molecules present in the endoplasmic reticulum bind to a chaperone protein called invariant (Ii) chain. The binding of Ii prevents the premature binding of self antigens to the nascent MHC molecules in the ER and also guides MHC molecules to endocytic compartments. In the acidic endosomal environment, Ii is degraded in a stepwise manner, ultimately to free the class II peptide-binding groove for loading of antigenic peptides. Exogenous antigens are internalized by the APC by receptor mediated endocytosis, phagocytosis or pinocytosis into endocytic compartments of MHC class II positive cells, where engulfed antigens are degraded in a low pH environment by multiple acidic proteases, generating MHC class II epitopes. Antigenic peptides are then loaded into the class II ligand-binding groove. The resulting class II peptide complexes then move to the cell surface, where they are scanned by CD4+ T cells for specific recognition (Berger & Roche 2009, Zhou & Blum 2004, Watts 2004, Landsverk et al. 2009).
cGMP and cAMP dependent protein kinases (PKG and PKA respectively) phosphorylate the Rap1 GTPase activating RAP1GAP2 at serine 7 (Schultess et al. 2007). This reduces the binding of inhibitory 14-3-3 proteins to RAP1GAP2.
Antigen processing and loading on to MHC class II molecules occurs in late endocytic/lysosomal vesicles, where epitopes which require extensive proteolytic processing are generated (Bryant & Ploegh 2003). These late endosome/lysosomal-like compartments are enriched in MHC II and are referred to as MIICs (MHC class II compartments) (Peters et al. 1991). A variety of lysosomal proteases like cathepsins S, D, B etc. and Asparaginyl endopeptidase (AEP) are suggested to be involved in the processing of antigens to generate CD4+ T cell epitopes (Deusing et al. 1998, Shi et al. 1999, Pluger et al. 2002, Watts et al. 2005). An initial cleavage by endopeptidases (AEP) would be necessary to unlock the antigen and allow further trimming of the ends by exopeptidases (Cathepsins). In the acidic environment of the lysosome, cathepsins are generally activated by autocatalytic cleavage of a propeptide which otherwise blocks the active site.
TRIF-related adapter molecule (TRAM or also known as TICAM2) is a sorting adapter which recruits TRIF to activated TLR4. Like TLR4, TRAM was detected both at the plasma membrane and in the endosomal compartment. TRAM was reported to recruit TRIF to the plasma membrane [Tanimuro N et al 2008]. However, TRAM did not induce TRIF-mediated signaling from the cell surface, instead, TRAM endocytosis was required for activation of IRF3 and induction of IFN-beta [Tanimuro N et al 2008; Kagan JC et al 2008]. Although, endocytosis of both TLR4 and TRAM and their association are required to trigger TRIF-mediated signaling, TRAM can target endosomes independently on its interaction with TLR4. TRAM cellular localization is controlled by myristoylation and phosphorylation of its N-terminal bipartite sorting signal motif [Kagan JC et al 2008]. TRAM has been shown to undergo phosphorylation on Ser-16 by protein kinase C epsilon in LPS-treated human THP1 and murine embryonic fibroblasts (MEF) cells [McGettrick AF et al 2006].
Adaptive immunity refers to antigen-specific immune response efficiently involved in clearing the pathogens. The adaptive immune system is comprised of B and T lymphocytes that express receptors with remarkable diversity tailored to recognize aspects of particular pathogens or antigens. During infection, dendritic cells (DC) which act as sentinels in the peripheral tissues recognize and pick up the pathogen in the form of antigenic determinants and then process these antigens and present them to T cells. These T cells of appropriate specificity respond to the antigen, and either kill the pathogen directly or secrete cytokines that will stimulate B lymphocyte response. B cells provide humoral immunity by secreting antibodies specific for the pathogen or antigen.
Rap1 (Ras-proximate-1) is a small G protein in the Ras superfamily. Like all G proteins, Rap1 is activated when bound GDP is exchanged for GTP. Rap1 is targeted to lipid membranes by the covalent attachment of lipid moieties to its carboxyl terminus. Movement of Rap1 from endosomal membranes to the plasma membrane upon activation has been reported in several cell types including Jurkat T cells and megakaryocytes. On activation, Rap1 undergoes conformational changes that facilitate recruitment of a variety of effectors, triggering it's participation in integrin signaling, ERK activation, and others.
Rap1 signalling is terminated by the hydrolysis of bound GTP to GDP. The intrinsic GTPase activity of Rap1 is greatly enhanced by GTP-ase activating proteins (GAPs).
After incorporation at the branch the actin bound to VCA domain in WASP/WAVE undergoes ATP hydrolysis and this destabilizes its interaction with WASP/WAVE. This dissociates the branched junction from the membrane-bound WASP/WAVE (Kovar 2006).
Once activated, the ARP2/3 complex nucleates new actin filaments that extend from the sides of pre-existing mother actin filaments at a 70-degree angle to form Y-branched networks (Firat-Karalar & Welch 2010). These branched actin filaments push the cell membrane forward to form a pseudopod. The ARP2/3 complex is composed of two Arps (actin-related proteins), ARP2 and ARP3, and five unique proteins ARPC1, ARPC2, ARPC3, ARPC4 and ARPC5 (Gournier et al. 2001). Both ARP2 and ARP3 subunit binds ATP. There are two proposed models to explain the process of actin nucleation by ARP2/3 complex: the barbed-end branching model and the dendritic nucleation/side branching model (Le Clainche & Carlier 2008). In barbed-end branching model the branching/ternary complex (G-actin-WASP/WAVE-Arp2/3 complex) binds to the barbed end of the mother filament. G-actin bound to VCA domain or one of the Arp subunit would incorporate into the mother filament at the barbed end, thus positioning ARP2/3 complex to initiate the daughter branch on the side of the the mother filament. ARP2/3 nucleates the formation of a new actin filament branches, which elongate at the barbed ends (Le Clainche & Carlier 2008, Pantaloni et al 2000, Le Clainche et al. 2003, Egile et al. 2005). In side branching model the branching complex binds to the side of the mother actin filament and mimics an actin nucleus and initiates lateral branch (Le Clainche & Carlier 2008, Amann & Pollard 2001).
PAK1, a downstream effector of CDC42 and RAC1, is found localized in phagosomes. Upon activation, PAK1 phosphorylates LIMK, which directly phosphorylates and inactivates cofilin, a protein that mediates depolymerization of actin filaments. Thus, RAC and CDC42 coordinate actin dynamics by inducing actin polymerization via ARP2/3 on one hand, and inhibiting actin depolyerization via LIMK and cofilin on the other (Garcia-Garcia & Rosales 2002). PAK1 exists as homodimer in a trans-inhibited conformation. The kinase inhibitory (KI) domain of one PAK1 molecule binds to the C-terminal catalytic domain of the other and inhibits catalytic activity. GTPases RAC1/CDC42 bind the GBD domain of PAK1 thereby altering the conformation of the KI domain, relieving inhibition of its catalytic domain, and allowing PAK1 autophosphorylation that is required for full kinase activity (Parrini et al. 2002, Zhao & Manser 2005).
ATP bound G-actin monomers are added to the fast growing barbed ends of both the mother and the daughter filaments and the polymerization of these filaments drives membrane protrusion. Pseudopodia extend around the antibody bound particle to form the phagocytic cup. This elongation continues until the filament reaches a steady state equilibrium with free G-actin monomers.
LIM-kinase is responsible for the tight regulation of the activity of cofilin (a protein that depolymerizes actin filaments) and thus maintains the balance between actin assembly and disassembly. LIMK is one of the downstream targets of PAK1 and is activated through phosphorylation by PAK1 on T508 within its activation loop.
PAK1 needs autophosphorylation for complete activation. PAK1 is autophosphorylated at several sites, but S144 flanking the kinase inhibitor region and T423 within the catalytic domain are the two conserved sites that regulate the catalytic activity (Chong et al. 2001, Parrini et al. 2001).
The actin cytoskeleton is fundamental for phagocytosis and members of the Rho family GTPases RAC and CDC42 are involved in actin cytoskeletal regulation leading to pseudopod extension. Active RAC and CDC42 exert their action through the members of WASP family proteins (WASP/N-WASP/WAVE) and ARP2/3 complex. Actin filaments move from the bottom toward the top of the phagocytic cup during pseudopod extension.
Cofilin is a member of the ADF (actin-depolymerizing factor) protein family, that is involved in regulating actin dynamics in the growth cone. It binds to actin in a one-to-one molar ratio, and stimulates both the severing of actin filaments and depolymerization of actin subunits from the actin filament end. Activated LIMK phosphorylates cofilin on conserved serine 3 (Ser3/S3), located near the actin binding site. After phosphorylation cofilin is inactive and looses its affinity for actin and releases from G-actin monomers. Now the ADP-actin monomers are free and can exchange ADP with cytoplasmic ATP and they are ready for reincorporation at the barbed end of the a growing filament.
RNA Pol II (unphosphorylated) largest subunit
DNA-directed RNA polymerase II largest subunit
E1B-AP5 nucleocytoplasmic transport protein
The DNA-dependent protein kinase interacts with DNA to form a protein-DNA complex that is disrupted by phosphorylation.
Inositol 1,4,5-triphosphate (IP3) is a second messenger produced by phospholipase C (PLC) metabolism of phosphoinositol 4,5-bisphosphate (PIP2) (Canossa et al. 2001).
Diacylglycerol (DAG) positively regulates the autophosphorylation of protein kinase C-delta (PKC-delta), which stimulates ERK1/2 and triggers neurite outgrowth. DAG also stimulates the translocation of PKC from the cytosol to the plasma membrane. PKC-delta contributes to growth factor specificity and response to neuronal cells by promoting cell-type-specific differences in growth factor signalling. DAG can also activate PKC-epsilon in the same manner.
Heterogenous nuclear ribonucleoprotein U
Heterogeneous nuclear ribonucleoprotein I
STING (stimulator of IFN genes; also known as MITA/ERIS/MPYS/TMEM173) is an endoplasmic reticulum (ER) resident, which is required for effective type I IFN production in response to nucleic acids. Indeed, select pathogen-derived DNA or RNA were shown to activate STING in human and mouse cells (Ishikawa H and Barber GN 2008; Ishikawa H et al. 2009; Sun W et al. 2009; Prantner D et al. 2010). Importantly, in vitro studies have shown that STING is essential for Mycobacterium tuberculosis (Manzanillo PS et al. 2012), Plasmodium falciparum (Sharma S et al. 2011) and human immunodeficiency virus (HIV) induced type I IFN production [Yan N et al 2010]. Mycobacterium tuberculosis, plasmodium falciparum and HIV are three deadliest pathogens, which kill millions of people each year worldwide. STING has been also implicated in type I IFN response which was stimulated by fusion of viral and target-cell membrane in a manner independent of DNA, RNA and viral capsid [Holm CK et al 2012]. Under steady state conditions, STING is positioned at the translocon complex within the ER membrane. However upon stimulation with intracellular DNA it translocates from ER to perinuclear vesicles via the Golgi by mechanisms that remain unclear (Ishikawa H and Barber GN 2008; Sun W et al. 2009; Ishikawa H et al. 2009; Saitoh T et al. 2009). Mouse Sting trafficking in dsDNA-stimulated mouse embryonic fibroblasts (MEF) cells was found to depend on autophagy-related gene 9a (Atg9a) (Saitoh T et al. 2009). STING was reported to function as a signaling adaptor or coreceptor in response to cytosolic dsDNA (Unterholzner L et al. 2010; Zhang Z et al. 2011). STING was also shown to function as a direct DNA sensor to induce the innate immune response in human telomerase fibroblasts (hTERT-BJ1) and murine embryonic fibroblasts (MEFs) (Abe T et al. 2013). Additionally, STING is thought to function as a direct sensor of cyclic dinucleotides. STING was shown to interact directly with c-di-GMP in human embryonic kidney HEK293T cell lysates (Burdette DL et al. 2011). Once STING is stimulated, its C-terminus serves as a signaling scaffold to recruit IRF3 and TBK1, which leads to TBK1-dependent phosphorylation of IRF3 (Tanaka Y and Chen ZJ 2012). Mouse, but not human STING, can also bind vascular disrupting agents 5,6-dimethylxanthenone-4-acetic acid (DMXAA) and the antiviral small molecule 10-carboxymethyl-9-acridanone (CMA) to induce type I IFN production, suggesting a species-specific drug effect on the STING-mediated host response (Conlon J et al. 2013; Cavlar T et al. 2013).
The helicase DDX41 was shown to sense exogenous DNA in human and mouse cells (Zhang Z et al. 2011, Parvatiyar K et al. 2012). DDX41 was also reported to sense and interact with bacterial secondary messengers cyclic di-GMP or cyclic di-AMP (Parvatiyar K et al. 2012). Mutagenesis analysis with DDX41 deletion constructs revealed that the central DEAD-box domain of DDX41 mediated the binding with DNA (Zhang Z et al. 2011, Parvatiyar K et al. 2012). Knockdown of DDX41 or STING in human cells (THP-1 and PBMC cells) and mouse dendritic cells significantly reduced the cytokine production in response to pathogen-derived DNA or poly(dG:dC) (Zhang Z et al. 2011, Parvatiyar K et al. 2012). DDX41 localized together with STING in the cytoplasm when both DDX41 and STING were co-expressed in HEK293T cells (Zhang Z et al. 2011). Mouse Ddx41 was found to bind Sting and Tbk1 in both resting and poly(dA:dT)-stimulated mouse splenic myeloid dendritic cell (D2SC mDCs) (Zhang Z et al. 2011). Ddx41-Sting interaction was also observed in c-di-GMP- or c-di-AMP-treated D2SC cells (Parvatiyar K et al. 2012). Moreover, knockdown of Ddx41 or Sting inhibited phosphorylation of Tbk1, Irf3, p65 subunit of NF-kappaB and other signal transducers in DNA-stimulated mouse bone marrow-derived (BMDCs) and D2SC cells (Zhang Z et al. 2011, Parvatiyar K et al. 2012). Collectively, these data suggest that DNA triggers DDX41 downstream signaling to type I interferon in a STING-dependent manner. The E3 ubiquitin ligase TRIM21 was reported to promote the K48-linked ubiquitination and degradation of DDX41 leading to downregulation of the type I interferon production in mouse mDC and human monocytes THP-1 (Zhang Z et al. 2013).
RIG-I-like helicases (RLHs) the retinoic acid inducible gene-I (RIG-I) and melanoma differentiation associated gene 5 (MDA5) are RNA helicases that recognize viral RNA present within the cytoplasm. Functionally RIG-I and MDA5 positively regulate the IFN genes in a similar fashion, however they differ in their response to different viral species. RIG-I is essential for detecting influenza virus, Sendai virus, VSV and Japanese encephalitis virus (JEV), whereas MDA5 is essential in sensing encephalomyocarditis virus (EMCV), Mengo virus and Theiler's virus, all of which belong to the picornavirus family. RIG-I and MDA5 signalling results in the activation of IKK epsilon and (TKK binding kinase 1) TBK1, two serine/threonine kinases that phosphorylate interferon regulatory factor 3 and 7 (IRF3 and IRF7). Upon phosphorylation, IRF3 and IRF7 translocate to the nucleus and subsequently induce interferon alpha (IFNA) and interferon beta (IFNB) gene transcription.
Presence of pathogen-associated DNA in cytosol induces type I IFN production. Several intracellular receptors have been implicated to some degree. These include DNA-dependent activator of interferon (IFN)-regulatory factors (DAI) (also called Z-DNA-binding protein 1, ZBP1), absent in melanoma 2 (AIM2), RNA polymerase III (Pol III), IFN-inducible protein IFI16, leucine-rich repeat flightless interacting protein-1 (LRRFIP1), DEAH-box helicases (DHX9 and DHX36), DEAD-box helicase DDX41, meiotic recombination 11 homolog A (MRE11), DNA-dependent protein kinase (DNA-PK), cyclic GMP-AMP synthase (cGAS) and stimulator of interferon genes (STING). Detection of cytosolic DNA requires multiple and possibly redundant sensors leading to activation of the transcription factor NF-kappaB and TBK1-mediated phosphorylation of the transcription factor IRF3. Cytosolic DNA also activates caspase-1-dependent maturation of the pro-inflammatory cytokines interleukin IL-1beta and IL-18. This pathway is mediated by AIM2.
DHX36 and DHX9 are aspartate-glutamate-any amino acid aspartate/histidine (DExD/H) box helicase (DHX) proteins that localize in the cytosol. The DHX RNA helicases family includes a large number of proteins that are implicated in RNA metabolism. Members of this family, RIG-1 and MDA5, have been shown to sense a non-self RNA leading to type I IFN production. RNA helicases DHX36 and DHX9 were found to trigger host responses to non-self DNA in MyD88-dependent manner. DHX36 sensed CpG class A, while DHX9 sensed CpG class B. Both DHX36 and DHX9 were critical for antiviral immune responses in viral DNA-stimulated human plasmacytoid dendritic cells (pDC) (Kim T et al. 2010).
DHX9 binds CpG-B in human plasmacytoid dendritic cells (pDC). The DUF domain of DHX9 was shown to be essential for binding CpG-B [Kim T et al 2010].
RNA polymerase III (POL III) was reported to sense and transcribe cytosolic AT-rich dsDNA into 5'-triphosphate poly(A-U) RNA in human and mouse cells. This dsRNA ligand in turn activated retinoic acid-inducible gene I (RIG-I) leading to production of type I interferon and activation of the transcription factor NF-kappaB (Chiu YH et al. 2009, Ablasser A et al. 2009). Knockdown of POL III expression by siRNA or inhibition of its enzymatic activity by specific chemical inhibitor ML-60218 prevented IFN beta induction in HEK293 cells stimulated with DNA viruses or poly(dA-dT) (Chiu YH et al. 2009, Ablasser A et al. 2009). Moreover, Pol-III inhibition blocked interferon induction by intracellular Legionella pneumophila bacteria [Chiu YH et al 2009]. This project represents cytosolic RNA polymerase III as a complex comprising 17 subunits, although the precise biochemical composition of the cytosolic holoenzyme complex which specifically recognizes AT-rich DNA is not yet known.
Once activated the VCA region in WAVE2 or WASP/N-WASP becomes available for binding to ARP2/3 and actin monomer. The actin monomer binds to the V domain and ARP2/3 complex binds to the CA domain. The simultaneous binding of G-actin and the ARP2/3 complex to the VCA region contributes to the activation of ARP2/3-complex-mediated actin polymerization. The VCA module acts as a platform on which an actin monomer binds to the ARP2/3 complex to trigger actin polymerization (Takenawa & Suetsugu 2007).
FCGR mediated phagocytosis requires CDC42 to stimulate actin polymerization, generating the force for phagocytic cup protrusion or pseudopod extension. CDC42 activation is restricted at the advancing edge of the phagocytic cup, where actin is concentrated, and is deactivated at the base of the phagocytic cup (Beemiller et al 2010). The mechanism behind the recruitment and activation of CDC42 during FCGR phagocytosis is unknown. VAV regulates the activation of RAC1 but not CDC42 and the GEF responsible for CDC42 activation during FCGR-mediated phagocytosis remains unidentified (Adam et al 2004, Patel et al 2002).
Wiskott-Aldrich syndrome protein (WASP) and Neural-WASP (N-WASP) proteins are scaffolds that transduce signals from cell surface receptors to the activation of the ARP2/3 complex and actin polymerization. WASP and N-WASP possess a central GTPase binding domain (GBD) and an NH2-terminal WASP homology domain 1 (WH1), adjacent to this is a basic region (B) and a C-terminal containing VCA region that contains: a V domain (verprolin homology/WASP homology 2), a C domain (connecting), and an A motif (acidic). The VCA region is responsible for binding to and activating the ARP2/3 complex (Bompard & Caron 2004, Callebaut et al 1998). Under resting conditions, WASP and N-WASP are maintained in an autoinhibition state via interaction of the N-terminal GBD and the C-terminal VCA domains. This prevents access of the ARP2/3 complex to the VCA region. Activated CDC42 binds to the GBD region in N-WASP and this interaction releases the VCA region from autoinhibition enabling binding of the ARP2/3 complex stimulating actin polymerization (Kim et al 2000, Park & Cox 2009). Phosphoinositides (PtdIns(4,5)P2) interact with the basic (B) region in WASP and this interaction is important for activation of the WASP and ARP2/3 complex.(Higgs & Pollard 2000).
DNAX activation protein of 12kDa (DAP12) is an immunoreceptor tyrosine-based activation motif (ITAM)-bearing adapter molecule that transduces activating signals in natural killer (NK) and myeloid cells. It mediates signalling for multiple cell-surface receptors expressed by these cells, associating with receptor chains through complementary charged transmembrane amino acids that form a salt-bridge in the context of the hydrophobic lipid bilayer (Lanier et al. 1998). DAP12 homodimers associate with a variety of receptors expressed by macrophages, monocytes and myeloid cells including TREM2, Siglec H and SIRP-beta, as well as activating KIR, LY49 and the NKG2C proteins expressed by NK cells. DAP12 is expressed at the cell surface, with most of the protein lying on the cytoplasmic side of the membrane (Turnbull & Colonna 2007, Tessarz & Cerwenka 2008).
In response to receptor ligation, the tyrosine residues in DAP12's immunoreceptor tyrosine-based activation motif (ITAM) are phosphorylated by Src family kinases. These phosphotyrosines form the docking site for the protein tyrosine kinase SYK in myeloid cells and SYK and ZAP70 in NK cells. DAP12-bound SYK autophosphorylates and phosphorylates the scaffolding molecule LAT, recruiting the proximal signaling molecules phosphatidylinositol-3-OH kinase (PI3K), phospholipase-C gamma (PLC-gamma), GADS (GRB2-related adapter downstream of SHC), SLP76 (SH2 domain-containing leukocyte protein of 76 kDa), GRB2:SOS (Growth factor receptor-bound protein 2:Son of sevenless homolog 1) and VAV. All of these intermediate signalling molecules result in the recruitment and activation of kinases AKT, CBL (Casitas B-lineage lymphoma) and ERK (extracellular signal-regulated kinase), and rearrangement of the actin cytoskeleton (actin polymerization) finally leading to cellular activation. PLC-gamma generates the secondary messengers diacylglycerol (DAG) and inositol-1,4,5-trisphosphate (InsP3), leading to activation of protein kinase C (PKC) and calcium mobilization, respectively (Turnbull & Colonna 2007, Klesney-Tait et al. 2006).
Calcineurin (CaN), also called protein phosphatase 2B (PP2B), is a calcium/Calmodulin (CaM)-dependent serine/threonine protein phosphatase. It exists as a heterodimer consisting of CaM-binding catalytic subunit CaN A chain and a Ca+2 binding regulatory CaN B chain. At low calcium concentrations, CaN exists in an inactive state, where the autoinhibitory domain (AID) binds to the active-site cleft. Upon an increase in calcium concentration CaM binds to Ca+2 ions and gets activated. Active CaM binds to CaN regulatory domain (RD) and this causes release of the AID and activation of the phosphatase (Rumi-Masante et al. 2012). Binding of calcium to CaN B regulatory chain also causes a conformational change of the RD of CaN A chain (Yang & Klee 2000).
LYN localized in lipid rafts undergoes an intermolecular autophosphorylation at tyrosine 396. This residue is present in the activation loop, and its phosphorylation promotes LYN kinase activity.
One important physiological role for Calmodulin is the regulation of adenylylcyclases. Four of the nine known adenylylcyclases are calcium sensitive, in particular type 8 (AC8).
The Ca2+-calmodulin-dependent protein kinase (CaM kinase) cascade includes three kinases: CaM-kinase kinase (CaMKK); and the CaM kinases CaMKI and CaMKIV, which are phosphorylated and activated by CaMKK. Members of this cascade respond to elevation of intracellular Ca2+ levels. CaMKK and CaMKIV localize both to the nucleus and to the cytoplasm, whereas CaMKI is only cytosolic. Nuclear CaMKIV regulates transcription through phosphorylation of several transcription factors, including CREB. In the cytoplasm, there is extensive cross-talk between CaMKK, CaMKIV and other signaling cascades, including those that involve the cAMP-dependent kinase (PKA), MAP kinases and protein kinase B (PKB/Akt).
This pathway describes the generation of DAG and IP3 by the PLCgamma-mediated hydrolysis of PIP2 and the subsequent downstream signaling events.
Calmodulin (CaM) is a small acidic protein that contains four EF-hand motifs, each of which can bind a calcium ion, therefore it can bind up to four calcium ions. The protein has two approximately symmetrical domains, separated by a flexible hinge region. Calmodulin is the prototypical example of the EâF-hand family of Ca2+-sensing proteins. Changes in intracellular Ca2+ concentration regulate calmodulin in three distinct ways. First, by directing its subcellular distribution. Second, by promoting association with different target proteins. Third, by directing a variety of conformational states in calmodulin that result in target-specific activation. Calmodulin binds and activates several effector protein (e.g. the CaM-dependent adenylyl cyclases, phosphodiesterases, protein kinases and the protein phosphatase calcineurin).
Autophosphorylation of the N-terminus Ser12-Ser13 is required for full activation after Ca2+/calmodulin binding and phosphorylation of the Ca2+/calmodulin-bound enzyme on Thr200 by a Ca2+/calmodulin-dependent protein kinase kinase.
The calmodulin:CaMK IV complex enters the nucleus.
Insulin-stimulated phosphorylation of the Akt substrate AS160 is impaired in skeletal muscle of type 2 diabetic subjects
Cyclic adenosine 3',5'-monophosphate (cAMP) induces gene transcription through activation of cAMP-dependent protein kinase (PKA), and subsequent phosphorylation of the transcription factor cAMP response element-binding protein, CREB, at serine-133.
Chk2/hCds1 functions as a DNA damage checkpoint in G(1) by stabilizing p53.
When cAMP level rises, the PKA catalytic subunit (C subunit) released from the holoenzyme enters the nucleus by passive diffusion whereas termination of signaling to the nucleus involves an active mechanism. In the nucleus, the C subunit binds to the heat-stable protein kinase inhibitor (PKI), and this binding not only inactivates the C subunit but also by conformational change unveils a nuclear export signal in PKI which leads to export of the C-PKI complex from the nucleus.
The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2) phosphorylate p53 at multiple DNA damage-inducible sites.
A number of inactive tetrameric PKA holoenzymes are produced by the combination of homo- or heterodimers of the different regulatory subunits associated with two catalytic subunits. When cAMP binds to two specific binding sites on the regulatory subunits, these undergo a conformational change that causes the dissociation of a dimer of regulatory subunits bound to four cAMP from two monomeric, catalytically active PKA subunits.
The four protein kinase A (PKA) regulatory subunit isoforms differ in their tissue specificity and functional characteristics. The specific isoform activated in response to glucagon signalling is not known. The PKA kinase is a tetramer of two regulatory and two catalytic. The regulatory subunits block the catalytic subunits. Binding of cAMP to the regulatory subunit leads to the dissociation of the tetramer into two active dimers made up of a regulatory and a catalytic subunit.
Adenylate cyclase is responsive to calcium and calmodulin and produces cAMP. One important physiological role for Calmodulin is the regulation of adenylylcyclases. Four of the ten known adenylylcyclases are calcium sensitive, in particular type 8 (AC8).
Phagocytosis is one of the important innate immune responses that function to eliminate invading infectious agents. Monocytes, macrophages, and neutrophils are the professional phagocytic cells. Phagocytosis is a complex process involving the recognition of invading foreign particles by specific types of phagocytic receptors and the subsequent internalization of the particles. Fc gamma receptors (FCGRs) are among the best studied phagocytic receptors that bind to Fc portion of immunoglobulin G (IgG). Through their antigen binding F(ab) end, antibodies bind to specific antigen while their constant (Fc) region binds to FCGRs on phagocytes. The clustering of FCGRs by IgG antibodies on the phagocyte initiates a variety of signals, which lead, through the reorganisation of actin cytoskeleton and membrane remodelling, to the formation of pseudopod and phagosome. Fc gamma receptors are classified into three classes: FCGRI, FCGRII and FCGRIII. Each class of these FCGRs consists of several individual isoforms. Among all these isoforms FCGRI, FCGRIIA and FCGRIIIA, are able to mediate phagocytosis (Joshi et al. 2006, Garcia Garcia & Rosales 2002, Nimmerjahn & Ravetch 2006).
Phospholipases play an integral role in phagocytosis by generating essential second messengers. An early step in phagocytic signaling is the association of PIP2 and IP3 with the phagocytic cup. These are formed by the activity of phosphoinositol kinases and phospholipases. PI3K is has been shown to accumulate at phagocytic cups and converts PI (4,5)P2 to PI (3,4,5)P3. These phosphoinositides are capable of binding and increasing the activity of proteins that regulate the actin cytoskeleton. Phospholipases are lipid modifying enzymes that produce lipid mediators such as diacylglycerol (DAG), arachidonic acid (AA) and IP3. Phopsholipases PLA, PLC and PLD have been shown to be involved in antibody (IgG) mediated phagocytosis. The PLC product IP3 stimulates release of calcium from the endoplasmic reticulum. This Ca+2 concentration increase is greatest in the cytoplasm surrounding the phagocytic cup. Calcium is involved in the various stages of phagosome formation, including phagocytic ingestion and phagosome maturation.
Several members of phospholipase A (PLA) are involved in phagocytosis. Macrophages express three classes of PLA2: secreted Ca-dependent (sPLA2), cytosolic Ca-dependent (cPLA2) and cytosolic Ca-independent (iPLA2) of which iPLA2 is involved in FCGR mediated arachidonic acid (AA) production. Aggregation of FCGR triggers phosphorylation and membrane translocation of iPLA2. Protein kinase C (PKC), ERK and p38MAPK seems to regulate iPLA2 in monocytes, neutrophils and macrophages. Phosphorylated iPLA2 then mediates production of AA and lysoophospholipids from phosphatidylcholine. iPLA2 inhibitors (bromoenol lactone) block AA release and phagocytosis which can be restored upon addition of exogenous AA, suggesting a critical role for iPLA2 in FCGR phagocytosis (Lennartz et al. 1993, Tay & Melendez). Release of AA by activated iPLA2 changes the physical characteristic of the membrane which may facilitate pseudopod extension.
Phospholipase D (PLD) catalyses the hydrolysis of the membrane phospholipid, phosphatidylcholine (PC) to generate choline and metabolically active phosphatidic acid (PA) (Lennartz 1999). Pharmacological inhibition studies show that PLD participates in FCGR-mediated phagocytosis (Kusner et al. 1996). There is an increase in the activity of PLD following the activation of phagocytosis via FCGR (Kusner et al. 1999). Following activation of FCGR, PLD translocates to the plasma membrane at the phagocytic cup and generate PA. This PA can be converted to DAG through the action of phosphatidic acid phosphatase-1 (PAP-1). Thus activation of PLD may be an additional pathway leading to PKC activation. The two isoforms PLD1 and PLD2 are both shown to be essential for the formation of phagosome at different stages. PLD1 is localized on the endosomal/lysosomal compartment and PLD2 is localized at the plasma membrane. PLD2 may be linked to phagosome formation whereas PLD1 may be involved in the focal exocytosis at the plasma membrane and also in the maturation process (Carrotte et al. 2006).
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CaMKIV becomes fully activated after a three-step mechanism: Upon a transient increase in intracellular calcium, calcium-bound calmodulin (Ca2+/CaM) binds to its autoregulatory domain, which relieves intersteric inhibition. An activating protein kinase, calcium/calmodulin-dependent protein kinase kinase (CaMKK), binds to the Ca2+/CaM:CaMKIV complex and phosphorylates CaMKIV on a threonine residue in the activation loop. After full activation by the three-step mechanism mentioned above, the activity of CaMKIV becomes autonomous and no longer requires bound Ca2+/CaM. This activity is required for CaMKIV-mediated transcriptional regulation. The CaMKIV-associated PP2A then dephosphorylates CaMKIV, thereby terminating autonomous activity and CaMKIV-mediated gene transcription.
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Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE)
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Congenital disorder of glycosylation type Ik (CDG-Ik): a defect of mannosyltransferase I
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Cytokines are small proteins that regulate and mediate immunity, inflammation, and hematopoiesis. They are secreted in response to immune stimuli, and usually act briefly, locally, at very low concentrations. Cytokines bind to specific membrane receptors, which then signal the cell via second messengers, to regulate cellular activity.
Humans are exposed to millions of potential pathogens daily, through contact, ingestion, and inhalation. Our ability to avoid infection depends on the adaptive immune system and during the first critical hours and days of exposure to a new pathogen, our innate immune system.
The ISG proteins generated by IFN pathways plays key roles in the induction of innate and adaptive immune responses.
Interferons (IFNs) are cytokines that play a central role in initiating immune responses, especially antiviral and antitumor effects. There are three types of IFNs:Type I (IFN-alpha, -beta and others, such as omega, epsilon, and kappa), Type II (IFN-gamma) and Type III (IFN-lamda). In this module we are mainly focusing on type I IFNs alpha and beta and type II IFN-gamma. Both type I and type II IFNs exert their actions through cognate receptor complexes, IFNAR and IFNGR respectively, present on cell surface membranes. Type I IFNs are broadly expressed heterodimeric receptors composed of the IFNAR1 and IFNAR2 subunits, while the type II IFN receptor consists of IFNGR1 and IFNGR2. Type III interferon lambda has three members: lamda1 (IL-29), lambda2 (IL-28A), and lambda3 (IL-28B) respectively. IFN-lambda signaling is initiated through unique heterodimeric receptor composed of IFN-LR1/IF-28Ralpha and IL10R2 chains. Type I IFNs typically recruit JAK1 and TYK2 proteins to transduce their signals to STAT1 and 2; in combination with IRF9 (IFN-regulatory factor 9), these proteins form the heterotrimeric complex ISGF3. In nucleus ISGF3 binds to IFN-stimulated response elements (ISRE) to promote gene induction. Type II IFNs in turn rely upon the activation of JAKs 1 and 2 and STAT1. Once activated, STAT1 dimerizes to form the transcriptional regulator GAF (IFNG activated factor) and this binds to the IFNG activated sequence (GAS) elements and initiate the transcription of IFNG-responsive genes. Like type I IFNs, IFN-lambda recruits TYK2 and JAK1 kinases and then promote the phosphorylation of STAT1/2, and induce the ISRE3 complex formation.
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PIP2 hydrolysis appers to be an important mechanism for netrin-1 mediated neurite elongation. Netrin-1 alone could not elicit hydrolysis of PIP2 but depends on the stimulation of DCC and PLCgamma.
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The levels of second messengers such as Ca+2, cAMP and cGMP may regulate the response of the growth cone to a particular cue. Netrin-1 as a guidance molecule depends on intracellular Ca+2 concentration, coactivation of PI3K and PLCgamma, and the type of response depends on the levels of cAMP. Netrin first stimulates its receptor DCC, resulting in the activation of the enzyme phospholipase C. This then produces the messenger molecules, inositol-1,4,5-trisphosphate (IP3) and DAG, which in turn causes the release of Ca+2 from intracellular stores. Ca+2 release from the stores then activates TRPC channels on the cell surface. DAG activates TRPC3 and TRPC6 in a direct, membrane delimited manner, and IP3 may activate TRPC channels by depleting the ER Ca+2 levels.
Activated Rac1 bound to plexin-A might modulate actin dynamics through the sequential phosphorylation and activation of PAK, LIMK1 and cofilin.
Deficiency of GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase causes congenital disorder of glycosylation type Ik
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Semaphorins are a large family of cell surface and secreted guidance molecules divided into eight classes on the basis of their structures. They all have an N-terminal conserved sema domain. Semaphorins signal through multimeric receptor complexes that include other proteins such as plexins and neuropilins.
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Netrins are secreted proteins that play a crucial role in neuronal migration and in axon guidance during the development of the nervous system. To date, several Netrins have been described in mouse and humans: Netrin-1, -3/NTL2, -4/h and G-Netrins. Netrin-1 is the most studied member of the family and has been shown to play a crucial role in neuronal navigation during nervous system development mainly through its interaction with its receptors DCC and UNC5. Members of the Deleted in colorectal cancer (DCC) family- which includes DCC and Neogenin in vertebrates- mediate netrin-induced axon attraction, whereas the C. elegans UNC5 receptor and its four vertebrate homologs Unc5a-Unc5d mediate repulsion.
In its bound state PAK dimers are arranged in head-to-tail fashion and are maintained in inactive conformation in which the catalytic domain binds the kinase inhibitory (KI) domain. All PAK family members are direct effectors of Rac1. Rac1 binds to a conserved Cdc42/Rac interactive binding (CRIB) domain in PAK1. This binding stimulates serine/threonine kinase activity of PAK1 by a mechanism involving autophosphorylation. Phosphorylation of S-144 and T-423 are required for the activation of PAK1. This phosphorylation disables the KI-domain-kinase interaction and thereby reduces the affinity of the PAK dimers. Its been demonstarted that L1 stimulation propagates through VAV2-Rac1-Pak1 to MEK-ERK. It has been shown that Pak1 is able to phosphoarylate T292 and S298 on MEK, which is essential for the functional association of MEK with Raf.
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1D-myo-Inositol 1,3,4,5-tetrakisphosphate
1D-myo-Inositol 1,3,4,5-tetrakisphosphate [ChEBI:808]
D-myo-Inositol 1,3,4,5-tetrakisphosphate
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Dephosphorylated NFAT-calcineurin (CaN) complex translocates to nucleus, where it activates transcription of several cytokine genes (e.g..IL2).
Increase of intracellular calcium in mast cells is most crucial for mast cell degranulation. Elevation of intracellular calcium is achieved by activation of PLC-gamma. Mast cells express both PLC-gamma1 and PLC-gamma2 isoforms and activation of these enzymes leads to conversion of phosphatidylinositol 4,5-bisphosphate (PIP2) into inositol triphosphate (IP3) and diacylglycerol (DAG). The production of IP3 leads to mobilization of intracellular Ca+2, which later results in a sustained Ca+2 flux response that is maintained by an influx of extracellular Ca+2. In addition to degranulation, an increase in intracellular calcium concentration also activates the Ca2+/calmodulin-dependent serine phosphatase calcineurin. Calcineurin dephosphorylates the nuclear factor for T cell activation (NFAT) which exposes nuclear-localization signal sequence triggering translocation of the dephosphorylated NFAT-CaN complex to the nucleus. Once in the nucleus, NFAT regulates the transcription of several cytokine genes (Kambayashi et al. 2007, Hoth & Penner 1992, Ebinu et al. 2000, Siraganian et al).
Ras guanyl nucleotide-releasing proteins (RasGRPs) are guanyl nucleotide exchange factors (GEFs) that activate Ras ultimately leading to MAPK activation. RasGRPs have a catalytic domain composed of Ras exchange motif (REM) and a CDC25 domain, an atypical pair of EF hands that bind calcium and a DAG-binding C1 domain. After PIP2 hydrolysis, RasGRPs are recruited to the plasma membrane by binding to DAG and calcium (Stone 2011, Liu et al. 2007). Upon T-cell activation RasGRP1 specifically interacts with and activates Ras on Golgi instead of the plasma membrane (Bivona et al. 2003). It remains to be determined whether activation of N-Ras by RasGRP1 in mast cells occurs in the Golgi or the plasma membrane (Liu et al. 2007). RasGRP4 is mast cell specific and is involved in the controls Ras activation.
T219, T538 at the activation loop, S676 at the turn motif and S695 at the hydrophobic motif are autophosphorylated in cis-maanner. Posphorylation of T538 is critical for kinase activation and it stabilises the open active conformation. Some studies suggest the involvement of PDK1 (3-phosphoinositide-dependent protein kinase 1) and GLK kinases in the phosphorylation T538.
The increase in intracellular Ca+2 in conjunction with DAG also activates PKC and RasGRP, which inturn contributes to cytokine production by mast cells (Kambayashi et al. 2007). Activation of the FCERI engages CARMA1, BCL10 and MALT1 complex to activate NF-kB through PKC-theta (Klemm et al. 2006, Chen et al. 2007). FCERI stimulation leads to phosphorylation, and degradation of IkB which allows the release and nuclear translocation of the NF-kB proteins. Activation of the NF-kB transcription factors then results in the synthesis of several cytokines.
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The lipid raft resident adaptor molecules LAT1 and Non-T cell activation linker (NTAL), also known as linker for activation of B cells (LAB)/LAT2 are known participants in the regulation of mast cell calcium responses. Both LAT and NTAL are expressed and phosphorylated following engagement of FCERI on mast cells. NTAL is functionally and topographically different from LAT. There is a considerable debate on the role of NTAL in mast cell. Depending on the circumstances, NTAL appears to have a dual role as positive and negative regulator of MC responses elicited via FCERI. Studies conducted in bone marrow-derived mast cells (BMMCs) of mice lacking NTAL displayed enhanced FCERI-mediated tyrosine phosphorylation of several substrates, calcium response, degranulation, and cytokine production. This indicated that NTAL negatively regulates FCERI-mediated degranulation. However, in mice lacking both LAT and NTAL showed severe block in FCERI-mediated signaling than BMMCs deficient in LAT alone, suggesting that NTAL also shares a redundant function with LAT to play a positive role (Draberova et al. 2007, Orr & McVicar. 2011, Zhu et al. 2004, Volna et al. 2004). The major steps in NTAL mediated Ca+2 influx involves NTAL--> GAB2--> PI3K
Mast cells (MC) are distributed in tissues throughout the human body and have long been recognized as key cells of type I hypersensitivity reactions. They also play important roles in inflammatory and immediate allergic reactions. Activation through FCERI-bound antigen-specific IgE causes release of potent inflammatory mediators, such as histamine, proteases, chemotactic factors, cytokines and metabolites of arachidonic acid that act on the vasculature, smooth muscle, connective tissue, mucous glands and inflammatory cells (Borish & Joseph 1992, Amin 2012, Metcalfe et al. 1993). FCERI is a multimeric cell-surface receptor that binds the Fc fragment of IgE with high affinity. On mast cells and basophils FCERI exists as a tetrameric complex consisting of one alpha-chain, one beta-chain, and two disulfide-bonded gamma-chains, and on dendritic cells, Langerhans cells, macrophages, and eosinophils it exists as a trimeric complex with one alpha-chain and two disulfide-bonded gamma-chains (Wu 2011, Kraft & Kinet 2007). FCERI signaling in mast cells includes a network of signaling molecules and adaptor proteins. These molecules coordinate ultimately leading to effects on degranulation, eicosanoid production, and cytokine and chemokine production and cell migration and adhesion, growth and survival. The first step in FCERI signaling is the phosphorylation of the tyrosine residues in the ITAM of both the beta and the gamma subunits of the FCERI by LYN, which is bound to the FCERI beta-chain. The phosphorylated ITAM then recruits the protein tyrosine kinase SYK (spleen tyrosine kinase) which then phosphorylates the adaptor protein LAT. Phosphorylated LAT (linker for activation of T cells) acts as a scaffolding protein and recruits other cytosolic adaptor molecules GRB2 (growth-factor-receptor-bound protein 2), GADS (GRB2-related adaptor protein), SHC (SRC homology 2 (SH2)-domain-containing transforming protein C) and SLP76 (SH2-domain-containing leukocyte protein of 76 kDa), as well as the exchange factors and adaptor molecules VAV and SOS (son of sevenless homologue), and the signalling enzyme phospholipase C gamma1 (PLC-gamma1). Tyrosoine phosphorylation of enzymes and adaptors, including VAV, SHC GRB2 and SOS stimulate small GTPases such as RAC, RAS and RAF. These pathways lead to activation of the ERK, JNK and p38 MAP kinases, histamine release and cytokine production. FCERI activation also triggers the phosphorylation of PLC-gamma which upon membrane localisation hydrolyse PIP2 to form IP3 and 1,2-diacylglycerol (DAG) - second messengers that release Ca2+ from internal stores and activate PKC, respectively. Degranulation or histamine release follows the activation of PLC-gamma and protein kinase C (PKC) and the increased mobilization of calcium (Ca2+). Receptor aggregation also results in the phosphorylation of adaptor protein NTAL/LAT2 which then recruits GAB2. PI3K associates with phosphorylated GAB2 and catalyses the formation of PIP3 in the membrane, which attracts many PH domain proteins like BTK, PLC-gamma, AKT and PDK. PI3K mediated activation of AKT then regulate the mast cell proliferation, development and survival (Gu et al. 2001).
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Innate immunity encompases the nonspecific part of immunity tha are part of an individual's natural biologic makeup
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Ubiquitin ligase UBE1L is the ISG15 activating enzyme. UBE1L activates ISG15 in an ATP-dependent process that links UBE1L to ISG15 via a thioester bond. Arginine 153 (R153) in human ISG15 is identified as the key residue for ISG15 and UBE1L's interaction.
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Interferon-stimulated gene 15 (ISG15) is a member of the ubiquitin-like (Ubl) family. It is strongly induced upon exposure to type I Interferons (IFNs), viruses, bacterial LPS, and other stresses. Once released the mature ISG15 conjugates with an array of target proteins, a process termed ISGylation. ISGylation utilizes a mechanism similar to ubiquitination, requiring a three-step enzymatic cascade. UBE1L is the ISG15 E1 activating enzyme which specifically activates ISG15 at the expense of ATP. ISG15 is then transfered from E1 to the E2 conjugating enzyme UBCH8 and then to the target protein with the aid of an ISG15 E3 ligase, such as HERC5 and EFP. Hundreds of target proteins for ISGylation have been identified. Several proteins that are part of antiviral signaling pathways, such as RIG-I, MDA5, Mx1, PKR, filamin B, STAT1, IRF3 and JAK1, have been identified as targets for ISGylation. ISG15 also conjugates some viral proteins, inhibiting viral budding and release. ISGylation appears to act either by disrupting the activity of a target protein and/or by altering its localization within the cell.
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The pericentriolar stacks of Golgi cisternae undergo extensive fragmentation and reorganization in mitosis. In mammalian cells, Golgi apparatus consists of stacked cisternae that are connected by tubules to form a ribbon-like structure in the perinuclear region, in vicinity of the centrosome. Reorganization of the Golgi apparatus during cell division allows both daughter cells to inherit this organelle, and may play additional roles in the organization of the mitotic spindle. First changes in the structure of the Golgi apparatus likely start in G2 and are subtle, involving unlinking of the Golgi ribbon into separate stacks. These changes are required for the entry of mammalian cells into mitosis (Sutterlin et al. 2002). This initial unlinking of the Golgi ribbon depends on GRASP proteins and on CTBP1 (BARS) protein, which induces the cleavage of the tubular membranes connecting the stacks (Hidalgo Carcedo et al. 2004, Colanzi et al. 2007), but the exact mechanism is not known. Activation of MEK1/2 also contributes to unlinking of the Golgi ribbon in G2 (Feinstein and Linstedt 2007). From prophase to metaphase, Golgi cisternae undergo extensive fragmentation that is a consequence of unstacking of Golgi cisternae and cessation of transport through Golgi. At least three mitotic kinases, CDK1, PLK1 and MEK1, regulate these changes. CDK1 in complex with cyclin B phosphorylates GOLGA2 (GM130) and GORASP1 (GRASP65), constituents of a cis-Golgi membrane complex (Lowe et al. 1998, Preisinger et al. 2005). Phosphorylation of GOLGA2 prevents binding of USO1 (p115), a protein localizing to the membrane of ER (endoplasmic reticulum) to Golgi transport vesicles and cis-Golgi, thereby impairing fusion of these vesicles with cis-Golgi cisternae and stopping ER to Golgi transport (Lowe et al. 1998, Seeman et al. 2000, Moyer et al. 2001). Phosphorylation of GORASP1 by CDK1 enables further phosphorylation of GORASP1 by PLK1 (Sutterlin et al. 2001, Preisinger et al. 2005). Phosphorylation of GORASP1 by CDK1 and PLK1 impairs stacking of Golgi cisternae by interfering with formation of GORASP1 trans-oligomers that would normally link the Golgi cisternae together (Wang et al. 2003, Wang et al. 2005, Sengupta and Linstedt 2010). In the median Golgi, GORASP2 (GRASP55), a protein that forms a complex with BLFZ1 (Golgin-45) and RAB2A GTPase and contributes to cisternae stacking and Golgi trafficking (Short et al. 2001), is also phosphorylated in mitosis. Phosphorylation of GORASP2 by MEK1/2-activated MAPK1 (ERK2) and/or MAPK3-3 (ERK1b in human, Erk1c in rat) contributes to Golgi unlinking in G2 and fragmentation of Golgi cisternae in mitotic prophase (Acharya et al. 1998, Jesch et al. 2001, Colanzi et al. 2003, Shaul and Seger 2006, Duran et al. 2008, Feinstein and Linstedt 2007, Feinstein and Linstedt 2008, Xiang and Wang 2010).
At the beginning of mitosis, MASTL (GWL, Greatwall kinase) is activated by phosphorylation at several key sites. Many of these sites, including functionally important threonine residues T194, T207 and T741 (corresponding to Xenopus residues T193, T206 and T748), are proline directed, matching CDK1 consensus sequence, and thus probably phosphorylated by CDK1, as shown by in vitro studies (Yu et al. 2006. Blake-Hodek et al. 2012). Phosphorylation of the serine residue S875 (S883 in Xenopus) is implicated as critical for the mitotic function of MASTL (Vigneron et al. 2011) and likely occurs through autophosphorylation (Blake-Hodek et al. 2012). Other kinases, such as PLK1 (Vigneron et al. 2011) and other MASTL phosphorylation sites may also be involved in mitotic activation of MASTL (Yu et al. 2006, Vigneron et al. 2011, Blake-Hodek et al. 2012). Phosphorylation of the serine residue S102 (S101 in Xenopus) is functionally important but the responsible kinase has not been identified (Blake-Hodek et al. 2012).
As a first step towards capturing the array of processes by which a fertilized egg gives rise to the diverse tissues of the body, examples of three kinds of processes have been annotated. These are aspects of the roles of cell adhesion molecules in axonal guidance and myogenesis, of transcriptional regulation in hematopoiesis (specifically, B lymphopoiesis), pancreatic beta cell and white adipocyte differentiation, and molecular events of "nodal" signaling.
CDK1-mediated phosphorylation of GORASP1 (GRASP65) enables GORASP1 to recruit PLK1 (Preisinger et al. 2005). PLK1 phosphorylates GORASP1 on serine residue S189 (Sengupta and Linstedt 2010). This serine residue is near the GORASP1 region involved in GORASP1 dimerization and oligomerization, a process underlying the stacking of cis-Golgi cisternae (Wang et al. 2003). The phosphorylation of S189 by PLK1 impairs Golgi cisternae stacking (tethering), contributing to Golgi unlinking and fragmentation in mitosis, probably by preventing formation of GORASP1 dimers and oligomers (Sutterlin et al. 2001, Sengupta and Linstedt, 2010). Two other potential phosphorylation sites that match PLK1 substrate consensus sequence exist in GORASP1, but their functional significance has not yet been examined (Sengupta and Linstedt, 2010).
Critical role for Ebf1 and Ebf2 in the adipogenic transcriptional cascade
The GLUT4 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Adipogenesis is the process of cell differentiation by which preadipocytes become adipocytes. During this process the preadipocytes cease to proliferate, begin to accumulate lipid droplets and develop morphologic and biochemical characteristics of mature adipocytes such as hormone responsive lipogenenic and lipolytic programs. The most intensively studied model system for adipogenesis is differentiation of the mouse 3T3-L1 preadipocyte cell line by an induction cocktail of containing mitogens (insulin/IGF1), glucocorticoid (dexamethasone), an inducer of cAMP (IBMX), and fetal serum (Cao et al. 1991, reviewed in Farmer 2006). More recently additional cellular models have become available to study adipogenesis that involve almost all stages of development (reviewed in Rosen and MacDougald 2006). In vivo knockout mice lacking putative adipogenic factors have also been extensively studied. Human pathways are traditionally inferred from those discovered in mouse but are now beginning to be validated in cellular models derived from human adipose progenitors (Fischer-Posovszky et al. 2008, Wdziekonski et al. 2011). Adipogenesis is controlled by a cascade of transcription factors (Yeh et al. 1995, reviewed in Farmer 2006, Gesta et al. 2007). One of the first observable events during adipocyte differentiation is a transient increase in expression of the CEBPB (CCAAT/Enhancer Binding Protein Beta, C/EBPB) and CEBPD (C/EBPD) transcription factors (Cao et al. 1991, reviewed in Lane et al. 1999). This occurs prior to the accumulation of lipid droplets. However, it is the subsequent inductions of CEBPA and PPARG that are critical for morphological, biochemical and functional adipocytes. Ectopic expression of CEBPB alone is capable of inducing substantial adipocyte differentiation in fibroblasts while CEBPD has a minimal effect. CEBPB is upregulated in response to intracellular cAMP (possibly via pCREB) and serum mitogens (possibly via Krox20). CEBPD is upregulated in response to glucocorticoids. The exact mechanisms that upregulate the CEBPs are not fully known. CEBPB and CEBPD act directly on the Peroxisome Proliferator-activated Receptor Gamma (PPARG) gene by binding its promoter and activating transcription. CEBPB and CEBPD also directly activate the EBF1 gene (and possibly other EBFs) and KLF5 (Jimenez et al. 2007, Oishi 2005). The EBF1 and KLF5 proteins, in turn bind, and activate the PPARG promoter. Other hormones, such as insulin, affect PPARG expression and other transcription factors, such as ADD1/SREBP1c, bind the PPARG promoter. This is an area of ongoing research. During adipogenesis the PPARG gene is transcribed to yield 2 variants. The adipogenic variant 2 mRNA encodes 30 additional amino acids at the N-terminus compared to the widely expressed variant 1 mRNA. PPARG encodes a type II nuclear hormone receptor (remains in the nucleus in the absence of ligand) that forms a heterodimer with the Retinoid X Receptor Alpha (RXRA). The heterodimer was initially identified as a complex regulating the aP2/FABP4 gene and named ARF6 (Tontonoz et al. 1994). The PPARG:RXRA heterodimer binds a recognition sequence that consists of two hexanucleotide motifs (DR1 motifs) separated by 1 nucleotide. Binding occurs even in the absence of ligands, such as fatty acids, that activate PPARG. In the absence of activating ligands, the PPARG:RXRA complex recruits repressors of transcription such as SMRT/NCoR2, NCoR1, and HDAC3 (Tontonoz and Spiegelman 2008). Each molecule of PPARG can bind 2 molecules of activating ligands. Although, the identity of the endogenous ligands of PPARG is unknown, exogenous activators include fatty acids and the thiazolidinedione class of antidiabetic drugs (reviewed in Berger et al. 2005, Heikkinen et al. 2007, Lemberger et al. 1996). The most potent activators of PPARG in vitro are oxidized derivatives of unsaturated fatty acids.. Upon binding activating ligands PPARG causes a rearrangement of adjacent factors: Corepressors such as SMRT/NCoR2 are lost and coactivators such as TIF2, PRIP, CBP, and p300 are recruited (Tontonoz and Spiegelman). PPARG also binds directly to the TRAP220 subunit of the TRAP/Mediator complex that recruits RNA polymerase II. Thus binding of activating ligand by PPARG causes transcription of PPARG target genes. Targets of PPARG include genes involved in differentiation (PGAR/HFARP, Perilipin, aP2/FABP4, CEBPA), fatty acid transport (LPL, FAT/CD36), carbohydrate metabolism (PEPCK-C, AQP7, GK, GLUT4), and energy homeostasis (LEPTIN and ADIPONECTIN) (Perera et al. 2006). Within 10 days of differentiation CEBPB and CEBPD are no longer located at the PPARG promoter. Instead CEBPA is present. EBF1 and PPARG bind the CEBPA promoter and activate transcription of CEBPA, one of the key transcription factors in adipogenesis. A current hypothesis posits a self-reinforcing loop that maintains PPARG expression and the differentiated state: PPARG activates CEBPA and CEBPA activates PPARG. Additionally EBF1 (and possibly other EBFs) activates CEBPA, CEBPA activates EBF1, and EBF1 activates PPARG.
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Phosphorylation of CDCA5 (Sororin) coincides with dissociation of CDCA5 from chromosomal arms in prometaphase. Several serine and threonine residues in CDCA5 are phosphorylated by CDK1 in prometaphase, but only the three sites that perfectly match the CDK1 consensus phosphorylation sequence are shown here - serines S21 and S75 and threonine T159 (Drier et al. 2011, Zhang et al. 2011).
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Prior to anaphase onset, sister-chromatids are held together by cohesin complexes. PLK1-dependent phosphorylation of the cohesin subunit STAG2 (SA2) (Hauf et al. 2005) promotes dissociation of cohesins from chromosomal arms in prometaphase (Hauf et al. 2001). Besides phosphorylating STAG2, PLK1 also phosphorylates RAD21 cohesin subunit, but the phosphorylation of RAD21 is not required for the dissociation of cohesin from chromosomal arms in early mitosis (Hauf et al. 2005). There are several potential PLK1 phosphorylation sites in STAG2 and RAD21, but the exact positions of in vivo phosphorylation of STAG2 and RAD21 by PLK1 have not been explicitly established (Hauf et al. 2005). It is likely that the phosphorylation of cohesin-bound CDCA5 (Sororin) by CDK1 creates a docking site for PLK1 at threonine T159 of CDCA5, thus enabling PLK1 to phosphorylate cohesin subunits (Zhang et al. 2011).
The activity of MASTL, also known as the Greatwall kinase (GWL), is necessary for the entry and progression of mitosis. MASTL is activated by phosphorylation of several key residues during mitotic entry. Phosphorylation on the serine residue S875 (S883 in Xenopus), likely through autophosphorylation (Blake-Hodek et al. 2012) appears to be critical (Vigneron et al. 2011). Several other sites, including putative CDK1 targets T194, T207 and T741, contribute to the full activation of MASTL (Yu et al. 2006, Blake-Hodek et al. 2012). Other kinases, such as PLK1 (Vigneron et al. 2011) and other MASTL phosphorylation sites may also be functionally important (Yu et al. 2006, Blake-Hodek et al. 2012). Activated MASTL phosphorylates ARPP19 and ENSA on serines S62 and S67, respectively, enabling them to bind to and inhibit the phosphatase activity of PP2A complexed with the regulatory subunit PPP2R2D (B55-delta). Inhibition of PP2A-PPP2R2D activity by ARPP19 or ENSA prevents dephosphorylation of CDK1 targets, hence allowing entry and maintenance of mitosis (Mochida et al. 2010, Gharbi-Ayachi et al. 2010, Burgess et al. 2010).
During prophase, the chromatin in the nucleus condenses, and the nucleolus disappears. Centrioles begin moving to the opposite poles or sides of the cell. Some of the fibers that extend from the centromeres cross the cell to form the mitotic spindle.
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Concerted action of two cation filters in the aquaporin water channel
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The L1 family of cell adhesion molecules (L1CAMs) are a subfamily of the immunoglobulin superfamily of transmembrane receptors, comprised of four structurally related proteins: L1, Close Homolog of L1 (CHL1), NrCAM, and Neurofascin. These CAMs contain six Ig like domains, five or six fibronectin like repeats, a transmembrane region and a cytoplasmic domain. The L1CAM family has been implicated in processes integral to nervous system development, including neurite outgrowth, neurite fasciculation and inter neuronal adhesion. L1CAM members are predominately expressed by neuronal, as well as some nonneuronal cells, during development. Except CHL1 all the other members of L1 family contain an alternatively spliced 12-nclueotide exon, encoding the amino acid residues RSLE in the neuronal splice forms but missing in the non-neuronal cells. The extracellular regions of L1CAM members are divergent and differ in their abilities to interact with extracellular, heterophilic ligands. The L1 ligands include other Ig-domain CAMs (such as NCAM, TAG-1/axonin and F11), proteoglycans type molecules (neurocan), beta1 integrins, and extra cellular matrix protein laminin, Neuropilin-1, FGF and EGF receptors. Some of these L1-interacting proteins also bind to other L1CAM members. For example TAG-1/axonin interact with L1 and NrCAM; L1, neurofascin and CHL1 binds to contactin family members. The cytoplasmic domains of L1CAM members are most highly conserved. Nevertheless, they have different cytoplasmic binding partners, and even those with similar binding partners may be involved in different signaling complexes and mechanisms. The most conserved feature of L1CAMs is their ability to interact with the actin cytoskeletal adapter protein ankyrin. The cytoplasmic ankyrin-binding domain, exhibits the highest degree of amino acid conservation throughout the L1 family.
Axon guidance / axon pathfinding is the process by which neurons send out axons to reach the correct targets. Growing axons have a highly motile structure at the growing tip called the growth cone, which senses the guidance cues in the environment through guidance cue receptors and responds by undergoing cytoskeletal changes that determine the direction of axon growth. Guidance cues present in the surrounding environment provide the necessary directional information for the trip. These extrinsic cues have been divided into attractive or repulsive signals that tell the growth cone where and where not to grow. Genetic and biochemical studies have led to the identification of highly conserved families of guidance molecules and their receptors that guide axons. These include netrins, Slits, semaphorins, and ephrins, and their cognate receptors, DCC and or uncoordinated-5 (UNC5), roundabouts (Robo), neuropilin and Eph. In addition, many other classes of adhesion molecules are also used by growth cones to navigate properly which include NCAM and L1CAM.
The GLUT2 gene is transcribed, its mRNA is translated, and the protein product is localized to the plasma membrane. GLUT2 expression is positively regulated by HNF1A. In vivo, pancreatic GLUT2 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) and interactions between the HNF1A protein product and the GLUT2 promoter have been demomstrated in vitro (Ban et al. 2002). However, the molecular details of GLUT2 expression in intact pancreatic beta cells have not been studied in humans, but are inferred from corresponding ones worked out in the mouse.
At the end of this reaction, 1 molecule of 'pyruvate kinase, liver and RBC' is present. This reaction takes place in the 'nucleus'.
Besides adhesive roles in cell cell interaction, L1 functions as a signal transducing receptor providing neurons with cues from their environment for axonal growth and guidance. L1 associates with beta1 integrins on the cell surface to induce a signaling pathway involving sequential activation of pp60csrc, Vav2 -GEF, Rac1, PAK1, MEK and ERK1/2. L1 stimulates cell migration and neurite outgrowth through the MAP kinases ERK1/2. CHL1 also associates with integrins and activates a MAPK signaling pathway via pp60c-src, MEK and ERK1/2. L1 also binds the Sema3A receptor neuropilin1 and acts as an obligate coreceptor to mediate Sema3A induced growth cone collapse and axon repulsion. This repulsion can be converted to attraction by homophilic binding of L1 on an apposing cell in trans with L1 complexed with Neuropilin1 (NP1) in the responding neuron. L1 also interacts with FGF receptor and activates PLC gamma and DAG, resulting in the production of arachidonic acid and subsequent opening of voltage-gated channels.
The Platelet glycoprotein IV gene (CD36, PAS IV, GPIV) is transcribed to yield mRNA and the mRNA is translated to yield proteind.
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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.
Two transcription factors, PDX1 and HNF1A, play key roles in maintaining the gene expression pattern characteristic of mature beta cells in the endocrine pancreas. Targets of these regulatory molecules include genes encoding insulin, the GLUT2 glucose transporter, the liver- (and pancreas) specific form of pyruvate kinase and other transcription factors including HNF4A, HNF4G, and FOXA3. PDX1 expression in turn is controlled by the activities of MAFA, FOXA2, and PAX6, and negatively regulated via AKT (Chakrabarti and Mirmira 2003; Servitja and Ferrer 2004).
The normal development of the pancreas during gestation has been intensively investigated over the past decade especially in the mouse (Servitja and Ferrer 2004; Chakrabarti and Mirmira 2003). Studies of genetic defects associated with maturity onset diabetes of the young (MODY) has provided direct insight into these processes as they take place in humans (Fajans et al. 2001). During embryogenesis, committed epithelial cells from the early pancreatic buds differentiate into mature endocrine and exocrine cells. It is helpful to schematize this process into four consecutive cellular stages, to begin to describe the complex interplay of signal transduction pathways and transcriptional networks. The annotations here are by no means complete - factors in addition to the ones described here must be active, and even for the ones that are described, only key examples of their regulatory effects and interactions have been annotated. It is also important to realize that in the human, unlike the mouse, cells of the different stages can be present simultaneously in the developing pancreas and the linear representation of these developmental events shown here is an over-simplification of the actual developmental process (e.g., Sarkar et al. 2008). The first stage of this process involves the predifferentiated epithelial cells of the two pancreatic anlagen that arise from the definitive endoderm at approximately somite stages 11-15 and undergo budding from somite stages 20-22. This period corresponds to gestational days 8.75-9.5 in the mouse, and 26 in the human. Pancreatic buds subsequently coalesce to form a single primitive gland, while concomitantly a ductal tree lined by highly proliferative epithelial cells is formed. A subset of such epithelial cells is thought to differentiate into either endocrine or acinar exocrine cells. A third cellular stage is defined by the endocrine-committed progenitors that selectively express the basic helix-loop-helix transcription factor NEUROG3. NEUROG3 is known to activate a complex transcriptional network that is essential for the specification of endocrine cells. Many transcription factors that are activated by NEUROG3 are also involved in islet-subtype cellular specification and in subsequent stages of differentiation of endocrine cells. This transient cellular stage thus leads to the generation of all known pancreatic endocrine cells, including insulin-producing beta-cells, and glucagon-producing alpha cells, the final stage of this schematic developmental process. The diagram below summarizes interactions that take place between transcription factors and transcription factor target genes during these cellular stages, and shows cases where there is both functional evidence that a transcription factor is required for the target gene to be expressed, and biochemical evidence that this interaction is direct. We also describe instances where a signaling pathway is known to regulate a transcription factor gene in this process, even if the intervening signaling pathway is not fully understood.
The PEPCK-C gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Expression of the AQP-1 water channel in normal human tissues: a semiquantitative study using tissue microarray technology
A yeast chromosomal origin of DNA replication defined by multiple functional elements.
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Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy
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Communication between the synapse and the nucleus in neuronal development, plasticity, and disease
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The Akt activation inhibitor TCN-P inhibits Akt phosphorylation by binding to the PH domain of Akt and blocking its recruitment to the plasma membrane
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Mechanisms of transcription-coupled DNA repair.
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Insulin action on glucose transporters through molecular switches, tracks and tethers
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(S)-alpha-amino-beta-(3-indolyl)-propionic acid
Congenital Disorders of Glycosylation Overview
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Biochemical differences between rat and human cytochrome P450c17 support the different steroidogenic needs of these two species
The Mammalian Proteins MMS19, MIP18, and ANT2 Are Involved in Cytoplasmic Iron-Sulfur Cluster Protein Assembly
Cell cycle- and cell growth-regulated proteolysis of mammalian CDC6 is dependent on APC-CDH1.
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beta-catenin destruction complex: insights and questions from a structural perspective
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Enzymatic inactivation of leukotriene B4 by a novel enzyme found in the porcine kidney. Purification and properties of leukotriene B4 12-hydroxydehydrogenase
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Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis
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The kinesin-like protein CENP-E is kinetochore-associated throughout poleward chromosome segregation during anaphase-A
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Systematic analysis of myotubularins: heteromeric interactions, subcellular localisation and endosome related functions
A role for the endoplasmic reticulum protein retrotranslocation machinery during crosspresentation by dendritic cells
Multistep regulation of DNA replication by Cdk phosphorylation of HsCdc6.
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sn-Glycero-3-phosphocholine [ChEBI:10646]
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Expression cloning and characterization of a cDNA encoding a novel membrane protein required for the formation of O-acetylated ganglioside: a putative acetyl-CoA transporter
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Magnesium transporters: properties, regulation and structure
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The human homolog of the rat inositol phosphate multikinase is an inositol 1,3,4,6-tetrakisphosphate 5-kinase
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E2F mediated regulation of DNA replication
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1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate [ChEBI:16851]
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
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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
A novel microtubule-based motor protein (KIF4) for organelle transports, whose expression is regulated developmentally
Cloning, characterization, and chromosomal mapping of human aquaporin of collecting duct
Nicotinate phosphoribosyltransferase of human erythrocytes. Purification and properties.
Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers
Heterogeneous nuclear ribonucleoprotein R
Heterogeneous nuclear ribonucleoprotein A0
Heterogeneous nuclear ribonucleoprotein A3
U1 small nuclear ribonucleoprotein 70 kDa
Lysosomal disorders: from storage to cellular damage
The Golgi mitotic checkpoint is controlled by BARS-dependent fission of the Golgi ribbon into separate stacks in G2
Heterogeneous nuclear ribonucleoprotein A1
Heterogeneous nuclear ribonucleoproteins A2/B1
Heterogeneous nuclear ribonucleoprotein L
Heterogeneous nuclear ribonucleoprotein D0
Bile salt transporters: molecular characterization, function, and regulation
Vesicle pools, docking, priming, and release
Fractionation and characterization of a cyclic adenine ribonucleotide formed by tissue particles
NAGLU mutations underlying Sanfilippo syndrome type B
Structure-function analysis of human Spt4: evidence that hSpt4 and hSpt5 exert their roles in transcriptional elongation as parts of the DSIF complex.
Structure and expression of human dihydropteridine reductase.
Protein sorting receptors in the early secretory pathway
Translocation after synthesis of a four-nucleotide RNA commits RNA polymerase II to promoter escape.
Corticosteroid 11-beta-dehydrogenase, isozyme 1
The spindle checkpoint: structural insights into dynamic signalling
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High incidence of translocations t(11;14)(q13;q32) and t(4;14)(p16;q32) in patients with plasma cell malignancies
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Isolation and characterization of a human thiamine pyrophosphokinase cDNA
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Mutations in the urocanase gene UROC1 are associated with urocanic aciduria
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Live-cell imaging reveals a stable cohesin-chromatin interaction after but not before DNA replication
Developmental control of a G1-S transcriptional program in Drosophila
FGFR3-related dwarfism and cell signaling
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UDP-N-acetyl-D-galactosamine [ChEBI:9820]
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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
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Oxidation of tamoxifen by human flavin-containing monooxygenase (FMO) 1 and FMO3 to tamoxifen-N-oxide and its novel reduction back to tamoxifen by human cytochromes P450 and hemoglobin
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Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response
Protein kinase C phosphorylation of syntaxin 4 in thrombin-activated human platelets
Central spindle assembly and cytokinesis require a kinesin-like protein/RhoGAP complex with microtubule bundling activity
Isolation and characterization of propionyl-CoA carboxylase from normal human liver. Evidence for a protomeric tetramer of nonidentical subunits
Human glutamine phosphoribosylpyrophosphate amidotransferase. Two molecular forms interconvertible by purine ribonucleotides and phosphoribosylpyrophosphate
Endocytosis, recycling, and regulated exocytosis of glucose transporter 4
Identification of human intestinal alkaline sphingomyelinase as a novel ecto-enzyme related to the nucleotide phosphodiesterase family
Dynamics and function of phospholipase D and phosphatidic acid during phagocytosis
Characterization of human PLD2 and the analysis of PLD isoform splice variants
Structure-function analysis of Friedreich's ataxia mutants reveals determinants of frataxin binding and activation of the Fe-S assembly complex
Novel inositol polyphosphate 5-phosphatase localizes at membrane ruffles
Members of the Dedicator of cytokinesis (DOCK) family, also known as the Dock180 superfamily, are Rho GTPase guanine nucleotide exchange factors (GEFs), modulating Rho GTPase activity (Cote & Vuori 2002). All eleven human members share the presence of two evolutionarily conserved protein domains, termed DHR-1 and DHR-2 (Cote & Vuori 2007). The DHR-2 domains of several DOCKs interact with the nucleotide-free forms of Rho GTPases, intermediates in the catalytic reaction leading to the exchange of GDP for GTP. DHR-2 domains have been shown necessary and sufficient to promote specific guanine nucleotide exchange on various Rho GTPases, both in vitro and in vivo. Inactivation of the DHR-2 domain in DOCK1 (Dock180) has been shown to block Rac activation, cell migration and phagocytosis (Brugnera et al. 2002, Grimsley et al. 2004, Cote & Vuori 2002). The DHR-1 domain of DOCK1 was shown to mediate a specific interaction with PIP2 and PIP3 signaling lipids in vitro and in cells (Cote et al. 2005). Mutations of the DOCK1 DHR-1 domain blocked Rac-dependent cell elongation and cell migration suggesting that the role of DHR-1 is to position DOCK1 at sites of PIP3 production by PI3-kinase, coupling this to Rac signaling (Cote & Vuori 2007).
Chromokinesins consist of the kinesin-4 and kinesin-10 families.They act in various steps of mitosis, including chromosome condensation, metaphase alignment, chromosome segregation and cytokinesis (Mazumdar & Misteli 2005). Both families consist of homodimeric microtubule-based plus-end directed motor proteins (Sekine et al. 1994, Yajima et al. 2003).
Identification and characterization of choline transporter-like protein 2, an inner ear glycoprotein of 68 and 72 kDa that is the target of antibody-induced hearing loss
Inositol-tetrakisphosphate 1-kinase (ITPK1) phosphorylates Ins(1,3,4)P3 on O-5 to form Ins(1,3,4,5)P4.
Inositol-tetrakisphosphate 1-kinase (ITPK1) can phosphorylate inositol polyphosphates Ins(3,4,5,6)P4 at position 1 to form Ins(1,3,4,5,6)P5. This reaction is thought to have regulatory importance, since Ins(3,4,5,6)P4 is an inhibitor of plasma membrane Ca2+-activated Cl- channels.
Platelet activation begins with the initial binding of adhesive ligands and of the excitatory platelet agonists (released or generated at the sites of vascular trauma) to cognate receptors on the platelet membrane (Ruggeri 2002). Intracellular signaling reactions then enhance the adhesive and procoagulant properties of tethered platelets or of platelets circulating in the proximity. Once platelets have adhered they degranulate, releasing stored secondary agents such as ADP, ATP, and synthesize thromboxane A2. These amplify the response, activating and recruiting further platelets to the area and promoting platelet aggregation. These amplify the response, activating and recruiting further platelets to the area and promoting platelet aggregation. Adenosine nucleotides signal through P2 purinergic receptors on the platelet membrane. ADP activates P2Y1 and P2Y12, which signal via both the alpha and gamma:beta components of the heterotrimeric G-protein (Hirsch et al. 2001, 2006), while ATP activates the ionotropic P2X1 receptor (Kunapuli et al. 2003). Activation of these receptors initiates a complex signaling cascade that ultimately results in platelet activation, aggregation and thrombus formation (Kahner et al. 2006). Integrin AlphaIIbBeta3 is the most abundant platelet receptor, with 40 000 to 80 000 copies per resting platelet, acting as a major receptor for fibrinogen and other adhesive molecules (Wagner et al. 1996). Activation of AlphaIIbBeta3 enhances adhesion and leads to platelet-platelet interactions, and thus aggregation (Philips et al. 1991). GP VI is the most potent collagen receptor initiating signal generation, an ability derived from its interaction with the FcRI gamma chain. This results in the phosphorylation of the gamma-chain by non-receptor tyrosine kinases of the Src family (1). The phosphotyrosine motif is recognized by the SH2 domains of Syk, a tyrosine kinase. This association activates the Syk enzyme, leading to activation (by tyrosine phosphorylation) of PLC gamma2 (2). Thrombin is an important platelet agonist generated on the membrane of stimulated platelets. Thrombin acts via cell surface Protease Activated Receptors (PARs). PARs are G-protein coupled receptors activated by a proteolytic cleavage in an extracellular loop (Vu, 1991) (3). Activated PARs signal via G alpha q (4) and via the beta:gamma component of the G-protein (5). Both stimulate PLC giving rise to PIP2 hydrolysis and consequent activation of PI3K (6). PLCgamma2 activation also gives rise to IP3 (7) which stimulates the IP3 receptor (8) leading to increased intracellular calcium. Platelet activation further results in the scramblase-mediated transport of negatively-charged phospholipids to the platelet surface. These phospholipids provide a catalytic surface (with the charge provided by phosphatidylserine and phosphatidylethanolamine) for the tenase complex (formed by the activated forms of the blood coagulation factors factor VIII and factor I).
Activation of phospholipase C enzymes results in the generation of second messengers of the phosphatidylinositol pathway. The events resulting from this pathway are a rise in intracellular calcium and activation of Protein Kinase C (PKC). Phospholipase C cleaves the phosphodiester bond in PIP2 to form 1,2 Diacylglycerol (DAG) and 1,4,5-inositol trisphosphate (IP3). IP3 opens Ca2+ channels in the platelet dense tubular system, raising intracellular Ca2+ levels. DAG is a second messenger that regulates a family of Ser/Thr kinases consisting of PKC isozymes (Nishizuka 1995). DAG achieves activation of PKC isozymes by increasing their affinity for phospholipid. Most PKC enzymes are also calcium-dependent, so their activation is in synergy with the rise in intracellular Ca2+. Platelets contain several PKC isoforms that can be activated by DAG and/or Ca2+ (Chang 1997).
Actin capping protein (CP) was named for its ability to bind the barbed ends of actin filaments. CP inhibits the addition and loss of actin subunits at the barbed end and is important for the dynamics of actin filament assembly, and therefore important for the control of cell shape and movement. CP was called beta-actinin when first characterized and purified from muscle (Maruyama 1966). Actin polymerization is controlled by a large cellular excess of capping proteins which bind to the barbed end of actin filaments preventing elongation.
F-actin-capping protein binds in a Ca2+-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits. Unlike other capping proteins (such as gelsolin and severin), they do not sever actin filaments.
Leucine rich repeat-containing protein 16A (CARMIL homolog) binds F-actin capping protein (CP) with high affinity, significantly decreasing the affinity of CP for actin barbed ends. Actin polymerization occurs at the barbed end; proteins like CP that cap the barbed end inhibit elongation. Inhibition of CP therefore enhances the rate of barbed-end actin polymerization. In cells, GFP-LRRC16A was seen to be concentrated in lamellipodia and increased the fraction of cells with large lamellipodia. Decreasing LRRC16A levels with siRNA lowered F-actin levels, decreased lamellipodia protrusion and slowed cell migration.
Inositol-tetrakisphosphate 1-kinase (ITPK1) phosphorylates Ins(1,3,4)P3 on O-6 to form Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate (InsP6) pathway.
Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1)
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).
Human kinesin-7, or CENP-E was one of the first kinesins to be discovered (Yen et al. 1991). It is essential for mammalian development, having a role in stabilizing kinetochore-microtubule capture (Putkey et al. 2002), CENP-E is an integral component of kinetochore corona fibers that link centromeres to spindle microtubules and localizes to kinetochores throughout all phases of mitotic chromosome movement (early premetaphase through anaphase A). Though originally reported to be minus-end-directed it is now believed to be a plus-end-directed dimeric kinesin (Espeut et al. 2008). It is sequestered in the cytoplasm until nuclear envelope breakdown and then localizes to its chromosomal cargo at the kinetochores (Brown et al. 1996).
Cytokinesis requires the central spindle, which forms during anaphase by the bundling of antiparallel nonkinetochore microtubules. Microtubule bundling and completion of cytokinesis require MKLP1, a kinesin-6 family member, and RACGAP1 (MgcRacGap), which contains a RhoGAP domain. These form a heterotetrameric complex known as centralspindlin. Centralspindlin, but not its individual components, strongly promotes microtubule bundling in vitro.
Kinesin-14 proteins have a C-terminal motor domain. At least four members of the group (Dm Ncd, Sc KAR3, Cg CHO2, At KCBP) have been demonstrated to be minus-end directed motors (Walker et al. 1990), in contrast to the usual plus-end directed motility of other kinesin proteins. During spindle formation, Kinesin-14 cross-links antiparallel microtubules and slides them together (thereby generating inward forces) to balance the outward forces generated by plus-end-directed kinesins of the Kinesin-5 family. Kinesin-14 family members also gather microtubule minus-ends and focus them into spindle poles. Mutation or inhibition of Kinesin-14 family members often results in disordered or splayed meiotic spindle poles (Ambrose et al. 2005).
Kinesin-8 is a plus-end-directed dimeric kinesin with an internal motor domain (Loughlin et al. 2008) that can depolymerize stable microtubuless specifically at their plus-ends (Pereira et al. 1997) in a length-dependent manner (Varga et al. 2006). Human kinesin-8 KIF18A is believed to promote chromosome congression by attenuating chromosome oscillation magnitudes (Stumpff et al. 2008).
Kinesins are a superfamily of microtubule-based motor proteins that have diverse functions in transport of vesicles, organelles and chromosomes, and regulate microtubule dynamics. There are 14 families of kinesins, all reprsented in humans. A standardized nomenclature was published in 2004 (Lawrence et al.).
Kinesins consume ATP to power the motor which allows them to move along microtubules. The motor region contains highly conserved Switch 1 (SSRSH) and 2 (DLAGSE) motifs which change conformation during ATP hydrolysis (Rice et al. 1999). These form a salt-bridge that, in myosin, closes the nucleotide-binding cleft, enabling the motor to hydrolyze ATP (Geeves & Holmes 1999). This closed conformation has now been seen by cryo-electron microscopy in human conventional kinesin (Sindelar & Downing 2010) and in a crystal structure of the frog kinesin-5 Eg5 (Parke et al. 2010).
Hemostasis is a physiological response that culminates in the arrest of bleeding from an injured vessel. Under normal conditions the vascular endothelium supports vasodilation, inhibits platelet adhesion and activation, suppresses coagulation, enhances fibrin cleavage and is anti-inflammatory in character. Under acute vascular trauma, vasoconstrictor mechanisms predominate and the endothelium becomes prothrombotic, procoagulatory and proinflammatory in nature. This is achieved by a reduction of endothelial dilating agents: adenosine, NO and prostacyclin; and by the direct action of ADP, serotonin and thromboxane on vascular smooth muscle cells to elicit their contraction (Becker et al. 2000). The chief trigger for the change in endothelial function that leads to the formation of a haemostatic thrombus is the loss of the endothelial cell barrier between blood and extracellular matrix components (Ruggeri 2002). Circulating platelets identify and discriminate areas of endothelial lesions; here, they adhere to the exposed sub endothelium. Their interaction with the various thrombogenic substrates and locally generated or released agonists results in platelet activation. This process is described as possessing two stages, firstly, adhesion - the initial tethering to a surface, and secondly aggregation - the platelet-platelet cohesion (Savage & Cattaneo et al. 2001). Three mechansism contribute to the loss of blood following vessel injury. The vessel constricts, reducing the loss of blood. Platelets adhere to the site of injury, become activated and aggregate with fibrinogen into a soft plug that limits blood loss, a process termed primary hemostasis. Proteins and small molecules are released from granules by activated platelets, stimulating the plug formation process. Fibrinogen from plasma forms bridges between activated platelets. These events initiate the clotting cascade (secondary hemostasis). Negatively-charged phospholipids exposed at the site of injury and on activated platelets interact with tissue factor, leading to a cascade of reactions that culminates with the formation of an insoluble fibrin clot.
Megakaryocytes (MKs) give rise to circulating platelets (thrombocytes) through terminal differentiation of MKs which release cytoplasmic fragments as circulating platelets. As MKs mature they undergo endoreduplication (polyploidisation) and expansion of cytoplasmic mass to cell sizes larger than 50-100 microns, and ploidy ranges up to 128 N. As MK's mature, the polyploid nucleus becomes horseshoe-shaped, the cytoplasm expands, and platelet organelles and the demarcation membrane system are amplified. Proplatelet projections form which give rise to de novo circulating platelets (Deutsch & Tomer 2006). The processes of megakaryocytopoiesis and platelet production occur within a complex microenvironment where chemokines, cytokines and adhesive interactions play major roles (Avecilla et al. 2004). Megakaryocytopoiesis is regulated at several levels including proliferation, differentiation and platelet release (Kaushansky 2003). Thrombopoietin (TPO/c-Mpl ligand) is the most potent cytokine stimulating proliferation and maturation of MK progenitors (Kaushansky 2005) but many other growth factors are involved. MK development is controlled by the action of multiple Transcriptin Factors, many MK-specific genes are co-regulated by GATA and friend of GATA (FOG), RUNX1 and ETS proteins. Nuclear factor erythroid 2 (NF-E2) which has an MK-erythroid specific 45-kDa subunit controls terminal MK maturation, proplatelet formation and platelet release (Schulze & Shivdasani 2004). NF-E2 deficient mice have profound thrombocytopenia (Shiraga et al. 1999). c-myb functions with p300 as a negative regulator of thrombopoiesis (Metcalf et al. 2005). During MK maturation, internal membrane systems, granules and organelles are assembled. Cytoplasmic fragmentation requires changes in the MK cytoskeleton and formation of organelles and channels. Individual organelles migrate from the cell body to the proplatelet ends, with approximately 30 percent of organelles/granules in motion at any given time (Richardson et al. 2005).
Kinesin-5 motors are bipolar homotetramers with two motor domains at each end, separated by a stalk/tail region (Cole et al. 1994). During mitosis, Kinesin-5 motors function near the spindle midzone to maintain pole to pole distance. Motor domains attach to microtubules from opposite poles and translocate towards the plus ends, thereby pushing the spindle poles apart (Kapitein et al. 2005). Kinesin-5 is also involved in axon growth (Myers & Baas 2007).
Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9
ABCC4 (Multidrug resistance protein 4 /MOAT-B) is a member of the MRP/ABCC subfamily of ATP-binding cassette transporters, capable of pumping a wide variety of endogenous and xenobiotic anionic compounds out of the cell. ABCC4 also transports molecules involved in cellular signalling, including cyclic nucleotides, eicosanoids, urate and conjugated steroids. ABCC4 has a dual localisation in polarised cells that suggests a key function in cellular protection and extracellular signalling pathways. It is also highly expressed on platelet dense granule membranes where it is believed to contribute to the accumulation of dense granule content.
At the beginning of this reaction, 1 molecule of 'ATP', and 1 molecule of 'Syntaxin 4' are present. At the end of this reaction, 1 molecule of 'Phosphorylated syntaxin 4', and 1 molecule of 'ADP' are present. This reaction is mediated by the 'calcium-dependent protein kinase C activity' of 'Activated Ca++ and DAG dependent PKC'.
Platelet releasate contains a range of proteins that do not originate in specialized storage granules. In some cases platelet lysis may contribute to the presence of these proteins in the platelet relesate.
Alpha granules contain mainly polypeptides such as fibrinogen, von Willebrand factor, growth factors and protease inhibitors that supplement thrombin generation at the site of injury. In addtion to their role in hemostasis, platelets also contain angiogenesis stimulators and inhibitors (Italiano et al. 2008).
Constituents of the platelet alpha granule membrane are incorporated into the platelet membrane following exocytosis of granule content.
Platelets function as exocytotic cells, secreting a plethora of effector molecules at sites of vascular injury. Platelets contain a number of distinguishable storage granules including alpha granules, dense granules and lysosomes. On activation platelets release a variety of proteins, largely from storage granules but also as the result of apparent cell lysis. These act in an autocrine or paracrine fashion to modulate cell signaling. Alpha granules contain mainly polypeptides such as fibrinogen, von Willebrand factor, growth factors and protease inhibitors that that supplement thrombin generation at the site of injury. Dense granules contain small molecules, particularly adenosine diphosphate (ADP), adenosine triphosphate (ATP), serotonin and calcium, all recruit platelets to the site of injury.
After Platelet activation 'Proactivator polypeptide' from the lysosomal lumen is released in to the extracellular platelet releasate.
After Platelet activation '78 kDa glucose-regulated protein' from the endoplasmic reticulum lumen is released in to the extracellular platelet releasate.
A transforming mutation in the pleckstrin homology domain of AKT1 in cancer
Mitogen-activated protein kinase kinase 1-dependent Golgi unlinking occurs in G2 phase and promotes the G2/M cell cycle transition
Developmental regulation and cellular distribution of human cytosolic malate dehydrogenase (MDH1)
At the sites of vascular injury bioactive molecules such as thrombin, ADP, collagen, fibrinogen and thrombospondin are generated, secreted or exposed. These stimuli activate platelets, converting the major platelet integrin alphaIIbbeta3 from a resting state to an active conformation, in a process termed integrin priming or âinside-out signallingâ. Integrin activation refers to the change required to enhance ligand-binding activity. The activated alphaIIbbeta3 interacts with the fibrinogen and links platelets together in an aggregate to form a platelet plug. AlphaIIbbeta3 bound to fibrin generates more intracellular signals (outside-in signalling), causing further platelet activation and platelet-plug retraction. In the resting state the alpha and beta tails are close together. This interaction keeps the membrane proximal regions in a bent conformation that maintains alphaIIbbeta3 in a low affinity state. Integrin alphaIIbbeta3 is released from its inactive state by interaction with the protein talin. Talin interacts with the beta3 cytoplasmic domain and disrupts the salt bridge between the alpha and beta chains. This separation in the cytoplasmic regions triggers the conformational change in the extracellular domain that increases its affinity to fibrinogen. Much of talin exists in an inactive cytosolic pool, and the Rap1 interacting adaptor molecule (RIAM) is implicated in talin activation and translocation to beta3 integrin cytoplasmic domain.
The tethering of platelets to the site of vascular injury is the first step in the formation of a platelet thrombus. Firm adhesion of these tethered platelets, as well as the additional recruitment of others onto their surface leads to the formation of large platelet aggregates. The formation of a thrombus is strictly dependent on the formation of interplatelet bonds.
Calcium and DAG regulated guanine nucleotide exchange factors (CalDAG-GEFs, also called RasGRPs) contain a regulatory C1 diacylglycerol (DAG) -binding domain analogous to the C1 domain found in Protein Kinase C, and a pair of calcium-binding EF-hand domains. All forms show enhanced activity in response to DAG and bind calcium, but the effect of Ca2+ seems to differ between isoforms. CalDAG-GEFI exhibited additive enhancement of Rap1 activation in response to Ca2+ ionophore and phorbol ester (Kawasaki et al. 1998). RasGRP2, an isofom of CalDAG-GEFI with an alternatively spliced N-terminal extension, reported to target it to the plasma membrane, was stimulated by diacylglycerol but inhibited by calcium (Clyde-Smith et al. 2000). CalDAG-GEF II/RasGRP1 was additively stimulated by Ca2+ ionophore and phorbol ester. CalDAG-GEFI was found to primarily target Rap1A and inhibit Ras-dependent activation of the Erk/MAP kinase cascade (Kawasaki et al. 1998). RasGRP2 selectively activated N- and Ki-Ras, but not Ha-Ras. It also had Rap1A stimulating activity, but less than CalDAG-GEFI. The difference in substrate specificity seen for these isoforms may be due to their different cellular locations, as prolonged exposure to phorbol esters, or growth in serum, resulted in localization of CalDAG-GEFI to the cell membrane and restoration of Ras exchange activity (Clyde-Smith et al. 2000). CalDAG-GEF II/RasGRP1 targeted Ras proteins rather than Rap (Kawasaki et al. 1998, Ebinu et al. 1998). Mouse platelets that lack CalDAG-GEFI are severely compromised in integrin-dependent aggregation as a consequence of their inability to signal through CalDAG-GEFI to its target, the small GTPase Rap1 (Crittenden et al. 2004)
Activation of the novel Protein Kinase C (nPKC) isoforms (delta, epsilon, eta and theta) requires binding to the membrane lipid diacylglycerol (DAG). nPKC activation is sensitive to DAG concentration.
DNA end-joining catalyzed by human cell-free extracts.
Monoacylglycerol lipase (MAGL) is a key enzyme in the hydrolysis of the endocannabinoid 2-arachidonoylglycerol to arachidonate and glycerol. In adipocytes MAGL and hormone-sensitive lipase (LIPE) hydrolyze intracellular triglyceride stores. MAGL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides.
Diacylglycerol (DAG) is an important source of arachidonic acid, a signalling molecule and the precursor of the prostaglandins. In human platelet almost all the DAG produced from phosphatidylinositol degradation contains arachidonate (Takamura et al. 1987). DAG is hydrolysed by DAG lipase to 2-arachidonylglycerol (2-AG) which is further hydrolysed by monoacylglycerol lipase. 2-AG is an agonist of cannabinoid receptor 1.
Hydrolysis of phosphatidyl inositol-bisphosphate (PIP2) by phospholipase C (PLC) produces diacylglycerol (DAG) and inositol triphosphate (IP3). Both are potent second messengers. IP3 diffuses into the cytosol, but as DAG is a hydrophobic lipid it remains within the plasma membrane. IP3 stimulates the release of calcium ions from the smooth endoplasmic reticulum, while DAG activates the conventional and unconventional protein kinase C (PKC) isoforms, facilitating the translocation of PKC from the cytosol to the plasma membrane. The effects of DAG are mimicked by tumor-promoting phorbol esters. DAG is also a precursor for the biosynthesis of prostaglandins, the endocannabinoid 2-arachidonoylglycerol and an activator of a subfamily of TRP-C (Transient Receptor Potential Canonical) cation channels 3, 6, and 7.
Diacylglycerol kinases (DGKs) are intracellular lipid kinases that use ATP to phosphorylate diacylglycerol (DAG)., generating phosphatidic acid (PA). This lowers membrane DAG levels, regulating signalling proteins that require DAG for membrane association such as Protein Kinase C. PA is a signalling molecule that regulates Raf-1 and PKC zeta, and a substrate for the resynthesis of phosphatidylinositol.
At the beginning of this reaction, 1 molecule of 'ATP', and 1 molecule of 'Platelet SEC1 protein' are present. At the end of this reaction, 1 molecule of 'Phosphorylated platelet SEC1 protein', and 1 molecule of 'ADP' are present. This reaction is mediated by the 'calcium-dependent protein kinase C activity' of 'Activated Ca++ and DAG dependent PKC'.
The conventional Protein Kinase C (cPKC) isoforms have two membrane-targetting domains, a C1 domain which binds to the membrane lipid diacylglycerol (DAG) and a C2 domain which binds membrane phospholipids such as phosphatidylserine, in a calcium-dependent manner. Association of both domains with the plasma membrane produces a conformational change that releases an autoinhibitory pseudosubstrate segment from the substrate-binding cavity, allowing substrate binding and downstream signaling.
The human gene for 11 beta-hydroxysteroid dehydrogenase. Structure, tissue distribution, and chromosomal localization.
Activation of Src lies selectively downstream of P2Y1, but not P2Y12. The precise mechanism is not known, but Src regulation of the PI3K component of the intracellular calcium response downstream of P2Y12 represents a point of reciprocal cross-talk between P2Y1 and P2Y12 receptors.
Co-activation of P2Y1 and P2Y12 is necessary for complete platelet activation. P2Y1 is coupled to Gq and helps trigger the release of calcium from internal stores, leading to weak and reversible platelet aggregation. P2Y12 is Gi coupled, inhibiting adenylate cyclase, leading to decreased cAMP, a consequent decrease in cAMP-dependent protein kinase activity which increases cytoplasmic [Ca2+], necessary for activation (Woulfe et al. 2001). In activated platelets, P2Y12 signaling is required for the amplification of aggregation induced by all platelet agonists including collagen, thrombin, thromboxane, adrenaline and serotonin. P2Y12 activation causes potentiation of thromboxane generation, secretion leading to irreversible platelet aggregation and thrombus stabilization.
Nitric Oxide (NO) inhibits smooth muscle cell proliferation and migration, oxidation of low-density lipoproteins, and platelet aggregation and adhesion. It can stimulate vasodilatation of the endothelium, disaggregation of Â preformed platelet aggregates and inhibits activated platelet recruitment to the aggregate. NO is synthesized from L-arginine by a family of isoformic enzymes known as nitric oxide synthase (NOS). Three isoforms, namely endothelial, neuronal, and inducible NOS (eNOS, nNOS, and iNOS, respectively), have been identified. The eNOS isoform is found in the endothelium and platelets. NO regulation of cyclic guanosine-3,5-monophosphate (cGMP), via activation of soluble guanylate cyclase, is the principal mechanism of negative control over platelet activity. Defects in this control mechanism have been associated with platelet hyperaggregability and associated thrombosis.
Under normal conditions the vascular endothelium supports vasodilation, inhibits platelet adhesion and activation, suppresses coagulation, enhances fibrin cleavage and is anti-inflammatory in character. Under acute vascular trauma, vasoconstrictor mechanisms predominate and the endothelium becomes prothrombotic, procoagulatory and proinflammatory in nature. This is achieved by a reduction of endothelial dilating agents: adenosine, NO and prostacyclin; and by the direct action of ADP, serotonin and thromboxane on vascular smooth muscle cells to elicit their contraction (Becker et al. 2000). Cyclooxygenase-2 (COX-2) and endothelial nitric oxide synthase (eNOS) are primarily expressed in endothelial cells. Both are important regulators of vascular function. Under normal conditions, laminar flow induces vascular endothelial COX-2 expression and synthesis of Prostacyclin (PGI2) which in turn stimulates endothelial Nitric Oxide Synthase (eNOS) activity. PGI2 and NO both oppose platelet activation and aggregation, as does the CD39 ecto-ADPase, which decreases platelet activation and recruitment by metabolizing platelet-released ADP.
Phosphatidylinositol-4-phosphate 5-kinase isozymes catalyze the synthesis of 3-phosphate-containing phosphatidylinositol signaling molecules
Cyclic guanosine monophosphate (cGMP) is an important secondary messenger synthesized by guanylate cyclases. cGMP has effects on phosphodiesterases (PDE), ion-gated channels, and the cGMP-dependent protein kinases (cGK, Protein Kinase G or PKG). It is involved in regulation of several physiological functions including vasodilation, platelet aggregation and neurotransmission. Elevation of intracellular cGMP activates PKG (Haslam et al. 1999) which regulates several intracellular molecules and pathways including the vasodilator-stimulated phosphoprotein (VASP) (Halbrugge et al. 1990) and the ERK pathway (Hood and Granger 1998, Li et al. 2001). cGMP mediates nitric oxide (NO)-induced vascular smooth muscle relaxation (Furchgott and Vanhoutte 1989). Phosphodiesterase 5 (PDE5) hydrolyzes cGMP; the PDE5 inhibitor sildenafil (Viagra) increases intracellular cGMP and thereby can be used as a treatment for erectile dysfunction (Corbin and Francis 1999). The role of the cGMP and PKG in platelet activation was controversial as increases in platelet cGMP levels were observed in response to both platelet agonists (thrombin, ADP or collagen) and inhibitors (NO donors such as sodium nitroprusside), but it is currently accepted that PKG inhibits platelet activation (Haslam et al. 1999). Consistent with this, nitric oxide (NO) donors that inhibit platelet activation enhance intracellular cGMP (Haslam et al. 1999). cGMP also plays an important stimulatory role in GPIb-IX-mediated platelet activation. Platelet responses to cGMP have been proposed to be biphasic, consisting of an early stimulatory response that promotes platelet activation followed by a delayed platelet inhibition that serves to limit the size of platelet aggregates (Li et al 2003).
The GPVI receptor is a complex of the GPVI protein with Fc epsilon R1 gamma (FcR). The Src family kinases Fyn and Lyn constitutively associate with the GPVI-FcR complex in platelets and initiate platelet activation through phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) in the FcR gamma chain, leading to binding and activation of the tyrosine kinase Syk. Downstream of Syk, a series of adapter molecules and effectors lead to platelet activation. The GPVI receptor signaling cascade is similar to that of T- and B-cell immune receptors, involving the formation of a signalosome composed of adapter and effector proteins. At the core of the T-cell receptor signalosome is the transmembrane adapter LAT and two cytosolic adapters SLP-76 and Gads. While LAT is essential for signalling to PLCgamma1 downstream of the T-cell receptor, the absence of LAT in platelets only impairs the activation of PLCgamma2, the response to collagen and GPVI receptor ligands remains sufficient to elicit a full aggregation response. In contrast, GPVI signalling is almost entirely abolished in the absence of SLP-76.
3-phosphoinositide dependent protein kinase-1 (PDK1, also known as PKB kinase because of its activity at Protein kinase B) phosphorylates T410 of Protein kinase C zeta type (PKC zeta), leading to activation. The motif surrounding T410 is highly conserved in other PKC family members suggesting that PDK1 might activate other PKCs.
3-phosphoinositide dependent protein kinase-1 (PDK1) and Protein kinase C zeta type (PKC zeta) are associated in fibroblasts. PDK1, also known as Protein kinase B kinase (PKBK), is known to co-localise with Protein kinase B (PKB) in transfected fibroblasts and platelets, suggesting a complex of PDK1, PKB and PKC zeta.
Phosphatidylinositides generated by PI3K recruit phosphatidylinositide-dependent protein kinase 1 (PDK1) and AKT (also known as protein kinase B) to the membrane, through their PH (pleckstrin-homology) domains. The binding of PIP3 to the PH domain of AKT is the rate-limiting step in AKT activation. In mammals there are three AKT isoforms (AKT1-3) encoded by three separate genes. The three isoforms share a high degree of amino acid identity and have indistinguishable substrate specificity in vitro. However, isoform-preferred substrates in vivo cannot be ruled out. The relative expression of the three isoforms differs in different mammalian tissues: AKT1 is the predominant isoform in the majority of tissues, AKT2 is the predominant isoform in insulin-responsive tissues, and AKT3 is the predominant isoform in brain and testes. All 3 isoforms are expressed in human and mouse platelets (Yin et al. 2008; O'Brien et al. 2008). Note: all data in the pathway refer to AKT1, which is the most studied.
In the initial response to injury, platelets adhere to damaged blood vessels, responding to the exposure of collagen from the vascular epithelium. Once adhered they degranulate, releasing stored secondary agents such as ADP and ATP, and synthesized thromboxane A2. These amplify the response, activating and recruiting further platelets to the area and promoting platelet aggregation. Adenosine nucleotides secreted following platelet activation signal through P2 purinergic receptors on the platelet membrane. ADP activates P2Y1 and P2Y12 while ATP activates the ionotropic P2X1 receptor (Kunapuli et al. 2003). Activation of these receptors initiates a complex signaling cascade that ultimately results in platelet activation and thrombus formation (Kahner et al. 2006). ADP stimulation of P2Y1 and P2Y12 involves signaling via both the alpha and gamma:beta components of the heterotrimeric G-protein (Hirsch et al. 2001, 2006).
Clinical and genetic spectrum of pyruvate dehydrogenase deficiency: dihydrolipoamide acetyltransferase (E2) deficiency
Molecular cloning of human mitochondrial glycerophosphate dehydrogenase gene: genomic structure, chromosomal localization, and existence of a pseudogene
The binding of the primer recognition complex involves the loading of proliferating cell nuclear antigen (PCNA). Replication Factor C transiently opens the PCNA toroid in an ATP-dependent reaction, and then allows PCNA to re-close around the double helix adjacent to the primer terminus. This leads to the formation of the "sliding clamp".
Replication factor C is proposed to dissociate from PCNA following sliding clamp formation, and the DNA toroid alone tethers pol delta to the DNA.
After the primers are synthesized on the G-Rich strand, Replication Factor C binds to the 3'-end of the initiator DNA to trigger polymerase switching. The non-processive nature of pol alpha catalytic activity and the tight binding of Replication Factor C to the primer-template junction presumably lead to the turnover of the pol alpha:primase complex. After the Pol alpha-primase primase complex is displaced from the primer, the proliferating cell nuclear antigen (PCNA) binds to form a "sliding clamp" structure. Replication Factor C then dissociates, and DNA polymerase delta binds and catalyzes the processive synthesis of DNA.
Due to the antiparallel nature of DNA, DNA polymerization is unidirectional, and one strand is synthesized discontinuously. This strand is called the lagging strand. Although the polymerase switching on the lagging strand is very similar to that on the leading strand, the processive synthesis on the two strands proceeds quite differently. Short DNA fragments, about 100 bases long, called Okazaki fragments are synthesized on the RNA-DNA primers first. Strand-displacement synthesis occurs, whereby the primer-containing 5'-terminus of the adjacent Okazaki fragment is folded into a single-stranded flap structure. This flap structure is removed by endonucleases, and the adjacent Okazaki fragments are joined by DNA ligase.
Cyclic GMP phosphodiesterase are hydrolases selective for cAMP (PDE4, 7 and 8), cGMP (PDE5, 6 and 9) or able to hydrolyse both cAMP and cGMP (PDE1, 2, 3, 10 and 11). Â The dual-specificity PDEs allow for cross-regulation of the cAMP and cGMP pathways, e.g. PDE2 can hydrolyse both, but binding of cGMP to the regulatory GAF-B domain increases cAMP affinity and hydrolysis. PDE2, 3 and 5 are expressed in platelets.
Four SLC gene families encode proteins that mediate the transport of bile salts and organic anions; SLC10, SLC13, SLC16 and SLC47 (He L et al, 2009).
Telomeres are protein-DNA complexes at the ends of linear chromosomes that are important for genome stability. Telomeric DNA in humans, as in many eukaryotic organisms, consists of tandem repeats (Blackburn and Gall 1978; Moyzis et al. 1988; Meyne et al. 1989). The repeats at human telomeres are composed of TTAGGG sequences and stretch for several kilobase pairs. Another feature of telomeric DNA in many eukaryotes is a G-rich 3' single strand overhang, which in humans is estimated to be approximately 50-300 bases long (Makarov et al. 1997; Wright et al. 1997; Huffman et al. 2000). Telomeric DNA isolated from humans and several other organisms can form a lasso-type structure called a t-loop in which the 3' single-strand end is presumed to invade the double stranded telomeric DNA repeat tract (Griffith et al. 1999). Telomeric DNA is bound by multiple protein factors that play important roles in regulating telomere length and in protecting the chromosome end from recombination, non-homologous end-joining, DNA damage signaling, and unregulated nucleolytic attack (reviewed in de Lange 2005). DNA attrition can occur at telomeres, which can impact cell viability. Attrition can occur owing to the "end-replication problem", a consequence of the mechanism of lagging-strand synthesis (Watson 1972; Olovnikov 1973). Besides incomplete replication, nucleolytic processing also likely contributes to telomere attrition (Huffman et al. 2000). If telomeres become critically shortened, replicative senescence can result (Harley et al. 1990). Thus, in order to undergo multiple divisions, cells need a mechanism to replenish the sequence at their chromosome ends. The primary means for maintaining the sequence at chromosome ends in many eukaryotic organisms, including humans, is based on telomerase (Greider and Blackburn, 1985; Morin 1989). Telomerase is a ribonucleoprotein complex minimally composed of a conserved protein subunit containing a reverse transcriptase domain (telomerase reverse transcriptase, TERT) (Lingner et al. 1997; Nakamura et al. 1997) and a template-containing RNA (telomerase RNA component, TERC, TR, TER) (Greider and Blackburn, 1987; Feng et al 1995). Telomerase uses the RNA template to direct addition of multiple tandem repeats to the 3' G-rich single strand overhang. Besides extension by telomerase, maintenance of telomeric DNA involves additional activities, including C-strand synthesis, which fills in the opposing strand, and nucleolytic processing, which likely contributes to the generation of the 3' overhang.
Telomerase acts as reverse transcriptase in the elongation of telomeres (Smogorzewska and de Lange 2004).
Chromosome maintenance is critical for stable chromosome function in mammalian and other eukaryotic cells. Aspects of telomere maintenance and nucleosome assembly are covered here.
Presentation of cytosolic antigens via MHC class II molecules
From late mitosis through G1 phase APC/C:Cdh1 insures the continued degradation of the mitotic proteins and during mitotic exit and G1 its substrates include Cdc20, Plk1, Aurora A, Cdc6 and Geminin (see Castro et al., 2005). Rape et al. have recently demonstrated that the order in which APC/C targeted proteins are degraded is determined by the processivity of multiubiquitination of these substrates. Processive substrates acquire a polyubiquitin chain upon binding to the APC/C once and are degraded. Distributive substrates bind, dissociate and reassociate with the APC/C multiple times before acquiring an ubiquitin chain of sufficient length to insure degradation. In addition, distributive substrates that dissociate from the APC/C with short ubiquitin chains are targeted for deubiquitination (Rape et al., 2006).
At the beginning of this reaction, 3 molecules of 'ubiquitin', and 1 molecule of 'cell cycle proteins:phospho-APC/C:Cdh1 complex' are present. At the end of this reaction, 1 molecule of 'multiubiquitinated cell cycle protein:APC/C:Cdh1 complex' is present. This reaction takes place in the 'cytosol' and is mediated by the 'ubiquitin-protein ligase activity' of 'cell cycle proteins:phospho-APC/C:Cdh1 complex'.
The APC/C is activated by either Cdc20 or Cdh1. While both activators associate with the APC/C, they do so at different points in the cell cycle and their binding is regulated differently (see Zachariae and Nasmyth, 1999). Cdc20, whose protein levels increase as cells enter into mitosis and decrease upon mitotic exit, only associates with the APC/C during M phase. Cdh1 associates with the APC/C in G1. This interaction is inhibited at other times by Cdk1 phosphorylation.
Common and distinct elements in cellular signaling via EGF and FGF receptors
Interferon-gamma: an overview of signals, mechanisms and functions
Depletion of intracellular calcium stores activates a calcium current in mast cells
The replication of the genome and the subsequent segregation of chromosomes into daughter cells are controlled by a series of events collectively known as the cell cycle. DNA replication is carried out during a discrete temporal period known as the S (synthesis)-phase, and chromosome segregation occurs during a massive reorganization to cellular architecture at mitosis. Two gap-phases separate these major cell cycle events: G1 between mitosis and S-phase, and G2 between S-phase and mitosis. In the development of the human body, cells can exit the cell cycle for a period and enter a quiescent state known as G0, or terminally differentiate into cells that will not divide again, but undergo morphological development to carry out the wide variety of specialized functions of individual tissues. A family of protein serine/threonine kinases known as the cyclin-dependent kinases (CDKs) controls progression through the cell cycle. As the name suggests, the activity of the catalytic subunit is dependent on binding to a cyclin partner. The human genome encodes several cyclins and several CDKs, with their names largely derived from the order in which they were identified. The oscillation of cyclin abundance is one important mechanism by which these enzymes phosphorylate key substrates to promote events at the relevant time and place. Additional regulatory proteins and post-translational modifications ensure that CDK activity is precisely regulated, frequently confined to a narrow window of activity.
The complementary strand is synthesized by the polymerase primase complex using conventional RNA priming.
The Anaphase Promoting Complex or Cyclosome (APC/C) functions during mitosis to promote sister chromatid separation and mitotic exit through the degradation of mitotic cyclins and securin. This complex is also active in interphase insuring the appropriate length of the G1 phase (reviewed in Peters, 2002). The APC/C contains at least 12 subunits and functions as an ubiquitin-protein ligase (E3) promoting the multiubiquitination of its target proteins (see Gieffers et al., 2001). In the ubiquitination reaction, ubiquitin is activated by the formation of a thioester bond with the (E1) ubiquitin activating enzyme then transferred to a cysteine residue within the ubiquitin conjugating enzyme (E2) and ultimately to a lysine residue within the target protein, with the aid of ubiquitin-protein ligase activity of the APC/C. The ubiquitin chains generated are believed to target proteins for destruction by the 26S proteasome (Reviewed in Peters, 1994 ) The activity of the APC/C is highly periodic during the cell cycle and is controlled by a combination of regulatory events. The APC/C is activated by phosphorylation and the regulated recruitment of activating subunits and is negatively regulated by sequestration by kinetochore-associated checkpoint proteins. The Emi1 protein associates with Cdh1 and Cdc20, inhibiting the APC/C between G1/S and prophase. RSSA1 may play a similar role in ihibiting the APC during early mitosis. Following phosphorylation of the APC/C core subunits by mitotic kinases, the activating subunit, Cdc20 is recruited to the APC/C and is responsible for mitotic activities, including the initiation of sister chromatid separation and the timing of exit from mitosis (See Zachariae and Nasmyth, 1999). Substrates of the Cdc20:APC/C complex, which are recognized by a motif known as the destruction box (D box) include Cyclin A, Nek2, Securin and Cyclin B. Degradation of Securin and Cyclin B does not occur until the mitotic spindle checkpoint has been satisfied (see Castro et al. 2005). Cdc20 is degraded late in mitosis (Reviewed in Owens and Hoyt, 2005). At this time the activating subunit, Cdh1, previously maintained in an inactive phosphorylated state by mitotic kinases, is dephosphorylated and associates with and activates the APC/C. The APC/C:Cdh1 complex recognizes substrates containing a D box, a KEN box (Pfleger and Kirschner, 2000) or a D box activated (DAD) domain (Castro et al., 2002) sequence and promotes the ordered degration of mitotic cyclins and other mitotic proteins culminating with its own ubiquitin-conjugating enzyme (E2) subunit UbcH10 (Rape et al., 2006). This ordered degradation promotes the stability of Cyclin A at the end of G1. This stabilization, in turn, promotes the phosphorylation of Cdh1 and its abrupt dissociation from the APC/C, allowing accumulation of cyclins for the next G1/S transition (Sorensen et al., 2001).
Once the RNA-DNA primer is synthesized, replication factor C (RFC) initiates a reaction called "polymerase switching"; pol delta, the processive enzyme replaces pol alpha, the priming enzyme. RFC binds to the 3'-end of the RNA-DNA primer on the Primosome, to displace the pol alpha primase complex. The binding of RFC triggers the binding of the primer recognition complex.
DNA polymerases are not capable of de novo DNA synthesis and require synthesis of a primer, usually by a DNA-dependent RNA polymerase (primase) to begin DNA synthesis. In eukaryotic cells, the primer is synthesized by DNA polymerase alpha:primase. First, the DNA primase portion of this complex synthesizes approximately 6-10 nucleotides of RNA primer and then the DNA polymerase portion synthesizes an additional 20 nucleotides of DNA. There have been reports that TRF1 inhibits this activity at telomeres, though the mechanism and physiological relevance of this inhibition remain to be elucidated.
RIAM, an Ena/VASP and Profilin ligand, interacts with Rap1-GTP and mediates Rap1-induced adhesion
At mitotic entry Plk1 phosphorylates and inhibits Myt1 activity. Cyclin B1-bound Cdc2, which is the target of Myt1, functions in a feedback loop and phosphorylates and further inhibits Myt1.
It has been shown that Xenopus polo homolog,Plx1, directly phosphorylates and activates Cdc25C, which in turn dephosphoryates and activates Cdc2. This step is critical for the onset of mitosis. Since Plx1-dependent Cdc25C phosphorylation occurs in the absence of Cdc2 activity, it is likely that Plx1 is a triggering kinase, which leads to the activation of Cdc2 and therefore the normal onset of mitosis.
Functionality of alternative splice forms of the first enzymes involved in human molybdenum cofactor biosynthesis
Ror-family receptor tyrosine kinases in noncanonical Wnt signaling: their implications in developmental morphogenesis and human diseases
Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V
At mitotic entry, Plk1 phosphorylates and activates Cdc25C phosphatase, whereas it phosphorylates and down-regulates Wee1A. Plk1 also phosphorylates and inhibits Myt1 activity. Cyclin B1-bound Cdc2, which is the target of Cdc25C, Wee1A, and Myt1, functions in a feedback loop and phosphorylates the latter components (Cdc25C, Wee1A, Myt1). The Cdc2- dependent phosphorylation provides docking sites for the polo-box domain of Plk1, thus promoting the Plk1-dependent regulation of these components and, as a result, activation of Cdc2-Cyclin B1.
Cyclin A can also form complexes with Cdc2 (Cdk1). Together with three B-type cyclins, Cdc2 (Cdk1) regulates the transition from G2 into mitosis. These complexes are activated by dephosphorylation of T14 and Y15. Cyclin A, B - Cdc2 complexes phosphorylate several proteins involved in mitotic spindle structure and function, the breakdown of the nuclear envelope, and topological changes in chromosomes allowing resolution of their entanglement and condensation that is necessary for the ~2 meters of DNA to be segregated at mitosis.
At the G1/S transition, the Cdh1 subunit of the APC:Cdh1 complex is phosphorylated by Cyclin A:Cdk2 and dissociates from APC/C. This inactivates APC/C and permits the accumulation of cell cycle proteins required for DNA synthesis and entry into mitosis.
Following its association with SCF-ÃÂ²TrCP, phospho-Emi1 is poly-ubiquitinated.
Multiubiquitinated Emi1 is degraded by the 26S proteasome.
Emi1 destruction in early mitosis requires the SCFÃÂ²TrCP ubiquitin ligase complex. Binding of ÃÂ²TrCP to Emi1 occurs in late prophase and requires phosphorylation at the DSGxxS consensus motif as well as Cdk mediated phosphorylation. A two-step mechanism has been proposed in which the phosphorylation of Emi1 by Cdc2 occurs after the G2-M transition followed soon after by binding of ÃÂ²TrCP to the DSGxxS phosphorylation sites. Emi1 is then poly-ubiquitinated and degraded by the 26S proteasome.
At the onset of mitosis, Cdh1 is phosphorylated by Cyclin B-Cdc2 resulting in a conformational change that prevents Cdh1 from activating the APC/C.
The rapid translocation of cyclin B1:Cdc2 from the cytoplasm to the nucleus at the onset of mitosis is a result of an increase in the rate of import and, likely, a decreased rate of export. The increased rate of nuclear import is dependent upon phosphorylation of the CRS which creates a nuclear import signal in the amino terminus of cyclin B1 (Hagting et al, 1999).
The structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations
Role of cysteine-82 in the catalytic mechanism of human S-adenosylmethionine decarboxylase
*Plk1 is shown to phosphorylate Wee1A, an event that is likely critical for recognition and ubiquitination of Wee1A by SCF and therefore for the subsequent degradation of Wee1A . **Plk1 phosphorylates Wee1A at S53, creating the second phosphodegron, PD53. ** Evidence also exists in budding yeast that the budding yeast polo homolog Cdc5 directly phosphorylates and down-regulate the budding yeast Wee1 ortholog Swe1. Thus, polo kinase-dependent phosphorylation and degradation of Wee1A (or Swe1) is likely conserved throughout evolution and is critical for normal mitotic entry.
PLK1 is induced in S phase and can be find in both cytosol and nucleus in S and G2 phases of the cell cycle. PLK1 possesses a bipartite nuclear localization signal (NLS) that enables it to enter the nucleus (Taniguchi et al. 2002).
The kinase activity of PLK1 is required for cell cycle progression as PLK1 phosphorylates and regulates a number of cellular proteins during mitosis. Centrosomic AURKA (Aurora A kinase), catalytically activated through AJUBA facilitated autophosphorylation on threonine residue T288 at G2/M transition (Hirota et al. 2003), activates PLK1 on centrosomes by phosphorylating threonine residue T210 of PLK1, critical for PLK1 activity (Jang et al. 2002), in the presence of BORA (Macurek et al. 2008, Seki et al. 2008). Once activated, PLK1 phosphorylates BORA and targets it for ubiquitination mediated degradation by SCF-beta-TrCP ubiquitin ligases. Degradation of BORA is thought to allow PLK1 to interact with other substrates (Seki, Coppinger, Du et al. 2008, Seki et al. 2008). The interaction of PLK1 with OPTN (optineurin) provides a negative-feedback mechanism for regulation of PLK1 activity. Phosphorylated PLK1 binds and phosphorylates OPTN associated with the Golgi membrane GTPase RAB8, promoting dissociation of OPTN from Golgi and translocation of OPTN to the nucleus. Phosphorylated OPTN facilitates the mitotic phosphorylation of the myosin phosphatase subunit PPP1R12A (MYPT1) and myosin phosphatase activation (Kachaner et al. 2012). The myosin phosphatase complex dephosphorylates threonine residue T210 of PLK1 and inactivates PLK1 (Yamashiro et al. 2008).
At the beginning of this reaction, 1 molecule of 'Cyclin B2:phospho-Cdc2(Thr 14, Thr 161)', and 1 molecule of 'H2O' are present. At the end of this reaction, 1 molecule of 'Cyclin B2:phospho-Cdc2(Thr 161)', and 1 molecule of 'Orthophosphate' are present. This reaction takes place in the 'cytosol' and is mediated by the 'phosphoprotein phosphatase activity' of 'Cdc25'.
The two B-type cyclins localize to different regions within the cell and and are thought to have specific roles as CDK1-activating subunits (see Bellanger et al., 2007). Cyclin B1 is primarily cytoplasmic during interphase and translocates into the nucleus at the onset of mitosis (Jackman et al., 1995; Hagting et al., 1999). Cyclin B2 colocalizes with the Golgi apparatus and contributes to its fragmentation during mitosis (Jackman et al., 1995; Draviam et al., 2001).
A description of the mitotic proteins targeted by the mitotic cyclin:CDK complexes will be covered in a later release.
Cell cycle progression is regulated by cyclin-dependent protein kinases at both the G1/S and the G2/M transitions by cyclin-dependent protein kinases. The G2/M transition is regulated through the phosphorylation of nuclear lamins and histones (reviewed in Sefton, 2001).
The localization of the Cdc25A, B and C proteins is dynamic involving the shuttling of these proteins between the nucleus and the cytoplasm. Sequences in these proteins mediate both nuclear export and import (Kallstrom et al., 2005; Lindqvist et al., 2004; Graves et al, 2001; Takizawa and Morgan, 2000).
Following its translocation to the nucleus, Cdc25 dephosphorylates and activates nuclear cyclin B1:Cdc2 complexes (Strausfeld et al., 1991).
Activation of the mitotic cyclin:Cdc2 complexes at mitosis requires the removal of the inhibitory phosphate groups on Cdc2. This dephosphorylation is achieved by the activity of the Cdc25 family of phosphatases. The Cdc25 members, Cdc25A, Cdc25B, and Cdc25C are kept inactive during interphase and are activated at the G2/M transition. Cyclin B1:Cdc2 itself appears to participate in the full activation of Cdc25 in a process that involves an amplication loop (see Wolfe and Gould, 2004). The initial activation of the cyclin B1-Cdc2 complex occurs in the cytoplasm in prophase (Jackman et al., 2003). Cdc25B, which is present at highest concentrations in the cytoplasm at this time, is thought to trigger the activation of cyclin B1-Cdc2 (Lindqvist et al. 2004; Honda et al., 1993). Active cyclin B:Cdc2 then phosphorylates and activates Cdc25C and stabilizes Cdc25A (Strausfeld et al., 1994; Hoffman et al.,1993; Mailand et al, 2002). This creates positive feedback loops that allows Cdc25A and Cdc25C to dephosphorylate and further activate Cdc2.
At the onset of mitosis, cyclin B is phosphorylated in the CRS sequence which creates a nuclear import signal in the amino terminus. The kinase(s) responsible for this phosphorylation are not yet known (Hagting et al., 1999).
Cyclin dependent kinases are themselves catalytically inactive due to the fact that their active site is blocked by a portion of the Cdk molecule itself. Binding to their corresponding cyclin partner results in conformational change that partially exposes the active site.
During interphase, cyclin B1:Cdc2 shuttles continuously in and out of the nucleus. Cyclin B1:Cdc2 is transported into the nucleus by an unusual mechanism that requires importin b but not importin a or Ran. Dissociation of the cyclin-B1:Cdc2:importin complex in the nucleus requires ATP and involves other yet unidentified nuclear factors (Takizawa et al.,1991).
During interphase, cyclin B1 shuttles continuously in and out of the nucleus. The cyclin B cytoplasmic retention sequence (CRS), which is responsible for its interphase cytoplasmic localization, functions as a nuclear export sequence (Yang et al., 1998).
Cdc25B shuttles between the nucleus and the cytoplasm. Translocation out of the nucleus involves a nuclear export sequence in the N-terminus of Cdc25B (Lindqvist et al., 2004).
Cyclin A:Cdc2 complexes translocate to the nucleus in G1 and may associate with condensing chromosomes in prophase (Pines and Hunter 1991).
The human Wee1 kinase phosphorylates Cdc2 on tyrosine 15 inactivating the cyclin:CDK complex (Watanabe et al., 1995).
During interphase, phopshorylated Cdc25C is associated with 14-3-3 proteins preventing nuclear import. At the onset of mitosis, dephosphorylation of Cdc25C and dissociation of 14-3-3 increases the rate of import (see Takizawa and Morgan, 2000)
Activation of the mitotic cyclin:Cdc2 complexes at mitosis requires the removal of the inhibitory phosphate groups on Cdc2. This dephosphorylation is achieved by the activity of the Cdc25 family of phosphatases. The Cdc25 members, Cdc25A, Cdc25B, and Cdc25C are kept inactive during interphase and are activated at the G2/M transition (see Wolfe and Gould 2004)
Amyloid Oligomer Structures and Toxicity
Mutations in the X-linked pyruvate dehydrogenase (E1) alpha subunit gene (PDHA1) in patients with a pyruvate dehydrogenase complex deficiency
Neural cell adhesion molecule L1: signaling pathways and growth cone motility
Mutations in TMEM76* cause mucopolysaccharidosis IIIC (Sanfilippo C syndrome)
ChEBI:16723 4-methylthio-2-oxobutanoate (1-)
ChEBI:16728 2-acyl-sn-glycero-3-phosphocholine
Topology of acyltransferase motifs and substrate specificity and accessibility in 1-acyl-sn-glycero-3-phosphate acyltransferase 1
(IscS-IscU)2 complex structures provide insights into Fe2S2 biogenesis and transfer
Mini-review: Specificity and expression of CIITA, the master regulator of MHC class II genes
Molecular cloning, sequencing and expression of cDNA encoding human trehalase
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Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin
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Functional characterization and localization of AQP3 in the human colon
The ins and outs of IgE-dependent mast-cell exocytosis
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The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex localization
Tau oligomers and aggregation in Alzheimer's disease
New initiation factor activity required for globin mRNA translation.
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Protein kinase G mediates vascular endothelial growth factor-induced Raf-1 activation and proliferation in human endothelial cells
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Getting in and out from calnexin/calreticulin cycles
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The polo-like kinase Plx1 is required for activation of the phosphatase Cdc25C and cyclin B-Cdc2 in Xenopus oocytes
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Mitotic phosphorylation of Golgi reassembly stacking protein 55 by mitogen-activated protein kinase ERK2
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A new biochemical subtype of the Sanfilippo syndrome: characterization of the storage material in cultured fibroblasts of Sanfilippo C patients
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Diacylglycerol kinases: at the hub of cell signalling
A novel quality control compartment derived from the endoplasmic reticulum
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Stimulation of the cell death response by PAK-2p34
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Polyamines: metabolism and implications in human diseases
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Frataxin and mitochondrial FeS cluster biogenesis
Activating E17K mutation in the gene encoding the protein kinase AKT1 in a subset of squamous cell carcinoma of the lung
Translocation of lipid-linked oligosaccharides across the ER membrane requires Rft1 protein
Down-regulation of ZIP4 by RNA interference inhibits pancreatic cancer growth and increases the survival of nude mice with pancreatic cancer xenografts
MHC II and the endocytic pathway: regulation by invariant chain
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Mutations in the transporter ABCA12 are associated with lamellar ichthyosis type 2
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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
Natural resistance-associated macrophage protein 2
The t(1;9)(p34;q34) and t(8;12)(p11;q15) fuse pre-mRNA processing proteins SFPQ (PSF) and CPSF6 to ABL and FGFR1
Peptides corresponding to the N and C termini of IkappaB-alpha, -beta, and -epsilon as probes of the two catalytic subunits of IkappaB kinase, IKK-1 and IKK-2
Dissecting the role of 5'-AMP for allosteric stimulation, activation, and deactivation of AMP-activated protein kinase
RNA editing: complexity and complications.
Three-dimensional structure of the anaphase-promoting complex
Solute carrier family 2, facilitated glucose transporter member 9
Solute carrier family 2, facilitated glucose transporter member 7
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
Natural resistance-associated macrophage protein 1
Solute carrier family 2, facilitated glucose transporter member 8
Solute carrier family 2, facilitated glucose transporter member 6
TIR domains, which are conserved among all TLRs. Recent accumulating
A regulatory role for 1-acylglycerol-3-phosphate-O-acyltransferase 2 in adipocyte differentiation
Protein ligands to HuR modulate its interaction with target mRNAs in vivo
Solute carrier family 2, facilitated glucose transporter, member 3
RNA editing: cytidine to uridine conversion in apolipoprotein B mRNA.
Molecular characterization of the family of choline transporter-like proteins and their splice variants
Opposing roles for ATF6alpha and ATF6beta in endoplasmic reticulum stress response gene induction
A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNA(Met) is an important translation initiation intermediate in vivo.
Dealing with methionine/homocysteine sulfur: cysteine metabolism to taurine and inorganic sulfur
Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A)
Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription.
Dephosphorylation of human p34cdc2 kinase on both Thr-14 and Tyr-15 by human cdc25B phosphatase
Lysosomal degradation of glycoproteins is part of the cellular homeostasis of glycosylation (Winchester 2005). The steps outlined below describe the degradation of chondroitin sulfate and dermatan sulfate. Complete degradation of glycoproteins is required to avoid build up of glycosaminoglycan fragments which can cause lysosomal storage diseases. Complete degradation steps are not shown as they are repetitions of the main ones described here. The proteolysis of the core protein of the glycoprotein is not shown here.
Chondroitin sulfate (CS) is a sulfated glycosaminoglycan (GAG). CS chains are unbranched polysaccharides of varying length containing two alternating monosaccharides: D-glucuronic acid (GlcA) and N-acetyl-D-galactosamine (GalNAc). The chains are usually attached to proteins forming a proteoglycan. CS is an important structural component of cartilage due to it's ability to withstand compression. It is also a widely used dietary supplement for osteoarthritis. When some of the GlcA residues are epimerized into L-iduronic acid (IdoA) the resulting disaccharide is then referred to as dermatan sulfate (DS) (Silbert & Sugumaran 2002). DS is the most predominant GAG in skin but is also found in blood vessels, heart valves, tendons, and the lungs. It may play roles in cardiovascular disease, tumorigenesis, infection, wound repair and fibrosis (Trowbridge & Gallo 2002).
The acronym HS-GAG is used to describe both heparin and heparan sulfate. HS-GAG is a member of the glycosaminoglycan family and consists of a variably sulfated repeating disaccharide unit, the most common one (50% of the total) being glucuronic acid (GlcA) linked to N-acetylglucosamine (GlcNAc). GlcA can be epimerized to iduronic acid. Higher degrees of sulfation and iduronic acid content in the polysaccharide chain confers the name heparin rather than heparan sulfate to the chain. HS-GAG, like the majority of GAGs in the body, are linked to core proteins, forming proteoglycans (mucopolysaccharides). Two or three HS-GAG chains attach to a core protein on the cell surface or in the extracellular matrix (Sasisekharan & Venkataraman 2000). HS-GAG bound to a core protein can regulate many biological processes such as angiogenesis, blood coagulation and tumour metastasis (Stringer & Gallagher 1997, Tumova et al. 2000). Degradation of HS-GAG is required to maintain a natural turnover of GAGs. Defects in the degradative enzymes result in lysosomal storage diseases, where GAGs build up rather than being broken down and having pathological effects (Ballabio & Gieselmann 2009).
Beta-hexosaminidase A (bHEXA) cleaves the terminal N-acetyl galactosamine (GalNAc) from glucosaminoglycans (GAGs) and any other molecules containing a terminal GalNAc. There are two 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). Defects in the two subunits cause lysosomal storage diseases marked by the accumulation of GM2 gangliosides in neuronal cells. Defects in the alpha subunits are the cause of GM2-gangliosidosis type 1 (GM2G1) (MIM:272800), also known as Tay-Sachs disease (Nakano et al. 1988). Defects in the beta subunits are the cause of GM2-gangliosidosis type 2 (GM2G2) (MIM:268800), also known as Sandhoff disease (Banerjee et al. 1991).
Beta-galactosidase (GLB1) can cleave terminal galactose residues from the linker chain sequence of glycosaminoglycans (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).
Lysosomal degradation of glycoproteins is part of the cellular homeostasis of glycosylation (Winchester 2005). The steps outlined below describe the degradation of heparan sulfate/heparin. Complete degradation of glycoproteins is required to avoid build up of glycosaminoglycan fragments which can cause lysosomal storage diseases. The proteolysis of the core protein of the glycoprotein is not shown here.
A group of phospholipase C proteins (PLC(degh)) bind to the plasma membrane via their PH domains. These phospholipases hydrolyse phosphatidylinositol 4,5 bisphosphate (PI(4,5)P2) to inositol 1,4,5 trisphosphate (I(1,4,5)P3) and diacylglycerol (DAG). The C2 domains of the enzymes bind to PI(4,5)P2 at the membrane. The phospholipase C isoforms involved and their corresponding literature references are: phosphoinositide phospholipase C delta-1(PLCD1) (Cheng et al. 1995); epsilon-1 (PLCE1) (Song et al. 2001, Lopez et al. 2001); delta-3 (PLCD3) (Pawelczyk & Matecki 1997); gamma-1 (PLCG1) (Harita et al. 2009, Baldassare et al. 1989); gamma-2 (PLCG2) (Banno et al. 1988); eta-1 (PLCH1) (Hwang et al. 2005); and eta-2 (PLCH2) (Zhou et al 2005).
At the plasma membrane, a group of phospholipase C (PLC(bz)) proteins hydrolyse phosphatidylinositol 4,5 bisphosphate (PI(4,5)P2) to inositol 1,4,5 trisphosphate (I(1,4,5)P3) and diacylglycerol (DAG). This group of phospholipase C proteins lack a PH domain and so are is cytosolic. Their C2 domains bind to PI(4,5)P2 at the membrane. The PLC-beta proteins are thought to be responsible for the majority of PI(4,5)P2 hydrolysis. The phospholipase C isoforms involved and their corresponding literature references are: phosphoinositide phospholipase C beta-1 (PLCB1) (Caricasole et al. 2000, Jhon et al. 1993, Park et al. 1992); beta-2 (PLCB2) (Jhon et al. 1993, Park et al. 1992); beta-3 (PLCB3) (Carozzi et al. 1992, Jhon et al. 1993); beta-4 (PLCB4) (Alvarez et al. 1995, Lee et al. 1993); and zeta-1 (PLCZ1) (Kouchi et al. 2005, Rogers et al. 2004).
These pathways together are responsible for: 1) the extraction of energy and carbon skeletons for biosyntheses from dietary sugars and related molecules; 2) the short-term storage of glucose in the body (as glycogen) and its mobilization during a short fast; and 3) the synthesis of glucose from pyruvate during extended fasts.
Glycosaminoglycans (GAGs) are long, unbranched polysaccharides containing a repeating disaccharide unit composed of a hexosamine (either N-acetylgalactosamine (GalNAc) or N-acetylglucosamine (GlcNAc)) and a uronic acid (glucuronate or iduronate). They can be heavily sulfated. GAGs are located primarily in the extracellular matrix (ECM) and on cell membranes, acting as a lubricating fluid for joints and as part of signalling processes. They have structural roles in connective tissue, cartilage, bone and blood vessels (Esko et al. 2009). GAGs are degraded in the lysosome as part of their natural turnover. Defects in the lysosomal enzymes responsible for the metabolism of membrane-associated GAGs lead to lysosomal storage diseases called mucopolysaccharidoses (MPS). MPSs are characterised by the accumulation of GAGs in lysosomes resulting in chronic, progressively debilitating disorders that in many instances lead to severe psychomotor retardation and premature death (Cantz & Gehler 1976, Clarke 2008). The biosynthesis and breakdown of the main GAGs (hyaluronate, keratan sulfate, chondroitin sulfate, dermatan sulfate and heparan sulfate) is described here.
Beta-galactosidase (GLB1) can cleave terminal galactose residues from glycosaminoglycans such as keratan sulfate (KS) (Asp et al. 1969). Defects in GLB1 cause the lysosomal storage diseases GM1gangliosidosis (Yoshida et al. 1991) and Morquio syndrome type B (Oshima et al. 1991).
Keratan sulfate proteoglycans (KSPGs) are degraded in lysosomes as part of normal homeostasis of glycoproteins. Glycoproteins must be completely degraded to avoid undigested fragments building up and causing a variety of lysosomal storage diseases. KSPGs are Asn-linked glycoproteins and are acted upon by exo-glycosidases to release sugar monomers. The main steps of degradation are shown representing the types of cleavage reactions that occur so the full degradation of KS is not shown to avoid repetition. The proteolysis of the core protein of the glycoprotein is not shown here (Winchester 2005, Aronson & Kuranda 1989).
Keratan sulfate (KS) (a glycosaminoglycan, GAG) is a linear polysaccharide that consists of the repeating disaccharide unit GlcNAc-Gal (N-acetylglucosamine-galactose). KS can perform a structural function and is found in bone, cartilage and the cornea. In joints, it also acts as a shock absorber due to its highly hydrated nature. There are several classes of KS, KSI, II and III. KSI is N-linked to asparagine (Asn) residues in the core protein and is predominantly found in the cornea. KSII is O-linked to serine (Ser) or Thr (threonine) residues in the core protein and is found predominantly in cartilage linked to the protein aggrecan, forming the most abundant proteoglycan in cartilage. A third class of KS, KSIII, are proteoglycans in the brain. KSIII chains are linked to Ser/Thr residues in the core protein via mannose (Funderburgh 2000, Funderburgh 2002). Normally, the body degrades GAGs as a natural turnover. Defects in the degradative enzymes cause the autosomal recessive mucopolysaccharide storage disease Morquio's syndrome (also called mucopolysaccharidosis IV). This involves the build up of KS in lysosomes, manifesting clinically as skeletal, dental and corneal abnormalities (Tomatsu et al. 2005).
Keratan sulfate (KSI) is the best characterised keratan sulfate. It is 10 times more abundant in cornea than cartilage. KSI is attached to an asparagine (Asn) residue on the core protein via an N-linked branched oligosaccharide (an N-glycan core structure used as a precursor in N-glycan biosynthesis). KSI is elongated by the alternate additions of galactose (Gal) and N-acetylglucosamine (GlcNAc), mediated by glycosyltransferases. Elongation is terminated by the addition of a single N-acetylneuraminic acid (sialyl) residue. KSI is also sulfated on Gal and GlcNAc residues by at least two sulfotransferases (Funderburgh 2000, Funderburgh 2002, Quantock et al. 2010). KSI can be attached to asparagine residues on core proteins, creating so called proteoglycans (PGs). Seven common core proteins found in corneal and skeletal tissues are used as examples here.
Alpha-N-acetylglucosaminidase (NAGLU) also hydrolyses another non-reducing, terminal N-acetyl-D-glucosamine residue from heparan sulfate. The active form of the enzyme (77kDa) is derived from an 82kDa precursor (Weber et al. 1996). Defects in NAGLU cause Mucopolysaccharidosis type IIIB (MPSIIIB, MIM:252920), also known as Sanfilippo syndrome type B (Beesley et al. 2005).
Identification and characterization of human mitochondrial tryptophanyl-tRNA synthetase
Heparan-alpha-glucosaminide N-acetyltransferase (HGSNAT) acetylates the non-reducing terminal alpha-glucosamine residue of heparan sulfate. This is a critical reaction for the degradation of heparan sulfate because there is no enzyme that can act on the unacetylated glucosamine molecule. The mechanism by which HGSNAT uses cytosolic acetyl-CoA to transfer the acetyl group to the lysosomal luminal substrate is unknown (Fan et al. 2006). A catalytically inactive 77kDa precursor is transported to the lysosome and is cleaved into a 29kDa N-terminal alpha-chain and a 48kDa C-terminal beta-chain, which are assembled into active 440kDa oligomers in the lysosomal membrane (Durand et al. 2010). Defects in HGSNAT cause mucopolysaccharidosis type IIIC (MPSIIIC, MIM:252930), also called Sanfilippo C syndrome (Fan et al. 2006, Hrebicek et al. 2006).
Heparan sulfate (HS) and heparin (sometimes collectively called HS-GAG) consist of the disaccharide unit GlcNAc-GlcA (N-acetylglucosamine-glucuronic acid) connected by a beta1,4 linkage. Heparin is exclusively made in mast cells whereas HS is made by virtually every type of cell in the body. As the chain length increases, the polysaccharides can undergo modifcations such as epimerisation of glucuronic acid to iduronic acid and deacetylation and sulfation of GlcNAc to form sulfated glucosamine (Stringer & Gallagher 1997, Sasisekharan & Venkataraman 2000).
Heparan-alpha-glucosaminide N-acetyltransferase (HGSNAT) acetylates another non-reducing terminal alpha-glucosamine residue of heparan sulfate. This is a critical reaction for the degradation of heparan sulfate because there is no enzyme that can act on the unacetylated glucosamine molecule. The mechanism by which HGSNAT uses cytosolic acetyl-CoA to transfer the acetyl group to the lysosomal luminal substrate is unknown (Fan et al. 2006). A catalytically inactive 77kDa precursor is transported to the lysosome and is cleaved into a 29kDa N-terminal alpha-chain and a 48kDa C-terminal beta-chain, which are assembled into active 440kDa oligomers in the lysosomal membrane (Durand et al. 2010). Defects in HGSNAT cause mucopolysaccharidosis type IIIC (MPSIIIC, MIM:252930), also called Sanfilippo C syndrome (Fan et al. 2006, Hrebicek et al. 2006).
Alpha-N-acetylglucosaminidase (NAGLU) hydrolyses the non-reducing, terminal N-acetyl-D-glucosamine residue from heparan sulfate. The active form of the enzyme (77kDa) is derived from a 82kDa precursor (Weber et al. 1996). Defects in NAGLU cause of mucopolysaccharidosis type IIIB (MPSIIIB, MIM:252920) also known as Sanfilippo syndrome type B (Beesley et al. 2005).
In the nucleus, inositol polyphosphate multikinase (IPMK) phosphorylates inositol 1,4,5,6-tetrakisphosphate (I(1,4,5,6)P4) to inositol 1,3,4,5,6-pentakisphosphate (I(1,3,4,5,6)P5) (Nalaskowski et al. 2002, Chang & Majerus 2006).
In the nucleus, inositol-pentakisphosphate 2-kinase (IPPK - also known as IP5-2K) 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) (Verbsky et al. 2002, Brehm et al. 2007, Choi et al. 2007).
In the nucleus, inositol polyphosphate multikinase (IPMK) phosphorylates inositol 1,3,4,5-tetrakisphosphate (I(1,3,4,5)P4) to inositol 1,3,4,5,6-pentakisphosphate (I(1,3,4,5,6)P5) (Nalaskowski et al. 2002, Chang & Majerus 2006).
In the nucleus, inositol polyphosphate multikinase (IPMK) phosphorylates inositol 1,3,4,6-tetrakisphosphate (I(1,3,4,6)P4) to inositol 1,3,4,5,6-pentakisphosphate (I(1,3,4,5,6)P5) (Chang et al. 2002, Chang & Majerus 2006).
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) 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 1,3,4,5,6-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).
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).
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).
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).
At the endoplasmic reticulum (ER) membrane, phosphoinositide phospholipase C delta-4 (PLCD4) hydrolyses phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) to inositol 1,4,5-trisphosphate (I(1,4,5)P3) and diacylglycerol (DAG). PLCD4 (Leung et al. 2004, Lee et al. 2004) is attached to the ER membrane via its PH domain while its C2 domain binds to the PI(4,5)P2 in the membrane.
A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic
Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase aka phosphatase and tensin homolog (PTEN) dephosphorylates inositol 1,3,4,5-tetrakisphosphate (I(1,3,4,5)P4) to inositol 1,4,5-trisphosphate (I(1,4,5)P3) (Maehama & Dixon 1998, Han et al. 2000).
A group of inositol phosphatases and the broad specificity enzyme inositol-tetrakisphosphate 1-kinase (ITPK1) dephosphorylate inositol 1,3,4,5-tetrakisphosphate (I(1,3,4,5)P4) to inositol 1,3,4-trisphosphate (I(1,3,4)P3). The group of inositol phosphatases involved are: inositol polyphosphate 5-phosphatase OCRL-1 (OCRL), phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) aka SHIP1, phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2 (INPPL1) aka SHIP2, phosphatidylinositol 4,5-bisphosphate 5-phosphatase A (INPP5J) aka PIPP, and synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1 (SYNJ1). The following lists the above proteins with their corresponding literature references: OCRL (Chang et al. 2002, Zhang et al. 1995, Zhang et al. 1998, Schmid et al. 2004); INPP5D (Drayer et al. 1996, Kavanaugh et al. 1996); INPPL1 (Chi et al. 2004); INPP5J (Mochizuki & Thompson 1999); SYNJ1 (Schmid et al. 2004); ITPK1 (Ho et al. 2002).
The broad-specificity enzyme inositol-tetrakisphosphate 1-kinase (ITPK1) phosphorylates inositol 1,3,4-trisphosphate (I(1,3,4)P3) to inositol 1,3,4,5-tetrakisphosphate (I(1,3,4,5)P4) (Wilson & Majerus 1996).
Inositol-tetrakisphosphate 1-kinase (ITPK1) phosphorylates inositol 1,3,4-trisphosphate (I(1,3,4)P3) to inositol 1,3,4,6-tetrakisphosphate (I(1,3,4,6)P4) (Wilson & Majerus 1996, Yang & Shears 2000).
Inositol-tetrakisphosphate 1-kinase (ITPK1) dephosphorylates inositol 1,3,4,6-tetrakisphosphate (I(1,3,4,6)P4) to inositol 1,3,4-trisphosphate (I(1,3,4)P3) (Ho et al. 2002).
Inositol-tetrakisphosphate 1-kinase (ITPK1) dephosphorylates inositol 1,3,4,6-tetrakisphosphate (I(1,3,4,6)P4) to inositol 3,4,6-trisphosphate (I(3,4,6)P3) (Ho et al. 2002).
Recent progress in structure-function analyses of Nramp proton-dependent metal-ion transporters
Structure of a multifunctional protein. Mammalian phosphatidylinositol transfer protein complexed with phosphatidylcholine
The Wnt/Ca2+ pathway: a new vertebrate Wnt signaling pathway takes shape
An array of inositol trisphosphate (IP3) and tetrakisphosphate (IP4) molecules are synthesised by the action of various kinases and phosphatases in the cytosol (Irvine & Schell 2001, Bunney & Katan 2010).
Inositol-tetrakisphosphate 1-kinase (ITPK1) phosphorylates inositol 3,4,6-trisphosphate (I(3,4,6)P3) to inositol 1,3,4,6-tetrakisphosphate (I(1,3,4,6)P4) (Ho et al. 2002).
In the nucleus, inositol polyphosphate multikinase (IPMK) phosphorylates inositol 1,4,5-trisphosphate (I(1,4,5)P3) to inositol 1,3,4,5-tetrakisphosphate (I(1,3,4,5)P4) (Nalaskowski et al. 2002, Chang et al. 2002, Chang & Majerus 2006).
Cytosolic, non-phosphorylated PGYB dimers (b form) can reversibly bind AMP. This reaction is inferred from the AMP-binding properties of human PGYL and closely homologous PGYM proteins from other species (Newgard et al. 1989; Rath et al. 2000).
Glycogen, a highly branched glucose polymer, is formed and broken down in most human tissues, but is most abundant in liver and muscle, where it serves as a major stored fuel. Glycogen metabolism has been studied in most detail in muscle, although considerable experimental data are available concerning these reactions in liver as well. Glycogen metabolism in other tissues has not been studied as extensively, and is thought to resemble the muscle process (Hers 1976; Lomako et al. 2004; Villar-Palasi and Larner 1970). Glycogen synthesis involves five reactions. The first two, conversion of glucose 6-phosphate to glucose 1-phosphate and synthesis of UDP-glucose from glucose 1-phosphate and UTP, are shared with several other pathways. The next three reactions, the auto-catalyzed synthesis of a glucose oligomer on glycogenin, the linear extension of the glucose oligomer catalyzed by glycogen synthase, and the formation of branches catalyzed by glycogen branching enzyme, are unique to glycogen synthesis. These reactions are shown in the figure. Repetition of the last two reactions generates large, extensively branched glycogen polymers. The catalysis of several of these reactions by distinct isozymes in liver and muscle allows them to be regulated independently in the two tissues.
Cytosolic aldolase B (ALDOB) catalyzes the reaction of D-fructose 1-phosphate to form dihydroxyacetone phosphate and D-glyceraldehyde (Sakakibara et al. 1989). The active form of the enzyme is a tetramer (Dalby et al. 2001). Deficiencies in the enzyme are associated with hereditary fructose intolerance in vivo (e.g., Tolan 1995).
Fructose occurs naturally in foods as a free monosaccharide and as a component of the disaccharide sucrose. It is also widely used as a sweetener. In the body, fructose is converted to dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate, two intermediates in the glycolytic pathway, in a sequence of three reactions: fructose is phosphorylated, then cleaved by aldolase to yield dihydroxyacetone phosphate and D-glyceraldehyde, and the latter compound is phosphorylated to yield D-glyceraldehyde 3-phosphate. Other pathways exist for the conversion of D-glyceraldehyde to intermediates of glycolysis, but these appear to play only a minor role in normal fructose metabolism. The cleavage of fructose 1-phosphate is catalyzed by the same enzyme that catalyzes the reversible cleavage of fructose 1,6-bisphosphate in glycolysis. The isoform of this enzyme found in liver, kidney, and intestine (B) is approximately equally active with fructose 1-phosphate and fructose 1,6-bisphosphate as substrates, while the muscle and brain isoforms (A and C, respectively), have little activity with fructose 1-phosphate. Fructose metabolism thus occurs mainly in tissues expressing the B isoform, and mutations that affect the catalytic activity of this isoform are associated with hereditary fructose intolerance (Steinmann et al. 2001).
PI and PC transport between ER and Golgi membranes
Glycogen breakdown occurs via the same chemical steps in all tissues but is separately regulated via tissue specific isozymes and signaling pathways that enable distinct physiological fates for liver glycogen and that in other tissues. Glycogen phosphorylase, which can be activated by phosphorylase kinase, catalyzes the removal of glucose residues as glucose 1-phosphate from the ends of glycogen branches. The final four residues of each branch are removed in two steps catalyzed by debranching enzyme, and further glycogen phosphorylase activity completes the process of glycogen breakdown. The figure shows the actions of phosphorylase and debranching enzyme. The first glucose residue in each branch is released as free glucose; all other residues are released as glucose 1-phosphate. The latter molecule can be converted to glucose 6-phosphate in a step shared with other pathways (Villar-Palasi and Larner 1970; Hers 1976).
Glucose is the major form in which dietary sugars are made available to cells of the human body. Its breakdown is a major source of energy for all cells, and is essential for the brain and red blood cells. Glucose utilization begins with its uptake by cells and conversion to glucose 6-phosphate, which cannot traverse the cell membrane. Fates open to cytosolic glucose 6-phosphate include glycolysis to yield pyruvate, glycogen synthesis, and the pentose phosphate pathway. In some tissues, notably the liver and kidney, glucose 6-phosphate can be synthesized from pyruvate by the pathway of gluconeogenesis.
Induction of CHOP expression by amino acid limitation requires both ATF4 expression and ATF2 phosphorylation
Cytosolic, non-phosphorylated PGYM dimers (b form) complexed with AMP can reversibly dissociate (Rath et al. 2000).
UDP-N-acetylglucosamine/UDP-glucose/GDP-mannose transporter
UDP-galactose transporter-related protein 8
Cytosolic phosphoglucomutase (PGM) catalyzes the reversible conversion of glucose 1-phosphate to glucose 6-phosphate. Two PGM isoenzymes, both monomers, have been identified. PGM1 is the major form found in most tissues except erythrocytes, where PGM2 is abundant (March et al. 1993; Parrington et al. 1968; Putt et al. 1993). PGM2 also has substantial phosphopentomutase activity and its primary physiological in normal tissues in vivo is not clear.
Cytosolic, non-phosphorylated PGYB dimers (b form) complexed with AMP can reversibly dissociate. This reaction is inferred from the AMP-binding properties of the closely homologous PGYM complex (Rath et al. 2000).
Cytosolic, non-phosphorylated PGYM dimers (b form) can reversibly bind AMP. This reaction is negatively regulated by ATP and glucose 6-phosphate and is the means by which high levels of these molecules repress PGYM activity (Rath et al. 2000).
Peroxisome proliferator-activated receptor alpha (PPARalpha) and athero-sclerosis
Curr Drug Targets Cardiovasc Haematol Disord 5:513-23
A mitogen-activated protein kinase-dependent signaling pathway in the activation of platelet integrin alpha IIbbeta3
UDP-xylose and UDP-N-acetylglucosamine transporter
Cytosolic phosphoglycerate mutase dimer catalyzes the reversible isomerisation of 2- and 3-phosphoglycerate. There are two isoforms of this enzyme, PGAM1 (isoform B) and PGAM2 (isoform M). In the body, erythrocytes express only PGAM1, while skeletal muscle expresses only PGAM2. Other tissues express both isoforms (Repiso et al. 2005; Tsujino et al. 1993).
Cytosolic fructose-1,6-bisphosphatase catalyzes the physiologically irreversible hydrolysis of fructose-1,6-bisphosphate to form fructose-6-phosphate and orthophosphate. In the body, two isoforms of the enzyme are expressed, one ubiquitous and one muscle-specific (Kikawa et al. 1997; Tillmann and Eschrich 1998).
The reversible isomerization of fructose-6-phosphate to form glucose-6-phosphate is catalyzed by cytosolic phosphoglucose isomerase (Noltman 1972; Xu and Beutler 1994; Tsuboi et al. 1958).
The reactions of gluconeogenesis convert mitochondrial pyruvate to cytosolic glucose 6-phosphate which in turn can be hydrolyzed to glucose and exported from the cell. Gluconeogenesis is confined to cells of the liver and kidney and enables glucose synthesis from molecules such as lactate and alanine and other amino acids when exogenous glucose is not available (reviewed, e.g., by Gerich 1993). The process of gluconeogenesis as diagrammed below occurs in two parts: a network of reactions converts mitochondrial pyruvate to cytosolic phosphoenolpyruvate; then phosphoenolpyruvate is converted to glucose 6-phosphate in a single sequence of cytosolic reactions. Three variants of the first part of the process are physiologically important. 1) A series of transport and transamination reactions convert mitochondrial oxaloacetate to cytosolic oxaloacetate which is converted to phosphoenolpyruvate by a hormonally regulated, cytosolic isoform of phosphoenolpyruvate carboxykinase. This variant allows regulated glucose synthesis from lactate. 2) Mitochondrial oxaloacetate is reduced to malate, which is exported to the cytosol and re-oxidized to oxaloacetate. This variant provides reducing equivalents to the cytosol, needed for glucose synthesis from amino acids such as alanine and glutamine. 3) Constitutively expressed mitochondrial phosphoenolpyruvate carboxykinase catalyzes the conversion of mitochondrial oxaloacetate to phosphoenolpyruvate which is then transported to the cytosol. The exact path followed by any one molecule of pyruvate through this reaction network is determined by the tissue in which the reactions are occurring, the source of the pyruvate, and the physiological stress that triggered gluconeogenesis. In all cases, the synthesis of glucose from two molecules of pyruvate requires the generation and consumption of two reducing equivalents as cytosolic NADH + H+. For pyruvate derived from lactate (variants 1 and 3), NADH + H+ is generated with the oxidation of lactate to pyruvate in the cytosol (a reaction of pyruvate metabolism not shown in the diagram). For pyruvate derived from amino acids (variant 2), mitochondrial NADH + H+ generated by glutamate dehydrogenase (a reaction of amino acid metabolism, not shown) is used to reduce oxaloacetate to malate, which is transported to the cytosol and re-oxidized, generating cytosolic NADH + H+. The synthesis of glucose from pyruvate also requires the consumption of six high-energy phosphates, four from ATP and two from GTP. In the second part of gluconeogenesis, cytosolic phosphoenolpyruvate, however derived, is converted to fructose 1,6-bisphosphate by reactions that are the reverse of steps of glycolysis. Hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate is catalyzed by fructose 1,6-bisphosphatase, and fructose 6-phosphate is reversibly isomerized to glucose 6-phosphate.
Cytosolic phosphoglucomutase (PGM) catalyzes the reversible conversion of glucose 6-phosphate to glucose 1-phosphate (Drago et al. 1991). Two PGM isoenzymes, both monomers, have been identified. PGM1 is the major form found in most tissues except erythrocytes, where PGM2 is abundant (March et al. 1993; Parrington et al. 1968; Putt et al. 1993). PGM2 also has substantial phosphopentomutase activity and its primary physiological in normal tissues in vivo is not clear.
Equilibrative NBMPR-sensitive nucleoside transporter
Equilibrative nitrobenzylmercaptopurine riboside-sensitive nucleoside transporter
solute carrier family 29 (nucleoside transporters), member 1
Equilibrative nucleoside transporter 1 (Equilibrative nitrobenzylmercaptopurine riboside-sensitive nucleoside transporter) (Equilibrative NBMPR-sensitive nucleoside transporter) (Nucleoside transporter, es-type)
Cytosolic phosphoglycerate kinase complexed with magnesium catalyzes the reversible phosphorylation of 3-phosphoglycerate to form 1,3-bisphosphoglycerate (Huang et al. 1980a, 1980b).
Equilibrative nucleoside transporter 2 (Equilibrative nitrobenzylmercaptopurine riboside-insensitive nucleoside transporter) (Equilibrative NBMPR-insensitive nucleoside transporter) (Nucleoside transporter, ei-type) (36 kDa nucleolar protein HNP36) (Hydrophobic nucleolar protein, 36 kDa) (Delayed-early response protein 12)
solute carrier family 29 (nucleoside transporters), member 2
Equilibrative nitrobenzylmercaptopurine riboside-insensitive nucleoside transporter
Equilibrative NBMPR-insensitive nucleoside transporter
The reversible reduction of 1,3-bisphosphoglycerate to form glyceraldehyde-3-phosphate is catalyzed by cytosolic glyceraldehyde-3-phosphate dehydrogenase tetramer. There are multiple human glyceraldehyde 3-phosphate dehydrogenase-like pseudogenes, but only one glyceraldehyde 3-phosphate dehydrogenase gene expressed in somatic tissue (Benham and Povey 1989). Consistent with this conclusion, the homogeneous enzymes purified from various human tissues had indistinguishable physical and immunochemical properties (Heinz and Freimuller 1982), and studies of human erythrocytes of various ages suggested that variant forms of the enzyme arise as a result of post-translational modifications (Edwards et al. 1976). There is, however, an authentic second isoform of glyceraldehyde 3-phosphate dehydrogenase whose expression is confined to spermatogenic cells of the testis (Welch et al. 2000).
The reversible conversion of glyceraldehyde-3-phosphate to dihydroxyacetone phosphate is catalyzed by cytosolic triose phosphate isomerase (Watanabe et al. 1996; Lu et al. 1984).
In this freely reversible cytosolic reaction, dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate react to form D-fructose 1,6-bisphosphate. The active form of aldolase, the enzyme that catalyzes the reaction, is a homotetramer. Three aldolase isozymes have been identified which differ in their patterns of expression in various adult tissues and during development but are otherwise functionally indistinguishable (Ali and Cox 1995; Dunbar and Fothergill-Gilmore 1988).
Cytosolic UDP-glucose pyrophosphorylase 2 (UGP2) catalyzes the reaction of UTP and glucose 1-phosphate to form UDP glucose and pyrophosphate (Knop and Hansen 1970; Duggleby et al. 1996). UGP2 is inferred to occur in the cell as a homooctamer from studies of its bovine homologue (Levine et al. 1969).
Identification of a binding region for human origin recognition complex proteins 1 and 2 that coincides with an origin of DNA replication.
Cytosolic phophoribosyl pyrophosphate synthetase catalyzes the reaction of D-ribose 5-phosphate and ATP to form 5-phospho-alpha-D-ribose and AMP. Three isoforms of the enzyme have been described. The first has been purified and characterized biochemically (Fox and Kelley 1971). The others are known only as inferred protein products of cloned genes; their catalytic properties have not been determined.
Cytosolic phosphoribosyl pyrophosphate synthetase 1 catalyzes the reaction of D-ribose 5-phosphate and dATP to form 5-phospho-alpha-D-ribose 1-diphosphate and 2'-deoxyadenosine 5'-monophosphate. While phosphoribosyl pyrophosphate synthetase 1 works well with either ATP or dATP as a substrate in vitro, the extent of the dATP reaction in vivo is unclear, as cellular dATP concentrations are normally very low (Fox and Kelley 1971).
The pentose phosphate pathway is responsible for the generation of a substantial fraction of the cytoplasmic NADPH required for biosynthetic reactions, and for the generation of ribose 5-phosphate for nucleotide synthesis. Although the pentose phosphate pathway and glycolysis are distinct, they involve three common intermediates, glucose 6-phosphate, glyceraldehyde 3-phosphate, and fructose 6-phosphate, so the two pathways are interconnected. The pentose phosphate pathway consists of eight reactions:1. Conversion glucose 6-phosphate to D-glucono-1,5-lactone 6-phosphate, with the formation of NADPH; 2. Conversion of D-glucono-1,5-lactone 6-phosphate to 6-phospho-D-gluconate; 3. Conversion of 6-phospho-D-gluconate to ribulose 5-phosphate, with the formation of NADPH; 4. Conversion of ribulose 5-phosphate to xylulose 5-phosphate; 5. Conversion of ribulose 5-phosphate to ribose 5-phosphate; 6. Rearrangement of ribose 5-phosphate and xylulose 5-phosphate to form sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate; 7. Rearrangement of sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate to form erythrose 4-phosphate and fructose 6-phosphate; and 8. Rearrangement of xylulose 5-phosphate and erythrose 4-phosphate to form glyceraldehyde 3-phosphate and fructose-6-phosphate. The oxidative branch of the pentose phosphate pathway, reactions 1-3, generates NADPH and pentose 5-phosphate. The non-oxidative branch of the pathway, reactions 4-8, converts pentose 5-phosphate to other sugars. The overall pathway can operate to generate only NADPH (glucose 6-phosphate is converted to pentose 5-phosphates, which are directed to the synthesis of fructose 6-phosphate and glyceraldehyde 3-phosphate, which in turn are converted back to glucose 6-phosphate). The reactions of the non-oxidative branch can operate to generate net amounts of ribose 5-phosphate with no production of NADPH. Net flux through this network of reactions appears to depend on the metabolic state of the cell and the nature of the biosynthetic reactions underway (Casazza and Veech 1987). G6PD, the enzyme that catalyzes the first reaction of the pathway, is more extensively mutated in human populations than any other enzyme, pehaps because these mutant alleles confer malaria resistance (Luzzatto and Afolayan 1968). Mutations affecting other parts of the pathway are rare, though several have been described and studies of their effects have contributed to our understanding of the normal flux of metabolites through this network of reactions (Wamelink et al. 2008).
The reversible interconversion of ribose 5-phosphate and ribulose 5-phosphate is catalyzed by cytosolic ribose 5-phosphate isomerase (Huck et al. 2004).
Hyaluronan (hyaluronic acid, HA) is composed of repeating disaccharide units of glucuronic acid and N-acetylglucosamine [-4GlcAb1-3GlcNAcb1-]. It is synthesized in the cell membrane by adding monosaccharides to the reducing end of the chain using the precursors UDP-glucuronic acid and UDP-N-acetylglucosamine in the presence of Mg2+. The integral membrane dual-action glycosyltransferase proteins hyaluronan synthases, of which vertebrates have three types (HAS1-3), catalyze these monosaccharide additions. Unlike other GAGs, HA is synthesized as a free glycan, not attached to a protein (Laurent 1987, Weigel & DeAngelis, 2007). As HA is synthesised it is extruded from the cell by an ABC-type transporter into the extracellular medium.
5-Phospho-alpha-D-ribose 1-diphosphate (PRPP) is a key intermediate in both the de novo and salvage pathways of purine and pyrimidine synthesis. PRPP and the enzymatic activity responsible for its synthesis were first described by Kornberg et al. (1955). The enzyme, phosphoribosyl pyrophosphate synthetase 1, has been purified from human erythrocytes and characterized biochemically. The purified enzyme readily forms multimers; its smallest active form appears to be a dimer and for simplicity it is annotated as a dimer here. It specifically catalyzes the transfer of pyrophosphate from ATP or dATP to D-ribose 5-phosphate, and has an absolute requirement for Mg++ and orthophosphate (Fox and Kelley 1971; Roth et al. 1974). The significance of the reaction with dATP in vivo is unclear, as the concentration of cytosolic dATP is normally much lower than that of ATP. The importance of this enzyme for purine synthesis in vivo has been established by demonstrating excess phosphoribosyl pyrophosphate synthetase activity, correlated with elevated enzyme levels or altered enzyme properties, in individuals whose rates of uric acid production are constitutively abnormally high (Becker and Kim 1987; Roessler et al. 1993). Molecular cloning studies have revealed the existence of two additional genes that encode phosphoribosyl pyrophosphate synthetase-like proteins, one widely expressed (phosphoribosyl pyrophosphate synthetase 2) and one whose expression appears to be confined to the testis (phosphoribosyl pyrophosphate synthetase 1-like 1) (Taira et al. 1989; 1991). Neither of these proteins has been purified and characterized enzymatically, nor have variations in the abundance or sequence of either protein been associated with alterations in human nucleotide metabolism (Roessler et al. 1993; Becker et al. 1996), so their dimerization and ability to catalyze the synthesis of PRPP from D-ribose 5-phosphate are inferred here on the basis of their predicted amino acid sequence similarity to phosphoribosyl pyrophosphate synthetase 1.
As hyaluronan (HA) is synthesised, it is continually extruded from the cell by the ABC transporter C5 (ABCC5), also called multidrug resistance-associated protein 5 (MRP5) (Schulz et al. 2007).
Hyaluronan (HA) turnover can occur locally at the tissue of origin, where it is taken up by cells to be degraded, or released into the lymphatic and vascular systems, where it can be eliminated by the liver and kidneys. Uptake of HA into cells for degradation involves receptor-mediated processes. Once HA enters lysosomes, the acidic conditions favour hyaluronidases to cleave it into small oligosaccharides, the most common size being a tetrasaccharide. Beta-glucuronidases participate in degrading the small oligosaccharides in the lysosome. Ultimately, HA is degraded into its constituent sugars (glucuronic acid and N-acetylglucosamine) which can be used to reform many glycosaminoglycans (GAGs) when released from the lysosome. A third of the total HA content in humans is turned over daily and it has a short half life of minutes in circulation up to days in many tissues. The reasons why the body eliminates HA so rapidly are unknown but one possible explanation could be HA's role as a reactive oxygen species (ROS) scavenger. Removing these toxic compounds could explain the rapid elimination of HA (Lepperdinger et al. 2004, Menzel & Farr 1998, Erickson & Stern 2012, Stern 2003).
3-Methylglutaconic aciduria type I is caused by mutations in AUH.
Hyaluronan (hyaluronic acid, hyaluronate or HA) is an anionic glycosaminoglycan (GAG) distributed widely throughout connective, epithelial, and neural tissues and most abundant in the extracellular matrix and skin. HA is unique among the GAGs in that it is not sulfated and is not found covalently attached to proteins as a proteoglycan. HA polymers are very large (they can reach molecular weights of 10 million Da) and can displace a large volume of water making them excellent lubricators and shock absorbers. Another unique feature of HA is that it is synthesized at the plasma membrane unlike other GAGs which are formed in the Golgi. HA is a polymer of the disaccharide unit D-glucuronic acid and D-N-acetylglucosamine, linked via alternating beta-1,4 and beta-1,3 glycosidic bonds (Toole 2000, 2004, Volpi et al. 2009).
Identification and characterization of the gene encoding the human phosphopantetheine adenylyltransferase and dephospho-CoA kinase bifunctional enzyme (CoA synthase)
Cytosolic UDP-galactose 4-epimerase catalyzes the interconversion of UDP-D-galactose and UDPglucose (Schulz et al. 2004). The active form of the enzyme is a homodimer with one molecule of bound NAD per monomer (Thoden et al. 2000).
Cytosolic glucose-6-phosphate dehydrogenase (G6PD) catalyzes the reaction of glucose 6-phosphate and NADP+ to form D-glucono-1,5-lactone 6-phosphate and , and NADPH + H+. Biochemical studies indicate that both G6PD dimers and tetramers are catalytically active and capable or forming under physiological conditions in vivo (Au et al. 2000). Mutations that reduce the catalytic efficientcy of G6PD are remarkably common in human populations; these appear to have a protective effect against malaria (e.g., Luzzatto and Afolayan 1968).
The main sources of galactose in the human diet are milk and milk products. The disaccharide lactose from these sources is hydrolyzed in the intestine to its constituent monosaccharides, glucose and galactose. Galactose is metabolized primarily in the liver in a sequence of three reactions that yield one molecule of glucose 1-phosphate per molecule of galactose. First, it is phosphorylated to yield galactose 1-phosphate. Then, galactose 1-phosphate and UDP-glucose react to form UDP-galactose and glucose 1-phosphate, and UDP-galactose undergoes epimerization to form UDP-glucose. In a reaction shared with other pathways, glucose 1-phosphate can be converted into glucose 6-phosphate (Holton et al. 2001; Elsas and Lai 2001).
Cytosolic 6-phosphogluconolactonase (PGLS) catalyzes the hydrolysis of D-glucono-1,5-lactone 6-phosphate to form 6-phospho-D-gluconate (Beutler and Kuhl 1985; Collard et al. 1999).
Cytosolic phosphogluconate dehydrogenase (PGD) catalyzes the reaction of 6-phospho-D-gluconate and NADP+ to form D-ribulose 5-phosphate, CO2, and NADPH + H+ (Beutler and Kuhl 1985; Rippa et al. 1998). The PGD enzyme is dimeric (Dallocchio et al. 1985).
Cytosolic ribulose-5-phosphate-3-epimerase (RPE) catalyzes the reversible interconversion of D-ribulose 5-phosphate and D-xylulose 5-phosphate (Bose and 1985). The electrophoretic properties of RPE activity detected in extracts of mouse-human somatic cell hybrids suggest that the active form of the enzyme is a homodimer (Spencer and Hopkinson 1980).
Cytosolic ribulose-5-phosphate-3-epimerase (RPE) catalyzes the reversible interconversion of D-xylulose 5-phosphate and D-ribulose 5-phosphate (Bose and 1985). The electrophoretic properties of RPE activity detected in extracts of mouse-human somatic cell hybrids suggest that the active form of the enzyme is a homodimer (Spencer and Hopkinson 1980).
Cytosolic transaldolase (TALDO1) catalyzes the reversible reaction of D-glyceraldehyde 3-phosphate and sedoheptulose 7-phosphate to form D-erythrose 4-phosphate and D-fructose 6-phosphate. Protein expressed from the cloned gene has been characterized biochemically (Banki et al. 1994) and transaldolase deficiency in a patient has been correlated with a mutation in the TALDO1 gene (Verhoeven et al. 2001).
Cytosolic transaldolase (TALDO1) catalyzes the reversible reaction of D-erythrose 4-phosphate and D-fructose 6-phosphate to form D-glyceraldehyde 3-phosphate and sedoheptulose 7-phosphate. Protein expressed from the cloned gene has been characterized biochemically (Banki et al. 1994) and transaldolase deficiency in a patient has been correlated with a mutation in the TALDO1 gene (Verhoeven et al. 2001).
Analysis of GPIIb/IIIa receptor number by quantification of 7E3 binding to human platelets
The reversible interconversion of ribulose 5-phosphate and ribose 5-phosphate is catalyzed by cytosolic ribose 5-phosphate isomerase (Huck et al. 2004).
In vivo demonstration that {alpha}-synuclein oligomers are toxic
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Enzymatic synthesis and properties of 5-phosphoribosylpyrophosphate
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Ornithine delta-aminotransferase mutations in gyrate atrophy. Allelic heterogeneity and functional consequences.
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
Localization, regulation and function of type II phosphatidylinositol 5-phosphate 4-kinases
SLC25A1, in the inner mitochondrial membrane, mediates the exchange of cytosolic citrate for mitochondrial phosphoenolpyruvate. The exchange is physiologically irreversible because of the potential of the inner mitochondrial membrane. The gene encoding human SLC25A1 has been cloned and its expression pattern has been characterized (Heisterkamp et al. 1995; Iacobazzi et al. 1997), but the biochemical details of the transport process are inferred from those worked out for the well-characterized rat system (Robinson 1971; Soling et al. 1971; Kleineke et al. 1973).
PCK2 (phosphoenolcarboxykinase), located in the mitochondrial matrix, catalyzes the physiologically irreversible reaction of oxaloacetate and GTP to form phosphoenolpyruvate, GDP, and CO2 (Modaressi et al. 1996, 1998).
Cytosolic pyruvate kinase catalyzes the transfer of a high-energy phosphate from phosphoenolpyruvate to ADP, forming pyruvate and ATP. This reaction, an instance of substrate-level phosphorylation, is essentially irreversible under physiological conditions. Four isozymes of human pyruvate kinase have been described, L, R, M1 and M2. Isozymes L and R are encoded by alternatively spliced transcripts of the PKLR gene; isozymes M1 and M2 are encoded by alternatively spliced transcripts of PKM2. In the body, L pyruvate kinase is found in liver (Tani et al. 1988), R in red blood cells (Kanno et al. 1991), M1 in muscle, heart and brain (Takenaka et al. 1991), and M2 in early fetal tissues and tumors (e.g., Lee et al. 2008). In all cases, the active form of the enzyme is a homotetramer, activated by fructose 1,6-bisphosphate (Valentini et al. 2002; Dombrauckas et al. 2005). Mutations in PKLR have been associated with hemolytic anemias (e.g., Zanella et al. 2005).
Cytosolic phosphoglycerate mutase catalyzes the reversible isomerisation of 3- and 2-phosphoglycerate. The active form of the enzyme is a dimer. There are two isoforms of this enzyme, PGAM1 (isoform B, widely expressed in non-muscle tissue) and PGAM2 (isoform M, expressed in muscle) (Blouquit et al. 1988; Omenn and Cheung 1974; Repiso et al. 2005; Tsujino et al. 1993).
Cytosolic malate dehydrogenase catalyzes the reaction of malate and NAD+ to form oxaloacetate and NADH + H+ (Lo et al. 2005). The dimeric structure of the human dehydrogenase is inferred from that established for its well-studied pig homolog (Birktoft et al. 1989).
The reactions of glycolysis (e.g., van Wijk and van Solinge 2005) convert glucose 6-phosphate to pyruvate. The entire process is cytosolic. Glucose 6-phosphate is reversibly isomerized to form fructose 6-phosphate. Phosphofructokinase 1 catalyzes the physiologically irreversible phosphorylation of fructose 6-phosphate to form fructose 1,6-bisphosphate. In six reversible reactions, fructose 1,6-bisphosphate is converted to two molecules of phosphoenolpyruvate and two molecules of NAD+ are reduced to NADH + H+. Each molecule of phosphoenolpyruvate reacts with ADP to form ATP and pyruvate in a physiologically irreversible reaction. Under aerobic conditions the NADH +H+ can be reoxidized to NAD+ via electron transport to yield additional ATP, while under anaerobic conditions or in cells lacking mitochondria NAD+ can be regenerated via the reduction of pyruvate to lactate.
SLC25A12 and SLC25A13, located in the inner mitochondrial membrane, each mediate the exchange of cytosolic aspartate and mitochondrial glutamate. The exchange is physiologically irreversible because of the potential across the inner mitochondrial membrane (positive outside, negative inside). In the body, SLC25A12 (ARALAR1) is found mainly in heart, skeletal muscle, and brain, while SCL25A13 (CITRIN) is widely expressed but most abundant in liver (del Arco et al. 2000; Palmieri et al. 2001). Defects in SLC25A13 are associated with type II citrullinemia (Kobayashi et al. 1999).
Mitochondrial aspartate aminotransferase catalyzes the reversible reaction of oxaloacetate and glutamate to form aspartate and 2-oxoglutarate (alpha-ketoglutarate) (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.
The transfer of a high-energy phosphate bond from GTP to oxaloacetate, to form phosphoenolpyruvate, GDP, and CO2, is catalyzed by cytosolic phosphoenolpyruvate carboxykinase (Dunten et al. 2002). This reaction is irreversible under physiological conditions.
Cytosolic aspartate aminotransferase (glutamate oxaloacetate transaminase 1 - GOT1) catalyzes the reversible reaction of aspartate and 2-oxoglutarate (alpha-ketoglutarate) to form oxaloacetate and glutamate (Doyle et al. 1990). Unpublished crystallographic data (PBD 3IIO) suggest the enzyme is a homodimer).
Reactions specific to the complex N-glycan synthesis pathway
The bisretinoids of retinal pigment epithelium
ChEBI:16618 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
Cytosolic phosphoglycerate kinase catalyzes the reaction of ADP and 1,3-bisphosphoglycerate to form D glyceraldehyde 3-phosphate and ATP. The active form of the enzyme is a monomer and requires Mg++ (Yoshida and Watanabe 1972; Huang et al. 1980a,b). This is the first substrate level phosphorylation reaction in glycolysis.
Cytosolic glyceraldehyde 3-phosphate dehydrogenase catalyzes the reversible reaction of glyceraldehyde 3-phosphate, orthophosphate, and NAD+ to form NADH + H+ and 1,3-bisphosphoglycerate, the first energy rich intermediate of glycolysis. The biochemical details of this reaction were worked out by C and G Cori and their colleagues (Taylor et al. 1948; Cori et al. 1948). While there are multiple human glyceraldehyde 3-phosphate dehydrogenase-like pseudogenes, there is only one glyceraldehyde 3-phosphate dehydrogenase gene expressed in somatic tissue (Benham and Povey 1989; Heinz and Freimuller 1982; Ercolani et al. 1988), and studies of aged human erythrocytes suggest that variant forms of the enzyme arise as a result of post-translational modifications (Edwards et al. 1976). There is, however, an authentic second isoform of glyceraldehyde 3-phosphate dehydrogenase whose expression is confined to spermatogenic cells of the testis (Welch et al. 2000).
Cytosolic triose phosphate isomerase catalyzes the freely reversible interconversion of dihydroxyacetone phosphate and glyceraldehyde 3-phosphate (Lu et al. 1984). The active form of the enzyme is a homodimer (Kinoshita et al. 2005).
Extracellular trehalose, a disaccharide, is cleaved by trehalase associated with the plasma membrane to yield two molecules of glucose. Trehalase has been purified to homogeneity from rabbit intestine and shown to be a monomer attached to the plasma membrane by a GPI anchor (Galand 1984; Ruf et al. 1990). A human cDNA encoding a closely homologous protein has been cloned and the protein product of the clone has been shown to have trehalase activity in vitro (Ishihara et al. 1997). The human enzyme has not been characterized further, and so both the posttranslational modifications of the human enzyme and its activity in vivo have been inferred from the properties of the well studied rabbit enzyme.
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).
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.
Cytosolic aldolase catalyzes the cleavage of D-fructose 1,6-bisphosphate to yield dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. The active form of aldolase is a homotetramer. Three aldolase isozymes have been identified which differ in their patterns of expression in various adult tissues and during development but are otherwise functionally indistinguishable (Ali and Cox 1995; Freemont et al. 1984, 1988).
Cytosolic phosphofructokinase 1 catalyzes the reaction of fructose 6-phosphate and ATP to form fructose 1,6-bisphosphate and ADP. This reaction, irreversible under physiological conditions, is the rate limiting step of glycolysis. Phosphofructokinase 1 activity is allosterically regulated by ATP, citrate, and fructose 2,6-bisphosphate. Phosphofructokinase 1 is active as a tetramer (although higher order multimers, not annotated here, may form in vivo). Two isoforms of phosphofructokinase 1 monomer, L and M, are widely expressed in human tissues. Different tissues can contain different homotetramers or heterotetramers: L4 in liver, M4 in muscle, and all possible heterotetramers, L4, L3M, L2M2, LM3, and M4, in red blood cells, for example (Raben et al. 1995; Vora et al. 1980, 1987; Vora 1981). A third isoform, P, is abundant in platelets, where it is found in P4, P3L, P2L2, and PL3 tetramers (Eto et al. 1994; Vora et al. 1987).
Cytosolic phosphoglucose isomerase catalyzes the reversible interconversion of glucose 6-phosphate and fructose 6-phosphate (Tsuboi et al. 1958; Noltmann 1972; Bloxham and Lardy 1973). The active form of the enzyme is a homodimer (Read et al. 2001). Mutations in the enzyme are associated with hemolytic anemia (Xu and Beutler 1994).
Carbohydrate is a major component of the human diet, and includes starch (amylose and amylopectin) and disaccharides such as sucrose, lactose, maltose and, in small amounts, trehalose. The digestion of starch begins with the action of amylase enzymes secreted in the saliva and small intestine, which convert it to maltotriose, maltose, limit dextrins, and some glucose. Digestion of the limit dextrins and disaccharides, both dietary and starch-derived, to monosaccharides - glucose, galactose, and fructose - is accomplished by enzymes located on the luminal surfaces of enterocytes lining the microvilli of the small intestine (Semenza et al. 2001).
A proteasome inhibitor prevents activation of NF-kappa B and stabilizes a newly phosphorylated form of I kappa B-alpha that is still bound to NF-kappa B
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MicroRNAs: genomics, biogenesis, mechanism, and function
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Phenylalanine hydroxylase-stimulating protein/pterin-4 alpha-carbinolamine dehydratase from rat and human liver. Purification, characterization, and complete amino acid sequence.
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Mechanisms of type-I- and type-II-interferon-mediated signalling
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Synthesis of IP2, IP, and Ins in the cytosol
Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors
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Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha
(S)-alpha-Amino-1H-imidazole-4-propionic acid
Cardiolipin hydrolysis by human phospholipases A2. The multiple enzymatic activities of human cytosolic phospholipase A2
Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis
(S)-alpha-amino-beta-phenylpropionic acid
(S)-2-Amino-3-(p-hydroxyphenyl)propionic acid
TTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elements
Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia
Glucuronidation and the UDP-glucuronosyltransferases in health and disease
Phosphorylation of FANCD2 on two novel sites is required for mitomycin C resistance
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Triggering and amplifying pathways of regulation of insulin secretion by glucose
1-phosphatidyl-1D-myo-inositol 4,5- bisphosphate
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phosphatidylinositol 1,4,5-trisphosphate
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphates
1,2-Diacyl-sn-glycerol 3-phospho-L-serine
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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_24500.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=901054
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648122
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648127
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648126
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_139621.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648129
A human testis-specific mRNA for phosphoribosylpyrophosphate synthetase that initiates from a non-AUG codon
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
Diacylglycerol, when simplicity becomes complex
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.
Arp2/3 ATP hydrolysis: to branch or to debranch?
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.
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).
Ionizing radiation (IR) induces single-strand breaks i.e. cleavage of the phosphodiester backbone. When two single-strand breaks occur within approximately 10 base pairs, a DNA double-strand break results. IR-induced DSBs are complex DNA damage lesions, containing base damage and frequently containing 5'-OH groups and 3'-hydroxy or phosphoglycolate groups that must be removed prior to ligation in the final step of NHEJ (Friedberg et al, 1995; Nikjoo et al, 2001; Valerie and Povirk, 2003). The Ku70/80 heterodimer (Walker et al., 2001) binds to the ends of the double-strand break. Ku can translocate inwards from the site of the break in an ATP-independent manner (reviewed in Dynan and Yoo, 1998).
DNA-PKcs is recruited to the Ku-DNA end complex (Gottlieb and Jackson, 1993), causing Ku to translocate inwards (away from the break) approximately 10 bp (Yoo and Dynan, 1999). This forms the DNA-PK complex (DNA-PKcs plus Ku70/Ku80) at each end of the DNA double strand break.
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.
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.
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.
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'.
The NHEJ pathway is initiated in response to the formation of a DNA double-strand break (DSB) induced by a DNA-damaging agent such as ionizing radiation. First, the Ku70/80 heterodimer binds to the ends of the DSB. The catalytic subunit of the DNA-dependent protein kinase (DNA-PKcs) is then recruited to DNA-bound Ku to form the DNA-PK holoenzyme. The ends of the break are brought together as two molecules of DNA-PK (one at each end of the break) are joined in a synaptic complex. Other factors, such as polynucleotide kinase (PNK), Artemis, the MRE complex, hTdp1 or the Werner Syndrome protein (WRN) may be required for processing of the DNA ends prior to end rejoining, but exactly when processing takes place is not known. Following the formation of the synaptic complex, the XRCC4/DNA ligase IV complex is recruited. Prior to end rejoining, protein factors must be removed from the DNA. This may involve DNA-PK autophosphorylation (Chan and Lees-Miller, 1996; Douglas et al., 2001; 2002; Merkle et al., 2002). After removal of the repair factors, the DNA ends are ligated and the DNA is repaired. Both Mg-ATP and the protein kinase activity of DNA-PKcs are required for NHEJ (Kurimasa et al.,1999; Kienker et al, 2000; Baumann and West, 1998), probably through phosphorylation of DNA-PKcs and/or other proteins. In addition, inositol hexaphosphate (IP6) stimulates end joining in vitro (Hanakahi et al., 2000) and binds to Ku, but its precise role in NHEJ is unknown.
Two DNA-PK-DNA complexes, one on either side of the break, interact to bring the DNA ends together in synaptic complex (DeFazio et al., 2002).
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
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.
Autophosphorylation of DNA-PKcs is required for NHEJ in vivo (Chan et al, 2002; Ding et al, 2003).
B cell lymphoma 10 is essential for FcepsilonR-mediated degranulation and IL-6 production in mast cells
DNA Ligase 1 ligates the newly synthesized fragment to the gap in the template DNA.
Isoleucylation properties of native human mitochondrial tRNAIle and tRNAIle transcripts. Implications for cardiomyopathy-related point mutations (4269, 4317) in the tRNAIle gene
ChEBI:16496 5beta-Cholestane-3alpha,7alpha,12alpha-triol
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.
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'.
At the beginning of this reaction, 1 molecule of 'damaged DNA substrate ', and 1 molecule of 'Pol zeta complex' are present. At the end of this reaction, 1 molecule of 'Pol zeta:damaged DNA template complex' is present. This reaction takes place in the 'nucleus'.
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.
The enzymic chain elongation of fatty acids by rat-liver microsomes
Resolution of AP sites can occur through the single-nucleotide replacement pathway or through the multiple-nucleotide patch replacement pathway.
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 3ââ¬â¢ 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).
Pol zeta consists of two proteins: HREV3 with polymerase activity and HREV7, an accessory factor with unidentified activity. It has the ability to bypass pyrimidine dimers and other adducts in DNA.
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 'HREV7', and 1 molecule of 'HREV3' are present. At the end of this reaction, 1 molecule of 'Pol zeta complex' is present. This reaction takes place in the 'nucleus'.
Cyclic nucleotides and phosphodiesterases in platelets
At the beginning of this reaction, 1 molecule of 'dNTP', and 1 molecule of 'Pol zeta:damaged DNA template complex' are present. At the end of this reaction, 1 molecule of 'Pol zeta complex', 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 'Pol zeta:damaged DNA template complex'.
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 3ââ¬â¢->5ââ¬â¢ 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.
DNA damage can be directly reversed by dealkylation.
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).
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.
MRE11 has both manganese dependent ss DNA 3'-5' exonuclease and endonuclease activities. MRE11 associates with RAD50 resulting in increased 3'-5' exonuclease activity.
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.
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).
Structural determinants of water permeation through aquaporin-1
Mutations in the NSDHL gene, encoding a 3beta-hydroxysteroid dehydrogenase, cause CHILD syndrome
Signaling through platelet integrin alpha IIb beta 3: inside-out, outside-in, and sideways
At the beginning of this reaction, 1 molecule of '3' overhanging DNA at resected DSB ends', and 1 molecule of 'RAD52' are present. At the end of this reaction, 1 molecule of 'RAD52:DNA double-strand break' is present. This reaction takes place in the 'nucleus'.
Binding of the RAD51:RAD52 complex to ssDNA may provide nucleation sites promoting the association of free RAD51 with the growing nucleoprotein filament. This interaction may also play a role in stimulating the strand transfer reactions mediated by RAD51 (Baumann, 1999).
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'.
Human phosphoribosylpyrophosphate synthetase
Purification and properties of short chain acyl-CoA, medium chain acyl-CoA, and isovaleryl-CoA dehydrogenases from human liver.
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
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.
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.
The ââ¬Åroad blockââ¬Â 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 ââ¬Ërepair-transcription uncoupling factorââ¬â¢ 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 3ââ¬â¢ end of the nascent RNA product leading to the enhanced access to damage site on the corresponding template DNA.
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'.
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.
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 '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 '.
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 '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'.
Protein kinase C-delta is a negative regulator of antigen-induced mast cell degranulation
A fatal mitochondrial disease is associated with defective NFU1 function in the maturation of a subset of mitochondrial Fe-S proteins
Polymerization is carried out by DNA polymerases, delta and epsilon.
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 Cockayneââ¬â¢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 Cockayneââ¬â¢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.
ATR and ATM dependent phosphorylation of FANCD2 promotes the monoubiquitination of FANCD2 stimulating the FA pathway (Andreassen et al., 2004; Ho et al., 2006).
The Fanconi anemia DNA repair pathway is negatively regulated by the deubiquitination of FANCD2 an postively regulated by phosphorylation of the FANCD2 and FANCI. The USP1 deubiquitinating enzyme is responsible for FANCD2 deubiquitination and is activated by the WD40-repeat containing UAF1 protein through formation of a stable USP1/UAF1 protein complex (Cohn et al., 2007). ATR and ATM dependent phosphorylation of FANCD2 at T691 and S717 promotes the monoubiquitination of FANCD2 stimulating the FA pathway (Ho et al., 2006). Multiple phosphorylation sites within FANCI are functionally important for inducing monoubiquitination of FANCD2 and thus the activation of the FA pathway (Ishiai et al., 2008) .
Fanconi anemia (FA) is a genetic disease of genome instability characterized by congenital skeletal defects, aplastic anemia, susceptibility to leukemias, and cellular sensitivity to DNA damaging agents. Patients with FA have been categorized into at least 13 complementation groups (FA-A, -B, -C, -D1, -D2, -E, -F, -G, -I, -J, -L, -M, and -N). These complementation groups correspond to the genes FANCA, FANCB, FANCC, FANCD1/BRCA2, FANCD2, FANCE, FANCF, FANCG, FANCJ/BRIP1, FANCL, FANCM, and FANCN/PALB2. Although the functions of most of these proteins are mostly unknown, eight of them, FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, and FANCM products together with AAP24 and FAAP100 form a nuclear complex termed the FA core complex. The core complex is essential for FANCD2 and FANCI monoubiquitination after DNA damage. FANCD2 and FANCI are mutually dependent on one another for their respective monoubiquitination. After DNA damage and during S phase, FANCD2 localizes to chromatin, forming foci that overlap those containing proteins involved in homologous recombination, such as BRCA1 and RAD51. The FA pathway is regulated by the deubiquitination of FANCD2 and the phosphorylation FANCD2 and FANCI. The USP1/UAF1 complex is responsible for deubiquitination of FANCD2 and negatively regulates the FA pathway (Cohn et al., 2007) ATR and ATM dependent phosphorylation of FANCD2 promotes the monoubiquitination of FANCD2 stimulating the FA pathway (Cohn and D'Andrea, 2008; Wang, 2007).
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.
Nek2A does not appear to be recruited to the APC/C by Cdc20 but rather binds directly to the APC/C in an interaction involving the NEK2A C-terminal methionineââ¬âarginine (MR) dipeptide tail (Hayes et al., 2006).
Nek2A is ubiquitinated by the APC/C-Cdc20 ubiquitin ligase.
Molecular cloning of cDNA encoding human lanosterol synthase
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
Antiviral mechanism by IFN-stimulated genes
Biosynthesis of tetrahydrobiopterin. Purification and characterization of 6-pyruvoyl-tetrahydropterin synthase from human liver
Kerato-epithelin mutations in four 5q31-linked corneal dystrophies
Molecular aspects of the adenine nucleotide carrier from mitochondria
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'.
At the beginning of this reaction, 1 molecule of 'dNTP', and 1 molecule of 'POL Beta: APE1-bound DNA strand break containing incision 5' to AP site ' are present. At the end of this reaction, 1 molecule of 'pyrophosphate', and 1 molecule of 'POL Beta: APE1-bound 5' incised DNA strand break containing first resynthesized base ' are present. This reaction takes place in the 'nucleus' and is mediated by the 'beta DNA polymerase activity' of 'DNA polymerase beta (EC 2.7.7.7)'.
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 'LIG3:XRRC1-bound DNA strand containing the ligated residue' is present. At the end of this reaction, 1 molecule of 'LIG3:XRRC1 complex ', and 1 molecule of 'DNA strand containing replaced ligated residue' are present. This reaction takes place in the 'nucleus'.
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'.
A single enzyme catalyzes both platelet-activating factor production and membrane biogenesis of inflammatory cells. Cloning and characterization of acetyl-CoA:LYSO-PAF acetyltransferase
At the beginning of this reaction, 1 molecule of 'POL Beta: APE1-bound DNA strand break containing incision 5' to AP site ' is present. At the end of this reaction, 1 molecule of 'POL Beta-bound DNA strand break containing gap left by excised residue', 1 molecule of 'APE1', and 1 molecule of 'Sugar phosphate' are present. This reaction takes place in the 'nucleus' and is mediated by the 'DNA-(apurinic or apyrimidinic site) lyase activity' of 'DNA polymerase beta (EC 2.7.7.7)'.
DNA polymerase Beta mediates DNA synthesis that fills the gap left by the excised residue using the undamaged strand as a template.
At the beginning of this reaction, 1 molecule of 'LIG3:XRCC1:POL Beta:DNA strand break containing replaced unligated residue' is present. At the end of this reaction, 1 molecule of 'LIG3:XRRC1-bound DNA strand containing the ligated residue' is present. This reaction takes place in the 'nucleus' and is mediated by the 'DNA ligase activity' of 'DNA ligase III '.
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).
At the beginning of this reaction, 1 molecule of 'POL Beta-bound DNA strand break containing gap left by excised residue', and 1 molecule of 'LIG3:XRRC1 complex ' are present. At the end of this reaction, 1 molecule of 'LIG3:XRCC1:POL Beta complex at site of base repair' is present. This reaction takes place in the 'nucleus'.
At the beginning of this reaction, 1 molecule of 'DNA containing an hOGG1-bound apurinic/apyrimidinic site', and 1 molecule of 'APE1' are present. At the end of this reaction, 1 molecule of 'hOGG1 glycosylase', and 1 molecule of 'DNA containing an APE1-bound AP site' are present. This reaction takes place in the 'nucleus'.
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'.
Following cleavage of the damaged base, DNA glycosylase is displaced by APE1.
At the beginning of this reaction, 1 molecule of 'DNA containing an MYH-bound apurinic/apyrimidinic site', and 1 molecule of 'APE1' are present. At the end of this reaction, 1 molecule of 'MYH glycosylase', and 1 molecule of 'DNA containing an APE1-bound AP site' are present. This reaction takes place in the 'nucleus'.
At the beginning of this reaction, 1 molecule of 'APE1-bound DNA strand break containing an incision 5' to an AP site', and 1 molecule of 'DNA polymerase beta (EC 2.7.7.7)' are present. At the end of this reaction, 1 molecule of 'POL Beta: APE1-bound DNA strand break containing incision 5' to AP site ' is present. This reaction takes place in the 'nucleus'.
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'.
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'.
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.
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 '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'.
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'.
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'.
Base excision repair is initiated by a DNA glycosylase which first recognizes and removes a damaged or incorrect (e.g. mismatched) base.
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 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'.
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'.
DNA damage-induced activation of p53 by the checkpoint kinase Chk2.
Depurination of a damaged nucleotide is mediated by a purine-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 apurinic (AP) site.
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'.
Damaged purines are first cleaved by purine-specific glycosylases (see Lindahl and Wood 1999).
At the beginning of this reaction, 1 molecule of 'MYH glycosylase:adenine complex' is present. At the end of this reaction, 1 molecule of 'DNA containing an MYH-bound apurinic/apyrimidinic site', and 1 molecule of '8-oxoguanine' are present. This reaction takes place in the 'nucleus' and is mediated by the 'DNA N-glycosylase activity' of 'MYH glycosylase'.
The recognition and cleavage of an altered base by a DNA glycosylase is thought to involve the diffusion of the enzyme along the minor grove of the DNA molecule. The enzyme presumably compresses the backbone of the affected DNA strand at the site of damage. This compression is thought to result in an outward rotation of the damaged residue into a "pocket" of the enzyme that recognizes and cleaves the altered base (Parikh et al., 1998).
At the beginning of this reaction, 1 molecule of 'hOGG1 glycosylase: formamidopyrimidine complex' is present. At the end of this reaction, 1 molecule of 'DNA containing an hOGG1-bound apurinic/apyrimidinic site', and 1 molecule of 'formamidopyrimidine' are present. This reaction takes place in the 'nucleus' and is mediated by the 'purine-specific oxidized base lesion DNA N-glycosylase activity' of 'hOGG1 glycosylase'.
Insertion of residues 429 to 822 at 340 from UniProt:P11362 FGFR1 (in Homo sapiens)
At the beginning of this reaction, 1 molecule of 'hOGG1 glycosylase:8-oxo guanine complex' is present. At the end of this reaction, 1 molecule of '8-oxoguanine', and 1 molecule of 'DNA containing an hOGG1-bound apurinic/apyrimidinic site' are present. This reaction takes place in the 'nucleus' and is mediated by the 'purine-specific oxidized base lesion DNA N-glycosylase activity' of 'hOGG1 glycosylase'.
At the beginning of this reaction, 1 molecule of 'Double-strand DNA containing an adenine opposite to an 8-oxo guanine', and 1 molecule of 'MYH glycosylase' are present. At the end of this reaction, 1 molecule of 'MYH glycosylase:adenine complex' is present. This reaction takes place in the 'nucleus'.
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.
At the beginning of this reaction, 1 molecule of 'Double-strand DNA containing a formamidopyrimidine ', and 1 molecule of 'hOGG1 glycosylase' are present. At the end of this reaction, 1 molecule of 'hOGG1 glycosylase: formamidopyrimidine complex' is present. This reaction takes place in the 'nucleus'.
At the beginning of this reaction, 1 molecule of 'Double-strand DNA containing an 8-oxo guanine opposite to a cytosine', and 1 molecule of 'hOGG1 glycosylase' are present. At the end of this reaction, 1 molecule of 'hOGG1 glycosylase:8-oxo guanine complex' is present. This reaction takes place in the 'nucleus'.
Arachidonic acid metabolism by human cytochrome P450s 2C8, 2C9, 2E1, and 1A2: regioselective oxygenation and evidence for a role for CYP2C enzymes in arachidonic acid epoxygenation in human liver microsomes
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.
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.
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Bidirectional integrin alphaIIbbeta3 signalling regulating platelet adhesion under flow: contribution of protein kinase C
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Human SMG-1, a novel phosphatidylinositol 3-kinase-related protein kinase, associates with components of the mRNA surveillance complex and is involved in the regulation of nonsense-mediated mRNA decay
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Genomic organization, cDNA sequence, bacterial expression, and purification of human seryl-tRNA synthase
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Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15
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Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms
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Loss of human Greatwall results in G2 arrest and multiple mitotic defects due to deregulation of the cyclin B-Cdc2/PP2A balance
Proc. Natl. Acad. Sci. U.S.A. 107:12564-9
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The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast
Cross-talk between the endocytic pathway and the endoplasmic reticulum in cross-presentation by MHC class I molecules
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Full mass spectrometric characterization of human monoacylglycerol lipase generated by large-scale expression and single-step purification
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N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: a novel enzyme of the beta-lactamase fold family releasing anandamide and other N-acylethanolamines
Error-prone DNA polymerases: novel structures and the benefits of infidelity.
The crystallographic structure of a human dihydropteridine reductase NADH binary complex expressed in Escherichia coli by a cDNA constructed from its rat homologue
Distribution of AQP2 and AQP3 water channels in human tissue microarrays
2'-deoxyribonucleoside triphosphate [ChEBI:16516]
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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.
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Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits
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myo-Inositol 1,2,4,5,6-pentakisphosphate
1D-myo-Inositol 1,2,4,5,6-pentakisphosphate
D-myo-Inositol 1,2,4,5,6-pentakisphosphate [ChEBI:4273]
D-myo-Inositol 1,2,4,5,6-pentakisphosphate
ChEBI:16500 1-phosphatidyl-1D-myo-inositol 5-phosphate
1-phosphatidyl-1D-myo-inositol 5-phosphate
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NMD: RNA biology meets human genetic medicine
Mutant human adenosine deaminase alleles and their expression by transfection into fibroblasts
Spatial expression patterns and biochemical properties distinguish a second myo-inositol monophosphatase IMPA2 from IMPA1
Functional cloning of BRF1, a regulator of ARE-dependent mRNA turnover
Cyclin B2 suppresses mitotic failure and DNA re-replication in human somatic cells knocked down for both cyclins B1 and B2
Characterization of the proteins released from activated platelets leads to localization of novel platelet proteins in human atherosclerotic lesions
Indirubin-3'-monoxime inhibits autophosphorylation of FGFR1 and stimulates ERK1/2 activity via p38 MAPK
The DNA replication fork in eukaryotic cells.
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1D-myo-Inositol 1,3,4,5,6-pentakisphosphate
D-myo-Inositol 1,3,4,5,6-pentakisphosphate
1D-myo-Inositol 1,3,4,5,6-pentakisphosphate [ChEBI:807]
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ChEBI:16320 (R)-3-Amino-2-methylpropanoate
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Isolation and chromosomal localization of a novel FMS-like tyrosine kinase gene
Proline to arginine mutations in FGF receptors 1 and 3 result in Pfeiffer and Muenke craniosynostosis syndromes through enhancement of FGF binding affinity
Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria
Baillieres Clin Endocrinol Metab 7:551-86
At the beginning of this reaction, 1 molecule of 'ATP', and 1 molecule of 'pre-replicative complex' are present. At the end of this reaction, 1 molecule of 'phosphorylated Orc1', 1 molecule of 'pre-replicative complex (Orc1-minus)', and 1 molecule of 'ADP' are present. This reaction takes place in the 'nucleus' and is mediated by the 'kinase activity' of 'Cyclin A:Cdk2 complex'.
DNA polymerases are not capable of de novo DNA synthesis and require synthesis of a primer, usually by a DNA-dependent RNA polymerase (primase) to begin DNA synthesis. In eukaryotic cells, the primer is synthesized by DNA polymerase alpha:primase. First, the DNA primase portion of this complex synthesizes approximately 6-10 nucleotides of RNA primer and then the DNA polymerase portion synthesizes an additional 20 nucleotides of DNA (Frick & Richardson 2002; Wang et al 1984).
At the beginning of this reaction, 1 molecule of 'dTTP', 1 molecule of 'dGTP', 1 molecule of 'dATP', 1 molecule of 'RNA primer:origin duplex:DNA polymerase alpha:primase complex', and 1 molecule of 'dCTP' are present. At the end of this reaction, 1 molecule of 'RNA primer-DNA primer:origin duplex' is present. This reaction takes place in the 'nucleus' and is mediated by the 'DNA-directed DNA polymerase activity' of 'DNA polymerase alpha:primase'.
At the beginning of this reaction, 1 molecule of 'ubiquitinated Orc1' is present. At the end of this reaction, 1 molecule of 'ubiquitin' is present. This reaction takes place in the 'cytosol' and is mediated by the 'endopeptidase activity' of '26S proteasome'.
In this reaction, 1 molecule of 'ubiquitinated Orc1' is translocated from nucleoplasm to cytosol. This movement of the molecule occurs through the 'nuclear pore'.
At the beginning of this reaction, 1 molecule of 'ubiquitin', and 1 molecule of 'phosphorylated Orc1' are present. At the end of this reaction, 1 molecule of 'ubiquitinated Orc1' is present. This reaction takes place in the 'nucleus'.
At the beginning of this reaction, 1 molecule of 'ubiquitinated Cdc6' is present. At the end of this reaction, 1 molecule of 'ubiquitin' is present. This reaction takes place in the 'cytosol' and is mediated by the 'endopeptidase activity' of '26S proteasome'.
At the beginning of this reaction, 1 molecule of 'CDC6', and 1 molecule of 'ATP' are present. At the end of this reaction, 1 molecule of 'ADP', and 1 molecule of 'phosphorylated Cdc6' are present. This reaction takes place in the 'nucleus' and is mediated by the 'kinase activity' of 'CDK'.
In this reaction, 1 molecule of 'phosphorylated Cdc6' is translocated from nucleoplasm to cytosol. This movement of the molecule occurs through the 'nuclear pore'.
Mutations in the facilitative glucose transporter GLUT10 alter angiogenesis and cause arterial tortuosity syndrome
Mitotic checkpoint proteins HsMAD1 and HsMAD2 are associated with nuclear pore complexes in interphase
At the start of the elongation phase of DNA replication, the Mcm2-7 complex may re-arrange to function as the replicative helicase associated with the replication fork. In general, a replicative helicase is associated with the replication fork and unwinds DNA ahead of the polymerase. In yeast, the Mcm proteins associate with origin DNA in G1 phase and then exit the origin upon replication initiation, consistent with moving out of the origin with the replication fork. The Mcm2-7 complex is a ring-shaped hexamer. Complexes of Mcm4, Mcm6 and Mcm7 proteins from humans or S. pombe display a modest ATP-dependent helicase activity in vitro. Consistent with the hypothesis that eukaryotic Mcm complexes function as helicases, an archaeal Mcm homolog is a ring-shaped double hexamer that has a processive DNA unwinding activity. Mcm proteins may have additional functions during elongation, as uninterrupted function of all six is required for replication fork progression in budding yeast. Mcm4,6,7 helicase activity may be negatively regulated in two ways. Mcm2, Mcm4, Mcm6, and Mcm7 also form a stable complex which, however, has no helicase activity, suggesting that Mcm2 inhibits DNA unwinding by Mcm4,6,7. In addition, phosphorylation of human Mcm4,6,7 complex by CDK inhibits its helicase activity.
NOD-like receptors: role in innate immunity and inflammatory disease
As cells enter S phase, HsCdc6p is phosphorylated by CDK promoting its export from the nucleus (see Bell and Dutta 2002).
In budding yeast, all MCM proteins have been proved to be essential for elongation. The active form of this protein complex may be a heterohexamer. A subcomplex of MCM proteins consisting fo MCM4,6, and -7 has a weak helicase activity that may contribute to DNA unwinding.
Folic acid: nutritional biochemistry, molecular biology, and role in disease processes
By applying the chromatin immunoprecipitation technique to paused forks, certain proteins like DNA pol alpha, DNA pol delta, DNA pol epsilon, MCM2-7, CDC45, GINS and MCM10 were identified. By uncoupling a helicase at the site using a polymerase inhibitor, MCM2-7, GINS complex and CDC45 alone were found to be enriched at the paused fork suggesting these proteins may form a part of an "unwindosome" at the replicating fork.
The MCM2-7 related protein, MCM8, is required to replicate chromosomal DNA in Xenopus egg extracts. MCM8 binds chromatin upon initiation of DNA synthesis. It may function as an helicase in the elongation step.
DNA Replication is regulated accurately and precisely by various protein complexes. Many members of the MCM protein family are assembled into the pre-Replication Complexes (pre-RC) at the end of M phase of the cell cycle. DNA helicase activity of some of the MCM family proteins are important for the unwinding of DNA and initiation of replication processes. This section contains four events which have been proved in different eukaryotic experimental systems to involve various proteins for this essential step during DNA Replication.
After the primers are synthesized, Replication Factor C binds to the 3'-end of the initiator DNA to trigger polymerase switching. The non-processive nature of pol alpha catalytic activity and the tight binding of Replication Factor C to the primer-template junction presumably lead to the turnover of the pol alpha:primase complex. After the Pol alpha-primase primase complex is displaced from the primer, the proliferating cell nuclear antigen (PCNA) binds to form a "sliding clamp" structure. Replication Factor C then dissociates, and DNA polymerase delta binds and catalyzes the processive synthesis of DNA.
Phosphorylated Cyclin D1 is degraded during S phase by the 26S proteasome allowing for efficient DNA synthesis.
In this reaction, 1 molecule of 'phospho(T286)-Cyclin D1' is translocated from nucleoplasm to cytosol. This reaction takes place in the 'nuclear envelope'.
The actual synthesis of DNA occurs in the S phase of the cell cycle. This includes the initiation of DNA replication, when the first nucleotide of the new strand is laid down during the synthesis of the primer. The DNA replication preinitiation events begin in late M or early G1 phase.
Accurate and efficient genome duplication requires coordinated processes to replicate two template strands at eucaryotic replication forks. Knowledge of the fundamental reactions involved in replication fork progression is derived largely from biochemical studies of the replication of simian virus and from yeast genetic studies. Since duplex DNA forms an anti-parallel structure, and DNA polymerases are unidirectional, one of the new strands is synthesized continuously in the direction of fork movement. This strand is designated as the leading strand. The other strand grows in the direction away from fork movement, and is called the lagging strand. Several specific interactions among the various proteins involved in DNA replication underlie the mechanism of DNA synthesis, on both the leading and lagging strands, at a DNA replication fork. These interactions allow the replication enzymes to cooperate in the replication process (Hurwitz et al 1990; Brush et al 1996; Ayyagari et al 1995; Budd & Campbell 1997; Bambara et al 1997).
The key event that allows the processive synthesis on the lagging strand, is polymerase switching from pol alpha to pol delta, as on the leading strand. However, the processive synthesis on the lagging strand proceeds very differently. DNA synthesis is discontinuous, and involves the formation of short fragments called the Okazaki fragments. During the synthesis of Okazaki fragments, the RNA primer is folded into a single-stranded flap, which is removed by endonucleases. This is followed by the ligation of adjacent Okazaki fragments.
Removal of the flap by FEN-1 leads to the generation of a nick between the 3'-end of the upstream Okazaki fragment and the 5'-end of the downstream Okazaki fragment. DNA ligase I then seals the nicks between adjacent processed Okazaki fragments to generate intact double-stranded DNA.
The processive complex is responsible for synthesizing at least 5-10 kb of DNA in a continuous manner during leading strand synthesis. The incorporation of nucleotides by pol delta is quite accurate. However, incorporation of an incorrect nucleotide does occur occasionally. Misincorporated nucleotides are removed by the 3' to 5' exonucleolytic proofreading capability of pol delta.
Transport to the Golgi and subsequent modification
Functional characterization of novel human and mouse equilibrative nucleoside transporters (hENT3 and mENT3) located in intracellular membranes
After the Cyclin D serves the role of mediating reactions by Cdk4 and Cdk6, it is shuttled to the cytoplasm and degraded in a ubiquitin-dependent manner. Whether Cdk4 and Cdk6 are truly redundant is a topic still under investigation, although both the kinases are required for normal cell cycle progression. Destruction of the D type cyclins accompanies the end of the G1 phase, and the E type cyclins are involved in transition of the cell from G1 to S phase.
Acetyltransferases ESCO1 and ESCO2 are homologs of the S. cerevisiae acetyltransferase Eco1, essential for viability in yeast. ESCO1 and ESCO2 share sequence homology in the C-terminal region, consisting of a H2C2 zinc finger motif and an acetyltransferase domain (Hou and Zou 2005). Both ESCO1 and ESCO2 acetylate the cohesin subunit SMC3 on two lysine residues, K105 and K106 (Zhang et al. 2008), an important step in the establishment of sister-chromatid cohesion during the S-phase of the cell cycle. These dual acetylations on SMC3 are deacetylated by HDAC8 after the cohesin removal from chromatin for the dissociation and recycling of cohesin subunits (Deardorff et al. 2012). ESCO1 and ESCO2 differ in their N-termini, which are necessary for chromatin binding, and may perform distinct functions in sister chromatid cohesion (Hou and Zou 2005), as suggested by the study of Esco2 knockout mice (Whelan et al. 2012).
Cyclin D turnover is regulated by ubiquitination and proteasomal degradation which are positively regulated by cyclin D phosphorylation on threonine-286 (Diehl et al., 1997).
DNA replication is regulated at various levels via ORC proteins. This pathway includes annotation of individual events that lead to the regulation of replication.
Licensing factors are removed from the origin by various means like biochemical modification (phosphorylation) or by physical association with other proteins. This pathway includes the annotations of events in which the fates of different proteins at the origin are outlined.
Myt1, which localizes preferentially to the endoplasmic reticulum and Golgi complex, phosphorylates Cdc2 on threonine 14 ( Liu et al., 1997).
Cyclin A is synthesized and associates with Cdc2 in G1. Cyclin dependent kinases are themselves catalytically inactive due to the fact that their active sites are blocked by a portion of the CDK molecule itself. Binding to their corresponding cyclin partner results in a conformational change that partially exposes the active site.
The cohesin complex loads onto chromatin in telophase, but its association with chromatin remains transient, dynamic until the S-phase of the cell cycle, presumably because the cohesin-bound NIPBL:MAU2 (SCC2:SCC4) complex promotes chromatin loading, while cohesin-bound WAPAL promotes dissociation from chromatin. Stable binding of cohesin complexes to chromatin, measured by a mean residence time on chromatin, is triggered by DNA replication in S-phase (Gerlich et al. 2006), consistent with establishment of sister chromatid cohesion. In S-phase, acetyltransferases ESCO1 and ESCO2 acetylate the SMC3 cohesin subunit (Hou and Zou 2005, Zhang et al. 2008, Nishiyama et al. 2010, Whelan et al. 2012). The acetylation of SMC3, in addition to DNA replication and the presence of PDS5 on cohesin, facilitates the recruitment of CDCA5 (Sororin) to cohesin complexes, an essential step in the establishment of sister chromatid cohesion in mammalian cells (Rankin et al. 2005, Nishiyama et al. 2010). CDCA5 (Sororin) displaces WAPAL from PDS5, thus preventing WAPAL to interfere with the establishment of sister chromatid cohesion (Nishiyama et al. 2010). The establishment and temporal regulation of sister chromatid cohesion is necessary for equal segregation of replicated chromosomes to daughter cells.
Acetyltransferases ESCO1 and ESCO2 are homologs of the S. cerevisiae acetyltransferase Eco1, essential for viability in yeast. ESCO1 and ESCO2 share sequence homology in the C-terminal region, consisting of a H2C2 zinc finger motif and an acetyltransferase domain (Hou and Zou 2005). Both ESCO1 and ESCO2 acetylate the cohesin subunit SMC3 on two lysine residues, K105 and K106 (Zhang et al. 2008), an important step in the establishment of sister-chromatid cohesion during the S-phase of the cell cycle. Divergent N-termini of ESCO1 and ESCO2, necessary for chromatin binding, suggest that ESCO1 and ESCO2 may perform distinct functions in sister chromatid cohesion (Hou and Zou 2005). Several studies suggest that ESCO2 may be predominantly involved in acetylation of the SMC3 subunit of centromeric cohesin. A conditional targeting of Esco2 locus in mice leads to pre-implantational loss of homozygous Esco2 -/- embryos at the eight-cell stage. Prometaphase chromosomes isolated from two-cell stage Esco2 knockout embryos show marked cohesion defect at centromeres (Whelan et al. 2012). ESCO2 protein appears in the S-phase (Hou and Zou 2005, Whelan et al. 2012) and in mouse embryonic fibroblasts Esco2 predominantly localizes to pericentric heterochromatin (Whelan et al. 2012). Mutations in the ESCO2 gene (Vega et al. 2005) that impair ESCO2 acetyltransferase activity (Gordillo et al. 2008) are the cause of the Roberts syndrome, an autosomal recessive disorder characterized by craniofacial and limb abnormalities, and intellectual disability. Metaphase chromosomes of Roberts syndrome patients exhibit loss of cohesion at heterochromatic regions of centromeres and the Y chromosome, with a characteristic 'railroad track appearance' (Van den Berg and Francke 1993, Vega et al. 2005).
The eukaryotic six-subunit origin recognition complex (ORC) governs the initiation site of DNA replication and formation of the prereplication complex.
DNA synthesis occurs in the S phase, or the synthesis phase, of the cell cycle. The cell duplicates its hereditary material, and two copies of the chromosome are formed. As DNA replication continues, the E type cyclins shared by the G1 and S phases, are destroyed and the levels of the mitotic cyclins rise.
Characterization of the mechanisms controlling Greatwall activity
Cloning of the human MCCA and MCCB genes and mutations therein reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency.
The generation and the manipulation of human multipotent adipose-derived stem cells
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Mutations in PMM2, a phosphomannomutase gene on chromosome 16p13, in carbohydrate-deficient glycoprotein type I syndrome (Jaeken syndrome)
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.
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.
cdc25A protein is degraded by the ubiquitin-proteasome machinery in both terminally differentiating and cycling cells (Bernardi et al. 2000).
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.
Wee1, a nuclear kinase, phosphorylates cyclin B1:Cdc2 on tyrosine 15 inactivating the complex.
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.
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).
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.
Structure, function, and formation of biological iron-sulfur clusters
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'.
Detection of DNA damage caused by ionizing radiation results in the phosphorylation of Cdc25A at Ser-123 by Chk2.
Like Cyclin A, NIMA-related kinase 2A (Nek2A) is degraded during pro-metaphase in a checkpoint-independent manner.
Ionizing radiation results in an ATM-dependent movement of COP1 from the nucleus to the cytoplasm (Dornan et al., 2006).
ATM phosphorylation promotes autoubiquitination of COP1 in vitro (Dornan et al., 2006). The number of ubiquitin molecules shown in this reaction is set arbitrarily at 4.
Autoubiquitinated COP1 is degraded by the proteasome. The number of ubiquitin molecules shown in this reaction is arbitrarily set at 4. (Dornan et al., 2006).
COP1 is one of several E3 ubiquitin ligases responsible for the tight regulation of p53 abundance. Following DNA damage, COP1 dissociates from p53 and is inactivated by autodegradation via a pathway involving ATM phosphorylation of COP1 on Ser(387), autoubiquitination and proteasome mediated degradation. Destruction of COP1 results in abrogation of the ubiquitination and degradation of p53 (Dornan et al., 2006).
Later studies pin-pointed that a single serine (Ser-15) was phosphorylated by ATM and phosphorylation of Ser-15 was rapidly-induced in IR-treated cells and this response was ATM-dependent (Canman et al, 1998; Banin et al, 1998 and Khanna et al, 1998). ATM also regulates the phosphorylation of p53 at other sites, especially Ser-20, by activating other serine/threonine kinases in response to IR (Chehab et al, 2000; Shieh et al, 2000; Hirao et al 2000). Phosphorylation of p53 at Ser-20 interferes with p53-MDM2 interaction. MDM2 is transcriptionally activated by p53 and is a negative regulator of p53 that targets it for degradation (Haupt et al, 1997; Kubbutat et al, 1997). In addition modification of MDM2 by ATM also affects p53 stabilization (Maya et al, 2001).
Most of the damage-induced modifications of p53 are dependent on the ATM kinase. The first link between ATM and p53 was predicted based on the earlier studies that showed that AT cells exhibit a reduced and delayed induction of p53 following exposure to IR (Kastan et al, 1992 and Khanna and Lavin, 1993). Under normal conditions, p53 is a short-lived protein. The MDM2 protein, usually interacts with p53 (Haupt et al, 1997 and Kubbutat et al, 1997), and by virtue of its E3 ubiquitin ligase activity, shuttles p53 to the cytoplasm and mediates its degradation by the ubiquitin-proteasome machinery. Upon detection of DNA damage, the ATM kinase mediates the phosphorylation of the Mdm2 protein to block its interaction with p53. Also, phosphorylation of p53 at multiple loci, by the ATM kinase and by other kinases activated by the ATM kinase, stabilizes and activates the p53 protein. The p53 protein activates the transcription of cyclin-dependent kinase inhibitor, p21. p21 inactivates the CyclinE:Cdk2 complexes, and prevent entry of the cell into S phase, leading to G1 arrest. Under severe conditions, the cell may undergo apoptosis.
The arrest at G1/S checkpoint is mediated by the action of a widely known tumor suppressor protein, p53. Loss of p53 functions, as a result of mutations in cancer prevent the G1/S checkpoint (Kuerbitz et al, 1992). P53 is rapidly induced in response to damaged DNA. A number of kinases, phosphatases, histone acetylases and ubiquitin-conjugating enzymes regulate the stability as well as transcriptional activity of p53 after DNA damage.
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).
Molecular physiology of bestrophins: multifunctional membrane proteins linked to best disease and other retinopathies
Regulation of actin assembly associated with protrusion and adhesion in cell migration
Nek2A is degraded by the 26S proteasome following ubiquitylation by the E3 ubiquitin ligase APC/C: Cdc20.
Human mucopolysaccharidosis IIID: clinical, biochemical, morphological and immunohistochemical characteristics
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'.
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'.
Wee1 phosphorylates Cdk2, inhibiting entry into S-phase (Watanabe et al., 1995; Wu et al., 2001).
Follow their formation, the Cyclin E:Cdk2 complexes are translocated to the nucleus.
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.
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.
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.
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.
Upon release from the kinetochore, Mad2 associates with Cdc20, hBUBR1, and hBUB3 to form the Mitotic Checkpoint Complex (MCC). Assembly of this complex does not depend on kinetochores but this complex can only inhibit APC/C that has undergone mitotic modifications.
In the direct inhibition model, the cytosolic Mitotic Checkpoint Complex, consisting of hBUBR1, hBUB3, Cdc20 and Mad2, directly inhibits APC/C by binding to it.
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 signal from unattached kinetochores is amplified through a Mad2 inhibitory signal that is propagated by the binding of Mad1 to the kinetochore, the association of Mad2 with Mad1, the conversion of Mad2 conformation to an inhibitory form through its association with Mad1 and finally the release of the inhibitory form of Mad2 from the kinetochore.
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.
Mad2 is recruited to the kinetochore through an interaction with Mad1.
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).
Binding of yeast frataxin to the scaffold for Fe-S cluster biogenesis, Isu
The mechanism by which the conformationally altered inhibitory form of Mad2 is released from its association with Mad1 at the kinetochore is not known. Mad1 and Cdc20 have a common 10 residue Mad2 binding motif. Therefore, one possibility is that Mad2 is transferred competitively from Mad1 to Cdc20 (Luo et al., 2002; Sironi et al., 2002).
In vitro structural studies have shown that Mad2 undergoes a major conformational change upon binding to Mad1. This conformational change is postulated to activate Mad2 into a high affinity state which can bind and sequester Cdc20 from the APC.
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.
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.
At the beginning of this reaction, 1 molecule of 'DNA polymerase alpha:primase:DNA polymerase alpha:origin complex', and 1 molecule of 'NTP' are present. At the end of this reaction, 1 molecule of 'DNA polymerase epsilon', and 1 molecule of 'RNA primer:origin duplex:DNA polymerase alpha:primase complex' are present. This reaction takes place in the 'nucleus' and is mediated by the 'DNA-directed RNA polymerase activity' of 'DNA polymerase alpha:primase'.
Cyclin A:Cdk2 plays a key role in S phase entry by phosphorylation of proteins including Cdh1, Rb, p21 and p27. During G1 phase of the cell cycle, cyclin A is synthesized and associates with Cdk2. After forming in the cytoplasm, the Cyclin A:Cdk2 complexes are translocated to the nucleus (Jackman et al.,2002). Prior to S phase entry, the activity of Cyclin A:Cdk2 complexes is negatively regulated through Tyr 15 phosphorylation of Cdk2 (Gu et al., 1995) and also by the association of the cyclin kinase inhibitors (CKIs), p27 and p21. Phosphorylation of cyclin-dependent kinases (CDKs) by the CDK-activating kinase (CAK) is required for the activation of the CDK2 kinase activity (Aprelikova et al., 1995). The entry into S phase is promoted by the removal of inhibitory Tyr 15 phosphates from the Cdk2 subunit of Cyclin A:Cdk2 complex by the Cdc25 phosphatases (Blomberg and Hoffmann, 1999) and by SCF(Skp2)-mediated degradation of p27/p21 (see Ganoth et al., 2001). While Cdk2 is thought to play a primary role in regulating entry into S phase, recent evidence indicates that Cdk1 is equally capable of promoting entry into S phase and the initiation of DNA replication (see Bashir and Pagano, 2005). Thus, Cdk1 complexes may also play a significant role at this point in the cell cycle.
Active Cyclin A:Cdk2 complexes phosphorylate and inactivate proteins required for maintaining the G1/S phase including: Cdh1, RB1, p21 and p27. All this creates auto-amplification loops that render Cdk2 increasingly more active. In G2, Cdk2, in association with cyclin A, phosphorylates E2F1 and E2F3 resulting in the inactivation and possibly degradation of these two transcription factors (Dynlacht et al., 1994; Krek et al., 1994).
Cdc25A, and probably Cdc25B, regulate the entry into S phase cell cycle by removing inhibitory phosphates from the Cdk2 subunit of Cyclin A:Cdk2.
Progression through G1 and G1 to S-phase transition that initiates DNA synthesis involve many complexes that are regulated by RB1:E2F pathway. RB1:E2F pathway plays a key role in gene expression regulation in proliferating and differentiated cells. As a repressor, E2F remains bound to RB1; it can activate the expression of S-phase genes involved in DNA replication after the phosphorylation of RB1. E2F proteins regulate expression of genes involved in various processes thereby forming interlinks between cell cycle, DNA synthesis, DNA damage recognition etc. In this module, activation of replication related genes by E2F1 and two ways by which E2F1 regulates DNA replication initiation are annotated. Detailed connection between the E2F protein function and various pathways will be covered in future releases of Reactome.
Cyclin E - Cdk2 complexes control the transition from G1 into S-phase. In this case, the binding of p21Cip1/Waf1 or p27kip1 is inhibitory. Important substrates for Cyclin E - Cdk2 complexes include proteins involved in the initiation of DNA replication. The two Cyclin E proteins are subjected to ubiquitin-dependent proteolysis, under the control of an E3 ubiquitin ligase known as the SCF. Cyclin A - Cdk2 complexes, which are also regulated by p21Cip1/Waf1 and p27kip1, are likely to be important for continued DNA synthesis, and progression into G2. An additional level of control of Cdk2 is reversible phosphorylation of Threonine-14 (T14) and Tyrosine-15 (Y15), catalyzed by the Wee1 and Myt1 kinases, and dephosphorylation by the three Cdc25 phosphatases, Cdc25A, B and C.
After forming in the cytoplasm, the Cyclin A:Cdk2 complexes are translocated to the nucleus.
The CDK activity of the Cyclin A:Cdk2 complex is inhibited by phosphorylation at Tyr 15, presumably by the Wee1 kinase.
Nature and frequency of mutations in the alpha-galactosidase A gene that cause Fabry disease
During G1 phase of the cell cycle, cyclin A is synthesized and associates with Cdk2.
Transaldolase deficiency: liver cirrhosis associated with a new inborn error in the pentose phosphate pathway.
At the beginning of this reaction, 1 molecule of 'RNA primer-DNA primer:origin duplex' is present. At the end of this reaction, 1 molecule of 'DNA polymerase alpha:primase', and 1 molecule of 'RNA primer-DNA primer:origin duplex with DNA damage' are present. This reaction takes place in the 'nucleus'.
This event is inferred from the fission yeast. Cyclin B activity is thought to inhibit pre-RC formation by first associating with ORC during DNA replication.
Complete amino acid sequence of human phosphoglycerate kinase. Cyanogen bromide peptides and complete amino acid sequence.
At the end of this reaction, 1 molecule of 'Cyclin B:Cdk1 complex', and 1 molecule of 'Cdc25A' are present. This reaction takes place in the 'nucleus'.
Under specific conditions, Cyclin B, a mitotic cyclin, can inhibit the functions of pre-replicative complex. E2F1 activates Cdc25A protein which regulates Cyclin B in a positive manner. Cyclin B/Cdk1 function is restored which leads to the disruption of pre-replicative complex. This phenomenon has been demonstrated by Bosco et al (2001) in Drosophila.
The Myc/Max heterodimer binds to elements in the cdc25A gene and activates transcription in mid to late G1.
Two new proteases in the MHC class I processing pathway
Cdc25A dephosphorylates Cdk2 and activates cyclin E-Cdk2 and cyclin A-Cdk2 kinases (Blomberg and Hoffmann, 1999).
Evaluating the role of carbonic anhydrases in the transport of HCO3--related species
The stem-loop binding protein is required for efficient translation of histone mRNA in vivo and in vitro
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
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.
The E2F family of transcription factors regulate the transition from the G1 to the S phase in the cell cycle. E2F activity is regulated by members of the retinoblastoma protein (pRb) family, resulting in the tight control of the expression of E2F-responsive genes. Phosphorylation of pRb by cyclin D:CDK complexes releases pRb from E2F, inducing E2F-targeted genes such as cyclin E.
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Cloning of a novel phosphatidylinositol kinase-related kinase: characterization of the human SMG-1 RNA surveillance protein
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Isolation and characterization of a hydroxyacid-oxoacid transhydrogenase from rat kidney mitochondria
Differential hydrolysis of phospholipid molecular species during activation of human platelets with thrombin and collagen
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Participation of the microsomal CDP-diglycerides in the mitochondrial biosynthesis of phosphatidylglycerol
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Ectopic expression of Cdc25A accelerates the G(1)/S transition and leads to premature activation of cyclin E- and cyclin A-dependent kinases
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DNA polymerase switching: II. Replication factor C abrogates primer synthesis by DNA polymerase alpha at a critical length.
DNA polymerase switching: I. Replication factor C displaces DNA polymerase alpha prior to PCNA loading.
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The dynamic phagosomal proteome and the contribution of the endoplasmic reticulum
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The energy-less red blood cell is lost: erythrocyte enzyme abnormalities of glycolysis
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DARPP-32: an integrator of neurotransmission
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Cdc6 is regulated by E2F and is essential for DNA replication in mammalian cells.
The anaphase-promoting complex: it's not just for mitosis any more.
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Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT
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The circadian E-box: when perfect is not good enough
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4-(2-aminophenyl)-2,4-dioxobutanoic acid
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.
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A double-hexamer archaeal minichromosome maintenance protein is an ATP-dependent DNA helicase.
Conjugation of phenylacetate with glutamine
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Molecular cloning of PEPT 2, a new member of the H+/peptide cotransporter family, from human kidney
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B-cell antigen receptor stimulation activates the human Bruton's tyrosine kinase, which is deficient in X-linked agammaglobulinemia
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Regulation of phagocytosis by Rho GTPases
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Cytochrome P450s and other enzymes in drug metabolism and toxicity
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The subcellular localization of acetyl-CoA carboxylase 2
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Human 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/inosine 5'-monophosphate cyclohydrolase. A bifunctional protein requiring dimerization for transformylase activity but not for cyclohydrolase activity
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Phosphatidylethanolamine is the donor of the phosphorylethanolamine linked to the alpha1,4-linked mannose of yeast GPI structures
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Carbon dioxide transport and carbonic anhydrase in blood and muscle
Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa gene
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2-Hydroxy-1,2,3-propanetricarboxylic acid
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Base-free sugar-phosphate removal via the single-nucleotide replacement pathway
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Characterization of the advanced glycation end-product receptor complex in human vascular endothelial cells
Barttin activates ClC-K channel function by modulating gating
Lysine uptake by cloned hCAT-2B: comparison with hCAT-1 and with trophoblast surface membranes
Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities
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]
(Gal)1 (GalNAc)1 (Glc)1 (Neu5Ac)1 (Cer)1
phosphatidylinositol 1,3,4,5-tetrakisphosphate
1D-myo-inositol 3,4,5,6-tetrakisphosphate
myo-inositol 1,3,4,5,6-pentakisphosphate
G-strand Chromosome end with two additional single strand repeats - Telomeric
NNNNNNNNNNNTTAGGGTTATTAGGGTTATTAGGGTTA - 3' (in human)
Human amidophosphoribosyltransferase. An oxygen-sensitive iron-sulfur protein
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The molecular mechanism of lead inhibition of human porphobilinogen synthase
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Fibroblast growth factor receptor 1 is fused to FIM in stem-cell myeloproliferative disorder with t(8;13)
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)
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Recruitment and regulation of phosphatidylinositol phosphate kinase type 1 gamma by the FERM domain of talin
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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_79425.9
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nicotinic acid adenine dinucleotide phosphate
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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_134222.5
Mitochondrial targeting signals and mature peptides of 3-methylcrotonyl-CoA carboxylase
guanosine 5'-(3-(alpha-D-mannopyranosyl) dihydrogen diphosphate)
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_139833.5
Database identifier. Use 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
The H syndrome is caused by mutations in the nucleoside transporter hENT3
Reactome stable identifier. Use this 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=3650202
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26455.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650176
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650178
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_135392.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652316
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_99671.9
Mechanistic implications of mutations to the active site lysine of porphobilinogen synthase
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648814
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648813
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648817
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648815
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=948008
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_29855.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=948029
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26043.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648812
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647771
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647772
Plk1 promotes nuclear translocation of human Cdc25C during prophase
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=139836
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2541.1
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_154784.3
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_157225.3
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=3647773
N-glycosylase/DNA lyase (Includes: 8-oxoguanine DNA glycosylase (EC 3.2.2.-); DNA-(apurinic or apyrimidinic site) lyase (EC 4.2.99.18) (AP lyase))
DNA-(apurinic or apyrimidinic site) lyase
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641717
Endonuclease III-like protein 1 (EC 4.2.99.18)
Guanine nucleotide-binding protein G(i), alpha-2 subunit
Adenylate cyclase-inhibiting G alpha protein
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641751
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641630
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647775
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641726
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_159701.3
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=3641713
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_153228.3
Gamma-aminobutyric acid type B receptor subunit 1
Guanine nucleotide-binding protein G(k), alpha subunit
ATP hydrolysis on actin-related protein 2/3 complex causes debranching of dendritic actin arrays
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647198
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647200
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_153432.3
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=428819
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19505.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428802
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651725
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_154538.3
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=3651726
26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_157067.3
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=3647197
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647194
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647195
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647192
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647193
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647190
AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes.
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647191
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647188
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647189
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20174.1
Database identifier. Use 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_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=429148
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19915.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=429056
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19945.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=429078
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19454.1
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_158610.3
Phospho(S221,S363,S380,T573)- ribosomal S6 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=3641412
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641426
Endothelium-derived relaxing and contracting factors
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641375
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641367
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651994
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_110587.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651927
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641400
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_95177.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651926
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651989
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_35721.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643625
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_158555.3
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=3643623
Gamma-aminobutyric acid type B receptor subunit 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=3641339
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641442
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641347
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641418
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643622
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=189246
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2878.2
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=3641438
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=188995
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_9838.3
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=3648021
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=70115
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_95616.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_9840.2
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_98298.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=189219
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648023
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4078.3
cDNA cloning and mapping of a novel subtype of glutamine:fructose-6-phosphate amidotransferase (GFAT2) in human and mouse
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_91098.9
A novel single missense mutation identified along the RH50 gene in a composite heterozygous Rhnull blood donor of the regulator 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=3646427
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3646428
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652134
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644315
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641430
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641327
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641450
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641335
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640233
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643681
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640232
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643679
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640230
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640226
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640222
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640218
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640216
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641331
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_158058.3
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=3643645
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643646
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2883.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643674
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643675
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643647
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_9596.3
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_34351.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640242
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641731
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640244
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641660
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640243
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641343
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641759
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641651
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643635
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640250
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643643
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640249
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=164121
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640261
Resolution of AP sites via the single-nucleotide replacement pathway
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643644
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640259
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640246
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641592
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640245
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640248
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640247
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_107871.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643669
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643670
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The conserved kinetochore protein shugoshin protects centromeric cohesion during meiosis
Guanine nucleotide exchange factors for Rho GTPases: turning on the switch
Innate immune recognition of an AT-rich stem-loop DNA motif in the Plasmodium falciparum genome
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A quantitative model of human DNA base excision repair. I. Mechanistic insights
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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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Enhanced tyrosine phosphorylation in B lymphocytes upon complexing of membrane immunoglobulin
Endogenous retroviral sequence is fused to FGFR1 kinase in the 8p12 stem-cell myeloproliferative disorder with t(8;19)(p12;q13.3)
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Probable phospholipid-transporting ATPases
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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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Transformation of prostaglandin D2 to 9 alpha, 11 beta-(15S)-trihydroxyprosta-(5Z,13E)-dien-1-oic acid (9 alpha, 11 beta-prostaglandin F2): a unique biologically active prostaglandin produced enzymatically in vivo in humans
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Probable phospholipid-transporting ATPase IA
Regulation of nuclear processes by inositol polyphosphates
Two pore calcium channel proteins 1 and 2
Toward a molecular explanation for cross-presentation of antigens to the immune system
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Substrate specificity combined with stereopromiscuity in glutathione transferase A4-4-dependent metabolism of 4-hydroxynonenal
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Succinate-semialdehyde dehydrogenase, mitochondrial
KARAP/DAP12/TYROBP: three names and a multiplicity of biological functions
Phospho(S363,S380,T573)- ribosomal S6 kinase
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4-aminobutyrate aminotransferase, mitochondrial
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The processivity of multiubiquitination by the APC determines the order of substrate degradation
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Human taste cells express the G protein alpha-gustducin and neuron-specific enolase
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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
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Cloning and characterization of murine 1-acyl-sn-glycerol 3-phosphate acyltransferases and their regulation by PPARalpha in murine heart
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Molecular cloning and characterization of an aquaporin cDNA from salivary, lacrimal, and respiratory tissues
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Formation of a preinitiation complex by S-phase cyclin CDK-dependent loading of Cdc45p onto chromatin.
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In situ visualization of DNA double-strand break repair in human fibroblasts.
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Comparative mechanistic and substrate specificity study of inositol polyphosphate 5-phosphatase Schizosaccharomyces pombe Synaptojanin and SHIP2
Activator 1 36 kDa subunit (Replication factor C 36 kDa subunit) (A1 36 kDa subunit) (RF-C 36 kDa subunit) (RFC36)
Platelet-collagen interaction: is GPVI the central receptor?
Liver glucose transporter: a basolateral protein in hepatocytes and intestine and kidney cells
Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activating kinase
The role of flavin-containing monooxygenases in drug metabolism and development
Transcriptional control of megakaryocyte development
NGF signalling via TRKA from the plasma membrane
Small is beautiful: insulin-like growth factors and their role in growth, development, and cancer
Cholesterol homeostasis in human brain: turnover of 24S-hydroxycholesterol and evidence for a cerebral origin of most of this oxysterol in the circulation
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
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
DNA synthesis at individual replication forks requires the essential initiation factor Cdc45p.
In vivo expression and functional characterization of the zinc transporter ZnT8 in glucose-induced insulin secretion
Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase
Isozymes of human phosphofructokinase: identification and subunit structural characterization of a new system
STING mediated induction of host immune responses
Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms
Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3 beta-hydroxysterol delta 14-reductase deficiency due to mutations in the lamin B receptor gene
Isoforms of mammalian adenylyl cyclase: multiplicities of signaling
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).
Once both coatomer and the active form of Arf1 have been recruited to the Golgi membrane surface, ArfGAP joins the complex.
The hydrolysis of Arf1-bound GTP is induced by the recruited ArfGAP.
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.
Once loaded the vesicles become fully sculpted, pinch off from the ER and bud into the cytosol.
COPII components (known as Sec13p, Sec23p, Sec24p, Sec31p, and Sar1p in yeast) traffic cargo from the endoplasmic reticulum to the Golgi apparatus. COPII-coated vesicles were originally discovered in the yeast Saccharomyces cerevisiae using genetic approaches coupled with a cell-free assay. The mammalian counterpart of this pathway is represented here. Newly synthesized proteins destined for secretion are sorted into COPII-coated vesicles at specialized regions of the ER. These vesicles leave the ER, become uncoated and subsequently fuse with the Golgi apparatus membrane.
Secretory cargo destined to be secreted or to arrive at the plasma membrane (PM) leaves the ER via distinct exit sites. This cargo is destined for the Golgi apparatus.
The formation of the COPI coat requires membrane recruitment and activation of Arf1. Arf1 activation is normally mediated by guanine nucleotide exchange factors (GEFs) that convert Arf1 to its active GTP-bound state on the membrane. In this reaction that GEF is represented by GBF1.
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.
Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria.
Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1.
The platelet P2 receptors in arterial thrombosis
Synthesis of PIPs at the early endosome membrane
The nucleotide transporter MRP4 (ABCC4) is highly expressed in human platelets and present in dense granules, indicating a role in mediator storage
Expression and function of the human androgen-responsive gene ADI1 in prostate cancer
Nonsense-mediated mRNA decay in human cells: mechanistic insights, functions beyond quality control and the double-life of NMD factors
Slo3, a novel pH-sensitive K+ channel from mammalian spermatocytes
Homologous DNA pairing and strand exchange
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An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides
The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues
Protein kinase B is regulated in platelets by the collagen receptor glycoprotein VI
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Activation of purified human protein kinase C alpha and beta I isoenzymes in vitro by Ca2+, phosphatidylinositol and phosphatidylinositol 4,5-bisphosphate
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Myotubularin and MTMR2, phosphatidylinositol 3-phosphatases mutated in myotubular myopathy and type 4B Charcot-Marie-Tooth disease
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
The molecular genetic basis of muscle phosphoglycerate mutase (PGAM) deficiency
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Mucopolysaccharidosis type IVA (Morquio A disease): clinical review and current treatment
The protein kinase/endoribonuclease IRE1alpha that signals the unfolded protein response has a luminal N-terminal ligand-independent dimerization domain
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The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo
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IAP proteins: blocking the road to death's door
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Human ITPK1: a reversible inositol phosphate kinase/phosphatase that links receptor-dependent phospholipase C to Ca2+-activated chloride channels
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Conversion of palmitic acid to very long chain fatty acyl-CoAs
Synthesis of very long-chain fatty acyl-CoAs
Cloning of a putative human voltage-gated chloride channel (CIC-2) cDNA widely expressed in human tissues
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The identification of a distinct export step following the biosynthesis of leukotriene C4 by human eosinophils
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Serum levels of beta 2-microglobulin as a new form of amyloid protein in patients undergoing long-term hemodialysis
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Cellular functions of TC10, a Rho family GTPase: regulation of morphology, signal transduction and cell growth
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Regulation of purine synthesis de novo in human fibroblasts by purine nucleotides and phosphoribosylpyrophosphate
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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_117795.1
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Proximal tubular handling of phosphate: A molecular perspective
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Forearm blood flow during body temperature transients produced by leg exercise.
Respiratory electron transport, ATP synthesis by chemiosmotic coupling, and heat production by uncoupling proteins.
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Isolation and characterization of human and mouse ZIRTL, a member of the IRT1 family of transporters, mapping within the epidermal differentiation complex
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M-phase inducer phosphatase 1 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25A)
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Intact AQP0 performs cell-to-cell adhesion
Serine/threonine-protein kinase Chk2 (EC 2.7.1.-) (Cds1)
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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_116327.1
APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
Interfacial kinetic and binding properties of mammalian group IVB phospholipase A2 (cPLA2beta) and comparison with the other cPLA2 isoforms
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The SLC31 (Ctr) copper transporter family
Wee1-like protein kinase (EC 2.7.1.112) (WEE1hu)
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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_28923.10
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Identification and characterization of a sphingolipid delta 4-desaturase family
A unified model for apical caspase activation
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RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways
Subunit interactions in the mammalian alpha-ketoglutarate dehydrogenase complex. Evidence for direct association of the alpha-ketoglutarate dehydrogenase and dihydrolipoamide dehydrogenase components.
Characterization of human D-amino acid oxidase
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Mitotic spindle assembly checkpoint protein MAD2A (MAD2-like 1) (HsMAD2)
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Activation of phospholipase C-gamma by phosphatidylinositol 3,4,5-trisphosphate
DNA-dependent protein kinase catalytic subunit
DNA repair protein RAD51 homolog 1 (hRAD51) (HsRAD51)
ATP-dependent DNA helicase II, 70 kDa subunit
ATP-dependent DNA helicase II, 80 kDa subunit
Double-strand break repair protein MRE11A
6-O- methylguanine-DNA methyltransferase
Methylated-DNA--protein-cysteine methyltransferase
The subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and nonphosphorylated monomers
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
Excision repair protein ERCC-6 (Cockayne syndrome protein CSB)
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
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
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)
Loss of ETHE1, a mitochondrial dioxygenase, causes fatal sulfide toxicity in ethylmalonic encephalopathy
Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein
Aldehyde dehydrogenase, a diphosphopyridine nucleotide-linked enzyme
Identification of a putative lysosomal cobalamin exporter altered in the cblF defect of vitamin B12 metabolism
Mitotic spindle assembly checkpoint protein MAD2B
Mitotic spindle assembly checkpoint protein MAD2B (MAD2-like 2) (hREV7)
Expression of Human CTP synthetase in Saccharomyces cerevisiae reveals phosphorylation by protein kinase A
Methylated-DNA--protein-cysteine methyltransferase (EC 2.1.1.63) (6-O- methylguanine-DNA methyltransferase)
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Ammonium homeostasis and human Rhesus glycoproteins
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mannose (a1-2) mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI
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(ethanolamineP) mannose (a1-2) (ethanolamineP) mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI
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ATP-binding cassette (ABC) transporters in human metabolism and diseases
Human Sulfotransferases and Their Role in Chemical Metabolism
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Peroxisome proliferator-activated receptor alpha target genes
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Pig-n, a mammalian homologue of yeast Mcd4p, is involved in transferring phosphoethanolamine to the first mannose of the glycosylphosphatidylinositol
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Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis
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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 1,3,4,5,6-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).
Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein
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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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Inositol-tetrakisphosphate 1-kinase (ITPK1) dephosphorylates inositol 1,3,4,5,6-pentakisphosphate (I(1,3,4,5,6)P5) to inositol 3,4,5,6-tetrakisphosphate (I(3,4,5,6)P4) (Ho et al. 2002).
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Inositoltetrakisphosphate 1-kinase (ITPK1) phosphorylates inositol 3,4,5,6-tetrakisphosphate (I(3,4,5,6)P4) to inositol 1,3,4,5,6-pentakisphosphate (I(1,3,4,5,6)P5) (Yang & Shears 2000).
A heterodimeric coiled-coil protein required for mitotic chromosome condensation in vitro
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).
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).
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).
In the endoplasmic reticulum (ER) lumen, multiple inositol polyphosphate phosphatase 1 (MINPP1) dephosphorylates inositol 1,3,4,5-tetrakisphosphate (I(1,3,4,5)P4) to inositol 1,4,5-trisphosphate (I(1,4,5)P3) (Caffrey et al. 1999, Chi et al. 1999).
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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).
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Inositol-3-phosphate synthase 1 (ISYNA1) aka hIPS isomerises glucose 6-phosphate (Glc6P) to inositol 3-phosphate (I3P) (Ju et al. 2004).
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).
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).
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In the endoplasmic reticulum (ER) lumen, multiple inositol polyphosphate phosphatase 1 (MINPP1) dephosphorylates 1,2,3,4,5,6-hexakisphosphate (IP6) to inositol 1,2,4,5,6-pentakisphosphate (I(1,2,4,5,6)P5) (Caffrey et al. 1999, Chi et al. 1999, Deleu et al. 2006, Nogimori et al. 1991).
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In the endoplasmic reticulum (ER) lumen, inositol phosphates IP4, IP5, and IP6 are dephosphorylated by multiple inositol polyphosphate phosphatase 1 (MINPP1) (Caffrey et al. 1999, Chi et al. 1999, Deleu et al. 2006, Nogimori et al. 1991).
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In the endoplasmic reticulum (ER) lumen, multiple inositol polyphosphate phosphatase 1 (MINPP1) dephosphorylates inositol 1,3,4,5,6-pentakisphosphate (I(1,3,4,5,6)P5) to inositol 1,4,5,6-tetrakisphosphate (I(1,4,5,6)P4) (Caffrey et al. 1999, Chi et al. 1999).
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).
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).
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Two conserved sequence blocks within eukaryotic tRNA genes are major promoter elements
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Identification and characterization of a novel monoamine transporter in the human brain
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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).
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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).
Rat monoacylglycerol lipase (MGLL) catalyzes the hydrolysis of 2-acylglycerol to yield glycerol + fatty acid (Tornqvist and Belfrage 1976; Fredrikson et al. 1986). Localization of the enzyme to lipid particles is plausible, given its low solubility and its involvement in acylglycerol metabolism, but this localization has not been directly experimentally verified. 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.
SLC25A1, in the inner mitochondrial membrane, mediates the exchange of mitochondrial citrate for cytosolic malate.
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.
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.
Molecular basis of acid sphingomyelinase deficiency in a patient with Niemann-Pick disease type A
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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
Subcellular localization and lysophospholipase/transacylation activities of human group IVC phospholipase A2 (cPLA2gamma)
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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).
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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).
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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.
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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).
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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).
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).
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).
Competitive binding of AUF1 and TIAR to MYC mRNA controls its translation
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.
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.
Biosynthesis of diphosphopyridine nucleotide. II. Enzymatic aspects.
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).
The E3 ubiquitin ligase WWP1 selectively targets HER4 and its proteolytically derived signaling isoforms for degradation
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'.
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 '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'.
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 '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'.
Characterization of distinct nuclear and mitochondrial forms of human deoxyuridine triphosphate nucleotidohydrolase
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.
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).
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.
1-Hydroxypropane-1,2,3-tricarboxylic acid
The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase
The noncatalytic portion of human UDP-glucose: glycoprotein glucosyltransferase I confers UDP-glucose binding and transferase function to the catalytic domain
Methylmalonyl-CoA mutase (MUT aka MCM) (Jansen et al. 1989) utilises adenosylcobalamin (AdoCbl) as a cofactor and transfers an adenosyl group from AdoCbl to methylmalonyl-CoA to form succinyl-CoA, a precursor for the citric acid cycle. MUT has a homodimeric structure and is located in the mitochondrial matrix. Defects in MUT cause methylmalonic aciduria, mut type (MMAM; MIM:251000), an often fatal disorder of organic acid metabolism (Worgan et al. 2006). Methylmalonic aciduria type A protein (MMAA) is thought to act as a chaperone to MUT, the enzyme which utilises adenosylcobalamin (AdoCbl) as a cofactor. MMAA is suggested to play a dual role with regards to MUT protection and reactivation. Some AdoCbl-dependent enzymes undergo suicide inactivation after catalysis due to the oxidative inactivation of Cbl. MMAA is thought to play a protective role to prevent MUT being inactivated in this way. After the catalytic cycle when MUT is inactive, MMAA increases the enzymatic activity of MUT through exchange of the damaged cofactor. Whether this happens via GTP-mediated hydrolysis is unknown at present (Takahashi-Iniguez et al. 2011, Froese et al. 2010). Bacterial AdoCbl-containing enzymes possess reactivating factors which release the inactivated cofactor to allow the resulting apoenzyme to reconstitute into an active form. A bacterial orthologue of MMAA, MeaB, forms a stable complex with MUT and plays a role in its protection and reactivation (Padovani & Banerjee 2006). Defects in MMAA cause methylmalonic aciduria type cblA (cblA aka methylmalonic aciduria type A or vitamin B12-responsive methylmalonicaciduria of cblA complementation type; MIM:251100). Affected individuals accumulate methylmalonic acid in the blood and urine and are prone to potentially life threatening acidotic crises in infancy or early childhood (Dobson et al. 2002, Lerner-Ellis et al. 2004).
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.
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.
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'.
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).
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 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 '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 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.
Ubiquitin-dependent mechanism regulates rapid turnover of AU-rich cytokine mRNAs
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).
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).
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.
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).
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).
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).
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).
MicroRNAs: small RNAs with a big role in gene regulation
The PEX11A 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.
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 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).
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.
The ABCA1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The ACSL1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
The ANKRD1 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.
Post-translational palmitoylation and glycosylation of Wnt-5a are necessary for its signalling
The FHL2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
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).
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 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).
Identification of a specific telomere terminal transferase activity in Tetrahymena extracts
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).
25(S) 3alpha,7alpha-dihydroxy-5beta-cholest-24-enoyl-CoA
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).
(24R, 25R) 3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA
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).
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).
(24R, 25R) 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA
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).
The peroxisomal membrane transport protein PMP34 mediates the exchange of adenine nucleotides between the cytosol and the peroxisomal matrix. The localization of PMP34 has been established by immunofluoresence studies (Wylin et al. 1998). The cloned human protein restores adenine nucleotide transport in yeast whose endogenous peroxisomal transporter has been disrupted, and has adenine nucleotide transport activity in reconstituted lipid vesicles in vitro (Visser et al. 2002), consistent with its hypothesized role in vivo (Wanders and Waterham 2006).
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.
Chromosomal replication initiates and terminates at random sequences but at regular intervals in the ribosomal DNA of Xenopus early embryos.
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).
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).
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).
Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylase
Synthesis of serotonin by a second tryptophan hydroxylase isoform
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).
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 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).
5beta-cholesten-7alpha, 12alpha-diol-3-one
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).
PC and PE synthesis: mixed micellar analysis of the cholinephosphotransferase and ethanolaminephosphotransferase activities of human choline/ethanolamine phosphotransferase 1 (CEPT1)
The nucleotide sequence of porcine formiminotransferase cyclodeaminase. Expression and purification from Escherichia coli.
A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay
Direct observation of single kinesin molecules moving along microtubules
Posttranscriptional gene regulation by spatial rearrangement of the 3' untranslated region
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
Molecular cloning of the human UMP synthase gene and characterization of point mutations in two hereditary orotic aciduria families
Disruption of aquaporin-11 produces polycystic kidneys following vacuolization of the proximal tubule
Essential role for Gab2 in the allergic response
Translocation of PKC theta to plasma membrane
Translocation of PDK1 to Plasma membrane
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Structural basis of the suppressed catalytic activity of wild-type human glutathione transferase T1-1 compared to its W234R mutant
Activation of Protein Kinase C beta (PKC-beta)
Activation of RasGRP1 and RasGRP3 by Recruitment to the Membrane and Phosphorylation
Activation of RAS by RasGRP1 and RasGRP3
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14-3-3 Binds Phosphorylated AS160 (TBC1D4)
Myeloproliferative disorder FOP-FGFR1 fusion kinase recruits phosphoinositide-3 kinase and phospholipase Cgamma at the centrosome
Vamp2 associated secretory vesicle to plasma membrane transport
Vamp7 associated Lysosome to Plasma membrane transport
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CARMA1 coiled-coil domain is involved in the oligomerization and subcellular localization of CARMA1 and is required for T cell receptor-induced NF-kappaB activation
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Translocation of GLUT4 Vesicle and Docking at the Plasma Membrane
Fusion of GLUT4 Vesicle with the Plasma Membrane
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Congenital disorder of glycosylation id presenting with hyperinsulinemic hypoglycemia and islet cell hyperplasia
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Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia
beta-Hydroxy-beta-methylglutaryl coenzyme A
FCP1, a phosphatase specific for the heptapeptide repeat of the largest subunit of RNA polymerase II, stimulates transcription elongation.
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The human glutathione transferase alpha locus: genomic organization of the gene cluster and functional characterization of the genetic polymorphism in the hGSTA1 promoter
Role of aquaporin-7 and aquaporin-9 in glycerol metabolism; involvement in obesity
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The human phosphatidylinositol phosphatase SAC1 interacts with the coatomer I complex
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5'-AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase-2C alpha and native bovine protein phosphatase-2AC
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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_158267.3
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Discovery of the aquaporins and development of the field
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The ontogeny of human drug-metabolizing enzymes: phase II conjugation enzymes and regulatory mechanisms
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Tyrosine kinase inhibitors of FGFR1 fusion mutants
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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_128471.5
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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=3649152
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_147507.5
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Type beta transforming growth factor in human platelets: release during platelet degranulation and action on vascular smooth muscle 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_133361.5
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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_111723.1
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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_142296.5
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Horror autoinflammaticus: the molecular pathophysiology of autoinflammatory disease (*)
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Completion of mammalian lagging strand DNA replication using purified 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=3649194
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649193
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649192
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649191
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_111741.1
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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_111816.1
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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_145617.5
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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_126900.5
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Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET)
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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=3649202
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_127752.5
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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=3650154
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650155
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Microsomal enzymes of cholesterol biosynthesis from lanosterol. Solubilization and purification of steroid 8-isomerase.
Promoter clearance by RNA polymerase II is an extended, multistep process strongly affected by sequence.
Localization of phosphatidylinositol phosphate kinase IIgamma in kidney to a membrane trafficking compartment within specialized cells of the nephron
mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI
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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_95376.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_155565.3
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_156362.3
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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=3650096
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649020
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benzo[a]pyrene diol epoxide I [ChEBI:30614]
(+/-)-Benzo(a)pyrene-7,8-diol-9,10-epoxide, anti-
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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 pyrophosphate decarboxylase (MPD) decarboxylates mevalonate-5-pyrophosphate into isopentenyl pyrophosphate while hydrolysing ATP to ADP and orthophosphate.
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Mevalonate kinase (MK) catalyzes the phosphorylation of mevalonate to mevalonate-5-phosphate.
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.
Farnesyl diphosphate farnesyltransferase (FDFT; squalene synthase) catalyzes the reductive dimerization of two farnesyl diphosphate (FPP) molecules to form squalene. This happens in two distinct steps. The first step of dimerization forms presqualene diphosphate (Pandit et al. 2000).
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)
Squalene monooxygenase (squalene epoxidase, SE) is located on the endoplamic reticulum. It catalyzes the oxidation of squalene to squalene 2,3-epoxide. SE seems to be an important rate-limiting enzyme in cholesterol biosynthesis.
In the second step, FDFT catalyzes the reduction of presqualene diphosphate to squalene (Pandit et al. 2000).
Lanosterol synthase (LS) catalyzes the cyclization of squalene 2,3-epoxide to lanosterol, a reaction that forms the sterol nucleus.LS is located on the ER membrane and is active as the monomer (Ruf et al, 2004).
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Phase 1 - Functionalization of compounds
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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
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol and NADPH + H+ react to form 4,4-dimethylcholesta-8(9),24-dien-3beta-ol and NADP+, catalyzed by LBR in the nuclear envelope. LBR protein spans the inner nuclear envelope, has an aminoterminal region with properties of a laminin receptor and a carboxyterminal domain with sequence similarity to sterol delta14-reductases (Holmer et al. 1998). Studies of material from an individual with HEM/Greenberg skeletal dysplasia indicate that LBR catalyzes the sterol delta14-reductase step of cholesterol biosynthesis in vivo. DNA sequencing revealed homozygosity for a mutant LBR allele encoding a truncated protein in the affected individual, and cells from the individual accumulated cholesta-8,14-dien-3beta-ol in culture. Transfection of wild-type LBR into the cultured cells reversed the accumulation of cholesta-8,14-dien-3beta-ol (Waterham et al. 2003). This observation is surprising because a second gene, TM7SF2, encodes an efficient sterol delta14-reductase that is localized to the endoplasmic reticulum whose expression is up-regulated in response to sterol depletion (Bennati et al. 2006). The physiological roles of LBR and TM7SF2 in vivo remain to be determined.
Lanosterol, NADPH + H+, and O2 react to form 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, NADP+, H2O and formate. This oxidative demethylation reaction, in the endoplasmic reticulum, is catalyzed by lanosterol 14alpha-demethylase (CYP51A1). Although the reaction is annotated here as a single concerted event, studies with purified rat enzyme indicate that the methyl group is converted successively to an alcohol and an aldehyde before being released as formate (Trzaskos et al. 1986; Fischer et al. 1991; Gaylor 2002).
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).
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4-methyl,4-carboxycholesta-8(9),24-dien-3beta-ol and NAD+ react to form 4-methylcholesta-8(9),24-dien-3-one, CO2, and NADH + H+. This reaction occurs in the endoplasmic reticulum, catalyzed by NSDHL (Caldas and Herman 2003). Defects in this enzyme are associated with CHILD syndrome (Congenital Hemidysplasia with Ichthyosiform nevus and Limb Defects) (Konig et al. 2000), but cholesterol biosynthesis in cells and tissues from affected individuals has not been characterized. Instead, the mechanism and stoichiometry of the reaction are inferred from biochemical studies of partially purified rat enzyme (Rahimtula and Gaylor 1972).
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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).
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4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol and NADPH + H+ react to form 4,4-dimethylcholesta-8(9),24-dien-3beta-ol and NADP+, catalyzed by TM7SF2 in the endoplasmic reticulum. TM7SF2 protein has sterol delta14-reductase activity in vitro, and expression of the gene is induced by sterol starvation in human cells, as expected for a gene involved in sterol biosynthesis (Bennati et al. 2006). However, molecular studies of material from an individual with HEM/Greenberg skeletal dysplasia indicate that LBR, a protein that spans the inner nuclear membrane and has both laminin receptor and sterol delta14-reductase activities, is required for normal sterol 14delta-reductase activity in human cells. It remains to be determined whether both LBR and TM7SF2 catalyze this reaction in vivo, and whether the role of TM7SF2 is essential (Waterham et al. 2003).
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).
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).
Isomerization of zymosterol to cholesta-7,24-dien-3beta-ol is catalyzed by EBP in the endoplasmic reticulum. The biochemical details of the reaction have been established through studies of purified rat EBP; the role of the human enzyme has been established through studies of patients deficient in it (Derry et al. 1999; Braverman et al. 1999).
4-carboxycholesta-8(9),24-dien-3beta-ol and NAD+ react to form zymosterone (cholesta-8(9),24-dien-3-one), CO2, and NADH + H+. This reaction occurs in the endoplasmic reticulum, catalyzed by NSDHL (Caldas and Herman 2003). Defects in this enzyme are associated with CHILD syndrome (Congenital Hemidysplasia with Ichthyosiform nevus and Limb Defects) (Konig et al. 2000), but cholesterol biosynthesis in cells and tissues from affceted individuals has not been characterized. Instead, the mechanism and stoichiometry of the reaction are inferred from biochemical studies of partially purified rat enzyme (Rahimtula and Gaylor 1972).
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Cloning and initial characterization of a new subunit for mammalian serine-palmitoyltransferase
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Control of the SCF(Skp2-Cks1) ubiquitin ligase by the APC/C(Cdh1) ubiquitin ligase
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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).
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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.
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.
Characterization of yeast methyl sterol oxidase (ERG25) and identification of a human homologue
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.
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).
Feedback regulation of EGFR signalling: decision making by early and delayed loops
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).
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, 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, monoglyceride lipase (MGLL) hydrolyzes 2-monoacylglycerol (2-MAG) to form a fatty acid and glycerol (Dinh et al. 2004, Zvonok et al. 2008, Bertrand et al. 2010, Labar et al. 2010).
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).
Phosphorylation of RasGRP3 on threonine 133 provides a mechanistic link between PKC and Ras signaling systems in B cells
Benzo(a)pyrene-7,8-diol-glutathione conjugate
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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).
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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).
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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).
Phospholipase Czeta causes Ca2+ oscillations and parthenogenetic activation of human oocytes
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.
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 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).
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).
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).
Effects of phosphorylation by CAK on cyclin binding by CDC2 and CDK2.
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).
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).
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(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.
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.
4-cholesten-7alpha,12alpha,24(S)-triol-3-one and NADPH + H+ react to form 5beta-cholesten-7alpha,12alpha,24(S)-triol-3-one and NADP+. This reaction is catalyzed by AKR1D1 (3-oxo-5-beta-steroid 4-dehydrogenase). AKR1D1 is localized to the cytosol, and in the course of the reaction its steroid substrate moves from the endoplasmic reticulum membrane to the cytosol. It is unclear whether this translocation results simply from its increased hydrophilicity or is mediated by the enzyme or another transport protein (Russell 2003).
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).
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.
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.
(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.
4-Cholesten-7alpha, 12alpha-diol-3-one and NADPH + H+ react to form 5beta-cholesten-7alpha,12alpha-diol-3-one + NADP+. This reaction is catalyzed by AKR1D1 (3-oxo-5-beta-steroid 4-dehydrogenase). AKR1D1 is localized to the cytosol, and in the course of the reaction its steroid substrate moves from the endoplasmic reticulum membrane to the cytosol. It is unclear whether this translocation results simply from its increased hydrophilicity or is mediated by the enzyme or another transport protein (Russell 2003).
4-Cholesten-7alpha-ol-3-one, NADPH, and H+ react to form 5beta-cholestan-7alpha-ol-3-one and NADP+. This reaction is catalyzed by AKR1D1 (3-oxo-5-beta-steroid 4-dehydrogenase). AKR1D1 is localized to the cytosol, and in the course of the reaction its steroid substrate moves from the endoplasmic reticulum membrane to the cytosol. It is unclear whether this translocation results simply from its increased hydrophilicity or is mediated by the enzyme or another transport protein (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).
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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.
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).
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).
Odontogenic ameloblast-associated protein nature of the amyloid found in calcifying epithelial odontogenic tumors and unerupted tooth follicles
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).
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4-Cholesten-7alpha,12alpha,27-triol-3-one and NADPH + H+ react to form 5beta-cholesten-7alpha,12alpha,27-triol-3-one + NADP+. This reaction is catalyzed by AKR1D1 (3-oxo-5-beta-steroid 4-dehydrogenase). AKR1D1 is localized to the cytosol, and in the course of the reaction its steroid substrate moves from the endoplasmic reticulum membrane to the cytosol. It is unclear whether this translocation results simply from its increased hydrophilicity or is mediated by the enzyme or another transport protein (Russell 2003).
4-Cholesten-7alpha,27-diol-3-one, NADPH, and H+ react to form 5beta-cholestan-7alpha,27-diol-3-one and NADP+. This reaction is catalyzed by AKR1D1 (3-oxo-5-beta-steroid 4-dehydrogenase). AKR1D1 is localized to the cytosol, and in the course of the reaction its steroid substrate moves from the endoplasmic reticulum membrane to the cytosol. It is unclear whether this translocation results simply from its increased hydrophilicity or is mediated by the enzyme or another transport protein (Russell 2003).
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).
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.
4-Cholesten-7alpha,24(S)-diol-3-one, NADPH, and H+ react to form 5beta-cholestan-7alpha,24(S)-diol-3-one and NADP+. This reaction is catalyzed by AKR1D1 (3-oxo-5-beta-steroid 4-dehydrogenase). AKR1D1 is localized to the cytosol, and in the course of the reaction its steroid substrate moves from the endoplasmic reticulum membrane to the cytosol. It is unclear whether this translocation results simply from its increased hydrophilicity or is mediated by the enzyme or another transport protein (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 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).
Identification of a novel amidase motif in neutral ceramidase
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 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).
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).
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).
A synopsis of the unconjugated acidic transamination metabolites of phenylalanine in phenylketonuria
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.
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 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, lysocardiolipin acyltransferase 1 (LCLAT1) aka ALCAT1 acylates monolysocardiolipin (MLCL) to cardiolipin (CL) (Cao et al. 2004, Zhao et al. 2009).
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).
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).
At the endoplasmic reticulum (ER) membrane, lysocardiolipin acyltransferase 1 (LCLAT1) aka ALCAT1 acylates dilysocardiolipin (DLCL) to produce monolysocardiolipin (MLCL) (Zhao et al. 2009).
cAMP induces dissociation of inactive PKA tetramers
PKA catalytic subunit translocates to the nucleus
Production of AA by iPLA2 upon FCGR activation
Translocation of CaN:CaM:NFAT to nucleus
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 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).
Vitronectin receptor-mediated phagocytosis of cells undergoing apoptosis
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), 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).
Cross-linking of B cell antigen receptor-related structure of pre-B cell lines induces tyrosine phosphorylation of p85 and p110 subunits and activation of phosphatidylinositol 3-kinase
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.
Switching of origins to a post-replicative state
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 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 (Carvou et al. 2010, Shadan et al. 2008).
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).
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At the endoplasmic reticulum (ER) membrane, phosphatidylethanolamine N-methyltransferase (PEMT) methylates phosphatidylethanolamine (PE) and produces phosphatidylcholine (PC) (Vance & Ridgway 1998, Shields et al. 2001, Guan et al. 1999).
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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).
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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).
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).
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).
CENP-E, a novel human centromere-associated protein required for progression from metaphase to anaphase
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.
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).
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).
Molecular cloning and expression of CYP2J2, a human cytochrome P450 arachidonic acid epoxygenase highly expressed in heart
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.
Regulation of protein kinase C zeta by PI 3-kinase and PDK-1
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Mutations in iron-sulfur cluster scaffold genes NFU1 and BOLA3 cause a fatal deficiency of multiple respiratory chain and 2-oxoacid dehydrogenase enzymes
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Platelet activation and atherothrombosis
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).
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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 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).
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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).
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Translocation of antigenic peptides back to phagosomes via TAP
Antigen processing by cathepsin S in endosoytic vesicle
Mechanism of aminoacylation of tRNA. Proof of the aminoacyl adenylate pathway for the isoleucyl- and tyrosyl-tRNA synthetases from Escherichia coli K12
Carbohydrate response element binding protein directly promotes lipogenic enzyme gene transcription
Activation of Rap1 by membrane-associated GEFs
Proteasomal clevage of exogenous antigen
The anaphase-promoting complex: proteolysis in mitosis and beyond
Interaction of particulate antigens with dendritic cell receptors
Egress of internalized antigen to the cytosol via sec61
Engulfment of particulate antigen into phagocytic vesicle
Trimming of N-ter extended precursor fragments by cytosolic aminopeptidases
Branching and elongation of mother and daughter filaments
Attachment of preexisting mother filament and initiation of branching
Molybdenum cofactor biosynthesis and deficiency
Active site remodelling accompanies thioester bond formation in the SUMO E1
Ran-independent nuclear import of cyclin B1-Cdc2 by importin beta
An electric lobe suppressor for a yeast choline transport mutation belongs to a new family of transporter-like proteins
RNA polymerase III transcribes microbial dsDNA to dsRNA
Activation of CDC42 by unknown mechanism
The enzymes and control of eukaryotic mRNA turnover
WAVE2 or WASP/N-WASP activate the ARP2/3 complex
Subcellular localization and targeting of N-acetylglucosaminyl phosphatidylinositol de-N-acetylase, the second enzyme in the glycosylphosphatidylinositol biosynthetic pathway
How MHC class II molecules acquire peptide cargo: biosynthesis and trafficking through the endocytic pathway
Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis
Oxidoreductases in lipoxin A4 metabolic inactivation: a novel role for 15-oxoprostaglandin 13-reductase/leukotriene B4 12-hydroxydehydrogenase in inflammation
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Factor VIII-related antigen in human blood platelets: localization and release by thrombin and collagen
Characterization of a second member of the subfamily of calcium-binding mitochondrial carriers expressed in human non-excitable tissues
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MTABC3, a novel mitochondrial ATP-binding cassette protein involved in iron homeostasis
Herp is dually regulated by both the endoplasmic reticulum stress-specific branch of the unfolded protein response and a branch that is shared with other cellular stress pathways
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Enzymes and reactions at the eukaryotic DNA replication fork.
A direct role for GRASP65 as a mitotically regulated Golgi stacking factor
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Mevalonate kinase is a cytosolic enzyme in humans
Characteristics of the interaction of a synthetic human tristetraprolin tandem zinc finger peptide with AU-rich element-containing RNA substrates
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Exportin 5 is a RanGTP-dependent dsRNA-binding protein that mediates nuclear export of pre-miRNAs
Expression of cAMP-regulated guanine nucleotide exchange factors in pancreatic beta-cells
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1,2-Dihydroxy-3-oxo-methylthiopentene (1-)
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Subcellular localization and properties of alkaline inorganic pyrophosphatase in human polymorphonuclear leucocytes
Identification of LAT4, a novel amino acid transporter with system L activity
Human cytosolic thymidine kinase. Purification and physical characterization of the enzyme from HeLa cells
Molecular physiology of cation-coupled Cl- cotransport: the SLC12 family
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Cloning, characterization, and modeling of mouse and human guanylate kinases
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Isolation and characterization of the faciogenital dysplasia (Aarskog-Scott syndrome) gene: a putative Rho/Rac guanine nucleotide exchange factor
Mutations in the catalytic subunit of class IA PI3K confer leukemogenic potential to hematopoietic cells
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Analysis of phosphoinositide binding domain properties within the myotubularin-related protein MTMR3
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The extended protein kinase C superfamily
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Trimethylaminuria: the fish-odour syndrome
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Localization of human equilibrative nucleoside transporters, hENT1 and hENT2, in renal epithelial cells
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Structure of a type II thymidine kinase with bound dTTP
Subcellular locations of phosphatidylinositol 4-kinase isoforms
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Old and new generation lipid mediators in acute inflammation and resolution
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A unique fold of phospholipase C-beta mediates dimerization and interaction with G alpha q
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Distribution of the AQP4 water channel in normal human tissues: protein and tissue microarrays reveal expression in several new anatomical locations, including the prostate gland and seminal vesicles
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Deleterious mutation in the mitochondrial arginyl-transfer RNA synthetase gene is associated with pontocerebellar hypoplasia
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Interaction of recombinant human eIF2 subunits with eIF2B and eIF2alpha kinases
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Formation of transcription-coupled NER (TC-NER) repair complex
ZNF198-FGFR1 transforms Ba/F3 cells to growth factor independence and results in high level tyrosine phosphorylation of STATS 1 and 5
Pyruvate metabolism and Citric Acid (TCA) cycle
Biosynthesis and metabolism of leukotrienes
STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity
Identification of a mammalian mitochondrial porphyrin transporter
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2-acyl-sn-glycero-3-phosphoserine [ChEBI:37646]
Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe/S cluster biosynthesis
Evidence for a family of human glucose transporter-like proteins. Sequence and gene localization of a protein expressed in fetal skeletal muscle and other tissues
The mechanism of phospholipase C-gamma1 regulation
Isolation and complete sequence of a functional human glyceraldehyde-3-phosphate dehydrogenase gene
Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis
Autodegradation of the E3 ubiquitin ligase COP1
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Transient receptor potential 1 regulates capacitative Ca(2+) entry and Ca(2+) release from endoplasmic reticulum in B lymphocytes
ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex.
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Phosphoinositide signalling in cancer: beyond PI3K and PTEN
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Neurotrophin signaling: many exciting surprises!
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Lipid digestion, mobilization, and transport
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Molecular cloning and characterization of a novel muscle adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal cells
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FGFR1 is fused to the centrosome-associated protein CEP110 in the 8p12 stem cell myeloproliferative disorder with t(8;9)(p12;q33)
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Metabolism, function and mass spectrometric analysis of bis(monoacylglycero)phosphate and cardiolipin
Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation
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RNA Pol II CTD phosphorylation and interaction with CE
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ATM engages autodegradation of the E3 ubiquitin ligase COP1 after DNA damage
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Thiamin uptake by the human-derived renal epithelial (HEK-293) cells: cellular and molecular mechanisms
Functional characterization of a human aquaporin 0 mutation that leads to a congenital dominant lens cataract
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Microsomal enzymes of cholesterol biosynthesis. Purification of lanosterol 14 alpha-methyl demethylase cytochrome P-450 from hepatic microsomes.
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A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line
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In vitro processing of the human alkyl-dihydroxyacetonephosphate synthase precursor
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Human liver type pyruvate kinase: complete amino acid sequence and the expression in mammalian cells
Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells
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Regulation of PAK-2p34 activity by PS-GAP/RHG10
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Antigenic analysis of the major human phosphoglucomutase isozymes: PGM1, PGM2, PGM3 and PGM4
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Predominant expression and activation-induced tyrosine phosphorylation of phospholipase C-gamma 2 in B lymphocytes
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The collagen receptor subfamily of the integrins
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ZnT7, a novel mammalian zinc transporter, accumulates zinc in the Golgi apparatus
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Purification of an inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase activity from rat liver and the evaluation of its substrate specificity
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U-box proteins as a new family of ubiquitin ligases
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The conjugation of phenylacetic acid in man, sub-human primates and some non-primate species
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Methionine regeneration and aspartate aminotransferase in parasitic protozoa
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Molecular interactions of Polo-like-kinase 1 with the mitotic kinesin-like protein CHO1/MKLP-1
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Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business.
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(S)-3-Hydroxyisobutyryl-CoA [ChEBI:28259]
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Identification of a target RNA motif for RNA-binding protein HuR
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Regulation of activated PAK-2p34 by proteasome mediated degradation
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Beta oxidation of butanoyl-CoA to acetyl-CoA
The major sites of cellular phospholipid synthesis and molecular determinants of Fatty Acid and lipid head group specificity
GAPs galore! A survey of putative Ras superfamily GTPase activating proteins in man and Drosophila
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The p24 family and selective transport processes at the ER-Golgi interface
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The role of the tethering proteins p115 and GM130 in transport through the Golgi apparatus in vivo
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Expression and purification of recombinant tristetraprolin that can bind to tumor necrosis factor-alpha mRNA and serve as a substrate for mitogen-activated protein kinases
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Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics
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Synapsis of DNA ends by DNA-dependent protein kinase.
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Regulation of Ca2+ signaling in mast cells by tyrosine-phosphorylated and unphosphorylated non-T cell activation linker
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Pathways of chaperone-mediated protein folding in the cytosol
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Molecular mechanisms of translational control
A role for 14-3-3 in insulin-stimulated GLUT4 translocation through its interaction with the RabGAP AS160
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The mucopolysaccharidoses: inborn errors of glycosaminoglycan catabolism
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Identification of separate acyl- CoA:glycine and acyl-CoA:L-glutamine N-acyltransferase activities in mitochondrial fractions from liver of rhesus monkey and man
Human adenine phosphoribosyltransferase. Affinity purification, subunit structure, amino acid composition, and peptide mapping.
Concerted dephosphorylation of the transcription factor NFAT1 induces a conformational switch that regulates transcriptional activity
Alpha transducin is present in blue-, green-, and red-sensitive cone photoreceptors in the human retina
Differential role of human choline kinase alpha and beta enzymes in lipid metabolism: implications in cancer onset and treatment
Dynamics of lipid transfer by phosphatidylinositol transfer proteins in cells
Thrombopoietin: a tool for understanding thrombopoiesis
Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency
Three-step model for condensin activation during mitotic chromosome condensation
Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1
Interaction of retinitis pigmentosa GTPase regulator (RPGR) with RAB8A GTPase: implications for cilia dysfunction and photoreceptor degeneration
Cloning, characterization, and chromosomal localization of a gene frequently deleted in human liver cancer (DLC-1) homologous to rat RhoGAP
Complete coding sequence, promoter region, and genomic structure of the human ABCA2 gene and evidence for sterol-dependent regulation in macrophages
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Cloning and characterization of a novel human alkaline ceramidase. A mammalian enzyme that hydrolyzes phytoceramide
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Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity
Cobalamin uptake and reactivation occurs through specific protein interactions in the methionine synthase-methionine synthase reductase complex
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Subcellular targeting and trafficking of nitric oxide synthases
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The human Myt1 kinase preferentially phosphorylates Cdc2 on threonine 14 and localizes to the endoplasmic reticulum and Golgi complex.
Lysosomal degradation of Asn-linked glycoproteins
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Crystal structure of human prostaglandin F synthase (AKR1C3)
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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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A missense mutation in SLC33A1, which encodes the acetyl-CoA transporter, causes autosomal-dominant spastic paraplegia (SPG42)
The role of GRASP55 in Golgi fragmentation and entry of cells into mitosis
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Induction of ceruloplasmin synthesis by IFN-gamma in human monocytic cells
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The multidrug transporter, a double-edged sword
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Phosphoinositide 3-kinase: the key switch mechanism in insulin signalling.
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A roller coaster ride with the mitotic cyclins
G(1) to S transition: more than a cell cycle engine switch.
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Functional and molecular characterization of the human neutral solute channel aquaporin-9
Unspecific permeation and specific exchange of adenine nucleotides in
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Genetic basis of mitochondrial HMG-CoA synthase deficiency
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Phagosomal maturation (early endosomal stage)
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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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Regulation of Ras in lymphocytes: get a GRP
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The quality control of MHC class I peptide loading
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Quantitative studies on the release of platelet fibrinogen by thrombin
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Negative regulation of condensin I by CK2-mediated phosphorylation
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Molecular cloning and functional characterization of a novel mammalian sphingosine kinase type 2 isoform
Molecular cloning and expression of a cDNA for human kidney cysteine conjugate beta-lyase
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Specificty of human and rat orthologs of the concentrative nucleoside transporter, SPNT
The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells
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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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Morquio A syndrome: cloning, sequence, and structure of the human N-acetylgalactosamine 6-sulfatase (GALNS) gene
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Identification of the gene encoding the enzyme deficient in mucopolysaccharidosis IIIC (Sanfilippo disease type C)
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Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency
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Transmembrane transport of small molecules
Coiled bodies contain U7 small nuclear RNA and associate with specific DNA sequences in interphase human cells.
Ded1p, a DEAD-box protein required for translation initiation in Saccharomyces cerevisiae, is an RNA helicase.
The concentrative nucleoside transporter family, SLC28
Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway
A stop-codon mutation in the BRI gene associated with familial British dementia
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ErbB-3 and ErbB-4 function as the respective low and high affinity receptors of all Neu differentiation factor/heregulin isoforms
Arteriosclerosis, Thrombosis, and Vascular Biology 28:e162
Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS
Common origin and evolution of glycosyltransferases using Dol-P-monosaccharides as donor substrate
Aquaporins: highways for cells to recycle water with the outside world
Analysis of nucleocytoplasmic shuttling of NF kappa B proteins in human leukocytes
The gene mutated in thiamine-responsive anaemia with diabetes and deafness (TRMA) encodes a functional thiamine transporter
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Mutations in SLC19A2 cause thiamine-responsive megaloblastic anaemia associated with diabetes mellitus and deafness
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Mutations in a new gene encoding a thiamine transporter cause thiamine-responsive megaloblastic anaemia syndrome
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Functional analysis of the purified anandamide-generating phospholipase D as a member of the metallo-beta-lactamase family
Topological and functional analysis of the human reduced folate carrier by hemagglutinin epitope insertion
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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
Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation
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PIG-W is critical for inositol acylation but not for flipping of glycosylphosphatidylinositol-anchor
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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_158523.3
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The chromosomal association of condensin II is regulated by a noncatalytic function of PP2A
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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=3645301
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642767
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645280
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645281
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_98260.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_166367.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645285
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645284
Mutations in the gene encoding 3 beta-hydroxysteroid-delta 8, delta 7-isomerase cause X-linked dominant Conradi-Hunermann syndrome
Mutations in a delta 8-delta 7 sterol isomerase in the tattered mouse and X-linked dominant chondrodysplasia punctata. jderry@immunex.com.
Signalling functions and biochemical properties of pertussis toxin-resistant G-proteins
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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_153062.3
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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_149284.4
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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_88130.9
Inactivation of the p34cdc2-cyclin B complex by the human WEE1 tyrosine kinase
Phagocytosis of retinal rod and cone photoreceptors
Diversification of Neu differentiation factor and epidermal growth factor signaling by combinatorial receptor interactions
Cytosolic sulfonation of small molecules
Tuberculosis - metabolism and respiration in the absence of growth
A microRNA polycistron as a potential human oncogene
Regulation of deoxyadenosine and nucleoside analog phosphorylation by human placental adenosine kinase
Steroidogenic electron transport in adrenal cortex mitochondria
Acyl-CoA:lysophospholipid acyltransferases
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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_94375.9
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Tyrosine-phosphorylated Vav1 as a point of integration for T-cell receptor- and CD28-mediated activation of JNK, p38, and interleukin-2 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=3647144
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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=3646770
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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=3647143
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647850
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_158917.3
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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=3647842
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3646765
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=450605
Reactome stable identifier. Use this 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
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_156814.3
Human multidrug-resistant cell lines: increased mdr1 expression can precede gene amplification
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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_26577.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428275
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3648054
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647160
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_131669.5
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26315.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647164
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647869
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647165
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_27075.1
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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_140771.5
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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_19518.1
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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=3647818
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647177
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647820
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_87370.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_153257.3
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=3647174
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652210
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647175
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_34251.10
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Cdc25A stability is controlled by the ubiquitin-proteasome pathway during cell cycle progression and terminal differentiation
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Newly made phosphatidylserine and phosphatidylethanolamine are preferentially translocated between rat liver mitochondria and 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_20195.2
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=428694
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647829
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652207
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647136
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_34662.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647137
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647789
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647138
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_154593.3
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=3647139
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647140
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647828
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647142
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647824
Cleavage of oxidized guanine nucleotide and ADP sugar by human NUDT5 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_82292.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647844
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647148
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647135
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647803
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_133479.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647805
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647804
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428671
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647801
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647800
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_85343.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647807
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647806
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_126272.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647808
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19836.2
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=3647187
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_83668.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428682
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_19431.2
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=3647169
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428203
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647810
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647809
A point mutation in the coding sequence of the beta-hexosaminidase alpha gene results in defective processing of the enzyme protein in an unusual GM2-gangliosidosis variant
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_26387.1
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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=428193
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_108743.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652209
Reactome stable identifier. Use this 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
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647817
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_158313.3
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=3647832
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647182
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647185
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_106609.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=428663
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20116.2
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=3649920
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647264
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_20726.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647268
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_112806.8
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647270
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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_96238.9
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Cyclin A:Cdk2-associated events at S phase entry
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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_117015.1
Employment of the epidermal growth factor receptor in growth factor-independent signaling pathways
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Glycogenin: the primer for mammalian and yeast glycogen 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_2442.2
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Genes for human catecholamine-synthesizing enzymes
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LRRFIP1, a new FGFR1 partner gene associated with 8p11 myeloproliferative syndrome
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The sodium/calcium exchanger family-SLC8
Genomic organization, tissue distribution and deletion mutation of human pyridoxine 5'-phosphate oxidase
Antimicrobial mechanisms of phagocytes and bacterial evasion strategies
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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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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=74016
3alpha,7alpha-Dihydroxy-5beta-cholestane [ChEBI:1708]
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A novel family of membrane-bound E3 ubiquitin ligases
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A minus-end-directed kinesin with plus-end tracking protein activity is involved in spindle morphogenesis
RhoGDIgamma: a GDP-dissociation inhibitor for Rho proteins with preferential expression in brain and pancreas
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P110delta, a novel phosphoinositide 3-kinase in leukocytes
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Human p55(CDC)/Cdc20 associates with cyclin A and is phosphorylated by the cyclin A-Cdk2 complex
Wnt and calcium signaling: beta-catenin-independent pathways
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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_85582.9
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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
Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components
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10-formyltetrahydrofolyl polyglutamate macromolecule [ChEBI:28010]
10-formyltetrahydrofolyl polyglutamate macromolecule
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Advanced glycation endproduct (AGE) receptor 1 is a negative regulator of the inflammatory response to AGE in mesangial 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_90201.9
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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=428198
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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_19924.3
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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_153177.3
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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_149863.4
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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_20039.1
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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_85471.9
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Roles of aquaporin-3 water channels in volume-regulatory water flow in a human epithelial cell line
Cyclin E associated events during G1/S transition
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Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein
Purification of, generation of monoclonal antibodies to, and mapping of phosphoribosyl N-formylglycinamide amidotransferase
The pleckstrin homology domain of phosphoinositide-specific phospholipase Cdelta4 is not a critical determinant of the membrane localization of the enzyme
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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_101524.9
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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_149837.4
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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_158448.3
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Characterization of human type I and type II IMP dehydrogenases
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Phosphorylation of cyclin D1 at Thr 286 during S phase leads to its proteasomal degradation and allows efficient DNA synthesis
Internal control regions for transcription of eukaryotic tRNA genes
C-terminal binding domain of Rho GDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases
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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=113572
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Cellular targets for activation by the E2F1 transcription factor include DNA synthesis- and G1/S-regulatory genes
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Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans
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The mitochondrial ABC transporter Atm1p functions as a homodimer
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Citrin and aralar1 are Ca(2+)-stimulated aspartate/glutamate transporters in mitochondria
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A mutational analysis of the yeast proliferating cell nuclear antigen indicates distinct roles in DNA replication and DNA repair.
DNA replication initiates at multiple sites on plasmid DNA in Xenopus egg extracts.
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Fibroblast growth factors and their receptors in cancer
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Human acid sphingomyelinase. Isolation, nucleotide sequence and expression of the full-length and alternatively spliced cDNAs
The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex
In vitro and in vivo enzymatic syntheses and mass spectrometric database for N-glycans and o-glycans
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LAB/NTAL/Lat2: a force to be reckoned with in all leukocytes?
Lysine acetylation targets protein complexes and co-regulates major cellular functions
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Sprinter: a novel transmembrane protein required for Wg secretion and signaling
Mucopolysaccharidosis type II (Hunter syndrome): a clinical review and recommendations for treatment in the era of enzyme replacement therapy
Multidrug resistance mediated by the breast cancer resistance protein BCRP (ABCG2)
Global gene expression profiling and histochemical analysis of the developing human fetal pancreas
Angiogenesis is regulated by a novel mechanism: pro- and antiangiogenic proteins are organized into separate platelet alpha granules and differentially released
Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution.
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Identification of a novel glucose transporter-like protein-GLUT-12
Am J Physiol Endocrinol Metab 282:E733-8
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Regulated expression of three C/EBP isoforms during adipose conversion of 3T3-L1 cells
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Bora and the kinase Aurora a cooperatively activate the kinase Plk1 and control mitotic entry
Glyceraldehyde-3-phosphate dehydrogenase from human tissues.
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The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response
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Purification of a plasma membrane-associated GTPase-activating protein specific for rap1/Krev-1 from HL60 cells
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Molecular cloning and characterization of PLC-eta2
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Sequencing and expression of a cDNA for human glutathione synthetase
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Carbohydrate responsive element-binding protein (ChREBP): a key regulator of glucose metabolism and fat storage
The unfolded protein response is an important regulator of inflammatory genes in endothelial cells
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5,10-methenyltetrahydrofolate polyglutamate [ChEBI:65049]
5,10-methenyltetrahydrofolate polyglutamate
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Mutational analysis of a patient with mucopolysaccharidosis type VII, and identification of pseudogenes
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miRNAs on the move: miRNA biogenesis and the RNAi machinery
Human MTH3 (NUDT18) Protein Hydrolyzes Oxidized Forms of Guanosine and Deoxyguanosine Diphosphates: COMPARISON WITH MTH1 AND MTH2
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Phytanic acid and pristanic acid are oxidized by sequential peroxisomal and mitochondrial reactions in cultured fibroblasts
Planar cell polarity signaling: from fly development to human disease
Interactions between the endoplasmic reticulum, mitochondria, plasma membrane and other subcellular organelles
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The oncogenic properties of mutant p110alpha and p110beta phosphatidylinositol 3-kinases in human mammary epithelial cells
Proc. Natl. Acad. Sci. U.S.A. 102:18443-8
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Pentose phosphate pathway (hexose monophosphate shunt)
Amino acid synthesis and interconversion (transamination)
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Focal adhesions - the cytoskeletal connection
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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
Mechanistic and mutational studies of Escherichia coli molybdopterin synthase clarify the final step of molybdopterin biosynthesis
Phosphatidylinositol-5-phosphate activation and conserved substrate specificity of the myotubularin phosphatidylinositol 3-phosphatases
N-retinylidene-phosphatidylethanolamine is the preferred retinoid substrate for the photoreceptor-specific ABC transporter ABCA4 (ABCR)
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Identification and characterization of PS-GAP as a novel regulator of caspase-activated PAK-2
Phospholipase D signaling: orchestration by PIP2 and small GTPases
Naunyn Schmiedebergs Arch Pharmacol 374:399-411
Cytochromes P450 with bisallylic hydroxylation activity on arachidonic and linoleic acids studied with human recombinant enzymes and with human and rat liver microsomes
Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is selectively eliminated from the nucleus at the onset of S phase.
E2F-enabled inhibition of pre-replication complex formation
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Potential role of protein kinase B in insulin-induced glucose transport, glycogen synthesis, and protein synthesis
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The molecular mechanisms that control thrombopoiesis
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Nucleotide-binding domain, leucine rich repeat containing receptor (NLR) signaling pathways
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Rap1GAP2 is a new GTPase-activating protein of Rap1 expressed in human platelets
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Multisite autophosphorylation of p21-activated protein kinase gamma-PAK as a function of activation
Calmodulin-binding sites on adenylyl cyclase type VIII
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Cellular circadian pacemaking and the role of cytosolic rhythms
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6-methoxy-3-methyl-2-decaprenyl-1,4-benzoquinol [ChEBI:64181]
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2-methoxy-6-decaprenyl-1,4-benzoquinol [ChEBI:64180]
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The yeast mitochondrial carrier Leu5p and its human homologue Graves' disease protein are required for accumulation of coenzyme A in the matrix
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Cloning and characterization of a nuclear S6 kinase, S6 kinase-related kinase (SRK); a novel nuclear target of Akt
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The E3 ubiquitin ligase TRIM21 negatively regulates the innate immune response to intracellular double-stranded DNA
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IP3 receptor/Ca2+ channel: from discovery to new signaling concepts
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Cloning and characterization of human guanine deaminase. Purification and partial amino acid sequence of the mouse 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=3642381
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645080
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640859
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_32393.10
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Biochemistry of Lipids, Lipoproteins and Membranes, 5th Edition (Book): 213-244
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Somatic mutations in p85alpha promote tumorigenesis through class IA PI3K activation
Retinal stimulates ATP hydrolysis by purified and reconstituted ABCR, the photoreceptor-specific ATP-binding cassette transporter responsible for Stargardt 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_91845.9
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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_95863.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640317
Cloning of the human equilibrative, nitrobenzylmercaptopurine riboside (NBMPR)-insensitive nucleoside transporter ei by functional expression in a transport-deficient cell line
Conversion of Phosphatidylcholine to Phosphatidylglycerol with Phospholipase D and glycerol
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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_159936.3
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Identification and characterization of a novel inositol polyphosphate 5-phosphatase
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_109995.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_115206.8
FANCI phosphorylation functions as a molecular switch to turn on the Fanconi anemia pathway
Apert syndrome results from localized mutations of FGFR2 and is allelic with Crouzon syndrome
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Architecture of the human origin recognition complex.
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NRAGE, a p75 neurotrophin receptor-interacting protein, induces caspase activation and cell death through a JNK-dependent mitochondrial pathway
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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_93867.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3646556
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_18000.2
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=389664
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=389680
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_17481.2
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=3646534
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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=3646537
Fibroblast growth factor signalling: from development to cancer
BLNK mediates Syk-dependent Btk activation
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_17198.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=389843
Reactome stable identifier. Use this 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
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_17634.1
Pyrimidine nucleotide biosynthesis in animals: genes, enzymes, and regulation of UMP biosynthesis.
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A three-dimensional working model of the multienzyme complex of aminoacyl-tRNA synthetases based on electron microscopic placements of tRNA and 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=3646553
TARS dimer (name copied from entity in Homo sapiens)
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WARS dimer (name copied from entity in Homo sapiens)
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YARS 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=3640368
DARS2 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=3644102
FARS A2B2 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=3645932
GARS 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=3645934
SARS 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=3645936
IRE1 homodimer (phosphorylated):ADP (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=3640369
IRE1 homodimer (phosphorylated) (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=3640382
CARS 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_91082.9
PERK Homodimer (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_104331.9
Subcellular localization and regulation of coenzyme A synthase
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5182.4
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_17366.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29406
Ran:GTP:Exportin-5 (name copied from entity in Homo sapiens)
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Proximal signaling events in Fc epsilon RI-mediated mast cell activation
J. Allergy Clin. Immunol. 119:544-52; quiz 553-4
Ran:GTP (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_82503.9
pre-miRNA:Ran:GTP:Exportin-5 (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=113528
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2373.1
Ran-GTP (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_84343.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_77562.9
YARS2 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_95061.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640347
SARS2 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=3652138
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640363
KARS 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=3646562
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3640346
Isolated isobutyryl-CoA dehydrogenase deficiency: an unrecognized defect in human valine metabolism.
(un)folded protein:(GlcNAc)2 (Man)9 (name copied from entity in Homo sapiens)
glucosidase II (name copied from entity in Homo sapiens)
unfolded protein:glycan (no glucose) (name copied from entity in Homo sapiens)
unfolded protein:(Glc)3 (GlcNAc)2 (Man)9 (Asn)1 (name copied from entity in Homo sapiens)
unfolded protein:(Glc)2 (GlcNAc)2 (Man)9 (Asn)1 (name copied from entity in Homo sapiens)
Transgenic mice as a model of pre-clinical Alzheimer's disease
unfolded protein:(Glc)1 (GlcNAc)2 (Man)9 (Asn)1 (name copied from entity in Homo sapiens)
unfolded protein:(Glc)1 (GlcNAc)2 (Man)9 (Asn)1:chaperone (name copied from entity in Homo sapiens)
CALR:CANX (name copied from entity in Homo sapiens)
Vitamins B6 activation to pyridoxal phosphate
unfolded protein:(Glc)1 (GlcNAc)2 (Man)9 (Asn)1:chaperone:ERp57 (name copied from entity in Homo sapiens)
The role of mast cells in allergic inflammation
unfolded protein:glycan:chaperone:ERp57 (name copied from entity in Homo sapiens)
unfolded protein:glycan (name copied from entity in Homo sapiens)
IRE1 homodimer (name copied from entity in Homo sapiens)
MAN2A2:Zn2+ (name copied from entity in Homo sapiens)
MAN2A1:Zn2+ (name copied from entity in Homo sapiens)
Biochemistry of mammalian peroxisomes revisited
Protein misfolding, functional amyloid, and human disease
unfolded protein:(GlcNAc)2 (Man)8a (name copied from entity in Homo sapiens)
unfolded protein:(GlcNAc)2 (Man)7aa (name copied from entity in Homo sapiens)
unfolded protein:(GlcNAc)2 (Man)8b (name copied from entity in Homo sapiens)
unfolded protein:(GlcNAc)2 (Man)8c (name copied from entity in Homo sapiens)
unfolded protein:(Glc)1 (GlcNAc)2 (Man)9 (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=3645519
Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation
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Role, metabolism, chemical modifications and applications of hyaluronan
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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_77199.9
Database identifier. Use 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_31391.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645523
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645521
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652096
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_128380.5
2xUAP1 (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=3645507
Members of the human glyceraldehyde-3-phosphate dehydrogenase-related gene family map to dispersed chromosomal locations.
bis-(3'-5')-cyclic dimeric guanosine monophosphate
guanylyl-(3'->5')-3'-guanylic acid, cyclic 3'->5'''-nucleotide
2xGNPNAT1 (name copied from entity in Homo sapiens)
2xUAP1-2 (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=3645518
PIG-F:PIG-O 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_17814.2
PIG-F:GPI7 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=209911
DPM1,2,3 (name copied from entity in Homo sapiens)
GPI-N-acetylglucosaminyltransferase (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_28288.10
deoxyhypusine synthase 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=3652093
DOHH:Fe++ (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_34595.10
cofactor A:GTP:beta-tubulin folding intermediate (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=3652092
Cofactor D:GTP:beta tubulin (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_146201.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647429
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647430
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647427
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647428
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647434
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_129676.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647431
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647432
mRNA quality control: an ancient machinery recognizes and degrades mRNAs with nonsense codons
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647426
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647425
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647394
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647396
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_78774.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652191
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_143437.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647420
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647424
Integrating mRNA processing with transcription.
Caenorhabditis elegans mboa-7, a member of the MBOAT family, is required for selective incorporation of polyunsaturated fatty acids into phosphatidylinositol
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_34194.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=29514
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_2669.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=432019
Human aquaporin adipose (AQPap) gene. Genomic structure, promoter analysis and functional mutation
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Roles of C-terminal processing, and involvement in transacylation reaction of human group IVC phospholipase A2 (cPLA2gamma)
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XBP1 induces WFS1 through an endoplasmic reticulum stress response element-like motif in SH-SY5Y cells
RNA Polymerase III Transcription Initiation From Type 2 Promoter
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Uninterrupted MCM2-7 function required for DNA replication fork progression.
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Src-family kinases in B-cell development and signaling
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Redox-switch modulation of human SSADH by dynamic catalytic loop
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Phosphoglucomutase 1: a gene with two promoters and a duplicated first exon
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2-Methylbutyryl-coenzyme A dehydrogenase deficiency: a new inborn error of L-isoleucine metabolism.
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Metabolism of propionic acid in animal tissues. VIII. Crystalline propionyl carboxylase
Purification of peroxisomal acyl-CoA: dihydroxyacetonephosphate acyltransferase from human placenta
Characterization of RasGRP2, a plasma membrane-targeted, dual specificity Ras/Rap exchange factor
A stable complex of a novel transcription factor IIB- related factor, human TFIIIB50, and associated proteins mediate selective transcription by RNA polymerase III of genes with upstream promoter elements
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SLC2A9 is a newly identified urate transporter influencing serum urate concentration, urate excretion and gout
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Molecular cloning of a human cDNA encoding a trifunctional enzyme of carbamoyl-phosphate synthetase-aspartate transcarbamoylase-dihydroorotase in de Novo pyrimidine synthesis
Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates
BLNK: a central linker protein in B cell activation
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Mutations in antiquitin in individuals with pyridoxine-dependent seizures
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DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs.
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3-decaprenyl-4-hydroxybenzoic acid [ChEBI:64136]
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Neuregulin-1 only induces trans-phosphorylation between ErbB receptor heterodimer partners
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The cytochrome P450 superfamily: biochemistry, evolution and drug metabolism in humans
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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Adipocyte differentiation from the inside out
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Alkyl-dihydroxyacetonephosphate synthase. Presence and role of flavin adenine dinucleotide
Triggering and augmentation mechanisms, granule pools, and biphasic insulin secretion
Molecular genetic defects in endometrial carcinomas: microsatellite instability, PTEN and beta-catenin (CTNNB1) genes mutations
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Proteolytic processing of pro-alpha and pro-beta precursors from human beta-hexosaminidase. Generation of the mature alpha and beta a beta b subunits
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Cloning, sequencing, and expression of cDNA for human beta-galactosidase
Biochem. Biophys. Res. Commun. 157:238-44
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G-protein-coupled receptors and islet function-implications for treatment of type 2 diabetes
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The role of the Rho GTPases in neuronal development
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Identification of holocarboxylase synthetase (HCS) proteins in human placenta
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The spectrum of latent tuberculosis: rethinking the biology and intervention strategies
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GPI7 is the second partner of PIG-F and involved in modification of glycosylphosphatidylinositol
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Identification and characterization of a novel human phosphatidylinositol 4-kinase
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The presence and release of alpha 2-antiplasmin from human platelets
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Deficiency of 3-methylglutaconyl-coenzyme A hydratase in two siblings with 3-methylglutaconic aciduria.
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Identification of Gz alpha as a pertussis toxin-insensitive G protein in human platelets and megakaryocytes
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Protein folding: versatility of the cytosolic chaperonin TRiC/CCT
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Devising a pathway for hyaluronan catabolism: are we there yet?
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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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Isolation and characterization of a full-length expressible cDNA for human hypoxanthine phosphoribosyl transferase
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New insights into mechanism and regulation of actin capping protein
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Somatic mutations of the protein kinase gene family in human lung cancer
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beta-D-GlcpA-(1->3)-D-GlcpNAc [ChEBI:64024]
The eicosanoids: cyclooxygenase, lipoxygenase, and epoxygenase pathways
Biochemistry of Lipids, Lipoproteins and Membranes, 5th Edition (Book): 331-362
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Regulation of Water Balance by Renal Aquaporins
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The role of phosphatidylinositol 3-kinase in neural cell adhesion molecule-mediated neuronal differentiation and survival
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Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells
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A role for transportin in deposition of TTP to cytoplasmic RNA granules and mRNA decay
Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis
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Aquaporin expression in normal human kidney and in renal disease
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A human homologue of the checkpoint kinase Cds1 directly inhibits Cdc25 phosphatase
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Rapid association of cytoskeletal remodeling proteins with the developing phagosomes of human neutrophils
Mucopolysaccharidosis type I: current knowledge on its pathophysiological mechanisms
Characterization of the human gene encoding alpha-aminoadipate aminotransferase (AADAT).
NLR functions beyond pathogen recognition
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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_78611.9
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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_85844.9
Identification of the non-lysosomal glucosylceramidase as beta-glucosidase 2
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Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver
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Peroxisome proliferator activated receptors and lipoprotein metabolism
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Four isoforms of tyrosine hydroxylase are expressed in human brain
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Human beta-galactosidase gene mutations in morquio B disease
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ATP activates a reactive oxygen species-dependent oxidative stress response and secretion of proinflammatory cytokines in macrophages
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Deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion
Regulation of Ins(3,4,5,6)P(4) signaling by a reversible kinase/phosphatase
Crystal structures of human NUDT5 reveal insights into the structural basis of the substrate specificity
The distribution and function of phosphatidylserine in cellular membranes
Structure and activation of the visual pigment rhodopsin
The PI-3 kinase/Akt pathway and T cell activation: pleiotropic pathways downstream of PIP3
Vav1: a key signal transducer downstream of the TCR
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RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway
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Phosphorylation of mammalian CDC6 by cyclin A/CDK2 regulates its subcellular localization.
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Regulation of Geminin and Cdt1 expression by E2F transcription factors
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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_4964.2
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_4218.2
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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_4733.3
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Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1
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Inhibition of Mcm4,6,7 helicase activity by phosphorylation with cyclin A/Cdk2.
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Binding of MET-TRNAf and GTP to homogeneous initiation factor MP.
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Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane
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Immunoreceptor DAP12 bearing a tyrosine-based activation motif is involved in activating NK 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_31559.10
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5822.2
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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_3489.2
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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=189489
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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_29058.10
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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_95858.9
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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=189447
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_9774.2
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_9601.2
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Management of cellular energy by the AMP-activated protein kinase system
Mammalian G proteins and their cell type specific functions
Mapping the functional domains of the Golgi stacking factor GRASP65
Overexpression of a mammalian ethanolamine-specific kinase accelerates the CDP-ethanolamine pathway
Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase
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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=727787
Phagosomes are competent organelles for antigen cross-presentation
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Hyaluronidase and its substrate hyaluronan: biochemistry, biological activities and therapeutic uses
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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_23315.2
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ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells
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Requirement of TRPC channels in netrin-1-induced chemotropic turning of nerve growth cones
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(1R,2S)-1-Hydroxypropane-1,2,3-tricarboxylate [ChEBI:151]
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Control of translation and mRNA degradation by miRNAs and siRNAs
Condensins, chromosome condensation protein complexes containing XCAP-C, XCAP-E and a Xenopus homolog of the Drosophila Barren protein
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Human and murine glycerol kinase: influence of exon 18 alternative splicing on function
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Roberts syndrome is caused by mutations in ESCO2, a human homolog of yeast ECO1 that is essential for the establishment of sister chromatid cohesion
Reversible compartmentalization of de novo purine biosynthetic complexes in living cells
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Nuclear translocation of plk1 mediated by its bipartite nuclear localization signal
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Novel folding and stability defects cause a deficiency of human glutathione transferase omega 1
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Stimulation of the human CTP:phosphoethanolamine cytidylyltransferase gene by early growth response protein 1
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Association of TriC/CCT with target proteins during biosynthesis
NSDHL, an enzyme involved in cholesterol biosynthesis, traffics through the Golgi and accumulates on ER membranes and on the surface of lipid droplets
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SCF-beta-TrCP mediated degradation of Emi1
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Identification and characterization of novel spliced variants of neuregulin 4 in prostate cancer
Novel variants in human Aquaporin-4 reduce cellular water permeability
Human Bub1 defines the persistent cohesion site along the mitotic chromosome by affecting Shugoshin localization
Polymorphism in the intermediates and products of amyloid assembly
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A general map of iron metabolism and tissue-specific subnetworks
The Mad2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either Mad1 or Cdc20
Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1
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The gene for histone RNA hairpin binding protein is located on human chromosome 4 and encodes a novel type of RNA binding protein.
Kinesin-5 regulates the growth of the axon by acting as a brake on its microtubule array
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Phosphorylation and activation of 13S condensin by Cdc2 in vitro
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Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices
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Acid-sensing ion channels (ASICs): pharmacology and implication in pain
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[A NEW DYSOSTOSIS WITH URINARY ELIMINATION OF CHONDROITIN SULFATE B]
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The synthesis of inositol hexakisphosphate. Characterization of human inositol 1,3,4,5,6-pentakisphosphate 2-kinase
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A control region in the center of the 5S RNA gene directs specific initiation of transcription: II. The 3' border of the region.
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The isolation and characterisation of a platelet-specific beta-globulin (beta-thromboglobulin) and the detection of antiurokinase and antiplasmin released from thrombin-aggregated washed human platelets
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Inborn errors of ketogenesis and ketone body utilization
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Crystal structure of the tetrameric Mad1-Mad2 core complex: implications of a 'safety belt' binding mechanism for the spindle checkpoint
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Molecular cloning and expression of human hepatocyte growth factor
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Molecular organization of the presynaptic active zone
Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins
Low affinity Ca2+-binding sites of calcineurin B mediate conformational changes in calcineurin A
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Alternate exon insertion controls selective ubiquitination and degradation of different AUF1 protein isoforms
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XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
Cloning and characterization of human adenosine 5'-triphosphate-binding cassette, sub-family A, transporter 2 (ABCA2)
Enzymes of the human erythrocyte. IV. Phosphoglucose isomerase, purification and properties.
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A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol
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A role for Plk1 phosphorylation of NudC in cytokinesis
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Molecular cloning and expression of human bile acid beta-glucosidase
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Molecular machinations of the MHC-I peptide loading complex
The target of ezetimibe is Niemann-Pick C1-Like 1 (NPC1L1)
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Structural basis for the functional differences between type I and type II human methionine aminopeptidases
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Structure of PITPbeta in complex with phosphatidylcholine: comparison of structure and lipid transfer to other PITP isoforms
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Developmental origin of fat: tracking obesity to its source
Human cell growth requires a functional cytoplasmic exosome, which is involved in various mRNA decay pathways
Synthesis of bile acids and bile salts via 27-hydroxycholesterol
The human peroxisomal ABC half transporter ALDP functions as a homodimer and accepts acyl-CoA esters
Two human orthologues of Eco1/Ctf7 acetyltransferases are both required for proper sister-chromatid cohesion
Defective platelet activation in G alpha(q)-deficient mice
Peroxisomal multifunctional protein-2: the enzyme, the patients and the knockout mouse model
Characterization of the human fumarylacetoacetate hydrolase gene and identification of a missense mutation abolishing enzymatic activity.
COPI-coated ER-to-Golgi transport complexes segregate from COPII in close proximity to ER exit sites
The C-terminal nucleotide binding domain of the human retinal ABCR protein is an adenosine triphosphatase
Subcellular localization of human neutral ceramidase expressed in HEK293 cells
EGF receptor activation by GPCRs: an universal pathway reveals different versions
Biological & physiological aspects of action of insulin-like growth factor peptide family
Holocarboxylase synthetase: correlation of protein localisation with biological function
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Purification and characterization of a novel alpha-class glutathione transferase from human liver
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The transport of sulphate and sulphite in rat liver mitochondria
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Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity
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Platelet C1- inhibitor. A secreted alpha-granule protein.
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Isolation and characterization of human nuclear and cytosolic multisynthetase complexes and the intracellular distribution of p43/EMAPII
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Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization.
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Association of B cell antigen receptor with protein tyrosine kinase Lyn
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Kinetic characterization of human hydroxyacid-oxoacid transhydrogenase: relevance to D-2-hydroxyglutaric and gamma-hydroxybutyric acidurias
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A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells
The formation of citric and alpha-ketoglutaric acids in the mammalian body
The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation
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Human intestinal H+/peptide cotransporter. Cloning, functional expression, and chromosomal localization
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A control region in the center of the 5S RNA gene directs specific initiation of transcription: I. The 5' border of the region.
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Identification of the human methylmalonyl-CoA racemase gene based on the analysis of prokaryotic gene arrangements. Implications for decoding the human genome.
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Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members
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Ubiquinone. Biosynthesis of quinone ring and its isoprenoid side chain. Intracellular localization
HER4-mediated biological and biochemical properties in NIH 3T3 cells. Evidence for HER1-HER4 heterodimers
Decreased expression of cyclic adenosine monophosphate-regulated aldose reductase (AKR1B1) is associated with malignancy in human sporadic adrenocortical tumors
Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site
Identification of SLC39A4, a gene involved in acrodermatitis enteropathica
Adenylate kinases in man: evidence for a third locus
Core protein machinery for mammalian phosphatidylinositol 3,5-bisphosphate synthesis and turnover that regulates the progression of endosomal transport. Novel Sac phosphatase joins the ArPIKfyve-PIKfyve complex
ChEBI:27379 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA
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Cloning and identification of a new member of water channel (AQP10) as an aquaglyceroporin
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Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities
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4-Imidazolone-5-propanoate [ChEBI:27384]
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Inflammasome adaptors and sensors: intracellular regulators of infection and inflammation
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Metabolism of propionic acid in animal tissues. IX. Methylmalonyl coenzyme A racemase
Molecular cloning of human amidophosphoribosyltransferase
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ChEBI:27393 3alpha,7alpha-dihydroxy-5beta-cholest-24-enoyl-CoA
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Back in the water: the return of the inositol phosphates
PI3Kgamma is a key regulator of inflammatory responses and cardiovascular homeostasis
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Regulation of WASP/WAVE proteins: making a long story short
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Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies
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Purification and properties of human placental adenosine kinase
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Mutation in the 4a-carbinolamine dehydratase gene leads to mild hyperphenylalaninemia with defective cofactor metabolism.
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Nuclear organization of DNA replication in primary mammalian cells
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Structure-Function analysis of the CTLA-4 interaction with PP2A
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GlycoVis: visualizing glycan distribution in the protein N-glycosylation pathway in mammalian cells
Defective glucose transport across brain tissue barriers: a newly recognized neurological syndrome
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Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase
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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Expression and functional contribution of hTHTR-2 in thiamin absorption in human intestine
Am J Physiol Gastrointest Liver Physiol 286:G491-8
3alpha,7alpha,24-Trihydroxy-5beta-cholestanoyl-CoA [ChEBI:1701]
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Activation of type II adenylyl cyclase by the cloned mu-opioid receptor: coupling to multiple G proteins
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Sulfotransferase catalyzing sulfation of heterocyclic amines
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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_5376.2
Investigation of the ABC transporter MRP1 in selected patients with presumed defects in vitamin B12 absorption
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Codeposition of apolipoprotein A-IV and transthyretin in senile systemic (ATTR) amyloidosis
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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=3647382
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21130.2
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=437093
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_31177.10
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Red blood cell pH, the Bohr effect, and other oxygenation-linked phenomena in blood O2 and CO2 transport
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GTP hydrolysis by eRF3 facilitates stop codon decoding during eukaryotic translation termination
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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_20925.2
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Mutation of the fumarase gene in two siblings with progressive encephalopathy and fumarase deficiency
Characterization of human lysophospholipid acyltransferase 3
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Contraction regulates site-specific phosphorylation of TBC1D1 in skeletal muscle
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Presynaptic phase of homologous DNA pairing and strand exchange
Glycans (no glucose) bound to unfolded protein
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Similar idiotypic specificity for the membrane IgD and IgM of human B lymphocytes
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nascent polypeptide with signal sequence
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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_151603.1
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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_154342.3
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Molecular characterization of a third member of the guanylyl cyclase-activating protein subfamily
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(ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI
Golgi Cisternae Pericentriolar Stack Reorganization
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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_156176.3
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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_109257.9
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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_95532.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_154345.3
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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_152078.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642989
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1629759
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643043
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643042
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=72620
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_97216.9
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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=3651925
Sar1b:GTP:Sec23p:Sec24p (name copied from entity in Homo sapiens)
DNA with RNA Polymerase III Type 2 Closed Promoter
Sec23p:Sec24p Complex (name copied from entity in Homo sapiens)
elongating pre-mRNA Pol III transcript plus 1 nucleotide
Sar1b:GTP:Sec23p:Sec24p:Sec13p:Sec31p Complex (name copied from entity in Homo sapiens)
Polymerase III gene DNA with transcription bubble (single-stranded region)
Sec13p:Sec31p Complex (name copied from entity in Homo sapiens)
released pre-mRNA Pol III oligonucleotide
Sar1b:GTP Complex (name copied from entity in Homo sapiens)
Sar1b:Sec23p:Sec24p:Sec13p:Sec31p Complex (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=3650455
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650558
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_154997.3
Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis
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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=3644019
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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=1629736
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643051
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1629738
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_157648.3
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_151437.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643215
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643102
Polymerase III gene DNA with a termination site
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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=3650970
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_151186.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650448
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643217
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650485
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642669
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2023929
Reactome stable identifier. Use this 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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Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2023922
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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=3648374
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_156756.3
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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_153609.3
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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_151123.1
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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_157847.3
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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_150541.1
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_151792.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2023940
RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate
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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=3650525
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_155744.3
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DNA polymerase delta, an essential enzyme for DNA transactions.
High-resolution x-ray structure of human aquaporin 5
Purification and characterization of kynurenine aminotransferase I from human brain
Biochemical characterization of human GMP synthetase
Endosomal Sorting Complex Required For Transport (ESCRT)
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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_156373.3
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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=3650508
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_153634.3
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=3651475
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651473
Proteasomes: protein degradation machines of the cell
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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=3651466
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651472
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651470
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651465
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651464
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651463
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_92606.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651817
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_149237.4
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Two distinct proteolytic processes in the generation of a major histocompatibility complex class I-presented peptide
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Glucagon and regulation of glucose metabolism
Am J Physiol Endocrinol Metab 284:E671-8
Succinic semialdehyde dehydrogenase deficiency: lessons from mice and men
MicroRNAs: biogenesis, function and applications
Expression, purification, and characterization of human acetyl-CoA carboxylase 2
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Transcription initiation factor TFIID 20/15 kDa subunits
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Transcription initiation factor TFIID 250 kDa subunit
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Transcription initiation factor TFIID 18 kDa subunit
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The cellular response to neuregulins is governed by complex interactions of the erbB receptor family
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Transcription initiation factor TFIID 70 kDa subunit
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Stimulation of phosphatidylglycerolphosphate phosphatase activity by unsaturated fatty acids in rat heart
The human PICD gene encodes a cytoplasmic and peroxisomal NADP(+)-dependent isocitrate dehydrogenase
Transcription initiation factor TFIID 28 kDa subunit
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Transcription initiation factor TFIID 100 kDa subunit
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Transcription Factor IIA beta chain - p19
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template DNA:11 nucleotide transcript hybrid
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elongating pre-mRNA Pol III oligonucleotide
DNA with RNA Polymerase III Type 2 Open Promoter
Elongating transcript prior to separation
Human chromokinesin KIF4A functions in chromosome condensation and segregation
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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
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Identification of the alpha-aminoadipic semialdehyde synthase gene, which is defective in familial hyperlysinemia.
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Transcription elongation factor B polypeptide 1
RNA polymerase II transcription factor SIII subunit C
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A full-length cDNA of hREV3 is predicted to encode DNA polymerase zeta for damage-induced mutagenesis in humans.
RNA polymerase II transcription factor SIII subunit A1
Transcription elongation factor B polypeptide 3
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Human small-intestinal beta-galactosidases. Separation and characterization of one lactase and one hetero beta-galactosidase
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Mutations in SPTLC1, encoding serine palmitoyltransferase, long chain base subunit-1, cause hereditary sensory neuropathy type I
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Transcription initiation factor IIB (General transcription factor TFIIB) (S300-II)
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Transcription initiation factor IIE, alpha subunit
General transcription factor IIE 56 kDa subunit
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Transcription Factor IIA alpha chain - p35
Transcription initiation factor IIA gamma chain
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DNA-directed RNA polymerase I 135 kDa polypeptide
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DNA-directed RNA polymerase I largest subunit
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DNA double-strand breaks: signaling, repair and the cancer connection.
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ArfGAP1 dynamics and its role in COPI coat assembly on Golgi membranes of living cells
The crystal structure and mutational analysis of human NUDT9
Hemostasis and Thrombosis: Basic Principles and Clinical Practice
Leukotriene A4 hydrolase in human leukocytes. Purification and properties
Characterization of the enzymatic defect in late-onset muscle phosphofructokinase deficiency. New subtype of glycogen storage disease type VII.
Inactivation of NPC1L1 causes multiple lipid transport defects and protects against diet-induced hypercholesterolemia
When do Lasses (longevity assurance genes) become CerS (ceramide synthases)?: Insights into the regulation of ceramide synthesis
Mechanism of selectivity in aquaporins and aquaglyceroporins
T-complex protein 1 subunit zeta (TCP-1-zeta)
A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor
T-complex protein 1 subunit epsilon (TCP-1-epsilon)
T-complex protein 1 subunit beta (TCP-1-beta)
T-complex protein 1 subunit gamma (TCP-1-gamma)
T-complex protein 1 subunit eta (TCP-1-eta)
T-complex protein 1 subunit delta (TCP-1-delta)
T-complex protein 1 subunit theta (TCP-1-theta)
T-complex protein 1 subunit alpha (TCP-1-alpha)
Peroxisome proliferator-activated receptors: nuclear control of metabolism
Eukaryotic translation initiation factor 5A
Eukaryotic tranlation initiation factor 5A2
Eukaryotic translation initiation factor 5A-1
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TATA box-binding protein-associated factor, RNA polymerase III, subunit 2
Transcription factor IIIB 90 kDa subunit
Eukaryotic translation initiation factor 2 gamma subunit
eukaryotic translation initiation factor 2, subunit 3
Eukaryotic translation initiation factor 2 subunit 3
eukaryotic translation initiation factor 2, subunit 2
Eukaryotic translation initiation factor 2 subunit 2
eukaryotic translation initiation factor 2 beta subunit
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 3 subunit 6
eukaryotic translation initiation factor 3 subunit 8
eukaryotic translation initiation factor 3 subunit 9
eukaryotic translation initiation factor 3 subunit 11
Eukaryotic translation initiation factor 3 subunit 1
Cohesin acetyltransferase Esco2 is a cell viability factor and is required for cohesion in pericentric heterochromatin
ATR couples FANCD2 monoubiquitination to the DNA-damage response
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Cancer-derived mutations in the regulatory subunit p85alpha of phosphoinositide 3-kinase function through the catalytic subunit p110alpha
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Replication of UV-damaged DNA: new insights into links between DNA polymerases, mutagenesis and human disease.
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Eukaryotic translation initiation factor 3 subunit 4
eukaryotic translation initiation factor 3 subunit 5
Eukaryotic translation initiation factor 3 subunit 3
eukaryotic translation initiation factor 3 subunit 7
Translation initiation factor eIF-2B gamma subunit
eIF-2B GDP-GTP exchange factor, gamma subunit
translation initiation factor 2B gamma subunit
translation initiation factor 2B beta subunit
eIF-2B GDP-GTP exchange factor, beta subunit
Translation initiation factor eIF-2B beta subunit
Eukaryotic translation initiation factor 3 subunit 2
translation initiation factor 2B alpha subunit
Translation initiation factor eIF-2B alpha subunit
eIF-2B GDP-GTP exchange factor, alpha subunit
translation initiation factor 2B delta subunit
eIF-2B GDP-GTP exchange factor, delta subunit
Translation initiation factor eIF-2B delta subunit
eIF-2B GDP-GTP exchange factor, epsilon subunit
Translation initiation factor eIF-2B epsilon subunit
translation initiation factor 2B epsilon subunit
Signal recognition particle 68 kDa protein
The prosthetic group of crystalline D-glyceraldehyde-3-phosphate dehydrogenase
Crystalline D-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle
GABAB receptors: physiological functions and mechanisms of diversity
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 1623-1650
GABAB receptor coupling to G-proteins and ion channels
3alpha,7alpha,12alpha-Trihydroxy-5beta-cholest-24-enoyl-CoA [ChEBI:1695]
Metabolic characteristics and importance of the universal methionine salvage pathway recycling methionine from 5'-methylthioadenosine
Translocon-associated protein subunit alpha
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Specific protein domains mediate cooperative assembly of HuR oligomers on AU-rich mRNA-destabilizing sequences
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The Enzymes, 2nd ed (Boyer PD, Lardy H, Myrback K, editors) 6:75-83
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Scriver CR, et al., editors) 1:1553-1587
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The Menkes protein (ATP7A; MNK) cycles via the plasma membrane both in basal and elevated extracellular copper using a C-terminal di-leucine endocytic signal
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Scriver CR, et al., editors) 1:1489-1520
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Synthesis of Leukotrienes (LT) and Eoxins (EX)
The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II
Crystal structure of human aquaporin 4 at 1.8 A and its mechanism of conductance
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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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Cloning and expression of N-acetylglucosaminyltransferase I, the medial Golgi transferase that initiates complex N-linked carbohydrate formation
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Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1
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Cytosolic high Km 5'-nucleotidase and 5'(3')-deoxyribonucleotidase in substrate cycles involved in nucleotide metabolism
Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors
Enzymatic phosphorylation of nucleoside diphosphates
Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin
Cloning of the sulphamidase gene and identification of mutations in Sanfilippo A syndrome
Regulation of Insulin Secretion by Glucagon-like Peptide-1
Role of the cAMP sensor Epac as a determinant of KATP channel ATP sensitivity in human pancreatic beta-cells and rat INS-1 cells
ZnT-2, a mammalian protein that confers resistance to zinc by facilitating vesicular sequestration
Molecular cloning and expression of the cDNAs encoding human and yeast mevalonate pyrophosphate decarboxylase
Regulation of small GTPases at epithelial cell-cell junctions
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.
Fatty acid elongases in mammals: their regulation and roles in metabolism
Platelet factor 4 and adenosine diphosphate release during human platelet aggregation
Ghost homologue of phospho-Emi1:Cdc20/Cdh1 complexes
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Platelet releasate (inferred) cytosolic proteins
Identification of the human and bovine ATP:Cob(I)alamin adenosyltransferase cDNAs based on complementation of a bacterial mutant
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Threonine 308 phosphorylated form of Akt translocates to the nucleus of PC12 cells under nerve growth factor stimulation and associates with the nuclear matrix protein nucleolin
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HGSNAT oligomer (name copied from entity in Homo sapiens)
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Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase
f-actin (name copied from entity in Homo sapiens)
microtubule (name copied from entity in Homo sapiens)
Cell cycle-regulated nuclear import and export of Cdc47, a protein essential for initiation of DNA replication in budding yeast.
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mRNA Transcript Targeted by Tristetraproline
mRNA Transcript Targeted by HuR Phosphorylated on Ser158 and Ser318.
isovaleryl-CoA, a-methylbutyryl-CoA, isobutyryl-CoA
mRNA Transcript Targeted by AUF1(hnRNP D0)
a-ketoisocaproate, a-keto b-methylvalerate, a-ketoisovalerate
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xenobiotic/medium-chain fatty acid:CoA ligases
Identification and characterization of a novel inositol hexakisphosphate kinase
The solute carrier 26 family of proteins in epithelial ion transport
mature mRNA (eukaryotic, capped and deadenylated)
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Activity of phosphatidylethanolamine-N-methyltransferase in brain affected by Alzheimer's disease
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Molecular characterization of human and mouse photoreceptor guanylate cyclase-activating protein (GCAP) and chromosomal localization of the human gene.
Ghost homologue of G-protein gamma subunit
Protein kinase C conventional and novel isoforms
Structural basis for human monoglyceride lipase inhibition
Signaling mechanisms utilized by antigen receptors and integrins: common intermediates, different outcomes?
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mRNA with premature termination codon not preceding exon junction
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5,10-methylenetetrahydrofolate polyglutamate
ATP-Binding cassette cholesterol transporters and cardiovascular disease
Identification of the human mitochondrial oxodicarboxylate carrier. Bacterial expression, reconstitution, functional characterization, tissue distribution, and chromosomal location
mRNA with premature termination codon preceding exon junction
mRNA Transcript Targeted by HuR Phosphorylated on Ser221 and Ser318
mRNA Transcript Targeted by HuR with Unknown Phosphorylation
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Function of RIG-I-like receptors in antiviral innate immunity
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Identification and characterization of a mammalian mitochondrial ATP-binding cassette membrane protein
The lipoxin receptor ALX: potent ligand-specific and stereoselective actions in vivo
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Phosphorylation of the CARMA1 linker controls NF-kappaB activation
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Activation of p75NTR by proBDNF facilitates hippocampal long-term depression
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A novel and evolutionarily conserved PtdIns(3,4,5)P3-binding domain is necessary for DOCK180 signalling
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Sentrin-specific protease 2 ecNumber3.4.22.68/ecNumber
Sentrin-specific protease 1 ecNumber3.4.22.68/ecNumber
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Mechanisms of digestion and absorption of dietary vitamin A
Identification of autophosphorylation sites of HER2/neu
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PERK in the life and death of the pancreatic beta-cell
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The human telomere terminal transferase enzyme is a ribonucleoprotein that synthesizes TTAGGG repeats
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Guanine nucleotide-binding protein G(T), alpha-1 subunit
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The multiple actions of GLP-1 on the process of glucose-stimulated insulin secretion
Glycylpeptide N-tetradecanoyltransferase 1 ecNumber2.3.1.97/ecNumber
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Glycylpeptide N-tetradecanoyltransferase 2 ecNumber2.3.1.97/ecNumber
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Phosphoinositide phosphatases in cell biology and disease
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Retinol dehydrogenase 8 ecNumber1.1.1.300/ecNumber
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The proteasome and MHC class I antigen processing
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Immunoglobulin E receptor signaling and asthma
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STING specifies IRF3 phosphorylation by TBK1 in the cytosolic DNA signaling pathway
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Ribosomal scanning and start codon recognition
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11-epi-Prostaglandin F2alpha [ChEBI:730]
Fcgamma receptor signaling in phagocytes
GRASP55 regulates Golgi ribbon formation
Molecular cloning of a member of the facilitative glucose transporter gene family GLUT11 (SLC2A11) and identification of transcription variants
N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
PTEN Phosphatase Domain Missense Mutants
The PDGF family: four gene products form five dimeric isoforms
The Rap-B-Raf signalling pathway is activated by glucose and glucagon-like peptide-1 in human islet cells
Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells
Mutation spectrum and genotype-phenotype analyses in Cowden disease and Bannayan-Zonana syndrome, two hamartoma syndromes with germline PTEN mutation
Transcription initiation protein SPT4 homolog 1
Isocitrate dehydrogenase (NADP) cytoplasmic R132H
Chemistry and Biology of Hyaluronan (Book): 71-81
Multiple splice variants of the human calcium-independent phospholipase A2 and their effect on enzyme activity
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Genetic disorders of mitochondrial fatty acid oxidation.
Sentrin-specific protease 5 ecNumber3.4.22.68/ecNumber
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Three tRNA binding sites in rabbit liver ribosomes and role of the intrinsic ATPase in 80S ribosomes from higher eukaryotes
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The human photoreceptor rim protein gene (ABCR): genomic structure and primer set information for mutation analysis
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Transformation and Stat activation by derivatives of FGFR1, FGFR3, and FGFR4
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Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors
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Fcgamma receptor (FCGR) dependent phagocytosis
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Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein
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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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Systemic amyloid fibril main peptide chains
Medin amyloid fibril (name copied from entity in Homo sapiens)
Variant apolipoprotein AII fibril (name copied from entity in Homo sapiens)
Transthyretin fibril (name copied from entity in Homo sapiens)
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Elongating transcript in processive Pol II mediated elongation
Molecular cloning of human mevalonate kinase and identification of a missense mutation in the genetic disease mevalonic aciduria
Characterization and functional analysis of the nucleotide binding fold in human peroxisomal ATP binding cassette transporters
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Template DNA hybrid with phosphodiester-PPi intermediate
template DNA opened from -10 to +2, with first nucleotide base-paired at 5'-end
template DNA:3 nucleotide transcript hybrid
template DNA with first transcript dinucleotide, opened to +8 position
Open DNA -10 to +2 containing RNA Polymerase II promoter
DNA containing RNA Polymerase II promoter
Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis
template DNA:9 nucleotide transcript hybrid
template DNA:4 nucleotide transcript hybrid
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The family of glycogen phosphorylases: structure and function
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Thrombin and phorbol esters cause the selective phosphorylation of a G protein other than Gi in human platelets
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Both human ferredoxins 1 and 2 and ferredoxin reductase are important for iron-sulfur cluster biogenesis
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The TMEM16 protein family: a new class of chloride channels?
Phosphorylation of the cystic fibrosis transmembrane conductance regulator
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Mitotic inhibition of GRASP65 organelle tethering involves Polo-like kinase 1 (PLK1) phosphorylation proximate to an internal PDZ ligand
Adenosine deaminase-like protein 1 (ADAL1): characterization and substrate specificity in the hydrolysis of N(6)- or O(6)-substituted purine or 2-aminopurine nucleoside monophosphates
Motif analysis of the tumor suppressor gene MMAC/PTEN identifies tyrosines critical for tumor suppression and lipid phosphatase activity
Sororin, a substrate of the anaphase-promoting complex, is required for sister chromatid cohesion in vertebrates
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Pleiotropic effects of ATP.Mg2+ binding in the catalytic cycle of ubiquitin-activating enzyme
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Ca/calmodulin activated Adenylate Cyclase
RNA Polymerase III Transcription Termination
Double-strand DNA containing an adenine opposite to an 8-oxo guanine
Double-strand DNA containing an 8-oxo guanine opposite to a cytosine
Double-strand DNA containing a formamidopyrimidine
DNA containing an apurinic/apyrimidinic (AP) site
Double-strand DNA containing a cytosine glycol
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Glucagon signaling in metabolic regulation
Molybdenum cofactors, enzymes and pathways
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Function and biogenesis of iron-sulphur 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=189481
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_117033.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2162223
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113531
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_157200.3
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=1605715
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=189487
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_158329.3
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_9665.2
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=3652341
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644336
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_124014.2
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_81276.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650777
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_9839.1
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_34465.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644334
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2160848
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=189484
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644333
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641817
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_83080.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651774
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644370
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642924
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=391232
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642925
A multidrug resistance transporter from human MCF-7 breast 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=3644366
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644367
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641813
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644369
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3641814
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_77839.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642923
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=189408
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4623.2
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_9814.1
Prostaglandin and leukotriene omega-hydroxylases
Prostaglandins Other Lipid Mediat 68:345-62
Reduced phosphorylation of AS160 contributes to glucocorticoid-mediated inhibition of glucose uptake in human and murine adipocytes
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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_166091.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649896
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651598
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645506
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649895
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3651596
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649894
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645512
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650880
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649897
Perifosine, a novel alkylphospholipid, inhibits protein kinase B 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=2995348
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649892
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3645516
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649306
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_17066.2
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_165517.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649889
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649890
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2995328
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652032
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1678743
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_106748.9
Initiation of mammalian protein synthesis. II. The assembly of the initiation complex with purified initiation factors.
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_28039.10
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_122943.1
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_121895.1
Initiation of mammalian protein synthesis. I. Purification and characterization of seven initiation factors.
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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=3649885
The skeletal muscle chloride channel in dominant and recessive human myotonia
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_164643.1
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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=3651604
Isolation of a human cDNA that complements a mutant hamster cell defective in methotrexate uptake
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_168375.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652031
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_125048.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649996
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649879
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649878
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4299.2
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_123830.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=38985
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2104995
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_86330.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_116807.1
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_154724.3
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=3652041
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1605637
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_14175.2
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=3645624
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=211973
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2104997
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_122540.1
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_2414.3
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_33311.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=143501
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652342
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_166795.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652224
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=40727
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_131636.5
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5145.3
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=3652350
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_81156.9
Cloning and functional expression of human aquaporin8 cDNA and analysis of its gene
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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_2461.2
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=3642649
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_154576.3
Serine 228 is essential for catalytic activities of 85-kDa cytosolic phospholipase A2
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_140159.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649998
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_127751.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652313
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_134240.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3652225
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649979
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649945
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649994
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649972
Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S
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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_168856.1
Chondroitin sulfate/dermatan sulfate metabolism
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2090040
cDNA cloning and chromosome mapping of human dihydropyrimidine dehydrogenase, an enzyme associated with 5-fluorouracil toxicity and congenital thymine uraciluria
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_79107.9
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_124809.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2105012
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649953
Protein kinase C-theta (PKC theta): a key enzyme in T cell life and death
Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles
ABCG5 and ABCG8 are obligate heterodimers for protein trafficking and biliary cholesterol excretion
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649988
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649958
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649981
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649335
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2105010
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1605658
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_117464.1
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_122813.1
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_146243.5
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650217
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2090045
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_122786.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=2090080
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650215
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644112
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647467
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3644128
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647462
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649938
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647471
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647472
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3649956
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3647473
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3646660
Mitochondrial Iron-Sulfur Cluster Biogenesis
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_123208.1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3650209
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ATM-dependent phosphorylation of Mdm2 on serine 395: role in p53 activation by DNA damage.
Pathogen recognition with Toll-like receptors
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Nitric oxide, tetrahydrobiopterin, oxidative stress, and endothelial dysfunction in hypertension
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(S)-3-Hydroxydodecanoyl-CoA [ChEBI:27668]
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Signal transduction during Fc receptor-mediated phagocytosis
Mutational analysis in longest known survivor of mucopolysaccharidosis type VII
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Selective function of PKC-theta in T cells
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GLUT2 in pancreatic and extra-pancreatic gluco-detection (review)
The basis for selective E1-E2 interactions in the ISG15 conjugation system
The extended GLUT-family of sugar/polyol transport facilitators: nomenclature, sequence characteristics, and potential function of its novel members (review)
Intracellular mechanisms of antigen cross presentation in dendritic cells
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cDNA cloning, expression and characterization of human prostaglandin F synthase
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nicotinic acid adenine dinucleotide phosphate [ChEBI:31906]
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Disorders of propionate and methylmalonate metabolism
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 2165-2193
Mitochondrial fatty acid oxidation disorders
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 2297-2326
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In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis
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NLRs join TLRs as innate sensors of pathogens
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Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2
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Lysophospholipid acyltransferases: 1-acylglycerol-3-phosphate O-acyltransferases (AGPATs) From discovery to disease
CD28/CTLA-4 and CD80/CD86 families: signaling and function
1-phosphatidyl-1D-myo-inositol 3-phosphate
The human lamin B receptor/sterol reductase multigene family
1-phosphatidyl-1D-myo-inositol 4-phosphate
Identification and characterization of human cDNAs specific to BCS1, PET112, SCO1, COX15, and COX11, five genes involved in the formation and function of the mitochondrial respiratory chain
Structural basis of Wnt recognition by Frizzled
G proteins and opioid receptor-mediated signalling
1-phosphatidyl-1D-myo-inositol 4-phosphates
phosphorylated nuclear Cyclin B1:Cdc2 substrates
6Z,9Z,12Z,15Z,18Z,21Z-tetracosahexaenoyl-CoA (THA-CoA)
Cloning of a new aquaporin (AQP10) abundantly expressed in duodenum and jejunum
6Z,9Z,12Z,15Z,18Z-tetracosapentaenoyl-CoA (TPA-CoA)
Recycling of the general transcription factors during RNA polymerase II transcription.
damaged DNA substrate:nascent mRNA hybrid with dual incisions
damaged DNA substrate:nascent mRNA hybrid with 3' incision
repaired DNA template:nascent mRNA hybrid
Plasmalogens: biosynthesis and functions
damaged DNA substrate:nascent mRNA hybrid
RNA primer:origin duplex with DNA damage
Integration of DAG signaling systems mediated by PKC-dependent phosphorylation of RasGRP3
Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2
3' -UTR-mediated translational regulation
DNA strand break containing replaced unligated residue
DNA strand break containing single nucleotide gap
A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene causes carbohydrate-deficient glycoprotein syndrome type-Ic
DNA strand containing replaced ligated residue
Double-strand DNA containing a dihydrouracil
Double-strand DNA containing a thymine glycol
DNA strand break containing an incision 5' to an AP site
WD repeat domain phosphoinositide-interacting protein 1
Testis-specific Y-encoded-like protein 2
Novel fibroblast growth factor receptor 3 (FGFR3) mutations in bladder cancer previously identified in non-lethal skeletal disorders
Assembly and export of MHC class I peptide ligands
Keratan sulfate: structure, biosynthesis, and function
Elongated DNA template with bypassed lesion
Heteroduplex DNA with D-loop structure with extended pairing between invading strand and complementary heteroduplex strand and containing newly synthesized ends
Structure of apo-phosphatidylinositol transfer protein alpha provides insight into membrane association
Phenylalanyl-tRNA synthetase alpha chain
High-throughput mass spectrometry screening for inhibitors of phosphatidylserine decarboxylase
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Identification and characterization of human ethanolaminephosphotransferase1
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Proteases involved in MHC class II antigen presentation
Chemokine-mediated interaction of hematopoietic progenitors with the bone marrow vascular niche is required for thrombopoiesis
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SUMOylation and deSUMOylation at a glance
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Tryptophan nutrition and metabolism: an overview
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Involvement of enzymes other than CYPs in the oxidative metabolism of xenobiotics
Expert Opin Drug Metab Toxicol 2:895-921
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tetra-mu3-sulfido-tetrairon [ChEBI:49883]
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Characterization and functional expression of the cDNA encoding human brain quinolinate phosphoribosyltransferase
The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes.
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Protein kinase C theta is expressed in mast cells and is functionally involved in Fcepsilon receptor I signaling
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The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase
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Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPs
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The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments
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Remodeling of cardiolipin by phospholipid transacylation
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Molecular modeling of human P450c17 (17alpha-hydroxylase/17,20-lyase): insights into reaction mechanisms and effects of mutations
Human glyceraldehyde 3-phosphate dehydrogenase-2 gene is expressed specifically in spermatogenic cells.
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The kinesin-8 motor Kif18A suppresses kinetochore movements to control mitotic chromosome alignment
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Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity
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Molecular characterization of histidinemia: identification of four missense mutations in the histidase gene
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N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
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dolichyl-phosphate mannosyltransferase polypeptide 2
dolichyl-phosphate mannosyltransferase polypeptide 3
dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit
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Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes
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Unifying concepts in CD28, ICOS and CTLA4 co-receptor signalling
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Folding of glycoproteins: toward understanding the biophysics of the glycosylation code
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ER degradation-enhancing alpha-mannosidase-like 3
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
UDP-glucose:glycoprotein glucosyltransferase 1
UDP-glucose:glycoprotein glucosyltransferase 2
Expression and characterization of recombinant human and rat liver 6-pyruvoyl tetrahydropterin synthase. Modified cysteine residues inhibit the enzyme activity
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Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
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Homologous recombination repair of replication-independent double-strand breaks
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Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP(+) molecule and provides insights into enzyme deficiency
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Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
Two homologues encoding human UDP-glucose:glycoprotein glucosyltransferase differ in mRNA expression and enzymatic activity
Identification and characterization of all-trans-retinol dehydrogenase from photoreceptor outer segments, the visual cycle enzyme that reduces all-trans-retinal to all-trans-retinol.
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Role of the SCFSkp2 ubiquitin ligase in the degradation of p21Cip1 in S phase
Asparagine-linked glycosylation protein 11 homolog
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Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
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A revised picture of the E2F transcriptional network and RB function.
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GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase
Chitobiosyldiphosphodolichol beta-mannosyltransferase
UDP-N-acetylglucosamine transferase subunit ALG14 homolog
A "slow" homotetrameric kinesin-related motor protein purified from Drosophila embryos
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Physiological levels of PTEN control the size of the cellular Ins(1,3,4,5,6)P(5) pool
Still a puzzle: why is haem covalently attached in c-type cytochromes?
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Investigation of coenzyme Q biosynthesis in human fibroblast and HepG2 cells
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5-Hydroxy-12-oxo-delta5,8,11,14-eicosapolyenoic acid
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Dissociation of GDP dissociation inhibitor and membrane translocation are required for efficient activation of Rac by the Dbl homology-pleckstrin homology region of Tiam
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BRCA1 affects lipid synthesis through its interaction with acetyl-CoA carboxylase
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Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC
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Gap-filling DNA repair synthesis and ligation in TC-NER
Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
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Analysis of the gene sequences of the insulin receptor and the insulin-sensitive glucose transporter (GLUT-4) in patients with common-type non-insulin-dependent diabetes mellitus
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The classical human phosphoglucomutase (PGM1) isozyme polymorphism is generated by intragenic recombination
Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding
Genomic structure and expression of the human heme A:farnesyltransferase (COX10) gene
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
Ins and outs of cellular cobalamin transport
Cross-presentation of soluble exogenous antigens (endosomes)
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UDP-N-acetylhexosamine pyrophosphorylase
Glucosamine 6-phosphate N-acetyltransferase
Glucosamine--fructose-6-phosphate aminotransferase (isomerizing) 2
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Glucosamine--fructose-6-phosphate aminotransferase (isomerizing) 1
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Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate
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ChEBI:59084 (Glc)3 (GlcNAc)2 (Man)9 (Asn)1
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ChEBI:59081 (Glc)1 (GlcNAc)2 (Man)9 (PP-Dol)1
ChEBI:59082 (Glc)2 (GlcNAc)2 (Man)9 (Asn)1
Dolichyl-phosphate beta-glucosyltransferase
Mannose-1-phosphate guanyltransferase beta
UDP-N-acetylglucosamine transferase subunit ALG13 homolog
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Mannose-1-phosphate guanyltransferase alpha
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Ligand discrimination in signaling through an ErbB4 receptor homodimer
Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease.
The PI3K-PDK1 connection: more than just a road to PKB
A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage.
Interaction between PCNA and DNA ligase I is critical for joining of Okazaki fragments and long-patch base-excision repair.
Purification, cDNA cloning and heterologous expression of human phosphomannose isomerase
Binding of inositol phosphate to DNA-PK and stimulation of double-strand break repair.
ER-mediated phagocytosis: myth or reality?
Cloning of a human type II phosphatidylinositol 4-kinase reveals a novel lipid kinase family
Ghost homologue of E3 ligases in proteasomal degradation
beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl-yl group
beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl-yl group [ChEBI:63505]
beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl-yl group
beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl-yl group [ChEBI:63503]
beta-D-GalNAc-(1->4)-beta-D-IdoA-(1->3)-beta-D-GalNAc4S-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl-yl group [ChEBI:63516]
beta-D-GalNAc-(1->4)-beta-D-IdoA-(1->3)-beta-D-GalNAc4S-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl-yl group
Reconstitution of two recombinant LSm protein complexes reveals aspects of their architecture, assembly, and function
Origin, Recognition, Signaling and Repair of DNA Double-Strand Breaks in Mammalian Cells
Damage Surveillance and Repair (Keith Caldecott, editor)1-40
Biogenesis and regulation of insulin-responsive vesicles containing GLUT4
Purification and characterization of human liver "high Km" aldehyde dehydrogenase and its identification as glutamic gamma-semialdehyde dehydrogenase.
Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules
Nonhomologous end joining: repair of DNA double strand breaks after ionizing radiation
Pyrimidine pathways in health and disease
Hormone-sensitive lipase and monoacylglycerol lipase are both required for complete degradation of adipocyte triacylglycerol
Platelet activation, signaling and aggregation
(Z,Z,Z,Z)-18-hydroxy-5,8,11,14-icosatetraenoic acid
(5Z,8Z,11Z,14Z)-18-hydroxyicosa-5,8,11,14-tetraenoic acid
(Z,Z,Z,Z)-18-hydroxy-5,8,11,14-eicosatetraenoic acid
18-hydroxy-5Z,8Z,11Z,14Z-eicosatetraenoic acid
(5Z,8Z,11Z,14Z)-18-hydroxy-5,8,11,14-eicosatetraenoic acid
(5Z,8Z,11Z,14Z)-18-hydroxyeicosa-5,8,11,14-tetraenoic acid
18-hydroxyarachidonic acid [ChEBI:63579]
Quantitative and dynamic assessment of the contribution of the ER to phagosome formation
Molecular tinkering of G protein-coupled receptors: an evolutionary success
Insulin degradation: progress and potential.
Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation
HUT2 and HUT11 mediate urea transport in kidney and erythrocytes respectively
RhAG mediates ammounium export from red blood cells
Cellular copper transport is mediated by human copper transporter 1 hCTR1
RhCG mediates ammonium influx into kidney collecting duct cells
RhCG mediates ammonium efflux out of kidney collecting duct cells
RhBG mediates ammonium effflux out of kidney collecting duct cells
RhBG mediates ammonium influx into kidney collecting duct cells
Cho transports from the extracellular space to the cytosol
CTL1-5 can mediate the uptake of choline
Equilibrative transport (export) of nucleosides and free bases by solute carrier family 29 (nucleoside transporters), member 1
Retention of phospho-Cdc25C:14-3-3 complexes within the cytoplasm
Myt-1 mediated phosphorylation of Cyclin B:Cdc2 complexes
Wee1-mediated phosphorylation of Cyclin B1:phospho-Cdc2 complexes
MAD2 converted to an inhibitory state via interaction with Mad1
MAD2 associates with the Mad1 kinetochore complex
Release of activated MAD2 from kinetochores
Phosphorylation of Cdc25A at Ser-123 in response to DNA damage
Proteolytic degradation of ubiquitinated-Cdc25A
Phosphorylation of Cdc25A at Ser-123 by Chk2
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
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
A plus-end-directed motor enzyme that moves antiparallel microtubules in vitro localizes to the interzone of mitotic spindles
Autoubiquitination of phospho-COP1(Ser-387 )
Translocation of COP1 from the nucleus to the cytoplasm
Resumption of transcription after TC-NER
Ligation of newly synthesized repair patch to incised DNA in TC-NER
5' incision leading to excision of DNA fragment with lesion in TC-NER
3' incision of the lesioned strand of DNA in TC-NER
Formation of active Pol II complex with lesioned DNA template
Ligation of newly synthesized repair patch to incised DNA in GG-NER
Displacement of stalled Pol II from the lesion site
RNA Pol II is blocked by the lesion leading to reduced transcription
XPC binds to HR23B forming a heterodimeric complex
Synapsis, or interaction between two DNA-PK:DNA complexes at opposing ends of DNA DSB
Formation of ERCC1-XPF heterodimeric complex
XPC:HR23B complex binds to damaged DNA site with lesion
Aquaporins in the kidney: from molecules to medicine
Association of Ku heterodimer with ends of DNA double-strand break
Association of DNA-PKcs with Ku-bound ends of DNA double-strand breaks
Primary hyperoxaluria: from gene defects to designer drugs?
Structure-function relationships of rat hepatic tryptophan 2,3-dioxygenase: identification of the putative heme-ligating histidine residues
Association of RAD51 with the resected ends of the DNA double-strand break
Ligation of DNA and formation of Holliday structures following repair synthesis
Association of RAD52 with ssDNA at resected ends of double-strand break
Association of RAD51 with RAD52:DNA double-strand break ends
Binding of Pol zeta to lesioned DNA template
Excision of the abasic sugar phosphate (dRP) residue at the strand break
Recruitment of LIG3:XRRC1 complex to the site of repair by POL Beta
DNA ligation via the single-nucleotide replacement pathway
Dissociation of LIG3:XRCC1 complex from site of BER
POL Beta mediated incorporation of the first replacement nucleotide
Displacement of MYH glycosylase by APE1 at the AP site
Displacement of hOGG1 glycosylase by APE1 at the AP site
APE1 mediated endonucleolytic cleavage at the 5' side of the base-free deoxyribose residue
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.
The alpha- and beta-tubulin folding pathways
Graded activation of fibroblast growth factor receptor 3 by mutations causing achondroplasia and thanatophoric dysplasia
Cleavage of formamidopyrimidine by hNTH1 glycosylase
Displacement of hNTH1 glycosylase by APE1 at the AP site
Cleavage of cytosine glycol by hNTH1 glycosylase
Cleavage of dihydrouracil by hNTH1 glycosylase
hNTH1 glycosylase mediated recognition and binding of thymine glycol
Cleavage of thymine glycol by hNTH1 glycosylase
Transcriptional control of adipocyte formation
hNTH1 glycosylase mediated recognition and binding of formamidopyrimidine
hNTH1 glycosylase mediated recognition and binding of dihydrouracil
hNTH1 glycosylase mediated recognition and binding of cytosine glycol
Cleavage of formamidopyrimidine by hOGG1 glycosylase
Cleavage of 8-oxo guanine by hOGG1 glycosylase
IFNgamma signaling-does it mean JAK-STAT?
Concurrent versus individual binding of HuR and AUF1 to common labile target mRNAs
MYH glycosylase mediated recognition and binding of an adenine opposite to an 8-oxo guanine
hOGG1 glycosylase mediated recognition and binding of an 8-oxo guanine opposite to a cytosine
hOGG1 glycosylase mediated recognition and binding of a formamidopyrimidine
Cleavage 8-oxo guanine by MYH glycosylase
Conversion of GABA to Succinate Semialdehyde
Nonsense Mediated Decay Enhanced by the Exon Junction Complex
CLCN1/2/KA/KB transport cytosolic Cl- to extracellular region
Conversion of succinate semialdehyde to succinate
Expression of two succinyl-CoA synthetases with different nucleotide specificities in mammalian tissues
SLC35D2 mediates the antiport of GDP-mannose in exchange for GMP
Passive Transport of Water into Cells by Aquaporins
Passive Transport of Water out of Cells by Aquaporins
Phosphorylation of Mnk1 by caspase-activated Pak2/gamma-PAK inhibits phosphorylation and interaction of eIF4G with Mnk
Acidification of Tf:TfR1 containing endosome
Copper export from cells by copper-transporting ATPase1
ATP7A transports cytosolic Cu2+ to extracellular region
Copper sequestration by copper-transporting ATPase 2
ATP7B transports cytosolic Cu2+ to Golgi lumen
Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy
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
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
TPCN1/2 transport lysosomal Ca2+ to cytosol
Cytosolic Cl- is transported to extracellular region by ANOs
ANOs transport cytosolic Cl- to extracellular region
Role for NudC, a dynein-associated nuclear movement protein, in mitosis and cytokinesis
The DNA-dependent protein kinase: requirement for DNA ends and association with Ku antigen.
CATERPILLERs, pyrin and hereditary immunological disorders
Purification and characterization of kidney and intestinal brush-border membrane trehalases from the rabbit
A proposed role for the Azotobacter vinelandii NfuA protein as an intermediate iron-sulfur cluster carrier
Equilibrative transport (import) of nucleosides and adenine by solute carrier family 29 (nucleoside transporters), member 3
Equilibrative transport (export) of adenosine and biogenic amines by solute carrier family 29 (nucleoside transporters), member 4
Equilibrative transport (import) of nucleosides and free bases by solute carrier family 29 (nucleoside transporters), member 2
Equilibrative transport (export) of nucleosides and adenine by solute carrier family 29 (nucleoside transporters), member 3
SLC35B4 mediates the transport of UDP-xylose into the Golgi lumen
SLC35B4 mediates the transport of UDP-N-acetylglucosamine into the Golgi lumen
Equilibrative transport (import) of adenosine and biogenic amines by solute carrier family 29 (nucleoside transporters), member 4
AT1 transports acetyl-CoA into the Golgi lumen
UDP-glucuronate transport from the cytosol to ER lumen
SLC35C1 mediates the transport of UDP-fucose into the Golgi lumen
A novel bifunctional phospholipase c that is regulated by Galpha 12 and stimulates the Ras/mitogen-activated protein kinase pathway
Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras
Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase
Expression of the HsOrc1 gene, a human ORC1 homolog, is regulated by cell proliferation via the E2F transcription factor
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
Heregulin-dependent delay in mitotic progression requires HER4 and BRCA1
Transcript-selective translational silencing by gamma interferon is directed by a novel structural element in the ceruloplasmin mRNA 3' untranslated region
From molecular action to physiological outputs: peroxisome proliferator-activated receptors are nuclear receptors at the crossroads of key cellular functions
Molecular cloning and expression of a novel human aquaporin from adipose tissue with glycerol permeability
Smooth muscle contraction and relaxation
Beta-galactosidase deficiency (beta-galactosidosis): GM1 gangliosidosis and Morquio B disease
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book): 3775-3809
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
Inhibitory and stimulatory regulation of Rac and cell motility by the G12/13-Rho and Gi pathways integrated downstream of a single G protein-coupled sphingosine-1-phosphate receptor isoform
Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional alpha1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis
G beta:gamma signalling through PI3Kgamma
Mammalian cells express two VPS4 proteins both of which are involved in intracellular protein trafficking
alpha-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl-yl group
alpha-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl-yl group [ChEBI:63645]
Human and rat beta cells differ in glucose transporter but not in glucokinase gene expression
The Metabolic and Molecular Bases of Inherited Disease, 8th ed (Book)
Cloning and characterization of human ORNT2: a second mitochondrial ornithine transporter that can rescue a defective ORNT1 in patients with the hyperornithinemia-hyperammonemia-homocitrullinuria syndrome, a urea cycle disorder
ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage
Molecular mechanism underlying glucagon-like peptide 1 induced calcium mobilization from internal stores in insulin-secreting beta TC3 cells
Atomic structures of amyloid cross-beta spines reveal varied steric zippers
The FGF family: biology, pathophysiology and therapy
Molecular cloning and functional expression of human 3-hydroxyanthranilic-acid dioxygenase.
An atomic-level mechanism for activation of the kinesin molecular motors
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
Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1
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Neuronal TRP channels: thermometers, pathfinders and life-savers
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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
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Polo kinase regulates mitotic chromosome condensation by hyperactivation of condensin DNA supercoiling activity
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Long G tails at both ends of human chromosomes suggest a C strand degradation mechanism for telomere shortening
microRNA Biogenesis and Function : An overview
Diverse mutations in the aldolase B gene that underlie the prevalence of hereditary fructose intolerance
F-actin capping protein is a heterodimer
Kinesin-6 and RACGAP1 form the heterotetrameric complex centralspindlin
F-actin capping protein binds to the barbed end of elongating F-actin
ITPK1 converts Ins-1,3,4-P3 to Ins-1,3,4,6-P4
Molecular cloning and expression of ribosome releasing factor
Specific role for cathepsin S in the generation of antigenic peptides in vivo
Cables enhances cdk2 tyrosine 15 phosphorylation by Wee1, inhibits cell growth, and is lost in many human colon and squamous cancers
Localization of human Cdc25C is regulated both by nuclear export and 14-3-3 protein binding.
Functional consequences of PRODH missense mutations
RFC binding displaces Pol Alpha on the C-strand of the telomere
Loading of PCNA - Sliding Clamp Formation on the C-strand of the telomere
The primase component of DNA polymerase:primase synthesizes a 6-10 nucleotide RNA primer on the G strand of the telomere
The polymerase component of DNA polymerase alpha:primase synthesizes a 20-nucleotide primer on the G strand of the telomere
Phosphorylation of Cdh1 by Cyclin B1:Cdc2
Ubiquitination of cell cycle proteins targeted by the APC/C:Cdh1complex
Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors
G(z) signaling: emerging divergence from G(i) signaling
Phosphorylation of Cdh1 by Cyclin A:Cdk2
Phosphorylation of M phase proteins by active Cyclin B1:Cdc2 complexes
Dephosphorylation of cyclin B2:phospho-Cdc2 (Thr 14) by Cdc25
Cytosolic PLK1 translocates to the nucleus
Dephosphorylation of nuclear Cyclin B1:phospho-Cdc2 (Thr 14, Tyr15) complexes by Cdc25 phosphatases
Translocation of CRS phosphorylated Cyclin B1:Cdc2 complexes
Abortive initiation by RNA polymerase II in vitro at the adenovirus 2 major late promoter.
Translocation of Cdc25B to the cytoplasm
Translocation of Cyclin B1:phospho-Cdc2 to the cytoplasm
Phosphorylation of Cyclin B1 in the CRS domain
Dephosphorylation of cytoplasmic Cyclin B1:phospho-Cdc2 (Thr 14, Tyr 15) complexes by Cdc25 phosphatases
Release of platelet cytosolic components
Release of (inferred) platelet cytosolic components
Exocytosis of platelet alpha granule contents
Surface deployment of platelet alpha granule membrane components
ITPK1 converts Ins-1,3,4-P3 to Ins-1,3,4,5-P4
Release of 78 kDa glucose-regulated protein
ABCC4 accumulation of dense granule contents
PIP3 recruits PDK1 and AKT to the membrane
Calcium and Diacylglycerol activate CalDAG-GEFs (RasGRPs)
Activation of Protein Kinase C novel isoforms
DAG kinase produces phosphatidic acid from DAG
Activation of conventional Protein Kinase C
RFC dissociates after sliding clamp formation on the C-strand of the telomere
Src activation following P2Y purinoceptor activation
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
Dissociation of cohesin from chromosome arms and loss of arm cohesion during early mitosis depends on phosphorylation of SA2
Phosphorylated Orc1 is ubiquitinated while still associated with chromatin
Translocation of Cyclin A:Cdk2 complexes to the nucleus
Phosphorylation of Cyclin A:Cdk2 at Tyr 15
Cdc25A mediated dephosphorylation of Cyclin A:phospho-Cdk2
Phosphorylation of proteins involved in the G1/S transition by Cyclin A:Cdk2
Nascent pre-mRNA with 5'-GMP dissociated from CE
Nascent pre-mRNA with 5'-GMP associated with CE
Ghost homologue of CF I - 68 kDa subunit
Ubiquitinated Orc1 is degraded by the proteasome
Dephosphorylation of Cyclin E:Cdk2 complexes by Cdc25A
Detection of damage during initiation of DNA synthesis in S-phase
Phosphorylation of Cyclin E1:Cdk2 complexes by Myt1
Phosphorylation of Cyclin E2:Cdk2 complexes by Myt1
Translocation of Cyclin E:Cdk2 complex to the nucleus
Phosphorylation of Cyclin E:Cdk2 complexes by Wee-1
Activation of Cyclin B/Cdk1 by Cdc25a (string) protein
Ghost homologue of CF I - 72 kDa subunit
Association of Cyclin B/Cdk1 with replicative origin inhibits pre-RC formation
Proteasome mediated degradation of Cyclin D1
Acetylation of SMC3 subunit of chromosomal arm associated cohesin by ESCO1 or ESCO2
Acetylation of SMC3 subunit of centromeric chromatin associated cohesin by ESCO1 or ESCO2
Myt-1 mediated phosphorylation of Cyclin A:Cdc2
Translocation of Cyclin A:phospho-Cdc2 (Thr 14) to the nucleus
The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
Wee1-mediated phosphorylation of Cyclin A:phospho-Cdc2 complexes
Dephosphorylation of nuclear Cyclin A:phospho-Cdc2 complexes
Receptor-mediated phagocytosis elicits cross-presentation in nonprofessional antigen-presenting cells
Translocation of active Cdc25C to the nucleus
Translocation of Cyclin B1:phospho-Cdc2 complexes to the nucleus
Mcm4,6,7 trimer forms and associates with the replication fork
Rearrangement and mobilization of Mcm2-7
Phosphorylated Cdc6 is exported from the nucleus
Ubiquitinated Cdc6 is degraded by the proteasome
Multiple proteins are localized at replication fork
Phosphorylation of mitotic kinesin-like protein 2 by polo-like kinase 1 is required for cytokinesis
Relocalization of nuclearly localized Cyclin D1 to the cytoplasm
RFC dissociates after sliding clamp formation
Loading of PCNA - Sliding Clamp Formation
K48-polyubiquitinated partially digested Ag
Phosphorylation relieves autoinhibition of the kinetochore motor Cenp-E
Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy
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
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
Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster
Proc. Natl. Acad. Sci. U.S.A. 100:9762-7
The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
poly(deoxyadenylic-deoxythymidylic) acid
Mucopolysaccharidosis type III (Sanfilippo Syndrome): emerging treatment strategies
Mucopolysaccharidosis Type II (Hunter Syndrome): clinical picture and treatment
Ghost homologue of Dephosphorylated NFATC1/2/3
Inactivation of APC/C via CDC20 sequestration
Ghost homologue of Dephosphorylated NFAT
RNA polymerase III Transcription Complexes
Transcriptional Regulation, eds. McKnight, S.L., Yamamoto, K.R. 22:247-280
Cloning, expression, and characterization of a human 4'-phosphopantetheinyl transferase with broad substrate specificity
Platelets in thrombotic and non-thrombotic disorders.
Role of human sphingosine-1-phosphate phosphatase 1 in the regulation of intra- and extracellular sphingosine-1-phosphate levels and cell viability
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S-adenosylmethionine: nothing goes to waste
Nitric oxide and peroxynitrite in health and disease
Cross-presentation of particulate exogenous antigens (phagosomes)
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Human sphingosine kinase: purification, molecular cloning and characterization of the native and recombinant enzymes
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Phosphorylation and inactivation of the mitotic inhibitor Wee1 by the nim1/cdr1 kinase
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Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2
Cross-presentation: avoiding trafficking chaos?
Occurrence of surface IgM, IgD, and free light chains of human lymphocytes
The Protein Biosynthesis Elongation Cycle
Translational Control of Gene Expression89-127
Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase
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
The second messenger system of mouse epidermis. IV. Cyclic AMP and cyclic GMP phosphodiesterase.
Molecular Mechanisms of Phagocytosis (Book): 97-116
Localization of GAR transformylase in Escherichia coli and mammalian cells
Metabolism of alpha-linolenic acid in humans
Prostaglandins Leukot Essent Fatty Acids 75:161-8
Identification of galectin-3 as a high-affinity binding protein for advanced glycation end products (AGE): a new member of the AGE-receptor complex
The type 4 subfamily of P-type ATPases, putative aminophospholipid translocases with a role in human disease
Function of eukaryotic initiation factor 5 in the formation of an 80 S ribosomal polypeptide chain initiation complex.
A refined structure of human aquaporin-1
Beta oxidation of hexanoyl-CoA to butanoyl-CoA
Common variations in ALG9 are not associated with bipolar I disorder: a family-based study
Two highly homologous members of the ClC chloride channel family in both rat and human kidney
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
Binding and release of radiolabeled eukaryotic initiation factors 2 and 3 during 80 S initiation complex formation.
The role of calcium signaling in phagocytosis
Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates
RNA polymerase III transcribes human microRNAs
Role of multiple phosphorylation sites in the COOH-terminal tail of aquaporin-2 for water transport: evidence against channel gating
XTRPC1-dependent chemotropic guidance of neuronal growth cones
Emergence of a DNA-damage response network consisting of Fanconi anaemia and BRCA proteins
The human chromokinesin Kid is a plus end-directed microtubule-based motor
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IMMPORT:Bioinformatics for the future of immunology
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The ATP-binding cassette transporter ABCA4: structural and functional properties and role in retinal disease
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pXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response
Further studies on the activity and subcellular distribution of alanine:glyoxylate aminotransferase in the livers of patients with primary hyperoxaluria type 1
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Phosphoinositide-metabolizing enzymes at the interface between membrane traffic and cell signalling
Altered aquaporin 9 expression and localization in human hepatocellular carcinoma
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pH dependence, substrate specificity and inhibition of human kynurenine aminotransferase I
(24S)-7alpha,24-dihydroxy-5beta-cholestan-3-one [ChEBI:63829]
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alpha-D-GlcN-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl-yl group
alpha-D-GlcN-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl-yl group [ChEBI:63811]
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Membrane-binding and activation mechanism of PTEN
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Performing in vitro sumoylation reactions using recombinant enzymes
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beta-D-IdoA2S-(1->4)-alpha-D-GlcNS3S-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl-yl group [ChEBI:63808]
beta-D-IdoA2S-(1->4)-alpha-D-GlcNS3S-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl-yl group
Myotubularin regulates the function of the late endosome through the gram domain-phosphatidylinositol 3,5-bisphosphate interaction
Multiple roles of Rap1 in hematopoietic cells: complementary versus antagonistic functions
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4-carboxy-4-methylzymosterol [ChEBI:63842]
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Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms
(24S)-7alpha,12alpha,24-trihydroxycholest-4-en-3-one [ChEBI:63839]
(24S)-7alpha,24-dihydroxycholest-4-en-3-one [ChEBI:63838]
Clinical and molecular characterization of the first adult congenital disorder of glycosylation (CDG) type Ic patient
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(24S)-5beta-cholestane-3alpha,7alpha,24-triol [ChEBI:63831]
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(24S)-7alpha,12alpha,24-trihydroxy-5beta-cholestan-3-one [ChEBI:63830]
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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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MCD4 encodes a conserved endoplasmic reticulum membrane protein essential for glycosylphosphatidylinositol anchor synthesis in yeast
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alpha-D-GlcN-(1->4)-beta-D-IdoA2S-(1->4)-alpha-D-GlcNS3S-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl-yl group [ChEBI:63806]
alpha-D-GlcN-(1->4)-beta-D-IdoA2S-(1->4)-alpha-D-GlcNS3S-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl-yl group
alpha-D-GlcNAc-(1->4)-beta-D-IdoA2S-(1->4)-alpha-D-GlcNS3S-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl-yl group [ChEBI:63807]
alpha-D-GlcNAc-(1->4)-beta-D-IdoA2S-(1->4)-alpha-D-GlcNS3S-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl-yl group
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KSper, a pH-sensitive K+ current that controls sperm membrane potential
Proc. Natl. Acad. Sci. U.S.A. 104:7688-92
(E)-2,3-didehydropristanoyl-CoA [ChEBI:63803]
Mechanism of coenzyme binding to human methionine synthase reductase revealed through the crystal structure of the FNR-like module and isothermal titration calorimetry
Human cyclins B1 and B2 are localized to strikingly different structures: B1 to microtubules, B2 primarily to the Golgi apparatus
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5-phospho-alpha-D-ribose 1-diphosphate [ChEBI:17111]
The Arp2/3 complex branches filament barbed ends: functional antagonism with capping proteins
CalDAG-GEFI integrates signaling for platelet aggregation and thrombus formation
SUMO protease SENP1 induces isomerization of the scissile peptide bond
Heparan sulfate proteoglycans on the cell surface: versatile coordinators of cellular functions
beta-D-IdopA-(1->3)-beta-D-GalpNAc4S-(1->4)-beta-D-GlcpA-(1->3)-beta-D-Galp-(1->3)-beta-D-Galp-(1->4)-beta-D-Xylp [ChEBI:63873]
Molecular identification of mammalian phosphopentomutase and glucose-1,6-bisphosphate synthase, two members of the alpha-D-phosphohexomutase family
Activating mutations in the extracellular domain of the fibroblast growth factor receptor 2 function by disruption of the disulfide bond in the third immunoglobulin-like domain
Signal transduction induced by opioids in immune cells: a review
Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme
TRAM couples endocytosis of Toll-like receptor 4 to the induction of interferon-beta
beta-D-GlcpNAc6S-(1->3)-beta-D-Galp-(1->4)-beta-D-GlcpNAc6S-(1->3)-D-Galp [ChEBI:63851]
beta-D-GlcpNAc-(1->3)-beta-D-Galp-(1->4)-beta-D-GlcpNAc6S-(1->3)-D-Galp [ChEBI:63852]
beta-D-Galp-(1->4)-beta-D-GlcpNAc6S-(1->3)-D-Galp [ChEBI:63853]
Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation
beta-D-Galp-(1->4)-beta-D-GlcpNAc6S-(1->3)-beta-D-Galp-(1->4)-beta-D-GlcpNAc6S-(1->3)-D-Galp [ChEBI:63850]
Control of cross-over by single-strand DNA resection.
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
Aberrant expression of zinc transporter ZIP4 (SLC39A4) significantly contributes to human pancreatic cancer pathogenesis and progression
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
Multitasking in signal transduction by a promiscuous human Ins(3,4,5,6)P(4) 1-kinase/Ins(1,3,4)P(3) 5/6-kinase
Human porphobilinogen deaminase mutations in the investigation of the mechanism of dipyrromethane cofactor assembly and tetrapyrrole formation
Regulated transport of the glucose transporter GLUT4.
NUDT9, a member of the Nudix hydrolase family, is an evolutionarily conserved mitochondrial ADP-ribose pyrophosphatase
Biochemistry of signal transduction and regulation
Lysosomal cathepsin B plays an important role in antigen processing, while cathepsin D is involved in degradation of the invariant chain inovalbumin-immunized mice
Regulation of sororin by Cdk1-mediated phosphorylation
Ligand-independent activation of fibroblast growth factor receptors by point mutations in the extracellular, transmembrane, and kinase domains
Direct role of ChREBP.Mlx in regulating hepatic glucose-responsive genes.
Mast cell signaling: the role of protein tyrosine kinase Syk, its activation and screening methods for new pathway participants
cyclic purine dinucleotide [ChEBI:47037]
AU-rich elements and the control of gene expression through regulated mRNA stability
Mechanisms of COPII vesicle formation and protein sorting
triphopsphoric acid 1-xanthosin-5'-yl ester
Orc1 associates with Orc4:Orc5:Orc3:Orc2:origin complexes
Orc4 associates with Orc5:Orc3:Orc2:origin complexes
Orc5 associates with Orc3:Orc2:origin complexes
Orc3 associates with Orc2 constitutively bound at origins of replication
Regulation of KIF20A (MKL2) by phosphorylation
Cdc45 associates with the pre-replicative complex at the origin
Role of second messengers in netrin-1 signaling
DNA polymerase alpha:primase binds at the origin
CDC6 association with ORC:origin complexes mediated by MCM8
Mcm2-7 associates with the Cdt1:CDC6:ORC:origin complex, forming the pre-replicative complex (preRC)
Association of MCM8 with ORC:origin complex
The human kinesin Kif18A is a motile microtubule depolymerase essential for chromosome congression
Phosphorylation of cohesin by PLK1 at chromosomal arms
CDK1 phosphorylates CDCA5 (Sororin) at chromosomal arms
Molecular variation in relation to purine metabolism
J Clin Pathol Suppl (R Coll Pathol) 8:48-63
Activation of the Anaphase Promoting Complex (APC) by PLK1
Essentials of Glycobiology, 2nd edition (Book)
Dephosphorylation of CK2-modified condensin I
Regulation of KIF23 (MKLP1) by phosphorylation
Formation of the active Spliceosomal C complex
Formation of an intermediate Spliceosomal C complex
ATAC spliceosome mediated 3' splice site cleavage, exon ligation
Binding of SLBP to Replication-Dependent Histone Pre-mRNA
ATAC spliceosome mediated Lariat formation,5' splice site cleavage
isocaproaldehyde + NADPH + H+ => 4-methylpentan-1-ol + NADP+
Reduction of isocaproaldehyde to 4-methylpentan-1-ol
pregnenolone + NADPH + H+ => 17alpha-hydroxypregnenolone + NADP+ + H2O
Hydroxylation of pregnenolone to form 17alpha-hydroxypregnenolone
Recruitment of CstF to the CPSF Bound Pre-mRNA
DNA polymerase epsilon binds at the origin
Formation of the CE:GMP intermediate complex
Hydrolysis of the 5'-end of the nascent transcript by the capping enzyme
Transfer of GMP from the capping enzyme GT site to 5'-end of mRNA
Cloning and characterization of human FTCD on 21q22.3, a candidate gene for glutamate formiminotransferase deficiency.
P-glycoprotein-mediated active efflux of the anti-HIV1 nucleoside abacavir limits cellular accumulation and brain distribution
Dissociation of transcript with 5'-GMP from GT
Recognition and binding of the mRNA cap by the cap-binding complex
SPT5 subunit of Pol II binds the RNA triphosphatase (RTP)
Direct proteasome-independent cross-presentation of viral antigen by plasmacytoid dendritic cells on major histocompatibility complex class I
MTABC3 transports porphyrin into mitochondria
The ABCC family mediates organic anion transport
Organization and sequence of the gene for the human mitochondrial dicarboxylate carrier: evolution of the carrier family
The monotopic membrane protein human oxidosqualene cyclase is active as monomer
ABCA8, B1 and B5 mediate xenobiotic efflux
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Sulfate is exported to the cytosol in exchange for dicarboxylate
SLC7A3 (CAT-3)-mediated uptake of cationic amino acids
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The Wilson disease gene: spectrum of mutations and their consequences
SLC7A2, isoform B (CAT-2B)-mediated uptake of cationic amino acids
SLC7A2, isoform A (CAT-2A)-mediated uptake of cationic amino acids
Influence of differential induction of histidine catabolic enzymes on histidine degradation in vivo
SLC7A1 (CAT-1)-mediated uptake of cationic amino acids
SLC43A2 (LAT4)-mediated uptake of large neutral amino acids
SLC43A1 (LAT3)-mediated uptake of large neutral amino acids
atRAL(membrane) is transported to atRAL(cytosol) by ABCA4
cortisol + NADP+ => cortisone + NADPH + H+
Oxidation of cortisol to yield cortisone
17alpha-hydroxyprenenolone + NADPH + H+ + O2 => DHA (dehydroepiandrostenedione) + NADP+ + H2O + acetaldehyde
Side chain cleavage of 17alpha-hydroxypregnenolone to yield DHA
progesterone + NADPH + H+ + O2 => 17alpha-hydroxyprogesterone + NADP+ + H2O
Hydroxylation of progesterone to form 17alpha-hydroxyprogesterone
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RasGRP links T-cell receptor signaling to Ras
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ABCD1/D2/D3 mediate long chain fatty acid transport in to peroxisomes
ABC7, mABC1 and mABC2 mediate heme transport
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sterols[cytosol] + ATP => sterols[extracellular] + ADP + Pi
ABCG5:ABCG8-mediated export of cholesterol and phytosterols
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17alpha-hydroxyprogesterone + NADPH + H+ + O2 => 4-Androstene-3, 17-dione + NADP+ + H2O + acetaldehyde
Side chain cleavage of 17alpha-hydroxyprogesterone to form 4-Androstene-3, 17-dione
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Cloning, sequencing, purification, and Gq-dependent activation of phospholipase C-beta 3
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NRAMP1 transports divalent metal ions across phagosomal membranes of macrophages
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Regulation of Endoplasmic Reticulum Stress-induced Cell Death by ATF4 in Neuroectodermal Tumor Cells
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ZnT3 transports zinc into synaptic vesicles
ZnT2 facilitates zinc vesicular sequestration
ZnT1 mediates the efflux of zinc from the cell
DCT1 (NRAMP2) mediates divalent iron uptake across the apical membrane of enterocytes
ZnT8 transports zinc into the secretory vesicles of pancreatic beta cells specifically
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ZnT7 transports zinc into the golgi apparatus
ZnT5 transports zinc into secretory granules in pancreatic beta cells
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malate [mitochondrial matrix] + orthophosphate [cytosol] <=> malate [cytosol] + orthophosphate [mitochondrial matrix]
Mutation of BSND causes Bartter syndrome with sensorineural deafness and kidney failure
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extracellular fructose => cytosolic fructose
Proton-coupled di- and tri-peptide cotransport
Glucose is taken up across the plasma membrane by a glucose transport protein (GLUT)
alpha-D-glucose (extracellular) <=> alpha-D-glucose (cytosol)
cytosolic fructose, galactose, or glucose => extracellular fructose, galactose, or glucose
Transport (efflux) of fructose, galactose, and glucose by GLUT2
alpha-D-glucose (cytosol) <=> alpha-D-glucose (extracellular)
Glucose is secreted across the plasma membrane
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GLUT9 transports glucose, fructose and urate
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GLUT7 and GLUT11 transport glucose and fructose
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Cobalamin (Cbl, vitamin B12) transport and metabolism
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The structure and function of carbonic anhydrase isozymes in the respiratory system of vertebrates
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Messenger RNA decay in mammalian cells: the exonuclease perspective
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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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The state of the union: the cell biology of fertilization
GDIs: central regulatory molecules in Rho GTPase activation
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STING is a direct innate immune sensor of cyclic di-GMP
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Negative regulation of the PI3K/AKT network
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Integrins: dynamic scaffolds for adhesion and signaling in platelets
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Protein quality control in the ER: the recognition of misfolded proteins
3-hydroxy-2,6,10,14-tetramethylpentadecanoyl-coenzyme A
ATPase switches controlling DNA replication initiation.
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Emerging roles for E2F: beyond the G1/S transition and DNA replication.
5-methyltetrahydrofolyl polyglutamate macromolecule
5-methyltetrahydrofolyl polyglutamate macromolecule [ChEBI:63907]
Access of soluble antigens to the endoplasmic reticulum can explain cross-presentation by dendritic cells
Antigen processing: Ubiquitination & Proteasome degradation
A telomeric sequence in the RNA of Tetrahymena telomerase required for telomere repeat synthesis
ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Igamma
Glucose transporter isoforms GLUT1 and GLUT3 transport dehydroascorbic acid
Mechanisms of disease: molecular and metabolic mechanisms of insulin resistance and beta-cell failure in type 2 diabetes
Characterization of the gene encoding human cone transducin alpha-subunit (GNAT2)
Cloning, tissue distribution, and intrarenal localization of ClC chloride channels in human kidney
(R,R)-3,3'-thiobis-(2-aminopropanoic acid)
(R,R)-2,6-diamino-4-thiaheptanedioic acid
Tyrosine-phosphorylated forms of Ig beta, CD22, TCR zeta and HOSS are major ligands for tandem SH2 domains of Syk
Xenopus Cdc6 performs separate functions in initiating DNA replication.
Glycoprotein folding, quality control and ER-associated degradation
Vav regulates activation of Rac but not Cdc42 during FcgammaR-mediated phagocytosis
Semaphorins in axon regeneration: developmental guidance molecules gone wrong?
Philos Trans R Soc Lond B Biol Sci 361:1499-511
Neurotrophin-regulated signalling pathways
Philos Trans R Soc Lond B Biol Sci 361:1545-64
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Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis--Golgi tethering
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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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Interaction of Ku protein and DNA-dependent protein kinase catalytic subunit with nucleic acids.
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ABCA3 is a lamellar body membrane protein in human lung alveolar type II cells
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Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases
Pathogenic potential of human monoclonal immunoglobulin light chains: relationship of in vitro aggregation to in vivo organ deposition
Metabolism of carcinogenic heterocyclic and aromatic amines by recombinant human cytochrome P450 enzymes
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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
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Isolation and characterization of a human cDNA for mRNA 5'-capping enzyme.
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Purification of the serine palmitoyltransferase complex responsible for sphingoid base synthesis by using affinity peptide chromatography techniques
PI is phosphorylated to PI4P by PI4KA/2A/2B at the Golgi membrane
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PI4P is dephosphorylated to PI by SACM1L at the ER membrane
PI is phosphorylated to PI4P by PI4KA/2B at the ER membrane
Human cytosolic asparaginyl-tRNA synthetase: cDNA sequence, functional expression in Escherichia coli and characterization as human autoantigen
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CL and 1-acyl LPE are converted to MLCL and PE by TAZ (IM) (Reversible)
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MLCL and PE are converted to CL and 1-acyl LPE by TAZ (IM) (Reversible)
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CL and 1-acyl LPC are converted to MLCL and PC by TAZ (IM) (Reversible)
MLCL and PC are converted to CL and 1-acyl LPC by TAZ (IM) (Reversible)
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Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B
13,14-dihydro-15-keto-PGF2a [ChEBI:63976]
PC is transphosphatidylated to PG by PLD1-4/6
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Hyaluronan synthases: a decade-plus of novel glycosyltransferases
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PI is hydrolyzed to 1-acyl LPI by PLA2[11]
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GPCho is hydrolyzed to Cho and G3P by GPCPD1
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1-phosphatidyl-1D-myo-inositol 3-phosphate [ChEBI:17283]
GABA synthesis, release, reuptake and degradation
Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation
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13,14-dihydro-15-keto-Lipoxin A4 [ChEBI:63993]
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ChEBI:17278 5beta-cholestane-3alpha,7alpha,12alpha,26-tetrol
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Structure of human adenosine kinase at 1.5 A resolution.
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AMP kinase and malonyl-CoA: targets for therapy of the metabolic syndrome
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Cloning and expression of the human gene for transaldolase. A novel highly repetitive element constitutes an integral part of the coding sequence
Endogenous synthesis of coenzyme Q in eukaryotes
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Neurotransmitter Receptor Binding And Downstream Transmission In The Postsynaptic Cell
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Opening of an RNA polymerase II promoter occurs in two distinct steps and requires the basal transcription factors IIE and IIH.
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L-Glutamate 5-semialdehyde [ChEBI:17232]
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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
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Identification of inflammatory gene modules based on variations of human endothelial cell responses to oxidized lipids
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p21-activated protein kinase: a crucial component of morphological signaling?
Glucosylceramidase 2 cleaves the glucosidic bond of glucocerebroside to form ceramide (plasma membrane)
Sphingomyelin phosphodiesterase (SMPD1) hydrolyses sphingomyelin to ceramide (lysosome)
Alpha-galactosidase A removes a terminal galactose from alpha-D-galactoside oligomers
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Both hexosaminidase A and B can cleave GalNAc from globoside
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The vitelliform macular dystrophy protein defines a new family of chloride channels
Proc. Natl. Acad. Sci. U.S.A. 99:4008-13
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Neutral ceramidase hydrolyses ceramide into sphingosine and free fatty acid (plasma membrane)
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FPP and IPPP are combined into all-E-10PrP2 by PDSS1/2 tetramer
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Ectonucleotide pyrophosphatase/phosphodiesterase 7 (ENPP7) hydrolyses sphingomyelin
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MDMQ10H2 is methylated to DMQ10H2 by COQ5
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PHB and all-E-10PrP2 are combined into DHB by COQ2
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DMQ10H2 is hydroxylated to DeMQ10H2 by COQ7
Activation of Protein kinase C, alpha type by Diacylglycerol
Hormone-sensitive lipase: control of intracellular tri-(di-)acylglycerol and cholesteryl ester hydrolysis
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Production of formyl-CoA during peroxisomal alpha-oxidation of 3-methyl-branched fatty acids
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Arachidonic acid is hydroxylated to 20-HETE by CYP(3)
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Arachidonic acid is hydroxylated to 19-HETE by CYP(2)
Arachidonic acid is hydroxylated to 16/17/18-HETE by CYP(1)
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15k-LXA4 is reduced to dhk-LXA4 by PTGR1
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LTC4 is exported from the cytosol by ABCC1
ABCC1 mediates LTC4 export from the cell
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dihydroceramide + NAD(P)H + H+ + O2 => ceramide + NAD(P)+ + H2O
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dihydroceramide + NADPH + H+ + O2 => phytoceramide + NADP+ + H2O
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Arachidonic acid is epoxidated to 8,9/11,12/14,15-EET by CYP(5)
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Inactivation of APC/C via direct inhibition of the APC/C complex
3-ketosphinganine + NADPH + H+ => sphinganine + NADP+
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Arachidonic acid is epoxidated to 5,6-EET by CYP(4)
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Evidence that the head of kinesin is sufficient for force generation and motility in vitro
Destabilization of mRNA by AUF1 (hnRNP D0)
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sphinganine 1-phosphate + H2O => sphinganine + orthophosphate
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phytoceramide + H2O => stearate + phytosphingosine
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palmitoyl-CoA + serine => 3-ketosphinganine + CoASH + CO2
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sphinganine + stearyl-CoA => dihydroceramide + CoASH
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sphinganine (dihydrosphingosine) +ATP => sphinganine 1-phosphate + ADP
sphingosine 1-phosphate + H2O => sphingosine + orthophosphate [cytosolic - SGPP]
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sphingosine 1-phosphate => phosphoethanolamine + hexadec-2-enal
Beta-galactosidase hydrolyses GM1 to GM2
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Proximal events in Wnt signal transduction
Beta-galactosidase can also hydrolyse globosides to form cerebrosides
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sphinganine 1-phosphate => phosphoethanolamine + hexadecanal
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sphingosine +ATP => sphingosine 1-phosphate + ADP
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Identification and functional characterization of a new human kidney-specific H+/organic cation antiporter, kidney-specific multidrug and toxin extrusion 2
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PI3P is dephosphorylated to PI by MTM[2] at the early endosome membrane
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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PI3P is phosphorylated to PI(3,5)P2 by PIKFYVE at the late endosome membrane
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PI(3,5)P2 is dephosphorylated to PI5P by MTM[2] at the early endosome membrane
PI is phosphorylated to PI3P by PIK3C2A/3 at the early endosome membrane
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PI is phosphorylated to PI5P by PIKFYVE at the late endosome membrane
Recent developments in the investigation of inherited metabolic disorders using cultured human cells.
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PI is phosphorylated to PI3P by PIK3C2A/3 at the late endosome membrane
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PI(3,5)P2 is dephosphorylated to PI3P by FIG4 at the late endosome membrane
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PI(3,5)P2 is dephosphorylated to PI5P by MTM[3] at the late endosome membrane
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Membrane lipids: where they are and how they behave
Membrane recognition by phospholipid-binding domains
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Translocation of tetracosahexaenoyl-CoA to peroxisomes
Activation of alpha-linolenic acid to alpha-linolenoyl-CoA
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Atomic structure of GTP cyclohydrolase I
PI3P is dephosphorylated to PI by MTM[3] at the late endosome membrane
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Hydration of delta2-tetracosaheptaenoyl-CoA to 3-hydroxy tetracosahexaenoyl-CoA
Dehydrogenation of 3-hydroxy tetracosahexaenoyl-CoA
Formation of DHA-CoA catalysed by 3-ketoacyl-CoA thiolase
Activation of linoleic acid to linoleoyl-CoA
Translocation of tetracosapentaenoyl-CoA to peroxisomes
Prostaglandin E synthase isomerizes PGH2 to PGE2
Crystal structure of human cytosolic 5'-nucleotidase II: insights into allosteric regulation and substrate recognition
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PGD2 is reduced to 11-epi-PGF2a by AKRIC3
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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
15k-PGE2/F2a is reduced to dhk-PGE2/F2a by PTGR1
PI(3,5)P2 is dephosphorylated to PI3P by FIG4 at the Golgi membrane
PI4P is phosphorylated to PI(4,5)P2 by PIP5K1A-C at the plasma membrane
PI3P is dephosphorylated to PI by SACM1L at the Golgi membrane
PI3P is phosphorylated to PI(3,5)P2 by PIKFYVE at the Golgi membrane
PI4P is dephosphorylated to PI by SACM1L at the Golgi membrane
PI is phosphorylated to PI3P by PIK3C2A/3 at the Golgi membrane
PI4KB binds to ARF1/3:GTP at the Golgi membrane
Alteration of enzyme specificity by computational loop remodeling and design
PI is phosphorylated to PI4P by PI4KB at the Golgi membrane
PI(4,5)P2 is dephosphorylated to PI4P by SYNJ/INPP5[1] at the plasma membrane
PI(3,4)P2 is phosphorylated to PI(3,4,5)P3 by PIP5K1A-C at the plasma membrane
PI(3,4,5)P3 is dephosphorylated to PI(3,4)P2 by INPP5[2] at the plasma membrane
PI3P is phosphorylated to PI(3,5)P2 by PIP5K1A/B at the plasma membrane
PI(3,5)P2 is dephosphorylated to PI3P by SYNJ at the plasma membrane
PI(3,5)P2 is dephosphorylated to PI5P by SYNJ/MTM[1] at the plasma membrane
PI5P is phosphorylated to PI(4,5)P2 by PIP4K2A/B at the plasma membrane
PI(3,4)P2 is dephosphorylated to PI4P by PTEN at the plasma membrane
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
PI3P is phosphorylated to PI(3,4)P2 by PIP4K2/5K1 at the plasma membrane
PI3P is dephosphorylated to PI by SYNJ/MTM[1] at the plasma membrane
PI is phosphorylated to PI5P by PIP5K1A/B at the plasma membrane
PI4P is dephosphorylated to PI by SYNJ at the plasma membrane
PI(3,5)P2 is dephosphorylated to PI3P by FIG4 at the early endosome membrane
PI3P is phosphorylated to PI(3,5)P2 by PIKFYVE at the early endosome membrane
Proximity of the poly(A)-binding protein to a premature termination codon inhibits mammalian nonsense-mediated mRNA decay
Human Mcm proteins at a replication origin during the G1 to S phase transition.
Frequent deletions at Xq28 indicate genetic heterogeneity in Hunter syndrome
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Regulation and physiological functions of G12/13-mediated signaling pathways
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CaMK IV-mediated phosphorylation of CREB
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A natural ErbB4 isoform that does not activate phosphoinositide 3-kinase mediates proliferation but not survival or chemotaxis
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A MAP kinase-signaling pathway mediates neurite outgrowth on L1 and requires Src-dependent endocytosis
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Which DNA polymerases are used for DNA-repair in eukaryotes?
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Functions and regulatory mechanisms of Gq-signaling pathways
The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response
The role of Akt in the signaling pathway of the glycoprotein Ib-IX induced platelet activation
Histidine-rich glycoprotein is present in human platelets and is released following thrombin stimulation
Anaphase-promoting complex/cyclosome-dependent proteolysis of human cyclin A starts at the beginning of mitosis and is not subject to the spindle assembly checkpoint
Regulation of mammalian liver methionine adenosyltransferase
Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro.
A novel cardiolipin-remodeling pathway revealed by a gene encoding an endoplasmic reticulum-associated acyl-CoA:lysocardiolipin acyltransferase (ALCAT1) in mouse
Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2
Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with Oct-4 in regulating transcription
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CDK-mediated phosphorylation and removal of Cdc6
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Chromatin association of human origin recognition complex, cdc6, and minichromosome maintenance proteins during the cell cycle: assembly of prereplication complexes in late mitosis.
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Two distinct pathways remove mammalian cohesin from chromosome arms in prophase and from centromeres in anaphase
Monounsaturated fatty acid modification of Wnt protein: its role in Wnt secretion
CD28-mediated co-stimulation: a quantitative support for TCR signalling
The sugar is sIRVed: sorting Glut4 and its fellow travelers
BRCA2-dependent and independent formation of RAD51 nuclear foci.
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PTHP is reduced to BH4 by sepiapterin reductase (SPR)
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Separate SCF(CDC4) recognition elements target Cdc6 for proteolysis in S phase and mitosis.
Acetyl-CoA + H2O + Oxaloacetate => Citrate + CoA
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Oxidative decarboxylation of pyruvate to acetyl CoA by pyruvate dehydrogenase
pyruvate + CoASH + NAD+ => acetylCoA + CO2 + NADH + H+
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Oxidative decarboxylation of alpha-ketoglutarate to succinyl CoA by alpha-ketoglutarate dehydrogenase
alpha-ketoglutarate + CoASH + NAD+ => succinyl-CoA + CO2 + NADH + H+
NADPH + NAD+ + H+ [cytosol] => NADP+ + NADH + H+ [mitochondrial matrix]
isocitrate + NAD+ => alpha-ketoglutarate + CO2 + NADH + H+ [IDH3]
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ADP-ATP translocase maintains a high ADP:ATP ratio in the matrix
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Transport of Extracellular Glucose to the Cytosol by GLUT1 and GLUT2
AMP binds to gamma subunit of AMP kinase heterotrimer
Activation of PP2A by Xylulose-5-phosphate
GCH1 reduces GTP to dihydroneopterin triphosphate
LKB1 phosphorylates the alpha subunit of AMPK heterotrimer
DHNTP is dephosphorylated by PTPS to PTHP
5'-phosphoribosyl-5-formaminoimidazole-4-carboxamide (FAICAR) <=> inosine 5'-monophosphate + H2O
(S)-1-Pyrroline-5-carboxylate [ChEBI:17388]
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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-phosphoribosylglycinamide (GAR) + 10-formyl-tetrahydrofolate => 5'-phosphoribosylformylglycinamide (FGAR) + tetrahydrofolate
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5-phosphoribosylamine + glycine + ATP => 5-phosphoribosylglycinamide (GAR) + ADP + orthophosphate
5-Phosphoribosylamine + Glycine + ATP => GAR + ADP + Pi
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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
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Dissociation of phosphoribosyl pyrophosphate amidotransferase tetramer
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Formation of phosphoribosyl pyrophosphate amidotransferase tetramer
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Transfer of electrons from ETF to ubiquinone by ETF-QO
Reducing equivalents from beta-oxidation of fatty acids transfer to ETF
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A mutation in the Glut2 glucose transporter gene of a diabetic patient abolishes transport activity
5'-phosphoribosyl-5-aminoimidazole-4-carboxamide (AICAR) + 10-formyltetrahydrofolate => 5'-phosphoribosyl-5-formaminoimidazole-4-carboxamide (FAICAR) + tetrahydrofolate
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5'-phosphoribosylformylglycinamidine (FGAM) + ATP => 5'-phosphoribosyl-5-aminoimidazole (AIR) + ADP + orthophosphate
Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange.
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(R)-2-hydroxyglutarate + FAD => 2-oxoglutarate + FADH2
(S)-2-hydroxyglutarate + FAD => 2-oxoglutarate + FADH2
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GDP + Orthophosphate + Succinyl-CoA <=> GTP + Succinate + CoA
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Succinate <=> Fumarate (with FAD redox reaction on enzyme)
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ADP + Orthophosphate + Succinyl-CoA <=> ATP + Succinate + CoA
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2-oxoglutarate + 4-hydroxybutyrate <=> (R)-2-hydroxyglutarate + succinate semialdehyde
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(R)-2-hydroxyglutarate + succinate semialdehyde <=> 2-oxoglutarate + 4-hydroxybutyrate
Transfer of electrons through the succinate dehydrogenase complex
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Greatwall kinase participates in the Cdc2 autoregulatory loop in Xenopus egg extracts
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Mycobacterium tuberculosis and the intimate discourse of a chronic infection
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
The anoctamin family: TMEM16A and TMEM16B as calcium-activated chloride channels
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c-Kit--a hematopoietic cell essential receptor tyrosine kinase
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ADP-ribose + H2O => AMP + D-ribose 5-phosphate (cytosolic)
Cytosolic NUDT5 hydrolyses ADP-ribose to R5P and AMP
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PIG-A and PIG-H, which participate in glycosylphosphatidylinositol anchor biosynthesis, form a protein complex in the endoplasmic reticulum
G protein-independent activation of an inward Na(+) current by muscarinic receptors in mouse pancreatic beta-cells
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Condensation of phosphopantothenate with cysteine
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dehydroascorbate [extracellular] => dehydroascorbate [cytosol]
Dehydroascorbate transport across the plasma membrane
GLUT1/3 transports extracellular DHvitC to cytosol
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SLC19A2/3 transport extracellular THMN to cytosol
thiamin [extracellular] => thiamin [cytosol]
Thiamin transport across the plasma membrane
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COASY transfers an adenylyl group from ATP to PPANT
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Phosphopantothenoylcysteine is decarboxylated
SLC25A16 transports cytosolic CoA-SH to mitichondrial matrix
CoA transport across the inner mitochondrial membrane
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Phosphorylation of dephospho-CoA to produce CoA
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Half-site reactivity in 6-phosphogluconate dehydrogenase from human erythrocytes
Adrenoleukodystrophy gene: unexpected homology to a protein involved in peroxisome biogenesis
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ESCRTing proteins in the endocytic pathway
guanine or hypoxanthine + PRPP => GMP or IMP + PPi [HPRT1]
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Deamination of N6-methyl-AMP to form IMP
N6-methyl-AMP + H2O => IMP + methylamine
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(2'-deoxy)adenosine + ATP => (d)AMP + ADP [ADK]
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inosine 5'-monophosphate + L-aspartate + GTP => adenylosuccinate + guanosine 5'-diphosphate + orthophosphate
IMP + L-Aspartate + GTP => Adenylosuccinate + GDP + Pi [ADSS]
(2'-deoxy)adenosine + H2O => (2'-deoxy)inosine + NH3 [ADA]
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inosine 5'-monophosphate (IMP) + NAD+ + H2O => xanthosine 5'-monophosphate (XMP) + NADH + H+
IMP + H2O + NAD+ => XMP + NADH + H+ [IMPDH1,2]
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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
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(d)GMP or (d)IMP + H2O => (2'-deoxy)guanosine or (2'-deoxy)inosine + orthophosphate [NT5C2]
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all-trans-decaprenyl diphosphate [ChEBI:61011]
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Molecular characterization of methylmalonate semialdehyde dehydrogenase deficiency
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Plk1-dependent phosphorylation of optineurin provides a negative feedback mechanism for mitotic progression
Cellular uptake of sepiapterin and push-pull accumulation of tetrahydrobiopterin
orotate + 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) <=> orotidine 5'-monophosphate (OMP) + pyrophosphate
phosphoribosylation of orotate to form oritidine 5'-phosphate (OMP)
decarboxylation of Orotidine 5'-phosphate to form Uridine 5'-phosphate
orotidine 5'-monophosphate => uridine 5'-monophosphate + CO2
The structure and function of G-protein-coupled receptors
hydrolysis of 2'-deoxyuridine 5'-triphosphate to form 2'-deoxyuridine 5'-phosphate
cytidine or uridine + ATP => CMP or UMP + ADP [UCK1]
L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate
bicarbonate and glutamine combine to form carbamoyl phosphate
carbamoyl phosphate + L-aspartate <=> N-carbamoyl L-aspartate + orthophosphate
carbamoyl phosphate and L-aspartate combine to form N-Carbamoyl-L-aspartate
condensation of N-Carbamoyl-L-aspartate to form (S)-Dihydroorotate (ring closure)
N-carbamoyl L-aspartate + H+ <=> (S)-dihydroorotate + H2O
cytidine or uridine + ATP => CMP or UMP + ADP [UCK2]
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(deoxy)cytidine + H2O => (deoxy)uridine + NH4+ [CDA]
deamination of 2'-Deoxycytidine to 2'-Deoxyuridine
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thymidine + ATP => TMP (deoxythymidine 5'-monophosphate) + ADP [TK1]
phosphorylation of 2'-Deoxythymidine to dTMP
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beta-ureidopropionate + H2O => beta-alanine + NH4+ + CO2
conversion of 3-ureidopropionate to beta-alanine
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thymine + NADPH + H+ => 5,6-dihydrothymine + NADP+
reduction of thymine to form 5,6-Dihydrothymine
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uracil + NADPH + H+ => 5,6-dihydrouracil + NADP+
reduction of uracil to form dihydrouracil
conversion of 5,6-dihydrouracil to 3-ureidopropionate
5,6-dihydrouracil + H2O => beta-ureidopropionate
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conversion of 5,6-Dihydrothymine to 3-Ureidoisobutyrate
5,6-dihydrothymine + H2O => beta-ureidoisobutyrate
beta-ureidoisobutyrate + H2O => 3-aminoisobutyrate + NH4+ + CO2
conversion of 3-Ureidoiosbutyrate to 3-Aminoisobutyrate
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(d)CMP or UMP + ATP <=> (d)CDP or UDP + ADP [CMPK1]
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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_83084.9
(d)CDP or UDP + ADP <=> (d)CMP or UMP + ATP [CMPK1]
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dUMP or TMP + ATP <=> dUDP or TDP + ADP [DTYMK]
phosphorylation of dUMP or TMP to dUDP or TDP
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dUDP or TDP + ADP <=> dUMP or TMP + ATP [DTYMK]
amination of uridine 5'-triphosphate (UTP) to form cytidine 5'-triphosphate (CTP)
UTP + glutamine + ATP + H2O => CTP + glutamate + ADP + orthophosphate [CTPS]
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UTP + glutamine + ATP + H2O => CTP + glutamate + ADP + orthophosphate [CTPS2]
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glutathione (oxidized) + NADPH + H+ => 2 glutathione (reduced) + NADP+
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thioredoxin, oxidized (nucleus) <=> thioredoxin, oxidized (cytosol)
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(d)NDP + ATP <=> (d)NTP + ADP [NME1,2,3]
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thioredoxin, reduced (cytosol) <=> thioredoxin, reduced (nucleus)
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(d)NTP + ADP <=> (d)NDP + ATP [NME1,2,3]
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Mechanisms of glycerophospholipid homeostasis in mammalian cells
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Sanfilippo syndrome type C: deficiency of acetyl-CoA:alpha-glucosaminide N-acetyltransferase in skin fibroblasts
The ABC-transporter signature motif is required for peptide translocation but not peptide binding by TAP
Heparin and heparan sulfate: biosynthesis, structure and function
Disease-causing missense mutations affect enzymatic activity, stability and oligomerization of glutaryl-CoA dehydrogenase (GCDH)
Dissecting and manipulating the pathway for glycosylphosphatidylinositol-anchor biosynthesis
Expression of CD83 is regulated by HuR via a novel cis-active coding region RNA element
Cleavage and activation of p21-activated protein kinase gamma-PAK by CPP32 (caspase 3). Effects of autophosphorylation on activity
Phosphoinositide phosphatases in a network of signalling reactions
Tryptophan metabolism in the central nervous system: medical implications
MCM8 is an MCM2-7-related protein that functions as a DNA helicase during replication elongation and not initiation
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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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Dock4 is regulated by RhoG and promotes Rac-dependent cell migration
FGFR1 is fused with a novel zinc-finger gene, ZNF198, in the t(8;13) leukaemia/lymphoma syndrome
The relative role of PLCbeta and PI3Kgamma in platelet activation
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6-Pyruvoyl tetrahydropterin synthase, an enzyme with a novel type of active site involving both zinc binding and an intersubunit catalytic triad motif; site-directed mutagenesis of the proposed active center, characterization of the metal binding site and modelling of substrate binding
Analysis of Gz alpha by site-directed mutagenesis. Sites and specificity of protein kinase C-dependent phosphorylation
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A novel calcium-independent phospholipase A2, cPLA2-gamma, that is prenylated and contains homology to cPLA2
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myo-Inositol hexakisphosphate [ChEBI:10603]
D-myo-Inositol 1,2,3,4,5,6-hexakisphosphate
myo-Inositol 1,2,3,4,5,6-hexakisphosphate
1D-myo-Inositol 1,2,3,4,5,6-hexakisphosphate
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trans,trans-Farnesyl diphosphate [ChEBI:10700]
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Role of alpha-Asp181, beta-Asp192, and gamma-Asp190 in the distinctive subunits of human NAD-specific isocitrate dehydrogenase
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Replication factor C disengages from proliferating cell nuclear antigen (PCNA) upon sliding clamp formation, and PCNA itself tethers DNA polymerase delta to DNA.
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Identification of a novel prostaglandin reductase reveals the involvement of prostaglandin E2 catabolism in regulation of peroxisome proliferator-activated receptor gamma activation
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Targeting and trafficking of the human thiamine transporter-2 in epithelial cells
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Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class I is independent of mammalian ESCRTII
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ChEBI:17442 4-(2-aminophenyl)-2,4-dioxobutanoic acid
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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Purification, sequencing, and molecular identification of a mammalian PP-InsP5 kinase that is activated when cells are exposed to hyperosmotic stress
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Calcium signalling: past, present and future
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Rich tapestry of G protein-coupled receptor signaling and regulatory mechanisms
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Human X-linked phosphoribosylpyrophosphate synthetase superactivity is associated with distinct point mutations in the PRPS1 gene
Computational approach for determining the spectrum of DNA damage induced by ionizing radiation.
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Regulation of apoptosis: the ubiquitous way
Kit- and Fc epsilonRI-induced differential phosphorylation of the transmembrane adaptor molecule NTAL/LAB/LAT2 allows flexibility in its scaffolding function in mast cells
Association of Fyn and Lyn with the proline-rich domain of glycoprotein VI regulates intracellular signaling
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Crystal structure of human homogentisate dioxygenase.
Phospholipid meets all-trans-retinal: the making of RPE bisretinoids
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Voltage-dependent and -independent titration of specific residues accounts for complex gating of a ClC chloride channel by extracellular protons
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Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins
Structure, function, and biology of SHIP proteins
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Enzymatic characterization of the individual mammalian primase subunits reveals a biphasic mechanism for initiation of DNA replication.
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Specificity of the myotubularin family of phosphatidylinositol-3-phosphatase is determined by the PH/GRAM domain
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Whose end is destruction: cell division and the anaphase-promoting complex.
Three transitions in the RNA polymerase II transcription complex during initiation.
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What was the set of ubiquitin and ubiquitin-like conjugating enzymes in the eukaryote common ancestor?
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Phorbol esters modulate the Ras exchange factor RasGRP3
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Advances in the understanding of cobalamin assimilation and metabolism
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Receptor-mediated endocytosis: the intracellular journey of transferrin and its receptor
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3-Phospho-D-glycerate <=> 2-Phospho-D-glycerate
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pyrophosphate + H2O => 2 orthophosphate [mitochondrial]
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Kinesins move along microtubules consuming ATP
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pyrophosphate + H2O => 2 orthophosphate [cytosolic]
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D-fructose 1,6-bisphosphate <=> dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
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dihydroxyacetone phosphate <=> D-glyceraldehyde 3-phosphate
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Glucose 6-phosphate is isomerized to form fructose-6-phosphate
alpha-D-glucose 6-phosphate <=> D-fructose 6-phosphate
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D-fructose 6-phosphate + ATP => D-fructose 1,6-bisphosphate + ADP
Glyceraldehyde 3 phosphate, NAD+, and orthophosphate react to form 1,3 bisphosphoglycerate and NADH + H+
D-glyceraldehyde 3-phosphate + orthophosphate + NAD+ <=> 1,3-bisphospho-D-glycerate + NADH + H+
1,3-Bisphosphoglycerate and ADP react to form 3-phosphoglycerate and ATP
1,3-bisphospho-D-glycerate + ADP <=> 3-phospho-D-glycerate + ADP
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
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1,3-bisphospho-D-glycerate + NADH + H+ <=> D-glyceraldehyde 3-phosphate + Orthophosphate + NAD+
ATP + 3-Phospho-D-glycerate <=> ADP + 1,3-bisphospho-D-glycerate
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phosphoenolpyruvate + ADP => pyruvate + ATP
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(S)-malate + NAD+ <=> oxaloacetate + NADH + H+
malate + NAD+ <=> oxaloacetate + NADH + H+
oxaloacetate + glutamate <=> aspartate + alpha-ketoglutarate [GOT2]
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aspartate [mitochondrial matrix] + glutamate [cytosol] => aspartate [cytosol] + glutamate [mitochondrial matrix]
Exchange of cytosolic glutamate and mitochondrial aspartate
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aspartate + alpha-ketoglutarate <=> oxaloacetate + glutamate [GOT1]
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Oxaloacetate and GTP react to form phosphoenolpyruvate, CO2, and GDP [cytosol]
oxaloacetate + GTP => phosphoenolpyruvate + GDP + CO2 [cytosol]
oxaloacetate + GTP => phosphoenolpyruvate + GDP + CO2 [mitochondrial matrix]
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phosphoenolpyruvate [mitochondrial matrix] + citrate [cytosol] => phosphoenolpyruvate [cytosol] + citrate [mitochondrial matrix]
Exchange of cytosolic citrate for mitochondrial phosphoenolpyruvate
2-Phospho-D-glycerate <=> 3-Phospho-D-glycerate
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Inflammasome components NALP 1 and 3 show distinct but separate expression profiles in human tissues suggesting a site-specific role in the inflammatory response
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Regulation of actin dynamics for phagocytic cup formation
Emerging role of ISG15 in antiviral immunity
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The helicase DDX41 recognizes the bacterial secondary messengers cyclic di-GMP and cyclic di-AMP to activate a type I interferon immune response
Evidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabilization of tumor necrosis factor alpha mRNA
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N-Acetyl-D-glucosamine 1-phosphate [ChEBI:7125]
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HGSNAT acetylates the terminal N-glucosamine in heparan sulfate
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Alpha-N-acetylglucosaminidase (NAGLU) hydrolyses another N-acetyl-D-glucosamine residue from heparan
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Beta-galactosidase (GLB1) can cleave galactose from the linker chain
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Alpha-N-acetylglucosaminidase (NAGLU) hydrolyses N-acetyl-D-glucosamine residues from heparan sulfate
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HGSNAT acetylates another terminal N-glucosamine in heparan
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Beta-hexosaminidase A (BHEXA) cleaves the terminal GalNAc from small HA fragments
Growing HA is extruded from the cell by ABCC5
addition of diphosphate (PP) to ribose 5-phosphate to form 5'-Phospho-alpha-D-ribose 1-diphosphate (PRPP)
D-ribose 5-phosphate + ATP => 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) + adenosine 5'-monophosphate
D-ribose 5-phosphate + 2'-deoxyadenosine 5'-triphosphate (dATP) => 5-Phospho-alpha-D-ribose 1-diphosphate (PRPP) + 2'-deoxyadenosine 5'-monophosphate
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Beta-hexosaminidase A (BHEXA) cleaves the terminal GalNAc from keratan sulfate
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Beta-galactosidase (GLB1) can cleave galactose from a glycosaminoglycan
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I(1,3,4,5)P4 is dephosphorylated to I(1,3,4)P3 by INPP5[3]/ITPK1 in the cytosol
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I(1,3,4)P3 is phosphorylated to I(1,3,4,5)P4 by ITPK1 in the cytosol
I(1,3,4)P3 is phosphorylated to I(1,3,4,6)P4 by ITPK1 in the cytosol
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I(1,3,4,6)P4 is dephosphorylated to I(1,3,4)P3 by ITPK1 in the cytosol
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I(1,3,4,6)P4 is dephosphorylated to I(3,4,6)P3 by ITPK1 in the cytosol
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I(3,4,6)P3 is phosphorylated to I(1,3,4,6)P4 by ITPK1 in the cytosol
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PI(4,5)P2 is hydrolysed to I(1,4,5)P3 and DAG by cytosolic PLC[2] at the plasma membrane
Beta-hexosaminidase A (BHEXA) cleaves the terminal GalNAc from DS
PI(4,5)P2 is hydrolysed to I(1,4,5)P3 and DAG by PLCD4 at the ER membrane
PI(4,5)P2 is hydrolysed to I(1,4,5)P3 and DAG by tethered PLC[1] at the plasma membrane
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I(1,3,4,5)P4 is dephosphorylated to I(1,4,5)P3 by PTEN in the cytosol
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PGYM b dimer:AMP complex <=> PGYM dimer, b form + 2 AMP
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D-Glucose 1-phosphate <=> alpha-D-Glucose 6-phosphate
Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature
PGYM dimer, b form + 2 AMP <=> PGYM b dimer:AMP complex
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Cloning and expression of human phenylalanyl-tRNA synthetase in Escherichia coli: comparative study of purified recombinant enzymes
Mucin-type O-glycosylation and its potential use in drug and vaccine development
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PGYB b dimer:AMP complex <=> PGYB dimer, b form + 2 AMP
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PGYB dimer, b form + 2 AMP <=> PGYB b dimer:AMP complex
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UTP + D-glucose 1-phosphate <=> pyrophosphate + UDP-glucose
alpha-D-Glucose 6-phosphate <=> D-Glucose 1-phosphate
D-fructose 6-phosphate <=> alpha-D-Glucose 6-phosphate
D-fructose 1,6-bisphosphate + H2O => D-fructose 6-phosphate + orthophosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate <=> D-fructose 1,6-bisphosphate
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D-glyceraldehyde 3-phosphate <=> dihydroxyacetone phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate <=> D-erythrose 4-phosphate + D-fructose 6-phosphate
Cytoplasmic localization of human cdc25C during interphase requires an intact 14-3-3 binding site.
D-fructose 6-phosphate + D-erythrose 4-phosphate <=> sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribulose 5-phosphate <=> ribose 5-phosphate
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ribose 5-phosphate <=> D-ribulose 5-phosphate
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Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex
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Role of semaphorins during axon growth and guidance
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D-ribulose 5-phosphate <=> xylulose 5-phosphate
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6-phospho-D-gluconate + NADP+ => D-ribulose 5-phosphate + CO2 + NADPH + H+
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xylulose 5-phosphate <=> D-ribulose 5-phosphate
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D-fructose 1-phosphate <=> D-glyceraldehyde + dihydroxyacetone phosphate
D-glucono-1,5-lactone 6-phosphate + H2O => 6-phospho-D-gluconate
alpha-D-glucose 6-phosphate + NADP+ => D-glucono-1,5-lactone 6-phosphate + NADPH + H+
I4P is dephosphorylated to Ins by IMPA1/2 in the cytosol
I1P is dephosphorylated to Ins by IMPA1/2 in the cytosol
Glc6P is isomerised to I3P by ISYNA1 in the cytosol
Non-kinase second-messenger signaling: new pathways with new promise
I3P is dephosphorylated to Ins by IMPA1/2 in the cytosol
NPC1L1 + ezetimibe => NPC1L1:ezetimibe complex
A human transporter protein that mediates the final excretion step for toxic organic cations
Transport of Citrate from Mitochondrial Matrix to cytosol
2-acylglycerol + H2O -> glycerol + fatty acid
Mucopolysaccharidosis IV A: molecular cloning of the human N-acetylgalactosamine-6-sulfatase gene (GALNS) and analysis of the 5'-flanking region
Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1
acetyl-CoA + bicarbonate + ATP => malonyl-CoA + H2O + ADP + orthophosphate
Formation of Malonyl-CoA from Acetyl-CoA (liver)
Generation of Cytoplasmic Acetyl CoA from Citrate
palmitate + CoASH + ATP => palmitoyl-CoA + AMP + pyrophosphate + H2O [ACSL1]
Conversion of palmitic acid to palmitoyl-CoA
Human adrenoleukodystrophy protein and related peroxisomal ABC transporters interact with the peroxisomal assembly protein PEX19p
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I(1,4,5)P3 is phosphorylated to I(1,3,4,5)P4 by IPMK in the nucleus
I(1,3,4,5)P4 is phosphorylated to I(1,3,4,5,6)P5 by IPMK in the nucleus
I(1,3,4,6)P4 is phosphorylated to I(1,3,4,5,6)P5 by IPMK in the nucleus
I(1,4,5,6)P4 is phosphorylated to I(1,3,4,5,6)P5 by IPMK in the nucleus
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5-PP-IP5 is phosphorylated to 5-PPP-IP5 by IP6K1/2 in the nucleus
IP6 is phosphorylated to 5-PP-IP5 by IP6K1/2 in the nucleus
I(1,3,4,5,6)P5 is dephosphorylated to I(3,4,5,6)P4 by ITPK1 in the cytosol
The visual cycle of the cone photoreceptors of the retina
1-PP-IP5 is phosphorylated to 1,5-(PP)2-IP4 by IP6K1/2 in the nucleus
I(1,3,4,5,6)P5 is phosphorylated to IP6 by IPPK (IP5-2K) in the nucleus
5-PP-IP4 is phosphorylated to 1,5-(PP)2-IP3 by IP6K1/2 in the nucleus
I(1,3,4,5,6)P5 is phosphorylated to 5-PP-IP4 by IP6K1/2 in the nucleus
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I(1,3,4,5,6)P5 is phosphorylated to 5-PP-IP4 by IP6K1/3 in the cytosol
I(3,4,5,6)P4 is phosphorylated to I(1,3,4,5,6)P5 by ITPK1 in the cytosol
I(1,3,4,5,6)P5 is phosphorylated to IP6 by IPPK in the cytosol
RNA Polymerase I, RNA Polymerase III, and Mitochondrial Transcription
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I(1,4,5)P3 is dephosphorylated to I(1,4)P2 by INPP5(4) in the cytosol
IP6 is dephosphorylated to I(1,2,4,5,6)P5 by MINPP1 in the ER lumen
I(1,3,4,5,6)P5 is dephosphorylated to I(1,4,5,6)P4 by MINPP1 in the ER lumen
I(1,3,4,5)P4 is dephosphorylated to I(1,4,5)P3 by MINPP1 in the ER lumen
1-PP-IP5 is phosphorylated to 1,5-(PP)2-IP4 by IP6K1/3 in the cytosol
5-PP-IP5 is phosphorylated to 5-PPP-IP5 by IP6K1/3 in the cytosol
IP6 is phosphorylated to 5-PP-IP5 by IP6K1/3 in the cytosol
1-PP-IP4 is phosphorylated to 1,5-(PP)2-IP3 by IP6K1/3 in the cytosol
Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases: differential lability and tissue distribution
Mechanism of RNA polymerase II--specific initiation of transcription in vitro: ATP requirement and uncapped runoff transcripts.
Neuronal phosphoproteins. Mediators of signal transduction
Human ESCRT-II complex and its role in human immunodeficiency virus type 1 release
History of the events leading to the formulation of the apoptosis concept
Functions of replication factor C and proliferating-cell nuclear antigen: functional similarity of DNA polymerase accessory proteins from human cells and bacteriophage T4.
Gastrin-CREB signalling pathway via PKC and MAPK
Recognition and association of DNA glycosylase with site containing an affected purine
Sterol transfer by ABCG5 and ABCG8: in vitro assay and reconstitution
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
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ChEBI:17526 1-phosphatidyl-1D-myo-inositol 4-phosphates
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Molecular mechanism of phase I and phase II drug-metabolizing enzymes: implications for detoxification
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The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair.
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gamma-L-Glutamyl-L-cysteine [ChEBI:17515]
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Zinc efflux and compartmentalization by the SLC30 family
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Characterization of human RhCG and mouse Rhcg as novel nonerythroid Rh glycoprotein homologues predominantly expressed in kidney and testis
Complementary regulation of TBC1D1 and AS160 by growth factors, insulin and AMPK activators
RasGRP, a Ras guanyl nucleotide- releasing protein with calcium- and diacylglycerol-binding motifs
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Identification of a novel gene, FGFR1OP2, fused to FGFR1 in 8p11 myeloproliferative syndrome
Synthesis of Prostaglandins (PG) and Thromboxanes (TX)
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Characterisation of Cdc25B localisation and nuclear export during the cell cycle and in response to stress
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Similar regulation of human inducible nitric-oxide synthase expression by different isoforms of the RNA-binding protein AUF1
SLC4 base (HCO3 -, CO3 2-) transporters: classification, function, structure, genetic diseases, and knockout models
Regulatory proteins of R-Ras, TC21/R-Ras2, and M-Ras/R-Ras3
Metal transporters in intestine and brain: their involvement in metal-associated neurotoxicities
Expression and characterization of human mitochondrial ferredoxin reductase in Escherichia coli
Molecular mechanism of ADP-ribose hydrolysis by human NUDT5 from structural and kinetic studies
Energy dependent regulation of mTOR by LKB1-AMPK
Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant
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Transport of phosphoenolpyruvate by the tricarboxylate transporting system in mammalian mitochondria
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Both V(D)J recombination and radioresistance require DNA-PK kinase activity, though minimal levels suffice for V(D)J recombination.
Role of the Zn(2+) motif of E1 in SUMO adenylation
The Bcl2 family: regulators of the cellular life-or-death switch
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Kinetics and equilibria of pyrimidine nucleoside monophosphate kinase from human erythrocytes
Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases
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Allelism, non-allelism, and genetic compounds among the mucopolysaccharidoses
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Transport of vitamins, nucleosides, and related molecules
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Novel mutations in 3-phosphoglycerate dehydrogenase (PHGDH) are distributed throughout the protein and result in altered enzyme kinetics
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SUMO-specific proteases: a twist in the tail
Human microRNAs are processed from capped, polyadenylated transcripts that can also function as mRNAs
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Negative regulation of mast cell signaling and function by the adaptor LAB/NTAL
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Human mitochondrial pyrophosphatase: cDNA cloning and analysis of the gene in patients with mtDNA depletion syndromes
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Positive and negative regulation of FcepsilonRI-mediated signaling by the adaptor protein LAB/NTAL
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pAMPK inactivates ACC2 inhibiting malonyl-CoA synthesis
Structural characterization of a human cytosolic NMN/NaMN adenylyltransferase and implication in human NAD biosynthesis
1,2-diacyl-glycerol + acyl-CoA => triacylglycerol + CoASH [DGAT1]
Conversion of Diacylglycerol to Triacylglycerol [DGAT1]
Formation of Malonyl-CoA from Acetyl-CoA (muscle)
lysophosphatidic acid + fatty acyl CoA => phosphatidic acid + CoA (1)
1-acyl-glycerol 3-phosphate + acyl-CoA => 1,2-diacyl-glycerol 3-phosphate + CoASH
1-acyl LPA is acylated to PA by AGPAT (LPAAT)
Cloning and characterization of a novel mammalian zinc transporter, zinc transporter 5, abundantly expressed in pancreatic beta cells
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1,2-diacyl-glycerol 3-phosphate + H2O => 1,2-diacyl-glycerol + orthophosphate
Conversion of Phosphatidic Acid to Diacylglycerol
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Conversion of Glycerol to Glycerol-3-phosphate
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Conversion of glycerol-3-phosphate to lysophosphatidic acid
glycerol 3-phosphate + acyl-CoA => 1-acylglycerol 3-phosphate + CoASH [ER membrane-associated]
palmitate + CoASH + ATP => palmitoyl-CoA + AMP + pyrophosphate + H2O [ACSL6]
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trans-octadec-2-enoyl-CoA + NADPH + H+ => stearoyl-CoA + NADP+
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PIP kinase Igamma is the major PI(4,5)P(2) synthesizing enzyme at the synapse
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palmitate + CoASH + ATP => palmitoyl-CoA + AMP + pyrophosphate + H2O [ACSL5]
HMG CoA => acetoacetic acid + acetyl CoA
Oxidized LDL-induced endolysosomal phospholipidosis and enzymatically modified LDL-induced foam cell formation determine specific lipid species modulation in human macrophages
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The molecular basis of glutamate formiminotransferase deficiency
acetoacetyl-CoA+acetyl-CoA => HMG-CoA + CoASH
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propionyl-CoA + CO2 + ATP <=> D-methylmalonyl-CoA + ADP + orthophosphate
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D-methylmalonyl-CoA <=> L-methylmalonyl-CoA
Plexin signaling via off-track and rho family GTPases
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MUT transfers adenosyl group from AdoCbl to L-MM-CoA
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Regulation and Function of the RasGRP Family of Ras Activators in Blood Cells
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3-ketohexacosanoyl-CoA + CoASH => tetracosanoyl-CoA + acetyl-CoA
3-hydroxyhexacosanoyl-CoA + NAD+ => 3-ketohexacosanoyl-CoA + NADH + H+
PTEN loss in the continuum of common cancers, rare syndromes and mouse models
The control of male fertility by spermatozoan ion channels
trans-2,3-dehydrohexacosanoyl-CoA + H2O => 3-hydroxyhexacosanoyl-CoA
Mammalian ABC transporters in health and disease
The role of calmodulin recruitment in Ca2+ stimulation of adenylyl cyclase type 8
Gly-3-P+FAD->DHAP+FADH2 (catalyzed by mitochondrial Gly-Phos dehydrogenase)
PMP34-mediated exchange of cytosolic ATP for peroxisomal AMP
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acetoacetate + succinyl-CoA <=> acetoacetyl-CoA + succinate
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3-hydroxypristanoyl-CoA + NAD+ => 3-ketoxypristanoyl-CoA + NADH + H+
Mechanism and regulation of human non-homologous DNA end-joining.
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Peroxisomal uptake of very long-chain fatty acyl CoA
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2-hydroxyphytanoyl-CoA => pristanal + formyl-CoA
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trans-2,3-dehydropristanoyl-CoA + H2O => 3-hydroxypristanoyl-CoA
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Mevalonate-5-pyrophosphate is decarboxylated
Addition of isopentenyl pyrophosphate to DMAPP
Isopentenyl pyrophosphate rearranges to dimethylallyl pyrophosphate
Phosphatidylinositol 3-phosphate-interacting domains in PIKfyve. Binding specificity and role in PIKfyve. Endomenbrane localization
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palmitoyl-CoA + DHAP => 1-palmitoylglycerone phosphate + CoASH
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1-palmitoylglycerone phosphate + hexadecanol => O-hexadecylglycerone phosphate + palmitate
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isocitrate + NADP+ => 2-oxoglutarate + CO2 + NADPH + H+
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malonyl-CoA is decarboxylated to acetyl-CoA in peroxisome
Condensation of acetyl CoA with acetoacetyl CoA to form HMG-CoA
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Reduction of HMG-CoA produces mevalonate
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Mevalonate is phosphorylated to mevalonate-5-phosphate
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4-methyl,4-carboxycholesta-8(9),24-dien-3beta-ol is decarboxylated and oxidized to form 4-methylcholesta-8(9),24-dien-3-one
4-methyl,4-carboxycholesta-8(9),24-dien-3beta-ol + NAD+ => 4-methylcholesta-8(9),24-dien-3-one + CO2 + NADH + H+
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4-methylcholesta-8(9),24-dien-3beta-ol + 3 NADPH + 3 H+ + 3 O2 => 4-carboxycholesta-8(9),24-dien-3beta-ol + 3 NADP+ + 4 H2O
4-methylcholesta-8(9),24-dien-3beta-ol is oxidized to 4-carboxycholesta-8(9),24-dien-3beta-ol
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4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + NADPH + H+ => 4,4-dimethylcholesta-8(9),24-dien-3beta-ol + NADP+ [TM7SF2]
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol is reduced to 4,4-dimethylcholesta-8(9),24-dien-3beta-ol [TM7SF2]
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4,4-dimethylcholesta-8(9),24-dien-3beta-ol + 3 NADPH + 3 H+ + 3 O2 => 4-methyl,4-carboxycholesta-8(9),24-dien-3beta-ol + 3 NADP+ + 4 H2O
4,4-dimethylcholesta-8(9),24-dien-3beta-ol is oxidized to 4-methyl,4-carboxycholesta-8(9),24-dien-3beta-ol
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4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + NADPH + H+ => 4,4-dimethylcholesta-8(9),24-dien-3beta-ol + NADP+ [LBR]
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol is reduced to 4,4-dimethylcholesta-8(9),24-dien-3beta-ol [LBR]
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lanosterol + 3 NADPH + 3 H+ + 3 O2 => 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + 3 NADP+ + 4 H2O + formate
Lanosterol is oxidatively demethylated to 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol
Squalene 2,3-epoxide cyclizes, forming lanosterol
Reduction of presqualene diphosphate to form squalene
Two FPP molecules dimerize to form presqualene diphosphate
Another isopentenyl pyrophosphate is added to geranyl pyrophosphate
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3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA (THCA-CoA) is hydrated to (24R, 25R) 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA
3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA + H2O => (24R, 25R) 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA
Membrane-bound enzymes of cholesterol synthesis from lanosterol
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25(S) 3alpha,7alpha-dihydroxy-5beta-cholest-24-enoyl-CoA is hydrated to (24R, 25R) 3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA
25(S) 3alpha,7alpha-dihydroxy-5beta-cholest-24-enoyl-CoA + H2O => (24R, 25R) 3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA
Cholesterol, hydroxycholesterols, and bile acids
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(24R, 25R) 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA + NAD+ => 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-one-CoA + NADH + H+
(24R, 25R) 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA is oxidized to 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-one-CoA
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(24R, 25R) 3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA + NAD+ => 3alpha,7alpha-dihydroxy-5beta-cholest-24-one-CoA + NADH + H+
(24R, 25R) 3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA is oxidized to 3alpha,7alpha-dihydroxy-5beta-cholest-24-one-CoA
Familial deficiency of glutathione reductase in human blood cells
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5beta-cholestan-7alpha-ol-3-one+ NADPH + H+ => 5beta-cholestan-3alpha, 7alpha-diol + NADP+
5beta-cholestan-7alpha-ol-3-one is reduced to 5beta-cholestan-3alpha, 7alpha-diol
5Beta-cholesten-7alpha, 12alpha-diol-3-one + NADPH + H+ => 5beta-cholestan-3alpha, 7alpha, 12alpha-triol + NAPDP+
5Beta-cholesten-7alpha, 12alpha-diol-3-one is reduced to 5beta-cholestan-3alpha, 7alpha, 12alpha-triol
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4-cholesten-7alpha-ol-3-one + NADPH + H+ => 5beta-cholestan-7alpha-ol-3-one + NADP+
4-cholesten-7alpha-ol-3-one is reduced to 5beta-cholestan-7alpha-ol-3-one
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Zymosterol is isomerized to cholesta-7,24-dien-3beta-ol
Zymosterol => cholesta-7,24-dien-3beta-ol
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4-carboxycholesta-8(9),24-dien-3beta-ol is decarboxylated and oxidized to form cholesta-8(9),24-dien-3-one (zymosterone)
4-carboxycholesta-8(9),24-dien-3beta-ol + NAD+ => cholesta-8(9),24-dien-3-one (zymosterone) + CO2 + NADH + H+
4-cholesten-7alpha, 12alpha-diol-3-one + NADPH + H+ => 5beta-cholesten-7alpha,12alpha-diol-3-one + NADP+
4-cholesten-7alpha, 12alpha-diol-3-one is reduced to 5beta-cholesten-7alpha, 12alpha-diol-3-one
cholesta-5,7,24-trien-3beta-ol + NADPH + H+ => desmosterol + NADP+
Cholesta-5,7,24-trien-3beta-ol is reduced to desmosterol
A novel B lymphocyte-associated adaptor protein, Bam32, regulates antigen receptor signaling downstream of phosphatidylinositol 3-kinase
Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation
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4-cholesten-7alpha,27-diol-3-one + NADPH + H+ => 5beta-cholestan-7alpha,27-diol-3-one + NADP+
4-cholesten-7alpha,27-diol-3-one is reduced to 5beta-cholestan-7alpha,27-diol-3-one
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5Beta-cholestan-7alpha,12alpha,27-triol-3-one + NADPH + H+ => 5beta-cholestan-3alpha,7alpha,12alpha,27-tetrol + NAPDP+
5Beta-cholestan-7alpha,12alpha,27-triol-3-one is reduced to 5beta-cholestan-3alpha,7alpha,12alpha,27-tetrol
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1-acyl LPA is acylated to PA by AGPAT5 (OM)
PC is hydrolyzed to PA and choline by PLD1/2
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5beta-cholestan-7alpha,27-diol-3-one+ NADPH + H+ => 5beta-cholestan-3alpha,7alpha,27-triol + NADP+
5beta-cholestan-7alpha,27-diol-3-one is reduced to 5beta-cholestan-3alpha,7alpha,27-triol
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DHAP is converted to 1-acyl GO3P by GNPAT
5beta-cholestan-7alpha,24(S)-diol-3-one+ NADPH + H+ => 5beta-cholestan-3alpha,7alpha,24(S)-triol + NADP+
5beta-cholestan-7alpha,24(S)-diol-3-one is reduced to 5beta-cholestan-3alpha,7alpha,24(S)-triol
5Beta-cholestan-7alpha,12alpha,24(S)-triol-3-one + NADPH + H+ => 5beta-cholestan-3alpha,7alpha,12alpha,24(S)-tetrol + NAPDP+
5Beta-cholestan-7alpha,12alpha,24(S)-triol-3-one is reduced to 5beta-cholestan-3alpha,7alpha,12alpha,24(S)-tetrol
4-cholesten-7alpha,24(S)-diol-3-one + NADPH + H+ => 5beta-cholestan-7alpha,24(S)-diol-3-one + NADP+
4-cholesten-7alpha,24(S)-diol-3-one is reduced to 5beta-cholestan-7alpha,24(S)-diol-3-one
4-cholesten-7alpha,12alpha,24(S)-triol-3-one + NADPH + H+ => 5beta-cholestan-7alpha,12alpha,24(S)-triol-3-one + NADP+
4-cholesten-7alpha,12alpha,24(S)-triol-3-one is reduced to 5beta-cholestan-7alpha,12alpha,24(S)-triol-3-one
Complete amino acid sequence of human phosphoglycerate kinase. Isolation and amino acid sequence of tryptic peptides.
4-cholesten-7alpha,12alpha,27-triol-3-one + NADPH + H+ => 5beta-cholestan-7alpha,12alpha,27-triol-3-one + NADP+
4-cholesten-7alpha,12alpha,27-triol-3-one is reduced to 5beta-cholestan-7alpha,12alpha,27-triol-3-one
SRP-dependent cotranslational protein targeting to membrane
Asparaginyl endopeptidase: case history of a class II MHC compartment protease
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STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1
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CDP-ETA and DAG are converted to PE by CEPT1/EPT1
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PE is hydrolyzed to 1-acyl LPE by PLA2[2]
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GPETA is hydrolyzed to ETA and G3P by GPCPD1
2-MAG is hydrolyzed to fatty acid and glycerol by MGLL
PETA and CTP are condensed to CDP-ETA by PCY2
ETA is phosphorylated to PETA by CHK/ETNK
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cAMP sensor Epac as a determinant of ATP-sensitive potassium channel activity in human pancreatic beta cells and rat INS-1 cells
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Mechanisms of MHC class I-restricted antigen processing and cross-presentation
Lysosomes in iron metabolism, ageing and apoptosis
Cross-presentation: underlying mechanisms and role in immune surveillance
Discovery of molecular and catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases. An expanding Nudt family
Atherosclerosis and sterol 27-hydroxylase: evidence for a role of this enzyme in elimination of cholesterol from human macrophages
PCho and CTP are condensed to CDP-Cho by PCYT1 dimer
CDP-Cho and DAG are converted to PC by CEPT1 at the ER membrane
PC is hydrolyzed to 1-acyl LPC by PLA2[5]
Mapping of the rod photoreceptor ABC transporter (ABCR) to 1p21-p22.1 and identification of novel mutations in Stargardt's disease
PI:PITPNB is transported from the ER membrane to the Golgi membrane
CDP-Cho and DAG are converted to PC by CHPT1 at the Golgi membrane
PC:PITPNB is transported from the Golgi membrane to the ER membrane
The SLC20 family of proteins: dual functions as sodium-phosphate cotransporters and viral receptors
Molecular physiology and pathology of the nucleotide sugar transporter family (SLC35)
1-acyl LPC is hydrolyzed to GPCho by PLA2[8]
2-acyl LPC is hydrolyzed to GPCho by PLA2[8]
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
Stoichiometric and reversible phosphorylation of a 46-kDa protein in human platelets in response to cGMP- and cAMP-elevating vasodilators
A new fused transcript in Philadelphia chromosome positive acute lymphocytic leukaemia
Assembly of the human origin recognition complex.
Human cataract lens membrane at subnanometer resolution
Antigen processing and presentation by the class I major histocompatibility complex
Mapping iron binding sites on human frataxin: implications for cluster assembly on the ISU Fe-S cluster scaffold protein
Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis
Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor
Targeting death and decoy receptors of the tumour-necrosis factor superfamily
Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, and p95.
The proline-rich region of Vav binds to Grb2 and Grb3-3
Human Pat1b connects deadenylation with mRNA decapping and controls the assembly of processing bodies
The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate kinase
Structural requirements for PAK activation by Rac GTPases
Cloning of the human cDNA which can complement the defect of the yeast mannosyltransferase I-deficient mutant alg 1
Control of elongation by RNA polymerase II.
Guanylate kinases from human erythrocytes, hog brain, and rat liver
Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family.
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Trans-synaptic transmission of vesicular Wnt signals through Evi/Wntless
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Formation of RNA Pol II elongation complex
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(5Z,13E)-(15S)-9alpha,15-Dihydroxy-11-oxoprosta-5,13-dienoate [ChEBI:246]
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
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(5Z)-(15S)-11alpha-Hydroxy-9,15-dioxoprostanoate [ChEBI:244]
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Phosphorylation of hUPF1 induces formation of mRNA surveillance complexes containing hSMG-5 and hSMG-7
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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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An insight into the mechanism of human cysteine dioxygenase. Key roles of the thioether-bonded tyrosine-cysteine cofactor
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The microsomal cardiolipin remodeling enzyme acyl-CoA lysocardiolipin acyltransferase is an acyltransferase of multiple anionic lysophospholipids
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Gelsolin-related amyloidosis. Identification of the amyloid protein in Finnish hereditary amyloidosis as a fragment of variant gelsolin
4,4-Dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol [ChEBI:1743]
1D-myo-Inositol 1,4-bisphosphate [ChEBI:812]
Novel molecular defects of the delta-aminolevulinate dehydratase gene in a patient with inherited acute hepatic porphyria
Transcription factors IIE and IIH and ATP hydrolysis direct promoter clearance by RNA polymerase II.
Mouse, but not Human STING, Binds and Signals in Response to the Vascular Disrupting Agent 5,6-Dimethylxanthenone-4-Acetic Acid
Molecular basis for ADP-induced platelet activation. II. The P2Y1 receptor mediates ADP-induced intracellular calcium mobilization and shape change in platelets
Two distinct mechanisms for actin capping protein regulation--steric and allosteric inhibition
Chain gangs: new aspects of hyaluronan metabolism
ERAAP synergizes with MHC class I molecules to make the final cut in the antigenic peptide precursors in the endoplasmic reticulum
MAP kinase pathway-dependent phosphorylation of the L1-CAM ankyrin binding site regulates neuronal growth
Functional studies of human intestinal alkaline sphingomyelinase by deglycosylation and mutagenesis
Human Rad51 protein can form homologous joints in the absence of net strand exchange.
Seven novel mutations in the methylenetetrahydrofolate reductase gene and genotype/phenotype correlations in severe methylenetetrahydrofolate reductase deficiency
Characterization of ceramide synthesis. A dihydroceramide desaturase introduces the 4,5-trans-double bond of sphingosine at the level of dihydroceramide
Signaling, cytoskeletal and membrane mechanisms regulating GLUT4 exocytosis
Molecular basis of an adult form of beta-hexosaminidase B deficiency with motor neuron disease
Multiple phosphoinositide 3-kinase-dependent steps in activation of protein kinase B
Progesterone from the cumulus cells is the sperm chemoattractant secreted by the rabbit oocyte cumulus complex
Negative regulation of dE2F1 by cyclin-dependent kinases controls cell cycle timing
Expression, purification, and kinetic constants for human and Escherichia coli pyridoxal kinases
Unstable kinetochore-microtubule capture and chromosomal instability following deletion of CENP-E
Prog Nucleic Acid Res Mol Biol 42:259-287
Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases
Facilitative Na+-independent glucose transporters
endoplasmic reticulum quality control compartment
Characterization and tRNA recognition of mammalian mitochondrial seryl-tRNA synthetase
Association of licensing factors with the pre-replicative complex
GABAA receptors: properties and trafficking
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
Antigen processing and presentation in human muscle: cathepsin S is critical for MHC class II expression and upregulated in inflammatory myopathies
RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease
Expression, purification and kinetic properties of human recombinant phospholipase C delta 3
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The narrow substrate specificity of human tyrosine aminotransferase--the enzyme deficient in tyrosinemia type II
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Structural mechanism of RNA recognition by the RIG-I-like receptors
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G protein betagamma subunits: central mediators of G protein-coupled receptor signaling
Thioredoxin-like domain of human kappa class glutathione transferase reveals sequence homology and structure similarity to the theta class enzyme
Identification of a dehydrogenase acting on D-2-hydroxyglutarate
Rabbit small intestinal trehalase. Purification, cDNA cloning, expression, and verification of glycosylphosphatidylinositol anchoring.
NF-kappaB p52, RelB and c-Rel are transported into the nucleus via a subset of importin alpha molecules
(5-Deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt
Phosphorylation inhibits guanine nucleotide exchange on eukaryotic initiation factor 2.
Dehydroascorbic acid transport by GLUT4 in Xenopus oocytes and isolated rat adipocytes
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5-Formiminotetrahydrofolate [ChEBI:15639]
Desaturation and chain elongation of n - 3 and n - 6 polyunsaturated fatty acids in the human CaCo-2 cell line
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Structure and transcription of a human gene for H1 RNA, the RNA component of human RNase P
xanthosine 5'-monophosphate [ChEBI:15652]
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Piccolo, a Ca2+ sensor in pancreatic beta-cells. Involvement of cAMP-GEFII.Rim2.Piccolo complex in cAMP-dependent exocytosis
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Electron microscopic observation and single-stranded DNA binding activity of the Mcm4,6,7 complex.
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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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(S)-2-Methyl-3-oxopropanoyl-CoA [ChEBI:15466]
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(R)-2-Methyl-3-oxopropanoyl-CoA [ChEBI:15465]
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Distribution of aquaporin water channels AQP1 and AQP5 in the ductal system of the human pancreas
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(S)-3-Hydroxy-3-methylglutaryl-CoA [ChEBI:15467]
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Core exosome-independent roles for Rrp6 in cell cycle progression
Signaling by distinct classes of phosphoinositide 3-kinases
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Analysis of the biogenesis of heparan sulfate acetyl-CoA:alpha-glucosaminide N-acetyltransferase provides insights into the mechanism underlying its complete deficiency in mucopolysaccharidosis IIIC
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Receptor for advanced glycation end products (RAGE) regulates sepsis but not the adaptive immune response
Biochemical genetics of the pentose phosphate cycle: human ribose 5-phosphate isomerase (RPI) and ribulose 5-phosphate 3-epimerase (RPE)
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(2S,3S)-3-Hydroxy-2-methylbutanoyl-CoA [ChEBI:15449]
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Phospholipase C-gamma as a signal-transducing element
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Phosphorylation of acyclovir (acycloguanosine) monophosphate by GMP kinase
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Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2
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A Rap guanine nucleotide exchange factor enriched highly in the basal ganglia
AMPK phosphorylation of raptor mediates a metabolic checkpoint
Sphingosine-1-phosphate lyase in development and disease: sphingolipid metabolism takes flight
Synthesis and recycling of tetrahydrobiopterin in endothelial function and vascular disease
Genetic heterogeneity and clinical variability in the Sanfilippo syndrome (types A, B, and C)
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2'-deoxyadenosine 5'-monophosphate [ChEBI:17713]
Novel mutations in COX15 in a long surviving Leigh syndrome patient with cytochrome c oxidase deficiency
Epidermal Growth Factor Receptor (EGFR) signaling
Structural and functional characterization of human NAD kinase
Human geranylgeranyl diphosphate synthase. cDNA cloning and expression.
Formation of the 3' end of histone mRNA.
Ten years on: mediation of cell death by the common neurotrophin receptor p75(NTR)
Molecular basis of GM1 gangliosidosis and Morquio disease, type B. Structure-function studies of lysosomal beta-galactosidase and the non-lysosomal beta-galactosidase-like protein
The bipolar mitotic kinesin Eg5 moves on both microtubules that it crosslinks
Initiating DNA synthesis: from recruiting to activating the MCM complex.
Human CDC45 protein binds to minichromosome maintenance 7 protein and the p70 subunit of DNA polymerase alpha.
Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase
Glycosylation and palmitoylation of Wnt-3a are coupled to produce an active form of Wnt-3a
ExoS Rho GTPase-activating protein activity stimulates reorganization of the actin cytoskeleton through Rho GTPase guanine nucleotide disassociation inhibitor
Identification and characterization of human Golgi nucleotide sugar transporter SLC35D2, a novel member of the SLC35 nucleotide sugar transporter family
Initiation of eukaryotic DNA replication: origin unwinding and sequential chromatin association of Cdc45, RPA, and DNA polymerase alpha.
Distinct stem cell myeloproliferative/T lymphoma syndromes induced by ZNF198-FGFR1 and BCR-FGFR1 fusion genes from 8p11 translocations
Phosphoinositide 3-kinase in T cell activation and survival
Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm)
The role of EF-hand domains and C2 domain in regulation of enzymatic activity of phospholipase Czeta
Phospholipase Cgamma activates Ras on the Golgi apparatus by means of RasGRP1
Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases
The canonical Notch signaling pathway: unfolding the activation mechanism
Cloning of a human gene, PIG-F, a component of glycosylphosphatidylinositol anchor biosynthesis, by a novel expression cloning strategy
The CCT/TRiC chaperonin is required for maturation of sphingosine kinase 1
G(12)/G(13)-mediated signalling in mammalian physiology and disease
Fragmentation and dispersal of the pericentriolar Golgi complex is required for entry into mitosis in mammalian cells
Tandem phosphorylation of serine 221 and 318 by PKC{delta} coordinates mRNA binding and nucleo-cytoplasmic shuttling of HuR
Insights into lysosomal cobalamin trafficking: lessons learned from cblF disease
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Ubiquitin-dependent degradation of Cyclin D1
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A second mammalian N-myristoyltransferase
Studies on the initiation and elongation reactions in the simian virus 40 DNA replication system.
(5Z,13E)-11alpha-Hydroxy-9,15-dioxoprost-13-enoate [ChEBI:247]
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Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
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alpha-D-Glucose 6-phosphate [ChEBI:17665]
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Distinct patterns of bidirectional regulation of mammalian adenylyl cyclases
Amplification and kinetics of the activation steps in phototransduction
RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides
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PIG-V involved in transferring the second mannose in glycosylphosphatidylinositol
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The gene mutated in l-2-hydroxyglutaric aciduria encodes l-2-hydroxyglutarate dehydrogenase
Human platelet-derived mitogens. II. Subcellular localization of insulinlike growth factor I to the alpha-granule and release in response to thrombin.
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Transport of glucose and other sugars, bile salts and organic acids, metal ions and amine compounds
Expression of human asparagine synthetase in Escherichia coli
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Activation of p34cdc2 protein kinase by microinjection of human cdc25C into mammalian cells. Requirement for prior phosphorylation of cdc25C by p34cdc2 on sites phosphorylated at mitosis.
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Zinc influx into cells by the SLC39 gene family
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A theory of marginotomy. The incomplete copying of template margin in enzymic synthesis of polynucleotides and biological significance of the phenomenon.
Human origin recognition complex large subunit is degraded by ubiquitin-mediated proteolysis after initiation of DNA replication.
Formation of the active cofactor, UDP-glucuronate
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Distinct flippases translocate glycerophospholipids and oligosaccharide diphosphate dolichols across the endoplasmic reticulum
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The dissociation of cohesin from chromosomes in prophase is regulated by Polo-like kinase
The human solute carrier gene SLC35B4 encodes a bifunctional nucleotide sugar transporter with specificity for UDP-xylose and UDP-N-acetylglucosamine
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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Regulation of enterocyte apoptosis by acyl-CoA synthetase 5 splicing
Cori Cycle (interconversion of glucose and lactate)
Organic anion transport is the primary function of the SLC17/type I phosphate transporter family
The human sugar-phosphate/phosphate exchanger family SLC37
Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms
A human homolog of the Saccharomyces cerevisiae REV3 gene, which encodes the catalytic subunit of DNA polymerase zeta.
PIK3R1 (p85?) is somatically mutated at high frequency in primary endometrial cancer
Requirement of the MRN complex for ATM activation by DNA damage.
DNA replication control through interaction of E2F-RB and the origin recognition complex.
[Exchange between extra- and intramitochondrial adenine nucleotides]
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
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Identification of the expressed form of human cytosolic phospholipase A2beta (cPLA2beta): cPLA2beta3 is a novel variant localized to mitochondria and early endosomes
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Dolichyl phosphate D-mannose [ChEBI:4694]
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Dolichyl beta-D-glucosyl phosphate [ChEBI:4689]
The role of calcium-independent phospholipase A2 in cardiolipin remodeling in the spontaneously hypertensive heart failure rat heart
Crystal structure of human AUH protein, a single-stranded RNA binding homolog of enoyl-CoA hydratase
Cloning and characterization of a pH-sensing regulatory factor that modulates transport activity of the human H+/peptide cotransporter, PEPT1
WNT secretion and signalling in human disease
Leukocyte chemotactic factor 2: A novel renal amyloid protein
The class II phosphoinositide 3-kinase PI3K-C2alpha is concentrated in the trans-Golgi network and present in clathrin-coated vesicles
M-ABC2, a new human mitochondrial ATP-binding cassette membrane protein
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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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Orc6 involved in DNA replication, chromosome segregation, and cytokinesis.
Purification and functional characterization of aquaporin-8
A mutation in GLUT2, not in phosphorylase kinase subunits, in hepato-renal glycogenosis with Fanconi syndrome and low phosphorylase kinase activity
Two forms of Wilson disease protein produced by alternative splicing are localized in distinct cellular compartments
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The expanding role of the ER translocon in membrane protein folding
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Regulation of human separase by securin binding and autocleavage
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Control of muscle ryanodine receptor calcium release channels by proteins in the sarcoplasmic reticulum lumen
3-dehydro-4-methylzymosterol [ChEBI:50593]
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Adenosine 3',5'-bisphosphate [ChEBI:17985]
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D-myo-Inositol 3,4,5,6-tetrakisphosphate
1D-myo-Inositol 3,4,5,6-tetrakisphosphate [ChEBI:813]
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Differential recognition by CD28 of its cognate counter receptors CD80 (B7.1) and B70 (B7.2): analysis by site directed mutagenesis
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Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation
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Role of human cytochrome P450 1A1, 1A2, 1B1, and 3A4 in the 2-, 4-, and 16alpha-hydroxylation of 17beta-estradiol
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Surprising versatility of Na+-glucose cotransporters: SLC5
Interaction of Sororin protein with polo-like kinase 1 mediates resolution of chromosomal arm cohesion
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The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene
Direct phosphorylation of IkappaB by IKKalpha and IKKbeta: discrimination between free and NF-kappaB-bound substrate
The secondary structure of calcineurin regulatory region and conformational change induced by calcium/calmodulin binding
Clinical and biochemical manifestations of hyaluronidase deficiency
beta-D-galactosyl-(1->4)-beta-D-glucosylceramide [ChEBI:17950]
The molecular basis of Sanfilippo syndrome type B
Purification and properties of guanosine diphosphate hexose pyrophosphorylase from mammalian tissues
Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase
Proteases in MHC class I presentation and cross-presentation
Phosphotyrosine profiling identifies the KG-1 cell line as a model for the study of FGFR1 fusions in acute myeloid leukemia
RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2 biosynthesis
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L-2-Aminoadipate 6-semialdehyde [ChEBI:17917]
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(5Z,8Z,11Z)-14,15-Epoxyicosa-5.8.11-trienoic acid
all-cis-14,15-epoxyeicosa-5,8,11-trienoic acid
14,15-epoxy-5Z,8Z,11Z-icosatrienoic acid
(5Z,8Z,11Z)-14,15-Epoxyeicosa-5.8.11-trienoic acid
14,15-epoxy-5Z,8Z,11Z-eicosatrienoic acid
Ubiquitin-dependent degradation of Cyclin D
DNA topoisomerase I and PC4 can interact with human TFIIIC to promote both accurate termination and transcription reinitiation by RNA polymerase III.
Preferential DNA repair of an active gene in human cells.
The content of pentose-cycle intermediates in liver in starved, fed ad libitum and meal-fed rats.
Cytosolic sensors of pathogen-associated DNA
RNA Polymerase II Transcription Elongation
Cloning, heterologous expression, and enzymological characterization of human squalene monooxygenase
Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency.
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
Semaphorin signaling: progress made and promises ahead
The copper transporter (Ctr) family of Cu+ uptake systems
Complete amino acid sequence of human liver cytosolic alanine aminotransferase (GPT) determined by a combination of conventional and mass spectral methods
The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI
eNOS, COX-2, and prostacyclin production are impaired in endothelial cells from diabetics
Metabolism of amino acids and derivatives
Speed, sensitivity, and stability of the light response in rod and cone photoreceptors: facts and models
A molecular perspective of CTLA-4 function
The novel Cdc42 guanine nucleotide exchange factor, zizimin1, dimerizes via the Cdc42-binding CZH2 domain
ADP-ribosylation factor 1 transiently activates high-affinity adaptor protein complex AP-1 binding sites on Golgi membranes
The COQ7 gene encodes a protein in Saccharomyces cerevisiae necessary for ubiquinone biosynthesis
Comprehending the complex connection between PKCbeta, TAK1, and IKK in BCR signaling
Docosahexaenoic acid synthesis in human skin fibroblasts involves peroxisomal retroconversion of tetracosahexaenoic acid
Structural and kinetic features of amyloid beta-protein fibrillogenesis
Activating and inhibitory functions of DAP12
Plk1- and beta-TrCP-dependent degradation of Bora controls mitotic progression
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Tuberculosis: what we don't know can, and does, hurt us
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Toxic proteins released from mitochondria in cell death
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N-Acetyl-D-glucosamine 6-phosphate [ChEBI:7127]
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A defect in dolichol phosphate biosynthesis causes a new inherited disorder with death in early infancy
Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenase
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ChEBI:17899 7alpha-hydroxycholest-4-en-3-one
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The Deleted in Colorectal Cancer netrin guidance system: a molecular strategy for neuronal navigation
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3,4-Dihydroxy-L-phenylalanine [ChEBI:1377]
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Nicotinate D-ribonucleotide [ChEBI:7561]
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(R)-4'-Phosphopantothenoyl-L-cysteine [ChEBI:328]
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D-2-Hydroxyglutaric aciduria: unravelling the biochemical pathway and the genetic defect
Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins
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ATP hydrolysis in Eg5 kinesin involves a catalytic two-water mechanism
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Resolution of AP sites via the multiple-nucleotide patch replacement pathway
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2-Aminomuconate semialdehyde [ChEBI:15745]
FGF signaling pathways in endochondral and intramembranous bone development and human genetic disease
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Characterization of the proteins of isolated human platelet alpha-granules. Evidence for a separate alpha-granule-pool of the glycoproteins IIb and IIIa.
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Palmitoylglycerone phosphate [ChEBI:7900]
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Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15
Expression and characterization of a human cDNA that complements the temperature-sensitive defect in dolichol kinase activity in the yeast sec59-1 mutant: the enzymatic phosphorylation of dolichol and diacylglycerol are catalyzed by separate CTP-mediated kinase activities in Saccharomyces cerevisiae
Dermatan sulfate: new functions from an old glycosaminoglycan
Molecular mechanisms of conduction and selectivity in aquaporin water channels
Molecular analysis of patients with beta-glucuronidase deficiency presenting as hydrops fetalis or as early mucopolysaccharidosis VII
Disruption of alpha-mannosidase processing induces non-canonical hybrid-type glycosylation
The enzymes, regulation, and genetics of bile acid synthesis
Succinyl CoA: 3-oxoacid CoA transferase (SCOT): human cDNA cloning, human chromosomal mapping to 5p13, and mutation detection in a SCOT-deficient patient
2-Methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency is caused by mutations in the HADH2 gene.
HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells
Construction and expression of human aldolase A and B expression plasmids in Escherichia coli host
Early mitotic degradation of Nek2A depends on Cdc20-independent interaction with the APC/C
Dihydropyrimidinase deficiency: structural organization, chromosomal localization, and mutation analysis of the human dihydropyrimidinase gene
A stimulatory role for cGMP-dependent protein kinase in platelet activation
Generation of second messenger molecules
Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins
The identification of a phospholipase B precursor in human neutrophils
gamma -Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase
Mycobacterium tuberculosis activates the DNA-dependent cytosolic surveillance pathway within macrophages
FGFR1 amplification drives endocrine therapy resistance and is a therapeutic target in breast cancer
Identification of HsORC4, a member of the human origin of replication recognition complex.
Molecular analysis of a series of alleles in humans with reduced activity at the triosephosphate isomerase locus
Normal human chromosomes have long G-rich telomeric overhangs at one end
Analysis of Gas6 in human platelets and plasma
Promoter escape by RNA polymerase II. Formation of an escape-competent transcriptional intermediate is a prerequisite for exit of polymerase from the promoter.
Formation of the ternary complex, and subsequently, the 43S complex
Structure of human cytidine deaminase bound to a potent inhibitor
Organization and localization to chromosome 5 of the human UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I gene
The PtdIns3P phosphatase myotubularin is a cytoplasmic protein that also localizes to Rac1-inducible plasma membrane ruffles
Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex
Recombinational DNA repair and human disease.
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Cohesin cleavage by separase required for anaphase and cytokinesis in human cells
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
Human SGBS cells - a unique tool for studies of human fat cell biology
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Zinc fluxes and zinc transporter genes in chronic diseases
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Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction
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Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase
Mechanisms underlying differential responses to FGF signaling
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Role of the CLOCK protein in the mammalian circadian mechanism
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Catecholamines: role in health and disease
Isolation of a candidate gene for Menkes disease that encodes a potential heavy metal binding protein
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An interferon-induced protein with release factor activity is a tryptophanyl-tRNA synthetase
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Fc gamma receptor-mediated activation of phospholipase D regulates macrophage phagocytosis of IgG-opsonized particles
Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1
Determination of the organisation of coding sequences within the iduronate sulphate sulphatase (IDS) gene
The KEN box: an APC recognition signal distinct from the D box targeted by Cdh1
The DNA-dependent protein kinase is inactivated by autophosphorylation of the catalytic subunit.
The mitotic checkpoint: a signaling pathway that allows a single unattached kinetochore to inhibit mitotic exit
Cellular signaling by fibroblast growth factor receptors
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Biosynthesis of chondroitin/dermatan sulfate
RasGRP1 and RasGRP3 regulate B cell proliferation by facilitating B cell receptor-Ras signaling
cAMP-dependent protein kinase: framework for a diverse family of regulatory enzymes
ABCB5-mediated doxorubicin transport and chemoresistance in human malignant melanoma
Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants
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
Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis
Aquaporin-7 and glycerol permeability as novel obesity drug-target pathways
Uroporphyrinogen decarboxylase: complete human gene sequence and molecular study of three families with hepatoerythropoietic porphyria
Peeling by binding or twisting by cranking: models for promoter opening and transcription initiation by RNA polymerase II.
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Metabolism of carotenoids and retinoids related to vision
Rod and cone visual pigments and phototransduction through pharmacological, genetic, and physiological approaches
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Atrial amyloid deposits in the failing human heart display both atrial and brain natriuretic peptide-like immunoreactivity
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G proteins: transducers of receptor-generated signals
Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease
The type 1 insulin-like growth factor receptor pathway
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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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Peroxisome proliferator-activated receptors, coactivators, and downstream targets
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Stabilization of beta-catenin by a Wnt-independent mechanism regulates cardiomyocyte growth
Proc. Natl. Acad. Sci. U.S.A. 100:4610-5
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M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCFbeta-TrCP
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Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme
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Messenger RNA capping enzymes from eukaryotic cells.
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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
Sld3, which interacts with Cdc45 (Sld4), functions for chromosomal DNA replication in Saccharomyces cerevisiae.
The mechanism of axon growth: what we have learned from the cell adhesion molecule L1
A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate
T cell receptor signaling: beyond complex complexes
Molecular cloning and characterization of a novel phospholipase C, PLC-eta
Adhesion mechanisms in platelet function
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
Purification and characterization of homogeneous initiation factor M2A from rabbit reticulocytes.
CREB phosphorylation through the activation of CaMKK
Mechanisms of organelle transport and capture along proplatelets during platelet production
Identification of the human mitochondrial linoleoyl-coenzyme A monolysocardiolipin acyltransferase (MLCL AT-1)
8p11 myeloproliferative syndrome with a novel t(7;8) translocation leading to fusion of the FGFR1 and TIF1 genes
Processing of Capped Intron-Containing Pre-mRNA
Mechanism and regulation of eukaryotic protein synthesis
Disorders of cholesterol biosynthesis: prototypic metabolic malformation syndromes
Making heads or tails of phospholipids in mitochondria
Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair.
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
The crystal structure of human phosphoglucose isomerase at 1.6 A resolution: implications for catalytic mechanism, cytokine activity and haemolytic anaemia
Activation of Rac GTPase by p75 is necessary for c-jun N-terminal kinase-mediated apoptosis
5,10-methylenetetrahydrofolate polyglutamate macromolecule
5,10-methylenetetrahydrofolate polyglutamate macromolecule [ChEBI:60473]
Ectodomain cleavage of ErbB-4: characterization of the cleavage site and m80 fragment
Getting to the end: telomerase access in yeast and humans
Activation of Chaperone Genes by XBP1(S)
3-decaprenyl-4-hydroxy-5-methoxybenzoic acid
4-hydroxy-3-methoxy-5-decaprenylbenzoic acid
all-trans-4-hydroxy-3-methoxy-5-decaprenylbenzoic acid
3-decaprenyl-4-hydroxy-5-methoxybenzoic acid [ChEBI:50776]
all-trans-3-decaprenyl-4-hydroxy-5-methoxybenzoic acid
A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis
3-decaprenyl-4,5-dihydroxybenzoic acid [ChEBI:50775]
all-trans-3-decaprenyl-4,5-dihydroxybenzoic acid
all-trans-3,4-dihydroxy-5-decaprenylbenzoic acid
The structure of human liver fructose-1,6-bisphosphate aldolase
Acta Crystallogr D Biol Crystallogr 57:1526-33
Neuregulin-2, a new ligand of ErbB3/ErbB4-receptor tyrosine kinases
A complete inventory of all enzymes in the eukaryotic methionine salvage pathway
Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon
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
Functional characterization of the human high-affinity choline transporter
WASP and WAVE family proteins: key molecules for rapid rearrangement of cortical actin filaments and cell movement
P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II.
Biosynthesis of A2E, implicated in retinal degradation
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
Human serum biotinidase. cDNA cloning, sequence, and characterization
Translocation of GLUT4 to the Plasma Membrane
Uptake of Carbon Dioxide and Release of Oxygen by Erythrocytes
Overexpression of human alanine:glyoxylate aminotransferase in Escherichia coli: renaturation from guanidine-HCl and affinity for pyridoxal phosphate co-factor
Xylulose 5-phosphate mediates glucose-induced lipogenesis by xylulose 5-phosphate-activated protein phosphatase in rat liver
Activation of HER4 by heparin-binding EGF-like growth factor stimulates chemotaxis but not proliferation
Sequential initiation of lagging and leading strand synthesis by two different polymerase complexes at the SV40 DNA replication origin.
Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring
8p11 myeloproliferative syndrome: a review
Cloning and characterization of the human beta-glucuronidase gene
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Interconversion of 2-oxoglutarate and 2-hydroxyglutarate
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Exercise-induced TBC1D1 Ser237 phosphorylation and 14-3-3 protein binding capacity in human skeletal muscle
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Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II
Analysis of RNA chain elongation and termination by Saccharomyces cerevisiae RNA polymerase III.
Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia
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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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PKC beta regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1
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Mutations in the MMAA gene in patients with the cblA disorder of vitamin B12 metabolism
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Metabolism of water-soluble vitamins and cofactors
Calmodulin: a prototypical calcium sensor
Localized amyloidosis of the seminal vesicle: identification of lactoferrin immunoreactivity in the amyloid material
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
Characterization of kynurenine aminotransferase III, a novel member of a phylogenetically conserved KAT family
A humble hexose monophosphate pathway metabolite regulates short- and long-term control of lipogenesis
Processive synthesis on the lagging strand
The Cdc4/34/53 pathway targets Cdc6p for proteolysis in budding yeast.
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The Saccharomyces cerevisiae COQ6 gene encodes a mitochondrial flavin-dependent monooxygenase required for coenzyme Q biosynthesis
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AKT/PKB signaling: navigating downstream
A DNA damage-regulated BRCT-containing protein, TopBP1, is required for cell survival.
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Purification and kinetic properties of human erythrocyte Mg2+-dependent inorganic pyrophosphatase
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Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol
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Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution.
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Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution.
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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
The human Aquaporin-5 gene. Molecular characterization and chromosomal localization
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Structural mechanism of muscle contraction
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Tetrahydropterin-dependent amino acid hydroxylases
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Human RFT1 deficiency leads to a disorder of N-linked glycosylation
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Expression and characterization of the human mitochondrial leucyl-tRNA synthetase
The glucose-lactic acid cycle and gluconeogenesis
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
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
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
Trimming of the terminal mannose on the C branch
Trimming of the first mannose on the A branch
Removal of the third glucose by glucosidase II and release from the chaperone
Trimming of the terminal mannose on the B branch
Binding of calnexin/calreticulin to the unfolded protein
Glycoproteins with major folding defects are sent to degradation by EDEMs
Re-addition of a glucose on the alpha 1,3 branch
Substrate specificity of human nucleoside-diphosphate kinase revealed by transient kinetic analysis
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
Adipocyte-specific transcription factor ARF6 is a heterodimeric complex of two nuclear hormone receptors, PPAR gamma and RXR alpha
Trimming of the second mannose on the A branch
Addition of GlcNAc to the Tn antigen via a beta-1,6 linkage forms a Core 6 glycoprotein
Progressive trimming of alpha-1,2-linked mannose residues from Man7GlcNAc2 to produce Man5GlcNAc2
Human acyl-CoA:diacylglycerol acyltransferase is a tetrameric protein
Addition of GlcNAc to the glycan on the A arm
Trimming of mannoses on the alpha1,6 arm by MAN2A1
Addition of GlcNAc to the Tn antigen via an alpha-1,3 linkage forms a Core 5 glycoprotein
(ethanolamineP) mannose (a1-2) mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI -> (ethanolamineP) mannose (a1-2) (ethanolamineP) mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI
GlcNAc1P is dephosphorylated to UDP-N-acetyl-glucosamine
Acetylation of glucosamine 6-phosphate to GlcNAc6P
Formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine
Dephosphorylation of dolichyl diphosphate
Mannose-1-phosphate converted to GDP-Mannose
Mannose 6-phosphate isomerizes to Mannose 1-phosphate
Fructose 6-phosphate isomerizes to Mannose 6-phosphate
Addition of the second N-acetyl-glucosamine to the N-glycan precursor
Addition of the first mannose to the N-glycan precursor by ALG13/14
Addition of a second mannose to the N-glycan precursor by ALG2
Mammalian class Sigma glutathione S-transferases: catalytic properties and tissue-specific expression of human and rat GSH-dependent prostaglandin D2 synthases
Addition of a fourth and fifth mannose to the N-glycan precursor by ALG11
Addition of a third mannose to the N-glycan precursor by ALG2
Addition of the sixth mannose to the N-glycan precursor by ALG3.
Flipping of the N-glycan precursor to inside the ER
Addition of the eighth mannose to the N-glycan precursor by ALG12, inside the ER lumen
Addition of the seventh mannose to the N-glycan precursor by ALG9, inside the ER lumen
Addition of the last mannose to the N-glycan precursor by ALG3, inside the ER lumen.
Selective inhibition of heterotrimeric Gs signaling. Targeting the receptor-G protein interface using a peptide minigene encoding the Galpha(s) carboxyl terminus
Beta-tubulin:GTP + Cofactor D -> Beta-tubulin:GTP: Cofactor D
Beta-tubulin:GTP + Cofactor A -> Beta-tubulin:GTP: Cofactor A
Association of CCT/TriC with sphingosine kinase 1
Hydrolysis of ATP and release of folded actin from CCT/TriC
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
EIF5A + spermidine <=> EIF5A(Dhp) + 1,3-diaminopropane
Beta-tubulin:GTP: Cofactor A+ Cofactor D -> Beta-tubulin:GTP:Cofactor D + Cofactor A
EIF5A(Dhp) + 1,3-diaminopropane <=> EIF5A + spermidine
mannose(a1-4)glucosaminyl-acyl-PI + phosphatidylethanolamine -> (ethanolamineP) mannose(al1-4)glucosaminyl-acyl-PI + diacylglycerol
glucosaminyl-PI + fatty acyl-CoA -> glucosaminyl-acyl-PI + CoA-SH
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
(ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI + dolichol phosphate D-mannose -> mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI + dolichol phosphate
dolichyl phosphate + GDP-alpha-D-mannose -> dolichyl phosphate D-mannose
N-acetylglucosaminyl-PI + H2O -> glucosaminyl-PI + acetate
phosphatidylinositol + UDP-N-acetyl-D-glucosamine -> N-acetylglucosaminyl-PI + UDP
mannose (a1-2) mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI + phosphatidylethanolamine -> (ethanolamineP) mannose (a1-2) mannose (a1-6) (ethanolamineP) mannose (a1-4) glucosaminyl-acyl-PI (acyl-GPI) + diacylglycerol
Dissociation of L13a from the 60s ribosomal subunit
Association of phospho-L13a with GAIT element of Ceruloplasmin mRNA
Synthesis of nascent polypeptide containing signal sequence
Formation of the 43S pre-initiation complex
Release of eIF4E from the inactive eIF4E:4E-BP complex
The 60S subunit joins the translation initiation complex
Formation of eIF2:GDP:eIF2B intermediate
Tyrosine residues in phospholipase Cgamma 2 essential for the enzyme function in B-cell signaling
unfolded actin/tubulin associates with prefoldin
GTP Hydrolysis by eRF3 bound to the eRF1:mRNA:polypeptide:80S Ribosome complex
Polypeptide release from the eRF3-GDP:eRF1:mRNA:80S Ribosome complex
The SRP receptor binds the SRP:nascent peptide:ribosome complex
Translocation of signal-containing nascent peptide to Endoplasmic Reticulum
Association of a nascent polypeptide:mRNA:ribosome complex with a signal recognition particle (SRP)
GTP bound eRF3:eRF1 complex binds the peptidyl tRNA:mRNA:80S Ribosome complex
Signal peptide cleavage from ribosome-associated nascent protein
Peptide transfer from P-site tRNA to the A-site tRNA
RNA Polymerase III Promoter Opening at Type 2 Promoters
CLOCK/BMAL1 regulates human nocturnin transcription through binding to the E-box of nocturnin promoter
RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites
Assembly of RNA Polymerase I Holoenzyme (human)
RNA Polymerase III Abortive Initiation At Type 2 Open Promoters
RNA Polymerase III Productive Transcription
Hyperphosphorylation (Ser2) of RNA Pol II CTD by P-TEFb complex
Addition of nucleotides leads to transcript elongation
Pol II elongation complex moves on the template as transcript elongates
Separation of elongating transcript from template
Homologous recombinational repair of DNA ensures mammalian chromosome stability
Inborn errors of cobalamin absorption and metabolism
Am J Med Genet C Semin Med Genet 157:33-44
Metabolism of gammalinolenic acid in human neutrophils
4a-hydroxytetrahydrobiopterin [ChEBI:15374]
Niemann-Pick C1 Like 1 protein is critical for intestinal cholesterol absorption
Met-tRNAi binds to eIF2:GTP to form the ternary complex
Mechanism of two classes of cancer mutations in the phosphoinositide 3-kinase catalytic subunit
integral to lumenal side of endoplasmic reticulum membrane
Ubiquitination of Cyclin A by APC/C:Cdc20 complex
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
Sororin mediates sister chromatid cohesion by antagonizing Wapl
Regulation of cell migration by the C2 domain of the tumor suppressor PTEN
Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1
FYVE-DSP2, a FYVE domain-containing dual specificity protein phosphatase that dephosphorylates phosphotidylinositol 3-phosphate
Molecular mechanism of an oncogenic mutation that alters membrane targeting: Glu17Lys modifies the PIP lipid specificity of the AKT1 PH domain
1-acyl-sn-glycero-3-phosphoethanolamine [ChEBI:29017]
IFI16 is an innate immune sensor for intracellular DNA
2-Amino-3-carboxymuconate semialdehyde [ChEBI:29044]
GM1-gangliosidosis (genetic beta-galactosidase deficiency): identification of four mutations in different clinical phenotypes among Japanese patients
Cloning of a complete protein-coding sequence of human platelet-type phosphofructokinase isozyme from pancreatic islet.
(2R)-2-Hydroxy-3-(phosphonooxy)-propanal [ChEBI:29052]
Characterization of a cDNA encoding a novel human Golgi alpha 1, 2-mannosidase (IC) involved in N-glycan biosynthesis
Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.
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
ChEBI:29089 1,2-diacyl-sn-glycerol 3-phosphate
Latent infection of Homo sapiens with Mycobacterium tuberculosis
Requirement for the kinase activity of human DNA-dependent protein kinase catalytic subunit in DNA strand break rejoining.
Two steps in the assembly of complexes at yeast replication origins in vivo.
ZNF198-FGFR1 transforming activity depends on a novel proline-rich ZNF198 oligomerization domain
Human Nbp35 is essential for both cytosolic iron-sulfur protein assembly and iron homeostasis
glucosaminylphosphatidylinositol [ChEBI:24275]
Purification and molecular cloning of Plx1, a Cdc25-regulatory kinase from Xenopus egg extracts
Role of platelet-derived growth factors in physiology and medicine
Cyclin A is required at two points in the human cell cycle
Assignment of human beta-galactosidase-A gene to 3p21.33 by fluorescence in situ hybridization
Mutations in the holocarboxylase synthetase gene HLCS
The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits
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
The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
Control of mitosis by changes in the subcellular location of cyclin-B1-Cdk1 and Cdc25C
Peroxisome proliferator-activated receptors: a nuclear receptor signaling pathway in lipid physiology
Biosynthetic studies of A2E, a major fluorophore of retinal pigment epithelial lipofuscin
Posttranslational modification of the AU-rich element binding protein HuR by protein kinase Cdelta elicits angiotensin II-induced stabilization and nuclear export of cyclooxygenase 2 mRNA
Class C/3 (Metabotropic glutamate/pheromone receptors)
Tetrahydrobiopterin biosynthesis, regeneration and functions
Selective RNA binding by a single CCCH zinc-binding domain from Nup475 (Tristetraprolin)
Chaperone Hsp27, a novel subunit of AUF1 protein complexes, functions in AU-rich element-mediated mRNA decay
Tyrosine kinase inhibitors bind and inhibit FGFR1 fusion dimer phosphorylation
PTEN cancer mutants do not dephosphorylate PIP3
phenylalanine + H2O + O2 => phenylpyruvate + NH3 + H2O2
Molecular cloning and expression of cDNAs encoding human alpha-mannosidase II and a previously unrecognized alpha-mannosidase IIx isozyme
phenylalanine + oxaloacetate => phenylpyruvate + aspartate [CCBL1]
PLCgamma is phosphorylated by FGFR1-fusions
p-PLCgamma dissociates from FGFR1 fusions
Peptide binding and antigen presentation by class II histocompatibility glycoproteins
PIP2-bound p-S473-AKT1 mutant binds PIP2-bound PDPK1
AKT1 E17K mutant is phosphorylated by TORC2 complex
A 7 bp mutation converts a human RNA polymerase II snRNA promoter into an RNA polymerase III promoter
AKT1 E17K mutant translocates to the nucleus
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
AKT inhibitors block AKT membrane recruitment
2-oxoglutarate + NADPH + H+ => (R)-2-hydroxyglutarate + NADP+ [mutant IDH1]
Diffusion of inactive Arf1-GDP from membrane
RIG-I family RNA helicases: cytoplasmic sensor for antiviral innate immunity
GAP Recruitment to the Coatomer:Arf1-GTP Complex
Coatomer:Arf1-GTP:GAP lattice formation on golgi membrane
Sculpting and pinching-off of Golgi vessicle
Abortive termination of early transcription elongation by DSIF:NELF
TFIIS-mediated recovery of elongation from arrest
2-4 nt.backtracking of Pol II complex on the template leading to elongation pausing
Resumption of elongation after recovery from pausing
Formation of the closed pre-initiation complex
RNA Polymerase II Promoter Opening: First Transition
Abortive termination of elongation after arrest
Fall Back to Closed Pre-initiation Complex
NTP Binds Active Site of RNA Polymerase II
Synthesis of substrates in N-glycan biosythesis
The inositol hexakisphosphate kinase family. Catalytic flexibility and function in yeast vacuole biogenesis
Analysis of the putative role of 24-carbon polyunsaturated fatty acids in the biosynthesis of docosapentaenoic (22:5n-6) and docosahexaenoic (22:6n-3) acids
Newly Formed Phosphodiester Bond Stabilized and PPi Released
Nucleophillic Attack by 3'-hydroxyl Oxygen of nascent transcript on the Alpha Phosphate of NTP
Addition of the fourth nucleotide on the Nascent Transcript: Second Transition
Addition of the third nucleotide on the nascent transcript
Addition of nucleotides between position +11 and +30
Addition of nucleotides 10 and 11 on the growing transcript: Third Transition
Extrusion of 5'-end of 30 nt long transcript through the pore in Pol II complex
Phosphorylation (Ser5) of RNA pol II CTD
Hypophosphorylation of RNA Pol II CTD by FCP1P protein
DSIF complex binds to RNA Pol II (hypophosphorylated)
Interactions of CD80 and CD86 with CD28 and CTLA4
'SSB [nucleoplasm]' positively regulates 'RNA Polymerase III Termination and release of transcribed mRNA'
'RGS proteins active for G alpha (z) [plasma membrane]' positively regulates 'G alpha (z) auto-inactivates by hydrolysing GTP to GDP'
The molecular basis of insulin-stimulated glucose uptake: signalling, trafficking and potential drug targets
Deiodinases: implications of the local control of thyroid hormone action
Structure of S6 kinase 1 determines whether raptor-mTOR or rictor-mTOR
GAPs inactivate Rho GTPase:GTP by hydrolysis
'Cys [cytosol]' positively regulates 'Excess cysteine yields lanthionine and H2S'
'heme [mitochondrial matrix]' negatively regulates 'ALAS condenses SUCC-CoA and Gly to form dALA'
p75NTR indirectly activates RAC and Cdc42 via a guanyl-nucleotide exchange factor
'Pb2+ [mitochondrial matrix]' negatively regulates 'FECH binds Fe2+ to PRIN9 to form heme'
'GSH [cytosol]' negatively regulates 'gamma-glutamylcysteine combines with glycine to form glutathione'
'phospho-p-S722,S792-RPTOR-1 [cytosol]' negatively regulates 'Activation of S6K1'
'G-protein alpha (i):GTP:Adenylate cyclase (name copied from entity in Homo sapiens) [plasma membrane]' negatively regulates 'Adenylate cyclase converts ATP to 3',5'-cyclic AMP (cAMP) and pyrophosphate'
'G-protein alpha (z):GTP:Adenylate cyclase (name copied from entity in Homo sapiens) [plasma membrane]' negatively regulates 'Adenylate cyclase converts ATP to 3',5'-cyclic AMP (cAMP) and pyrophosphate'
'RGS proteins active for G alpha (i) [plasma membrane]' positively regulates 'G alpha (i) auto-inactivates by hydrolysing GTP to GDP'
'HCYS [cytosol]' positively regulates 'Excess homocysteine yields homolanthionine and H2S'
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
'L-Arg [mitochondrial matrix]' positively regulates 'glutamate + acetyl CoA => N-acetyl glutamate + CoA'
'L-Phe [cytosol]' negatively regulates 'kynurenine + pyruvate => 4-(2-aminophenyl)-2,4-dioxobutanoic acid + alanine [CCBL1]'
'Mg2+ [cytosol]' is required for 'A phosphoribosyl group is added to nicotinate to form nicotinate mononucleotide (NaMN)'
'ADP [mitochondrial matrix]' positively regulates 'alpha-ketoglutarate + NH4+ + NAD(P)H + H+ <=> glutamate + NAD(P)+ [GLUD1]'
G alpha (z) auto-inactivates by hydrolysing GTP to GDP
'Mg2+ [cytosol]' is required for 'ITPA hydrolyses XTP to XMP'
Adenylate cyclase converts ATP to 3',5'-cyclic AMP (cAMP) and pyrophosphate
'GTP [mitochondrial matrix]' negatively regulates 'glutamate + NAD(P)+ => alpha-ketoglutarate + NH4+ + NAD(P)H + H+ [GLUD1]'
Dissociation of Rho GTP:GDP from GDI complex
'S40L-PAH [cytosol]' negatively regulates 'phenylalanine + tetrahydrobiopterin + O2 => tyrosine + 4a-hydroxytetrahydrobiopterin + H2O'
G alpha (i) auto-inactivates by hydrolysing GTP to GDP
'GTP [mitochondrial matrix]' negatively regulates 'alpha-ketoglutarate + NH4+ + NAD(P)H + H+ <=> glutamate + NAD(P)+ [GLUD1]'
Liganded Gi-activating GPCR acts as a GEF for Gi
'ADP [mitochondrial matrix]' positively regulates 'glutamate + NAD(P)+ => alpha-ketoglutarate + NH4+ + NAD(P)H + H+ [GLUD1]'
Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway
Inactive catalytic PP2B is activated by the binding of calmodulin
Cloning of a gene for a novel epithelium-specific cytosolic phospholipase A2, cPLA2delta, induced in psoriatic skin
Structure, function and evolution of seryl-tRNA synthetases: implications for the evolution of aminoacyl-tRNA synthetases and the genetic code
Senile seminal vesicle amyloid is derived from semenogelin I
Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns
'GTP [cytosol]' is required for 'Met-tRNAi binds to eIF2:GTP to form the ternary complex'
Peripheral blood platelets express VEGF-C and VEGF which are released during platelet activation
Intraphagosomal pH is lowered to 5 by V-ATPase
Transfer of SUMO3 from E1 to UBE2I (UBC9)
'ATP [cytosol]' is required for 'Ribosomal scanning '
Amyloid precursor proteins form ordered fibrils
'Ac-CoA [cytosol]' negatively regulates 'phosphoenolpyruvate + ADP => pyruvate + ATP'
The helicase DDX41 senses intracellular DNA mediated by the adaptor STING in dendritic cells
'3',5'-Cyclic AMP [cytosol]' negatively regulates 'phosphoenolpyruvate + ADP => pyruvate + ATP'
'ATP [nucleoplasm]' negatively regulates 'phosphoenolpyruvate + ADP => pyruvate + ATP'
'D-Fructose 1,6-bisphosphate [cytosol]' positively regulates 'phosphoenolpyruvate + ADP => pyruvate + ATP'
Reconstitution, activities, and structure of the eukaryotic RNA exosome
'G6P [cytosol]' negatively regulates 'PGYM dimer, b form + 2 AMP <=> PGYM b dimer:AMP complex'
'CIT [cytosol]' positively regulates 'acetyl-CoA + bicarbonate + ATP => malonyl-CoA + H2O + ADP + orthophosphate'
'AMP [cytosol]' negatively regulates 'D-fructose 1,6-bisphosphate + H2O => D-fructose 6-phosphate + orthophosphate'
'ATP [cytosol]' negatively regulates 'PGYM dimer, b form + 2 AMP <=> PGYM b dimer:AMP complex'
'RAPGEF3:cAMP complex (name copied from entity in Homo sapiens) [plasma membrane]' positively regulates 'Exchange of GDP for GTP by Rap1A'
'RAPGEF4:cAMP Complex (name copied from entity in Homo sapiens) [plasma membrane]' positively regulates 'Exchange of GDP for GTP by Rap1A'
'NAADP [cytosol]' positively regulates 'TPCN1/2 transport lysosomal Ca2+ to cytosol '
'DAG [plasma membrane]' positively regulates 'Activation of conventional Protein Kinase C'
'XPO1 [nucleoplasm]' positively regulates 'Translocation of Cyclin B1:phospho-Cdc2 to the cytoplasm'
'Mg2+ [cytosol]' is required for 'pyrophosphate + H2O => 2 orthophosphate [cytosolic]'
'Mg2+ [mitochondrial matrix]' is required for 'pyrophosphate + H2O => 2 orthophosphate [mitochondrial]'
'ADP [cytosol]' positively regulates 'D-fructose 6-phosphate + ATP => D-fructose 1,6-bisphosphate + ADP'
'ATP [cytosol]' negatively regulates 'D-fructose 6-phosphate + ATP => D-fructose 1,6-bisphosphate + ADP'
'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 1,6-bisphosphate + ADP'
'AMP [cytosol]' positively regulates 'D-fructose 6-phosphate + ATP => D-fructose 1,6-bisphosphate + ADP'
'D-Fructose 1,6-bisphosphate [cytosol]' negatively regulates 'IMP + L-Aspartate + GTP => Adenylosuccinate + GDP + Pi [ADSS]'
'GDP [cytosol]' negatively regulates 'IMP + L-Aspartate + GTP => Adenylosuccinate + GDP + Pi [ADSS]'
'XMP [cytosol]' negatively regulates 'IMP + H2O + NAD+ => XMP + NADH + H+ [IMPDH1,2]'
'Formation of phosphoribosyl pyrophosphate amidotransferase tetramer' negatively regulates '5-phospho-alpha-D-ribose 1-diphosphate (PRPP) + H2O + L-glutamine <=> 5-phosphoribosylamine + L-glutamate +pyrophosphate'
Butyrate Response Factor1 (BRF1) Binds AU-rich Element in 3' UTR of mRNA
'Dissociation of phosphoribosyl pyrophosphate amidotransferase tetramer' positively regulates '5-phospho-alpha-D-ribose 1-diphosphate (PRPP) + H2O + L-glutamine <=> 5-phosphoribosylamine + L-glutamate +pyrophosphate'
Phosphorylation of BRF1 by Protein Kinase B/Akt
'PRPP [cytosol]' positively regulates 'Dissociation of phosphoribosyl pyrophosphate amidotransferase tetramer'
Tristetraproline (TTP) Binds AU-rich Elements in 3' UTR of Target mRNAs
Phosphorylated HuR (Ser221, Ser158) Binds mRNA
Phosphorylated HuR (Ser221, Ser318) Binds mRNA
SMG1 Phosphorylates UPF1 (Enhanced by Exon Junction Complex)
'Mg2+ [cytosol]' is required for 'ITPA hydrolyses ITP to IMP'
'Mg2+ [cytosol]' is required for 'ITPA hydrolyses dITP to dIMP'
'ADS [cytosol]' negatively regulates 'IMP + L-Aspartate + GTP => Adenylosuccinate + GDP + Pi [ADSS]'
Deficiency of the first mannosylation step in the N-glycosylation pathway causes congenital disorder of glycosylation type Ik
'GMP [cytosol]' negatively regulates 'IMP + L-Aspartate + GTP => Adenylosuccinate + GDP + Pi [ADSS]'
Formation of UPF1:eRF3 Complex on mRNA with a Premature Termination Codon and No Exon Junction Complex
'BH4 [cytosol]' negatively regulates 'GCH1 reduces GTP to dihydroneopterin triphosphate'
'L-Phe [cytosol]' positively regulates 'GCH1 reduces GTP to dihydroneopterin triphosphate'
'Co2+ [mitochondrial matrix]' positively regulates '(R)-2-hydroxyglutarate + FAD => 2-oxoglutarate + FADH2'
'ADP [mitochondrial matrix]' positively regulates 'isocitrate + NAD+ => alpha-ketoglutarate + CO2 + NADH + H+ [IDH3]'
Phosphorylation of Ribosomal protein S6 by activated S6K1
'XY5P [cytosol]' positively regulates 'Activation of PP2A by Xylulose-5-phosphate'
Dissociation of phosphorylated 4EBP1 from eIF4E
Phosphorylation and inactivation of eEF2K by activated S6K1
Phosphorylation of 4E-BP1 by activated mTORC1
Roles of AUF1 isoforms, HuR and BRF1 in ARE-dependent mRNA turnover studied by RNA interference
Assembly of the ORC complex at the origin of replication
'AMP [cytosol]' positively regulates 'Formation of phosphoribosyl pyrophosphate amidotransferase tetramer'
'Zn2+ [mitochondrial matrix]' positively regulates '(R)-2-hydroxyglutarate + FAD => 2-oxoglutarate + FADH2'
'Mn2+ [mitochondrial matrix]' positively regulates '(R)-2-hydroxyglutarate + FAD => 2-oxoglutarate + FADH2'
'IMP [cytosol]' positively regulates 'Formation of phosphoribosyl pyrophosphate amidotransferase tetramer'
'GMP [cytosol]' positively regulates 'Formation of phosphoribosyl pyrophosphate amidotransferase tetramer'
Mechanism of action and in vivo role of platelet-derived growth factor
integral to cytosolic side of endoplasmic reticulum membrane
Release of apoptotic factors from the mitochondria
Comparison of human B cell antigen receptor complexes: membrane-expressed forms of immunoglobulin (Ig)M, IgD, and IgG are associated with structurally related heterodimers
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.
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
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
Igf-I signaling and effects on longevity
Nestle Nutr Workshop Ser Pediatr Program 68:237-45; discussion 246-9
Differences between the trypanosomal and human GlcNAc-PI de-N-acetylases of glycosylphosphatidylinositol membrane anchor biosynthesis
Amyloid beta-protein assembly and Alzheimer disease
Inactivation, recovery and regulation of the phototransduction cascade
Molecular characterization of a phospholipase D generating anandamide and its congeners
Expression of aquaporin 8 in colonic epithelium with diarrhoea-predominant irritable bowel syndrome
Human homologue of murine tumor rejection antigen gp96: 5'-regulatory and coding regions and relationship to stress-induced proteins
Characterization of p150, an adaptor protein for the human phosphatidylinositol (PtdIns) 3-kinase. Substrate presentation by phosphatidylinositol transfer protein to the p150.Ptdins 3-kinase complex
Spatial and temporal regulation of Condensins I and II in mitotic chromosome assembly in human cells
Neuregulin-3 (NRG3): a novel neural tissue-enriched protein that binds and activates ErbB4
Cdc25 cell-cycle phosphatase as a target of c-myc
Tyrosine phosphorylation of phospholipase C induced by membrane immunoglobulin in B lymphocytes
Degradation of cysteine and homocysteine
Identification of eukaryotic DNA replication proteins using simian virus 40 in vitro replication system.
Synthesis of lysophosphatidic acid from dihydroxyacetone phosphate
The sequence of a human mitochondrial glycerol-3-phosphate dehydrogenase-encoding cDNA
Stem-loop binding protein facilitates 3'-end formation by stabilizing U7 snRNP binding to histone pre-mRNA.
Eukaryotic protein synthesis: still a mystery
Structural basis of double-stranded RNA recognition by the RIG-I like receptor MDA5
AT-AC pre-mRNA splicing mechanisms and conservation of minor introns in voltage-gated ion channel genes.
Polycystin-2 down-regulates cell proliferation via promoting PERK-dependent phosphorylation of eIF2alpha
Autophosphorylation of the DNA-dependent protein kinase catalytic subunit is required for rejoining of DNA double-strand breaks.
Dynamics of the interaction of human apurinic endonuclease (Ape1) with its substrate and product.
Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2/3 complex
Crystal structure of human beta-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay-Sachs disease
Phosphorylation of nucleosides and nucleoside analogs by mammalian nucleoside monophosphate kinases
Interfacial kinetic and binding properties of the complete set of human and mouse groups I, II, V, X, and XII secreted phospholipases A2
Adenosine triphosphate-adenosine-5'-monophosphate phosphotransferase from normal human liver mitochondria. Isolation, chemical properties, and immunochemical comparison with Duchenne muscular dystrophic serum aberrant adenylate kinase
Transfer of SUMO from E1 to E2 (UBE2I, UBC9)
The human and mouse replication-dependent histone genes
Syndromic craniosynostosis: from history to hydrogen bonds
Protease nexin-II (amyloid beta-protein precursor): a platelet alpha-granule protein
Biosynthesis of chondroitin sulfate: from the early, precursor discoveries to nowadays, genetics approaches
Functional evaluation of PTEN missense mutations using in vitro phosphoinositide phosphatase assay
Identification, purification and characterization of a novel phosphatidylinositol-specific phospholipase C, a third member of the beta subfamily
BMAL1:CLOCK/NPAS2 Activates Circadian Expression
Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1
XBP1 controls diverse cell type- and condition-specific transcriptional regulatory networks
mitochondrial fatty acid beta-oxidation of saturated fatty acids
Accumulation of dietary cholesterol in sitosterolemia caused by mutations in adjacent ABC transporters
Inactivation of NF-kappa B inhibitor I kappa B alpha: ubiquitin-dependent proteolysis and its degradation product
Rhesus glycoproteins mediate ammonium transport.
Prophase destruction of Emi1 by the SCF(betaTrCP/Slimb) ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase
Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction
Characterization of MTMR3. an inositol lipid 3-phosphatase with novel substrate specificity
Complete sequencing and characterization of 21,243 full-length human cDNAs
Identical mutations in three different fibroblast growth factor receptor genes in autosomal dominant craniosynostosis syndromes
Synthesis of pyrophosphates in the cytosol
Release of arachidonate from diglyceride in human platelets requires the sequential action of a diglyceride lipase and a monoglyceride lipase
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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A second canon. Functions and mechanisms of beta-catenin-independent Wnt signaling
Structure-function analysis of the bestrophin family of anion channels
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Evidence for protein-tyrosine-phosphatase catalysis proceeding via a cysteine-phosphate intermediate
Differential assembly of Cdc45p and DNA polymerases at early and late origins of DNA replication.
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Protein phosphatases regulate DNA-dependent protein kinase activity.
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The expression and functional characterization of ABCG2 in brain endothelial cells and vessels
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Selective degradation of AU-rich mRNAs promoted by the p37 AUF1 protein isoform
Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics
Raptor, a binding partner of target of rapamycin (TOR), mediates TOR
A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells
ARF mediates recruitment of PtdIns-4-OH kinase-beta and stimulates synthesis of PtdIns(4,5)P2 on the Golgi complex
Phospholipase C-gamma 1 and phospholipase C-gamma 2 are substrates of the B cell antigen receptor associated protein tyrosine kinase
Uptake of Oxygen and Release of Carbon Dioxide by Erythrocytes
Mitochondrial iron trafficking and the integration of iron metabolism between the mitochondrion and cytosol
Glyoxylate reductase/hydroxypyruvate reductase
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
Disassembly of exon junction complexes by PYM
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
5-aminolevulinate synthase, non-specific (pyridoxal phosphate cofactor)
5-aminolevulinate synthase, non-specific, mitochondrial
5-aminolevulinate synthase, erythroid (pyridoxal phosphate cofactor)
5-aminolevulinate synthase, erythroid-specific, mitochondrial precursor
Kid, a novel kinesin-like DNA binding protein, is localized to chromosomes and the mitotic spindle
Insights into COPI coat assembly and function in living cells
Protoheme IX farnesyltransferase, mitochondrial ecNumber2.5.1.-/ecNumber
Cytochrome c oxidase assembly protein COX15 homolog
Molecular structure of a novel cholesterol-responsive A subclass ABC transporter, ABCA9
Dimethylaniline monooxygenase (N-oxide-forming) 1
Coproporphyrinogen III oxidase, mitochondrial
RNA binding properties of the AU-rich element-binding recombinant Nup475/TIS11/tristetraprolin protein
Structures of the human orotidine-5'-monophosphate decarboxylase support a covalent mechanism and provide a framework for drug design
Dimethylaniline monooxygenase (N-oxide-forming) 2
Recognition and association of DNA glycosylase with site containing an affected pyrimidine
The role of assembly in insulin's biosynthesis
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Acetyl-coenzyme A synthetase 2-like, mitochondrial
acyl-CoA synthetase short-chain family member 1
Sulfotransferases in the bioactivation of xenobiotics
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Hepatic flavin-containing monooxygenase 3
Dimethylaniline monooxygenase (N-oxide forming) 3
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Identification of the peroxisomal beta-oxidation enzymes involved in the biosynthesis of docosahexaenoic acid
The phosphatidylinositol 3-kinase/Akt signaling pathway modulates the endocrine differentiation of trophoblast cells
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A conserved family of enzymes that phosphorylate inositol hexakisphosphate
Glutathione S-transferase theta-1 ecNumber2.5.1.18/ecNumber
Identification of Mn2+-binding aspartates from alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase
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Biochemical characterization of the human copper transporter Ctr1
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Overview of steroidogenic enzymes in the pathway from cholesterol to active steroid hormones
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Xenobiotic/medium-chain fatty acid:CoA ligase
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Glutathione S-transferase theta-2B ecNumber2.5.1.18/ecNumber
Regulation of repair of alkylation damage in mammalian genomes.
Prog Nucleic Acid Res Mol Biol 44:109-42
Iron-sulfur cluster assembly enzyme ISCU, mitochondrial
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NADPH:adrenodoxin oxidoreductase, mitochondrial
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N-retinylidene-N-retinylphosphatidylethanolamine [ChEBI:52592]
Cytosolic Fe-S cluster assembly factor NUBP1
NADPH-dependent diflavin oxidoreductase 1 ecNumber1.6.-.-/ecNumber
Cytosolic Fe-S cluster assembly factor NUBP2
DNA polymerase delta catalytic subunit ecNumber2.7.7.7/ecNumber
TFIIH basal transcription factor complex helicase XPD subunit ecNumber3.6.4.12/ecNumber
Mitotic spindle-associated MMXD complex subunit MIP18
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Guanosine triphosphate, the primary product of phosphorylation coupled to the breakdown of succinyl coenzyme A
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acylglucosaminylphosphatidylinositol [ChEBI:52572]
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Gamma linolenic acid: an antiinflammatory omega-6 fatty acid
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).
Spectrum of mutations in mut methylmalonic acidemia and identification of a common Hispanic mutation and haplotype
RNA Polymerase II Transcription Initiation
Primary megakaryocytes reveal a role for transcription factor NF-E2 in integrin alpha IIb beta 3 signaling
Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes
LAT and NTAL mediate immunoglobulin E-induced sustained extracellular signal-regulated kinase activation critical for mast cell survival
The complex route to MHC class I-peptide complexes
Molecular defects in Sanfilippo syndrome type B (mucopolysaccharidosis IIIB)
Assignment of the human and mouse prion protein genes to homologous chromosomes
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The kinase inhibitor TKI258 is active against the novel CUX1-FGFR1 fusion detected in a patient with T-lymphoblastic leukemia/lymphoma and t(7;8)(q22;p11)
Roles for LPS-dependent interaction and relocation of TLR4 and TRAM in TRIF-signaling
Transcription factors direct the development and function of pancreatic beta cells
The SLC2 family of facilitated hexose and polyol transporters
PMM (PMM1), the human homologue of SEC53 or yeast phosphomannomutase, is localized on chromosome 22q13
Endonucleolytic RNA cleavage by a eukaryotic exosome
Common themes in siRNA-mediated epigenetic silencing pathways
AKT phosphorylates targets in the cytosol
Organization and sequence of the human gene for the mitochondrial citrate transport protein
Chromokinesins: multitalented players in mitosis
Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis.
RNA Polymerase I Transcription Initiation
CREB phosphorylation through the activation of Ras
Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity
Inhibition of adenylyl cyclase by Gi alpha
Probable cytosolic iron-sulfur protein assembly protein CIAO1
Cytosolic Fe-S cluster assembly factor NARFL
MMS19 nucleotide excision repair protein homolog
Purification and properties of uroporphyrinogen decarboxylase from human erythrocytes. A single enzyme catalyzing the four sequential decarboxylations of uroporphyrinogens I and III.
Synthesis of PIPs at the late endosome membrane
Identification of two tyrosine phosphoproteins, pp70 and pp68, which interact with phospholipase Cgamma, Grb2, and Vav after B cell antigen receptor activation
Sequence of human tryptophan 2,3-dioxygenase (TDO2): presence of a glucocorticoid response-like element composed of a GTT repeat and an intronic CCCCT repeat
Signaling via mitogen-activated protein kinase kinase (MEK1) is required for Golgi fragmentation during mitosis
Localization of the human mitochondrial citrate transporter protein gene to chromosome 22Q11 in the DiGeorge syndrome critical region
Structural models of amyloid-like fibrils
Advanced glycosylation endproduct receptor signaling
Sodium-coupled monocarboxylate transporters in normal tissues and in cancer
FGFR activation in skeletal disorders: too much of a good thing
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
U6 snRNA-associated Sm-like protein LSm7
U6 snRNA-associated Sm-like protein LSm1
U6 snRNA-associated Sm-like protein LSm5
U6 snRNA-associated Sm-like protein LSm6
U6 snRNA-associated Sm-like protein LSm4
U6 snRNA-associated Sm-like protein LSm3
Regulation of histone mRNA in the unperturbed cell cycle: evidence suggesting control at two posttranscriptional steps.
Ways of dying: multiple pathways to apoptosis.
ChEBI:58548 S-methyl-5-thio-D-ribulose 1-phosphate(2?)
S-methyl-5-thio-D-ribulose 1-phosphate(2?)
RNA Polymerase II Transcription Initiation And Promoter Clearance
Homologues of K48poluUb-phospho-PAK-2p34(Thr402)
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
Temporal differences in the activation of three classes of non-transmembrane protein tyrosine kinases following B-cell antigen receptor surface engagement
TAX-responsive enhancer element binding protein 107
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Cell surface heparin binding protein HIP
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Human UDP-glucuronosyltransferases: metabolism, expression, and disease
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Polymerase II promoter activation: closed complex formation and ATP-driven start site opening.
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Human minichromosome maintenance proteins and human origin recognition complex 2 protein on chromatin.
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Eukaryotic peptide chain release factor subunit 1
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S-methyl-5-thio-?-D-ribose 1-phosphate(2?)
ChEBI:58533 S-methyl-5-thio-?-D-ribose 1-phosphate(2?)
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Mucopolysaccharidosis IV A: assignment of the human N-acetylgalactosamine-6-sulfate sulfatase (GALNS) gene to chromosome 16q24
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Multiple inositol polyphosphate phosphatase: evolution as a distinct group within the histidine phosphatase family and chromosomal localization of the human and mouse genes to chromosomes 10q23 and 19
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Molecular cloning and expression of the human delta7-sterol reductase
Post-Elongation Processing of the Transcript
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E2F mediates developmental and cell cycle regulation of ORC1 in Drosophila
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Cloning of full-length methylmalonyl-CoA mutase from a cDNA library using the polymerase chain reaction
Cyclic GMP phosphodiesterase-5: target of sildenafil
Aromatic amines can be N-hydroxylated or N-dealkylated by CYP1A2
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Subcellular localization and secretion of factor V from human platelets
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cDNA sequence and gene locus of the human retinal phosphoinositide-specific phospholipase-C beta 4 (PLCB4)
A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system
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The cytosolic exonuclease TREX1 inhibits the innate immune response to human immunodeficiency virus type 1
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N-retinylidenephosphatidylethanolamine [ChEBI:71063]
Human SPA-1 gene product selectively expressed in lymphoid tissues is a specific GTPase-activating protein for Rap1 and Rap2. Segregate expression profiles from a rap1GAP gene product
The AMP-activated protein kinase pathway--new players upstream and downstream
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
Unconventional Rac-GEF activity is mediated through the Dock180-ELMO complex
Characterization of human brain nicotinamide 5'-mononucleotide adenylyltransferase-2 and expression in human pancreas
Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways
Sequential actions of myotubularin lipid phosphatases regulate endosomal PI(3)P and growth factor receptor trafficking
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
The ALG10 locus of Saccharomyces cerevisiae encodes the alpha-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation
Clamping down on clamps and clamp loaders--the eukaryotic replication factor C.
SLIT-ROBO Rho GTPase-activating protein 1
Gene duplication and the evolution of group II chaperonins: implications for structure and function
Point mutations in a hinge linking the small and large domains of beta-actin result in trapped folding intermediates bound to cytosolic chaperonin CCT
Human securin proteolysis is controlled by the spindle checkpoint and reveals when the APC/C switches from activation by Cdc20 to Cdh1
Coming to grips with integrin binding to ligands
The role of CDP-diacylglycerol synthetase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content
Distinct functions of condensin I and II in mitotic chromosome assembly
Fatty acid, triacylglycerol, and ketone body metabolism
Mutation and polymorphism spectrum of the GALNS gene in mucopolysaccharidosis IVA (Morquio A)
Translational control by the 3'-UTR: the ends specify the means
Medin: an integral fragment of aortic smooth muscle cell-produced lactadherin forms the most common human amyloid
Identification of the erythrocyte Rh blood group glycoprotein as a mammalian ammonium transporter
53BP1 and NFBD1/MDC1-Nbs1 function in parallel interacting pathways activating ataxia-telangiectasia mutated (ATM) in response to DNA damage.
Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits
Identification and characterization of a lysophosphatidylcholine acyltransferase in alveolar type II cells
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
The neurotransmitter cycle and quantal size
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Endocytic compartments contain many cysteine proteases such as cathepsin S that can generate cross-presented peptides. Cathepsins may participate in the generation of MHC class II-presentated peptides (Villadangos et al. 1999). Shen et al. (2004) demonstrated that cathepsin S contributes to TAP-independent cross-presentation in vivo, showing that ovalbumin was cross-presented by denritic cells (DCs) through both TAP-dependent and TAP-independent pathways. The TAP-independent pathway was sensitive to the cystine protease inhibitor leupeptin, but not to proteasome inhibitors. Further experiments with knockout mice showed that cathepsin S contributed to cross-presentation. DCs lacking cathepsin S lack the TAP-independent pathway (Khor et al. 2008, Shen et al. 2004).
The other TAP-dependent cross-presentation mechanism in phagocytes is the endoplasmic reticulum (ER)-phagosome model. Desjardins proposed that ER is recruited to the cell surface, where it fuses with the plasma membrane, underneath phagocytic cups, to supply membrane for the formation of nascent phagosomes (Gagnon et al. 2002). Three independent studies simultaneously showed that ER contributes to the vast majority of phagosome membrane (Guermonprez et al. 2003, Houde et al. 2003, Ackerman et al. 2003). The composition of early phagosome membrane contains ER-resident proteins, the components required for cross-presentation. This model is similar to the phagosome-to-cytosol model in that Ag is translocated to cytosol for proteasomal degradation, but differs in that antigenic peptides are translocated back into the phagosome (instead of ER) for peptide:MHC-I complexes. ER fusion with phagosome introduces molecules that are involved in Ag transport to cytosol (Sec61) and proteasome-generated peptides back into the phagosome (TAP) for loading onto MHC-I. Through extensive biochemical assays, fluorescent imaging and electron microscopy-based experiments, most of the evidence in favor of ER-phagocytosis has been challenged (Touret et al. 2005a/b). Using quantitative proteomics Roger and Foster have shown that the percentage of PM and ER membranes on phagosomes 10 min after internalization was approximately 10% and 0.2% (Rogers et al. 2007). They concluded that ER contributes only a small part of phagosomal membranes. Although the ER-phagosome pathway is controversial, the concept remains attractive as it explains how peptide-receptive MHC-I molecules could intersect with a relatively high concentration of exogenous antigens, presumably a crucial prerequisite for efficient cross-presentation (Basha et al. 2008).
Exogenous antigens are thought to be processed for cross-presentation in much the same manner as endogenous proteins once they enter the cytosolic pathway (Rock et al. 2010). Immunoproteasome components are the major proteases involved in generating the antigenic fragments. The precurssor peptides are further trimmed by cytosolic aminopeptidases and shuttled to ER through TAP for MHC class I loading.
Some antigens are cross-presented through a vacuolar mechanism that involves generation of antigenic peptides and their loading on to MHC-I molecules within the endosomal compartment in a proteasome and TAP-independent manner. Antigens within the endosome are processed by cathepsin S and other proteases into antigenic peptides. Loading of these peptides onto MHC-I molecules occurs directly within early and late endosomal compartments. Why certain antigens are cross-presented exclusively by the cytosolic pathway while others use the vacuolar pathway is unknown. It may be because some epitopes cannot be generated by endosomal proteolysis, or are completely destroyed. Alternatively, the physical form of the antigen may influence its accessibility to the endosomal or vacuolar pathways (Shen et al. 2004).
CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution
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MHC class I molecules generally present peptide antigens derived from proteins synthesized by the cell itself to CD8+ T cells. However, in some circumstances, antigens from extracellular environment can be presented on MHC class I to stimulate CD8+ T cell immunity, a process termed cross-presentation (Rock & Shen. 2005). Cross-presentation/cross-priming is the ability of antigen presenting cells (APCs) to present exogenous antigens on MHC class I molecules to CD8+ T lymphocytes. Among all the APCs, Dendritic cells (DC) are the dominant antigen cross presenting cell types in vivo, although macrophages and B cells appear to cross present model antigens in vitro with a low degree of efficiency (Amigorena & Savina. 2010, Ackermann & Peter Cresswell. 2004). Compared to macrophages, DCs have low levels of lysosomal proteases and exhibit limited lysosomal degradation (Delamarre et al. 2005). This limited proteolysis of internalized antigens by DCs might contribute to their high efficiency for cross presentation (Monua & Trombetta. 2007). APCs acquire the exogenous antigens through endocytic mechanisms, especially phagosomes for particulate/cell-associated antigens and endosomes for soluble protein antigens. There does not seem to be a unique pathway for cross-presentation but rather different potential mechanisms of cross-presentation have been proposed. These proposed pathways can be classified according to the location where two key events occur: 1) processing of the antigenic protein and 2) loading of the processed peptide on to MHC I molecule (Blanchard & Shastri. 2010). Based on the requirement for TAP and cytosolic proteases two mechanisms have been described, a cytosolic pathway (TAP-dependent and proteasome-dependent) or a vacuolar pathway (TAP- and proteasome-independent) (Blanchard & Shastri. 2010, Amigorena & Savina. 2010). Regarding peptide-loading, MHC I could be loaded in the ER or in the phagosome and recycled to cell surface (Blanchard & Shastri. 2010). Exogenous soluble antigens are cross-presented by dendritic cells, albeit with lower efficiency than for particulate substrates. Soluble antigens destined for cross-presentation are taken up by distinct endocytosis mechanisms which route them into stable early endosomes and then to the cytoplasm for proteasomal degradation and peptide loading. The outcome of the cross presentation can be either tolerance or immunity (Rock & Shen. 2005).
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Exogenous soluble antigens are cross-presented by dendritic cells, albeit with lower efficiency than for particulate substrates. Soluble antigens destined for cross-presentation are taken up by distinct endocytosis mechanisms which route them into stable early endosomes and then to the cytoplasm for proteasomal degradation and peptide loading.
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Major histocompatibility complex (MHC) class I molecules play an important role in cell mediated immunity by reporting on intracellular events such as viral infection, the presence of intracellular bacteria or tumor-associated antigens. They bind peptide fragments of these proteins and presenting them to CD8+ T cells at the cell surface. This enables cytotoxic T cells to identify and eliminate cells that are synthesizing abnormal or foreign proteins. MHC class I is a trimeric complex composed of a polymorphic heavy chain (HC or alpha chain) and an invariable light chain, known as beta2-microglobulin (B2M) plus an 8-10 residue peptide ligand. Represented here are the events in the biosynthesis of MHC class I molecules, including generation of antigenic peptides by the ubiquitin/26S-proteasome system, delivery of these peptides to the endoplasmic reticulum (ER), loading of peptides to MHC class I molecules and display of MHC class I complexes on the cell surface.
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Cloning, expression, and cellular localization of the oncogenic 58-kDa inhibitor of the RNA-activated human and mouse protein kinase
Early phagosomes in dendritic cells form a cellular compartment sufficient for cross presentation of exogenous antigens
GTPase signaling: bridging the GAP between ARF and Rho
Presenilin-dependent ErbB4 nuclear signaling regulates the timing of astrogenesis in the developing brain
Mutations in the gene for the E1beta subunit: a novel cause of pyruvate dehydrogenase deficiency
How nucleotide excision repair protects against cancer.
Generation of major histocompatibility complex class I antigens: functional interplay between proteasomes and TPPII
Post-proteasomal antigen processing for major histocompatibility complex class I presentation
The exogenous pathway for antigen presentation on major histocompatibility complex class II and CD1 molecules
Red cell membrane CO2 permeability in normal human blood and in blood deficient in various blood groups, and effect of DIDS
Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia.
DAG and calcium activate protein kinase C beta (PKC-beta, Kochs et al. 1991) which phosphorylates CARMA1 and other proteins (Sommer et al. 2005). Phosphorylated CARMA1 recruits BCL10 and MALT1 to form the CBM complex (Sommer et al. 2005, Tanner et al. 2007) which, in turn, recruits the kinase TAK1 and the IKK complex (Sommer et al. 2005, Shinohara et al. 2005 using chicken cells). TAK1 phosphorylates the IKK-beta subunit, activating it (Wang et al. 2001). The IKK complex then phosphorylates IkB complexed with NF-kappaB dimers in the cytosol (Zandi et al. 1998, Burke et al. 1999, Heilker et al. 1999), resulting in the degradation of IkB (Miyamoto et al. 1994, Traenckner et al. 1994, Alkalay et al. 1995, DiDonato et al. 1995, Li et al. 1995, Lin et al. 1995, Scherer et al. 1995, Chen et al. 1995). NF-kappaB dimers are thereby released and are translocated to the nucleus where they activate transcription (Baeuerle and Baltimore 1988, Blank et al. 1991, Ghosh et al. 2008, Fagerlund et al. 2008).
Selectivity in post-translational biotin addition to five human carboxylases
RasGRP1 and RasGRP3 translocate to the plasma membrane where they bind diacylglycerol (Lorenzo et al. 2001) and are phosphorylated (Teixeira et al. 2003, Zheng et al. 2005). Though RasGRP3 is phosphorylated in vitro and in some cell lines (e.g. Ramos cells) by protein kinase C theta (PKC-theta, Zheng et al. 2005), normal B cells do not contain PKC-theta (Meller et al. 1999). Both Rasgrp1 and Rasgrp3 participate in activating Ras in response to BCR signaling in mouse B cells (Coughlin et al. 2005).
Mature B cells express IgM and IgD immunoglobulins which are complexed with Ig-alpha (CD79A, MB-1) and Ig-beta (CD79B, B29) to form the B cell receptor (BCR) (Fu et al. 1974, Fu et al. 1975, Kunkel et al. 1975, Van Noesal et al. 1992, Sanchez et al. 1993, reviewed in Brezski and Monroe 2008). Binding of antigen to the immunoglobulin activates phosphorylation of immunoreceptor tyrosine-based activation motifs (ITAMs) in the cytoplasmic tails of Ig-alpha and Ig-beta by Src family tyrosine kinases, including LYN, FYN, and BLK (Nel et al. 1984, Yamanashi et al. 1991, Flaswinkel and Reth 1994, Saouaf et al. 1994, Hata et al. 1994, Saouaf et al. 1995, reviewed in Gauld and Cambier 2004, reviewed in Harwood and Batista 2010). The protein kinase SYK may also be involved in phosphorylating the ITAMs. The protein kinase SYK binds the phosphorylated immunoreceptor tyrosine-activated motifs (ITAMs) on the cytoplasmic tails of Ig-alpha (CD79A, MB-1) and Ig-beta (CD79B, B29) (Wienands et al. 1995, Rowley et al. 1995, Tsang et al. 2008). The binding causes the activation and autophosphorylation of SYK (Law et al. 1994, Irish et al. 2006, Baldock et al. 2008, Tsang et al. 2008, reviewed in Bradshaw 2010). Activated SYK and other kinases phosphorylate BLNK (SLP-65, BASH) and BCAP. LYN and FYN phosphorylate CD19. Phosphorylated BLNK, BCAP, and CD19 serve as scaffolds which recruit effectors to the plasma membrane and assemble large complexes, the signalosomes. BCAP and CD19 recruit phosphoinositol 3-kinase (PI3K). BLNK recruits phospholipase C gamma (predominantly PLC-gamma2 in B cells, Coggeshall et al. 1992), NCK, BAM32, BTK, VAV1, and SHC. The effectors are phosphorylated by SYK and other kinases. Phosphorylated BCAP recruits PI3K, which is phosphorylated by a SYK-dependent mechanism (Kuwahara et al. 1996) and produces phosphatidylinositol-3,4,5-trisphosphate (PIP3). Phosphorylated CD19 likewise recruits PIP3K. PIP3 recruits BAM32 (Marshall et al. 2000) and BTK (de Weers et al. 1994, Baba et al. 2001) to the plasma membrane via their PH domains. PIP3 also recruits and activates PLC-gamma1 and PLC-gamma2 (Bae et al. 1998). BTK binds phosphorylated BLNK via its SH2 domain (Baba et al. 2001). BTK phosphorylates PLC-gamma2 (Rodriguez et al. 2001), which activates phospholipase activity (Carter et al. 1991, Roifman and Wang 1992, Kim et al. 2004, Sekiya et al. 2004). Phosphorylated BLNK recruits PLC-gamma, VAV, GRB2, and NCK (Fu and Chan 1997, Fu et al. 1998, Chiu et al. 2002). PLC-gamma hydrolyzes phosphatidylinositol-4,5-bisphosphate to yield inositol-1,4,5-trisphosphate (IP3) and diacylglycerol (Carter et al. 1991, Kim et al. 2004). IP3 binds receptors on the endoplasmic reticulum and causes release of Ca2+ ions from the ER into the cytosol. The depletion of calcium from the ER in turn activates STIM1 to interact with ORAI and TRPC1 channels (and possibly other TRP channels) in the plasma membrane, resulting in an influx of extracellular calcium ions (Mori et al. 2002, Muik et al. 2008, Luik et al. 2008, Park et al. 2009).
Human Protein kinase C beta (PKC-beta) is activated by calcium ions, diacylglycerol, and binds phosphatidylserine (Kochs et al. 1991). Experiments in mice have shown that knocking out PKC-beta causes severe defects in B cells, leading to the conclusion that PKC-beta is the predominant signaling PKC in these cells (Leitges et al. 1996, Su et al. 2002, Saijo et al. 2002).
GSK3 (glycogen synthase kinase-3) participates in the Wnt signaling pathway. It is implicated in the hormonal control of several regulatory proteins including glycogen synthase, and the transcription factors MYB and JUN. GSK3 phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA. GSK3 is inhibited when phosphorylated by AKT1.
Following activation, AKT can phosphorylate an array of target proteins in the cytoplasm, many of which are involved in cell survival control. Phosphorylation of TSC2 feeds positively to the TOR kinase, which, in turn, contributes to AKT activation (positive feedback loop).
RasGRP1 (Roose et al. 2007) and RasGRP3 (Ohba et al. 2000, Yamashita et al. 2000, Rebhun et al. 2000, Lorenzo et al. 2001) catalyze the exchange of GDP for GTP bound by RAS.
RasGRP1 and RasGRP3 bind diacylglycerol at the plasma membrane (Lorenzo et al. 2001) and are phosphorylated by protein kinase C (Teixeira et al. 2003, Zheng et al. 2005). Phosphorylated RasGRP1 (Roose et al. 2007) and RasGRP3 (Ohba et al. 2000, Yamashita et al. 2000, Rebhun et al. 2000, Lorenzo et al. 2001) then catalyze the exchange of GDP for GTP bound by RAS, thereby activating RAS.
AKT, phosphorylated at threonine (AKT1 308; AKT2 309; AKT3 305) and serine (AKT1 473; AKT2 474; AKT3 472) translocates to the nucleus, reaching a maximum after 15 min and returning to a basal level after 45 min of NGF stimulation. Control of the amount of nuclear AKT is achieved through the action of the phosphatase PP2A.
Ribosomal protein S6 kinase beta-2 (RSK) activation is a highly conserved mitogenic response, and the activities of RSK are stimulated by multiple serine/threonine phosphorylations by different upstream kinases, one of which is AKT.
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Epstein-Barr virus small RNA associated protein
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After translocation into the nucleus, AKT can phosphorylate a number of targets there such as CREB, forkhead transcription factors, SRK and NUR77.
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Once phosphorylated on serine residue S473, AKT bound to PIP3 forms a complex with PIP3-bound PDPK1 i.e. PDK1 (Scheid et al. 2002, Sarabassov et al. 2005)
Once AKT is localized at the plasma membrane, it is phosphorylated at two critical residues for its full activation. These residues are a threonine (T308 in AKT1) in the activation loop within the catalytic domain, and a serine (S473 in AKT1), in a hydrophobic motif (HM) within the carboxy terminal, non-catalytic region. PDPK1 (PDK1) is the activation loop kinase; this kinase can also directly phosphorylate p70S6K. The HM kinase, previously termed PDK2, has been identified as the mammalian TOR (Target Of Rapamycin; Sarbassov et al., 2005) but several other kinases are also able to phosphorylate AKT at S473. Phosphorylation of AKT at S473 by TORC2 complex is a prerequisite for PDPK1-mediated phosphorylation of AKT threonine T308 (Scheid et al. 2002, Sarabassov et al. 2005).
Roberts syndrome: a review of 100 cases and a new rating system for severity
PI3Ks can be activated by a number of different receptors, including the TcR (T cell receptor), co-stimulatory receptors (CD28), cytokine receptors and chemokine receptors. However, the specific roles of PI3Ks downstream of these receptors vary. CD28 contains the YMNM consensus PI3K-binding motif, and PI3K recruitment by CD28 contributes to or complements TCR-dependent PI3K signaling. Activation of PI3K promotes PIP3 production at the plasma membrane and several potential target molecules for this phospholipid have been implicated in PI3K pathways downstream of the TcR and CD28. Of these targets, at least Vav and Akt have been implicated in CD28 costimulation of T cell activation. AKT/PKB connects PI3K to signaling pathways that promote cytokine transcription, survival, cell-cycle entry and growth.
In its unbound state PAK is maintained in an inactive conformation through intra domain interactions. On stimulation PAK is translocated to the plasma membrane where it specifically interacts with Rho family GTP-binding proteins Rac1-GTP and Cdc42-GTP. All PAK isoforms are direct effectors of the Rac and Cdc42. Rac and Cdc42 bind to a highly conserved motif in the amino terminus of PAK known as p21-binding domain (PBD) or Cdc42/Rac interactive binding (CRIB) domain. This binding is thought to induce a conformational change in PAK that relieves autoinhibition of the catalytic carboxy terminal domain, thereby inducing autophosphorylation at several sites and enabling the phosphorylation of exogenous substrates.
CD28 binds to several intracellular proteins including PI3 kinase, Grb-2, Gads and ITK. Grb-2 specifically co-operates with Vav-1 in the up-regulation of NFAT/AP-1 transcription. CD28 costimulation resulted in a prolonged and sustained phosphorylation and membrane localization of Vav1 in comparison to T-cell receptor activation alone. Tyrosine-phosphorylated Vav1 is an early point of integration between the signaling routes triggered by the T-cell receptor and CD28. Vav1 transduces TCR and co-stimulatory signals to multiple biochemical pathways and several cytoskeleton-dependent processes. The products of Vav1 activation, Rac1 and Cdc42, in turn activate the mitogen-activated protein kinases JNK and p38. Vav1 is also required for TCR-induced calcium flux, activation of the ERK MAP kinase pathway, activation of the NF-kB transcription factor, inside-out activation of the integrin LFA-1, TCR clustering, and polarisation of the T cell.
In naive T cells, CD28 costimulation enhances cell cycle entry, potently stimulates expression of both the mitogenic lymphokine interleukin-2 (IL-2) and its receptor, and stimulates the activation of an antiapoptotic program. CD28 engages with one or both members of the B7 receptor family, B7.1 and B7.2. Upon ligand binding the tyrosines and proline-rich motifs present in the cytoplasmic tail of CD28 are phosphorylated by Lck or Fyn. Upon phosphorylation CD28 recruits and induces phosphorylation and activation of a more restricted set of intracellular signaling components that, together with those mobilized by the TCR, contribute to convert membrane-based biochemical and biophysical changes into gene activation events. Proteins like PI3K, Vav-1, Tec and Itk kinases, AKT, and the Dok-1 adaptor have been identified as elements of the CD28 signaling pathway by biochemical or genetic approaches or both.
When CTLA4 is engaged by B7 molecules, PP2A disassociates from CTLA4 in a phosphorylation dependent manner. Released PP2A acts downstream of early TCR and CD28 signaling, by inhibition of the PKB/Akt pathway.
CTLA4 is one of the best studied inhibitory receptors of the CD28 superfamily. CTLA4 inhibits Tcell activation by reducing IL2 production and IL2 expression, and by arresting T cells at the G1 phase of the cell cycle. CTLA-4 expressed by a T cell subpopulation exerts a dominant control on the proliferation of other T cells, which limits autoreactivity. CTLA4 also blocks CD28 signals by competing for the ligands B71 and B72 in the limited space between T cells and antigenpresenting cells. Though the mechanism is obscure, CTLA4 may also propagate inhibitory signals that actively counter those produced by CD28. CTLA4 can also function in a ligand-independent manner.? CTLA-4 regulates the activation of pathogenic T cells by directly modulating T cell receptor signaling (i.e. TCR-zeta chain phosphorylation) as well as downstream biochemical signals (i.e. ERK activation). The cytoplasmic region of CTLA4 contains a tyrosine motif YVKM and a proline rich region. After TCR stimulation, it undergoes tyrosine phosphorylation by src kinases, inducing surface retention.
Optimal activation of T-lymphocytes requires at least two signals. A primary one is delivered by the T-cell receptor (TCR) complex after antigen recognition and additional costimulatory signals are delivered by the engagement of costimulatory receptors such as CD28. The best-characterized costimulatory pathways are mediated by a set of cosignaling molecules belonging to the CD28 superfamily, including CD28, CTLA4, ICOS, PD1 and BTLA receptors. These proteins deliver both positive and negative second signals to T-cells by interacting with B7 family ligands expressed on antigen presenting cells. Different subsets of T-cells have very different requirements for costimulation. CD28 family mediated costimulation is not required for all T-cell responses in vivo, and alternative costimulatory pathways also exist. Different receptors of the CD28 family and their ligands have different regulation of expression. CD28 is constitutively expressed on naive T cells whereas CTLA4 expression is dependent on CD28/B7 engagement and the other receptor members ICOS, PD1 and BTLA are induced after initial T-cell stimulation. The positive signals induced by CD28 and ICOS molecules are counterbalanced by other members of the CD28 family, including cytotoxic T-lymphocyte associated antigen (CTLA)4, programmed cell death (PD)1, and B and T lymphocyte attenuator (BTLA), which dampen immune responses. The balance of stimulatory and inhibitory signals is crucial to maximize protective immune responses while maintaining immunological tolerance and preventing autoimmunity. The costimulatory receptors CD28, CTLA4, ICOS and PD1 are composed of single extracellular IgV-like domains, whereas BTLA has one IgC-like domain. Receptors CTLA4, CD28 and ICOS are covalent homodimers, due to an interchain disulphide linkage. The costimulatory ligands B71, B72, B7H2, B7H1 and B7DC, have a membrane proximal IgC-like domain and a membrane distal IgV-like domain that is responsible for receptor binding and dimerization. CD28 and CTLA4 have no known intrinsic enzymatic activity. Instead, engagement by their physiologic ligands B71 and B72 leads to the physical recruitment and activation of downstream T-cell effector molecules.
Upon increase in calcium concentration, calmodulin (CaM) is activated by binding to four calcium ions.
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RhoGDIs revisited: novel roles in Rho regulation
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After internalization, F-actin is depolymerized from the phagosome, and the newly denuded vacuole membrane becomes accessible to early endosomes (Aderem & Underhill. 1999).
Dendritic cells (DCs) take up and process exogenous particulate or cell-associated antigens such as microbes or tumor cells for MHC-I cross-presentation. Particulate antigens have been reported to be more efficiently cross-presented than soluble antigens by DCs (Khor et al. 2008). Particulate antigens are internalized by phagosomes. There are two established models that explain the mechanism by which exogenous particulate antigens are presented through MHC I; the cytosolic pathway where internalized antigens are somehow translocated from phagosomes into cytosol for proteasomal degradation and the vacuolar pathway (Lin et al. 2008, Amigorena et al. 2010).
Unlike other glycoproteins, correct folding of MHC class I molecules is not sufficient to trigger their exit from the ER, they exit only after peptide loading. Described here is the process of antigen presentation which consists of the folding, assembly, and peptide loading of MHC class I molecules. The newly synthesized MHC class I Heavy Chain (HC) is initially folded with the help of several chaperones (calnexin, BiP, ERp57) and then binds with Beta-2-microglobulin (B2M). This MHC:B2M heterodimer enters the peptide loading complex (PLC), a multiprotein complex that includes calreticulin, endoplasmic reticulum resident protein 57 (ERp57), transporter associated with antigen processing (TAP) and tapasin. Peptides generated from Ub-proteolysis are transported into the ER through TAP. These peptides are further trimmed by ER-associated aminopeptidase (ERAP) and loaded on to MHC class I molecules. Stable MHC class I trimers with high-affinity peptide are transported from the ER to the cell surface by the Golgi apparatus.
Dendritic cells (DCs) and macrophages recognize and phagocytose apoptotic cells/invading microorganisms using a variety of receptors including lectins, Mannose receptor (MR) (Stahl & Ezekowitz. 1998), CD36 (Savill 1997), CD14 (Devitt et al. 1998), scavenger receptor A (SR-A) (Platt et al. 1996) and integrin alphaVbeta5 (Savill et al. 1992, Savilli et al. 1990), then cross-present cell-associated antigens to CD8+ T cells. Ligands on apoptotic cell like sugars, phosphatidylserine and surface-bound thrombospondin (TSP) are recognized by these receptors and induce rearrangements in the actin cytoskeleton that lead to the internalization of the particle.
Ttransporter associated with antigen processing (TAP) is a heterodimeric complex, composed of TAP1 and TAP2 proteins, members of the ATP-binding cassette (ABC) superfamily. TAP consists of two transmembrane domains (TMDs) and two cytosolic nucleotide-binding domains. Peptide binding to the cytosolic-facing cavity formed by the TMDs causes it to undergo a conformational change that induces ATP hydrolysis, forcing the opening of a pore and translocation of the peptide into the ER lumen. TAP transports peptides in the range of 8-16 amino acids into the ER, which is the peptide length typically generated by the immunoproteasome.
Transporter associated with antigen processing (TAP) prefers peptides 8-16 residues long, slightly longer than the canonical 8-10 residue peptides that fit into class I MHC binding sites. These longer peptides are further trimmed at their N-termini by the ER-associated aminopeptidase (ERAP). ERAP trims peptides to a length of 8-10 residues, suitable for loading into the MHC class I binding groove.
Some peptides generated by the 26S proteasome are too long to bind to MHC class I molecules. These N-terminal extended precursor peptides may be trimmed by cytosolic aminopeptidases, such as Tripeptidyl peptidase II (TPP2), puromycin-sensitive aminopeptidase (PSA), bleomycin hydrolase (BH), and leucine aminopeptidase (LAP).
Intracellular foreign or aberrant host proteins are cleaved into peptide fragments of a precise size, such that they can be loaded on to class I MHC molecules and presented externally to cytotoxic T cells. The ubiquitin-26S proteasome system plays a central role in the generation of these class I MHC antigens. Ubiquitination is the mechanism of adding ubiquitin to lysine residues on substrate protein leading to the formation of a polyubiquitinated substrate. This process involves three classes of enzyme, an E1 ubiquitin-activating enzyme, an E2 ubiquitin-conjugating enzyme, and an E3 ubiquitin ligase. Polyubiquitination through lysine-48 (K48) generally targets the substrate protein for proteasomal destruction. The protease responsible for the degradation of K48-polyubiquitinated proteins is the 26S proteasome. This proteasome is a two subunit protein complex composed of the 20S (catalytic core) and 19S (regulatory) proteasome complexes. The proteasome eliminates most of the foreign and non-functional proteins from the cell by degrading them into short peptides; only a small fraction of the peptides generated are of the correct length to be presented by the MHC class I system. It has been calculated that between 994 and 3122 protein molecules have to be degraded for the formation of a single, stable MHC class I complex at the cell surface, with an average effciency of 1 in 2000 (Kloetzel et al. 2004, Princiotta et al. 2003).
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Multidrug resistance- associated protein MGr1-Ag
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After processing by the proteasome, some of the oligopeptides could be reinternalized to the phagosome lumen of the same phagosome through the TAP complex probably acquired during ER-phagosome fusion. Guermonprez et al. (2003) tested this model and observed abundant TAP complex in early phagosomes and its reduction over time. Electron microscopy analysis of purified phagosomes also showed the insertion of TAP2 into the phagosomal membrane.
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Proteasomes are usually localized to the cytoplasm but are also present in the nucleus and ER. Houde et al. (2003) investigated the distribution of proteasomes in J774 macrophages and observed them on phagosomes. The proteasomes present on phagosomes may not come directly from ER, but instead assemble on phagosomes to play a function at a precise point during phagolysosomal biogenesis. Houde et al. also observed polyubiquitinated proteins on the cytoplasmic side of phagosomes and highlighted the link between the ubiquitination process and proteasomal degradation; translocated peptides are ubiquitinated and processed by the proteasome complex assembled on the cytoplasmic side of phagosomes, leading to the generation of MHC class I binding peptides.
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Fusion of the maturing phagosome with the ER mediates the exchange of materials resulting in the formation of a hybrid ER-phagosome compartment (Gagnon et al. 2002, Guermonprez et al. 2003, Houde et al. 2003, Ackerman et al. 2003, Blanchard et al. 2010). This hybrid contains the retrotranslocon factor Sec61 that mediates the access of proteasomes on the cytosolic surface of the phagosome. Using fluorescence imaging, Houde et al. (2003) provided evidence for the role of Sec61 in the retrotranslocation of internalized exogenous proteins from phagosomes to the cytoplasmic face of J774 macrophages. Sec61 factor is a heterotrimeric complex composed of alpha, beta and gamma subunits forming the core of the mammalian ER translocon (Greenfield et al. 1999). Oligomers of the Sec61 complex form a transmembrane channel involved in the retrotranslocation of misfolded proteins from ER to the cytosol for degradation, and thus it has been proposed that Sec61 might be involved in the translocation of proteins in phagosomes to the cytosol (Kasturi et al. 2008).
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Signaling by AKT is one of the key outcomes of receptor tyrosine kinase (RTK) activation. AKT is activated by the cellular second messenger PIP3, a phospholipid that is generated by PI3K. In ustimulated cells, PI3K class IA enzymes reside in the cytosol as inactive heterodimers composed of p85 regulatory subunit and p110 catalytic subunit. In this complex, p85 stabilizes p110 while inhibiting its catalytic activity. Upon binding of extracellular ligands to RTKs, receptors dimerize and undergo autophosphorylation. The regulatory subunit of PI3K, p85, is recruited to phosphorylated cytosolic RTK domains either directly or indirectly, through adaptor proteins, leading to a conformational change in the PI3K IA heterodimer that relieves inhibition of the p110 catalytic subunit. Activated PI3K IA phosphorylates PIP2, converting it to PIP3; this reaction is negatively regulated by PTEN phosphatase. PIP3 recruits AKT to the plasma membrane, allowing TORC2 to phosphorylate a conserved serine residue of AKT. Phosphorylation of this serine induces a conformation change in AKT, exposing a conserved threonine residue that is then phosphorylated by PDPK1 (PDK1). Phosphorylation of both the threonine and the serine residue is required to fully activate AKT. The active AKT then dissociates from PIP3 and phosphorylates a number of cytosolic and nuclear proteins that play important roles in cell survival and metabolism. For a recent review of AKT signaling, please refer to Manning and Cantley, 2007.
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Second messengers (calcium, diacylglycerol, inositol 1,4,5-trisphosphate, and phosphatidyinositol 3,4,5-trisphosphate) trigger signaling pathways: NF-kappaB is activated via protein kinase C beta, RAS via RasGRP proteins, NF-AT via calcineurin, and AKT via PDK1 (reviewed in Shinohara and Kurosaki 2009, Stone 2006).
Mature B cells express IgM and IgD immunoglobulins which are complexed at the plasma membrane with Ig-alpha (CD79A, MB-1) and Ig-beta (CD79B, B29) to form the B cell receptor (BCR) (Fu et al. 1974, Fu et al. 1975, Kunkel et al. 1975, Van Noesel et al. 1992, Sanchez et al. 1993, reviewed in Brezski and Monroe 2008). Binding of antigen to the immunoglobulin activates phosphorylation of immunoreceptor tyrosine-based activation motifs (ITAMs) in the cytoplasmic tails of Ig-alpha and Ig-beta by Src family tyrosine kinases, including LYN, FYN, and BLK (Nel et al. 1984, Yamanashi et al. 1991, Flaswinkel and Reth 1994, Saouaf et al. 1994, Hata et al. 1994, Saouaf et al. 1995, reviewed in Gauld and Cambier 2004, reviewed in Harwood and Batista 2010). The protein kinase SYK binds the phosphorylated immunoreceptor tyrosine-activated motifs (ITAMs) on the cytoplasmic tails of Ig-alpha (CD79A, MB-1) and Ig-beta (CD79B, B29) (Wienands et al. 1995, Rowley et al. 1995, Tsang et al. 2008). The binding causes the activation and autophosphorylation of SYK (Law et al. 1994, Baldock et al. 2000, Irish et al. 2006, Tsang et al. 2008, reviewed in Bradshaw 2010). Activated SYK and other kinases phosphorylate BLNK (SLP-65), BCAP, and CD19 which serve as scaffolds for the assembly of large complexes, the signalosomes, by recruiting phosphoinositol 3-kinase (PI3K), phospholipase C gamma (predominantly PLC-gamma2 in B cells, Coggeshall et al. 1992), NCK, BAM32, BTK, VAV1, and SHC. The effectors are phosphorylated by SYK and other kinases. PLC-gamma associated with BLNK hydrolyzes phosphatidylinositol-4,5-bisphosphate to yield inositol-1,4,5-trisphosphate (IP3) and diacylglycerol (Carter et al. 1991, Kim et al. 2004). IP3 binds receptors on the endoplasmic reticulum and causes release of calcium ions from the ER into the cytosol. The depletion of calcium from the ER in turn activates STIM1 to interact with ORAI and TRPC1 channels in the plasma membrane, resulting in an influx of extracellular calcium ions (Muik et al. 2008, Luik et al. 2008, Park et al. 2009, Mori et al. 2002). PI3K associated with BCAP and CD19 phosphorylates phosphatidylinositol 4,5-bisphosphate to yield phosphatidyinositol 3,4,5-trisphosphate. Second messengers (calcium, diacylglycerol, inositol 1,4,5-trisphosphate, and phosphatidylinositol 3,4,5-trisphosphate) trigger signaling pathways: NF-kappaB is activated via protein kinase C beta, RAS is activated via RasGRP proteins, NF-AT is activated via calcineurin, and AKT (PKB) is activated via PDK1 (reviewed in Shinohara and Kurosaki 2009, Stone 2006).
Ubiquitin is activated in an ATP-dependent manner, catalyzed by E1 ubiquitin-activating enzymes. In the first step of ubiquitin activation, the E1 enzyme binds ATP, Mg+2 and ubiquitin, and catalyses ubiquitin C-terminal acyl-adenylation (Ubiquitin-AMP). In the second step, the catalytic cystine in the E1 attacks the ubiquitin-adenylate (Ub-AMP) to form the activated ubiquitin-E1 thioester-bonded complex and an AMP leaving group. The intermediate reaction involving the formation of the ubiquitin-AMP complex is not represented here.
The PI3K network is negatively regulated by phospholipid phosphatases that dephosphorylate PIP3, thus hampering AKT activation (Maehema et al. 1998). The tumour suppressor PTEN is the primary phospholipid phosphatase. The role of other phosphoinositide phosphatases (INPP5D, INPPL1, INPP5K, PTPRQ, INPP4B) in the negative regulation of PI3K/AKT signaling will be described in future editions of Reactome.
At the plasma membrane, phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase aka phosphatase and tensin homolog (PTEN) dephosphorylates phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) to phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) (Maehama & Dixon 1998, Myers et al. 1998, Das et al. 2003).
Characterization of solanesyl and decaprenyl diphosphate synthases in mice and humans
The PI3K/AKT network is negatively regulated by phosphatases that dephosphorylate PIP3, thus hampering AKT activation.
PDPK1 (PDK1) possesses low affinity for PIP2, so small amounts of PDPK1 are always present at the membrane, in the absence of PI3K activity (Currie et al. 1999).
Nomenclature of the GLUT/SLC2A family of sugar/polyol transport facilitators.
Am J Physiol Endocrinol Metab 282:E974-6
Activated ubiquitin is transferred from E1 to the active site cystine of ubiquitin conjugating enzymes (E2s) via a trans-esterification reaction. E2s catalyze covalent attachment of ubiquitin to target proteins. They all share an active-site ubiquitin-binding cysteine residue and are distinguished by the presence of a ubiquitin-conjugating catalytic (UBC) fold required for binding of distinct ubiquitin ligases or E3s. Once conjugated to ubiquitin, the E2 molecule binds one of several E3s (Glickman et al. 2002).
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The 26S proteasome complex consists of the 20S catalytic core particle which harbours the proteolytically active sites and the regulatory 19S particle which is responsible for substrate interaction. This process generates a vast number (perhaps hundreds) of different peptides, depending on the length and sequence of the substrate protein. Only a small fraction of these peptides (nearly 10%) form the exact length to be presented by class I MHC; most (approximately 70%) are too short to bind. The remaining proteasome products (10-20%) are N-terminally extended precursors that require additional cleavage by cytosolic aminopeptidases for presentation by MHC class I molecules.
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Monoubiquitinated substrate acquires additional ubiquitin modifications in the form of multiple single attachments or a ubiquitin chain. Polyubiquitin chains added through K48 residue of ubiquitin typically targets the substrate for degradation (Raymond et al. 2009).
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Human 1-D-myo-inositol-3-phosphate synthase is functional in yeast
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TBC1D1 phosphorylated on serine-237 binds 14-3-3 proteins in assays with yeast 14-3-3 proteins BMH1 and BMH2 (Chen et al. 2008, Frosig et al. 2010). Binding with human 14-3-3 proteins is inferred.
In response to muscle contraction and insulin signaling, AMPK-alpha2 phosphorylates TBC1D1 on serine 237 and probably other residues (Frosig et al. 2010, Vichaiwong et al. 2010). As inferred from rat L6 muscle cells TBC1D1 colocalizes with perinuclear vesicles bearing GLUT4 and may be involved in an early step that mobilizes them (Chen et al. 2008). Human TBC1D1 appears cytosolic and is believed to be concentrated near vesicle membranes (Park et al. 2011).
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.
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.
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.
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.
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.
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.
AS160 (TBC1D4) phosphorylated on serines 318, 341, 570, 588, and 751 and threonine 642 binds to all 14-3-3 proteins, although binding to 14-3-3 delta is comparatively low (Ramm et al. 2006, Howlett et al. 2007, Ngo et al. 2009, Treebak et al. 2009, Koumanov et al. 2011). As inferred from mouse, binding to 14-3-3 does not interfere with the interaction between AS160 and IRAP (LNPEP).
As inferred from mouse, AKT2 and, to a lesser extent, AKT1 phosphorylate AS160 (TBC1D4) in response to insulin signaling (Howlett et al. 2007, Karlsson et al 2005). AS160, a RAB GTPase activating protein, interacts with IRAP (LNPEP) and is associated with cytoplasmic vesicles containing GLUT4.
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ADP and platelets: the end of the beginning
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The lysosomal vesicle is targeted to and fused with the plasma membrane, releasing its contents into the extracellular space.
The vamp2 associated vesicle docks and fuses with the plasma membrane.
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 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.
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.
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.
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.
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.
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).
Inactive Arf1-GDP then diffuses away from the membrane, initiating the disassembly of the lattice.
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Structure, expression profile and alternative processing of the human phosphatidylethanolamine N-methyltransferase (PEMT) gene
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Mechanism of B-cell receptor-induced phosphorylation and activation of phospholipase C-gamma2
PIP3 generated by PI3K recruits phosphatidylinositide-dependent protein kinase 1 (PDPK1 i.e. PDK1) to the membrane, through its PH (pleckstrin-homology) domain. PDPK1 binds PIP3 with high affinity, and also shows low affinity for PIP2 (Currie et al. 1999).
The TCR is a multisubunit complex that consists of clonotypic alpha/beta chains noncovalently associated with the invariant CD3 delta/epsilon/gamma and TCR zeta chains. T cell activation by antigen presenting cells (APCs) results in the activation of protein tyrosine kinases (PTKs) that associate with CD3 and TCR zeta subunits and the co-receptor CD4. Members of the Src kinases (Lck), Syk kinases (ZAP-70), Tec (Itk) and Csk families of nonreceptor PTKs play a crucial role in T cell activation. Activation of PTKs following TCR engagement results in the recruitment and tyrosine phosphorylation of enzymes such as phospholipase C gamma1 and Vav as well as critical adaptor proteins such as LAT, SLP-76 and Gads. These proximal activation leads to reorganization of the cytoskeleton as well as transcription activation of multiple genes leading to T lymphocyte proliferation, differentiation and/or effector function.
Under conditions of growth and mitogen stimulation S473 phosphorylation of AKT is carried out by mTOR (mammalian Target of Rapamycin). This kinase is found in two structurally and functionally distinct protein complexes, named TOR complex 1 (TORC1) and TOR complex 2 (TORC2). It is TORC2 complex, which is composed of mTOR, RICTOR, SIN1 (also named MAPKAP1) and LST8, that phosphorylates AKT at S473 (Sarbassov et al., 2005). This complex also regulates actin cytoskeletal reorganization (Jacinto et al., 2004; Sarbassov et al., 2004). TORC1, on the other hand, is a major regulator of ribosomal biogenesis and protein synthesis (Hay and Sonenberg, 2004). TORC1 regulates these processes largely by the phosphorylation/inactivation of the repressors of mRNA translation 4E binding proteins (4E BPs) and by the phosphorylation/activation of ribosomal S6 kinase (S6K1). TORC1 is also the principal regulator of autophagy. In other physiological conditions, other kinases may be responsible for AKT S473 phosphorylation. Phosphorylation of AKT on S473 by TORC2 complex is a prerequisite for AKT phosphorylation on T308 by PDPK1 (Scheid et al. 2002, Sarabassov et al. 2005).
PIP3 generated by PI3K recruits AKT (also known as protein kinase B) to the membrane, through its PH (pleckstrin-homology) domains. The binding of PIP3 to the PH domain of AKT is the rate-limiting step in AKT activation (Scheid et al. 2002). In mammals there are three AKT isoforms (AKT1-3) encoded by three separate genes. The three isoforms share a high degree of amino acid identity and have indistinguishable substrate specificity in vitro. However, isoform-preferred substrates in vivo cannot be ruled out. The relative expression of the three isoforms differs in different mammalian tissues: AKT1 is the predominant isoform in the majority of tissues, AKT2 is the predominant isoform in insulin-responsive tissues, and AKT3 is the predominant isoform in brain and testes. All 3 isoforms are expressed in human and mouse platelets (Yin et al. 2008; O'Brien et al. 2008). Note: all data in the pathway refer to AKT1, which is the most studied.
DAG along with intracellular calcium signals cooperatively to activate PKCs, which then trigger other pathways such as the NF-kB pathway, ultimately leading to mast cell degranulation and cytokine production (Wu 2011). MCs express several Protein kinase C (PKC) isozymes and these kinases are involved in both the activation and termination of the degranulation process. PKC-delta is a negative regulator of FCERI mediated mast cell degranulation, whereas PKC-theta facilitates in degranulation (Leitges et al. 2002, Liu et al. 2001). In response to FCERI activation PKC-theta translocates to membrane by binding to DAG with its C1 domain. PKC-theta exists in two conformations closed/inactive and open/active state. In resting state, PKC-theta is autoinhibited where the pseudosubstrate sequence in the N-terminal regulatory region of PKC-theta forms intramolecular interaction with the substrate-binding region in the catalytic domain. This prevents the catalytic domain gaining access to substrates. The allosteric change of PKC-theta from closed to open state involves two important mechanisms: DAG binding to the C1 domains and autophosphorylation of T538 on the activation loop. Interaction with DAG induces conformational change resulting in the exposure of the activation loop of PKC-theta (Wang et al. 2012, Melowic et al. 2007).
PKC theta is a member of the Ca++ independent and DAG dependent, novel PKC subfamily expressed mainly in T cells. It contains, N-term C2 like domain, a pseudosubstrate (PS), DAG binding (C1) domain and a C-term kinase domain. The PS sequence resembles an ideal substrate with the exception that it contains an alanine residue instead of a substrate serine residue, is bound to the kinase domain in the resting state. As a result, PKC theta is maintained in a closed inactive state, which is inaccessible to cellular substrates.
Changes in gene expression are required for the T cell to gain full proliferative competence and to produce effector cytokines. Three transcription factors in particular have been found to play a key role in TCR-stimulated changes in gene expression, namely NF-kB, NFAT and AP-1. A key step in NF-kB activation is the stimulation and translocation of PKC theta. The critical element that effects PKC theta activation is PI3K. This enzyme complex translocates to the plasma membrane by interacting with phospho-tyrosines on CD28 via its two SH2 domains located in p85 subunit. The p110 subunit of PI3K phosphorylates the inositol ring of PIP2 to generate PIP3 (steps 17-18). PIP3 may also be dephosphorylated by the phosphatase SHIP to generate PI-3,4-P2. PIP3 and PI-3,4-P2 acts as binding sites to the PH domain of PKB/Akt and PDK1 (steps 19, 21 and 22). PKB is activated in response to PI3K stimulation by PDK1 (step 23). PDK1 has an essential role in regulating the activation of PKC theta and recruitment of CBM complex to the immune synapse. PKC theta is a member of novel class (DAG dependent, Ca++ independent) of PKC and the only member known to translocate to this synapse. Prior to TCR stimulation PKC theta exists in an inactive closed conformation. Upon release of DAG, it binds to PKC theta via the C1 domain and undergoes phosphorylation on tyrosine 90 by Lck to attain an open conformation. PKC theta is further phosphorylated by PDK1 on threonine 538. This step is critical for PKC activity (steps 24-26). CARMA1 translocates to the plasma membrane following the interaction of its SH3 domain with the 'PxxP' motif on PDK1. CARMA1 is phosphorylated by PKC-theta on residue S552, leading to the oligomerization of CARMA1. This complex acts as a scaffold, recruiting Bcl10 to the synapse by interacting with their CARD domains. Bcl10 undergoes phosphorylation mediated by the enzyme RIP2. Activated Bcl10 then mediates the ubiquitination of NEMO by recruiting MALT1 and TRAF6. MALT1 binds to Bcl10 with its Ig-like domains and undergoes oligomerization. TRAF6 binds to the oligomerized MALT1 and also undergoes oligomerization. Oligomerized TRAF6 acts as a ubiquitin-protein ligase, catalyzing auto-K63-linked polyubiquitination (steps 27-33). This K-63 ubiquitinated TRAF6 activates TAK1 kinase bound to TAB2 and also ubiquitinates NEMO/IKK-gamma in the IKK complex. TAK1 undergoes autophosphorylation on residues T184 and T187 and gets activated. Activated TAK1 kinase phosphorylates IKK-beta on residues S177 and S181 in the activation loop and activates the IKK kinase activity. IKK-beta phosphorylates the IkB-alpha bound to the NF-kB heterodimer, on residues S19 and S23 and directs IkB-beta to 26S proteasome degradation (step 34-38 & 40). The NF-kB heterodimer with a free NTS sequence finally migrates to the nucleus to regulate gene transcription (step 39).
Raft localized PKC theta is further phosphorylated and activated by PDK1. The threonine residue (T538) in the kinase domain is the potential target of PDK1. Phosphorylation of this site is critical for the PKC theta kinase activity, and its ability to activate NF-kB pathway. PKC theta is later trans-autophopshorylated on putative phosphorylation sites (S676, S695) for the fine-tuning of its kinase activity.
PI3K activation results in recruitment of the serine/threonine kinase PDK1, (3-phosphoinositide-dependent kinase 1) to the plasma membrane where PDK1 subsequently phosphorylates and activates AKT. PDK1 with its PH domain binds to either PIP3 or PIP2 and is translocated to the plasma membrane. PDK1 seems to exist in an active, phosphorylated configuration under basal conditions (Vanhaesebroeck & Alessi 2000).
PTEN dephosphorylates 3' position of PIP3 to generate PIP2 and negatively regulates the PI3K pathway and PKB activation.
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After the generation of PIP3 by PI3K, a part of it is further dephosphorylated to generate other forms of PI which are also involved in signaling. Two major routes for the degradation of PIP3 exists: dephosphorylation by the haematopoietic-specific SH2 domain-containing inositol 5' phosphatase SHIP-1 and dephosphorylation by the 3' phosphoinositide phosphatase PTEN. SHIP-1 appears to set an activation threshold on T cell signaling. SHIP-1 phosphatase activity removes the 5' phosphate of PIP3 and generate phosphatidylinositol 3,4-bisphosphate. PI(3,4)P2 along with PIP3 preferentially binds to the PH domains of PKB and PDK1.
In addition to serving as a scaffold via auto-phosphorylation, ZAP-70 also phosphorylates a restricted set of substrates following TCR stimulation - including LAT and SLP-76. These substrates have been recognized to play pivotal role in TCR signaling by releasing second messengers. When phosphorylated, LAT and SLP-76 act as adaptor proteins which serve as nucleation points for the construction of a higher order signalosome: GADS, PLC-gamma1 and GRB2 bind to the LAT on the phosphorylated tyrosine residues (steps 8 and 13). SLP-76 and SOS are then moved to the signalosome by interacting with the SH3 domains of GRB2 and GADS via their proline rich sequences (step 9). Three SLP-76 acidic domain N-term tyrosine residues are phosphorylated by ZAP-70, once SLP-76 binds to GADS (step 10). These phospho-tyrosine residues act as binding sites to the SH2 domains of PLC-gamma1, Vav and Itk (steps 11 and 12). PLC-gamma1 is activated by dual phosphorylation on the tyrosine residues at positions 771, 783 and 1254 by Itk and ZAP-70 (step 14). Phosphorylated PLC-gamma1 subsequently detaches from LAT and SLP-76 and translocates to the plasma membrane by binding to phosphatidylinositol-4,5-bisphosphate (PIP2) via its PH domain (step 15). PLC-gamma1 goes on to hydrolyse PIP2 to second messengers DAG and IP3. These second messengers are involved in PKC and NF-kB activation and calcium mobilization (step 16).
On recruitment to plasma membrane PLC-gamma1 then hydrolyses PIP2 producing two second messengers, diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). IP3 induces a transient increase in intracellular free Ca++, while DAG is a direct activator of protein kinase C (PKC theta). These process have been implicated in many cellular physiological functions like cell proliferation, cell growth and differentiation.
Activated PLA-gamma1 translocates to the plasmamembrane and interacts with the inositol ring of the membrane bound phosphatidylinositol 4,5-bisphosphate (PIP2) with its PH domain.
At the beginning of this reaction, 1 molecule of '1-Phosphatidyl-D-myo-inositol 4,5-bisphosphate' is present. At the end of this reaction, 1 molecule of '1D-myo-Inositol 1,4,5-trisphosphate', and 1 molecule of '1,2-Diacylglycerol' are present. This reaction is mediated by the 'phospholipase C activity' of 'Phosphorylated phospholipase C gamma 2'.
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.
In adipocytes and myocytes insulin signaling causes intracellular vesicles carrying the GLUT4 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.
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.
As inferred from mouse, GLUT4 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.
RAC-beta serine/threonine protein kinase
Phosphorylated heat- and acid-stable protein regulated by insulin 1
eukaryotic translation initiation factor 4E binding protein 1
Eukaryotic translation initiation factor 4E
Lanosterol 14 alpha-methyl demethylase. Isolation and characterization of the third metabolically generated oxidative demethylation intermediate.
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
Changes in methionine adenosyltransferase and S-adenosylmethionine homeostasis in alcoholic rat liver
Am J Physiol Gastrointest Liver Physiol 279:G178-85
ARE-mRNA degradation requires the 5'-3' decay pathway
Identification and functional analysis of a defect in the human ALG9 gene: definition of congenital disorder of glycosylation type IL
Activation of the pre-replicative complex
Amino acid and oligopeptide SLC transporters
Regulation of gene expression in beta cells
Water permeability and characterization of aquaporin-11
CD28 costimulation: a source of Vav-1 for TCR signaling with the help of SLP-76?
Identification of a novel system L amino acid transporter structurally distinct from heterodimeric amino acid transporters
Persistent initiation of DNA replication and chromatin-bound MCM proteins during the cell cycle in cdc6 mutants.
ORC5L, a new member of the human origin recognition complex, is deleted in uterine leiomyomas and malignant myeloid diseases.
Destabilization of mRNA by Tristetraprolin (TTP)
On the biosynthesis and biological role of eoxins and 15-lipoxygenase-1 in airway inflammation and Hodgkin lymphoma
Prostaglandins Other Lipid Mediat 89:120-5
Intracellular zinc homeostasis and zinc signaling
Cloning and expression analysis of a novel member of the facilitative glucose transporter family, SLC2A9 (GLUT9)
p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27
Calcineurin, testis-specific catalytic subunit
Calmodulin-dependent calcineurin A subunit, gamma isoform
Serine/threonine protein phosphatase 2B catalytic subunit, gamma isoform
The molecular mechanism underlying Roberts syndrome involves loss of ESCO2 acetyltransferase activity
Cloning and expression of the human N-acetylglutamate synthase gene.
Response to elevated platelet cytosolic Ca2+
T cell antigen-receptor signal transduction
Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes
Characterization of the ATP- and GTP-specific succinyl-CoA synthetases in pigeon. The enzymes incorporate the same alpha-subunit.
Factors involved in megakaryocyte development and platelet production
The WASP-WAVE protein network: connecting the membrane to the cytoskeleton
Semaphorin junction: making tracks toward neural connectivity
Integrin alpha(IIb)beta(3) signaling in platelet adhesion and aggregation
Mechanism of diacylglycerol-induced membrane targeting and activation of protein kinase Ctheta
MicroRNA genes are transcribed by RNA polymerase II
Targeting mutant fibroblast growth factor receptors in cancer
Quality control of eukaryotic mRNA: safeguarding cells from abnormal mRNA function
Localization by fluorescence in situ hybridization of the human functional beta-glucuronidase gene (GUSB) to 7q11.21 --> q11.22 and two pseudogenes to 5p13 and 5q13
1-acyl-sn-glycero-3-phosphoserine [ChEBI:52603]
Cascade regulation of terminal adipocyte differentiation by three members of the C/EBP family of leucine zipper proteins
Mitochondrial tRNA import: are there distinct mechanisms?
Molecular identification of a novel mammalian brain isoform of acyl-CoA:lysophospholipid acyltransferase with prominent ethanolamine lysophospholipid acylating activity, LPEAT2
Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations
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Direct interaction between survivin and Smac/DIABLO is essential for the anti-apoptotic activity of survivin during taxol-induced apoptosis.
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hZip2 and hZip3 zinc transporters are down regulated in human prostate adenocarcinomatous glands
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An essential role for RasGRP1 in mast cell function and IgE-mediated allergic response
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APC/C-mediated degradation of cell cycle proteins
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7alpha,12alpha,26-trihydroxy-5beta-cholestan-3-one [ChEBI:48834]
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SLIT-ROBO Rho GTPase-activating protein 3
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cDNA cloning of human and rat brain myo-inositol monophosphatase. Expression and characterization of the human recombinant enzyme
7alpha,26-dihydroxycholest-4-en-3-one [ChEBI:48825]
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Barttin is a Cl- channel beta-subunit crucial for renal Cl- reabsorption and inner ear K+ secretion
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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
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Structural determinants in AUF1 required for high affinity binding to A + U-rich elements
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Crystal structure of human kynurenine aminotransferase II, a drug target for the treatment of schizophrenia
Crystal structure of human kynurenine aminotransferase II
APC/C-mediated destruction of the centrosomal kinase Nek2A occurs in early mitosis and depends upon a cyclin A-type D-box
GLUT8, a novel member of the sugar transport facilitator family with glucose transport activity
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The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology
Am. J. Physiol., Cell Physiol. 302:C943-65
The molecular defect leading to Fabry disease: structure of human alpha-galactosidase
Pancreatic islet GLUT2 glucose transporter mRNA and protein expression in humans with and without NIDDM
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Cell death signalling via NRAGE, NRIF and NADE
Human protoporphyrinogen oxidase: expression, purification, and characterization of the cloned enzyme
Interaction of J-protein co-chaperone Jac1 with Fe-S scaffold Isu is indispensable in vivo and conserved in evolution
Evidence that the coproporphyrinogen oxidase activity of rat liver is situated in the intermembrane space of mitochondria
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
Inositol polyphosphate multikinase regulates inositol 1,4,5,6-tetrakisphosphate
Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of alpha-synuclein protein implicated in Parkinson's disease
Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin
Integrated view on 17beta-hydroxysteroid dehydrogenases
Regulation of the immune response by SHIP
The intracellular interactions of the L1 family of cell adhesion molecules
Mercury-sensitive residues and pore site in AQP3 water channel
Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig alpha/Ig beta immunoreceptor tyrosine activation motif binding and autophosphorylation
Efflux and compartmentalization of zinc by members of the SLC30 family of solute carriers
The sodium/glucose cotransport family SLC5
The SLC39 family of metal ion transporters
Antigen Presentation: Folding, assembly and peptide loading of class I MHC
The human homologue of yeast ArgRIII protein is an inositol phosphate multikinase with predominantly nuclear localization
Molecular basis of multidrug transport by ABC transporters
Human IL4I1 is a secreted L-phenylalanine oxidase expressed by mature dendritic cells that inhibits T-lymphocyte proliferation
ATP activates transcription initiation from promoters by RNA polymerase II in a reversible step prior to RNA synthesis.
Deficiency of the alpha subunit of succinate-coenzyme A ligase causes fatal infantile lactic acidosis with mitochondrial DNA depletion
The Nod-like receptor (NLR) family: a tale of similarities and differences
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Human liver alcohol dehydrogenase: purification, composition, and catalytic features.
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Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo
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Phosphorylation of carbovir enantiomers by cellular enzymes determines the stereoselectivity of antiviral activity
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Wnt/beta-catenin signaling: components, mechanisms, and diseases
Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression
Sulfation and sulfotransferases 1: Sulfotransferase molecular biology: cDNAs and genes
Resistance to thromboembolism in PI3Kgamma-deficient mice
BRF1 protein turnover and mRNA decay activity are regulated by protein kinase B at the same phosphorylation sites
Nonsense Mediated Decay Independent of the Exon Junction Complex
ChEBI:58828 5-(methylsulfanyl)-2,3-dioxopentyl phosphate(2?)
5-(methylsulfanyl)-2,3-dioxopentyl phosphate(2?)
Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells
Function and dysfunction of the PI system in membrane trafficking
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Rat liver adenosine triphosphate:adenosine monophosphate phosphotransferase activity. II. Subcellular localization of adenylate kinase isozymes
Telomerase catalytic subunit homologs from fission yeast and human
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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
Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein
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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.
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The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1
Mechanism of filament nucleation and branch stability revealed by the structure of the Arp2/3 complex at actin branch junctions
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Review of epidermal growth factor receptor biology
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Isolation and characterization of an allelic cDNA for human muscle fructose-1,6-bisphosphatase
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Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3',5'-cyclic nucleotide phosphodiesterases
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Characterization of human phosphoserine aminotransferase involved in the phosphorylated pathway of L-serine biosynthesis
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Protein kinase C beta controls nuclear factor kappaB activation in B cells through selective regulation of the IkappaB kinase alpha
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Platelet hyperaggregability: impaired responsiveness to nitric oxide ("platelet NO resistance") as a therapeutic target
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De novo sphingolipid biosynthesis: a necessary, but dangerous, pathway
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Alternative pathway therapy for urea cycle disorders: twenty years later
The single minichromosome maintenance protein of Methanobacterium thermoautotrophicum DeltaH contains DNA helicase activity.
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Identification and characterization of eukaryotic initiation factor 5A-2
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Cyclin A/B1 associated events during G2/M transition
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Phytanic acid alpha-oxidation, new insights into an old problem: a review
3-(4-Hydroxyphenyl)pyruvate [ChEBI:1431]
Clinical and molecular features of three patients with congenital disorders of glycosylation type Ih (CDG-Ih) (ALG8 deficiency)
Functional and genetic studies demonstrate that mutation in the COX15 gene can cause Leigh syndrome
Regulation of G(2)/M events by Cdc25A through phosphorylation-dependent modulation of its stability
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Madin-Darby canine kidney II cells: a pharmacologically validated system for NPC1L1-mediated cholesterol uptake
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Studies on the properties and tissue distribution of the isozymes of guanylate kinase in man
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Immunocytochemical localization of the Menkes copper transport protein (ATP7A) to the trans-Golgi network
6-Phosphogluconate dehydrogenase: the mechanism of action investigated by a comparison of the enzyme from different species
A comparison of the enzymatic and physicochemical properties of human glutathione transferase M4-4 and three other human Mu class enzymes
Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex
The nature of the phagosomal membrane: endoplasmic reticulum versus plasmalemma
Knockdown of hepatocyte aquaporin-8 by RNA interference induces defective bile canalicular water transport
Am J Physiol Gastrointest Liver Physiol 296:G93-100
Aurora B controls the association of condensin I but not condensin II with mitotic chromosomes
Oligosaccharide structure and amino acid sequence of the major glycopeptides of mature human beta-hexosaminidase
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
On the mechanism of sensing unfolded protein in the endoplasmic reticulum
Phosphorylation of Mcm4 at specific sites by cyclin-dependent kinase leads to loss of Mcm4,6,7 helicase activity.
Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine
Functions and mechanisms of RNA editing.
Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and degradation of the epidermal growth factor receptor family member, ErbB3
The Bcl-2 family: roles in cell survival and oncogenesis.
Role of immunoproteasomes in cross-presentation
(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA [ChEBI:52050]
Structural and functional modules in RNA interference
N-acetyl-D-glucosaminylphosphatidylinositol [ChEBI:15935]
A common variant in methionine synthase reductase combined with low cobalamin (vitamin B12) increases risk for spina bifida
Studies on human erythrocyte inorganic pyrophosphatase.
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8p12 stem cell myeloproliferative disorder: the FOP-fibroblast growth factor receptor 1 fusion protein of the t(6;8) translocation induces cell survival mediated by mitogen-activated protein kinase and phosphatidylinositol 3-kinase/Akt/mTOR pathways
ArPIKfyve homomeric and heteromeric interactions scaffold PIKfyve and Sac3 in a complex to promote PIKfyve activity and functionality
Ras superfamily and interacting proteins database
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Human methionine synthase: cDNA cloning and identification of mutations in patients of the cblG complementation group of folate/cobalamin disorders
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S-(2,4-Dinitrophenyl)glutathione [ChEBI:8927]
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NLR proteins: integral members of innate immunity and mediators of inflammatory diseases
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The human homolog of Saccharomyces cerevisiae CDC45.
Rap1 regulation of RIAM and cell adhesion
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Identification and characterization of SMPD1 mutations causing Niemann-Pick types A and B in Spanish patients
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Structure of human isovaleryl-CoA dehydrogenase at 2.6 A resolution: structural basis for substrate specificity,.
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Diseases associated with visual transduction
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Type I phosphatidylinositol-4-phosphate 5-kinases synthesize the novel lipids phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 5-phosphate
Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery
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Protein interactions with nitric oxide synthases: controlling the right time, the right place, and the right amount of nitric oxide
The biochemistry, metabolism and inherited defects of the pentose phosphate pathway: a review
RhAG protein of the Rhesus complex is a CO2 channel in the human red cell membrane
Transcriptional networks controlling pancreatic development and beta cell function
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Molecular cloning of a novel member of the GLUT family of transporters, SLC2a10 (GLUT10), localized on chromosome 20q13.1: a candidate gene for NIDDM susceptibility
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Extracellular transsulfuration generates hydrogen sulfide from homocysteine and protects endothelium from redox stress
Am J Physiol Heart Circ Physiol 299:H1568-76
Recruitment of repair and signaling proteins to double-strand breaks
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Cell cycle-dependent phosphorylation, nuclear localization, and activation of human condensin
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'Mg2+ [cytosol]' is required for 'ribose phosphate diphosphokinase activity of phosphoribosyl pyrophosphate synthetase 1 holoenzyme (name copied from entity in Homo sapiens) [cytosol]'
'GTP [cytosol]' positively regulates 'glutamate dehydrogenase [NAD(P)+] activity of GLUD1 hexamer (name copied from entity in Homo sapiens) [mitochondrial matrix]'
'GDP [cytosol]' positively regulates 'glutamate dehydrogenase [NAD(P)+] activity of GLUD1 hexamer (name copied from entity in Homo sapiens) [mitochondrial matrix]'
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New roles for cysteine and transsulfuration enzymes: production of H2S, a neuromodulator and smooth muscle relaxant
'Active Calmodulin (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]'
'Pi [cytosol]' is required for 'ribose phosphate diphosphokinase activity of phosphoribosyl pyrophosphate synthetase 1 holoenzyme (name copied from entity in Homo sapiens) [cytosol]'
Role of AMP-activated protein kinase in the metabolic syndrome and in heart disease
Active cyclin B1-Cdk1 first appears on centrosomes in prophase
Mutational analysis of 105 mucopolysaccharidosis type VI patients
Hereditary renal amyloidosis associated with a mutant fibrinogen alpha-chain
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Signal transduction via platelet-derived growth factor receptors
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Assembly of asparagine-linked oligosaccharides
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Bleeding due to disruption of a cargo-specific ER-to-Golgi transport complex
Inflammasomes: guardians of cytosolic sanctity
Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress
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Adrenodoxin: structure, stability, and electron transfer properties
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Fabry disease: identification of 50 novel alpha-galactosidase A mutations causing the classic phenotype and three-dimensional structural analysis of 29 missense mutations
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Control of mRNA decay by heat shock-ubiquitin-proteasome pathway
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Sterol dependent regulation of human TM7SF2 gene expression: role of the encoded 3beta-hydroxysterol Delta14-reductase in human cholesterol biosynthesis
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DAP10- and DAP12-associated receptors in innate immunity
Function of Nod-like receptors in microbial recognition and host defense
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Mechanisms of ubiquitin transfer by the anaphase-promoting complex
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Mechanisms of type-I interferon signal transduction
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Building ubiquitin chains: E2 enzymes at work
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An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases
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Isolation and characterization of human Nramp cDNA
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Unusual interplay of two types of Ras activators, RasGRP and SOS, establishes sensitive and robust Ras activation in lymphocytes
Traffic control: regulation of kinesin motors
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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
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Wnt proteins are lipid-modified and can act as stem cell growth factors
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Characterization of a mutant pancreatic eIF-2alpha kinase, PEK, and co-localization with somatostatin in islet delta cells
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N(epsilon)-(carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signaling pathways and modulate gene expression
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Phospholipase C delta-4 overexpression upregulates ErbB1/2 expression, Erk signaling pathway, and proliferation in MCF-7 cells
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UBE2T is the E2 in the Fanconi anemia pathway and undergoes negative autoregulation
Comparison of the intracellular signaling responses by three chimeric fibroblast growth factor receptors in PC12 cells
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Serine 19 of human 6-pyruvoyltetrahydropterin synthase is phosphorylated by cGMP protein kinase II
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Identification of a cDNA encoding an isoform of human CTP synthetase
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p53-Independent G1/S DNA damage checkpoint
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Identification and characterization of a novel human sphingosine-1-phosphate phosphohydrolase, hSPP2
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Proteasome and peptidase function in MHC-class-I-mediated antigen presentation
Cdc25A localisation and shuttling: characterisation of sequences mediating nuclear export and import
Human deoxythymidine kinase. I. Purification and general properties of the cytoplasmic and mitochondrial isozymes derived from blast cells of acute myelocytic leukemia
Assembly of AUF1 oligomers on U-rich RNA targets by sequential dimer association
Identification and characterization of hPEM-2, a guanine nucleotide exchange factor specific for Cdc42
Nucleotide receptor signaling in platelets
Genetic alterations in the tyrosine kinase transcriptome of human cancer cell lines
Structural and catalytic properties and homology modelling of the human nucleoside diphosphate kinase C, product of the DRnm23 gene
Reconstitution of proliferating cell nuclear antigen-dependent repair of apurinic/apyrimidinic sites with purified human proteins.
Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R)
Red cell pyruvate kinase deficiency: molecular and clinical aspects
Analysis of cytochrome P450 metabolites of arachidonic and linoleic acids by liquid chromatography-mass spectrometry with ion trap MS
PTM: gamma carboxylation, hypusine formation and arylsulfatase activation
Cloning and expression of human deoxyhypusine synthase cDNA. Structure-function studies with the recombinant enzyme and mutant proteins.
Characterization of SMG-9, an essential component of the nonsense-mediated mRNA decay SMG1C complex
Discovery of an arachidonoyl coenzyme A synthetase in human platelets
Regulation of the human WEE1Hu CDK tyrosine 15-kinase during the cell cycle
Electroneutral ammonium transport by basolateral rhesus B glycoprotein
The structure of apo human glutamate dehydrogenase details subunit communication and allostery
Shelterin: the protein complex that shapes and safeguards human telomeres
Adhesion molecule L1 stimulates neuronal migration through Vav2-Pak1 signaling
Class II MHC peptide loading by the professionals
MPF localization is controlled by nuclear export
Comprehensive proteomic analysis of the human spliceosome.
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
Zinc transporters and the cellular trafficking of zinc
Phosphoribosylpyrophosphate synthesis from glucose decreases during amino acid starvation of human lymphoblasts
Immunoglobulin heavy-chain-associated amyloidosis
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Mechanism of GTP hydrolysis by G-protein alpha subunits
Ral GTPase-activating protein subunit beta
5'-AMP-activated protein kinase subunit gamma-3
The dual phosphatase activity of synaptojanin1 is required for both efficient synaptic vesicle endocytosis and reavailability at nerve terminals
Ral GTPase-activating protein subunit alpha-2
5'-AMP-activated protein kinase subunit beta-1
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5'-AMP-activated protein kinase subunit gamma-1
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Enzymic conversion of squalene 2,3-oxide to lanosterol and cholesterol
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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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New mechanisms and functions of actin nucleation
Translation of the phosphoinositide code by PI effectors
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Uridine diphosphate glucose pyrophosphorylase. II
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Isolation of the human phosphomannomutase gene (PMM1) and assignment to chromosome 22q13
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Human glutamate pyruvate transaminase (GPT): localization to 8q24.3, cDNA and genomic sequences, and polymorphic sites.
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The citric acid (TCA) cycle and respiratory electron transport
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Adaptors and molecular scaffolds in immune cell signaling
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The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease
Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans.
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The ends of the affair: capping and polyadenylation.
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Purification and some properties of a monoacylglycerol-hydrolyzing enzyme of rat adipose tissue
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Regulation of the interaction of Pak2 with Cdc42 via autophosphorylation of serine 141
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Rh type B glycoprotein is a new member of the Rh superfamily and a putative ammonia transporter in mammals
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Phosphorylation of Nephrin Triggers Ca2+ Signaling by Recruitment and Activation of Phospholipase C-{gamma}1
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High-throughput immunoblotting. Ubiquitiin-like protein ISG15 modifies key regulators of signal transduction
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Distinct missense mutations of the FGFR3 lys650 codon modulate receptor kinase activation and the severity of the skeletal dysplasia phenotype
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Identification of a novel human nicotinamide mononucleotide adenylyltransferase
Acidosis, acid-sensing ion channels, and neuronal cell death
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Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis
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De-regulated FGF receptors as therapeutic targets in cancer
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Regulation of mRNA Stability by Proteins that Bind AU-rich Elements
Pre-mRNA splicing: the discovery of a new spliceosome doubles the challenge.
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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
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Multiple assembly pathways underlie amyloid-beta fibril polymorphisms
Apoptosis-inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis.
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Minireview: implication of mitochondria in insulin secretion and action
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Phospholipase C-gamma: diverse roles in receptor-mediated calcium signaling
Coordinate binding of ATP and origin DNA regulates the ATPase activity of the origin recognition complex.
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Isolation and characterization of one soluble and two membrane-associated forms of phosphoinositide-specific phospholipase C from human platelets
Vacuolar protein sorting-associated protein 4B
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Vacuolar protein sorting-associated protein VTA1 homolog
Vacuolar protein sorting-associated protein 4A
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Vacuolar protein-sorting-associated protein 36
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Ionizing radiation and UV induction of p53 protein by different pathways in ataxia-telangiectasia cells.
Vacuolar protein-sorting-associated protein 25
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ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1
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Mammalian CARMIL inhibits actin filament capping by capping protein
Phosphatidylinositol 5-phosphate biosynthesis is linked to PIKfyve and is involved in osmotic response pathway in mammalian cells
Cytoplasmic retention, DNA binding and processing of the NF-kappa B p50 precursor are controlled by a small region in its C-terminus
Biotinidase deficiency: the enzymatic defect in late-onset multiple carboxylase deficiency
Crystal structure of human recombinant ornithine aminotransferase.
Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity.
Krüppel-like transcription factor KLF5 is a key regulator of adipocyte differentiation
The ubiquitously expressed human CYP51 encodes lanosterol 14 alpha-demethylase, a cytochrome P450 whose expression is regulated by oxysterols
Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: molecular modeling and mutagenesis approaches to receptor structure and function
Inositol phosphate synthesis and the nuclear processes they affect
Type II chaperonins, prefoldin, and the tubulin-specific chaperones
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A current view of the mammalian aquaglyceroporins
A unique signal transduction from FLT tyrosine kinase, a receptor for vascular endothelial growth factor VEGF
FVT-1 is a mammalian 3-ketodihydrosphingosine reductase with an active site that faces the cytosolic side of the endoplasmic reticulum membrane
Diversity of the mammalian sodium/proton exchanger SLC9 gene family
Plasma concentrations of phenyllactic acid in phenylketonuria
Glucose transporters (GLUT and SGLT): expanded families of sugar transport proteins
Cdc20:Phospho-APC/C mediated degradation of Cyclin A
Despite substantial degradation, 2-arachidonoylglycerol is a potent full efficacy agonist mediating CB(1) receptor-dependent G-protein activation in rat cerebellar membranes
Tyrosine 3-monooxygenase ecNumber1.14.16.2/ecNumber
2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
A review of the pharmacokinetics of abacavir
Fibroblast Growth Factor Receptor (FGFR) signaling
Functional and structural analysis of ClC-K chloride channels involved in renal disease
Mechanisms and physiological significance of the cholinergic control of pancreatic beta-cell function
maleylacetoacetic acid isomerase apoenzyme monomer
Glutathione S- transferase zeta 1) (GSTZ1-1
delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial precursor
4-alpha- hydroxy-tetrahydropterin dehydratase
Phenylalanine hydroxylase- stimulating protein
pterin-4-alpha-carbinolamine dehydratase
Dimerization cofactor of hepatocyte nuclear factor 1-alpha
4-alpha-hydroxy-tetrahydropterin dehydratase
L-tyrosine:2-oxoglutarate aminotransferase
homogentisic acid oxidase apoenzyme monomer
Glutaryl-CoA dehydrogenase, mitochondrial
Mitochondrial 2-oxodicarboxylate carrier
L-kynurenine/alpha-aminoadipate aminotransferase
Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family
phenylalanine hydroxylase apoprotein monomer
Alpha-aminoadipic semialdehyde dehydrogenase
On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
lysine-ketoglutarate reductase /saccharopine dehydrogenase monomer
The emerging shape of the ESCRT machinery
Formimidoyltetrahydrofolate cyclodeaminase
Formiminotetrahydrofolate cyclodeaminase
formiminotransferase-cyclodeaminase apoenzyme monomer
3-hydroxyisobutyrate dehydrogenase, monomer
3-hydroxyisobutyrate dehydrogenase, mitochondrial precursor
methylmalonate semialdehyde dehydrogenase, monomer
Methylmalonate-semialdehyde dehydrogenase (acylating) (EC 1.2.1.27) (MMSDH)
Secretory protein trafficking and organelle dynamics in living cells
Segregation of MHC class II molecules from MHC class I molecules in the Golgi complex for transport to lysosomal compartments
2-methyl-3-hydroxybutyryl-CoA dehydrogenase
Endoplasmic reticulum-associated amyloid beta-peptide binding protein
3-hydroxyisobutyryl-coenzyme A hydrolase
Acyl-CoA dehydrogenase family member 8, mitochondrial precursor
Activator- recruited cofactor 42 kDa component
acyl-CoA dehydrogenase, short/branched chain specific
Acyl-CoA dehydrogenase, short/branched chain specific, mitochondrial precursor
2-methyl branched chain acyl-CoA dehydrogenase
2-methylbutyryl-coenzyme A dehydrogenase
Acyl-CoA dehydrogenase, short/branched chain specific, mitochondrial precursor (EC 1.3.99.-) (SBCAD) (2-methyl branched chain acyl-CoA dehydrogenase) (2-MEBCAD) (2-methylbutyryl-coenzyme A dehydrogenase) (2-methylbutyryl-CoA dehydrogenase)
branched chain keto acid dehydrogenase E1, alpha polypeptide
Isovaleryl-CoA dehydrogenase, mitochondrial precursor
dihydrolipoamide branched chain transacylase E2
branched chain keto acid dehydrogenase E1, beta polypeptide
Branched-chain amino acid aminotransferase, cytosolic
branched-chain amino acid aminotransferase, mitochondrial, apoenzyme
The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism
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ornithine aminotransferase, mitochondrial
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Glutamine- dependent asparagine synthetase
Asparagine synthetase (glutamine-hydrolyzing)
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Glutamate dehydrogenase 1, mitochondrial precursor
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TRF1 inhibits telomere C-strand DNA synthesis in vitro
Polymerase switching on the C-strand of the telomere
Trif-related adapter molecule is phosphorylated by PKC{epsilon} during Toll-like receptor 4 signaling
Effect of beta-actinin on the particle length of F-actin
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Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase
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1-hydroxy-5-(methylthio)-3-oxopent-1-en-2-olate (1-)
ChEBI:58795 1-hydroxy-5-(methylthio)-3-oxopent-1-en-2-olate (1-)
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Putative inorganic polyphosphate/ATP-NAD 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=3643179
Nicotinamide mononucleotide adenylyltransferase 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=3643183
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643189
Nicotinate-nucleotide pyrophosphorylase (carboxylating)
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643188
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643187
Nicotinamide mononucleotide adenylyltransferase 2
Nicotinamide mononucleotide adenylyltransferase 1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643231
methylcrotonyl-CoA carboxylase beta 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_159679.3
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=3643251
The t(8;17)(p11;q23) in the 8p11 myeloproliferative syndrome fuses MYO18A to FGFR1
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643238
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643237
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=113717
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643239
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643236
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643235
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_4250.2
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=3643199
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643194
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643209
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643174
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643200
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643190
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643198
Identification of arylsulfonamides as Aquaporin 4 inhibitors
Fcgamma RI-triggered generation of arachidonic acid and eicosanoids requires iPLA2 but not cPLA2 in human monocytic 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=3643244
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643241
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643243
Characterizing the specificity and cooperation of aminopeptidases in the cytosol and endoplasmic reticulum during MHC class I antigen presentation
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_34106.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643214
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643254
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_112553.8
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643255
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_103791.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643257
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_83658.9
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643211
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643212
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643213
gene ontology term for cellular function
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Diseases caused by defects in the visual cycle: retinoids as potential therapeutic agents
Annu. Rev. Pharmacol. Toxicol. 47:469-512
Human Smp3p adds a fourth mannose to yeast and human glycosylphosphatidylinositol precursors in vivo
Primary structure and tissue-specific expression of human beta-hydroxyisobutyryl-coenzyme A hydrolase.
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_34372.10
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642106
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643245
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3643246
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642127
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642123
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642128
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642133
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642104
Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and 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=3642110
Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642122
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642114
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642118
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642105
Purification, cDNA-cloning and expression of human diacylglycerol kinase
Human acetyl-CoA carboxylase 2. Molecular cloning, characterization, chromosomal mapping, and evidence for two 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=3642095
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642090
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=3642091
Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=109875
Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_5384.1