Regulation_of_BIRC2_on_CASP3_using_Physical Interaction
Regulation_of_BAD_on_BCL2_using_Physical Interaction
Regulation_of_CRADD_on_RIPK1_using_Physical Interaction
Regulation_of_BAD_on_BCL2L2_using_Physical Interaction
Regulation_of_TNFSF10_on_TNFRSF10C_using_Physical Interaction
Regulation_of_CASP3_on_EIF3J_using_Proteolytic Processing
Regulation_of_EIF4G2_on_BCL2_using_Translational Regulation
Regulation_of_EIF2S2_on_protein translation_using_Other
Regulation_of_EIF4G2_on_EIF4G2_using_Translational Regulation
Regulation_of_DFFA_on_DFFB_using_Physical Interaction
Regulation_of_TRADD_on_FADD_using_Physical Interaction
Regulation_of_MCL1_on_BAK1_using_Physical Interaction
Regulation_of_CASP2_on_BID_using_Proteolytic Processing
Regulation_of_TNFRSF10A_on_TNFRSF10B_using_Physical Interaction
Regulation_of_TNFRSF10B_on_FADD_using_Physical Interaction
Regulation_of_BIRC3_on_CASP9_using_Physical Interaction
Regulation_of_CASP3_on_EIF4G1_using_Proteolytic Processing
Regulation_of_ENDOG_on_DNA fragmentation_using_Other
Regulation_of_BCL2L11_on_BCL2_using_Physical Interaction
Regulation_of_BCL2L2_on_BAX_using_Physical Interaction
Regulation_of_CASP3_on_CASP9_using_Proteolytic Processing
Regulation_of_cytosk. stability_on_membrane blebbing_using_Other
Regulation_of_BIRC6_on_CASP9_using_Physical Interaction
Regulation_of_DIABLO_on_BIRC6_using_Physical Interaction
Regulation_of_MYL7_on_myosin II_using_Other
Regulation_of_MYL5_on_myosin II_using_Other
Regulation_of_EIF4B_on_protein translation_using_Other
Regulation_of_EIF4G2_on_cap-independent translation_using_Other
Regulation_of_TNF_on_TNFRSF1A_using_Physical Interaction
Regulation_of_CASP6_on_LMNA_using_Proteolytic Processing
Regulation_of_CASP7_on_PARP1_using_Proteolytic Processing
Regulation_of_BAX_on_BAX_using_Physical Interaction
Regulation_of_CASP3_on_EIF2S3_using_Proteolytic Processing
Regulation_of_CTNNB1_on_cytosk. stability_using_Other
Regulation_of_LRDD_on_RIPK1_using_Physical Interaction
Regulation_of_EIF4EBP1_on_protein translation_using_Other
Regulation_of_FADD_on_ATG5_using_Physical Interaction
Regulation_of_TNFSF10_on_TNFRSF10B_using_Physical Interaction
Regulation_of_TNFRSF10A_on_RIPK1_using_Physical Interaction
Regulation_of_CASP3_on_DFFA_using_Proteolytic Processing
Regulation_of_LRDD_on_CASP2_using_Physical Interaction
Regulation_of_HTRA2_on_BIRC2_using_Physical Interaction
Regulation_of_APAF1_on_CASP9_using_Physical Interaction
Regulation_of_CASP3_on_EIF4G3_using_Proteolytic Processing
Regulation_of_BID_on_BCL2L1_using_Physical Interaction
Regulation_of_BAK1_on_BAK1_using_Physical Interaction
Regulation_of_GOLGA3_on_Golgi fragmentation_using_Other
Regulation_of_TNFSF10_on_TNFRSF10A_using_Physical Interaction
Regulation_of_CASP3_on_CASP8_using_Proteolytic Processing
Regulation_of_CASP2_on_GOLGA3_using_Proteolytic Processing
Regulation_of_NAIP_on_CASP3_using_Physical Interaction
Regulation_of_TRAF2_on_IKK_using_Physical Interaction
Regulation_of_BCL2L11_on_MCL1_using_Physical Interaction
Regulation_of_XIAP_on_CASP3_using_Physical Interaction
Regulation_of_CASP3_on_CTNNB1_using_Proteolytic Processing
Regulation_of_CASP9_on_BIRC6_using_Proteolytic Processing
Regulation_of_EIF4G2_on_XIAP_using_Translational Regulation
Regulation_of_PMAIP1_on_BAX_using_Physical Interaction
Regulation_of_LRDD_on_CRADD_using_Physical Interaction
Regulation_of_BIRC5_on_CASP3_using_Physical Interaction
This model is from the article: Systems biology analysis of programmed cell death Shani Bialik, Einat Zalckvar, Yaara Ber, Assaf D. Rubinstein, Adi Kimchi Trends in Biochemical Sciences Volume 35, Issue 10, 556-564, 27 May 2010 20537543 , Abstract: Systems biology, a combined computational and experimental approach to analyzing complex biological systems, has recently been applied to understanding the pathways that regulate programmed cell death. This approach has become especially crucial because recent advances have resulted in an expanded view of the network, to include not just a single death module (apoptosis) but multiple death programs, including programmed necrosis and autophagic cell death. Current research directions in the systems biology field range from quantitative analysis of subprocesses of individual death pathways to the study of interconnectivity among the various death modules of the larger network. These initial studies have provided great advances in our understanding of programmed cell death and have important clinical implications for drug target research. Brief Note about the model: This model is an export of 26 SPIKE Apoptosis Networks to SBML format. This is a pathway model (not quantitative model) of Apoptosis. Apoptosis, or type I cell death, is a form of programmed cell death characterized by fragmentation of the cytoplasm and nucleus, chromatin condensation and fragmentation, cytoskeletal collapse, membrane blebbing, and finally, disintegration of the cell into apoptotic bodies, which are engulfed by adjacent cells, thereby avoiding an inflammatory response. It serves to model tissues during embryonic development, to regulate cell number by eliminating excess cells, and to remove damaged, mutated or infected cells. Defective or excessive apoptosis can lead to cancer or autoimmune and degenerative diseases, respectively. Apoptosis is executed by a family of cysteine proteases, the caspases, which function in a proteolytic cascade that is initiated by either the intrinsic mitochondrial-based pathway leading to apoptosome formation, or the extrinsic pathway, which involves activation of death receptors by their extracellular ligands to form the DISC. The most distal caspases, known as the executioner caspases, cleave numerous cellular substrates, thereby leading to specific dismantling of the cell. Apoptosis is regulated by multiple proteins at several levels, including the Bcl-2 family, which regulate the release of apoptogenic factors from the mitochondria, and the IAP family, which regulate caspase activity, and is countered by survival signals eminating from the NF-kB signaling pathway. Although most of the regulation occurs at the post-translational level, involving protein-protein interactions, proteolysis, changes in subcellular localization and phosphorylation, transcriptional control, such as by p53, can also modulate the expression levels of several key apoptotic proteins. This model originates from BioModels Database: A Database of Annotated Published Models (http://www.ebi.ac.uk/biomodels/). It is copyright (c) 2005-2011 The BioModels.net Team. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information. In summary, you are entitled to use this encoded model in absolutely any manner you deem suitable, verbatim, or with modification, alone or embedded it in a larger context, redistribute it, commercially or not, in a restricted way or not. . To cite BioModels Database, please use: Li C, Donizelli M, Rodriguez N, Dharuri H, Endler L, Chelliah V, Li L, He E, Henry A, Stefan MI, Snoep JL, Hucka M, Le Novère N, Laibe C (2010) BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. BMC Syst Biol., 4:92.
Regulation_of_EIF4G2_on_APAF1_using_Translational Regulation
Regulation_of_CASP10_on_BID_using_Proteolytic Processing
Regulation_of_TNFRSF1A_on_RIPK1_using_Physical Interaction
Regulation_of_myosin II_on_membrane blebbing_using_Dephosphorylation
Regulation_of_CRADD_on_CASP2_using_Physical Interaction
Regulation_of_MYL12B_on_myosin II_using_Other
Regulation_of_DIABLO_on_BIRC5_using_Physical Interaction
Regulation_of_CASP3_on_ROCK1_using_Proteolytic Processing
Regulation_of_FADD_on_CASP10_using_Physical Interaction
Regulation_of_CASP3_on_PARP1_using_Proteolytic Processing
Regulation_of_PARP1_on_DNA repair_using_Other
Regulation_of_FADD_on_RIPK1_using_Physical Interaction
Regulation_of_CFLAR_on_FADD_using_Physical Interaction
Regulation_of_TRADD_on_RIPK1_using_Physical Interaction
Regulation_of_BID_on_BAK1_using_Physical Interaction
mysoin light chains, regulatory non muscle
Regulation_of_BCL2L2_on_BAK1_using_Physical Interaction
Regulation_of_CASP8_on_CASP3_using_Proteolytic Processing
Regulation_of_CASP2_on_RIPK1_using_Physical Interaction
Regulation_of_BBC3_on_MCL1_using_Physical Interaction
Regulation_of_DYNLL1_on_BCL2L11_using_Physical Interaction
Regulation_of_CASP3_on_EIF4B_using_Proteolytic Processing
Regulation_of_CASP10_on_CASP3_using_Proteolytic Processing
Regulation_of_CASP3_on_GORASP1_using_Proteolytic Processing
Regulation_of_HTRA2_on_XIAP_using_Physical Interaction
Regulation_of_CASP8_on_RIPK1_using_Proteolytic Processing
Regulation_of_CASP2_on_TRAF2_using_Physical Interaction
Regulation_of_GORASP1_on_Golgi fragmentation_using_Other
Regulation_of_TNFRSF10A_on_TRADD_using_Physical Interaction
Regulation_of_BIRC5_on_CASP9_using_Physical Interaction
Regulation_of_CASP3_on_BIRC6_using_Proteolytic Processing
Regulation_of_TNFRSF10A_on_FADD_using_Physical Interaction
Regulation_of_CASP7_on_DFFA_using_Proteolytic Processing
Regulation_of_MYL10_on_myosin II_using_Other
Regulation_of_DIABLO_on_XIAP_using_Physical Interaction
Regulation_of_BIRC8_on_CASP3_using_Physical Interaction
Regulation_of_EIF2A_on_protein translation_using_Other
Regulation_of_CASP9_on_CASP3_using_Proteolytic Processing
Active_DISC (Primary complex) FADD, CASP8, CASP10
Regulation_of_BIRC3_on_CASP7_using_Physical Interaction
Regulation_of_CASP3_on_CASP10_using_Proteolytic Processing
Regulation_of_CFLAR_on_CASP10_using_Physical Interaction
Regulation_of_BIRC3_on_CASP3_using_Physical Interaction
Regulation_of_BBC3_on_BCL2_using_Physical Interaction
Regulation_of_BBC3_on_BAX_using_Physical Interaction
Regulation_of_CASP3_on_ACIN1_using_Proteolytic Processing
Regulation_of_CASP3_on_CASP2_using_Proteolytic Processing
Regulation_of_CASP3_on_CASP6_using_Proteolytic Processing
Regulation_of_BCL2L11_on_BCL2L1_using_Physical Interaction
Regulation_of_ACIN1_on_chromatin condensation_using_Transcription Regulation
Regulation_of_DIABLO_on_BIRC3_using_Physical Interaction
Regulation_of_EIF4G2_on_CDK1_using_Translational Regulation
Regulation_of_HTRA2_on_BIRC3_using_Physical Interaction
Regulation_of_XIAP_on_CASP9_using_Physical Interaction
Regulation_of_TNFRSF1A_on_TRADD_using_Physical Interaction
Regulation_of_BAD_on_BCL2L1_using_Physical Interaction
Regulation_of_EIF4G3_on_protein translation_using_Other
Regulation_of_BCL2L11_on_BCL2L2_using_Physical Interaction
Regulation_of_RIPK1_on_FADD_using_Physical Interaction
Regulation_of_BID_on_BAX_using_Physical Interaction
Regulation_of_BAK1_on_BAX_using_Physical Interaction
DISC (Primary complex) FADD, CASP8, CASP10_containment
Regulation_of_CASP3_on_EIF4EBP1_using_Proteolytic Processing
Regulation_of_FAS_on_FADD_using_Physical Interaction
Regulation_of_BCL2L1_on_BAX_using_Physical Interaction
Regulation_of_AIFM1_on_DNA fragmentation_using_Other
Regulation_of_SH3GLB1_on_BAX_using_Physical Interaction
Regulation_of_GSN_on_cytosk. stability_using_Other
Regulation_of_FASLG_on_FAS_using_Physical Interaction
Regulation_of_BCL2_on_BAK1_using_Physical Interaction
Regulation_of_BBC3_on_BCL2L1_using_Physical Interaction
Regulation_of_CASP3_on_GSN_using_Proteolytic Processing
Regulation_of_EIF4G1_on_protein translation_using_Other
Regulation_of_TNFRSF10B_on_RIPK1_using_Physical Interaction
Regulation_of_CASP9_on_CASP7_using_Proteolytic Processing
Regulation_of_CASP3_on_SPTAN1_using_Proteolytic Processing
Regulation_of_MYL12A_on_myosin II_using_Other
Regulation_of_BCL2L1_on_BAK1_using_Physical Interaction
Regulation_of_BIRC6_on_CASP7_using_Physical Interaction
Regulation_of_BIRC2_on_CASP7_using_Physical Interaction
Regulation_of_BID_on_BCL2L2_using_Physical Interaction
Regulation_of_BIRC5_on_CASP7_using_Physical Interaction
Regulation_of_TRADD_on_TRAF2_using_Physical Interaction
Regulation_of_EIF3J_on_protein translation_using_Dephosphorylation
Regulation_of_SH3GLB1_on_BAK1_using_Physical Interaction
Regulation_of_CFLAR_on_CASP8_using_Physical Interaction
Regulation_of_CASP10_on_RIPK1_using_Proteolytic Processing
Regulation_of_EIF4G2_on_BIRC2_using_Translational Regulation
Regulation_of_CASP3_on_EIF2A_using_Proteolytic Processing
Regulation_of_RIPK1_on_IKK_using_Physical Interaction
Regulation_of_BIRC6_on_CASP3_using_Physical Interaction
Regulation_of_CASP3_on_EIF4G2_using_Proteolytic Processing
Regulation_of_BBC3_on_BCL2L2_using_Physical Interaction
Regulation_of_CASP8_on_BID_using_Proteolytic Processing
Regulation_of_TNFRSF10B_on_TRADD_using_Physical Interaction
Regulation_of_HTRA2_on_BIRC6_using_Physical Interaction
Regulation_of_DFFB_on_DNA fragmentation_using_Transcription Regulation
Regulation_of_EIF2S3_on_protein translation_using_Other
Regulation_of_FADD_on_CASP8_using_Physical Interaction
Regulation_of_BIRC2_on_CASP9_using_Physical Interaction
Regulation_of_CASP3_on_EIF2S2_using_Proteolytic Processing
Regulation_of_ATP_on_APAF1_using_Physical Interaction
Regulation_of_PMAIP1_on_MCL1_using_Physical Interaction
Regulation_of_DIABLO_on_BIRC2_using_Physical Interaction
Regulation_of_CYCS_on_APAF1_using_Physical Interaction
Regulation_of_CASP3_on_BCL2_using_Proteolytic Processing
Regulation_of_XIAP_on_CASP7_using_Physical Interaction
Regulation_of_PMAIP1_on_BCL2_using_Physical Interaction
Regulation_of_BIRC7_on_CASP3_using_Physical Interaction
Regulation_of_CASP3_on_BIRC2_using_Proteolytic Processing
Regulation_of_BCL2L11_on_BAK1_using_Physical Interaction
Regulation_of_CASP3_on_CASP7_using_Proteolytic Processing
Regulation_of_LMNA_on_nuclear integrity_using_Other