{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,14]],"date-time":"2026-08-14T05:26:10Z","timestamp":1786685170288,"version":"3.56.0"},"reference-count":109,"publisher":"Public Library of Science (PLoS)","issue":"9","license":[{"start":{"date-parts":[[2006,9,15]],"date-time":"2006-09-15T00:00:00Z","timestamp":1158278400000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.ploscompbiol.org"],"crossmark-restriction":false},"short-container-title":["PLoS Comput Biol"],"DOI":"10.1371\/journal.pcbi.0020120","type":"journal-article","created":{"date-parts":[[2006,9,12]],"date-time":"2006-09-12T21:37:38Z","timestamp":1158097058000},"page":"e120","update-policy":"https:\/\/doi.org\/10.1371\/journal.pcbi.corrections_policy","source":"Crossref","is-referenced-by-count":205,"title":["Mathematical Modeling Identifies Inhibitors of Apoptosis as Mediators of Positive Feedback and Bistability"],"prefix":"10.1371","volume":"2","author":[{"given":"Stefan","family":"Legewie","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nils","family":"Bl\u00fcthgen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hanspeter","family":"Herzel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2006,9,15]]},"reference":[{"key":"pcbi-0020120-b001","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1128\/MMBR.64.4.821-846.2000","article-title":"Proteases for cell suicide: Functions and regulation of caspases.","volume":"64","year":"2000","journal-title":"Microbiol Mol Biol Rev"},{"key":"pcbi-0020120-b002","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1038\/nrm830","article-title":"IAP proteins: Blocking the road to death's door.","volume":"3","year":"2002","journal-title":"Nat Rev Mol Cell Biol"},{"key":"pcbi-0020120-b003","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1126\/science.275.5303.1129","article-title":"Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked.","volume":"275","year":"1997","journal-title":"Science"},{"key":"pcbi-0020120-b004","doi-asserted-by":"crossref","first-page":"1132","DOI":"10.1126\/science.275.5303.1132","article-title":"The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis.","volume":"275","year":"1997","journal-title":"Science"},{"key":"pcbi-0020120-b005","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1083\/jcb.144.2.281","article-title":"Ordering the cytochrome c\u2013initiated caspase cascade: Hierarchical activation of caspases-2, \u22123, \u22126, \u22127, \u22128, and \u221210 in a caspase-9-dependent manner.","volume":"144","year":"1999","journal-title":"J Cell Biol"},{"key":"pcbi-0020120-b006","doi-asserted-by":"crossref","first-page":"16127","DOI":"10.1074\/jbc.275.21.16127","article-title":"Determinants of cytochrome c pro-apoptotic activity. The role of lysine 72 trimethylation.","volume":"275","year":"2000","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b007","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1084\/jem.20021862","article-title":"The apoptosome pathway to caspase activation in primary human neutrophils exhibits dramatically reduced requirements for cytochrome C.","volume":"197","year":"2003","journal-title":"J Exp Med"},{"key":"pcbi-0020120-b008","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/S0092-8674(00)80085-9","article-title":"Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c.","volume":"86","year":"1996","journal-title":"Cell"},{"key":"pcbi-0020120-b009","doi-asserted-by":"crossref","first-page":"41985","DOI":"10.1074\/jbc.M107419200","article-title":"Physiological concentrations of K+ inhibit cytochrome c-dependent formation of the apoptosome.","volume":"276","year":"2001","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b010","doi-asserted-by":"crossref","first-page":"7533","DOI":"10.1073\/pnas.1031631100","article-title":"Direct activation of the apoptosis machinery as a mechanism to target cancer cells.","volume":"100","year":"2003","journal-title":"Proc Natl Acad Sci U S A"},{"key":"pcbi-0020120-b011","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1083\/jcb.144.5.883","article-title":"The release of cytochrome c from mitochondria during apoptosis of NGF-deprived sympathetic neurons is a reversible event.","volume":"144","year":"1999","journal-title":"J Cell Biol"},{"key":"pcbi-0020120-b012","doi-asserted-by":"crossref","first-page":"1192","DOI":"10.1038\/sj.cdd.4400782","article-title":"The \u201charmless\u201d release of cytochrome c.","volume":"7","year":"2000","journal-title":"Cell Death Differ"},{"key":"pcbi-0020120-b013","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/s10495-005-0802-x","article-title":"Constitutive presence of cytochrome c in the cytosol of a chemoresistant leukemic cell line.","volume":"10","year":"2005","journal-title":"Apoptosis"},{"key":"pcbi-0020120-b014","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1083\/jcb.153.2.319","article-title":"Cytochrome c maintains mitochondrial transmembrane potential and ATP generation after outer mitochondrial membrane permeabilization during the apoptotic process.","volume":"153","year":"2001","journal-title":"J Cell Biol"},{"key":"pcbi-0020120-b015","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1083\/jcb.150.1.131","article-title":"Caspase inhibition extends the commitment to neuronal death beyond cytochrome c release to the point of mitochondrial depolarization.","volume":"150","year":"2000","journal-title":"J Cell Biol"},{"key":"pcbi-0020120-b016","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/S0300-9084(02)01372-X","article-title":"Mitochondrial involvement in the point of no return in neuronal apoptosis.","volume":"84","year":"2002","journal-title":"Biochimie"},{"key":"pcbi-0020120-b017","doi-asserted-by":"crossref","first-page":"50842","DOI":"10.1074\/jbc.M207622200","article-title":"Early mitochondrial activation and cytochrome c up-regulation during apoptosis.","volume":"277","year":"2002","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b018","doi-asserted-by":"crossref","first-page":"50834","DOI":"10.1074\/jbc.M209369200","article-title":"Apocytochrome c blocks caspase-9 activation and Bax-induced apoptosis.","volume":"277","year":"2002","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b019","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1038\/ncb751","article-title":"IAPs are essential for GDNF-mediated neuroprotective effects in injured motor neurons in vivo.","volume":"4","year":"2002","journal-title":"Nat Cell Biol"},{"key":"pcbi-0020120-b020","doi-asserted-by":"crossref","first-page":"5026","DOI":"10.1523\/JNEUROSCI.19-12-05026.1999","article-title":"Attenuation of ischemia-induced cellular and behavioral deficits by X chromosome-linked inhibitor of apoptosis protein overexpression in the rat hippocampus.","volume":"19","year":"1999","journal-title":"J Neurosci"},{"key":"pcbi-0020120-b021","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1038\/sj.cdd.4400712","article-title":"The X-linked inhibitor of apoptosis (XIAP) prevents cell death in axotomized CNS neurons in vivo.","volume":"7","year":"2000","journal-title":"Cell Death Differ"},{"key":"pcbi-0020120-b022","doi-asserted-by":"crossref","first-page":"9126","DOI":"10.1523\/JNEUROSCI.20-24-09126.2000","article-title":"Protection by synergistic effects of adenovirus-mediated X-chromosome-linked inhibitor of apoptosis and glial cell line-derived neurotrophic factor gene transfer in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine model of Parkinson's disease.","volume":"20","year":"2000","journal-title":"J Neurosci"},{"key":"pcbi-0020120-b023","doi-asserted-by":"crossref","first-page":"3805","DOI":"10.1093\/emboj\/16.13.3805","article-title":"Caspase activity is required for commitment to Fas-mediated apoptosis.","volume":"16","year":"1997","journal-title":"EMBO J"},{"key":"pcbi-0020120-b024","doi-asserted-by":"crossref","first-page":"23490","DOI":"10.1074\/jbc.M411607200","article-title":"Reversibility of caspase activation and its role during glycochenodeoxycholate-induced hepatocyte apoptosis.","volume":"280","year":"2005","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b025","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1016\/S0955-0674(02)00314-9","article-title":"Self-perpetuating states in signal transduction: Positive feedback, double-negative feedback and bistability.","volume":"14","year":"2002","journal-title":"Curr Opin Cell Biol"},{"key":"pcbi-0020120-b026","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1091\/mbc.01-05-0265","article-title":"Testing a mathematical model of the yeast cell cycle.","volume":"13","year":"2002","journal-title":"Mol Biol Cell"},{"key":"pcbi-0020120-b027","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1038\/ncb954","article-title":"Building a cell cycle oscillator: Hysteresis and bistability in the activation of Cdc2.","volume":"5","year":"2003","journal-title":"Nat Cell Biol"},{"key":"pcbi-0020120-b028","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1073\/pnas.0235349100","article-title":"Hysteresis drives cell-cycle transitions in Xenopus laevis egg extracts.","volume":"100","year":"2003","journal-title":"Proc Natl Acad Sci U S A"},{"key":"pcbi-0020120-b029","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1038\/nature02089","article-title":"A positive-feedback-based bistable \u201cmemory module\u201d that governs a cell fate decision.","volume":"426","year":"2003","journal-title":"Nature"},{"key":"pcbi-0020120-b030","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1083\/jcb.200308060","article-title":"Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades.","volume":"164","year":"2004","journal-title":"J Cell Biol"},{"key":"pcbi-0020120-b031","first-page":"137","article-title":"Molecular switches at the synapse emerge from receptor and kinase traffic.","volume":"1","year":"2005","journal-title":"PLoS Comput Biol"},{"key":"pcbi-0020120-b032","doi-asserted-by":"crossref","first-page":"4197","DOI":"10.1073\/pnas.072544399","article-title":"Oligomerization and activation of caspase-9, induced by Apaf-1 CARD.","volume":"99","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"pcbi-0020120-b033","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1016\/S1097-2765(00)80095-7","article-title":"Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization.","volume":"1","year":"1998","journal-title":"Mol Cell"},{"key":"pcbi-0020120-b034","doi-asserted-by":"crossref","first-page":"8091","DOI":"10.1074\/jbc.M204783200","article-title":"Regulation of the Apaf-1\/caspase-9 apoptosome by caspase-3 and XIAP.","volume":"278","year":"2003","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b035","doi-asserted-by":"crossref","first-page":"998","DOI":"10.1093\/emboj\/20.5.998","article-title":"Recruitment, activation and retention of caspases-9 and \u22123 by Apaf-1 apoptosome and associated XIAP complexes.","volume":"20","year":"2001","journal-title":"EMBO J"},{"key":"pcbi-0020120-b036","doi-asserted-by":"crossref","first-page":"2134","DOI":"10.1038\/sj.emboj.7600210","article-title":"Analysis of the composition, assembly kinetics and activity of native Apaf-1 apoptosomes.","volume":"23","year":"2004","journal-title":"EMBO J"},{"key":"pcbi-0020120-b037","doi-asserted-by":"crossref","first-page":"e183","DOI":"10.1371\/journal.pbio.0030183","article-title":"Engineering a dimeric caspase-9: A re-evaluation of the induced proximity model for caspase activation.","volume":"3","year":"2005","journal-title":"PLoS Biol"},{"key":"pcbi-0020120-b038","doi-asserted-by":"crossref","first-page":"3179","DOI":"10.1101\/gad.13.24.3179","article-title":"Caspase-9 and APAF-1 form an active holoenzyme.","volume":"13","year":"1999","journal-title":"Genes Dev"},{"key":"pcbi-0020120-b039","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/S0300-9084(02)01376-7","article-title":"The Apaf-1 apoptosome: A large caspase-activating complex.","volume":"84","year":"2002","journal-title":"Biochimie"},{"key":"pcbi-0020120-b040","doi-asserted-by":"crossref","first-page":"13432","DOI":"10.1074\/jbc.272.20.13432","article-title":"A sequential two-step mechanism for the production of the mature p17:p12 form of caspase-3 in vitro.","volume":"272","year":"1997","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b041","doi-asserted-by":"crossref","first-page":"27084","DOI":"10.1074\/jbc.273.42.27084","article-title":"Pro-caspase-3 is a major physiologic target of caspase-8.","volume":"273","year":"1998","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b042","doi-asserted-by":"crossref","first-page":"27099","DOI":"10.1074\/jbc.271.43.27099","article-title":"The Ced-3\/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32.","volume":"271","year":"1996","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b043","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1038\/sj.cdd.4400824","article-title":"Caspase-9 processing by caspase-3 via a feedback amplification loop in vivo.","volume":"8","year":"2001","journal-title":"Cell Death Differ"},{"key":"pcbi-0020120-b044","first-page":"4386","article-title":"Caspase-3 is essential for procaspase-9 processing and cisplatin-induced apoptosis of MCF-7 breast cancer cells.","volume":"60","year":"2000","journal-title":"Cancer Res"},{"key":"pcbi-0020120-b045","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1016\/S0092-8674(01)00274-4","article-title":"Structural basis for the inhibition of caspase-3 by XIAP.","volume":"104","year":"2001","journal-title":"Cell"},{"key":"pcbi-0020120-b046","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1038\/40901","article-title":"X-linked IAP is a direct inhibitor of cell-death proteases.","volume":"388","year":"1997","journal-title":"Nature"},{"key":"pcbi-0020120-b047","doi-asserted-by":"crossref","first-page":"2215","DOI":"10.1093\/emboj\/17.8.2215","article-title":"IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases.","volume":"17","year":"1998","journal-title":"EMBO J"},{"key":"pcbi-0020120-b048","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/S1097-2765(03)00054-6","article-title":"Mechanism of XIAP-mediated inhibition of caspase-9.","volume":"11","year":"2003","journal-title":"Mol Cell"},{"key":"pcbi-0020120-b049","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1083\/jcb.152.3.483","article-title":"DIABLO promotes apoptosis by removing MIHA\/XIAP from processed caspase 9.","volume":"152","year":"2001","journal-title":"J Cell Biol"},{"key":"pcbi-0020120-b050","doi-asserted-by":"crossref","first-page":"36892","DOI":"10.1074\/jbc.M404893200","article-title":"Bistability analyses of a caspase activation model for receptor-induced apoptosis.","volume":"279","year":"2004","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b051","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1038\/35065125","article-title":"A conserved XIAP-interaction motif in caspase-9 and Smac\/DIABLO regulates caspase activity and apoptosis.","volume":"410","year":"2001","journal-title":"Nature"},{"key":"pcbi-0020120-b052","doi-asserted-by":"crossref","first-page":"11345","DOI":"10.1074\/jbc.M109893200","article-title":"Bcl-2 and Bcl-xL inhibit CD95-mediated apoptosis by preventing mitochondrial release of Smac\/DIABLO and subsequent inactivation of X-linked inhibitor-of-apoptosis protein.","volume":"277","year":"2002","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b053","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/S0960-9822(99)80068-2","article-title":"Bcl-2 regulates amplification of caspase activation by cytochrome c.","volume":"9","year":"1999","journal-title":"Curr Biol"},{"key":"pcbi-0020120-b054","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1038\/35023595","article-title":"Hsp27 negatively regulates cell death by interacting with cytochrome c.","volume":"2","year":"2000","journal-title":"Nat Cell Biol"},{"key":"pcbi-0020120-b055","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/S1097-2765(05)00021-3","article-title":"Aven, a novel inhibitor of caspase activation, binds Bcl-xL and Apaf-1.","volume":"6","year":"2000","journal-title":"Mol Cell"},{"key":"pcbi-0020120-b056","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1038\/35004029","article-title":"The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant.","volume":"2","year":"2000","journal-title":"Nat Cell Biol"},{"key":"pcbi-0020120-b057","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1083\/jcb.200303123","article-title":"Real-time single cell analysis of Smac\/DIABLO release during apoptosis.","volume":"162","year":"2003","journal-title":"J Cell Biol"},{"key":"pcbi-0020120-b058","doi-asserted-by":"crossref","first-page":"24506","DOI":"10.1074\/jbc.M110789200","article-title":"Single-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a rapid process. Role of caspase-3.","volume":"277","year":"2002","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b059","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1128\/MCB.18.1.608","article-title":"Human IAP-like protein regulates programmed cell death downstream of Bcl-xL and cytochrome c.","volume":"18","year":"1998","journal-title":"Mol Cell Biol"},{"key":"pcbi-0020120-b060","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1016\/S1525-0016(03)00146-1","article-title":"RU486-inducible retrovirus-mediated caspase-3 overexpression is cytotoxic to bcl-xL-expressing myeloma cells in vitro and in vivo.","volume":"8","year":"2003","journal-title":"Mol Ther"},{"key":"pcbi-0020120-b061","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/S1097-2765(00)80032-5","article-title":"Autoproteolytic activation of pro-caspases by oligomerization.","volume":"1","year":"1998","journal-title":"Mol Cell"},{"key":"pcbi-0020120-b062","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1016\/S1097-2765(03)00051-0","article-title":"A unified model for apical caspase activation.","volume":"11","year":"2003","journal-title":"Mol Cell"},{"key":"pcbi-0020120-b063","doi-asserted-by":"crossref","first-page":"1318","DOI":"10.1126\/science.282.5392.1318","article-title":"Regulation of cell death protease caspase-9 by phosphorylation.","volume":"282","year":"1998","journal-title":"Science"},{"key":"pcbi-0020120-b064","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1038\/sj.cdd.4400808","article-title":"Pro-caspase-3 overexpression sensitises ovarian cancer cells to proteasome inhibitors.","volume":"8","year":"2001","journal-title":"Cell Death Differ"},{"key":"pcbi-0020120-b065","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/S0014-4827(03)00073-9","article-title":"Expression of Smac\/DIABLO in ovarian carcinoma cells induces apoptosis via a caspase-9-mediated pathway.","volume":"286","year":"2003","journal-title":"Exp Cell Res"},{"key":"pcbi-0020120-b066","doi-asserted-by":"crossref","first-page":"24453","DOI":"10.1074\/jbc.C100074200","article-title":"Apaf-1\/cytochrome c-independent and Smac-dependent induction of apoptosis in multiple myeloma (MM) cells.","volume":"276","year":"2001","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b067","doi-asserted-by":"crossref","first-page":"4417","DOI":"10.1021\/jm040037k","article-title":"Discovery of potent antagonists of the antiapoptotic protein XIAP for the treatment of cancer.","volume":"47","year":"2004","journal-title":"J Med Chem"},{"key":"pcbi-0020120-b068","doi-asserted-by":"crossref","first-page":"1471","DOI":"10.1126\/science.1098231","article-title":"A small molecule Smac mimic potentiates TRAIL- and TNFalpha-mediated cell death.","volume":"305","year":"2004","journal-title":"Science"},{"key":"pcbi-0020120-b069","doi-asserted-by":"crossref","first-page":"40622","DOI":"10.1074\/jbc.M405963200","article-title":"Neuronal apoptosis-inhibitory protein does not interact with Smac and requires ATP to bind caspase-9.","volume":"279","year":"2004","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b070","first-page":"50","article-title":"Interactions of fluorochrome-labeled caspase inhibitors with apoptotic cells: A caution in data interpretation.","volume":"55","year":"2003","journal-title":"Cytometry A"},{"key":"pcbi-0020120-b071","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1002\/(SICI)1097-0320(20000601)40:2<151::AID-CYTO9>3.0.CO;2-9","article-title":"Flow cytometry detection of caspase 3 activation in preapoptotic leukemic cells.","volume":"40","year":"2000","journal-title":"Cytometry"},{"key":"pcbi-0020120-b072","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1083\/jcb.200406073","article-title":"Decreased apoptosome activity with neuronal differentiation sets the threshold for strict IAP regulation of apoptosis.","volume":"167","year":"2004","journal-title":"J Cell Biol"},{"key":"pcbi-0020120-b073","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1083\/jcb.200307130","article-title":"Critical function of endogenous XIAP in regulating caspase activation during sympathetic neuronal apoptosis.","volume":"163","year":"2003","journal-title":"J Cell Biol"},{"key":"pcbi-0020120-b074","first-page":"2826","article-title":"Antisense oligonucleotides targeting XIAP induce apoptosis and enhance chemotherapeutic activity against human lung cancer cells in vitro and in vivo.","volume":"9","year":"2003","journal-title":"Clin Cancer Res"},{"key":"pcbi-0020120-b075","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1126\/science.1070919","article-title":"Stochastic gene expression in a single cell.","volume":"297","year":"2002","journal-title":"Science"},{"key":"pcbi-0020120-b076","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1038\/sj.cdd.4401069","article-title":"XIAP inhibition of caspase-3 preserves its association with the Apaf-1 apoptosome and prevents CD95- and Bax-induced apoptosis.","volume":"9","year":"2002","journal-title":"Cell Death Differ"},{"key":"pcbi-0020120-b077","doi-asserted-by":"crossref","first-page":"31733","DOI":"10.1074\/jbc.M910231199","article-title":"XIAP regulates DNA damage-induced apoptosis downstream of caspase-9 cleavage.","volume":"275","year":"2000","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b078","doi-asserted-by":"crossref","first-page":"9070","DOI":"10.1158\/0008-5472.CAN-04-2344","article-title":"Insulin regulates cleavage of procaspase-9 via binding of X chromosome-linked inhibitor of apoptosis protein in HT-29 cells.","volume":"64","year":"2004","journal-title":"Cancer Res"},{"key":"pcbi-0020120-b079","doi-asserted-by":"crossref","first-page":"36152","DOI":"10.1074\/jbc.C000533200","article-title":"Molecular determinants of the caspase-promoting activity of Smac\/DIABLO and its role in the death receptor pathway.","volume":"275","year":"2000","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b080","doi-asserted-by":"crossref","first-page":"1423","DOI":"10.1038\/sj.cdd.4401950","article-title":"Mechanisms of cytochrome c release from mitochondria.","volume":"13","year":"2006","journal-title":"Cell Death Differ"},{"key":"pcbi-0020120-b081","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1111\/j.1471-4159.2004.02918.x","article-title":"Cytochrome c release from rat brain mitochondria is proportional to the mitochondrial functional deficit: Implications for apoptosis and neurodegenerative disease.","volume":"92","year":"2005","journal-title":"J Neurochem"},{"key":"pcbi-0020120-b082","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1083\/jcb.200105137","article-title":"APAF1 is a key transcriptional target for p53 in the regulation of neuronal cell death.","volume":"155","year":"2001","journal-title":"J Cell Biol"},{"key":"pcbi-0020120-b083","first-page":"18","article-title":"Smac is required for cytochrome c-induced apoptosis in prostate cancer LNCaP cells.","volume":"62","year":"2002","journal-title":"Cancer Res"},{"key":"pcbi-0020120-b084","doi-asserted-by":"crossref","first-page":"2210","DOI":"10.1158\/0008-5472.CAN-05-3923","article-title":"Enhanced sensitivity to cytochrome c-induced apoptosis mediated by PHAPI in breast cancer cells.","volume":"66","year":"2006","journal-title":"Cancer Res"},{"key":"pcbi-0020120-b085","doi-asserted-by":"crossref","first-page":"49517","DOI":"10.1074\/jbc.M310061200","article-title":"Requirement of both the second and third BIR domains for the relief of X-linked inhibitor of apoptosis protein (XIAP)-mediated caspase inhibition by Smac.","volume":"278","year":"2003","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b086","doi-asserted-by":"crossref","first-page":"2266","DOI":"10.1074\/jbc.M411106200","article-title":"Mitochondrial release of pro-apoptotic proteins: Electrostatic interactions can hold cytochrome c but not Smac\/DIABLO to mitochondrial membranes.","volume":"280","year":"2005","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b087","doi-asserted-by":"crossref","first-page":"1174","DOI":"10.1016\/j.yexcr.2006.01.026","article-title":"Relative timing of redistribution of cytochrome c and Smac\/DIABLO from mitochondria during apoptosis assessed by double immunocytochemistry on mammalian cells.","volume":"312","year":"2006","journal-title":"Exp Cell Res"},{"key":"pcbi-0020120-b088","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1007\/s10495-005-0803-9","article-title":"Smac\/DIABLO and cytochrome c are released from mitochondria through a similar mechanism during UV-induced apoptosis.","volume":"10","year":"2005","journal-title":"Apoptosis"},{"key":"pcbi-0020120-b089","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1038\/nrm1573","article-title":"Do inducers of apoptosis trigger caspase-independent cell death?.","volume":"6","year":"2005","journal-title":"Nat Rev Mol Cell Biol"},{"key":"pcbi-0020120-b090","doi-asserted-by":"crossref","first-page":"5242","DOI":"10.1093\/emboj\/18.19.5242","article-title":"Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases.","volume":"18","year":"1999","journal-title":"EMBO J"},{"key":"pcbi-0020120-b091","first-page":"1818","article-title":"Inhibitor of apoptosis protein hILP undergoes caspase-mediated cleavage during T lymphocyte apoptosis.","volume":"60","year":"2000","journal-title":"Cancer Res"},{"key":"pcbi-0020120-b092","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1038\/sj.cdd.4400503","article-title":"Expression and biological activity of X-linked inhibitor of apoptosis (XIAP) in human malignant glioma.","volume":"6","year":"1999","journal-title":"Cell Death Differ"},{"key":"pcbi-0020120-b093","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/S0014-5793(02)02774-6","article-title":"cIAP-1, but not XIAP, is cleaved by caspases during the apoptosis induced by TGF-beta in fetal rat hepatocytes.","volume":"520","year":"2002","journal-title":"FEBS Lett"},{"key":"pcbi-0020120-b094","doi-asserted-by":"crossref","first-page":"7141","DOI":"10.1074\/jbc.273.12.7141","article-title":"Caspase-dependent cleavage of signaling proteins during apoptosis. A turn-off mechanism for anti-apoptotic signals.","volume":"273","year":"1998","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b095","doi-asserted-by":"crossref","first-page":"5405","DOI":"10.1074\/jbc.M312044200","article-title":"Akt phosphorylation and stabilization of X-linked inhibitor of apoptosis protein (XIAP).","volume":"279","year":"2004","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b096","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1038\/nrm1618","article-title":"Translational control in stress and apoptosis.","volume":"6","year":"2005","journal-title":"Nat Rev Mol Cell Biol"},{"key":"pcbi-0020120-b097","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1038\/sj.cdd.4400502","article-title":"Synthesis of procaspases-3 and \u22127 during apoptosis in prostate cancer cells.","volume":"6","year":"1999","journal-title":"Cell Death Differ"},{"key":"pcbi-0020120-b098","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1084\/jem.184.2.765","article-title":"Selective cleavage of nuclear autoantigens during CD95 (Fas\/APO-1)-mediated T cell apoptosis.","volume":"184","year":"1996","journal-title":"J Exp Med"},{"key":"pcbi-0020120-b099","doi-asserted-by":"crossref","first-page":"6165","DOI":"10.1523\/JNEUROSCI.17-16-06165.1997","article-title":"Establishment of a cell-free system of neuronal apoptosis: comparison of premitochondrial, mitochondrial, and postmitochondrial phases.","volume":"17","year":"1997","journal-title":"J Neurosci"},{"key":"pcbi-0020120-b100","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1038\/sj.cdd.4401360","article-title":"Catalytic activity of caspase-3 is required for its degradation: Stabilization of the active complex by synthetic inhibitors.","volume":"11","year":"2004","journal-title":"Cell Death Differ"},{"key":"pcbi-0020120-b101","doi-asserted-by":"crossref","first-page":"7829","DOI":"10.1128\/MCB.23.21.7829-7837.2003","article-title":"Diarylurea compounds inhibit caspase activation by preventing the formation of the active 700-kilodalton apoptosome complex.","volume":"23","year":"2003","journal-title":"Mol Cell Biol"},{"key":"pcbi-0020120-b102","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1083\/jcb.200404158","article-title":"Mathematical modeling reveals threshold mechanism in CD95-induced apoptosis.","volume":"166","year":"2004","journal-title":"J Cell Biol"},{"key":"pcbi-0020120-b103","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1038\/77589","article-title":"A mathematical model of caspase function in apoptosis.","volume":"18","year":"2000","journal-title":"Nat Biotechnol"},{"key":"pcbi-0020120-b104","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.1529\/biophysj.105.068122","article-title":"Bistability in apoptosis: Roles of bax, bcl-2, and mitochondrial permeability transition pores.","volume":"90","year":"2006","journal-title":"Biophys J"},{"key":"pcbi-0020120-b105","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.jtbi.2004.11.011","article-title":"Mathematical modeling of the regulation of caspase-3 activation and degradation.","volume":"234","year":"2005","journal-title":"J Theor Biol"},{"key":"pcbi-0020120-b106","doi-asserted-by":"crossref","first-page":"27058","DOI":"10.1074\/jbc.M102415200","article-title":"X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and \u22127 in distinct modes.","volume":"276","year":"2001","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b107","doi-asserted-by":"crossref","first-page":"9677","DOI":"10.1074\/jbc.272.15.9677","article-title":"Substrate specificities of caspase family proteases.","volume":"272","year":"1997","journal-title":"J Biol Chem"},{"key":"pcbi-0020120-b108","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1038\/sj.emboj.7600544","article-title":"XIAP inhibits caspase-3 and \u22127 using two binding sites: Evolutionarily conserved mechanism of IAPs.","volume":"24","year":"2005","journal-title":"EMBO J"},{"key":"pcbi-0020120-b109","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/j.molcel.2006.03.030","article-title":"Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine.","volume":"22","year":"2006","journal-title":"Mol Cell"}],"container-title":["PLoS Computational Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pcbi.0020120","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,5,6]],"date-time":"2020-05-06T21:48:51Z","timestamp":1588801731000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pcbi.0020120"}},"subtitle":[],"editor":[{"given":"Chris","family":"Sander","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2006,9,15]]},"references-count":109,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2006,9,15]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pcbi.0020120","relation":{},"ISSN":["1553-7358"],"issn-type":[{"value":"1553-7358","type":"electronic"}],"subject":[],"published":{"date-parts":[[2006,9,15]]}}}