| pubmed-article:11230124 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11230124 | lifeskim:mentions | umls-concept:C0664613 | lld:lifeskim |
| pubmed-article:11230124 | lifeskim:mentions | umls-concept:C1657248 | lld:lifeskim |
| pubmed-article:11230124 | lifeskim:mentions | umls-concept:C0271510 | lld:lifeskim |
| pubmed-article:11230124 | lifeskim:mentions | umls-concept:C0333117 | lld:lifeskim |
| pubmed-article:11230124 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:11230124 | lifeskim:mentions | umls-concept:C1332098 | lld:lifeskim |
| pubmed-article:11230124 | lifeskim:mentions | umls-concept:C1337109 | lld:lifeskim |
| pubmed-article:11230124 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:11230124 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:11230124 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:11230124 | pubmed:dateCreated | 2001-3-20 | lld:pubmed |
| pubmed-article:11230124 | pubmed:abstractText | During apoptosis, release of cytochrome c initiates dATP-dependent oligomerization of Apaf-1 and formation of the apoptosome. In a cell-free system, we have addressed the order in which apical and effector caspases, caspases-9 and -3, respectively, are recruited to, activated and retained within the apoptosome. We propose a multi-step process, whereby catalytically active processed or unprocessed caspase-9 initially binds the Apaf-1 apoptosome in cytochrome c/dATP-activated lysates and consequently recruits caspase-3 via an interaction between the active site cysteine (C287) in caspase-9 and a critical aspartate (D175) in caspase-3. We demonstrate that XIAP, an inhibitor-of-apoptosis protein, is normally present in high molecular weight complexes in unactivated cell lysates, but directly interacts with the apoptosome in cytochrome c/dATP-activated lysates. XIAP associates with oligomerized Apaf-1 and/or processed caspase-9 and influences the activation of caspase-3, but also binds activated caspase-3 produced within the apoptosome and sequesters it within the complex. Thus, XIAP may regulate cell death by inhibiting the activation of caspase-3 within the apoptosome and by preventing release of active caspase-3 from the complex. | lld:pubmed |
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| pubmed-article:11230124 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11230124 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11230124 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11230124 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11230124 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11230124 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:11230124 | pubmed:author | pubmed-author:WalkerGG | lld:pubmed |
| pubmed-article:11230124 | pubmed:author | pubmed-author:CohenG MGM | lld:pubmed |
| pubmed-article:11230124 | pubmed:author | pubmed-author:FuFF | lld:pubmed |
| pubmed-article:11230124 | pubmed:author | pubmed-author:AlnemriE SES | lld:pubmed |
| pubmed-article:11230124 | pubmed:author | pubmed-author:ButterworthMM | lld:pubmed |
| pubmed-article:11230124 | pubmed:author | pubmed-author:SrinivasulaS... | lld:pubmed |
| pubmed-article:11230124 | pubmed:author | pubmed-author:BrattonS BSB | lld:pubmed |
| pubmed-article:11230124 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11230124 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11230124 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:11230124 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11230124 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11230124 | pubmed:pagination | 998-1009 | lld:pubmed |
| pubmed-article:11230124 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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