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| pubmed-article:9390557 | lifeskim:mentions | umls-concept:C1332098 | lld:lifeskim |
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| pubmed-article:9390557 | lifeskim:mentions | umls-concept:C1707310 | lld:lifeskim |
| pubmed-article:9390557 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:9390557 | lifeskim:mentions | umls-concept:C1548602 | lld:lifeskim |
| pubmed-article:9390557 | lifeskim:mentions | umls-concept:C1516044 | lld:lifeskim |
| pubmed-article:9390557 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9390557 | pubmed:dateCreated | 1997-12-23 | lld:pubmed |
| pubmed-article:9390557 | pubmed:abstractText | We report here the purification of the third protein factor, Apaf-3, that participates in caspase-3 activation in vitro. Apaf-3 was identified as a member of the caspase family, caspase-9. Caspase-9 and Apaf-1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of cytochrome c and dATP, an event that leads to caspase-9 activation. Activated caspase-9 in turn cleaves and activates caspase-3. Depletion of caspase-9 from S-100 extracts diminished caspase-3 activation. Mutation of the active site of caspase-9 attenuated the activation of caspase-3 and cellular apoptotic response in vivo, indicating that caspase-9 is the most upstream member of the apoptotic protease cascade that is triggered by cytochrome c and dATP. | lld:pubmed |
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| pubmed-article:9390557 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9390557 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:9390557 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:9390557 | pubmed:author | pubmed-author:AhmadMM | lld:pubmed |
| pubmed-article:9390557 | pubmed:author | pubmed-author:LiPP | lld:pubmed |
| pubmed-article:9390557 | pubmed:author | pubmed-author:WangXX | lld:pubmed |
| pubmed-article:9390557 | pubmed:author | pubmed-author:AlnemriE SES | lld:pubmed |
| pubmed-article:9390557 | pubmed:author | pubmed-author:SrinivasulaS... | lld:pubmed |
| pubmed-article:9390557 | pubmed:author | pubmed-author:BudihardjoII | lld:pubmed |
| pubmed-article:9390557 | pubmed:author | pubmed-author:NijhawanDD | lld:pubmed |
| pubmed-article:9390557 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9390557 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:9390557 | pubmed:volume | 91 | lld:pubmed |
| pubmed-article:9390557 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9390557 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9390557 | pubmed:pagination | 479-89 | lld:pubmed |
| pubmed-article:9390557 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:9390557 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9390557 | pubmed:articleTitle | Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. | lld:pubmed |
| pubmed-article:9390557 | pubmed:affiliation | Howard Hughes Medical Institute, and Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, 75235, USA. | lld:pubmed |
| pubmed-article:9390557 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9390557 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9390557 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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