| pubmed-article:20022954 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20022954 | lifeskim:mentions | umls-concept:C0042216 | lld:lifeskim |
| pubmed-article:20022954 | lifeskim:mentions | umls-concept:C0910167 | lld:lifeskim |
| pubmed-article:20022954 | lifeskim:mentions | umls-concept:C0042736 | lld:lifeskim |
| pubmed-article:20022954 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:20022954 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:20022954 | pubmed:dateCreated | 2010-2-15 | lld:pubmed |
| pubmed-article:20022954 | pubmed:abstractText | Apoptosis plays important roles in host defense, including the elimination of virus-infected cells. The executioners of apoptosis are caspase family proteases. We report that vaccinia virus-encoded F1L protein, previously recognized as anti-apoptotic viral Bcl-2 family protein, is a caspase-9 inhibitor. F1L binds to and specifically inhibits caspase-9, the apical protease in the mitochondrial cell death pathway while failing to inhibit other caspases. In cells, F1L inhibits apoptosis and proteolytic processing of caspases induced by overexpression of caspase-9 but not caspase-8. An N-terminal region of F1L preceding the Bcl-2-like fold accounts for caspase-9 inhibition and significantly contributes to the anti-apoptotic activity of F1L. Viral F1L thus provides the first example of caspase inhibition by a Bcl-2 family member; it functions both as a suppressor of proapoptotic Bcl-2 family proteins and as an inhibitor of caspase-9, thereby neutralizing two sequential steps in the mitochondrial cell death pathway. | lld:pubmed |
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| pubmed-article:20022954 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20022954 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20022954 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:20022954 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20022954 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:20022954 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:20022954 | pubmed:author | pubmed-author:ReedJohn CJC | lld:pubmed |
| pubmed-article:20022954 | pubmed:author | pubmed-author:JinChaofangC | lld:pubmed |
| pubmed-article:20022954 | pubmed:author | pubmed-author:SalvesenGuy... | lld:pubmed |
| pubmed-article:20022954 | pubmed:author | pubmed-author:ChenLiliL | lld:pubmed |
| pubmed-article:20022954 | pubmed:author | pubmed-author:ChenHanH | lld:pubmed |
| pubmed-article:20022954 | pubmed:author | pubmed-author:WelshKateK | lld:pubmed |
| pubmed-article:20022954 | pubmed:author | pubmed-author:ZhaiDayongD | lld:pubmed |
| pubmed-article:20022954 | pubmed:author | pubmed-author:LiddingtonRob... | lld:pubmed |
| pubmed-article:20022954 | pubmed:author | pubmed-author:ShiauChung-we... | lld:pubmed |
| pubmed-article:20022954 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20022954 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:20022954 | pubmed:volume | 285 | lld:pubmed |
| pubmed-article:20022954 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20022954 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20022954 | pubmed:pagination | 5569-80 | lld:pubmed |
| pubmed-article:20022954 | pubmed:dateRevised | 2011-7-25 | lld:pubmed |
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