| pubmed-article:11106668 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11106668 | lifeskim:mentions | umls-concept:C0205242 | lld:lifeskim |
| pubmed-article:11106668 | lifeskim:mentions | umls-concept:C1531411 | lld:lifeskim |
| pubmed-article:11106668 | lifeskim:mentions | umls-concept:C0010656 | lld:lifeskim |
| pubmed-article:11106668 | lifeskim:mentions | umls-concept:C1708096 | lld:lifeskim |
| pubmed-article:11106668 | lifeskim:mentions | umls-concept:C1332414 | lld:lifeskim |
| pubmed-article:11106668 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:11106668 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:11106668 | pubmed:dateCreated | 2001-5-25 | lld:pubmed |
| pubmed-article:11106668 | pubmed:abstractText | Although human c-IAP1 and c-IAP2 have been reported to possess antiapoptotic activity against a variety of stimuli in several mammalian cell types, we observed that full-length c-IAP1 and c-IAP2 failed to protect cells from apoptosis induced by Bax overexpression, tumor necrosis factor alpha treatment or Sindbis virus infection. However, deletion of the C-terminal RING domains of c-IAP1 and c-IAP2 restored antiapoptotic activity, indicating that this region negatively regulates the antiapoptotic function of the N-terminal BIR domain. This finding is consistent with the observation by others that the spacer region and RING domain of c-IAP1 functions as an E3 ligase, promoting autoubiquitination and degradation of c-IAP1. In addition, we found that c-IAP1 is cleaved during apoptosis to 52- and 35-kDa fragments. Both fragments contain the C-terminal end of c-IAP1 including the RING finger. In vitro cleavage of c-IAP1 with apoptotic cell extracts or with purified recombinant caspase-3 produced similar fragments. Furthermore, transfection of cells with the spacer-RING domain alone suppressed the antiapoptotic function of the N-terminal BIR domain of c-IAP1 and induced apoptosis. Optimal death-inducing activity of the spacer-RING required both the spacer region and the zinc-binding RING domain of c-IAP1 but did not require the caspase recruitment domain located within the spacer region. To the contrary, deletion of the caspase recruitment domain increased proapoptotic activity, apparently by stabilizing the C-terminal fragment. | lld:pubmed |
| pubmed-article:11106668 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11106668 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11106668 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11106668 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11106668 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11106668 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11106668 | pubmed:author | pubmed-author:HardwickJ MJM | lld:pubmed |
| pubmed-article:11106668 | pubmed:author | pubmed-author:DuckettC SCS | lld:pubmed |
| pubmed-article:11106668 | pubmed:author | pubmed-author:ThornberryN... | lld:pubmed |
| pubmed-article:11106668 | pubmed:author | pubmed-author:HeW WWW | lld:pubmed |
| pubmed-article:11106668 | pubmed:author | pubmed-author:ClemR JRJ | lld:pubmed |
| pubmed-article:11106668 | pubmed:author | pubmed-author:RichterB WBW | lld:pubmed |
| pubmed-article:11106668 | pubmed:author | pubmed-author:SheuT TTT | lld:pubmed |
| pubmed-article:11106668 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11106668 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:11106668 | pubmed:volume | 276 | lld:pubmed |
| pubmed-article:11106668 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11106668 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11106668 | pubmed:pagination | 7602-8 | lld:pubmed |
| pubmed-article:11106668 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11106668 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11106668 | pubmed:articleTitle | c-IAP1 is cleaved by caspases to produce a proapoptotic C-terminal fragment. | lld:pubmed |
| pubmed-article:11106668 | pubmed:affiliation | Department of Molecular Microbiology and Immunology, Johns Hopkins Schools of Public Health and Medicine, Baltimore, Maryland 21205, USA. | lld:pubmed |
| pubmed-article:11106668 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11106668 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11106668 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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