| pubmed-article:10862606 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10862606 | lifeskim:mentions | umls-concept:C0291573 | lld:lifeskim |
| pubmed-article:10862606 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:10862606 | lifeskim:mentions | umls-concept:C0077678 | lld:lifeskim |
| pubmed-article:10862606 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:10862606 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:10862606 | lifeskim:mentions | umls-concept:C1332415 | lld:lifeskim |
| pubmed-article:10862606 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:10862606 | lifeskim:mentions | umls-concept:C1513486 | lld:lifeskim |
| pubmed-article:10862606 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:10862606 | pubmed:issue | 35 | lld:pubmed |
| pubmed-article:10862606 | pubmed:dateCreated | 2000-10-3 | lld:pubmed |
| pubmed-article:10862606 | pubmed:abstractText | The inhibitor of apoptosis, cIAP2, contains a putative Ring finger motif at the C terminus. Using in vitro ubiquitination assays, we found that the Ring finger of cIAP2 alone possesses intrinsic ubiquitin ligase activity and promotes substrate-independent ubiquitination. It also promotes ubiquitination of caspases 3 and 7 but not caspase-1. The Ring fingers of c-Cbl and Apc11 failed to promote caspase-7 ubiquitination, suggesting that the Ring finger of cIAP2 itself is involved in substrate recognition. | lld:pubmed |
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| pubmed-article:10862606 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10862606 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10862606 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10862606 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:10862606 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10862606 | pubmed:author | pubmed-author:KamadaSS | lld:pubmed |
| pubmed-article:10862606 | pubmed:author | pubmed-author:HunterTT | lld:pubmed |
| pubmed-article:10862606 | pubmed:author | pubmed-author:JoazeiroC ACA | lld:pubmed |
| pubmed-article:10862606 | pubmed:author | pubmed-author:BonfocoEE | lld:pubmed |
| pubmed-article:10862606 | pubmed:author | pubmed-author:LeversonJ DJD | lld:pubmed |
| pubmed-article:10862606 | pubmed:author | pubmed-author:HuangH kH | lld:pubmed |
| pubmed-article:10862606 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10862606 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:10862606 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10862606 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10862606 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10862606 | pubmed:pagination | 26661-4 | lld:pubmed |
| pubmed-article:10862606 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10862606 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10862606 | pubmed:articleTitle | The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7. | lld:pubmed |
| pubmed-article:10862606 | pubmed:affiliation | Molecular Biology and Virology Laboratory, The Salk Institute for Biological Studies and the Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA. | lld:pubmed |
| pubmed-article:10862606 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10862606 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10862606 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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