| pubmed-article:9430630 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9430630 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:9430630 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
| pubmed-article:9430630 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:9430630 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:9430630 | lifeskim:mentions | umls-concept:C0376515 | lld:lifeskim |
| pubmed-article:9430630 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:9430630 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:9430630 | lifeskim:mentions | umls-concept:C0445450 | lld:lifeskim |
| pubmed-article:9430630 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9430630 | pubmed:dateCreated | 1998-2-26 | lld:pubmed |
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| pubmed-article:9430630 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9430630 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9430630 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9430630 | pubmed:abstractText | Certain members of the Bcl-2 family inhibit apoptosis while others facilitate this physiological process of cell death. An expression screen for proteins that bind to Bcl-2 yielded a small novel protein, denoted Bim, whose only similarity to any known protein is the short (nine amino acid) BH3 motif shared by most Bcl-2 homologues. Bim provokes apoptosis, and the BH3 region is required for Bcl-2 binding and for most of its cytotoxicity. Like Bcl-2, Bim possesses a hydrophobic C-terminus and localizes to intracytoplasmic membranes. Three Bim isoforms, probably generated by alternative splicing, all induce apoptosis, the shortest being the most potent. Wild-type Bcl-2 associates with Bim in vivo and modulates its death function, whereas Bcl-2 mutants that lack survival function do neither. Significantly, Bcl-xL and Bcl-w, the two closest homologues of Bcl-2, also bind to Bim and inhibit its activity, but more distant viral homologues, adenovirus E1B19K and Epstein-Barr virus BHRF-1, can do neither. Hence, Bim appears to act as a 'death ligand' which can only neutralize certain members of the pro-survival Bcl-2 sub-family. | lld:pubmed |
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| pubmed-article:9430630 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9430630 | pubmed:citationSubset | IM | lld:pubmed |
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