| pubmed-article:8621473 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8621473 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:8621473 | lifeskim:mentions | umls-concept:C0376515 | lld:lifeskim |
| pubmed-article:8621473 | lifeskim:mentions | umls-concept:C0920679 | lld:lifeskim |
| pubmed-article:8621473 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:8621473 | pubmed:dateCreated | 1996-6-20 | lld:pubmed |
| pubmed-article:8621473 | pubmed:abstractText | Bcl-2 and Bax are members of a family of cytoplasmic proteins that regulate apoptosis. The two proteins have highly similar amino acid sequences but are functionally opposed: Bcl-2 acts to inhibit apoptosis, whereas Bax counteracts this effect. The antagonism appears to depend upon dimerization between Bcl-2 and Bax, but its mechanism is otherwise unknown. Here we report that overexpressing Bax induces apoptosis in a mammalian fibroblast cell line, and we identify a novel, short "suicide domain" in Bax that is required for this effect. Inserting this domain in place of the corresponding, divergent sequence in Bcl-2 converts Bcl-2 from an inhibitor into an activator of cell death. These findings imply that a specific region in Bax confers an active propensity for apoptosis in mammalian cells and support the view that Bcl-2 may block death primarily by suppressing Bax activity. | lld:pubmed |
| pubmed-article:8621473 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8621473 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8621473 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8621473 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8621473 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8621473 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8621473 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8621473 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8621473 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8621473 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8621473 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8621473 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8621473 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8621473 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8621473 | pubmed:author | pubmed-author:ParslowT GTG | lld:pubmed |
| pubmed-article:8621473 | pubmed:author | pubmed-author:HunterJ JJJ | lld:pubmed |
| pubmed-article:8621473 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8621473 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:8621473 | pubmed:volume | 271 | lld:pubmed |
| pubmed-article:8621473 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8621473 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8621473 | pubmed:pagination | 8521-4 | lld:pubmed |
| pubmed-article:8621473 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8621473 | pubmed:meshHeading | pubmed-meshheading:8621473-... | lld:pubmed |
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| pubmed-article:8621473 | pubmed:meshHeading | pubmed-meshheading:8621473-... | lld:pubmed |
| pubmed-article:8621473 | pubmed:meshHeading | pubmed-meshheading:8621473-... | lld:pubmed |
| pubmed-article:8621473 | pubmed:meshHeading | pubmed-meshheading:8621473-... | lld:pubmed |
| pubmed-article:8621473 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8621473 | pubmed:articleTitle | A peptide sequence from Bax that converts Bcl-2 into an activator of apoptosis. | lld:pubmed |
| pubmed-article:8621473 | pubmed:affiliation | Department of Pathology, University of California, San Francisco, 94143-0506, USA. | lld:pubmed |
| pubmed-article:8621473 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8621473 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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