| pubmed-article:9202007 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9202007 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:9202007 | lifeskim:mentions | umls-concept:C0376515 | lld:lifeskim |
| pubmed-article:9202007 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:9202007 | lifeskim:mentions | umls-concept:C1706395 | lld:lifeskim |
| pubmed-article:9202007 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9202007 | lifeskim:mentions | umls-concept:C0205254 | lld:lifeskim |
| pubmed-article:9202007 | pubmed:issue | 27 | lld:pubmed |
| pubmed-article:9202007 | pubmed:dateCreated | 1997-7-31 | lld:pubmed |
| pubmed-article:9202007 | pubmed:abstractText | Interactions among proteins in the Bcl-2 family regulate the onset of programmed cell death. Previous work has shown that the death-inhibiting family members Bcl-2 and Bcl-xL form heterodimers with the death-promoting homologue Bax and that certain site-directed mutants of Bcl-2 and Bcl-xL lose both biological activity and the ability to bind Bax. To better understand the structural basis of heterodimer formation, we have used a yeast two-hybrid assay to screen for mutants of Bax that regain the ability to bind to these inactive Bcl-2(G145A) and Bcl-xL(G138A) mutants. This screen identified a series of C-terminally truncated Bax molecules that contain complete BH3 (Bcl-2 homology domain 3) domains but that have lost BH1 and BH2 sequences. These results indicate that while the Bcl-2 and Bcl-xL mutants fail to bind full-length Bax, they still retain a binding site for the critical BH3 domain. This suggests that conformational constraints in full-length Bax regulate its ability to bind to other Bcl-2 family members. Furthermore, we demonstrate that the normally inert Bcl-2(G145A) mutant effectively blocks apoptosis induced by a C-terminally truncated Bax molecule, but does not block apoptosis induced by wild-type Bax. This demonstrates that cell protection can be effected by directly binding pro-apoptotic members of the Bcl-2 family. | lld:pubmed |
| pubmed-article:9202007 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9202007 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9202007 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9202007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9202007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9202007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9202007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9202007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9202007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9202007 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9202007 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:9202007 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9202007 | pubmed:author | pubmed-author:WilsonGG | lld:pubmed |
| pubmed-article:9202007 | pubmed:author | pubmed-author:McConnellMM | lld:pubmed |
| pubmed-article:9202007 | pubmed:author | pubmed-author:WangYY | lld:pubmed |
| pubmed-article:9202007 | pubmed:author | pubmed-author:ChangJJ | lld:pubmed |
| pubmed-article:9202007 | pubmed:author | pubmed-author:FritzL CLC | lld:pubmed |
| pubmed-article:9202007 | pubmed:author | pubmed-author:OttilieSS | lld:pubmed |
| pubmed-article:9202007 | pubmed:author | pubmed-author:OltersdorfTT | lld:pubmed |
| pubmed-article:9202007 | pubmed:author | pubmed-author:WeeksSS | lld:pubmed |
| pubmed-article:9202007 | pubmed:author | pubmed-author:DiazJ LJL | lld:pubmed |
| pubmed-article:9202007 | pubmed:author | pubmed-author:TuffoK MKM | lld:pubmed |
| pubmed-article:9202007 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9202007 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:9202007 | pubmed:volume | 272 | lld:pubmed |
| pubmed-article:9202007 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9202007 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9202007 | pubmed:pagination | 16955-61 | lld:pubmed |
| pubmed-article:9202007 | pubmed:dateRevised | 2006-5-1 | lld:pubmed |
| pubmed-article:9202007 | pubmed:meshHeading | pubmed-meshheading:9202007-... | lld:pubmed |
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| pubmed-article:9202007 | pubmed:meshHeading | pubmed-meshheading:9202007-... | lld:pubmed |
| pubmed-article:9202007 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9202007 | pubmed:articleTitle | Structural and functional complementation of an inactive Bcl-2 mutant by Bax truncation. | lld:pubmed |
| pubmed-article:9202007 | pubmed:affiliation | IDUN Pharmaceuticals, Inc., La Jolla, California 92037, USA. sottilie@idun.com | lld:pubmed |
| pubmed-article:9202007 | pubmed:publicationType | Journal Article | lld:pubmed |
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