| pubmed-article:17671092 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17671092 | lifeskim:mentions | umls-concept:C1273518 | lld:lifeskim |
| pubmed-article:17671092 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:17671092 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:17671092 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:17671092 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
| pubmed-article:17671092 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:17671092 | lifeskim:mentions | umls-concept:C1516044 | lld:lifeskim |
| pubmed-article:17671092 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:17671092 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:17671092 | pubmed:dateCreated | 2007-8-2 | lld:pubmed |
| pubmed-article:17671092 | pubmed:abstractText | Homo-oligomerization of Bax (or Bak) has been hypothesized to be responsible for cell death through the mitochondria-dependent apoptosis pathway. However, partly due to a lack of structural information on the Bax homo-oligomerization and apoptosis inducing domain(s), this hypothesis has remained difficult to test. In this study, we identified a three-helix unit, comprised of the BH3 (helix 2) and BH1 domains (helix 4 and helix 5), as the homo-oligomerization domain of Bax. When targeted to mitochondria, this minimum oligomerization unit induced apoptosis in Bax(-/-)Bak(-/-) mouse embryonic fibroblasts (DKO). Strikingly, the central helix of Bax (helix 5), when replacing the corresponding helix (helix 5) of Bcl-xL, an anti-apoptotic Bcl-2 family protein structurally homologous to Bax, converted Bcl-xL into a Bax-like molecule capable of forming oligomers and causing apoptosis in the DKO cells. Finally, a series of systematic mutagenesis analyses revealed that homo-oligomerization is both necessary and sufficient for the apoptotic activity of Bax. These results suggest that active Bax causes mitochondrial damage through homo-oligomers of a three-helix functional unit. | lld:pubmed |
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| pubmed-article:17671092 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17671092 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17671092 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17671092 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17671092 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17671092 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:17671092 | pubmed:issn | 0890-9369 | lld:pubmed |
| pubmed-article:17671092 | pubmed:author | pubmed-author:LuoXuX | lld:pubmed |
| pubmed-article:17671092 | pubmed:author | pubmed-author:GeorgeNichola... | lld:pubmed |
| pubmed-article:17671092 | pubmed:author | pubmed-author:EvansJacquely... | lld:pubmed |
| pubmed-article:17671092 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17671092 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:17671092 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:17671092 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17671092 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17671092 | pubmed:pagination | 1937-48 | lld:pubmed |
| pubmed-article:17671092 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:17671092 | pubmed:meshHeading | pubmed-meshheading:17671092... | lld:pubmed |
| pubmed-article:17671092 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17671092 | pubmed:articleTitle | A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax. | lld:pubmed |
