| pubmed-article:16474435 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16474435 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:16474435 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:16474435 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:16474435 | lifeskim:mentions | umls-concept:C0376515 | lld:lifeskim |
| pubmed-article:16474435 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:16474435 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16474435 | pubmed:dateCreated | 2006-2-13 | lld:pubmed |
| pubmed-article:16474435 | pubmed:abstractText | Commitment of cells to apoptosis is governed largely by protein-protein interactions between members of the Bcl-2 protein family. Its three sub-families have distinct roles: the BH3-only proteins trigger apoptosis by binding via their BH3 domain to pro-survival relatives, while the pro-apoptotic Bax and Bak have an essential downstream role involving disruption of organellar membranes and induction of caspase activation. The BH3-only proteins act as damage sensors, held inert until their activation by stress signals. Once activated, they were thought to bind promiscuously to pro-survival protein targets but unexpected selectivity has recently emerged from analysis of their interactions. Some BH3-only proteins also bind to Bax and Bak. Whether Bax and Bak are activated directly by these BH3-only proteins, or indirectly as a consequence of BH3-only proteins neutralizing their pro-survival targets is the subject of intense debate. Regardless of this, a detailed understanding of the interactions between family members, which are often selective, has notable implications for designing anti-cancer drugs to target the Bcl-2 family. | lld:pubmed |
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| pubmed-article:16474435 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16474435 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16474435 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16474435 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16474435 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:16474435 | pubmed:issn | 1001-0602 | lld:pubmed |
| pubmed-article:16474435 | pubmed:author | pubmed-author:HuangDavid... | lld:pubmed |
| pubmed-article:16474435 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:16474435 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16474435 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:16474435 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16474435 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16474435 | pubmed:pagination | 203-13 | lld:pubmed |
| pubmed-article:16474435 | pubmed:dateRevised | 2008-7-9 | lld:pubmed |
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| pubmed-article:16474435 | pubmed:meshHeading | pubmed-meshheading:16474435... | lld:pubmed |
| pubmed-article:16474435 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16474435 | pubmed:articleTitle | How the Bcl-2 family of proteins interact to regulate apoptosis. | lld:pubmed |
| pubmed-article:16474435 | pubmed:affiliation | The Walter and Eliza Hall Institute of Medical Research, and Department of Medical Biology, University of Melbourne, Parkville, Victoria 3010, Australia. | lld:pubmed |
| pubmed-article:16474435 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16474435 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:16474435 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16474435 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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