pubmed-article:11973609 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11973609 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:11973609 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:11973609 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
pubmed-article:11973609 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
pubmed-article:11973609 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:11973609 | pubmed:dateCreated | 2002-4-25 | lld:pubmed |
pubmed-article:11973609 | pubmed:abstractText | BH3-only proteins are structurally distant members of the Bcl-2 protein family that trigger apoptosis. Genetic experiments have shown that these proteins are essential initiators of programmed cell death in species as distantly related as mice and C. elegans. BH3-only proteins share with each other and with the remainder of the Bcl-2 family only a nine amino acid BH3 (Bcl-2 Homology) region. Mutational analyses have demonstrated that this domain is required for their ability to bind to Bcl-2-like pro-survival proteins and to initiate apoptosis. So far only one BH3-only protein, EGL-1, has been identified in C. elegans and it is required for all developmentally programmed death of somatic cells in this species. In contrast, mammals have at least 10 BH3-only proteins that differ in their expression pattern and mode of activation. Studies in gene targeted mice have indicated that different BH3-only proteins are required for the initiation of distinct apoptotic stimuli. The pro-apoptotic activities of BH3-only proteins are stringently controlled by a variety of mechanisms. C. elegans egl-1 as well as mammalian hrk/dp5, noxa, puma/bbc3 and bim/bod are regulated by a diverse range of transcription factors. Certain BH3-only proteins, including Bad, Bik/Nbk, Bid, Bim/Bod and Bmf, are restrained by post-translational modifications that cause their sequestration from pro-survival Bcl-2 family members. In this review we describe current knowledge of the functions and transcriptional as well as post-translational control mechanisms of BH3-only proteins. | lld:pubmed |
pubmed-article:11973609 | pubmed:language | eng | lld:pubmed |
pubmed-article:11973609 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11973609 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11973609 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11973609 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11973609 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11973609 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:11973609 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11973609 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11973609 | pubmed:month | May | lld:pubmed |
pubmed-article:11973609 | pubmed:issn | 1350-9047 | lld:pubmed |
pubmed-article:11973609 | pubmed:author | pubmed-author:StrasserAA | lld:pubmed |
pubmed-article:11973609 | pubmed:author | pubmed-author:PuthalakathHH | lld:pubmed |
pubmed-article:11973609 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11973609 | pubmed:volume | 9 | lld:pubmed |
pubmed-article:11973609 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11973609 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11973609 | pubmed:pagination | 505-12 | lld:pubmed |
pubmed-article:11973609 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:11973609 | pubmed:meshHeading | pubmed-meshheading:11973609... | lld:pubmed |
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pubmed-article:11973609 | pubmed:meshHeading | pubmed-meshheading:11973609... | lld:pubmed |
pubmed-article:11973609 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:11973609 | pubmed:articleTitle | Keeping killers on a tight leash: transcriptional and post-translational control of the pro-apoptotic activity of BH3-only proteins. | lld:pubmed |
pubmed-article:11973609 | pubmed:affiliation | The Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia. | lld:pubmed |
pubmed-article:11973609 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11973609 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:11973609 | pubmed:publicationType | Review | lld:pubmed |
pubmed-article:11973609 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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