| pubmed-article:9804769 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9804769 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
| pubmed-article:9804769 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:9804769 | lifeskim:mentions | umls-concept:C0035687 | lld:lifeskim |
| pubmed-article:9804769 | lifeskim:mentions | umls-concept:C0597712 | lld:lifeskim |
| pubmed-article:9804769 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
| pubmed-article:9804769 | lifeskim:mentions | umls-concept:C0376515 | lld:lifeskim |
| pubmed-article:9804769 | lifeskim:mentions | umls-concept:C1511012 | lld:lifeskim |
| pubmed-article:9804769 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:9804769 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:9804769 | pubmed:issue | 46 | lld:pubmed |
| pubmed-article:9804769 | pubmed:dateCreated | 1998-12-8 | lld:pubmed |
| pubmed-article:9804769 | pubmed:abstractText | Bok (Bcl-2-related ovarian killer) is a proapoptotic Bcl-2 family protein identified in the ovary based on its dimerization with the antiapoptotic protein Mcl-1. In addition to the Bcl-2 homology (BH) domains 1 and 2 and the transmembrane sequence, Bok also has a BH3 domain believed to be important for dimerization with selective antiapoptotic Bcl-2 proteins and cell killing. We identified a splicing variant of Bok mRNA with a deletion of 43 residues from the full-length protein (Bok-L), leading to the fusion of the N-terminal-half of its BH3 domain to the C-terminal-half of the BH1 domain. Genomic analysis indicated that the Bok has five exons, and the short form of Bok (Bok-S) represents the splicing out of exon three during transcription. Although Bok-S retains the apoptosis-inducing activity in transfected cells, it has lost the ability to dimerize with antiapoptotic proteins in vitro. Additional BH3 domain mutations of Bok-L also led to defective heterodimerization without affecting its proapoptotic action. Furthermore, similar deletions for the related channel-forming proapoptotic Bax and Bak did not impair their cell killing ability. Thus, the naturally occurring Bok-S variant represents a new form of proapoptotic protein that induces cell killing without heterodimerization with antiapoptotic Bcl-2 proteins. This variant appears to contain the minimal module spanning BH1 and BH2 domains and the transmembrane sequence for apoptosis induction by channel-forming Bcl-2 proteins. | lld:pubmed |
| pubmed-article:9804769 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9804769 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9804769 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9804769 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9804769 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9804769 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9804769 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9804769 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9804769 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9804769 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9804769 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9804769 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9804769 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9804769 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9804769 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9804769 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9804769 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:9804769 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9804769 | pubmed:author | pubmed-author:HsuehA JAJ | lld:pubmed |
| pubmed-article:9804769 | pubmed:author | pubmed-author:HsuS YSY | lld:pubmed |
| pubmed-article:9804769 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9804769 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:9804769 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:9804769 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9804769 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9804769 | pubmed:pagination | 30139-46 | lld:pubmed |
| pubmed-article:9804769 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:9804769 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9804769 | pubmed:articleTitle | A splicing variant of the Bcl-2 member Bok with a truncated BH3 domain induces apoptosis but does not dimerize with antiapoptotic Bcl-2 proteins in vitro. | lld:pubmed |
| pubmed-article:9804769 | pubmed:affiliation | Division of Reproductive Biology, Department of Gynecology and Obstetrics, Stanford University Medical School, Stanford, California 94305-5317, USA. | lld:pubmed |
| pubmed-article:9804769 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9804769 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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