| pubmed-article:9461218 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9461218 | lifeskim:mentions | umls-concept:C0007620 | lld:lifeskim |
| pubmed-article:9461218 | lifeskim:mentions | umls-concept:C0010749 | lld:lifeskim |
| pubmed-article:9461218 | lifeskim:mentions | umls-concept:C0376515 | lld:lifeskim |
| pubmed-article:9461218 | lifeskim:mentions | umls-concept:C0030685 | lld:lifeskim |
| pubmed-article:9461218 | lifeskim:mentions | umls-concept:C0680255 | lld:lifeskim |
| pubmed-article:9461218 | lifeskim:mentions | umls-concept:C0391871 | lld:lifeskim |
| pubmed-article:9461218 | lifeskim:mentions | umls-concept:C1283071 | lld:lifeskim |
| pubmed-article:9461218 | lifeskim:mentions | umls-concept:C1963578 | lld:lifeskim |
| pubmed-article:9461218 | pubmed:issue | 6666 | lld:pubmed |
| pubmed-article:9461218 | pubmed:dateCreated | 1998-2-17 | lld:pubmed |
| pubmed-article:9461218 | pubmed:abstractText | Following exposure of cells to stimuli that trigger programmed cell death (apoptosis), cytochrome c is rapidly released from mitochondria into the cytoplasm where it activates proteolytic molecules known as caspases that specifically cleave the amino-acid sequence DEVD and are crucial for the execution of apoptosis. The protein Bcl-2 interferes with this activation of caspases by preventing the release of cytochrome c. Here we study these molecular interactions during apoptosis induced by the protein Bax, a pro-apoptotic homologue of Bcl-2. We show that in cells transiently transfected with bax, Bax localizes to mitochondria and induces the release of cytochrome c, activation of caspase-3, membrane blebbing, nuclear fragmentation, and cell death. Caspase inhibitors do not affect Bax-induced cytochrome c release but block caspase-3 activation and nuclear fragmentation. Unexpectedly, Bcl-2 also fails to prevent Bax-induced cytochrome c release, although it co-localizes with Bax to mitochondria. Cells overexpressing both Bcl-2 and Bax show no signs of caspase activation and survive with significant amounts of cytochrome c in the cytoplasm. These findings indicate that Bcl-2 can interfere with Bax killing downstream of and independently of cytochrome c release. | lld:pubmed |
| pubmed-article:9461218 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461218 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9461218 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461218 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9461218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9461218 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9461218 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:9461218 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:9461218 | pubmed:author | pubmed-author:JansenBB | lld:pubmed |
| pubmed-article:9461218 | pubmed:author | pubmed-author:OlivierRR | lld:pubmed |
| pubmed-article:9461218 | pubmed:author | pubmed-author:BornerCC | lld:pubmed |
| pubmed-article:9461218 | pubmed:author | pubmed-author:MonneyLL | lld:pubmed |
| pubmed-article:9461218 | pubmed:author | pubmed-author:FellayII | lld:pubmed |
| pubmed-article:9461218 | pubmed:author | pubmed-author:RosséTT | lld:pubmed |
| pubmed-article:9461218 | pubmed:author | pubmed-author:RagerMM | lld:pubmed |
| pubmed-article:9461218 | pubmed:author | pubmed-author:ConusSS | lld:pubmed |
| pubmed-article:9461218 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9461218 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:9461218 | pubmed:volume | 391 | lld:pubmed |
| pubmed-article:9461218 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9461218 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9461218 | pubmed:pagination | 496-9 | lld:pubmed |
| pubmed-article:9461218 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:9461218 | pubmed:meshHeading | pubmed-meshheading:9461218-... | lld:pubmed |
| pubmed-article:9461218 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9461218 | pubmed:articleTitle | Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c. | lld:pubmed |
| pubmed-article:9461218 | pubmed:affiliation | Institute of Biochemistry, University of Fribourg, Switzerland. | lld:pubmed |
| pubmed-article:9461218 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9461218 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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