pubmed-article:10469173 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10469173 | lifeskim:mentions | umls-concept:C0042666 | lld:lifeskim |
pubmed-article:10469173 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
pubmed-article:10469173 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
pubmed-article:10469173 | lifeskim:mentions | umls-concept:C0010656 | lld:lifeskim |
pubmed-article:10469173 | lifeskim:mentions | umls-concept:C0441472 | lld:lifeskim |
pubmed-article:10469173 | lifeskim:mentions | umls-concept:C0376515 | lld:lifeskim |
pubmed-article:10469173 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
pubmed-article:10469173 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
pubmed-article:10469173 | lifeskim:mentions | umls-concept:C1749565 | lld:lifeskim |
pubmed-article:10469173 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
pubmed-article:10469173 | pubmed:issue | 7 | lld:pubmed |
pubmed-article:10469173 | pubmed:dateCreated | 1999-10-12 | lld:pubmed |
pubmed-article:10469173 | pubmed:abstractText | Upon Fas stimulation, procaspase-8 is recruited to the death-inducing signalling complex where autoactivation of caspase-8 occurs. Active caspase-8 can directly activate downstream caspases (e.g. caspase-3, 6, and 7) for the execution of apoptosis (mitochondria-independent pathway), while caspase-8 can also lead to executioner caspase activation through mitochondrial damage (mitochondria-dependent pathway). Caspase activation results in the dismantling of intracellular structure through specific proteolysis. | lld:pubmed |
pubmed-article:10469173 | pubmed:language | eng | lld:pubmed |
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pubmed-article:10469173 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10469173 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10469173 | pubmed:month | Jul | lld:pubmed |
pubmed-article:10469173 | pubmed:issn | 1356-9597 | lld:pubmed |
pubmed-article:10469173 | pubmed:author | pubmed-author:MorishimaNN | lld:pubmed |
pubmed-article:10469173 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10469173 | pubmed:volume | 4 | lld:pubmed |
pubmed-article:10469173 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10469173 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10469173 | pubmed:pagination | 401-14 | lld:pubmed |
pubmed-article:10469173 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:10469173 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10469173 | pubmed:articleTitle | Changes in nuclear morphology during apoptosis correlate with vimentin cleavage by different caspases located either upstream or downstream of Bcl-2 action. | lld:pubmed |
pubmed-article:10469173 | pubmed:affiliation | Biodesign Research Group, RIKEN (the Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. morishim@postman.riken.go.jp | lld:pubmed |
pubmed-article:10469173 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10469173 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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