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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1999-10-12
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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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD95,
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CASP8 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CASP9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Calpain,
http://linkedlifedata.com/resource/pubmed/chemical/Casp3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Casp8 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Casp9 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 8,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 9,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Lamins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Poly(ADP-ribose) Polymerases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Vimentin
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1356-9597
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
401-14
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10469173-Amino Acid Sequence,
pubmed-meshheading:10469173-Animals,
pubmed-meshheading:10469173-Antigens, CD95,
pubmed-meshheading:10469173-Apoptosis,
pubmed-meshheading:10469173-Calpain,
pubmed-meshheading:10469173-Caspase 3,
pubmed-meshheading:10469173-Caspase 8,
pubmed-meshheading:10469173-Caspase 9,
pubmed-meshheading:10469173-Caspases,
pubmed-meshheading:10469173-Cell Nucleus,
pubmed-meshheading:10469173-Cysteine Proteinase Inhibitors,
pubmed-meshheading:10469173-HeLa Cells,
pubmed-meshheading:10469173-Humans,
pubmed-meshheading:10469173-Jurkat Cells,
pubmed-meshheading:10469173-Lamins,
pubmed-meshheading:10469173-Mice,
pubmed-meshheading:10469173-Mutation,
pubmed-meshheading:10469173-Nuclear Proteins,
pubmed-meshheading:10469173-Poly(ADP-ribose) Polymerases,
pubmed-meshheading:10469173-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:10469173-Recombinant Fusion Proteins,
pubmed-meshheading:10469173-Vimentin
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pubmed:year |
1999
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pubmed:articleTitle |
Changes in nuclear morphology during apoptosis correlate with vimentin cleavage by different caspases located either upstream or downstream of Bcl-2 action.
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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
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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