rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1999-6-9
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pubmed:abstractText |
Cysteine proteases of the caspase family are crucial mediators of apoptosis. All mammalian cells contain a large number of caspases. Although many caspases are activated in a cell committed to apoptosis, recent data from caspase gene knockout mice suggest that individual caspases may be involved in the cell and stimulus-specific pathways of cell death. The gene disruption studies also establish the functional hierarchy between two structurally distinct classes of caspases. The present review discusses these recent findings and elaborates on how these mutant mouse models have helped the understanding of the mechanisms that govern programmed cell death in the immune and other systems.
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
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 2,
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/Cytokines,
http://linkedlifedata.com/resource/pubmed/chemical/Fadd protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Fas-Associated Death Domain Protein
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0818-9641
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
77
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
58-63
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10101687-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:10101687-Animals,
pubmed-meshheading:10101687-Apoptosis,
pubmed-meshheading:10101687-Carrier Proteins,
pubmed-meshheading:10101687-Caspase 2,
pubmed-meshheading:10101687-Caspase 8,
pubmed-meshheading:10101687-Caspase 9,
pubmed-meshheading:10101687-Caspases,
pubmed-meshheading:10101687-Cytokines,
pubmed-meshheading:10101687-Enzyme Activation,
pubmed-meshheading:10101687-Fas-Associated Death Domain Protein,
pubmed-meshheading:10101687-Mice,
pubmed-meshheading:10101687-Mice, Knockout,
pubmed-meshheading:10101687-Mitochondria,
pubmed-meshheading:10101687-Models, Biological,
pubmed-meshheading:10101687-Protein Processing, Post-Translational
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pubmed:year |
1999
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pubmed:articleTitle |
Targeted disruption of caspase genes in mice: what they tell us about the functions of individual caspases in apoptosis.
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pubmed:affiliation |
Hanson Centre for Cancer Research, Institute of Medical and Veterinary Science, Adelaide, Australia.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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