Source:http://linkedlifedata.com/resource/pubmed/id/15157443
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7
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| pubmed:dateCreated |
2004-5-25
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| pubmed:abstractText |
An expanding family of cysteine proteases, of which interleukin-1beta-converting enzyme (ICE) is the prototype, has been shown to play a key role in mammalian cell apoptosis. ICE is both a structural and functional homologue of the nematode 'death gene' ced-3. Here, Moira Whyte discusses how functional characterization of these ICE-like proteases and identification of their substrates is helping to elucidate the biochemical processes underlying the stereotyped morphology of apoptosis and to identify potential targets for therapy.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
0962-8924
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
6
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
245-8
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| pubmed:year |
1996
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| pubmed:articleTitle |
ICE/CED-3 proteasesin apoptosis.
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| pubmed:affiliation |
Moira Whyte is at the Dept of Medicine and Pharmacology (Section of Respiratory Medicine), University of Sheffield, Royal Hallamshire Hospital, Sheffield, UK S10 2JF.
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| pubmed:publicationType |
Journal Article
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