| pubmed-article:10578171 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10578171 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:10578171 | lifeskim:mentions | umls-concept:C0010656 | lld:lifeskim |
| pubmed-article:10578171 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:10578171 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:10578171 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:10578171 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:10578171 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:10578171 | pubmed:dateCreated | 2000-2-29 | lld:pubmed |
| pubmed-article:10578171 | pubmed:abstractText | Caspases play an essential role during apoptotic cell death. These enzymes define a new class of cysteine proteases and comprise a multi-gene family with more than a dozen distinct mammalian family members. The discrete and highly limited subset of cellular polypeptides that are cleaved by these proteases is sufficient to account for the majority of cellular and morphological events that occur during cell death. In some cases, caspases also play a contributory role in escalating the propensity for apoptosis, and in doing so may exacerbate disease pathogenesis. | lld:pubmed |
| pubmed-article:10578171 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10578171 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578171 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10578171 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578171 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578171 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10578171 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:10578171 | pubmed:issn | 1350-9047 | lld:pubmed |
| pubmed-article:10578171 | pubmed:author | pubmed-author:NicholsonD... | lld:pubmed |
| pubmed-article:10578171 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10578171 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:10578171 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10578171 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10578171 | pubmed:pagination | 1028-42 | lld:pubmed |
| pubmed-article:10578171 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
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| pubmed-article:10578171 | pubmed:meshHeading | pubmed-meshheading:10578171... | lld:pubmed |
| pubmed-article:10578171 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10578171 | pubmed:articleTitle | Caspase structure, proteolytic substrates, and function during apoptotic cell death. | lld:pubmed |
| pubmed-article:10578171 | pubmed:affiliation | Merck Frosst Centre for Therapeutic Research, Merck Frosst Canada & Co., PO Box 1005, Pointe Claire-Dorval, Quebec, Canada, H9R 4P8. donald_nicholson@merck.com | lld:pubmed |
| pubmed-article:10578171 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10578171 | pubmed:publicationType | Review | lld:pubmed |
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