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rdf:type |
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lifeskim:mentions |
umls-concept:C0004015,
umls-concept:C0007587,
umls-concept:C0037791,
umls-concept:C0061878,
umls-concept:C0086418,
umls-concept:C0127400,
umls-concept:C0291573,
umls-concept:C0450363,
umls-concept:C0596311,
umls-concept:C0678594,
umls-concept:C1330957,
umls-concept:C1363844,
umls-concept:C1554080,
umls-concept:C1706198,
umls-concept:C1707455
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pubmed:issue |
4
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pubmed:dateCreated |
2001-4-30
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pubmed:abstractText |
Granzyme B, one of the most abundant granzymes in cytotoxic T-lymphocyte (CTL) granules, and members of the caspase (cysteine aspartyl proteinases) family have a unique cleavage specificity for aspartic acid in P1 and play critical roles in the biochemical events that culminate in cell death.
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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/Aspartic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Casp3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Casp3 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/GZMB protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Granzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Gzmb protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Gzmb protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1074-5521
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
357-68
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11325591-Amino Acid Sequence,
pubmed-meshheading:11325591-Animals,
pubmed-meshheading:11325591-Apoptosis,
pubmed-meshheading:11325591-Aspartic Acid,
pubmed-meshheading:11325591-Binding Sites,
pubmed-meshheading:11325591-Caspase 3,
pubmed-meshheading:11325591-Caspases,
pubmed-meshheading:11325591-Computational Biology,
pubmed-meshheading:11325591-Crystallography, X-Ray,
pubmed-meshheading:11325591-Enzyme Inhibitors,
pubmed-meshheading:11325591-Granzymes,
pubmed-meshheading:11325591-Humans,
pubmed-meshheading:11325591-Hydrogen Bonding,
pubmed-meshheading:11325591-Mice,
pubmed-meshheading:11325591-Models, Molecular,
pubmed-meshheading:11325591-Molecular Sequence Data,
pubmed-meshheading:11325591-Protein Structure, Secondary,
pubmed-meshheading:11325591-Protein Structure, Tertiary,
pubmed-meshheading:11325591-Rats,
pubmed-meshheading:11325591-Sequence Alignment,
pubmed-meshheading:11325591-Sequence Homology, Amino Acid,
pubmed-meshheading:11325591-Serine Endopeptidases,
pubmed-meshheading:11325591-Static Electricity,
pubmed-meshheading:11325591-Substrate Specificity
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pubmed:year |
2001
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pubmed:articleTitle |
The three-dimensional structure of human granzyme B compared to caspase-3, key mediators of cell death with cleavage specificity for aspartic acid in P1.
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pubmed:affiliation |
Department of Endocrinology and Chemical Biology, Merck Research Laboratories, Rahway, NJ 07065-0900, USA. rotonda@merck.com
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, Non-P.H.S.
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