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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2000-1-31
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pubmed:abstractText |
The proteasome is a large multicatalytic protease complex (700 kDa) involved in a number of highly regulated processes. It has three major catalytic activities: a chymotrypsin-like activity, a trypsin-like activity and a post-glutamyl peptide hydrolyzing (PGPH) activity. To be useful as molecular probes, which could help dissect the cellular functions of the proteasome, inhibitors should be specific for the proteasome, active in vivo and selectively block only one of the three catalytic activities. To date, few inhibitors fulfill these requirements so we set out to make novel proteasome inhibitors that incorporate these characteristics.
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pubmed:grant |
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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/Chymotrypsin,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Epoxy Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamates,
http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Irritants,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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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 |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
811-22
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pubmed:dateRevised |
2008-11-20
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pubmed:meshHeading |
pubmed-meshheading:10574782-Animals,
pubmed-meshheading:10574782-Aorta,
pubmed-meshheading:10574782-Cattle,
pubmed-meshheading:10574782-Cell Division,
pubmed-meshheading:10574782-Cells, Cultured,
pubmed-meshheading:10574782-Chymotrypsin,
pubmed-meshheading:10574782-Cysteine Endopeptidases,
pubmed-meshheading:10574782-Cysteine Proteinase Inhibitors,
pubmed-meshheading:10574782-Drug Design,
pubmed-meshheading:10574782-Endothelium, Vascular,
pubmed-meshheading:10574782-Epoxy Compounds,
pubmed-meshheading:10574782-Glutamates,
pubmed-meshheading:10574782-Indicators and Reagents,
pubmed-meshheading:10574782-Irritants,
pubmed-meshheading:10574782-Kinetics,
pubmed-meshheading:10574782-Macromolecular Substances,
pubmed-meshheading:10574782-Mice,
pubmed-meshheading:10574782-Molecular Conformation,
pubmed-meshheading:10574782-Multienzyme Complexes,
pubmed-meshheading:10574782-Peptides,
pubmed-meshheading:10574782-Proteasome Endopeptidase Complex,
pubmed-meshheading:10574782-Trypsin
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pubmed:year |
1999
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pubmed:articleTitle |
Towards subunit-specific proteasome inhibitors: synthesis and evaluation of peptide alpha',beta'-epoxyketones.
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pubmed:affiliation |
Departments of Molecular, Cellular and Developmental Biology, Organic Chemistry, Yale University, New Haven, CT 06520-8103, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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