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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
18
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pubmed:dateCreated |
2000-12-26
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pubmed:abstractText |
Human rhinovirus (HRV) 3C protease was inactivated by a series of S-nitrosothiols. These compounds exhibited different inhibitory activities in a time- and concentration-dependent manner with second-order rate constants (kinact/K(I)) ranging from 131 to 5360 M(-1) min(-1). The inactive enzyme could be re-activated by DTT, GSH and ascorbate, which indicated the inactivation mechanism was through an S-transnitrosylation process.
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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/3C proteases,
http://linkedlifedata.com/resource/pubmed/chemical/Antiviral Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Ascorbic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Dithiothreitol,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Mercaptoethanol,
http://linkedlifedata.com/resource/pubmed/chemical/Nitroso Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/S-Nitrosothiols,
http://linkedlifedata.com/resource/pubmed/chemical/S-nitrosomercaptoethanol,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0960-894X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2097-100
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10999479-Antiviral Agents,
pubmed-meshheading:10999479-Ascorbic Acid,
pubmed-meshheading:10999479-Cysteine Endopeptidases,
pubmed-meshheading:10999479-Cysteine Proteinase Inhibitors,
pubmed-meshheading:10999479-Dithiothreitol,
pubmed-meshheading:10999479-Dose-Response Relationship, Drug,
pubmed-meshheading:10999479-Enzyme Activation,
pubmed-meshheading:10999479-Glutathione,
pubmed-meshheading:10999479-Humans,
pubmed-meshheading:10999479-Kinetics,
pubmed-meshheading:10999479-Mercaptoethanol,
pubmed-meshheading:10999479-Nitroso Compounds,
pubmed-meshheading:10999479-Rhinovirus,
pubmed-meshheading:10999479-S-Nitrosothiols,
pubmed-meshheading:10999479-Structure-Activity Relationship,
pubmed-meshheading:10999479-Viral Proteins
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pubmed:year |
2000
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pubmed:articleTitle |
S-nitrosothiols as novel, reversible inhibitors of human rhinovirus 3C protease.
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pubmed:affiliation |
Department of Chemistry, Wayne State University, Detroit, MI 48202, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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