Source:http://linkedlifedata.com/resource/pubmed/id/15686898
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2005-2-2
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pubmed:abstractText |
Docking experiments using a number of published crystal structures of HMG-CoA reductase with the potent hypocholesterolemic agent alpha-asarone are described. The results indicate that alpha-asarone binds in the enzyme's active site. The methoxy groups play a key role in the binding and probably also in its biological activity, as shown by extensive SAR studies reported for analogues of alpha-asarone. The docking results will be valuable for the structure-based design of novel hypolipidemic agents.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0960-894X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
989-94
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:15686898-Anisoles,
pubmed-meshheading:15686898-Binding Sites,
pubmed-meshheading:15686898-Catalytic Domain,
pubmed-meshheading:15686898-Computer Simulation,
pubmed-meshheading:15686898-Humans,
pubmed-meshheading:15686898-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:15686898-Hydroxymethylglutaryl CoA Reductases,
pubmed-meshheading:15686898-Hydroxymethylglutaryl-CoA Reductase Inhibitors,
pubmed-meshheading:15686898-Models, Molecular,
pubmed-meshheading:15686898-Protein Binding,
pubmed-meshheading:15686898-Structure-Activity Relationship
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pubmed:year |
2005
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pubmed:articleTitle |
Molecular docking of the highly hypolipidemic agent alpha-asarone with the catalytic portion of HMG-CoA reductase.
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pubmed:affiliation |
Departamento de Farmacia, Facultad de Química, Universidad Nacional Autónoma de México, Circuito Exterior, Ciudad Universitaria, 04510 México, D.F., Mexico.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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