Source:http://linkedlifedata.com/resource/pubmed/id/10322126
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1999-6-22
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pubmed:abstractText |
The substrate sites of enzymes are attractive targets for structure-based inhibitor design. Two difficulties hinder efforts to discover and elaborate new (nonsubstrate-like) inhibitors for these sites. First, novel inhibitors often bind at nonsubstrate sites. Second, a novel scaffold introduces chemistry that is frequently unfamiliar, making synthetic elaboration challenging.
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pubmed:grant | |
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 |
May
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pubmed:issn |
1074-5521
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pubmed:author | |
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 |
319-31
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10322126-Catalytic Domain,
pubmed-meshheading:10322126-Drug Design,
pubmed-meshheading:10322126-Enzyme Inhibitors,
pubmed-meshheading:10322126-Folic Acid Antagonists,
pubmed-meshheading:10322126-Lactobacillus casei,
pubmed-meshheading:10322126-Models, Molecular,
pubmed-meshheading:10322126-Structure-Activity Relationship,
pubmed-meshheading:10322126-Thymidylate Synthase
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pubmed:year |
1999
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pubmed:articleTitle |
Structure-based discovery and in-parallel optimization of novel competitive inhibitors of thymidylate synthase.
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pubmed:affiliation |
Department of Molecular Pharmacology and Biological Chemistry, Northwestern University, Chicago, IL 60611-3008, 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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