Source:http://linkedlifedata.com/resource/pubmed/id/10411481
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
14
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pubmed:dateCreated |
1999-8-2
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pubmed:abstractText |
Several phosphinic pseudo-tripeptides of general formula R-XaaPsi(PO(2)-CH(2))Xaa'-Yaa'-NH(2) were synthesized and evaluated for their in vitro activities to inhibit stromelysin-3, gelatinases A and B, membrane type-1 matrix metalloproteinase, collagenases 1 and 2, and matrilysin. With the exception of collagenase-1 and matrilysin, phosphinic pseudo-tripeptides behave as highly potent inhibitors of matrix metalloproteinases, provided they contain in P(1)' position an unusual long aryl-alkyl substituent. Study of structure-activity relationships regarding the influence of the R and Xaa' substituents in this series may contribute to the design of inhibitors able to block only a few members of the matrix metalloproteinase family.
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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 |
Jul
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pubmed:issn |
0022-2623
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pubmed:author |
pubmed-author:BassetPP,
pubmed-author:BeanAA,
pubmed-author:CuniassePP,
pubmed-author:DiveVV,
pubmed-author:GeorgiadisDD,
pubmed-author:KannanRR,
pubmed-author:KnäuperVV,
pubmed-author:Lucet-LevannierKK,
pubmed-author:MuchaAA,
pubmed-author:MurphyGG,
pubmed-author:SinL DLD,
pubmed-author:VassiliouSS,
pubmed-author:YiotakisAA
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
42
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2610-20
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10411481-Kinetics,
pubmed-meshheading:10411481-Magnetic Resonance Spectroscopy,
pubmed-meshheading:10411481-Metalloendopeptidases,
pubmed-meshheading:10411481-Oligopeptides,
pubmed-meshheading:10411481-Phosphines,
pubmed-meshheading:10411481-Protease Inhibitors,
pubmed-meshheading:10411481-Structure-Activity Relationship
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pubmed:year |
1999
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pubmed:articleTitle |
Phosphinic pseudo-tripeptides as potent inhibitors of matrix metalloproteinases: a structure-activity study.
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pubmed:affiliation |
CEA, Département d'Ingénierie et d'Etudes des Protéines, 91191 Gif/Yvette Cedex, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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