Linked Life Data

15320723

Source:http://linkedlifedata.com/resource/pubmed/id/15320723

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2004-8-23
pubmed:abstractText
Matrix metalloproteinases (MMPs), of which at least 26 are known in humans, have been linked to a number of pathological conditions including tumor metastasis, inflammation, neurological and cardiovascular diseases. Inhibition of MMPs has been widely sought as a strategy in intervention of these disease processes. Whereas a large number of broad-spectrum MMP inhibitors have been developed over the past decade, these inhibitors have not met the promise and expectations in clinical trials. The broad-spectrum inhibition, which besides MMPs often targets other metalloproteinases, has been considered one of the potential problems that affects the therapeutic efficacy of MMPs inhibitors. Several MMP inhibitors that show selectivity for various MMPs have been reported in the past few years. This report describes the structural and inhibitory properties of these novel inhibitors, which hold considerable promise for effective targeting of these important enzymes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1568-0266
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1227-38
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Quest for selectivity in inhibition of matrix metalloproteinases.
pubmed:affiliation
Department of Chemistry and Biochemistry, 423 Nieuwland Science Center, University of Notre Dame, IN 46556, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review