Linked Life Data

12161133

Source:http://linkedlifedata.com/resource/pubmed/id/12161133

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2002-8-5
pubmed:abstractText
The design of conformationally restricted eight-membered ring diketones as transition state mimics of the mechanism of action of cyclotheonamides on serine proteases is described. Two target compounds are prepared from mutilin, derived from the natural product pleuromutilin. Compound 3 shows significant inhibition of plasmin and urokinase in enzyme rate assays, but an analogue 4 in which the amide moiety has been omitted does not. An X-ray crystal structure of the diketone 3 confirms the conformational predictions made by molecular modelling.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0960-894X
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2359-62
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Design and synthesis of conformationally restricted eight-Membered ring diketones as potential serine protease inhibitors.
pubmed:affiliation
GlaxoSmithKline Pharmaceuticals, New Frontiers Science Park North, Third Avenue, The Pinnacles, Harlow, Essex, UK.
pubmed:publicationType
Journal Article