Linked Life Data

10960188

Source:http://linkedlifedata.com/resource/pubmed/id/10960188

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7-8
pubmed:dateCreated
2000-10-18
pubmed:abstractText
Replacement of the thiol in a benzophenone-based CAAX-peptidomimetic farnesyltransferase inhibitor by a carboxylic acid moiety resulted in a marked drop in inhibitory potency. Transformation of these carboxylic acid derivatives into bisubstrate analogues by addition of a lipophilic alkyl chain, which should be able to occupy considerable portions of the farnesyl binding region in the farnesyltransferase's active site, resulted in a regain of the inhibitory activity. These bisubstrate analogues represent new lead structures for non-thiol farnesyltransferase inhibitors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0223-5234
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
721-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Non-thiol farnesyltransferase inhibitors: the concept of benzophenone-based bisubstrate analogue farnesyltransferase inhibitors.
pubmed:affiliation
Institut für Pharmazeutische Chemie, Philipps-Universität Marburg, Marbacher Weg 6, D-35032, Marburg, Germany. schlitze@mailer.uni-marburg.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't