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pubmed-article:15615530pubmed:dateCreated2004-12-23lld:pubmed
pubmed-article:15615530pubmed:abstractTextWe recently described a novel series of CA(1)A(2)X peptidomimetics as farnesyl transferase inhibitors (FTIs). These compounds possess an N-(4-piperidinyl)benzamide scaffold mimicking A(1)A(2) residue. Extensive exploration of structure--activity relationships revealed that replacement of cysteine by substituted benzylimidazoles provided nanomolar FTIs with in vitro activities (18e, IC(50) = 4.60 nM on isolated enzyme, EC(50) = 20.0 nM for growth inhibition on a tumor cell line). The molecular docking of 18e and 19e in the active site of the enzyme provided details of key interactions with the protein and showed that the methionine or phenylalanine residue fits into the aryl binding site.lld:pubmed
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pubmed-article:15615530pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:15615530pubmed:year2004lld:pubmed
pubmed-article:15615530pubmed:articleTitlePotent and selective farnesyl transferase inhibitors.lld:pubmed
pubmed-article:15615530pubmed:affiliationInstitut de Chimie Pharmaceutique Albert Lespagnol, EA 2692, Université de Lille 2, BP 83 rue du Professeur Laguesse, 59006 Lille, France.lld:pubmed
pubmed-article:15615530pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15615530pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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