title: Non-thiol farnesyltransferase inhibitors: utilization of the far aryl binding site by arylthienylacryloylaminobenzophenones.
abstract: We recently described two novel aryl binding sites of farnesyltransferase. The 4- and 5-arylsubstituted thienylacryloyl moieties turned out as appropriate substituents for our benzophenone-based AAX-peptidomimetic capable for occupying the far aryl binding site.
authors.affiliation: Institut für Pharmazeutische Chemie, Philipps-Universität Marburg, Marburg, Germany.
authors.forename: Andreas
authors.initials: A
authors.lastname: Mitsch
authors.forename: Mirko
authors.initials: M
authors.lastname: Altenkämper
authors.forename: Isabel
authors.initials: I
authors.lastname: Sattler
authors.forename: Martin
authors.initials: M
authors.lastname: Schlitzer
mesh_terms: D000178:Acrylamides / Q000737:chemistry*; D019883:Alkyl and Aryl Transferases / Q000037:antagonists & inhibitors* / Q000737:chemistry*; D001577:Benzophenones / Q000737:chemistry*; D001665:Binding Sites; D051231:Farnesyltranstransferase; D013329:Structure-Activity Relationship; D013876:Thiophenes / Q000737:chemistry*
chemical_list: D000178:Acrylamides; D001577:Benzophenones; D013876:Thiophenes; D019883:Alkyl and Aryl Transferases; D051231:Farnesyltranstransferase