title: Non-thiol farnesyltransferase inhibitors: utilization of the far aryl binding site by 5-cinnamoylaminobenzophenones.
abstract: We recently described two novel aryl binding sites of farnesyltransferase. In this study, the cinnamoyl residue was designed as an appropriate substituent for our benzophenone-based AAX-peptidomimetic compound capable of occupying the far aryl binding site.
authors.affiliation: Institut für Pharmazeutische Chemie, Philipps-Universität Marburg, Germany.
authors.forename: Andreas
authors.initials: A
authors.lastname: Mitsch
authors.forename: Pia
authors.initials: P
authors.lastname: Wissner
authors.forename: Markus
authors.initials: M
authors.lastname: Böhm
authors.forename: Katrin
authors.initials: K
authors.lastname: Silber
authors.forename: Gerhard
authors.initials: G
authors.lastname: Klebe
authors.forename: Isabel
authors.initials: I
authors.lastname: Sattler
authors.forename: Martin
authors.initials: M
authors.lastname: Schlitzer
mesh_terms: D019883:Alkyl and Aryl Transferases / Q000037:antagonists & inhibitors*; D001577:Benzophenones / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D001665:Binding Sites; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D051231:Farnesyltranstransferase; D008958:Models, Molecular; D018716:Molecular Mimicry; D015394:Molecular Structure; D013329:Structure-Activity Relationship; D015003:Yeasts / Q000201:enzymology
chemical_list: D001577:Benzophenones; D004791:Enzyme Inhibitors; D019883:Alkyl and Aryl Transferases; D051231:Farnesyltranstransferase