title: A switch in enantiomer preference between mitochondrial F1F0-ATPase chemotypes.
abstract: The preferred absolute configuration of two series of F(1)F(0)-ATP synthase inhibitors was determined. Although the configuration of the active enantiomer in each series is different, each series presents the same 'triaryl' pharmacophore to the enzyme binding site.
authors.affiliation: Department of Discovery Chemistry, Bristol-Myers Squibb, Pharmaceutical Research Institute, Princeton, NJ 08543-4000, USA.
authors.forename: Sharon N
authors.initials: SN
authors.lastname: Bisaha
authors.forename: Mary F
authors.initials: MF
authors.lastname: Malley
authors.forename: Andrew
authors.initials: A
authors.lastname: Pudzianowski
authors.forename: Hossain
authors.initials: H
authors.lastname: Monshizadegan
authors.forename: Paulina
authors.initials: P
authors.lastname: Wang
authors.forename: Cort S
authors.initials: CS
authors.lastname: Madsen
authors.forename: Jack Z
authors.initials: JZ
authors.lastname: Gougoutas
authors.forename: Philip D
authors.initials: PD
authors.lastname: Stein
mesh_terms: D001665:Binding Sites; D008928:Mitochondria / Q000201:enzymology*; D008958:Models, Molecular; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D013237:Stereoisomerism
chemical_list: D006180:Proton-Translocating ATPases