Identification of Residues in the Drug Translocation Pathway of the Human Multidrug Resistance P-glycoprotein by Arginine Mutagenesis

Data-driven homology modelling of P-glycoprotein in the ATP-bound state indicates flexibility of the transmembrane domains

(2009) Thomas Stockner et al.   FEBS Journal

Rhodamine Inhibitors of P-Glycoprotein: An Amide/Thioamide “Switch” for ATPase Activity

(2009) Michael K. Gannon et al.   JOURNAL OF MEDICINAL CHEMISTRY

Structure of a multidrug transporter

(2009) Michael M Gottesman et al.   NATURE BIOTECHNOLOGY

Structure of P-Glycoprotein Reveals a Molecular Basis for Poly-Specific Drug Binding

(2009) S. G. Aller et al.   SCIENCE

Molecular models of human P-glycoprotein in two different catalytic states

(2009) Jean-Paul Becker et al.   BMC STRUCTURAL BIOLOGY

Mutational analysis of ABC proteins

(2008) Tip W. Loo et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

Identification of Putative Binding Sites of P-glycoprotein Based on its Homology Model

(2008) Christoph Globisch et al.   ChemMedChem

Arginines in the First Transmembrane Segment Promote Maturation of a P-glycoprotein Processing Mutant by Hydrogen Bond Interactions with Tyrosines in Transmembrane Segment 11

(2008) Tip W. Loo et al.   JOURNAL OF BIOLOGICAL CHEMISTRY