Associated Papers
Mapping the Role of P-gp in Multidrug Resistance: Insights from Recent Structural Studies.
Tia ST et al.
International Journal of Molecular Sciences, 2025
Nucleotide asymmetry and flexible linker dynamics modulate drug efflux cycle of P-glycoprotein, A computational study.
Han SB et al.
Computational and Structural Biotechnology Journal, 2025
How Cryo-EM Has Expanded Our Understanding of Membrane Transporters.
Baril SA et al.
Drug Metabolism and Disposition: the Biological Fate of Chemicals, 2023
Conformational changes in the nucleotide-binding domains of P-glycoprotein induced by ATP hydrolysis.
Dehghani-Ghahnaviyeh S et al.
Febs Letters, 2021
Does the ATP-bound EQ mutant reflect the pre- or post-ATP hydrolysis state in the catalytic cycle of human P-glycoprotein (ABCB1)?
Lusvarghi S et al.
Febs Letters, 2021
Reversing the direction of drug transport mediated by the human multidrug transporter P-glycoprotein.
Sajid A et al.
Proceedings of the National Academy of Sciences of the United States of America, 2020
Human ABCB1 with an ABCB11-like degenerate nucleotide binding site maintains transport activity by avoiding nucleotide occlusion.
Goda K et al.
Plos Genetics, 2020
In vivo FRET analyses reveal a role of ATP hydrolysis-associated conformational changes in human P-glycoprotein.
Futamata R et al.
The Journal of Biological Chemistry, 2020
Active transport of rhodamine 123 by the human multidrug transporter P-glycoprotein involves two independent outer gates.
Nasim F et al.
Pharmacology Research & Perspectives, 2020
Multidrug transporters: recent insights from cryo-electron microscopy-derived atomic structures and animal models.
Lusvarghi S et al.
F1000research, 2020
ATP-dependent thermostabilization of human P-glycoprotein (ABCB1) is blocked by modulators.
Lusvarghi S et al.
The Biochemical Journal, 2019
Dissecting the Forces that Dominate Dimerization of the Nucleotide Binding Domains of ABCB1.
Szöllősi D et al.
Biophysical Journal, 2018
A short cross-linker activates human P-glycoprotein missing a catalytic carboxylate.
Loo TW et al.
Biochemical Pharmacology, 2017
Cryo-EM Analysis of the Conformational Landscape of Human P-glycoprotein (ABCB1) During its Catalytic Cycle.
Frank GA et al.
Molecular Pharmacology, 2016
Human-Mouse Chimeras with Normal Expression and Function Reveal That Major Domain Swapping Is Tolerated by P-Glycoprotein (ABCB1).
Pluchino KM et al.
Biochemistry, 2016
Drug-protein hydrogen bonds govern the inhibition of the ATP hydrolysis of the multidrug transporter P-glycoprotein.
Chufan EE et al.
Biochemical Pharmacology, 2016
The Q loops of the human multidrug resistance transporter ABCB1 are necessary to couple drug binding to the ATP catalytic cycle.
Zolnerciks JK et al.
Faseb Journal : Official Publication of the Federation of American Societies for Experimental Biology, 2014
Cysteines introduced into extracellular loops 1 and 4 of human P-glycoprotein that are close only in the open conformation spontaneously form a disulfide bond that inhibits drug efflux and ATPase activity.
Loo TW et al.
The Journal of Biological Chemistry, 2014
Elucidation of the structural basis of interaction of the BCR-ABL kinase inhibitor, nilotinib (Tasigna) with the human ABC drug transporter P-glycoprotein.
Shukla S et al.
Leukemia, 2014
Mutations in intracellular loops 1 and 3 lead to misfolding of human P-glycoprotein (ABCB1) that can be rescued by cyclosporine A, which reduces its association with chaperone Hsp70.
Kapoor K et al.
The Journal of Biological Chemistry, 2013
Multiple transport-active binding sites are available for a single substrate on human P-glycoprotein (ABCB1).
Chufan EE et al.
Plos One, 2013
Corrector-mediated rescue of misprocessed CFTR mutants can be reduced by the P-glycoprotein drug pump.
Loo TW et al.
Biochemical Pharmacology, 2012
Catalytic cycle of ATP hydrolysis by P-glycoprotein: evidence for formation of the E.S reaction intermediate with ATP-gamma-S, a nonhydrolyzable analogue of ATP.
Sauna ZE et al.
Biochemistry, 2007
Evidence for a Sav1866-like architecture for the human multidrug transporter P-glycoprotein.
Zolnerciks JK et al.
Faseb Journal : Official Publication of the Federation of American Societies for Experimental Biology, 2007
Genomics and the mechanism of P-glycoprotein (ABCB1).
Sauna ZE et al.
Journal of Bioenergetics and Biomembranes, 2007
Nucleotide binding, ATP hydrolysis, and mutation of the catalytic carboxylates of human P-glycoprotein cause distinct conformational changes in the transmembrane segments.
Loo TW et al.
Biochemistry, 2007
Combined mutation of catalytic glutamate residues in the two nucleotide binding domains of P-glycoprotein generates a conformation that binds ATP and ADP tightly.
Tombline G et al.
The Journal of Biological Chemistry, 2004
Analysis of catalytic carboxylate mutants E552Q and E1197Q suggests asymmetric ATP hydrolysis by the two nucleotide-binding domains of P-glycoprotein.
Carrier I et al.
Biochemistry, 2003
Importance of the conserved Walker B glutamate residues, 556 and 1201, for the completion of the catalytic cycle of ATP hydrolysis by human P-glycoprotein (ABCB1).
Sauna ZE et al.
Biochemistry, 2002