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The multidrug transporter Pdr5 on the 25th anniversary of its discovery: an important model for the study of asymmetric ABC transporters

Biochemical journal, 2015-05, Vol.467 (3), p.353-363

2015

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Pdr5: A Master of Asymmetry

Drug resistance updates, 2023-11, Vol.71, p.101010-101010, Article 101010

2023

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The Deviant ATP-binding Site of the Multidrug Efflux Pump Pdr5 Plays an Active Role in the Transport Cycle

The Journal of biological chemistry, 2013-10, Vol.288 (42), p.30420-30431

2013

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The Transmission Interface of the Saccharomyces cerevisiae Multidrug Transporter Pdr5: Val-656 Located in Intracellular Loop 2 Plays a Major Role in Drug Resistance

Antimicrobial Agents and Chemotherapy, 2013-02, Vol.57 (2), p.1025-1034

2013

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Nonsynonymous Mutations in Linker-2 of the Pdr5 Multidrug Transporter Identify a New RNA Stability Element

G3 : genes - genomes - genetics, 2020-01, Vol.10 (1), p.357-369

2020

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How fungal multidrug transporters mediate hyper resistance through DNA amplification and mutation

Molecular microbiology, 2022-07, Vol.118 (1-2), p.3-15

2022

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Studies with Novel Pdr5p Substrates Demonstrate a Strong Size Dependence for Xenobiotic Efflux

The Journal of biological chemistry, 2003-02, Vol.278 (8), p.5963-5969

2003

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Expression of an ATP-binding cassette transporter-encoding gene (YOR1) is required for oligomycin resistance in Saccharomyces cerevisiae

Molecular and Cellular Biology, 1995-12, Vol.15 (12), p.6875-6883

1995

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Second-site suppressor mutations reveal connection between the drug-binding pocket and nucleotide-binding domain 1 of human P-glycoprotein (ABCB1)

Drug resistance updates, 2023-11, Vol.71, p.101009-101009, Article 101009

2023

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Residues forming the gating regions of asymmetric multidrug transporter Pdr5 also play roles in conformational switching and protein folding

The Journal of biological chemistry, 2022-12, Vol.298 (12), p.102689-102689, Article 102689

2022

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Correction: Residues forming the gating regions of asymmetric multidrug transporter Pdr5 also play roles in conformational switching and protein folding

The Journal of biological chemistry, 2023-04, Vol.299 (4), p.104666-104666, Article 104666

2023

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Robust, pleiotropic drug resistance 5 (Pdr5)-mediated multidrug resistance is vigorously maintained in Saccharomyces cerevisiae cells during glucose and nitrogen limitation

FEMS yeast research, 2018-06, Vol.18 (4), p.1

2018

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An A666G mutation in transmembrane helix 5 of the yeast multidrug transporter Pdr5 increases drug efflux by enhancing cooperativity between transport sites

Molecular microbiology, 2019-10, Vol.112 (4), p.1131-1144

2019

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Mutations Define Cross-talk between the N-terminal Nucleotide-binding Domain and Transmembrane Helix-2 of the Yeast Multidrug Transporter Pdr5

The Journal of biological chemistry, 2008-12, Vol.283 (50), p.35010-35022

2008

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Robust, pleiotropic drug resistance 5

FEMS yeast research, 2018-06, Vol.18 (4), p.1

2018

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Evidence for a molecular diode-based mechanism in a multispecific ATP-binding cassette (ABC) exporter: SER-1368 as a gatekeeping residue in the yeast multidrug transporter Pdr5

The Journal of biological chemistry, 2014-09, Vol.289 (38), p.26597-26606

2014

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Evidence for a Molecular Diode-based Mechanism in a Multispecific ATP-binding cassette (ABC) Exporter

The Journal of biological chemistry, 2014-09, Vol.289 (38), p.26597-26606

2014

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The yeast Pdr5p multidrug transporter: How does it recognize so many substrates?

Biochemical and biophysical research communications, 2007-04, Vol.356 (1), p.1-5

2007

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The Signaling Interface of the Yeast Multidrug Transporter Pdr5 Adopts a Cis Conformation, and There Are Functional Overlap and Equivalence of the Deviant and Canonical Q-Loop Residues

Biochemistry (Easton), 2010-06, Vol.49 (21), p.4440-4449

2010

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Mutations Define Cross-talk between the N-terminal Nucleotide-binding Domain and Transmembrane Helix-2 of the Yeast Multidrug Transporter Pdr5: POSSIBLE CONSERVATION OF A SIGNALING INTERFACE FOR COUPLING ATP HYDROLYSIS TO DRUG TRANSPORT

The Journal of biological chemistry, 2008-12, Vol.283 (50), p.35010-35022

2008

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Cuomarin‐6‐sulfonamides May be Useful Photoaffinity‐labeling Reagents for Analyzing the Kinetics of Drug Transport and ATP Hydrolysis in ABC Multidrug Transporters

The FASEB journal, 2011-04, Vol.25 (S1), p.932.7-932.7

2011

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Complete Inhibition of the Pdr5p Multidrug Efflux Pump ATPase Activity by Its Transport Substrate Clotrimazole Suggests that GTP as Well as ATP May Be Used as an Energy Source

Biochemistry (Easton), 2007-11, Vol.46 (45), p.13109-13119

2007

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Chemical Specificity of the PDR5Multidrug Resistance Gene Product of Saccharomyces cerevisiae Based on Studies with Tri-n-Alkyltin Chlorides

Antimicrobial Agents and Chemotherapy, 2000-01, Vol.44 (1), p.134-138

2000

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Interaction of the yeast pleiotropic drug resistance genes PDR1 and PDR5

Current genetics, 1992-05, Vol.21 (6), p.431-436

1992

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The Role of Hydrogen Bond Acceptor Groups in the Interaction of Substrates with Pdr5p, a Major Yeast Drug Transporter

Biochemistry (Easton), 2005-07, Vol.44 (28), p.9703-9713

2005

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The multidrug transporter Pdr5 on the 25th anniversary of its discovery: an important model for the study of asymmetric ABC transporters

Pdr5: A Master of Asymmetry

The Deviant ATP-binding Site of the Multidrug Efflux Pump Pdr5 Plays an Active Role in the Transport Cycle

The Transmission Interface of the Saccharomyces cerevisiae Multidrug Transporter Pdr5: Val-656 Located in Intracellular Loop 2 Plays a Major Role in Drug Resistance

Nonsynonymous Mutations in Linker-2 of the Pdr5 Multidrug Transporter Identify a New RNA Stability Element

How fungal multidrug transporters mediate hyper resistance through DNA amplification and mutation

Studies with Novel Pdr5p Substrates Demonstrate a Strong Size Dependence for Xenobiotic Efflux

Expression of an ATP-binding cassette transporter-encoding gene (YOR1) is required for oligomycin resistance in Saccharomyces cerevisiae

Second-site suppressor mutations reveal connection between the drug-binding pocket and nucleotide-binding domain 1 of human P-glycoprotein (ABCB1)

Residues forming the gating regions of asymmetric multidrug transporter Pdr5 also play roles in conformational switching and protein folding

Correction: Residues forming the gating regions of asymmetric multidrug transporter Pdr5 also play roles in conformational switching and protein folding

Robust, pleiotropic drug resistance 5 (Pdr5)-mediated multidrug resistance is vigorously maintained in Saccharomyces cerevisiae cells during glucose and nitrogen limitation

An A666G mutation in transmembrane helix 5 of the yeast multidrug transporter Pdr5 increases drug efflux by enhancing cooperativity between transport sites

Mutations Define Cross-talk between the N-terminal Nucleotide-binding Domain and Transmembrane Helix-2 of the Yeast Multidrug Transporter Pdr5

Robust, pleiotropic drug resistance 5

Evidence for a molecular diode-based mechanism in a multispecific ATP-binding cassette (ABC) exporter: SER-1368 as a gatekeeping residue in the yeast multidrug transporter Pdr5

Evidence for a Molecular Diode-based Mechanism in a Multispecific ATP-binding cassette (ABC) Exporter

The yeast Pdr5p multidrug transporter: How does it recognize so many substrates?

The Signaling Interface of the Yeast Multidrug Transporter Pdr5 Adopts a Cis Conformation, and There Are Functional Overlap and Equivalence of the Deviant and Canonical Q-Loop Residues

Mutations Define Cross-talk between the N-terminal Nucleotide-binding Domain and Transmembrane Helix-2 of the Yeast Multidrug Transporter Pdr5: POSSIBLE CONSERVATION OF A SIGNALING INTERFACE FOR COUPLING ATP HYDROLYSIS TO DRUG TRANSPORT

Cuomarin‐6‐sulfonamides May be Useful Photoaffinity‐labeling Reagents for Analyzing the Kinetics of Drug Transport and ATP Hydrolysis in ABC Multidrug Transporters

Complete Inhibition of the Pdr5p Multidrug Efflux Pump ATPase Activity by Its Transport Substrate Clotrimazole Suggests that GTP as Well as ATP May Be Used as an Energy Source

Chemical Specificity of the PDR5Multidrug Resistance Gene Product of Saccharomyces cerevisiae Based on Studies with Tri-n-Alkyltin Chlorides

Interaction of the yeast pleiotropic drug resistance genes PDR1 and PDR5

The Role of Hydrogen Bond Acceptor Groups in the Interaction of Substrates with Pdr5p, a Major Yeast Drug Transporter

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