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Structural modeling of an outer membrane electron conduit from a metal-reducing bacterium suggests electron transfer via periplasmic redox partners

The Journal of biological chemistry, 2018-05, Vol.293 (21), p.8103-8112

2018

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Mapping the Binding Site of the Inhibitor Tariquidar That Stabilizes the First Transmembrane Domain of P-glycoprotein

The Journal of biological chemistry, 2015-12, Vol.290 (49), p.29389-29401

2015

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Human P-glycoprotein Contains a Greasy Ball-and-Socket Joint at the Second Transmission Interface

The Journal of biological chemistry, 2013-07, Vol.288 (28), p.20326-20333

2013

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Location of the Rhodamine-binding Site in the Human Multidrug Resistance P-glycoprotein

The Journal of biological chemistry, 2002-11, Vol.277 (46), p.44332-44338

2002

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Simultaneous Binding of Two Different Drugs in the Binding Pocket of the Human Multidrug Resistance P-glycoprotein

The Journal of biological chemistry, 2003-10, Vol.278 (41), p.39706-39710

2003

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

The Journal of biological chemistry, 2009-09, Vol.284 (36), p.24074-24087

2009

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The Transmission Interfaces Contribute Asymmetrically to the Assembly and Activity of Human P-glycoprotein

The Journal of biological chemistry, 2015-07, Vol.290 (27), p.16954-16963

2015

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Correctors Promote Maturation of Cystic Fibrosis Transmembrane Conductance Regulator (CFTR)-processing Mutants by Binding to the Protein

The Journal of biological chemistry, 2007-11, Vol.282 (46), p.33247-33251

2007

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Processing Mutations Disrupt Interactions between the Nucleotide Binding and Transmembrane Domains of P-glycoprotein and the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR)

The Journal of biological chemistry, 2008-10, Vol.283 (42), p.28190-28197

2008

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The "LSGGQ" motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing walker A sequence

The Journal of biological chemistry, 2002-11, Vol.277 (44), p.41303-41306

2002

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Determining the Dimensions of the Drug-binding Domain of Human P-glycoprotein Using Thiol Cross-linking Compounds as Molecular Rulers

The Journal of biological chemistry, 2001-10, Vol.276 (40), p.36877-36880

2001

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Defining the Drug-binding Site in the Human Multidrug Resistance P-glycoprotein Using a Methanethiosulfonate Analog of Verapamil, MTS-verapamil

The Journal of biological chemistry, 2001-05, Vol.276 (18), p.14972-14979

2001

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Identification of the Distance between the Homologous Halves of P-glycoprotein That Triggers the High/Low ATPase Activity Switch

The Journal of biological chemistry, 2014-03, Vol.289 (12), p.8484-8492

2014

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Locking Intracellular Helices 2 and 3 Together Inactivates Human P-glycoprotein

The Journal of biological chemistry, 2014-01, Vol.289 (1), p.229-236

2014

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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

The Journal of biological chemistry, 2014-09, Vol.289 (36), p.24749-24758

2014

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The ATPase Activity of the P-glycoprotein Drug Pump Is Highly Activated When the N-terminal and Central Regions of the Nucleotide-binding Domains Are Linked Closely Together

The Journal of biological chemistry, 2012-08, Vol.287 (32), p.26806-26816

2012

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Drug Binding in Human P-glycoprotein Causes Conformational Changes in Both Nucleotide-binding Domains

The Journal of biological chemistry, 2003-01, Vol.278 (3), p.1575-1578

2003

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Disulfide Cross-linking Analysis Shows That Transmembrane Segments 5 and 8 of Human P-glycoprotein Are Close Together on the Cytoplasmic Side of the Membrane

The Journal of biological chemistry, 2004-02, Vol.279 (9), p.7692-7697

2004

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Substrate-induced conformational changes in the transmembrane segments of human P-glycoprotein. Direct evidence for the substrate-induced fit mechanism for drug binding

The Journal of biological chemistry, 2003-04, Vol.278 (16), p.13603

2003

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Identification of Residues within the Drug-binding Domain of the Human Multidrug Resistance P-glycoprotein by Cysteine-scanning Mutagenesis and Reaction with Dibromobimane

The Journal of biological chemistry, 2000-12, Vol.275 (50), p.39272-39278

2000

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Methanethiosulfonate Derivatives of Rhodamine and Verapamil Activate Human P-glycoprotein at Different Sites

The Journal of biological chemistry, 2003-12, Vol.278 (50), p.50136-50141

2003

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

The Journal of biological chemistry, 2008-09, Vol.283 (36), p.24860-24870

2008

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The Transmembrane Domains of the Human Multidrug Resistance P-glycoprotein Are Sufficient to Mediate Drug Binding and Trafficking to the Cell Surface

The Journal of biological chemistry, 1999-08, Vol.274 (35), p.24759-24765

1999

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Suppressor Mutations in the Transmembrane Segments of P-glycoprotein Promote Maturation of Processing Mutants and Disrupt a Subset of Drug-binding Sites

The Journal of biological chemistry, 2007-11, Vol.282 (44), p.32043-32052

2007

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Correction of Defective Protein Kinesis of Human P-glycoprotein Mutants by Substrates and Modulators

The Journal of biological chemistry, 1997-01, Vol.272 (2), p.709-712

1997

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Structural modeling of an outer membrane electron conduit from a metal-reducing bacterium suggests electron transfer via periplasmic redox partners

Mapping the Binding Site of the Inhibitor Tariquidar That Stabilizes the First Transmembrane Domain of P-glycoprotein

Human P-glycoprotein Contains a Greasy Ball-and-Socket Joint at the Second Transmission Interface

Location of the Rhodamine-binding Site in the Human Multidrug Resistance P-glycoprotein

Simultaneous Binding of Two Different Drugs in the Binding Pocket of the Human Multidrug Resistance P-glycoprotein

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

The Transmission Interfaces Contribute Asymmetrically to the Assembly and Activity of Human P-glycoprotein

Correctors Promote Maturation of Cystic Fibrosis Transmembrane Conductance Regulator (CFTR)-processing Mutants by Binding to the Protein

Processing Mutations Disrupt Interactions between the Nucleotide Binding and Transmembrane Domains of P-glycoprotein and the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR)

The "LSGGQ" motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing walker A sequence

Determining the Dimensions of the Drug-binding Domain of Human P-glycoprotein Using Thiol Cross-linking Compounds as Molecular Rulers

Defining the Drug-binding Site in the Human Multidrug Resistance P-glycoprotein Using a Methanethiosulfonate Analog of Verapamil, MTS-verapamil

Identification of the Distance between the Homologous Halves of P-glycoprotein That Triggers the High/Low ATPase Activity Switch

Locking Intracellular Helices 2 and 3 Together Inactivates Human P-glycoprotein

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

The ATPase Activity of the P-glycoprotein Drug Pump Is Highly Activated When the N-terminal and Central Regions of the Nucleotide-binding Domains Are Linked Closely Together

Drug Binding in Human P-glycoprotein Causes Conformational Changes in Both Nucleotide-binding Domains

Disulfide Cross-linking Analysis Shows That Transmembrane Segments 5 and 8 of Human P-glycoprotein Are Close Together on the Cytoplasmic Side of the Membrane

Substrate-induced conformational changes in the transmembrane segments of human P-glycoprotein. Direct evidence for the substrate-induced fit mechanism for drug binding

Identification of Residues within the Drug-binding Domain of the Human Multidrug Resistance P-glycoprotein by Cysteine-scanning Mutagenesis and Reaction with Dibromobimane

Methanethiosulfonate Derivatives of Rhodamine and Verapamil Activate Human P-glycoprotein at Different Sites

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

The Transmembrane Domains of the Human Multidrug Resistance P-glycoprotein Are Sufficient to Mediate Drug Binding and Trafficking to the Cell Surface

Suppressor Mutations in the Transmembrane Segments of P-glycoprotein Promote Maturation of Processing Mutants and Disrupt a Subset of Drug-binding Sites

Correction of Defective Protein Kinesis of Human P-glycoprotein Mutants by Substrates and Modulators

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