Associated Papers
The human ABCG2 transporter engages three gates to control multidrug extrusion.
Khunweeraphong N et al.
Iscience, 2025
Long-range communication between transmembrane- and nucleotide-binding domains does not depend on drug binding to mutant P-glycoprotein.
Bonito CA et al.
Journal of Biomolecular Structure & Dynamics, 2023
ConVarT: a search engine for matching human genetic variants with variants from non-human species.
Pir MS et al.
Nucleic Acids Research, 2022
Vincristine-Induced Peripheral Neuropathy in Childhood Acute Lymphoblastic Leukemia: Genetic Variation as a Potential Risk Factor.
Yang QY et al.
Frontiers in Pharmacology, 2021
Theoretical insights on helix repacking as the origin of P-glycoprotein promiscuity.
Bonito CA et al.
Scientific Reports, 2020
Comparison of mechanistic transport cycle models of ABC exporters.
Szöllősi D et al.
Biochimica Et Biophysica Acta. Biomembranes, 2018
Polymorphisms of the drug transporters ABCB1, ABCG2, ABCC2 and ABCC3 and their impact on drug bioavailability and clinical relevance.
Bruhn O et al.
Expert Opinion on Drug Metabolism & Toxicology, 2014
Polymorphisms of the vincristine pathway and response to treatment in children with childhood acute lymphoblastic leukemia.
Ceppi F et al.
Pharmacogenomics, 2014
Relationship between response to colchicine treatment and MDR1 polymorphism in familial Mediterranean fever patients.
Uludag A et al.
Genetic Testing and Molecular Biomarkers, 2014
A conserved interdomain communication pathway of pseudosymmetrically distributed residues affects substrate specificity of the fungal multidrug transporter Cdr1p.
Kolaczkowski M et al.
Biochimica Et Biophysica Acta, 2013
An update on ABCB1 pharmacogenetics: insights from a 3D model into the location and evolutionary conservation of residues corresponding to SNPs associated with drug pharmacokinetics.
Wolf SJ et al.
The Pharmacogenomics Journal, 2011
Association between ABCB1 (MDR1) gene 3435 C>T polymorphism and colchicine unresponsiveness of FMF patients.
Ozen F et al.
Renal Failure, 2011
A synonymous polymorphism in a common MDR1 (ABCB1) haplotype shapes protein function.
Fung KL et al.
Biochimica Et Biophysica Acta, 2009
Function-altering SNPs in the human multidrug transporter gene ABCB1 identified using a Saccharomyces-based assay.
Jeong H et al.
Plos Genetics, 2007
Genetic polymorphisms of ATP-binding cassette transporters ABCB1 and ABCG2: therapeutic implications.
Sakurai A et al.
Expert Opinion on Pharmacotherapy, 2005
The relationship between the pharmacology of antiepileptic drugs and human gene variation: an overview.
Ferraro TN et al.
Epilepsy & Behavior : E&b, 2005
Single amino acid (482) variants of the ABCG2 multidrug transporter: major differences in transport capacity and substrate recognition.
Ozvegy-Laczka C et al.
Biochimica Et Biophysica Acta, 2005
High-speed screening of human ATP-binding cassette transporter function and genetic polymorphisms: new strategies in pharmacogenomics.
Ishikawa T et al.
Methods in Enzymology, 2005
Pharmacogenomics of drug transporters: a new approach to functional analysis of the genetic polymorphisms of ABCB1 (P-glycoprotein/MDR1).
Ishikawa T et al.
Biological & Pharmaceutical Bulletin, 2004
Improved energy coupling of human P-glycoprotein by the glycine 185 to valine mutation.
Omote H et al.
Biochemistry, 2004
[MDR1 genotypes related to pharmacokinetics and MDR1 expression].
Nakamura T
Yakugaku Zasshi : Journal of the Pharmaceutical Society of Japan, 2003
MDR1 genotype-related pharmacokinetics and pharmacodynamics.
Sakaeda T et al.
Biological & Pharmaceutical Bulletin, 2002
Distinct haplotype profiles and strong linkage disequilibrium at the MDR1 multidrug transporter gene locus in three ethnic Asian populations.
Tang K et al.
Pharmacogenetics, 2002
Transmembrane domain (TM) 9 represents a novel site in P-glycoprotein that affects drug resistance and cooperates with TM6 to mediate [125I]iodoarylazidoprazosin labeling.
Song J et al.
Molecular Pharmacology, 2001
Coordinate changes in drug resistance and drug-induced conformational transitions in altered-function mutants of the multidrug transporter P-glycoprotein.
Ruth A et al.
Biochemistry, 2001
Identification of residues in the drug-binding domain of human P-glycoprotein. Analysis of transmembrane segment 11 by cysteine-scanning mutagenesis and inhibition by dibromobimane.
Loo TW et al.
The Journal of Biological Chemistry, 1999
Structural flexibility of the linker region of human P-glycoprotein permits ATP hydrolysis and drug transport.
Hrycyna CA et al.
Biochemistry, 1998
Mutations in the nucleotide-binding sites of P-glycoprotein that affect substrate specificity modulate substrate-induced adenosine triphosphatase activity.
Beaudet L et al.
Biochemistry, 1998
Mutational analysis of the P-glycoprotein first intracellular loop and flanking transmembrane domains.
Kwan T et al.
Biochemistry, 1998
Characterization of the human multidrug resistance protein containing mutations in the ATP-binding cassette signature region.
Bakos E et al.
The Biochemical Journal, 1997
Mutagenesis of transmembrane domain 11 of P-glycoprotein by alanine scanning.
Hanna M et al.
Biochemistry, 1996
Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug-stimulated ATPase activities.
Loo TW et al.
The Journal of Biological Chemistry, 1995
Functional evidence that transmembrane 12 and the loop between transmembrane 11 and 12 form part of the drug-binding domain in P-glycoprotein encoded by MDR1.
Zhang X et al.
The Journal of Biological Chemistry, 1995
Functional expression of human P-glycoprotein in Schizosaccharomyces pombe.
Ueda K et al.
Febs Letters, 1993