Associated Papers
Revisiting the Role of the Leucine Plug/Valve in the Human ABCG2 Multidrug Transporter.
Mózner O et al.
International Journal of Molecular Sciences, 2025
The human ABCG2 transporter engages three gates to control multidrug extrusion.
Khunweeraphong N et al.
Iscience, 2025
Tumor-acquired somatic mutation affects conformation to abolish ABCG2-mediated drug resistance.
Gose T et al.
Drug Resistance Updates : Reviews and Commentaries in Antimicrobial and Anticancer Chemotherapy, 2024
How Cryo-EM Has Expanded Our Understanding of Membrane Transporters.
Baril SA et al.
Drug Metabolism and Disposition: the Biological Fate of Chemicals, 2023
Structures of ABCG2 under turnover conditions reveal a key step in the drug transport mechanism.
Yu Q et al.
Nature Communications, 2021
Medically Important Alterations in Transport Function and Trafficking of ABCG2.
Homolya L
International Journal of Molecular Sciences, 2021
The transport pathway in the ABCG2 protein and its regulation revealed by molecular dynamics simulations.
Nagy T et al.
Cellular and Molecular Life Sciences : Cmls, 2021
The ABCG2/BCRP transporter and its variants - from structure to pathology.
Sarkadi B et al.
Febs Letters, 2020
The first intracellular loop is essential for the catalytic cycle of the human ABCG2 multidrug resistance transporter.
Khunweeraphong N et al.
Febs Letters, 2020
3D structure of the transporter ABCG2-What's new?
Eckenstaler R et al.
British Journal of Pharmacology, 2020
ABCG2 requires a single aromatic amino acid to "clamp" substrates and inhibitors into the binding pocket.
Gose T et al.
Faseb Journal : Official Publication of the Federation of American Societies for Experimental Biology, 2020
ABCG2 Overexpression Contributes to Pevonedistat Resistance.
Kathawala RJ et al.
Cancers, 2020
Disruption of the Unique ABCG-Family NBD:NBD Interface Impacts Both Drug Transport and ATP Hydrolysis.
Kapoor P et al.
International Journal of Molecular Sciences, 2020
Tivantinib, A c-Met Inhibitor in Clinical Trials, Is Susceptible to ABCG2-Mediated Drug Resistance.
Wu ZX et al.
Cancers, 2020
ABCG2/BCRP: variants, transporter interaction profile of substrates and inhibitors.
Safar Z et al.
Expert Opinion on Drug Metabolism & Toxicology, 2019
Polymorphisms of the Multidrug Pump ABCG2: A Systematic Review of Their Effect on Protein Expression, Function, and Drug Pharmacokinetics.
Heyes N et al.
Drug Metabolism and Disposition: the Biological Fate of Chemicals, 2018
Residues contributing to drug transport by ABCG2 are localised to multiple drug-binding pockets.
Cox MH et al.
The Biochemical Journal, 2018
Generation of multidrug resistant human tissues by overexpression of the ABCG2 multidrug transporter in embryonic stem cells.
Erdei Z et al.
Plos One, 2018
Pharmacogenetic Aspects of the Interaction of AT1 Receptor Antagonists With ATP-Binding Cassette Transporter ABCG2.
Ripperger A et al.
Frontiers in Pharmacology, 2018
Structure-function relationships in ABCG2: insights from molecular dynamics simulations and molecular docking studies.
Ferreira RJ et al.
Scientific Reports, 2017
The structure of the human ABC transporter ABCG2 reveals a novel mechanism for drug extrusion.
Khunweeraphong N et al.
Scientific Reports, 2017
The linker region of breast cancer resistance protein ABCG2 is critical for coupling of ATP-dependent drug transport.
Macalou S et al.
Cellular and Molecular Life Sciences : Cmls, 2016
Jump into a New Fold-A Homology Based Model for the ABCG2/BCRP Multidrug Transporter.
László L et al.
Plos One, 2016
A-803467, a tetrodotoxin-resistant sodium channel blocker, modulates ABCG2-mediated MDR in vitro and in vivo.
Anreddy N et al.
Oncotarget, 2015
Identification of residues in ABCG2 affecting protein trafficking and drug transport, using co-evolutionary analysis of ABCG sequences.
Haider AJ et al.
Bioscience Reports, 2015
Mutations of the central tyrosines of putative cholesterol recognition amino acid consensus (CRAC) sequences modify folding, activity, and sterol-sensing of the human ABCG2 multidrug transporter.
Gál Z et al.
Biochimica Et Biophysica Acta, 2015
Linsitinib (OSI-906) antagonizes ATP-binding cassette subfamily G member 2 and subfamily C member 10-mediated drug resistance.
Zhang H et al.
The International Journal of Biochemistry & Cell Biology, 2014
Masitinib antagonizes ATP-binding cassette subfamily G member 2-mediated multidrug resistance.
Kathawala RJ et al.
International Journal of Oncology, 2014
Regulation of the function of the human ABCG2 multidrug transporter by cholesterol and bile acids: effects of mutations in potential substrate and steroid binding sites.
Telbisz Á et al.
Drug Metabolism and Disposition: the Biological Fate of Chemicals, 2014
Impact of genetic variability in the ABCG2 gene on ABCG2 expression, function, and interaction with AT1 receptor antagonist telmisartan.
Deppe S et al.
Biochemical and Biophysical Research Communications, 2014
Human ABC transporter ABCG2/BCRP expression in chemoresistance: basic and clinical perspectives for molecular cancer therapeutics.
Noguchi K et al.
Pharmacogenomics and Personalized Medicine, 2014
Sequence mutations of the substrate binding pocket of stem cell factor and multidrug resistance protein ABCG2 in renal cell cancer: a possible link to treatment resistance.
Zoernig I et al.
Oncology Reports, 2013
Predicting substrates of the human breast cancer resistance protein using a support vector machine method.
Hazai E et al.
Bmc Bioinformatics, 2013
Effects of the lipid environment, cholesterol and bile acids on the function of the purified and reconstituted human ABCG2 protein.
Telbisz Á et al.
The Biochemical Journal, 2013
Overexpression of ATP-binding cassette transporter ABCG2 as a potential mechanism of acquired resistance to vemurafenib in BRAF(V600E) mutant cancer cells.
Wu CP et al.
Biochemical Pharmacology, 2013
Interaction of the EGFR inhibitors gefitinib, vandetanib, pelitinib and neratinib with the ABCG2 multidrug transporter: implications for the emergence and reversal of cancer drug resistance.
Hegedüs C et al.
Biochemical Pharmacology, 2012
Different roles of TM5, TM6, and ECL3 in the oligomerization and function of human ABCG2.
Mo W et al.
Biochemistry, 2012
Breast cancer resistance protein (BCRP/ABCG2): its role in multidrug resistance and regulation of its gene expression.
Nakanishi T et al.
Chinese Journal of Cancer, 2012
Arginine 482 to glycine mutation in ABCG2/BCRP increases etoposide transport and resistance to the drug in HEK-293 cells.
Eddabra L et al.
Oncology Reports, 2012
Analysis of the effect of the bovine adenosine triphosphate-binding cassette transporter G2 single nucleotide polymorphism Y581S on transcellular transport of veterinary drugs using new cell culture models.
Real R et al.
Journal of Animal Science, 2011
Prognostic value of the multidrug resistance transporter ABCG2 gene polymorphisms in Chinese patients with de novo acute leukaemia.
Wang F et al.
European Journal of Cancer (oxford, England : 1990), 2011
Sildenafil reverses ABCB1- and ABCG2-mediated chemotherapeutic drug resistance.
Shi Z et al.
Cancer Research, 2011
Recombinant synthesis of human ABCG2 expressed in the yeast Saccharomyces cerevisiae: an experimental methodological study.
Jacobs A et al.
The Protein Journal, 2011
The ABCG2 transporter and its relations with the pharmacokinetics, drug interaction and lipid-lowering effects of statins.
Hu M et al.
Expert Opinion on Drug Metabolism & Toxicology, 2011
Variation and evolution of the ABC transporter genes ABCB1, ABCC1, ABCG2, ABCG5 and ABCG8: implication for pharmacogenetics and disease.
Silverton L et al.
Drug Metabolism and Drug Interactions, 2011
Role of basic residues within or near the predicted transmembrane helix 2 of the human breast cancer resistance protein in drug transport.
Cai X et al.
The Journal of Pharmacology and Experimental Therapeutics, 2010
Pharmacological interaction with sunitinib is abolished by a germ-line mutation (1291T>C) of BCRP/ABCG2 gene.
Kawahara H et al.
Cancer Science, 2010