Associated Papers
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
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
Pharmacological interaction with sunitinib is abolished by a germ-line mutation (1291T>C) of BCRP/ABCG2 gene.
Kawahara H et al.
Cancer Science, 2010
The nature of amino acid 482 of human ABCG2 affects substrate transport and ATP hydrolysis but not substrate binding.
Ejendal KF et al.
Protein Science : a Publication of the Protein Society, 2006
The role of the human ABCG2 multidrug transporter and its variants in cancer therapy and toxicology.
Cervenak J et al.
Cancer Letters, 2006
ABCG2 harboring the Gly482 mutation confers high-level resistance to various hydrophilic antifolates.
Shafran A et al.
Cancer Research, 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
Single amino acid substitutions in the transmembrane domains of breast cancer resistance protein (BCRP) alter cross resistance patterns in transfectants.
Miwa M et al.
International Journal of Cancer, 2003
Mutations at amino-acid 482 in the ABCG2 gene affect substrate and antagonist specificity.
Robey RW et al.
British Journal of Cancer, 2003
Characterization of drug transport, ATP hydrolysis, and nucleotide trapping by the human ABCG2 multidrug transporter. Modulation of substrate specificity by a point mutation.
Ozvegy C et al.
The Journal of Biological Chemistry, 2002
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