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Biochemical Pharmacology|September 24, 2016
Polymorphic variants of MRP4/ABCC4 differentially modulate the transport of methylated arsenic metabolites and physiological organic anionsMayukh Banerjee, Vanessa Marensi, Gwenaëlle Conseil, et al.
Drug Metabolism and Disposition: the Biological Fate of Chemicals|March 27, 2013
Chalcogenopyrylium dyes as differential modulators of organic anion transport by multidrug resistance protein 1 (MRP1), MRP2, and MRP4Robert L Myette, Gwenaëlle Conseil, Sean P Ebert, et al.
The Journal of Biological Chemistry|October 22, 2002
Multiple membrane-associated tryptophan residues contribute to the transport activity and substrate specificity of the human multidrug resistance protein, MRP1Koji Koike, Curtis J Oleschuk, Anass Haimeur, et al.
Biochemistry|August 20, 2003
Characterization of the role of polar amino acid residues within predicted transmembrane helix 17 in determining the substrate specificity of multidrug resistance protein 3Da-Wei Zhang, Hong-Mei Gu, Monika Vasa, et al.
Biochemistry|December 3, 2003
Identification of the structural and functional boundaries of the multidrug resistance protein 1 cytoplasmic loop 3Christopher J Westlake, Yue-Ming Qian, Mian Gao, et al.
Plos One|March 24, 2012
Mechanism of RPE cell death in α-crystallin deficient mice: a novel and critical role for MRP1-mediated GSH effluxParameswaran G Sreekumar, Christine Spee, Stephen J Ryan, et al.
Molecular Pharmacology|August 18, 2005
Analysis of human multidrug resistance protein 1 (ABCC1) by matrix-assisted laser desorption ionization/time of flight mass spectrometry: toward identification of leukotriene C4 binding sitesPeng Wu, Curtis J Oleschuk, Qingcheng Mao, et al.
The Journal of Biological Chemistry|September 5, 2003
Functional importance of polar and charged amino acid residues in transmembrane helix 14 of multidrug resistance protein 1 (MRP1/ABCC1): identification of an aspartate residue critical for conversion from a high to low affinity substrate binding stateDa-Wei Zhang, Hong-Mei Gu, Donna Situ, et al.
Drug Metabolism and Disposition: the Biological Fate of Chemicals|January 18, 2006
Mutational analysis of polar amino acid residues within predicted transmembrane helices 10 and 16 of multidrug resistance protein 1 (ABCC1): effect on substrate specificityDa-Wei Zhang, Kenichi Nunoya, Monika Vasa, et al.
The Journal of Biological Chemistry|October 17, 2003
Molecular modeling correctly predicts the functional importance of Phe594 in transmembrane helix 11 of the multidrug resistance protein, MRP1 (ABCC1)Jeff D Campbell, Koji Koike, Christophe Moreau, et al.
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