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The anti-tumour agent lonidamine is a potent inhibitor of the mitochondrial pyruvate carrier and plasma membrane monocarboxylate transporters. , Nancolas B., Biochem J. April 1, 2016; 473 (7): 929-36.
Identification of key binding site residues of MCT1 for AR-C155858 reveals the molecular basis of its isoform selectivity. , Nancolas B., Biochem J. February 15, 2015; 466 (1): 177-88.
Rapid downregulation of the rat glutamine transporter SNAT3 by a caveolin-dependent trafficking mechanism in Xenopus laevis oocytes. , Balkrishna S., Am J Physiol Cell Physiol. November 1, 2010; 299 (5): C1047-57.
The inhibition of monocarboxylate transporter 2 ( MCT2) by AR-C155858 is modulated by the associated ancillary protein. , Ovens MJ., Biochem J. October 15, 2010; 431 (2): 217-25.
AR-C155858 is a potent inhibitor of monocarboxylate transporters MCT1 and MCT2 that binds to an intracellular site involving transmembrane helices 7-10. , Ovens MJ., Biochem J. January 15, 2010; 425 (3): 523-30.
Studies on the DIDS-binding site of monocarboxylate transporter 1 suggest a homology model of the open conformation and a plausible translocation cycle. , Wilson MC., J Biol Chem. July 24, 2009; 284 (30): 20011-21.
Nonenzymatic proton handling by carbonic anhydrase II during H+-lactate cotransport via monocarboxylate transporter 1. , Becker HM., J Biol Chem. August 1, 2008; 283 (31): 21655-67.
The role of charged residues in the transmembrane helices of monocarboxylate transporter 1 and its ancillary protein basigin in determining plasma membrane expression and catalytic activity. , Manoharan C., Mol Membr Biol. January 1, 2006; 23 (6): 486-98.
The loop between helix 4 and helix 5 in the monocarboxylate transporter MCT1 is important for substrate selection and protein stability. , Gali S., Biochem J. December 1, 2003; 376 (Pt 2): 413-22.
Characterization of the high-affinity monocarboxylate transporter MCT2 in Xenopus laevis oocytes. , Bröer S., Biochem J. August 1, 1999; 341 ( Pt 3) 529-35.