Published in J Biol Chem on August 22, 1997
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Cysteines introduced into extracellular loops 1 and 4 of human P-glycoprotein that are close only in the open conformation spontaneously form a disulfide bond that inhibits drug efflux and ATPase activity. J Biol Chem (2014) 0.78
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Global alteration of the drug-binding pocket of human P-glycoprotein (ABCB1) by substitution of fifteen conserved residues reveals a negative correlation between substrate size and transport efficiency. Biochem Pharmacol (2017) 0.75
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Pharmacokinetic-pharmacodynamic modelling of the antimalarial activity of mefloquine. Parasitology (2001) 1.18
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Modelling the chloroquine chemotherapy of falciparum malaria: the value of spacing a split dose. Parasitology (1998) 1.15
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Combined effects of ATP and phosphate on rubidium exchange mediated by Na-K-ATPase reconstituted into phospholipid vesicles. J Physiol (1982) 1.01
P-glycoprotein substrates and antagonists cluster into two distinct groups. Mol Pharmacol (1997) 0.99
The new permeability pathways induced by the malaria parasite in the membrane of the infected erythrocyte: comparison of results using different experimental techniques. J Membr Biol (2004) 0.97
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Rejection criteria for the asymmetric carrier and their application to glucose transport in the human red blood cell. Biochim Biophys Acta (1972) 0.95
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Effects of atp or phosphate on passive rubidium fluxes mediated by Na-K-ATPase reconstituted into phospholipid vesicles. J Physiol (1982) 0.95
A simple resolution of the kinetic anomaly in the exchange of different sugars across the membrane of the human red blood cell. Biochim Biophys Acta (1972) 0.94
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