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- W1573592020 abstract "Publisher Summary This chapter discusses P-glycoprotein drug-binding data that suggest the existence of multiple drug-binding sites and overlapping sites within the P-glycoprotein structure. P-Glycoprotein is encoded by a family of two closely linked genes (MDR1 and MDR2) on chromosome 7 in humans, three genes in Chinese hamsters ( pgpl , pgp2 , and pgp3 ), and three genes in mice ( mdrl , mdr2 , and mdr3 , or mdr1b , mdr2 , and mdr1a , respectively). The kinetic results present in the chapter suggests the presence of a binding site for vinblastine, verapamil, cyclosporin A, phenothiazines and related agents; a second binding site for dihydropyridine calcium channel blockers; a third site for the calcium channel blockers bepridil and prenylamine, megestrol acetate, a synthetic congener of progesterone; and a fourth binding site for I-AAP. Therefore, the substrates for P-glycoprotein interact competitively and allosterically for binding to this protein. This transport is temperature and adenosine triphosphate (ATP) dependent; it occurs against concentration gradients and follows Michaelis–Menten kinetics." @default.
- W1573592020 created "2016-06-24" @default.
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- W1573592020 date "1998-01-01" @default.
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- W1573592020 title "[21] Photoaffinity labels for characterizing drug interaction sites of P-glycoprotein" @default.
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- W1573592020 doi "https://doi.org/10.1016/s0076-6879(98)92023-7" @default.
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