Locking intracellular helices 2 and 3 together inactivates human P-glycoprotein.
about
Identification of the distance between the homologous halves of P-glycoprotein that triggers the high/low ATPase activity switch.Recent advances in the exploration of the bile salt export pump (BSEP/ABCB11) function.The Transmission Interfaces Contribute Asymmetrically to the Assembly and Activity of Human P-glycoproteinCysteines 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.Mapping the Binding Site of the Inhibitor Tariquidar That Stabilizes the First Transmembrane Domain of P-glycoprotein.Conformational dynamics of P-glycoprotein in lipid nanodiscs and detergent micelles reveal complex motions on a wide time scale.
P2860
Locking intracellular helices 2 and 3 together inactivates human P-glycoprotein.
description
2013 nî lūn-bûn
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2013年の論文
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2013年論文
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2013年論文
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name
Locking intracellular helices 2 and 3 together inactivates human P-glycoprotein.
@en
type
label
Locking intracellular helices 2 and 3 together inactivates human P-glycoprotein.
@en
prefLabel
Locking intracellular helices 2 and 3 together inactivates human P-glycoprotein.
@en
P2860
P356
P1476
Locking intracellular helices 2 and 3 together inactivates human P-glycoprotein
@en
P2093
David M Clarke
P2860
P304
P356
10.1074/JBC.M113.527804
P407
P577
2013-11-25T00:00:00Z