Identification of the distance between the homologous halves of P-glycoprotein that triggers the high/low ATPase activity switch.
about
Equilibrated atomic models of outward-facing P-glycoprotein and effect of ATP binding on structural dynamics.Distinct conformational spectrum of homologous multidrug ABC transporters.Structures of the Multidrug Transporter P-glycoprotein Reveal Asymmetric ATP Binding and the Mechanism of Polyspecificity.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.Substrate-induced conformational changes in the nucleotide-binding domains of lipid bilayer-associated P-glycoprotein during ATP hydrolysis.
P2860
Identification of the distance between the homologous halves of P-glycoprotein that triggers the high/low ATPase activity switch.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 12 February 2014
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Identification of the distance ...... gh/low ATPase activity switch.
@en
Identification of the distance ...... gh/low ATPase activity switch.
@nl
type
label
Identification of the distance ...... gh/low ATPase activity switch.
@en
Identification of the distance ...... gh/low ATPase activity switch.
@nl
prefLabel
Identification of the distance ...... gh/low ATPase activity switch.
@en
Identification of the distance ...... gh/low ATPase activity switch.
@nl
P2860
P356
P1476
Identification of the distance ...... igh/low ATPase activity switch
@en
P2093
David M Clarke
P2860
P304
P356
10.1074/JBC.M114.552075
P407
P577
2014-02-12T00:00:00Z