000 01774 a2200457 4500
005 20250516224001.0
264 0 _c20150128
008 201501s 0 0 eng d
022 _a1083-351X
024 7 _a10.1074/jbc.M114.583021
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aLoo, Tip W
245 0 0 _aCysteines 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.
_h[electronic resource]
260 _bThe Journal of biological chemistry
_cSep 2014
300 _a24749-58 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't
650 0 4 _aATP Binding Cassette Transporter, Subfamily B
_xchemistry
650 0 4 _aAdenosine Triphosphatases
_xmetabolism
650 0 4 _aAdenosine Triphosphate
_xmetabolism
650 0 4 _aAnimals
650 0 4 _aBinding Sites
_xgenetics
650 0 4 _aCell Line
650 0 4 _aCysteine
_xchemistry
650 0 4 _aDisulfides
_xchemistry
650 0 4 _aDithiothreitol
_xpharmacology
650 0 4 _aDrug Resistance, Multiple
_xdrug effects
650 0 4 _aGlycoside Hydrolases
_xmetabolism
650 0 4 _aHEK293 Cells
650 0 4 _aHumans
650 0 4 _aHydrolysis
650 0 4 _aImmunoblotting
650 0 4 _aModels, Molecular
650 0 4 _aMutation
650 0 4 _aPharmaceutical Preparations
_xmetabolism
650 0 4 _aProtein Conformation
650 0 4 _aProtein Structure, Secondary
650 0 4 _aProtein Structure, Tertiary
700 1 _aClarke, David M
773 0 _tThe Journal of biological chemistry
_gvol. 289
_gno. 36
_gp. 24749-58
856 4 0 _uhttps://doi.org/10.1074/jbc.M114.583021
_zAvailable from publisher's website
999 _c24034554
_d24034554