Human-Mouse Chimeras with Normal Expression and Function Reveal That Major Domain Swapping Is Tolerated by P-Glycoprotein (ABCB1).
about
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.Mapping discontinuous epitopes for MRK-16, UIC2 and 4E3 antibodies to extracellular loops 1 and 4 of human P-glycoproteinEvidence for the critical role of transmembrane helices 1 and 7 in substrate transport by human P-glycoprotein (ABCB1)
P2860
Human-Mouse Chimeras with Normal Expression and Function Reveal That Major Domain Swapping Is Tolerated by P-Glycoprotein (ABCB1).
description
article científic
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article scientifique
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articolo scientifico
@it
artigo científico
@pt
bilimsel makale
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scientific article published on 28 January 2016
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Human-Mouse Chimeras with Norm ...... ted by P-Glycoprotein (ABCB1).
@en
Human-Mouse Chimeras with Norm ...... Is Tolerated by P-Glycoprotein
@nl
type
label
Human-Mouse Chimeras with Norm ...... ted by P-Glycoprotein (ABCB1).
@en
Human-Mouse Chimeras with Norm ...... Is Tolerated by P-Glycoprotein
@nl
prefLabel
Human-Mouse Chimeras with Norm ...... ted by P-Glycoprotein (ABCB1).
@en
Human-Mouse Chimeras with Norm ...... Is Tolerated by P-Glycoprotein
@nl
P2093
P2860
P1433
P1476
Human-Mouse Chimeras with Norm ...... ated by P-Glycoprotein (ABCB1)
@en
P2093
Eduardo E Chufan
Kristen M Pluchino
Matthew D Hall
Michael M Gottesman
Patricia A Fetsch
Stephen C Hyde
Suneet Shukla
Suresh V Ambudkar
P2860
P304
P356
10.1021/ACS.BIOCHEM.5B01064
P407
P577
2016-02-10T00:00:00Z