P-glycoprotein is fully active after multiple tryptophan substitutions
about
Directed evolution of P-glycoprotein cysteines reveals site-specific, non-conservative substitutions that preserve multidrug resistance.Pore-exposed tyrosine residues of P-glycoprotein are important hydrogen-bonding partners for drugs.Global marine pollutants inhibit P-glycoprotein: Environmental levels, inhibitory effects, and cocrystal structure
P2860
P-glycoprotein is fully active after multiple tryptophan substitutions
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
P-glycoprotein is fully active after multiple tryptophan substitutions
@ast
P-glycoprotein is fully active after multiple tryptophan substitutions
@en
type
label
P-glycoprotein is fully active after multiple tryptophan substitutions
@ast
P-glycoprotein is fully active after multiple tryptophan substitutions
@en
prefLabel
P-glycoprotein is fully active after multiple tryptophan substitutions
@ast
P-glycoprotein is fully active after multiple tryptophan substitutions
@en
P2093
P2860
P1476
P-glycoprotein is fully active after multiple tryptophan substitutions
@en
P2093
Douglas J Swartz
Ina L Urbatsch
Joachim Weber
P2860
P304
P356
10.1016/J.BBAMEM.2012.12.005
P407
P577
2012-12-19T00:00:00Z