Toward understanding the mechanism of action of the yeast multidrug resistance transporter Pdr5p: a molecular modeling study.
about
A mutation in intracellular loop 4 affects the drug-efflux activity of the yeast multidrug resistance ABC transporter Pdr5pJump into a New Fold-A Homology Based Model for the ABCG2/BCRP Multidrug TransporterTransporter engineering for improved tolerance against alkane biofuels in Saccharomyces cerevisiaeFrom laptop to benchtop to bedside: structure-based drug design on protein targets.The signaling interface of the yeast multidrug transporter Pdr5 adopts a cis conformation, and there are functional overlap and equivalence of the deviant and canonical Q-loop residues.Evidence for a molecular diode-based mechanism in a multispecific ATP-binding cassette (ABC) exporter: SER-1368 as a gatekeeping residue in the yeast multidrug transporter Pdr5Specific interactions between the Candida albicans ABC transporter Cdr1p ectodomain and a D-octapeptide derivative inhibitor.Mutational Analysis of Intracellular Loops Identify Cross Talk with Nucleotide Binding Domains of Yeast ABC Transporter Cdr1p.The transmission interface of the Saccharomyces cerevisiae multidrug transporter Pdr5: Val-656 located in intracellular loop 2 plays a major role in drug resistance.The multidrug transporter Pdr5 on the 25th anniversary of its discovery: an important model for the study of asymmetric ABC transportersThe deviant ATP-binding site of the multidrug efflux pump Pdr5 plays an active role in the transport cycle.Structures of the Multidrug Transporter P-glycoprotein Reveal Asymmetric ATP Binding and the Mechanism of Polyspecificity.Identification and functional characterization of Penicillium marneffei pleiotropic drug resistance transporters ABC1 and ABC2.Protein engineering of Saccharomyces cerevisiae transporter Pdr5p identifies key residues that impact Fusarium mycotoxin export and resistance to inhibition.Generating symmetry in the asymmetric ATP-binding cassette (ABC) transporter Pdr5 from Saccharomyces cerevisiae.Insight into pleiotropic drug resistance ATP-binding cassette pump drug transport through mutagenesis of Cdr1p transmembrane domains.Positive regulation of the Candida albicans multidrug efflux pump Cdr1p function by phosphorylation of its N-terminal extension.Newly identified motifs in Candida albicans Cdr1 protein nucleotide binding domains are pleiotropic drug resistance subfamily-specific and functionally asymmetric.Mutations of charged amino acids at the cytoplasmic end of transmembrane helix 2 affect transport activity of the budding yeast multidrug resistance protein Pdr5p.
P2860
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P2860
Toward understanding the mechanism of action of the yeast multidrug resistance transporter Pdr5p: a molecular modeling study.
description
2010 nî lūn-bûn
@nan
2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
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2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Toward understanding the mecha ...... p: a molecular modeling study.
@ast
Toward understanding the mecha ...... p: a molecular modeling study.
@en
Toward understanding the mecha ...... p: a molecular modeling study.
@nl
type
label
Toward understanding the mecha ...... p: a molecular modeling study.
@ast
Toward understanding the mecha ...... p: a molecular modeling study.
@en
Toward understanding the mecha ...... p: a molecular modeling study.
@nl
prefLabel
Toward understanding the mecha ...... p: a molecular modeling study.
@ast
Toward understanding the mecha ...... p: a molecular modeling study.
@en
Toward understanding the mecha ...... p: a molecular modeling study.
@nl
P2093
P2860
P1476
Toward understanding the mecha ...... p: a molecular modeling study.
@en
P2093
Lothar Esser
Robert M Rutledge
P2860
P304
P356
10.1016/J.JSB.2010.10.012
P577
2010-10-27T00:00:00Z