Substrate specificity of the RND-type multidrug efflux pumps AcrB and AcrD of Escherichia coli is determined predominantly by two large periplasmic loops.
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Multidrug resistance in bacteriaInteraction between polyketide synthase and transporter suggests coupled synthesis and export of virulence lipid in M. tuberculosis.Recent advances toward a molecular mechanism of efflux pump inhibitionDrug export pathway of multidrug exporter AcrB revealed by DARPin inhibitorsTransport of drugs by the multidrug transporter AcrB involves an access and a deep binding pocket that are separated by a switch-loopThe ins and outs of RND efflux pumps in Escherichia coliStructural basis of RND-type multidrug exportersFitting periplasmic membrane fusion proteins to inner membrane transporters: mutations that enable Escherichia coli AcrA to function with Pseudomonas aeruginosa MexBMolecular basis of pyoverdine siderophore recycling in Pseudomonas aeruginosaXenobiotic efflux in bacteria and fungi: a genomics updateTolC--the bacterial exit duct for proteins and drugs.Efflux-mediated heavy metal resistance in prokaryotes.Cloning, sequencing, and characterization of the SdeAB multidrug efflux pump of Serratia marcescens.Exploring the HME and HAE1 efflux systems in the genus BurkholderiaMultidrug efflux pump MdtBC of Escherichia coli is active only as a B2C heterotrimerβ-Lactam selectivity of multidrug transporters AcrB and AcrD resides in the proximal binding pocket.Single nucleotide polymorphism analysis of the major tripartite multidrug efflux pump of Escherichia coli: functional conservation in disparate animal reservoirs despite exposure to antimicrobial chemotherapyAminoglycosides are captured from both periplasm and cytoplasm by the AcrD multidrug efflux transporter of Escherichia coli.Contribution of the Mycobacterium tuberculosis MmpL protein family to virulence and drug resistanceGenomics of rapid adaptation to antibiotics: convergent evolution and scalable sequence amplificationEngineering microbial biofuel tolerance and export using efflux pumpsDiffering ability to transport nonmetal substrates by two RND-type metal exporters.A periplasmic drug-binding site of the AcrB multidrug efflux pump: a crystallographic and site-directed mutagenesis study.Microbial efflux pump inhibition: tactics and strategies.Structure and mechanism of RND-type multidrug efflux pumpsMammalian steroid hormones are substrates for the major RND- and MFS-type tripartite multidrug efflux pumps of Escherichia coli.Mechanisms of RND multidrug efflux pumpsRepressive mutations restore function-loss caused by the disruption of trimerization in Escherichia coli multidrug transporter AcrB.In vivo and in vitro evidence that TtgV is the specific regulator of the TtgGHI multidrug and solvent efflux pump of Pseudomonas putida.AcrB multidrug efflux pump of Escherichia coli: composite substrate-binding cavity of exceptional flexibility generates its extremely wide substrate specificity.Structure and function of efflux pumps that confer resistance to drugsSubstrate binding accelerates the conformational transitions and substrate dissociation in multidrug efflux transporter AcrB.Membrane-Targeting DCAP Analogues with Broad-Spectrum Antibiotic Activity against Pathogenic BacteriaSubstrate competition studies using whole-cell accumulation assays with the major tripartite multidrug efflux pumps of Escherichia coliInteraction of antibacterial compounds with RND efflux pumps in Pseudomonas aeruginosaInvolvement of the AcrAB-TolC efflux pump in the resistance, fitness, and virulence of Enterobacter cloacaeSQ109 targets MmpL3, a membrane transporter of trehalose monomycolate involved in mycolic acid donation to the cell wall core of Mycobacterium tuberculosis.Chimeric analysis of AcrA function reveals the importance of its C-terminal domain in its interaction with the AcrB multidrug efflux pumpDrug-induced conformational changes in multidrug efflux transporter AcrB from Haemophilus influenzaeVacuuming the periplasm.
P2860
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P2860
Substrate specificity of the RND-type multidrug efflux pumps AcrB and AcrD of Escherichia coli is determined predominantly by two large periplasmic loops.
description
2002 nî lūn-bûn
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2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված
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2002年の論文
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2002年学术文章
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2002年学术文章
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2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
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2002年學術文章
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name
Substrate specificity of the R ...... y two large periplasmic loops.
@ast
Substrate specificity of the R ...... y two large periplasmic loops.
@en
Substrate specificity of the R ...... y two large periplasmic loops.
@nl
type
label
Substrate specificity of the R ...... y two large periplasmic loops.
@ast
Substrate specificity of the R ...... y two large periplasmic loops.
@en
Substrate specificity of the R ...... y two large periplasmic loops.
@nl
prefLabel
Substrate specificity of the R ...... y two large periplasmic loops.
@ast
Substrate specificity of the R ...... y two large periplasmic loops.
@en
Substrate specificity of the R ...... y two large periplasmic loops.
@nl
P2860
P1476
Substrate specificity of the R ...... y two large periplasmic loops.
@en
P2093
Christopher A Elkins
Hiroshi Nikaido
P2860
P304
P356
10.1128/JB.184.23.6490-6499.2002
P407
P577
2002-12-01T00:00:00Z