On the mechanism of substrate specificity by resistance nodulation division (RND)-type multidrug resistance pumps: the large periplasmic loops of MexD from Pseudomonas aeruginosa are involved in substrate recognition.
about
Multidrug resistance in bacteriaRecent advances toward a molecular mechanism of efflux pump inhibitionFitting 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 aeruginosaFunctional relevance of AcrB Trimerization in pump assembly and substrate bindingXenobiotic efflux in bacteria and fungi: a genomics updateEfflux-mediated heavy metal resistance in prokaryotes.Exploring the HME and HAE1 efflux systems in the genus Burkholderiaβ-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 chemotherapyContribution of the Mycobacterium tuberculosis MmpL protein family to virulence and drug resistanceMechanism of recognition of compounds of diverse structures by the multidrug efflux pump AcrB of Escherichia coli.Determination of real-time efflux phenotypes in Escherichia coli AcrB binding pocket phenylalanine mutants using a 1,2'-dinaphthylamine efflux assay.A periplasmic drug-binding site of the AcrB multidrug efflux pump: a crystallographic and site-directed mutagenesis study.Cell division defects in Escherichia coli deficient in the multidrug efflux transporter AcrEF-TolCMicrobial efflux pump inhibition: tactics and strategies.Structure and mechanism of RND-type multidrug efflux pumpsPhenothiazinium antimicrobial photosensitizers are substrates of bacterial multidrug resistance pumps.Mechanisms of RND multidrug efflux pumpsAcrB drug-binding pocket substitution confers clinically relevant resistance and altered substrate specificity.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 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 aeruginosaDrug-induced conformational changes in multidrug efflux transporter AcrB from Haemophilus influenzaeVacuuming the periplasm.Modeling the tripartite drug efflux pump archetype: structural and functional studies of the macromolecular constituents reveal more than their names imply.Structural and functional aspects of the multidrug efflux pump AcrB.Multicomponent drug efflux complexes: architecture and mechanism of assembly.Broad-specificity efflux pumps and their role in multidrug resistance of Gram-negative bacteria.Analysis of the topology of Vibrio cholerae NorM and identification of amino acid residues involved in norfloxacin resistance.A census of RND superfamily proteins in the Burkholderia genus.Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli.Efflux of cytoplasmically acting antibiotics from gram-negative bacteria: periplasmic substrate capture by multicomponent efflux pumps inferred from their cooperative action with single-component transporters.Differential impact of MexB mutations on substrate selectivity of the MexAB-OprM multidrug efflux pump of Pseudomonas aeruginosa.Evidence of a Substrate-Discriminating Entrance Channel in the Lower Porter Domain of the Multidrug Resistance Efflux Pump AcrBMutations in the central cavity and periplasmic domain affect efflux activity of the resistance-nodulation-division pump EmhB from Pseudomonas fluorescens cLP6a.Assembly of the MexAB-OprM multidrug efflux system of Pseudomonas aeruginosa: identification and characterization of mutations in mexA compromising MexA multimerization and interaction with MexB.Site-directed mutagenesis reveals putative substrate binding residues in the Escherichia coli RND efflux pump AcrB.Molecular Rationale behind the Differential Substrate Specificity of Bacterial RND Multi-Drug Transporters.
P2860
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P2860
On the mechanism of substrate specificity by resistance nodulation division (RND)-type multidrug resistance pumps: the large periplasmic loops of MexD from Pseudomonas aeruginosa are involved in substrate recognition.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
On the mechanism of substrate ...... lved in substrate recognition.
@en
On the mechanism of substrate specificity by resistance nodulation division
@nl
type
label
On the mechanism of substrate ...... lved in substrate recognition.
@en
On the mechanism of substrate specificity by resistance nodulation division
@nl
prefLabel
On the mechanism of substrate ...... lved in substrate recognition.
@en
On the mechanism of substrate specificity by resistance nodulation division
@nl
P2093
P2860
P1476
On the mechanism of substrate ...... lved in substrate recognition.
@en
P2093
Deborah S Black
Mark S Warren
Naomasa Gotoh
Olga Lomovskaya
Takahumi Satou
Takeshi Murata
Takeshi Nishino
Weimin Mao
P2860
P304
P356
10.1046/J.1365-2958.2002.03223.X
P407
P577
2002-11-01T00:00:00Z