Threonine-978 in the transmembrane segment of the multidrug efflux pump AcrB of Escherichia coli is crucial for drug transport as a probable component of the proton relay network.
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Efflux-mediated drug resistance in bacteria: an updateStructures of intermediate transport states of ZneA, a Zn(II)/proton antiporterStructural basis of RND-type multidrug exportersFunctional relevance of AcrB Trimerization in pump assembly and substrate bindingExploring the HME and HAE1 efflux systems in the genus BurkholderiaMultidrug efflux pump MdtBC of Escherichia coli is active only as a B2C heterotrimerCrystal structures of the Burkholderia multivorans hopanoid transporter HpnNMechanism of recognition of compounds of diverse structures by the multidrug efflux pump AcrB of Escherichia coli.Structure and mechanism of RND-type multidrug efflux pumpsHigh salt concentrations increase permeability through OmpC channels of Escherichia coli.Mechanisms of RND multidrug efflux pumpsConformation of the AcrB multidrug efflux pump in mutants of the putative proton relay pathway.Coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump AcrBEfflux pumps of the resistance-nodulation-division family: a perspective of their structure, function, and regulation in gram-negative bacteria.Substrate binding accelerates the conformational transitions and substrate dissociation in multidrug efflux transporter AcrB.The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria.Reversal of the Drug Binding Pocket Defects of the AcrB Multidrug Efflux Pump Protein of Escherichia coli.MexXY multidrug efflux system of Pseudomonas aeruginosa.Permeation rates of penicillins indicate that Escherichia coli porins function principally as nonspecific channelsAssembly and transport mechanism of tripartite drug efflux systems.Structural and functional aspects of the multidrug efflux pump AcrB.Molecular Dynamics Computer Simulations of Multidrug RND Efflux PumpsEfflux pump-mediated antibiotics resistance: insights from computational structural biology.Transport of lipophilic carboxylates is mediated by transmembrane helix 2 in multidrug transporter AcrB.Landscape of Resistance-Nodulation-Cell Division (RND)-Type Efflux Pumps in Enterobacter cloacae Complex.Covalently linked trimer of the AcrB multidrug efflux pump provides support for the functional rotating mechanism.Tripartite efflux pumps: energy is required for dissociation, but not assembly or opening of the outer membrane channel of the pumpStructures and transport dynamics of a Campylobacter jejuni multidrug efflux pump.Substrate path in the AcrB multidrug efflux pump of Escherichia coli.Catch me if you can: a biotinylated proteoliposome affinity assay for the investigation of assembly of the MexA-MexB-OprM efflux pump from Pseudomonas aeruginosa.Expression of homologous RND efflux pump genes is dependent upon AcrB expression: implications for efflux and virulence inhibitor design.Energy-coupling mechanism of the multidrug resistance transporter AcrB: Evidence for membrane potential-driving hypothesis through mutagenic analysis.Physiological responses of Pseudomonas putida to formaldehyde during detoxification.Site-directed disulfide cross-linking shows that cleft flexibility in the periplasmic domain is needed for the multidrug efflux pump AcrB of Escherichia coli.Ligand-transporter interaction in the AcrB multidrug efflux pump determined by fluorescence polarization assay.Hoisting-Loop in Bacterial Multidrug Exporter AcrB Is a Highly Flexible Hinge That Enables the Large Motion of the Subdomains.Covalently Linked Trimers of RND (Resistance-Nodulation-Division) Efflux Transporters to Study Their Mechanism of Action: Escherichia coli AcrB Multidrug Exporter as an Example.Constant pH Molecular Dynamics Reveals How Proton Release Drives the Conformational Transition of a Transmembrane Efflux Pump.Contribution of RaeB, a Putative RND-Type Transporter to Aminoglycoside and Detergent Resistance in Riemerella anatipestifer.Energy coupling mechanisms of AcrB-like RND transporters.
P2860
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P2860
Threonine-978 in the transmembrane segment of the multidrug efflux pump AcrB of Escherichia coli is crucial for drug transport as a probable component of the proton relay network.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Threonine-978 in the transmemb ...... t of the proton relay network.
@en
Threonine-978 in the transmemb ...... t of the proton relay network.
@nl
type
label
Threonine-978 in the transmemb ...... t of the proton relay network.
@en
Threonine-978 in the transmemb ...... t of the proton relay network.
@nl
prefLabel
Threonine-978 in the transmemb ...... t of the proton relay network.
@en
Threonine-978 in the transmemb ...... t of the proton relay network.
@nl
P2860
P921
P356
P1476
Threonine-978 in the transmemb ...... t of the proton relay network.
@en
P2093
Hiroshi Nikaido
Yumiko Takatsuka
P2860
P304
P356
10.1128/JB.00683-06
P407
P577
2006-10-01T00:00:00Z