Sequential mechanism of assembly of multidrug efflux pump AcrAB-TolC. - Wikidata - wikimedia - TriplyDB

Sequential mechanism of assembly of multidrug efflux pump AcrAB-TolC.

Sequential mechanism of assembly of multidrug efflux pump AcrAB-TolC.

http://www.wikidata.org/entity/Q34863109

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RND-type drug eﬄux pumps from Gram-negative bacteria: molecular mechanism and inhibition Mechanism of coupling drug transport reactions located in two different membranes Assembly and Channel Opening of Outer Membrane Protein in Tripartite Drug Efflux Pumps of Gram-negative Bacteria Structure of the AcrAB–TolC multidrug efflux pump The ins and outs of RND efflux pumps in Escherichia coli Structural basis of RND-type multidrug exporters Structure-function analysis of the ATP-driven glycolipid efflux pump DevBCA reveals complex organization with TolC/HgdD.A data-driven approach to modeling the tripartite structure of multidrug resistance efflux pumps.Architecture and roles of periplasmic adaptor proteins in tripartite eﬄux assemblies Coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump AcrB Mechanism and Function of the Outer Membrane Channel TolC in Multidrug Resistance and Physiology of Enterobacteria.The periplasmic membrane proximal domain of MacA acts as a switch in stimulation of ATP hydrolysis by MacB transporter.The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria.Improving olefin tolerance and production in E. coli using native and evolved AcrB.Interaction of antibacterial compounds with RND eﬄux pumps in Pseudomonas aeruginosa Reversal of the Drug Binding Pocket Defects of the AcrB Multidrug Efflux Pump Protein of Escherichia coli.Non-equivalent roles of two periplasmic subunits in the function and assembly of triclosan pump TriABC from Pseudomonas aeruginosa.Role of ATP binding and hydrolysis in assembly of MacAB-TolC macrolide transporter.Tripartite assembly of RND multidrug efflux pumps.Permeability Barrier of Gram-Negative Cell Envelopes and Approaches To Bypass It.On the role of TolC in multidrug efflux: the function and assembly of AcrAB-TolC tolerate significant depletion of intracellular TolC protein Breaking the Permeability Barrier of Escherichia coli by Controlled Hyperporination of the Outer Membrane.Molecular Dynamics Computer Simulations of Multidrug RND Efflux Pumps Structure and mechanism of the tripartite CusCBA heavy-metal efflux complex.Efflux pump-mediated antibiotics resistance: insights from computational structural biology.AcrB-AcrA Fusion Proteins That Act as Multidrug Efflux Transporters.Genomic analysis of the multi-drug-resistant clinical isolate Myroides odoratimimus PR63039.Genome Sequence of Riemerella anatipestifer Strain RCAD0122, a Multidrug-Resistant Isolate from Ducks.Tripartite efflux pumps: energy is required for dissociation, but not assembly or opening of the outer membrane channel of the pump Reviving Antibiotics: Efflux Pump Inhibitors That Interact with AcrA, a Membrane Fusion Protein of the AcrAB-TolC Multidrug Efflux Pump.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.Computational study of correlated domain motions in the AcrB efflux transporter.Evidence for the assembly of a bacterial tripartite multidrug pump with a stoichiometry of 3:6:3.Interaction between the α-barrel tip of Vibrio vulnificus TolC homologs and AcrA implies the adapter bridging model.Adaptor protein mediates dynamic pump assembly for bacterial metal efflux.Elastic network model-based normal mode analysis reveals the conformational couplings in the tripartite AcrAB-TolC multidrug efflux complex.Dynamics of Intact MexAB-OprM Efflux Pump: Focusing on the MexA-OprM Interface.Enhancing isoprenoid production through systematically assembling and modulating efflux pumps in Escherichia coli.Trans-envelope multidrug efflux pumps of Gram-negative bacteria and their synergism with the outer membrane barrier.Stoichiometry of the MexA-OprM binding, as investigated by blue native gel electrophoresis.

P2860

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P2860

Sequential mechanism of assembly of multidrug efflux pump AcrAB-TolC.

http://www.wikidata.org/entity/Q34863109

description

2011 nî lūn-bûn

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2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2011 թվականի ապրիլին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Sequential mechanism of assembly of multidrug efflux pump AcrAB-TolC.

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Sequential mechanism of assembly of multidrug efflux pump AcrAB-TolC.

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Sequential mechanism of assembly of multidrug efflux pump AcrAB-TolC.

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type

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Sequential mechanism of assembly of multidrug efflux pump AcrAB-TolC.

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Sequential mechanism of assembly of multidrug efflux pump AcrAB-TolC.

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Sequential mechanism of assembly of multidrug efflux pump AcrAB-TolC.

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Sequential mechanism of assembly of multidrug efflux pump AcrAB-TolC.

@ast

Sequential mechanism of assembly of multidrug efflux pump AcrAB-TolC.

@en

Sequential mechanism of assembly of multidrug efflux pump AcrAB-TolC.

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J.CHEMBIOL.2011.02.011

P1433

Chemistry and Biology

P1476

Sequential mechanism of assembly of multidrug efflux pump AcrAB-TolC.

@en

P2093

Elena B Tikhonova

http://www.w3.org/2001/XMLSchema#string

Helen I Zgurskaya

http://www.w3.org/2001/XMLSchema#string

Yoichi Yamada

http://www.w3.org/2001/XMLSchema#string

P2860

Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors

Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export

Crystal structure of bacterial multidrug efflux transporter AcrB

Assembly and Channel Opening in a Bacterial Drug Efflux Machine

The assembled structure of a complete tripartite bacterial multidrug efflux pump

Structures of sequential open states in a symmetrical opening transition of the TolC exit duct

Antibacterial resistance worldwide: causes, challenges and responses

Conformational flexibility in the multidrug efflux system protein AcrA.

Structure and function of TolC: the bacterial exit duct for proteins and drugs.

The C-terminal domain of AcrA is essential for the assembly and function of the multidrug efflux pump AcrAB-TolC.

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454-463

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scholarly article

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10.1016/J.CHEMBIOL.2011.02.011

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21513882

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