Extramembrane central pore of multidrug exporter AcrB in Escherichia coli plays an important role in drug transport.
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Efflux-mediated drug resistance in bacteria: an updateDrug export pathway of multidrug exporter AcrB revealed by DARPin inhibitorsFunctional relevance of AcrB Trimerization in pump assembly and substrate bindingThe role of trimerization in the osmoregulated betaine transporter BetPSmall molecule functional analogs of peptides that inhibit lambda site-specific recombination and bind Holliday junctionsβ-Lactam selectivity of multidrug transporters AcrB and AcrD resides in the proximal binding pocket.A periplasmic drug-binding site of the AcrB multidrug efflux pump: a crystallographic and site-directed mutagenesis study.Structure and mechanism of RND-type multidrug efflux pumpsQuantitative modeling of chloride conductance in yeast TRK potassium transportersMechanisms of RND multidrug efflux pumpsThe challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria.Interaction of antibacterial compounds with RND efflux pumps in Pseudomonas aeruginosaVacuuming the periplasm.Modeling the tripartite drug efflux pump archetype: structural and functional studies of the macromolecular constituents reveal more than their names imply.Pentanol and Benzyl Alcohol Attack Bacterial Surface Structures DifferentlyStructural and functional importance of transmembrane domain 3 (TM3) in the aspartate:alanine antiporter AspT: topology and function of the residues of TM3 and oligomerization of AspTAssembly and transport mechanism of tripartite drug efflux systems.AcrB-AcrA Fusion Proteins That Act as Multidrug Efflux Transporters.The chromosomally encoded cation diffusion facilitator proteins DmeF and FieF from Wautersia metallidurans CH34 are transporters of broad metal specificity.Mutations in the central cavity and periplasmic domain affect efflux activity of the resistance-nodulation-division pump EmhB from Pseudomonas fluorescens cLP6a.Substrate path in the AcrB multidrug efflux pump of Escherichia coli.The outer membrane TolC-like channel HgdD is part of tripartite resistance-nodulation-cell division (RND) efflux systems conferring multiple-drug resistance in the Cyanobacterium Anabaena sp. PCC7120.Optimized Nile Red efflux assay of AcrAB-TolC multidrug efflux system shows competition between substratesCrystal structures of a multidrug transporter reveal a functionally rotating mechanism.Adaptive laboratory evolution of cadmium tolerance in sp. PCC 6803
P2860
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P2860
Extramembrane central pore of multidrug exporter AcrB in Escherichia coli plays an important role in drug transport.
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2003 nî lūn-bûn
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2003年の論文
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name
Extramembrane central pore of ...... ortant role in drug transport.
@en
Extramembrane central pore of ...... ortant role in drug transport.
@nl
type
label
Extramembrane central pore of ...... ortant role in drug transport.
@en
Extramembrane central pore of ...... ortant role in drug transport.
@nl
prefLabel
Extramembrane central pore of ...... ortant role in drug transport.
@en
Extramembrane central pore of ...... ortant role in drug transport.
@nl
P2093
P2860
P356
P1476
Extramembrane central pore of ...... ortant role in drug transport.
@en
P2093
Akihito Yamaguchi
Asami Saito
Norihisa Tamura
Takahiro Hirata
P2860
P304
P356
10.1074/JBC.M308893200
P407
P577
2003-10-23T00:00:00Z