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注意：仅列出部分参考文献，下载原文获取全部文献信息。Multidrug Resistance in Bacteria
Hiroshi Nikaido
ANNUAL REVIEW OF BIOCHEMISTRY (2009)
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Covalently Linked Trimer of the AcrB Multidrug Efflux Pump Provides Support for the Functional Rotating Mechanism
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A coordinated network of transporters with overlapping specificities provides a robust survival strategy
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Kinetic behavior of the major multidrug efflux pump AcrB of Escherichia coli
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Site-Directed Mutagenesis Reveals Putative Substrate Binding Residues in the Escherichia coli RND Efflux Pump AcrB
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Engineered disulfide bonds support the functional rotation mechanism of multidrug efflux pump AcrB
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NATURE STRUCTURAL & MOLECULAR BIOLOGY (2008)
Site-directed disulfide cross-linking shows that cleft flexibility in the periplasmic domain is needed for the multidrug efflux pump AcrB of Eschetichia coli
Yumiko Takatsuka et al.
JOURNAL OF BACTERIOLOGY (2007)
Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors
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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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JOURNAL OF BACTERIOLOGY (2006)
Conformation of the AcrB multidrug efflux pump in mutants of the putative proton relay pathway
Chih-Chia Su et al.
JOURNAL OF BACTERIOLOGY (2006)
Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
Satoshi Murakami et al.
NATURE (2006)
Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism
Markus A. Seeger et al.
SCIENCE (2006)
A periplasmic drug-binding site of the AcrB multidrug efflux pump: a crystallographic and site-directed mutagenesis study
EW Yu et al.
JOURNAL OF BACTERIOLOGY (2005)
Selected arylpiperazines are capable of reversing multidrug resistance in Escherichia coli overexpressing RND efflux pumps
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ANTIMICROBIAL AGENTS AND CHEMOTHERAPY (2005)
Structural mechanism of the simultaneous binding of two drugs to a multidrug-binding protein
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EMBO JOURNAL (2004)
Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump
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Structure validation by Cα geometry:: φ,ψ and Cβ deviation
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PROTEINS-STRUCTURE FUNCTION AND GENETICS (2003)
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
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Crystal structure of bacterial multidrug efflux transporter AcrB
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The BaeSR two-component regulatory system activates transcription of the yegMNOB (mdtABCD) transporter gene cluster in Escherichia coli and increases its resistance to novobiocin and deoxycholate
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The putative response regulator BaeR stimulates multidrug resistance of Escherichia coli via a novel multidrug exporter system, MdtABC
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Mystery of multidrug transporters: the answer can be simple
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Identification and characterization of inhibitors of multidrug resistance efflux pumps in Pseudomonas aeruginosa: Novel agents for combination therapy
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Entry into and release of solvents by Escherichia coli in an organic-aqueous two-liquid-phase system and substrate specificity of the AcrAB-TolC solvent-extruding pump
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