Membrane topology of a multidrug efflux transporter, AcrB, in Escherichia coli.
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Crystal structure of bacterial multidrug efflux transporter AcrBAlgorithms for incorporating prior topological information in HMMs: application to transmembrane proteinsTransmembrane protein topology mapping by the substituted cysteine accessibility method (SCAM(TM)): application to lipid-specific membrane protein topogenesisCharacterization of a resistance-nodulation-cell division transporter system associated with the syr-syp genomic island of Pseudomonas syringae pv. syringae.Conformation of the AcrB multidrug efflux pump in mutants of the putative proton relay pathway.Structure and function of efflux pumps that confer resistance to drugsPlasmid-encoded multidrug efflux pump conferring resistance to olaquindox in Escherichia coli.AcrAB-TolC directs efflux-mediated multidrug resistance in Salmonella enterica serovar typhimurium DT104.AcrB-AcrA Fusion Proteins That Act as Multidrug Efflux Transporters.Evidence of a Substrate-Discriminating Entrance Channel in the Lower Porter Domain of the Multidrug Resistance Efflux Pump AcrBEffects of efflux transporter genes on susceptibility of Escherichia coli to tigecycline (GAR-936).Random mutagenesis of the multidrug transporter AcrB from Escherichia coli for identification of putative target residues of efflux pump inhibitorsOxa1-ribosome complexes coordinate the assembly of cytochrome C oxidase in mitochondria.Study of polytopic membrane protein topological organization as a function of membrane lipid composition.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.Membrane topology of ABC-type macrolide antibiotic exporter MacB in Escherichia coli.Extramembrane central pore of multidrug exporter AcrB in Escherichia coli plays an important role in drug transport.Design, synthesis and evaluation of the antibacterial enhancement activities of amino dihydroartemisinin derivatives.Amino Acid Substitution in the Major Multidrug Efflux Transporter Protein AcrB Contributes to Low Susceptibility to Azithromycin in Haemophilus influenzae.Crystallographic Analysis of Drug and Inhibitor-Binding Structure of RND-Type Multidrug Exporter AcrB in Physiologically Relevant Asymmetric Crystals.
P2860
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P2860
Membrane topology of a multidrug efflux transporter, AcrB, in Escherichia coli.
description
2002 nî lūn-bûn
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2002年の論文
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2002年学术文章
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2002年学术文章
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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
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2002年學術文章
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name
Membrane topology of a multidrug efflux transporter, AcrB, in Escherichia coli.
@en
Membrane topology of a multidrug efflux transporter, AcrB, in Escherichia coli.
@nl
type
label
Membrane topology of a multidrug efflux transporter, AcrB, in Escherichia coli.
@en
Membrane topology of a multidrug efflux transporter, AcrB, in Escherichia coli.
@nl
prefLabel
Membrane topology of a multidrug efflux transporter, AcrB, in Escherichia coli.
@en
Membrane topology of a multidrug efflux transporter, AcrB, in Escherichia coli.
@nl
P2093
P1476
Membrane topology of a multidrug efflux transporter, AcrB, in Escherichia coli.
@en
P2093
Akihito Yamaguchi
Erika Fujihira
Norihisa Tamura
P304
P356
10.1093/OXFORDJOURNALS.JBCHEM.A003069
P577
2002-01-01T00:00:00Z