Identification and characterization of TriABC-OpmH, a triclosan efflux pump of Pseudomonas aeruginosa requiring two membrane fusion proteins
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Efflux-mediated drug resistance in bacteria: an updateRND-type drug efflux pumps from Gram-negative bacteria: molecular mechanism and inhibitionMechanism of coupling drug transport reactions located in two different membranesThe crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmRStructure of the AcrAB–TolC multidrug efflux pumpResponses of Pseudomonas aeruginosa to antimicrobialsCharacterization of a MexAB-OprM efflux system necessary for productive metabolism of Pseudomonas azelaica HBP1 on 2-hydroxybiphenylDraft genome sequences of eight bacteria isolated from the indoor environment: Staphylococcus capitis strain H36, S. capitis strain H65, S. cohnii strain H62, S. hominis strain H69, Microbacterium sp. strain H83, ...Complete genome sequence of the multiresistant taxonomic outlier Pseudomonas aeruginosa PA7.Microbial efflux systems and inhibitors: approaches to drug discovery and the challenge of clinical implementationArchitecture and roles of periplasmic adaptor proteins in tripartite efflux assembliesProfound perturbation induced by triclosan exposure in mouse gut microbiome: a less resilient microbial community with elevated antibiotic and metal resistomes.Differing ability to transport nonmetal substrates by two RND-type metal exporters.Evidence of MexT-independent overexpression of MexEF-OprN multidrug efflux pump of Pseudomonas aeruginosa in presence of metabolic stress.Functional relationships between the AcrA hairpin tip region and the TolC aperture tip region for the formation of the bacterial tripartite efflux pump AcrAB-TolC.High-level tolerance to triclosan may play a role in Pseudomonas aeruginosa antibiotic resistance in immunocompromised hosts: evidence from outbreak investigation.Structure and mechanism of RND-type multidrug efflux pumpsThe TetR-type MfsR protein of the integrative and conjugative element (ICE) ICEclc controls both a putative efflux system and initiation of ICE transfer.The impact of triclosan on the spread of antibiotic resistance in the environment.Funnel-like hexameric assembly of the periplasmic adapter protein in the tripartite multidrug efflux pump in gram-negative bacteria.Antibacterial-resistant Pseudomonas aeruginosa: clinical impact and complex regulation of chromosomally encoded resistance mechanisms.Structure of the tripartite multidrug efflux pump AcrAB-TolC suggests an alternative assembly modeThe challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria.RX-P873, a Novel Protein Synthesis Inhibitor, Accumulates in Human THP-1 Monocytes and Is Active against Intracellular Infections by Gram-Positive (Staphylococcus aureus) and Gram-Negative (Pseudomonas aeruginosa) Bacteria.Non-equivalent roles of two periplasmic subunits in the function and assembly of triclosan pump TriABC from Pseudomonas aeruginosa.Focus on the Outer Membrane Factor OprM, the Forgotten Player from Efflux Pumps Assemblies.Sclerotiamide: The First Non-Peptide-Based Natural Product Activator of Bacterial Caseinolytic Protease P.Assembly and transport mechanism of tripartite drug efflux systems.Complete Genome Sequence of the Triclosan- and Multidrug-Resistant Pseudomonas aeruginosa Strain B10W Isolated from Municipal Wastewater.Triclosan - an update.Molecular architecture of the bacterial tripartite multidrug efflux pump focusing on the adaptor bridging model.An overview of bacterial efflux pumps and computational approaches to study efflux pump inhibitors.Tripartite efflux pumps: energy is required for dissociation, but not assembly or opening of the outer membrane channel of the pumpThe Vibrio cholerae var regulon encodes a metallo-β-lactamase and an antibiotic efflux pump, which are regulated by VarR, a LysR-type transcription factor.Evidence for the assembly of a bacterial tripartite multidrug pump with a stoichiometry of 3:6:3.Characterization of all RND-type multidrug efflux transporters in Vibrio parahaemolyticus.Opening the Channel: the Two Functional Interfaces of Pseudomonas aeruginosa OpmH with the Triclosan Efflux Pump TriABC.Comparison of transcriptomes of wild-type and isothiazolone-resistant Pseudomonas aeruginosa by using RNA-seq.Antimicrobial targets localize to the extracellular vesicle-associated proteome of Pseudomonas aeruginosa grown in a biofilm.Triclosan can select for an AdeIJK-overexpressing mutant of Acinetobacter baumannii ATCC 17978 that displays reduced susceptibility to multiple antibiotics.
P2860
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P2860
Identification and characterization of TriABC-OpmH, a triclosan efflux pump of Pseudomonas aeruginosa requiring two membrane fusion proteins
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh
2007年學術文章
@zh-hant
name
Identification and characteriz ...... g two membrane fusion proteins
@ast
Identification and characteriz ...... g two membrane fusion proteins
@en
type
label
Identification and characteriz ...... g two membrane fusion proteins
@ast
Identification and characteriz ...... g two membrane fusion proteins
@en
prefLabel
Identification and characteriz ...... g two membrane fusion proteins
@ast
Identification and characteriz ...... g two membrane fusion proteins
@en
P2093
P2860
P356
P1476
Identification and characteriz ...... g two membrane fusion proteins
@en
P2093
Herbert P Schweizer
Margarita Gomez-Escalada
Swati Joshi
Takehiko Mima
P2860
P304
P356
10.1128/JB.00850-07
P407
P577
2007-08-24T00:00:00Z