Structural basis for the inhibition of bacterial multidrug exporters - Wikidata - awgldk - TriplyDB

Structural basis for the inhibition of bacterial multidrug exporters

Structural basis for the inhibition of bacterial multidrug exporters

http://www.wikidata.org/entity/Q27685149

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RND-type drug eﬄux pumps from Gram-negative bacteria: molecular mechanism and inhibition Recent advances toward a molecular mechanism of efflux pump inhibition Understanding the structural mechanisms of antibiotic resistance sets the platform for new discovery Structural basis of RND-type multidrug exporters Identification of natural compound inhibitors for multidrug efflux pumps of Escherichia coli and Pseudomonas aeruginosa using in silico high-throughput virtual screening and in vitro validation Protein modeling: what happened to the "protein structure gap"?A data-driven approach to modeling the tripartite structure of multidrug resistance efflux pumps.Current Advances in Developing Inhibitors of Bacterial Multidrug Efflux Pumps Crystal structure of the Neisseria gonorrhoeae MtrD inner membrane multidrug efflux pump.Molecular mechanism of MBX2319 inhibition of Escherichia coli AcrB multidrug efflux pump and comparison with other inhibitors Multidrug efflux pumps from Enterobacteriaceae, Vibrio cholerae and Staphylococcus aureus bacterial food pathogens Coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump AcrB AcrB drug-binding pocket substitution confers clinically relevant resistance and altered substrate specificity.Structure-activity relationships of a novel pyranopyridine series of Gram-negative bacterial efflux pump inhibitors.The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria.Interaction of antibacterial compounds with RND eﬄux pumps in Pseudomonas aeruginosa The Structure and Interactions of Periplasmic Domains of Crucial MmpL Membrane Proteins from Mycobacterium tuberculosis.Stepwise substrate translocation mechanism revealed by free energy calculations of doxorubicin in the multidrug transporter AcrB.Genome-wide mapping of mutations at single-nucleotide resolution for protein, metabolic and genome engineering.Aminoacyl β-naphthylamides as substrates and modulators of AcrB multidrug efflux pump Mechanisms of Resistance to Aminoglycoside Antibiotics: Overview and Perspectives Tripartite assembly of RND multidrug efflux pumps.Permeability Barrier of Gram-Negative Cell Envelopes and Approaches To Bypass It.Focus on the Outer Membrane Factor OprM, the Forgotten Player from Efflux Pumps Assemblies.Molecular basis for inhibition of AcrB multidrug efflux pump by novel and powerful pyranopyridine derivatives Structural basis for the blockade of MATE multidrug efflux pumps Structures of multidrug and toxic compound extrusion transporters and their mechanistic implications.Structure of human Niemann-Pick C1 protein.Berberine Is a Novel Type Efflux Inhibitor Which Attenuates the MexXY-Mediated Aminoglycoside Resistance in Pseudomonas aeruginosa Design of New Antibacterial Enhancers Based on AcrB's Structure and the Evaluation of Their Antibacterial Enhancement Activity.Multidrug efflux pumps in Gram-negative bacteria and their role in antibiotic resistance.An overview of bacterial efflux pumps and computational approaches to study efflux pump inhibitors.Multidrug Efflux Systems in Microaerobic and Anaerobic Bacteria Effect of site-directed mutations in multidrug efflux pump AcrB examined by quantitative efflux assays.Targeting efflux pumps to overcome antifungal drug resistance.Optimization of a novel series of pyranopyridine RND efflux pump inhibitors.Structural and mechanistic diversity of multidrug transporters.Transport of lipophilic carboxylates is mediated by transmembrane helix 2 in multidrug transporter AcrB.Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 and Ebola virus interactions.Molecular Epidemiology of Mutations in Antimicrobial Resistance Loci of Pseudomonas aeruginosa Isolates from Airways of Cystic Fibrosis Patients.

P2860

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P2860

Structural basis for the inhibition of bacterial multidrug exporters

http://www.wikidata.org/entity/Q27685149

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2013 nî lūn-bûn

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2013 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

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2013 թվականի օգոստոսին հրատարակված գիտական հոդված

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2013年の論文

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年學術文章

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Structural basis for the inhibition of bacterial multidrug exporters

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Structural basis for the inhibition of bacterial multidrug exporters

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Structural basis for the inhibition of bacterial multidrug exporters

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Structural basis for the inhibition of bacterial multidrug exporters

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Structural basis for the inhibition of bacterial multidrug exporters

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Structural basis for the inhibition of bacterial multidrug exporters

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Structural basis for the inhibition of bacterial multidrug exporters

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Structural basis for the inhibition of bacterial multidrug exporters

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Structural basis for the inhibition of bacterial multidrug exporters

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Structural basis for the inhibition of bacterial multidrug exporters

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Akihito Yamaguchi

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

Chikahiro Nagata

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

Katsuhiko Hayashi

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

Kazuki Hoshino

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

Keisuke Sakurai

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

Kunihiko Nishino

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

Ryosuke Nakashima

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

Seiji Yamasaki

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

Yoshikuni Onodera

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P2860

The SWISS-MODEL Repository and associated resources

Processing of X-ray diffraction data collected in oscillation mode

Crystal structure of bacterial multidrug efflux transporter AcrB

The assembled structure of a complete tripartite bacterial multidrug efflux pump

Crystal structure of the multidrug exporter MexB from Pseudomonas aeruginosa

Transport of drugs by the multidrug transporter AcrB involves an access and a deep binding pocket that are separated by a switch-loop

The complete genome sequence of Escherichia coli K-12

Evaluation of multidrug efflux pump inhibitors by a new method using microfluidic channels

Contribution of the MexX-MexY-oprM efflux system to intrinsic resistance in Pseudomonas aeruginosa

Mechanism of recognition of compounds of diverse structures by the multidrug efflux pump AcrB of Escherichia coli.

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10.1038/NATURE12300

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7460

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500

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