Designed to penetrate: time-resolved interaction of single antibiotic molecules with bacterial pores. - Wikidata - awgldk - TriplyDB

Designed to penetrate: time-resolved interaction of single antibiotic molecules with bacterial pores.

Designed to penetrate: time-resolved interaction of single antibiotic molecules with bacterial pores.

http://www.wikidata.org/entity/Q34075592

about

Altered antibiotic transport in OmpC mutants isolated from a series of clinical strains of multi-drug resistant E. coli Nanopores: maltoporin channel as a sensor for maltodextrin and lambda-phage Obstructing toxin pathways by targeted pore blockage The Binding of Antibiotics in OmpF Porin Toward Understanding the Outer Membrane Uptake of Small Molecules by Pseudomonas aeruginosa How beta-lactam antibiotics enter bacteria: a dialogue with the porins Porin involvement in cephalosporin and carbapenem resistance of Burkholderia pseudomallei Molecular basis of bacterial outer membrane permeability revisited Generation of artificial channels by multimerization of β-strands from natural porin.Redesign of a plugged beta-barrel membrane protein.Phenotypic characterization of pore mutants of the Vibrio cholerae porin OmpU High resolution crystal structures and molecular dynamics studies reveal substrate binding in the porin Omp32.Outer membrane porin M35 of Moraxella catarrhalis mediates susceptibility to aminopenicillins Enhancement of transport selectivity through nano-channels by non-specific competition.Pseudomonas aeruginosa porin OprF: properties of the channel Mitochondrial ion channels as therapeutic targets.Blockage of anthrax PA63 pore by a multicharged high-affinity toxin inhibitor.Blocking anthrax lethal toxin at the protective antigen channel by using structure-inspired drug design.Down-regulation of porin M35 in Moraxella catarrhalis by aminopenicillins and environmental factors and its potential contribution to the mechanism of resistance to aminopenicillins Residue ionization and ion transport through OmpF channels.Implication of porins in beta-lactam resistance of Providencia stuartii.Salting out the ionic selectivity of a wide channel: the asymmetry of OmpF Optimizing transport of metabolites through large channels: molecular sieves with and without binding.High salt concentrations increase permeability through OmpC channels of Escherichia coli.New insights into the mechanism of permeation through large channels Interaction of zwitterionic penicillins with the OmpF channel facilitates their translocation.Genome-wide analysis of the Pho regulon in a pstCA mutant of Citrobacter rodentium.Is MAC the knife that cuts cytochrome c from mitochondria during apoptosis?Dynamical determinants of drug-inducible gene expression in a single bacterium.Molecular transport through channels and pores: effects of in-channel interactions and blocking.Enhancing molecular flux through nanopores by means of attractive interactions Applications of biological pores in nanomedicine, sensing, and nanoelectronics Structure, Dynamics, and Substrate Specificity of the OprO Porin from Pseudomonas aeruginosa.The fitness costs and trade-off shapes associated with the exclusion of nine antibiotics by OmpF porin channels.Enzyme screening with synthetic multifunctional pores: focus on biopolymers.Noise in solid-state nanopores.Inspection of the engineered FhuA ΔC/Δ4L protein nanopore by polymer exclusion.Optimizing diffusive transport through a synthetic membrane channel Structure, Function and Regulation of Outer Membrane Proteins Involved in Drug Transport in Enterobactericeae: the OmpF/C - TolC Case Connexin channel permeability to cytoplasmic molecules.

P2860

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P2860

Designed to penetrate: time-resolved interaction of single antibiotic molecules with bacterial pores.

http://www.wikidata.org/entity/Q34075592

description

2002 nî lūn-bûn

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2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2002 թվականի հուլիսին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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Designed to penetrate: time-re ...... olecules with bacterial pores.

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Designed to penetrate: time-re ...... olecules with bacterial pores.

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Designed to penetrate: time-re ...... olecules with bacterial pores.

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Designed to penetrate: time-re ...... olecules with bacterial pores.

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Proceedings of the National Academy of Sciences of the United States of America

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Designed to penetrate: time-re ...... olecules with bacterial pores.

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P2093

Christophe Danelon

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Ekaterina M Nestorovich

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Sergey M Bezrukov

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P2860

Characterization of individual polynucleotide molecules using a membrane channel

Crystal structures explain functional properties of two E. coli porins

Structural and functional alterations of a colicin-resistant mutant of OmpF porin from Escherichia coli

Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

General and specific porins from bacterial outer membranes.

Molecular architecture and electrostatic properties of a bacterial porin.

The three-dimensional structure of porin from Rhodobacter capsulatus at 3 A resolution.

Ion channels as molecular coulter counters to probe metabolite transport.

Molecular mechanisms that confer antibacterial drug resistance.

Substitutions in the eyelet region disrupt cefepime diffusion through the Escherichia coli OmpF channel

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9789-9794

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scholarly article

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10.1073/PNAS.152206799

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15

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99

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Mathias Winterhalter

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2002-07-15T00:00:00Z

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11260250

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12119404

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125017

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