Interaction of zwitterionic penicillins with the OmpF channel facilitates their translocation. - Wikidata - awgldk - TriplyDB

Interaction of zwitterionic penicillins with the OmpF channel facilitates their translocation.

Interaction of zwitterionic penicillins with the OmpF channel facilitates their translocation.

http://www.wikidata.org/entity/Q34354272

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Altered antibiotic transport in OmpC mutants isolated from a series of clinical strains of multi-drug resistant E. coli The Binding of Antibiotics in OmpF Porin How beta-lactam antibiotics enter bacteria: a dialogue with the porins Porin involvement in cephalosporin and carbapenem resistance of Burkholderia pseudomallei Generation of artificial channels by multimerization of β-strands from natural porin.Phenotypic characterization of pore mutants of the Vibrio cholerae porin OmpU Outer membrane porin M35 of Moraxella catarrhalis mediates susceptibility to aminopenicillins Down-regulation of porin M35 in Moraxella catarrhalis by aminopenicillins and environmental factors and its potential contribution to the mechanism of resistance to aminopenicillins Implication of porins in beta-lactam resistance of Providencia stuartii.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.Permeation rates of penicillins indicate that Escherichia coli porins function principally as nonspecific channels Synthetic lipid membrane channels formed by designed DNA nanostructures Outer membrane permeability and antibiotic resistance.Broad-specificity efflux pumps and their role in multidrug resistance of Gram-negative bacteria.Controlling molecular transport through nanopores.Pharmacokinetics and pharmacodynamics of antibacterials, antifungals, and antivirals used most frequently in neonates and infants.Role of Electroosmosis in the Permeation of Neutral Molecules: CymA and Cyclodextrin as an Example.Anti-infectives in Drug Delivery-Overcoming the Gram-Negative Bacterial Cell Envelope.Orientation of the OmpF Porin in Planar Lipid Bilayers.Pseudomonas aeruginosa: targeting cell-wall metabolism for new antibacterial discovery and development.Exploiting the porin pathway for polar compound delivery into Gram-negative bacteria.Size and dynamics of the Vibrio cholerae porins OmpU and OmpT probed by polymer exclusion.Exploring bacterial outer membrane barrier to combat bad bugs.Understanding ion conductance on a molecular level: an all-atom modeling of the bacterial porin OmpF.Bridging timescales and length scales: from macroscopic flux to the molecular mechanism of antibiotic diffusion through porins.Uni-molecular detection and quantification of selected β-lactam antibiotics with a hybrid α-hemolysin protein pore.Improved detection of antibiotic compounds by bacterial reporter strains achieved by manipulations of membrane permeability and efflux capacity.Mechanisms of envelope permeability and antibiotic influx and efflux in Gram-negative bacteria.Interaction of protamine with gram-negative bacteria membranes: possible alternative mechanisms of internalization in Escherichia coli, Salmonella typhimurium and Pseudomonas aeruginosa.A mixture theory model of fluid and solute transport in the microvasculature of normal and malignant tissues. I. Theory.Amelioration of the Fitness Costs of Antibiotic Resistance Due To Reduced Outer Membrane Permeability by Upregulation of Alternative Porins.First-passage-time analysis of atomic-resolution simulations of the ionic transport in a bacterial porin.Mechanisms of ceftazidime and ciprofloxacin transport through porins in multidrug-resistance developed by extended-spectrum beta-lactamase E.coli strains.Interaction of cephalosporins with outer membrane channels of Escherichia coli. Revealing binding by fluorescence quenching and ion conductance fluctuations.Effects of conjugated and unconjugated bile acids on the activity of the Vibrio cholerae porin OmpT Ampicillin permeation across OmpF, the major outer-membrane channel in Analysis of fast channel blockage: revealing substrate binding in the microsecond range Antibiotic translocation through porins studied in planar lipid bilayers using parallel platforms

P2860

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P2860

Interaction of zwitterionic penicillins with the OmpF channel facilitates their translocation.

http://www.wikidata.org/entity/Q34354272

description

2005 nî lūn-bûn

@nan

2005 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

@wuu

name

Interaction of zwitterionic pe ...... cilitates their translocation.

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Interaction of zwitterionic pe ...... cilitates their translocation.

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Interaction of zwitterionic pe ...... cilitates their translocation.

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type

label

Interaction of zwitterionic pe ...... cilitates their translocation.

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Interaction of zwitterionic pe ...... cilitates their translocation.

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Interaction of zwitterionic pe ...... cilitates their translocation.

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prefLabel

Interaction of zwitterionic pe ...... cilitates their translocation.

@ast

Interaction of zwitterionic pe ...... cilitates their translocation.

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Interaction of zwitterionic pe ...... cilitates their translocation.

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P356

BIOPHYSJ.105.075192

P1433

Biophysical Journal

P1476

Interaction of zwitterionic pe ...... cilitates their translocation.

@en

P2093

Christophe Danelon

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

Ekaterina M Nestorovich

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Matteo Ceccarelli

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

Sergey M Bezrukov

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

P2860

Structure-based design guides the improved efficacy of deacylation transition state analogue inhibitors of TEM-1 beta-Lactamase(,)

Role of charged residues at the OmpF porin channel constriction probed by mutagenesis and simulation

Crystal structures explain functional properties of two E. coli porins

VMD: visual molecular dynamics

Molecular basis of bacterial outer membrane permeability revisited

Computer simulations of the OmpF porin from the outer membrane of Escherichia coli.

A fast in silico simulation of ion flux through the large-pore channel proteins.

Ion channels as molecular coulter counters to probe metabolite transport.

Steered molecular dynamics and mechanical functions of proteins.

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

P304

1617-1627

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scholarly article

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10.1529/BIOPHYSJ.105.075192

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5

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90

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Mathias Winterhalter

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2005-12-09T00:00:00Z

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7429691

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16339889

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1367313

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