نتایج جستجو برای: پروتیین ompf

تعداد نتایج: 1692  

Journal: :Antimicrobial agents and chemotherapy 2000
L Martínez-Martínez M C Conejo A Pascual S Hernández-Allés S Ballesta E Ramírez De Arellano-Ramos V J Benedí E J Perea

Forty clonally related clinical isolates of Escherichia coli from hospitalized patients were resistant to cefoxitin (MICs, >256 microg/ml) and ceftazidime (MICs, 32 to 256 microg/ml) and were intermediate or resistant to cefotaxime (MICs, 16 to 128 microg/ml) but susceptible to both cefepime (MICs, 0.5 to 2 microg/ml) and imipenem (MICs, 0.125 to 0.25 microg/ml). Resistance to beta-lactams was ...

2012
Annemarie Brauser Indra Schroeder Thomas Gutsmann Cristian Cosentino Anna Moroni Ulf-Peter Hansen Mathias Winterhalter

Antibiotics have to penetrate the outer membrane to enter Gram-negative bacteria. One possible pathway is the diffusion through the lipid phase (Ribeiro et al., 2011), especially for the hydrophobic first-generation quinolones (Delcour, 2009). However, the outer membrane also contains a plethora of channel-forming pro teins called porins. Recent studies on multidrug resistance revealed modified...

2003
KEVIN LIN ALICE WANG

UV-induced mutation frequency and cell survivability was examined in Escherichia coli K12 strains. The effects of UV (254nm) induced damage on deoxyribonucleic acid (DNA) was investigated using two protocols termed Direct-Plate Irradiation (DPI) and Liquid-Plate Irradiation (LPI). A biological system needed to be designed to facilitate future experiments involving UV and gene mutation frequenci...

Journal: :Frontiers in bioscience : a journal and virtual library 2004
Stanislav D Zakharov William A Cramer

Colicins and phages parasitize outer membrane receptors whose physiological purpose is the transport of metabolites, metals, vitamins, and sugars. From mutagenesis studies, it is known that several colicins require the function of two outer membrane protein (Omp) receptors for cytotoxicity. A formidable list of problems associated with an understanding of a two receptor mechanism for colicin tr...

Journal: :Journal of bacteriology 1984
R Morona U Henning

The Escherichia coli K-12 outer membrane protein OmpA functions as the receptor for bacteriophage Ox2. We isolated a host range mutant of this phage which was able to grow on an Ox2-resistant ompA mutant producing an altered OmpA protein. From this mutant, Ox2h5, a second-step host range mutant was recovered which formed turbid plaques on a strain completely lacking the OmpA protein. From one o...

Journal: :Physical chemistry chemical physics : PCCP 2009
Marcel Aguilella-Arzo Andreu Andrio Vicente M Aguilella Antonio Alcaraz

Water molecules in confined geometries like nanopores and biological ion channels exhibit structural and dynamical properties very different from those found in free solution. Protein channels that open aqueous pores through biological membranes provide a complex spatial and electrostatic environment that decreases the translational and rotational mobility of water molecules, thus altering the ...

Journal: :Molecular microbiology 2015
Zhi-Soon Chong Wei-Fen Woo Shu-Sin Chng

Gram-negative bacteria can survive in harsh environments in part because the asymmetric outer membrane (OM) hinders the entry of toxic compounds. Lipid asymmetry is established by having phospholipids (PLs) confined to the inner leaflet of the membrane and lipopolysaccharides (LPS) to the outer leaflet. Perturbation of OM lipid asymmetry, characterized by PL accumulation in the outer leaflet, d...

Journal: :Journal of bacteriology 2007
Melissa Pagel Valérie Simonet Jie Li Mathilde Lallemand Brian Lauman Anne H Delcour

General-diffusion porins form large beta-barrel channels that control the permeability of the outer membrane of gram-negative bacteria to nutrients, some antibiotics, and external signals. Here, we have analyzed the effects of mutations in the OmpU porin of Vibrio cholerae at conserved residues that are known to affect pore properties in the Escherichia coli porins OmpF and OmpC. Various phenot...

Journal: :Antimicrobial agents and chemotherapy 1983
A Jaffé Y A Chabbert E Derlot

beta-Lactam-resistant mutants of Escherichia coli K-12 were selected by using 12 different beta-lactam derivatives. The mutants fell into three categories showing (i) altered permeation through reduction or loss of outer membrane porin proteins (including ompF, ompR, and envZ alleles); (ii) increase in the rate of synthesis of chromosomally mediated beta-lactamase; or (iii) defective synthesis ...

Journal: :Nano letters 2006
Pavel Broz Sergey Driamov Joerg Ziegler Nadav Ben-Haim Stephan Marsch Wolfgang Meier Patrick Hunziker

To develop an intelligent sensor-effector functionality on the nanoscale, a pH-switchable, controlled nanoreactor based on amphiphilic copolymer membranes was built. The nanovesicles were equipped with bacterial transmembrane ompF pore proteins and the pH-sensitive enzyme acid phosphatase, resulting in a switchable substrate processing at pH 4-6.5. Ideal pH and substrate concentrations for the ...

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