نتایج جستجو برای: porin a

تعداد نتایج: 13432370  

Journal: :Journal of bacteriology 2006
Sandeep Tamber Martina M Ochs Robert E W Hancock

To circumvent the permeability barrier of its outer membrane, Pseudomonas aeruginosa has evolved a series of specific porins. These channels have binding sites for related classes of molecules that facilitate uptake under nutrient-limited conditions. Here, we report on the identification of a 19-member family of porins similar to the basic-amino-acid-specific porin OprD. The members of this fam...

Journal: :Antimicrobial agents and chemotherapy 1992
G Cornaglia L Guan R Fontana G Satta

The outer membrane permeability to meropenem and imipenem in Escherichia coli K-12 was investigated, and its porin-deficient mutants were transformed with a constructed vector carrying the carbapenem-hydrolyzing CphA metallo-beta-lactamase gene. By using the method of Zimmermann and Rosselet, meropenem was shown to penetrate through the outer membrane of E. coli K-12 five times faster than ceph...

Journal: :Biochimica et biophysica acta 1981
R Benz R E Hancock

The incorporation of porin protein F from the outer membrane of Pseudomonas aeruginosa into artificial lipid bilayers results in an increase of the membrane conductance by many orders of magnitude. The membrane conductance is caused by the formation of large ion-permeable channels with a single-channel conductance in the order of 5 nS for 1 M alkali chlorides. The conductance has an ohmic curre...

Journal: :The Journal of biological chemistry 2014
Seiji Kojima Hiroshi Nikaido

OmpF and OmpC porin channels are responsible for the passage of small hydrophilic solutes across the outer membrane of Escherichia coli. Although these channels are two of the most extensively studied porin channels, what had yet remained elusive was the reason why OmpC shows markedly lower permeability than OmpF, despite having little difference in its channel size. The OmpC channel, however, ...

Journal: :Journal of biochemistry 2004
Jalal A Al-jamal

Voltage-dependent anion-selective channel proteins (VDACs) are pore-forming proteins found in the outer mitochondrial membrane of all eukaryotes and in brain postsynaptic membranes. VDACs regulate anion fluxes of a series of metabolites including ATP, thus regulating mitochondrial metabolic functions. Hexokinase binds to porin. The mitochondrially bound hexokinase can greatly increase the rate ...

Journal: :Applied and environmental microbiology 2007
Nuria de María Angeles Guevara M Teresa Serra Isabel García-Luque Alfonso González-Sama Mario García de Lacoba M Rosario de Felipe Mercedes Fernández-Pascual

Application of glyphosate (N-[phosphonomethyl] glycine) to Bradyrhizobium sp. (Lupinus)-nodulated lupin plants caused modifications in the protein pattern of bacteroids. The most significant change was the presence of a 44-kDa polypeptide in bacteroids from plants treated with the higher doses of glyphosate employed (5 and 10 mM). The polypeptide has been characterized by the amino acid sequenc...

Journal: :Journal of bacteriology 1996
D R Blanco C I Champion M M Exner E S Shang J T Skare R E Hancock J N Miller M A Lovett

We recently reported the cloning and sequencing of the gene encoding a 31-kDa Treponema pallidum subsp. pallidum rare outer membrane porin protein, designated Tromp1 (D. R. Blanco, C. I. Champion, M. M. Exner, H. Erdjument-Bromage, R. E. W. Hancock, P. Tempst, J. N. Miller, and M. A. Lovett, J. Bacteriol. 177:3556-3562, 1995). Here, we report the stable expression of recombinant Tromp1 (rTromp1...

Journal: :Enfermedades infecciosas y microbiologia clinica 2017
Inmaculada López-Hernández Noemí Alonso Marta Fernández-Martínez Laura Zamorano Alba Rivera Antonio Oliver M Carmen Conejo Luis Martínez-Martínez Ferrán Navarro Alvaro Pascual

INTRODUCTION Antimicrobial resistance in Enterobacteriaceae is increasing worldwide and is making treating infections caused by multidrug-resistant Enterobacteriaceae a challenge. The use of β-lactam agents is compromised by microorganisms harboring extended-spectrum β-lactamases (ESBLs) and other mechanisms of resistance. Avibactam is a non β-lactam agent that inhibits clinically relevant β-la...

Journal: :Journal of bacteriology 1986
S K Armstrong T R Parr C D Parker R E Hancock

The major outer membrane protein of molecular weight 40,000 (the 40K protein) of a virulent isolate of Bordetella pertussis was purified to apparent homogeneity. The purified protein formed an oligomer band (of apparent molecular weight 90,000) on sodium dodecyl sulfate-polyacrylamide gels after solubilization at low temperatures. The porin function of this protein was characterized by the blac...

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