نتایج جستجو برای: porins

تعداد نتایج: 718  

2012
Stefania Galdiero Annarita Falanga Marco Cantisani Rossella Tarallo Maria Elena Della Pepa Virginia D’Oriano Massimiliano Galdiero

Gram negative bacteria have evolved many mechanisms of attaching to and invading host epithelial and immune cells. In particular, many outer membrane proteins (OMPs) are involved in this initial interaction between the pathogen and their host. The outer membrane (OM) of Gram-negative bacteria performs the crucial role of providing an extra layer of protection to the organism without compromisin...

Journal: :Infection and immunity 1997
V Cusumano M A Tufano G Mancuso M Carbone F Rossano M T Fera F A Ciliberti E Ruocco R A Merendino G Teti

The aim of this study was to examine the ability of Pseudomonas aeruginosa components to induce release of cytokines from human leukocytes. Human whole-blood cultures were incubated with several concentrations of purified P. aeruginosa products, including porins, exomucopolysaccharide, lipopolysaccharide, and toxin A. Supernatants were assayed for tumor necrosis factor alpha (TNF-alpha) and int...

Journal: :Antimicrobial agents and chemotherapy 2011
Laura García-Sureda Antonio Doménech-Sánchez Mariette Barbier Carlos Juan Joan Gascó Sebastián Albertí

Clinical isolates of Klebsiella pneumoniae resistant to carbapenems are being isolated with increasing frequency. Loss of the expression of the major nonspecific porins OmpK35/36 is a frequent feature in these isolates. In this study, we looked for porins that could compensate for the loss of the major porins in carbapenem-resistant organisms. Comparison of the outer membrane proteins from two ...

Journal: :Journal of bacteriology 1998
D A Fajardo J Cheung C Ito E Sugawara H Nikaido R Misra

A novel porin, OmpG, is produced in response to a chromosomal mutation termed cog-192. Molecular characterization of cog-192 revealed that it is a large chromosomal deletion extending from the 3' end of pspA through to the 5' end of an open reading frame located immediately upstream of ompG. As a result of this 13.1-kb deletion, the expression of ompG was placed under the control of the pspA pr...

Journal: :Applied sciences 2023

Gram-negative bacteria can resist antibiotics by changing the permeability via their outer membrane. These have a complex cell envelope that incorporates an membrane separating periplasm from external environment. This contains many protein channels, also known as porins or nanopores, which mainly allow influx of hydrophilic compounds, including antibiotics. One probable way may possibly develo...

Journal: :iranian journal of basic medical sciences 0
mohammad ali atlasi anatomical sciences research center, kashan university of medical sciences, kashan, iran jose luis perez velazquez department of neurology and pediatrics, the hospital for sick children, brain and behavior programme, university of toronto, ontario, canada

objective (s) porin is a mitochondrial outer membrane channel, which usually functions as the pathway for the movement of various substances in and out of the mitochondria and is considered to be a component of the permeability transition (pt) pore complex that plays a role in the pt. we addressed the hypothesis that porin interacts with other mitochondrial proteins after ischemic injury. mater...

2015
Thomas Ferenci Katherine Phan Jonathan Iredell Sally Partridge

Variations in porin proteins are common in Gram-negative pathogens. Altered or absent porins reduce access of polar antibiotics across the outer membrane and can thus contribute to antibiotic resistance. Reduced permeability has a cost however, in lowering access to nutrients. This trade-off between permeability and nutritional competence is the source of considerable natural variation in porin...

Journal: :Current opinion in microbiology 1998
P E Klebba S M Newton

Porins mediate the uptake of nutrients across the outer membrane of Gram-negative bacteria. For general porins like OmpF, electrophysicoloigcal experiments now establish that the charged residues within their channels primarily modulate pore selectivity, rather than voltage-gated switching between open and closed states. Recent studies on the maltoporin, LamB, solidify the importance of its 'gr...

Journal: :FEMS Microbiology Letters 2001

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