Results 21 to 30 of about 28,026 (256)

Porin from Rhodopseudomonas sphaeroides [PDF]

open access: yesJournal of Bacteriology, 1984
A protein homooligomer was purified from both the cell envelope fractions and the saline extracts of Rhodopseudomonas sphaeroides cells. This oligomer exhibited strong porin activity when reconstituted into proteoliposomes with egg phosphatidylcholine. In the saline extracts of both chemotrophically and phototrophically grown cells, the porin oligomer ...
J, Weckesser, L S, Zalman, H, Nikaido
openaire   +2 more sources

The porin and the permeating antibiotic: A selective diffusion barrier in gram-negative bacteria [PDF]

open access: yes, 2008
Gram-negative bacteria are responsible for a large proportion of antibiotic resistant bacterial diseases. These bacteria have a complex cell envelope that comprises an outer membrane and an inner membrane that delimit the periplasm.
A Baslé   +95 more
core   +1 more source

Distinct Roles of Outer Membrane Porins in Antibiotic Resistance and Membrane Integrity in Escherichia coli

open access: yesFrontiers in Microbiology, 2019
A defining characteristic of Gram-negative bacteria is the presence of an outer membrane, which functions as an additional barrier inhibiting the penetration of toxic chemicals, such as antibiotics.
Umji Choi, Chang-Ro Lee
doaj   +1 more source

The Small RNA NcS25 Regulates Biological Amine-Transporting Outer Membrane Porin BCAL3473 in Burkholderia cenocepacia

open access: yesmSphere, 2023
Regulation of porin expression in bacteria is complex and often involves small-RNA regulators. Several small-RNA regulators have been described for Burkholderia cenocepacia, and this study aimed to characterize the biological role of the conserved small ...
Andrea M. Sass, Tom Coenye
doaj   +1 more source

Single-channel measurements of an N-acetylneuraminic acid-inducible outer membrane channel in Escherichia coli [PDF]

open access: yes, 2012
NanC is an Escherichia coli outer membrane protein involved in sialic acid (Neu5Ac, i.e., N-acetylneuraminic acid) uptake. Expression of the NanC gene is induced and controlled by Neu5Ac. The transport mechanism of Neu5Ac is not known.
Eisenberg, Bob   +4 more
core   +1 more source

Porins of Brucella species [PDF]

open access: yesInfection and Immunity, 1984
The outer membrane of Brucella species contains two major proteins, denoted as group 2 and group 3 proteins (Verstreate et al., Infect. Immun. 35:979-989, 1982). We reconstituted proteoliposomes from the purified proteins and egg phosphatidylcholine and showed that group 2 proteins, but not a group 3 protein, had the porin activity. The influx rates of
J T, Douglas   +4 more
openaire   +2 more sources

Salmonella Typhi Porins OmpC and OmpF Are Potent Adjuvants for T-Dependent and T-Independent Antigens

open access: yesFrontiers in Immunology, 2017
Several microbial components, such as bacterial DNA and flagellin, have been used as experimental vaccine adjuvants because of their inherent capacity to efficiently activate innate immune responses.
Marisol Pérez-Toledo   +15 more
doaj   +1 more source

Molecular genetic characteristics of the carbapenem resistant Klebsiella pneumoniae KP254 strain as a representative of the highly virulent strain evolutionary branch

open access: yesИнфекция и иммунитет, 2021
Here we provide molecular and genetic characteristics of the Klebsiella pneumoniae KP254 clinical strain belonging to clonal group 23 based on the genome-wide sequencing data.
A. E. Alekseeva   +2 more
doaj   +1 more source

Biophysical Effects Of Ion Concenteration On The Affinity Between Nanopore, OmpF Lumen and Passing Nucleotide [PDF]

open access: yes, 2010
OmpF an outer-membrane porin channel of _E. Coli_ posses beta-barrel structure, whose conductivity and gating phenomena are affected by changes in pH, salt concentration and so on. The distribution of amino acids in OmpF induces a non homologous electric
Hamid Mobasheri, Saeid Hadi
core   +2 more sources

Porin fromThiobacillus versutus [PDF]

open access: yesFEMS Microbiology Letters, 1989
The porin of Thiobacillus versutus IFO 14567 was isolated by extraction of cell-envelopes with sodium dodecyl sulfate. It exhibited strong porin-activity after reconstitution into artificial lipid bilayer membranes. The diameter of the pore was determined as 1.6 nm, with a weak selectivity for cations being observed. The porin migrated as a single band
D, Woitzik   +3 more
openaire   +2 more sources

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