نتایج جستجو برای: porin a

تعداد نتایج: 13432370  

Journal: :Infection and immunity 1995
P Lutwyche M M Exner R E Hancock T J Trust

A protein with an apparent M(r) of 28,000 was isolated from outer membrane preparations of Aeromonas salmonicida A440. The protein was tested for the ability to form pores, using a planar lipid bilayer model membrane system. The protein appeared to be a monomer with a single-channel conductance in 1.0 M KCl of 1.96 nS and a cation/anion permeability ratio of 2.91 +/- 0.68. These data show that ...

Journal: :FEBS letters 1982
H Freitag G Genchi R Benz F Palmieri W Neupert

Mitochondrial porin forms channels in the outer mitochondrial membrane which allows the passage of molecules with diameters up to -20 A [l-6]. We have described the purification of this protein [7] from purified outer membranes by differential extraction with detergents and anionic exchange chromatography. The purified porin displayed an app. Mr of 31 000 as judged by polyacrylamide gel electro...

2008
Jo-Anne Hutsul Elizabeth Worobec

Department of Microbiology, University of Manitoba, Winnipeg, Manitoba, Canada R3T 2N2 An oligonucleotide that encodes the N-terminal portion of a 41 kDa porin of Serratia marcescens was used to probe S. marcescens UOC-51 genomic DNA. An 11 kb EcoRl fragment which hybridized with the oligonucleotide was subcloned into Escherichia coli, examined for expression, and sequenced. The product express...

Journal: :Antimicrobial agents and chemotherapy 1986
A J Godfrey M S Shahrabadi L E Bryan

Pseudomonas aeruginosa common surface antigens were compared in a permeability mutant (PCC118) and its parent (PAO503). The distribution of lipopolysaccharide and porin antigens in the mutant supports the conclusion that beta-lactam permeability was affected by lipopolysaccharide-side chain presentation rather than by a change in porin number.

Journal: :Infection and immunity 1999
J P Derrick R Urwin J Suker I M Feavers M C Maiden

The porin proteins of the pathogenic Neisseria species, Neisseria gonorrhoeae and Neisseria meningitidis, are important as serotyping antigens, putative vaccine components, and for their proposed role in the intracellular colonization of humans. A three-dimensional structural homology model for Neisseria porins was generated from Escherichia coli porin structures and N. meningitidis PorA and Po...

Journal: :The Journal of infectious diseases 1999
F G Mackinnon Y Ho M S Blake F Michon A Chandraker M H Sayegh L M Wetzler

A T cell-dependent immune response to group C meningococcal capsular polysaccharide (CPS) can be elicited when CPS is conjugated to the class 3 neisserial porin (CPS-porin). Treatment of CPS-porin-immunized mice with B7-2 blocking monoclonal antibody (MAb) caused a dramatic reduction in the CPS-specific IgG response, treatment with anti-B7-1 MAb had no effect, and concurrent blockade of B7-1 an...

2012
Amanda K. Petrus Kristen S. Swithers Chaman Ranjit Si Wu Heather M. Brewer J. Peter Gogarten Ljiljana Pasa-Tolic Kenneth M. Noll

The unifying structural characteristic of members of the bacterial order Thermotogales is their toga, an unusual cell envelope that includes a loose-fitting sheath around each cell. Only two toga-associated structural proteins have been purified and characterized in Thermotoga maritima: the anchor protein OmpA1 (or Ompα) and the porin OmpB (or Ompβ). The gene encoding OmpA1 (ompA1) was cloned a...

Journal: :Biology letters 2012
Nadine Flinner Enrico Schleiff Oliver Mirus

The eukaryotic porin superfamily consists of two families, voltage-dependent anion channel (VDAC) and Tom40, which are both located in the mitochondrial outer membrane. In Trypanosoma brucei, only a single member of the VDAC family has been described. We report the detection of two additional eukaryotic porin-like sequences in T. brucei. By bioinformatic means, we classify both as putative VDAC...

Journal: :Antimicrobial agents and chemotherapy 2008
Olga Danilchanka Mikhail Pavlenok Michael Niederweis

The outer membrane of mycobacteria presents an effective permeability barrier for many antibiotics. Transport pathways across this membrane are unknown for most drugs. Here, we examined which antibiotics utilize the porin pathway across the outer membrane of the model organism Mycobacterium smegmatis. Deletion of the porins MspA and MspC drastically increased the resistance of M. smegmatis ML10...

Journal: :Antimicrobial agents and chemotherapy 1989
J S Chapman A Bertasso N H Georgopapadakou

Spontaneous fleroxacin-resistant mutants of Escherichia coli K-12 were isolated at a frequency of 10(-10) to 10(-11) mutants per CFU plated. All mutants exhibited quinolone-resistant replicative DNA biosynthesis, and 4 of 11 mutants also had decreased amounts of OmpF or OmpC porin. None of the mutants had changes solely in porin proteins.

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