نتایج جستجو برای: Porin A

تعداد نتایج: 13432370  

Jose Luis Perez Velazquez Mohammad Ali Atlasi,

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...

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...

Journal: :The Journal of biological chemistry 1985
R Pfaller H Freitag M A Harmey R Benz W Neupert

Mitochondrial porin, the outer membrane pore-forming protein, was isolated in the presence of detergents and converted into a water-soluble form. This water-soluble porin existed under nondenaturing conditions as a mixture of dimers and oligomers. The proportion of dimers increased with decreasing porin concentration during conversion. Water-soluble porin inserted spontaneously into artificial ...

Journal: :Applied and environmental microbiology 1998
M L Davey R E Hancock L M Mutharia

Vibrio anguillarum serotype O2 strains express a 40-kDa outer membrane porin protein. Immunoblot analysis revealed that antigenic determinants of the V. anguillarum O2 40-kDa porin were conserved within bacterial species of the genus Vibrio. The relative amounts of the V. anguillarum O2 40-kDa porin were enhanced by growth of V. anguillarum O2 in CM9 medium containing 5 to 10% sucrose or 0.1 to...

Journal: :Infection and immunity 1993
S Muthukkumar V R Muthukkaruppan

Investigations were undertaken to characterize the protective immunity induced by porin-lipopolysaccharide (LPS) against Salmonella typhimurium infection in mice. Mice immunized with porin-LPS showed higher levels of antiporin immunoglobulin G than mice which received porin alone. Further, T cells from porin-LPS-immunized mice showed an augmented proliferative response to porin in vitro compare...

1999
ANTONIO DOMÉNECH-SÁNCHEZ SANTIAGO HERNÁNDEZ-ALLÉS LUIS MARTÍNEZ-MARTÍNEZ VICENTE J. BENEDÍ

Klebsiella pneumoniae porin genes were analyzed to detect mutations accounting for the porin deficiency observed in many b-lactam-resistant strains. PCR and Southern blot analysis revealed the existence of a third porin gene in addition to the OmpK36 and OmpK35 porin genes previously described. This new porin gene was designated ompK37 and is present in all of the clinical isolates tested. The ...

Journal: :Journal of bacteriology 1999
A Doménech-Sánchez S Hernández-Allés L Martínez-Martínez V J Benedí S Albertí

Klebsiella pneumoniae porin genes were analyzed to detect mutations accounting for the porin deficiency observed in many beta-lactam-resistant strains. PCR and Southern blot analysis revealed the existence of a third porin gene in addition to the OmpK36 and OmpK35 porin genes previously described. This new porin gene was designated ompK37 and is present in all of the clinical isolates tested. T...

Journal: :Journal of bacteriology 1978
R Benz B A Boehler-Kohler R Dieterle W Boos

Osmotic shock fluid of Escherichia coli exhibited pore-forming activity. This activity could be followed by an in vitro assay based on the conductivity increase for ions due to the presence of pores in black lipid membranes. The histogram (the distribution of conductivity increments in a single pore experiment) obtained with osmotic shock fluid from E. coli was identical to the histogram obtain...

Journal: :Plant physiology 1997
S. Reumann M. Bettermann R. Benz H. W. Heldt

Glyoxysomes of endosperm tissue of castor bean (Ricinus communis L.) seedlings were solubilized in a detergent and added to a lipid bilayer. Conductivity measurements revealed that the glyoxysomal preparation contained a porin-like channel. Using an electrophysiological method, which we established for semiquantitative determination of porin activity, we were able to demonstrate that glyoxysoma...

Journal: :The Journal of Cell Biology 2001
Thomas Krimmer Doron Rapaport Michael T. Ryan Chris Meisinger C. Kenneth Kassenbrock Elizabeth Blachly-Dyson Michael Forte Michael G. Douglas Walter Neupert Frank E. Nargang Nikolaus Pfanner

Porin, also termed the voltage-dependent anion channel, is the most abundant protein of the mitochondrial outer membrane. The process of import and assembly of the protein is known to be dependent on the surface receptor Tom20, but the requirement for other mitochondrial proteins remains controversial. We have used mitochondria from Neurospora crassa and Saccharomyces cerevisiae to analyze the ...

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