Results 41 to 50 of about 68,429 (275)
Porins are crucial proteins located in the outer membrane that directly influence antimicrobial resistance mechanisms and virulence in bacteria. In this study, a porin gene (Vp-porin) was cloned in V.
Jinyuan Che +8 more
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Biophysical Effects Of Ion Concenteration On The Affinity Between Nanopore, OmpF Lumen and Passing Nucleotide [PDF]
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
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Cholera Vibrio Membrane Protein OmpT as an Omptin Belonging to Vibrionaceae Family
Concerned are the issues related to enterobacteria omptins, their structure and functionality, as well as alternative role in pathogenesis of the infections induced by them.
B. N. Mishan’Kin +4 more
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Mitochondrial Porin Is Involved in Development, Virulence, and Autophagy in Fusarium graminearum
Mitochondrial porin, the voltage-dependent anion-selective channel (VDAC), is the most abundant protein in the outer membrane, and is critical for the exchange of metabolites and phospholipids in yeast and mammals.
Xueqin Han +9 more
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A mitochondrial porin cDNA predicts the existence of multiple human porins
Pores formed in the outer membrane of mitochondria by mitochondrial porin make it permeable to water-soluble metabolites smaller than approximately 5 kDa. We have isolated a full-length cDNA encoding a human porin. This probe detects a single approximately 1.5-kilobase mRNA species on Northern blots, but multiple hybridizing bands on genomic Southern ...
H, Ha +3 more
openaire +2 more sources
Dimeric porin from Paracoccus denitrificans [PDF]
Paracoccus denitrificans was shown to contain a 33,000-dalton porin, which produced pores of large (1.6 to 1.8 nm) diameter. Cross-linking studies showed that the porin existed as dimers in the outer membrane.
L S, Zalman, H, Nikaido
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Sucrose-specific porin (ScrY) is a transmembrane protein that allows for the uptake of sucrose under growth-limiting conditions. The crystal structure of ScrY was resolved before by X-ray crystallography, both in its uncomplexed form and with bound ...
Liping eSun +4 more
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Eukaryotic porin, also known as Voltage-Dependent Anion Channel (VDAC), is the most frequent protein in the outer membrane of mitochondria that are responsible for cellular respiration.
Roland Benz
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A water-soluble form of porin from the mitochondrial outer membrane of Neurospora crassa [PDF]
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.
Benz, Roland +4 more
core
Evaluation of the Blue-Carba test for rapid detection of carbapenemases in gram-negative Bacilli [PDF]
The Blue-Carba test (BCT) is a biochemical test for rapid (2 h)detection of carbapenemase production in Gram-negative bacillidirectly from bacterial culture .
Albornoz, Ezequiel Pablo +7 more
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