Zobrazeno 1 - 9 of 9 pro vyhledávání: '"Olga Portnyagina"'
1
Porin from Marine Bacterium Marinomonas primoryensis KMM 3633T: Isolation, Physico-Chemical Properties, and Functional Activity
Autor: Ekaterina I. Aksenova, Lyudmila A. Romanenko, Natalia N. Ryzhova, Olga Portnyagina, Galina N. Likhatskaya, V. A. Khomenko, Olga D. Novikova, Natalia Yu Kim, Olga L. Voronina, Tamara F. Solov'eva, M.S. Kunda
Publikováno v: Molecules
Molecules, Vol 25, Iss 3131, p 3131 (2020)
Volume 25
Issue 14
Marinomonas primoryensis KMM 3633T, extreme living marine bacterium was isolated from a sample of coastal sea ice in the Amursky Bay near Vladivostok, Russia. The goal of our investigation is to study outer membrane channels determining cell permeabi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb489c9c4e11aff31d1511b82d4ac4d8
http://europepmc.org/articles/PMC7397200
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2
OmpF porin from Yersinia ruckeri as pathogenic factor: Surface antigenic sites and biological properties
Autor: V. A. Khomenko, Olga Novikova, Viktoriya Davidova, L. S. Shevchenko, Sergey A. Dyshlovoy, Olga Portnyagina, D. K. Chistyulin
Publikováno v: Microbial Pathogenesis. 150:104694
Bacterium Yersinia ruckeri as a pathogen induces causative agent of intestinal fish disease called enteric redmouth disease (ERM) is known. In this study, outer membrane OmpF porin from the Y. ruckeri (YrOmpF) has been identified as a pathogenic fact
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6088e57a8f992f9993d27dc644921d9
https://doi.org/10.1016/j.micpath.2020.104694
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3
Peculiarities of thermal denaturation of OmpF porin from Yersinia ruckeri
Autor: Valery L. Shnyrov, Vladimir N. Uversky, V. A. Khomenko, Olga D. Novikova, Olga Portnyagina, D. K. Chistyulin, Tamara F. Solov'eva, Nina M. Sanina, Evgeny V. Sidorin, Natalya Yu. Kim
Publikováno v: Molecular bioSystems. 13(9)
Irreversible denaturation of membrane proteins in detergent solutions is similar to unfolding of water-soluble multidomain proteins and represents a complex, multistage process. Pore-forming proteins of Gram-negative bacteria are heat-modifiable prot
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e0878c1f35a45ba7ae6cf1bd734e743
https://pubmed.ncbi.nlm.nih.gov/28726924
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4
In silico and in vitro analysis of cross-reactivity between Yersinia pseudotuberculosis OmpF porin and thyroid-stimulating hormone receptor
Autor: Olga Portnyagina, V. A. Khomenko, Elena Zelepuga, Olga Novikova, Elena Solov’eva, Tamara F. Solov'eva
Publikováno v: International journal of biological macromolecules. 107
This work is devoted to the ascertainment of serological cross-reactivity between OmpF porin from Yersinia pseudotuberculosis (YpOmpF) and human thyroid-stimulating hormone receptor (hTSHR). Extracts containing hTSHR were isolated from surgical thyro
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92cc7e25aedd32b21be1501d370aaa3b
https://pubmed.ncbi.nlm.nih.gov/29079441
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5
Production of recombinant porin from Y. pseudotuberculosis in a water-soluble form for pseudotuberculosis diagnostics
Autor: Olga Novikova, V. A. Golotin, Olga Portnyagina, Valery A. Rasskazov, Natalia Kim, Natalia Chopenko
Publikováno v: Biological chemistry. 398(11)
OmpF porin from the outer membrane ofYersinia pseudotuberculosiswas cloned into pET-40b(+) plasmid. UsingE. coliRosetta (DE3) strain, MX medium, IPTG concentration of 0.2 mmand post-induction cultivation at 14°C overnight allowed us to obtain a wate
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d557a6342be3fb860f1e6f5fc33973b8
https://pubmed.ncbi.nlm.nih.gov/28723607
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6
Study of effect of substitution of the penultimate amino acid residue on expression, structure, and functional properties of Yersinia pseudotuberculosis OmpY porin
Autor: Galina N. Likhatskaya, Natalya Yu. Kim, V. A. Khomenko, Olga D. Novikova, Marina Isaeva, N. M. Tischenko, Olga Portnyagina, Tamara F. Solov'eva
Publikováno v: Biochemistry (Moscow). 79:694-705
The purpose of the study was to compare the expression of two Yersinia pseudotuberculosis proteins, wild-type porin OmpY and the mutant porin OmpY designated as OmpY-Q having the uncharged amino acid residue Gln instead of positively charged Arg at t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88b678a4c9d4bf8202c015331706a198
https://doi.org/10.1134/s0006297914070116
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7
Modified and Mutant Porins in the Study on Molecular Basis of Non- Specific Diffusion
Autor: Tamara F. Solov'eva, Olga Portnyagina, Olga D. Novikova
Publikováno v: Current proteinpeptide science. 18(3)
Site-directed mutagenesis allows elucidation of the basic principles of the porin-driven membrane permeability and opens the possibility for the modulation of functional states of porin channels. The review is aimed to show the advantages of using mu
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63908a62c210c9a6cf3e988f186af34a
https://pubmed.ncbi.nlm.nih.gov/27593088
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9
Immunochemical Properties of Recombinant Ompf Porin from Outer Membrane of Yersinia pseudotuberculosis
Autor: Marina P. Issaeva, V. A. Khomenko, Olga D. Novikova, Tamara F. Solov'eva, Olga Sidorova, Olga Portnyagina
Porins from outer membranes (OM) of Gram-negative bacteria exist in intact membranes as homotrimers forming water-filled pores or channels that provide low-molecular compounds transportation. Surface localization of the porins and their structural pe
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7b131ce756d2e4218bd9078ab95a769c
https://doi.org/10.5772/35207
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