Zobrazeno 1 - 10
of 18
pro vyhledávání: '"D. K. Chistyulin"'
Publikováno v:
Biochemistry (Moscow), Supplement Series A: Membrane and Cell Biology. 16:175-179
Autor:
Galina N. Likhatskaya, V. A. Khomenko, Olga D. Novikova, Elena Zelepuga, D. K. Chistyulin, O. Yu. Portnyagina, Yuri N. Antonenko
Publikováno v:
Acta Naturae
Electrophysiological experiments on bilayer lipid membranes showed that the isolated outer membrane major porin of Yersinia ruckeri (YrOmpF) exhibits activity typical of porins from Gram-negative bacteria, forming channels with a mean conductance of
Autor:
O. Yu. Portnyagina, G. A. Naberezhnykh, D. K. Chistyulin, L. S. Shevchenko, Olga D. Novikova, I. Yu. Kokoreva
Publikováno v:
Russian Journal of Marine Biology. 43:190-195
This study investigates the spreading of the Gram-negative bacterium Yersinia ruckeri, pathogenic for fish, among representatives of the marine flora and fauna of the Sea of Okhotsk. The enzyme-linked immunosorbent assay (ELISA) revealed the presence
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
Autor:
D. K. Chistyulin, N. Yu. Kim, T. F. Solovyeva, O. Yu. Portnyagina, Galina N. Likhatskaya, V. A. Khomenko, Olga D. Novikova
Publikováno v:
Biophysics. 61:851-859
The spatial organization of outer-membrane porins is studied by optical spectroscopy and molecular modeling. It was found that the OmpF and OmpC porins from Yеrsiniа ruckeri are β-structured membrane proteins typical of the pore-forming proteins o
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
Autor:
N. Yu. Kim, Tamara F. Solov'eva, V. A. Khomenko, Olga D. Novikova, D. K. Chistyulin, O. V. Sidorova, O. Yu. Portnyagina, Galina N. Likhatskaya, T. I. Vakorina
Publikováno v:
Biochemical and Biophysical Research Communications. 445:428-432
Recombinant mutant OmpF porins from Yersinia pseudotuberculosis outer membrane were obtained using site-directed mutagenesis. Here we used four OmpF mutants where single extracellular loops L1, L4, L6, and L8 were deleted one at a time. The proteins
Autor:
O. Yu. Portnyagina, Vakorina Ti, D. K. Chistyulin, Galina N. Likhatskaya, V. A. Khomenko, Olga D. Novikova, Marina Isaeva, N. Yu. Kim, Tamara F. Solov'eva
Publikováno v:
Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology. 6:235-242
The polypeptide profile of the porin protein fraction of Yersinia ruckeri, a Gram-negative bacterium causing yersiniosis in fish, has been shown to depend on cultivation temperature. OmpF-like porins are expressed mainly in the outer membrane (OM) of
Autor:
Salinas, Rafael A.1 (AUTHOR), Martínez Tolibia, Shirlley E.1 (AUTHOR), Galdámez‐Martínez, Andrés2 (AUTHOR), Romero, Josué E.3 (AUTHOR), García‐Barrera, Laura J.4,5 (AUTHOR), Orduña, Abdú4 (AUTHOR), Ramos, Carlos David1 (AUTHOR), Santana Rodríguez, Guillermo1 (AUTHOR), Dutt, Ateet1 (AUTHOR) adutt@iim.unam.mx
Publikováno v:
Advanced Nanobiomed Research. Nov2024, Vol. 4 Issue 11, p1-13. 13p.
Autor:
O. V. Sidorova, Tamara F. Solov'eva, Marina Isaeva, N. Yu. Kim, V. A. Khomenko, Olga D. Novikova, O. Yu. Portnyagina, D. K. Chistyulin, Galina N. Likhatskaya
Publikováno v:
Bioorganicheskaia khimiia. 38(2)
Yersinia pseudotuberculosis outer membrane (OM) recombinant mutant OmpF porins with deletions of the external loops L1, L6 and L8 were obtained using site-directed mutagenesis of the recombinant plasmid including ompF gene. Heterologeous expression o