Zobrazeno 1 - 7
of 7
pro vyhledávání: '"M. A. Nemykh"'
Autor:
Nina Rodionova, Lyudmila A. Baratova, Marina V. Serebryakova, Olga Karpova, M. A. Nemykh, E. V. Lukashina, Evgeny N. Dobrov, Anna A. Mukhamedzhanova, Alexander L. Ksenofontov, G. A. Badun, Natalia V. Fedorova
Publikováno v:
FEBS Journal. 276:7006-7015
Alterations in Potato virus X (PVX) coat protein structure after binding of the protein, encoded by the first gene of PVX triple gene block (triple gene block 1 protein, TGBp1), to the virions were studied using tritium planigraphy. Previously, it ha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::13708b1cdaadb8cdf4fbc1a5d2fdec69
https://doi.org/10.1111/j.1742-4658.2009.07408.x
https://doi.org/10.1111/j.1742-4658.2009.07408.x
Autor:
Lyudmila A. Baratova, Alexander V. Efimov, Alexander M. Arutyunyan, V. A. Drachev, E. V. Lukashina, M. A. Nemykh, V.K. Novikov, Evgeny N. Dobrov, Victor N. Orlov
Publikováno v:
Virology. 373:61-71
We found that a 2-h incubation of potato virus X (PVX) virions in 10 mM Tris-HCl buffer pH 7.5 at -20 degrees C results in a strong but reversible drop in virion stability. Under these conditions, the PVX virions are completely disrupted by low (star
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0be726b37f59d1a9d03484e01a29f4b2
https://doi.org/10.1016/j.virol.2007.11.024
https://doi.org/10.1016/j.virol.2007.11.024
Autor:
M. A. Nemykh, Ludmila A. Baratova, E. N. Dobrov, V. A. Drachev, Alexander V. Efimov, E. V. Lukashina
Publikováno v:
Molecular Biology. 41:638-641
A modified model was proposed for the tertiary structure of the coat protein (CP) molecules in potato virus X (PVX) virions, similar to the original model of 2001 describing the structure of CP of potato virus A, a member of another group of filament
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b7afe4502d3aabe2cdef3678eae9a3ca
https://doi.org/10.1134/s0026893307040176
https://doi.org/10.1134/s0026893307040176
Autor:
Boris I. Kurganov, Evgeny N. Dobrov, V. A. Drachev, Lev S. Yaguzhinsky, M. A. Nemykh, Alexander M. Arutyunyan, Yuliy V. Panyukov, E. R. Rafikova
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 38:533-543
Ordered and amorphous protein aggregation causes numerous diseases. Tobacco mosaic virus coat protein for many decades serves as the classical model of ordered protein aggregation ("polymerization"). It was also found to be highly prone to heat-induc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07c13bb8583eeab889478e4eee6a28b8
https://doi.org/10.1016/j.biocel.2005.10.014
https://doi.org/10.1016/j.biocel.2005.10.014
Publikováno v:
Molekuliarnaia biologiia. 41(4)
We propose the modified model of the structure of coat protein (CP) subunits in filamentous virions of potato virus X (PVX). The model is similar to the one proposed by us in 2001 for the CP of another helical plant virus (potato virus A) belonging t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7c30dfacf9428280069cf249f02e638f
https://pubmed.ncbi.nlm.nih.gov/17936992
https://pubmed.ncbi.nlm.nih.gov/17936992
Publikováno v:
Molekuliarnaia biologiia. 41(4)
With help of several optical methods and differential scanning calorimetry we studied the structure and stability of molecules of coat protein (CP) of filamentous of potato virus X (PVX) in free state and in the virions. According to the results of a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::366f730c2a3d2e8af7429648558aafe4
https://pubmed.ncbi.nlm.nih.gov/17936991
https://pubmed.ncbi.nlm.nih.gov/17936991
Publikováno v:
Macromolecular bioscience. 8(2)
The interactions of non-ionic surfactant Triton X-100 and the coat protein of tobacco mosaic virus, which is an established model for both ordered and non-ordered protein aggregation, were studied using turbidimetry, differential scanning calorimetry
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61d2ed98149d7c221831d0713f768b8b
https://pubmed.ncbi.nlm.nih.gov/17886326
https://pubmed.ncbi.nlm.nih.gov/17886326