Zobrazeno 1 - 10
of 66
pro vyhledávání: '"Alexey D. Nikulin"'
Autor:
Alexander G. Bobylev, Elmira I. Yakupova, Liya G. Bobyleva, Nikolay V. Molochkov, Alexander A. Timchenko, Maria A. Timchenko, Hiroshi Kihara, Alexey D. Nikulin, Azat G. Gabdulkhakov, Tatiana N. Melnik, Nikita V. Penkov, Michail Y. Lobanov, Alexey S. Kazakov, Miklós Kellermayer, Zsolt Mártonfalvi, Oxana V. Galzitskaya, Ivan M. Vikhlyantsev
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 2, p 1056 (2023)
A giant multidomain protein of striated and smooth vertebrate muscles, titin, consists of tandems of immunoglobulin (Ig)- and fibronectin type III (FnIII)-like domains representing β-sandwiches, as well as of disordered segments. Chicken smooth musc
Externí odkaz:
https://doaj.org/article/96162e0c6c21471db5f065e42ee34326
Autor:
Tatiana A. Bessonova, Maria S. Fando, Olga S. Kostareva, Maria N. Tutukina, Olga N. Ozoline, Mikhail S. Gelfand, Alexey D. Nikulin, Svetlana V. Tishchenko
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 15, p 8379 (2022)
ExuR and UxuR are paralogous proteins belonging to the GntR family of transcriptional regulators. Both are known to control hexuronic acid metabolism in a variety of Gammaproteobacteria but the relative impact of each of them is still unclear. Here,
Externí odkaz:
https://doaj.org/article/dd8e2ebfde194d85bcc47c84ff2411a6
Autor:
Liya G. Bobyleva, Sergey A. Shumeyko, Elmira I. Yakupova, Alexey K. Surin, Oxana V. Galzitskaya, Hiroshi Kihara, Alexander A. Timchenko, Maria A. Timchenko, Nikita V. Penkov, Alexey D. Nikulin, Mariya Yu. Suvorina, Nikolay V. Molochkov, Mikhail Yu. Lobanov, Roman S. Fadeev, Ivan M. Vikhlyantsev, Alexander G. Bobylev
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 2, p 731 (2021)
This work investigated in vitro aggregation and amyloid properties of skeletal myosin binding protein-C (sMyBP-C) interacting in vivo with proteins of thick and thin filaments in the sarcomeric A-disc. Dynamic light scattering (DLS) and transmission
Externí odkaz:
https://doaj.org/article/d9e0468936b24d599eb5cb6e12a529b5
Autor:
Olga M. Selivanova, Elizaveta I. Grigorashvili, Mariya Yu. Suvorina, Ulyana F. Dzhus, Alexey D. Nikulin, Victor V. Marchenkov, Alexey K. Surin, Oxana V. Galzitskaya
Publikováno v:
Data in Brief, Vol 8, Iss , Pp 108-113 (2016)
The data presented in this article are related to the research article entitled “One of the possible mechanisms of amyloid fibrils formation based on the sizes of primary and secondary folding nuclei of Aβ40 and Aβ42” (Dovidchenko et al., 2016)
Externí odkaz:
https://doaj.org/article/0c5a23618d29459893cf9b413d1131af
Autor:
Svetlana Tishchenko, O. S. Nikonov, Elena Stolboushkina, E. Yu. Nikonova, Alexey D. Nikulin, N. V. Lekontseva, A. O. Mikhailina
Publikováno v:
Crystallography Reports. 66:726-736
Abstract Structural studies of RNA–protein complexes are important for understanding many molecular mechanisms occurring in cells (e.g., regulation of protein synthesis and RNA-chaperone activity of proteins). Various objects investigated at the In
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::478e468742d6ecdfce5bf52669fb6318
https://doi.org/10.1134/s1063774521050217
https://doi.org/10.1134/s1063774521050217
Autor:
A. A. Alipov, Svetlana Tishchenko, Alexey D. Nikulin, M. S. Fando, A. O. Mikhailina, N. V. Lekontseva
Publikováno v:
Crystallography Reports. 66:791-796
The bacterial protein Hfq is a member of a large family of Lsm proteins, which are characterized by a conserved tertiary structure and form a stable ring-shaped quaternary structure composed of several monomers. The bacterial proteins form hexamers,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6a6400e4c2bc8372da4e86fd9cac3962
https://doi.org/10.1134/s1063774521050023
https://doi.org/10.1134/s1063774521050023
Publikováno v:
Biochemistry (Moscow). 86:S38-S49
Members of the Lsm protein family are found in all three domains of life: bacteria, archaea, and eukarya. They are involved in numerous processes associated with RNA processing and gene expression regulation. A common structural feature of all Lsm fa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc58fae9508c83ace42540777365464c
https://doi.org/10.1134/s0006297921140042
https://doi.org/10.1134/s0006297921140042
Autor:
Alexey D. Nikulin, N. V. Lekontseva, A. O. Mikhailina, O. V. Kravchenko, Svetlana Tishchenko, Vitaly A. Balobanov, M. S. Fando
Publikováno v:
Biochimie. 175:1-12
Sm and Sm-like (Lsm) proteins are considered as an evolutionary conserved family involved in RNA metabolism in organisms from bacteria and archaea to human. Currently, the function of Sm-like archaeal proteins (SmAP) is not well understood. Here, we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbde3f3462c0ddc1f2aac4e24b657cde
https://doi.org/10.1016/j.biochi.2020.05.001
https://doi.org/10.1016/j.biochi.2020.05.001
Autor:
Oxana V. Galzitskaya, Ivan M. Vikhlyantsev, Elmira I Yakupova, A. G. Bobylev, Sergey A Shumeyko, Alexey D. Nikulin, D. A. Yurshenas, L. G. Bobyleva
Publikováno v:
Молекулярная биология. 54:643-652
In this paper, the property of the muscle titin protein to form in vitro specific amyloid-like aggregates is discussed. The main difference from the known amyloid aggregates is the formation of a quaternary structure that resembles cross-β, with no
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c20f063795539e4692aa79d441064708
https://doi.org/10.31857/s0026898420040047
https://doi.org/10.31857/s0026898420040047
Autor:
Alexey D. Nikulin
Publikováno v:
Biochemistry. Biokhimiia. 86(8)
The review discusses differences between the specific protein interactions with single- and double-stranded RNA molecules using the data on the structure of RNA-protein complexes. Proteins interacting with the single-stranded RNAs form contacts with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::617365add1b475e3ee4616988205a389
https://pubmed.ncbi.nlm.nih.gov/34488578
https://pubmed.ncbi.nlm.nih.gov/34488578