Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Alexander G, Bobylev"'
Autor:
Anastasiia O. Kosolapova, Mikhail V. Belousov, Maksim I. Sulatsky, Anna V. Tsyganova, Anna I. Sulatskaya, Alexander G. Bobylev, Oksana Y. Shtark, Viktor E. Tsyganov, Kirill V. Volkov, Vladimir A. Zhukov, Igor A. Tikhonovich, Anton A. Nizhnikov
Publikováno v:
Frontiers in Plant Science, Vol 13 (2022)
Amyloids represent protein aggregates with highly ordered fibrillar structure associated with the development of various disorders in humans and animals and involved in implementation of different vital functions in all three domains of life. In prok
Externí odkaz:
https://doaj.org/article/a4dc8dbf3b1546b8beb7a1cc79ea4a34
Autor:
Kirill S Antonets, Mikhail V Belousov, Anna I Sulatskaya, Maria E Belousova, Anastasiia O Kosolapova, Maksim I Sulatsky, Elena A Andreeva, Pavel A Zykin, Yury V Malovichko, Oksana Y Shtark, Anna N Lykholay, Kirill V Volkov, Irina M Kuznetsova, Konstantin K Turoverov, Elena Y Kochetkova, Alexander G Bobylev, Konstantin S Usachev, Oleg N Demidov, Igor A Tikhonovich, Anton A Nizhnikov
Publikováno v:
PLoS Biology, Vol 18, Iss 7, p e3000564 (2020)
Amyloids are protein aggregates with a highly ordered spatial structure giving them unique physicochemical properties. Different amyloids not only participate in the development of numerous incurable diseases but control vital functions in archaea, b
Externí odkaz:
https://doaj.org/article/f8927a4807e746d39343a88533d84ce8
Autor:
Elmira I. Yakupova, Liya G. Bobyleva, Sergey A. Shumeyko, Ivan M. Vikhlyantsev, Alexander G. Bobylev
Publikováno v:
Biology, Vol 10, Iss 5, p 394 (2021)
Proteins can perform their specific function due to their molecular structure. Partial or complete unfolding of the polypeptide chain may lead to the misfolding and aggregation of proteins in turn, resulting in the formation of different structures s
Externí odkaz:
https://doaj.org/article/4acabea1aeb34d0eb95667ab2f290f1e
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; Volume 24; Issue 2; Pages: 1056
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://explore.openaire.eu/search/publication?articleId=doi_dedup___::81e301cf5357ef15490a66ed9e2f30f7
Autor:
Daniel V, Kachkin, Kirill V, Volkov, Julia V, Sopova, Alexander G, Bobylev, Sergei A, Fedotov, Sergei G, Inge-Vechtomov, Oxana V, Galzitskaya, Yury O, Chernoff, Aleksandr A, Rubel, Anna Y, Aksenova
Publikováno v:
International journal of molecular sciences. 23(19)
RAD51 is a central protein of homologous recombination and DNA repair processes that maintains genome stability and ensures the accurate repair of double-stranded breaks (DSBs). In this work, we assessed amyloid properties of RAD51
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d603640ea4c211c46d7c44ef2d7f8ee8
https://pubmed.ncbi.nlm.nih.gov/36232958
https://pubmed.ncbi.nlm.nih.gov/36232958
Autor:
Anastasiia O, Kosolapova, Mikhail V, Belousov, Maksim I, Sulatsky, Anna V, Tsyganova, Anna I, Sulatskaya, Alexander G, Bobylev, Oksana Y, Shtark, Viktor E, Tsyganov, Kirill V, Volkov, Vladimir A, Zhukov, Igor A, Tikhonovich, Anton A, Nizhnikov
Publikováno v:
Frontiers in plant science. 13
Amyloids represent protein aggregates with highly ordered fibrillar structure associated with the development of various disorders in humans and animals and involved in implementation of different vital functions in all three domains of life. In prok
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b720982c02dc17f0c840b8cb640ca088
https://pubmed.ncbi.nlm.nih.gov/36388578
https://pubmed.ncbi.nlm.nih.gov/36388578
Publikováno v:
Journal of immunoassayimmunochemistry. 41(2)
The giant muscle protein, titin, is the third most abundant protein in muscle (after myosin and actin). It was shown previously that smooth muscle titin (SMT) with a molecular mass of 500 kDa can form in vitro amorphous amyloid aggregates in two cond
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::653e7e88a1d24e3e523b755657617b08
https://pubmed.ncbi.nlm.nih.gov/31744373
https://pubmed.ncbi.nlm.nih.gov/31744373