Zobrazeno 1 - 10
of 51
pro vyhledávání: '"Vitaly V. Kushnirov"'
Publikováno v:
Biomolecules, Vol 11, Iss 12, p 1884 (2021)
Amyloids are filamentous protein aggregates that are associated with a number of incurable diseases, termed amyloidoses. Amyloids can also manifest as infectious or heritable particles, known as prions. While just one prion is known in humans and ani
Externí odkaz:
https://doaj.org/article/84869c5e218946c0b8b55f7cfd412dc7
Publikováno v:
Journal of Fungi, Vol 7, Iss 10, p 884 (2021)
The biosynthesis of cyclic tetrapyrrol chromophores such as heme, siroheme, and chlorophyll involves the formation of fluorescent porphyrin precursors or compounds, which become fluorescent after oxidation. To identify Ogataea polymorpha mutations af
Externí odkaz:
https://doaj.org/article/c6bfe49a7828440da34147ac7f338f62
Autor:
Alexander I. Alexandrov, Erika V. Grosfeld, Alexander A. Dergalev, Vitaly V. Kushnirov, Roman N. Chuprov-Netochin, Pyotr A. Tyurin-Kuzmin, Igor I. Kireev, Michael D. Ter-Avanesyan, Sergey V. Leonov, Michael O. Agaphonov
Publikováno v:
Biology Open, Vol 8, Iss 7 (2019)
Proteins can aggregate in response to stresses, including hyperosmotic shock. Formation and disassembly of aggregates is a relatively slow process. We describe a novel instant response of the cell to hyperosmosis, during which chaperones and other pr
Externí odkaz:
https://doaj.org/article/e14b1ee309e44399abceb98a0ccf2a90
Publikováno v:
International journal of molecular sciences. 23(10)
Amyloids are protein aggregates with a specific filamentous structure that are related to a number of human diseases, and also to some important physiological processes in animals and other kingdoms of life. Amyloids in yeast can stably propagate as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b80b5f476318084e6f2557ed0f66404
https://pubmed.ncbi.nlm.nih.gov/35628548
https://pubmed.ncbi.nlm.nih.gov/35628548
Publikováno v:
Molecular Microbiology. 115:774-788
Gorkovskiy et al. observed that many [PSI+ ] prion isolates, obtained in yeast with the mutant Hsp104T160M chaperone, propagate poorly in wild-type cells and suggested that Hsp104 is part of the cellular anti-prion system, curing many nascent [PSI+ ]
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a909a3b3bad6718b78bc057c47bad038
https://doi.org/10.1111/mmi.14643
https://doi.org/10.1111/mmi.14643
Autor:
A. V. Nostaeva, Sergey E. Dmitriev, Vitaly V. Kushnirov, V. A. Bidiuk, I. V. Kukhtevich, R. Schneider, Vadim N. Gladyshev, Olga V. Mitkevich, E. S. Shilov, Alexander I. Alexandrov, E. V. Grosfeld
Cell death plays a major role in development, pathology and aging and can be triggered by various types of acute external and internal stimuli, such as chemicals or mutations. However, little is known about chronic cell death in the context of contin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eeeb8e21def0b435ef091ddc588b63af
https://doi.org/10.1101/2021.10.20.465133
https://doi.org/10.1101/2021.10.20.465133
Publikováno v:
Prion
Amyloids and their infectious subset, prions, represent fibrillary aggregates with regular structure. They are formed by proteins that are soluble in their normal state. In amyloid form, all or part of the polypeptide sequence of the protein is resis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d43cbfe5292b7ca3842e17a3c16684b
https://doi.org/10.1080/19336896.2019.1704612
https://doi.org/10.1080/19336896.2019.1704612
Autor:
Alexander I Alexandrov, Alla B Polyanskaya, Genrikh V Serpionov, Michael D Ter-Avanesyan, Vitaly V Kushnirov
Publikováno v:
PLoS ONE, Vol 7, Iss 10, p e46458 (2012)
Fragmentation of amyloid polymers by the chaperone Hsp104 allows them to propagate as prions in yeast. The factors which determine the frequency of fragmentation are unclear, though it is often presumed to depend on the physical strength of prion pol
Externí odkaz:
https://doaj.org/article/157a3fd95c4e4485873e4b54f1b8f2fe
Autor:
Pyotr A. Tyurin-Kuzmin, Alexander I. Alexandrov, Igor I. Kireev, Alexander A. Dergalev, Erika V. Grosfeld, Roman N. Chuprov-Netochin, Michael O. Agaphonov, Michael D. Ter-Avanesyan, Sergey V. Leonov, Vitaly V. Kushnirov
Publikováno v:
Biology Open, Vol 8, Iss 7 (2019)
Biology Open
Biology Open
Proteins can aggregate in response to stresses, including hyperosmotic shock. Formation and disassembly of aggregates is a relatively slow process. We describe a novel instant response of the cell to hyperosmosis, during which chaperones and other pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::228afcf2d8ab96afe8b2872f1bb4475b
http://bio.biologists.org/content/8/7/bio044529
http://bio.biologists.org/content/8/7/bio044529
Autor:
Vitaly V. Kushnirov, Alexander A. Dergalev, Roman I. Ivannikov, Alexander I. Alexandrov, Michael D. Ter-Avanesyan
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 11, p 2633 (2019)
International Journal of Molecular Sciences
Volume 20
Issue 11
International Journal of Molecular Sciences
Volume 20
Issue 11
The yeast [PSI+] prion, formed by the Sup35 (eRF3) protein, can exist as multiple structural variants exhibiting phenotypic variation in the strength of nonsense suppression and mitotic stability. Structure of [PSI+] and its variation is only partly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d58ca51523c3c568845e4da5c08be13d
https://www.mdpi.com/1422-0067/20/11/2633
https://www.mdpi.com/1422-0067/20/11/2633