Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Olga V. Mitkevich"'
Autor:
Alexander I. Alexandrov, Valery N. Urakov, Sergey E. Dmitriev, Dmitri A. Bykov, Nadezhda E. Makarova, Olga V. Mitkevich, Yanislav S. Hrytseniuk, Desislava S. Makeeva, Artyom A. Egorov, Ivan V. Kulakovskiy
Publikováno v:
F1000Research, Vol 10 (2021)
In eukaryotes, stalled and collided ribosomes are recognized by several conserved multicomponent systems, which either block protein synthesis in situ and resolve the collision locally, or trigger a general stress response. Yeast ribosome-binding GTP
Externí odkaz:
https://doaj.org/article/1dc1d4566e1e4849b37a092295e42a10
Autor:
Erika V. Grosfeld, Victoria A. Bidiuk, Olga V. Mitkevich, Eslam S. M. O. Ghazy, Vitaliy V. Kushnirov, Alexander I. Alexandrov
Publikováno v:
Journal of Fungi, Vol 7, Iss 11, p 886 (2021)
Cell death in response to distinct stimuli can manifest different morphological traits. It also depends on various cell death signaling pathways, extensively characterized in higher eukaryotes but less so in microorganisms. The study of cell death in
Externí odkaz:
https://doaj.org/article/e54b56a746f94ad18f358f1d5f5cc011
Autor:
Artyom A, Egorov, Desislava S, Makeeva, Nadezhda E, Makarova, Dmitri A, Bykov, Yanislav S, Hrytseniuk, Olga V, Mitkevich, Valery N, Urakov, Alexander I, Alexandrov, Ivan V, Kulakovskiy, Sergey E, Dmitriev
Publikováno v:
F1000Research
In eukaryotes, stalled and collided ribosomes are recognized by several conserved multicomponent systems, which either block protein synthesis in situ and resolve the collision locally, or trigger a general stress response. Yeast ribosome-binding GTP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9da44103a3e6fe46f05055eddd05a66d
https://pubmed.ncbi.nlm.nih.gov/34900236
https://pubmed.ncbi.nlm.nih.gov/34900236
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
Autor:
Olga V. Mitkevich, Erika V. Grosfeld, Victoria A. Bidiuk, Alexander I. Alexandrov, Vitaliy Vladimirovich Kushnirov, Eslam S. M. O. Ghazy
Publikováno v:
Journal of Fungi, Vol 7, Iss 886, p 886 (2021)
Journal of Fungi
Journal of Fungi
Cell death in response to distinct stimuli can manifest different morphological traits. It also depends on various cell death signaling pathways, extensively characterized in higher eukaryotes but less so in microorganisms. The study of cell death in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7eb78779022d4c9b5aab2132a31e154c
https://www.mdpi.com/2309-608X/7/11/886
https://www.mdpi.com/2309-608X/7/11/886
Autor:
Valery N. Urakov, Ivan V. Kulakovskiy, Olga V. Mitkevich, Nadezhda E. Makarova, Alexander I. Alexandrov, Desislava S. Makeeva, Yanislav S. Hrytseniuk, Sergey E. Dmitriev, Dmitri A. Bykov, Artyom A. Egorov
Publikováno v:
F1000Research. 10:1162
In eukaryotes, stalled and collided ribosomes are recognized by several conserved multicomponent systems, which either block protein synthesis in situ and resolve the collision locally, or trigger a general stress response. Yeast ribosome-binding GTP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c8342fce8d56f074d8aee4eb26add653
https://doi.org/10.12688/f1000research.74727.1
https://doi.org/10.12688/f1000research.74727.1
The [PSI+] nonsense-suppressor determinant of Saccharomyces cerevisiae is based on the formation of heritable amyloids of the Sup35 (eRF3) translation termination factor. [PSI+] amyloids have variants differing in amyloid structure and in the strengt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4e86ee300aca67177421cf164116898a
https://doi.org/10.20944/preprints201810.0173.v1
https://doi.org/10.20944/preprints201810.0173.v1
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 19, Iss 11, p 3663 (2018)
Volume 19
Issue 11
International Journal of Molecular Sciences, Vol 19, Iss 11, p 3663 (2018)
Volume 19
Issue 11
The [PSI+] nonsense-suppressor determinant of Saccharomyces cerevisiae is based on the formation of heritable amyloids of the Sup35 (eRF3) translation termination factor. [PSI+] amyloids have variants differing in amyloid structure and in the strengt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec478702a84c5046f9f2c9117c1c1407
https://pubmed.ncbi.nlm.nih.gov/30463309
https://pubmed.ncbi.nlm.nih.gov/30463309
Publikováno v:
The FEBS journal. 284(12)
In eukaryotes, termination of translation is controlled by polypeptide chain release factors eRF1 and eRF3, of which the former recognizes nonsense codons, while the latter interacts with eRF1 and stimulates polypeptide release from the ribosome in a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::640bbff07eae658317986792d116caf0
https://pubmed.ncbi.nlm.nih.gov/28467675
https://pubmed.ncbi.nlm.nih.gov/28467675
Autor:
Irina S. Kolotushkina, John R. Shainoff, Patricia M. DiBello, Olga V. Mitkevich, Paul D. Bishop, David C. Teller, Vivien C. Yee, Gary B. Smejkal, Gennady P. Samokhin, Karl Fickenscher
Publikováno v:
Journal of Biological Chemistry. 273:14387-14391
Coagulation factor XIIIa, plasma transglutaminase (endo-γ-glutamine:e-lysine transferase EC2.3.2.13) catalyzes isopeptide bond formation between glutamine and lysine residues and rapidly cross-links fibrin clots. A monoclonal antibody (5A2) directed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3171f73ddd01663d60e6e08c56915066
https://doi.org/10.1074/jbc.273.23.14387
https://doi.org/10.1074/jbc.273.23.14387