Zobrazeno 1 - 10
of 67
pro vyhledávání: '"Michael D Ter-Avanesyan"'
Autor:
Anastasia V Fokina, Maria B Chechenova, Azamat V Karginov, Michael D Ter-Avanesyan, Michael O Agaphonov
Publikováno v:
PLoS ONE, Vol 10, Iss 12, p e0145915 (2015)
Processes taking place in the secretory organelles require Ca2+ and Mn2+, which in yeast are supplied by the Pmr1 ion pump. Here we observed that in the yeast Hansenula polymorpha Ca2+ deficiency in the secretory pathway caused by Pmr1 inactivation i
Externí odkaz:
https://doaj.org/article/a57866cef46f46e9a3262afbf36fbea3
Autor:
Anton A Nizhnikov, Alexander I Alexandrov, Tatyana A Ryzhova, Olga V Mitkevich, Alexander A Dergalev, Michael D Ter-Avanesyan, Alexey P Galkin
Publikováno v:
PLoS ONE, Vol 9, Iss 12, p e116003 (2014)
Despite extensive study, progress in elucidation of biological functions of amyloids and their role in pathology is largely restrained due to the lack of universal and reliable biochemical methods for their discovery. All biochemical methods develope
Externí odkaz:
https://doaj.org/article/837709eedf4c406cba2ae25bde0fa025
Publikováno v:
PLoS ONE, Vol 7, Iss 1, p e29832 (2012)
BackgroundPolyglutamine expansion is responsible for several neurodegenerative disorders, among which Huntington disease is the most well-known. Studies in the yeast model demonstrated that both aggregation and toxicity of a huntingtin (htt) protein
Externí odkaz:
https://doaj.org/article/a126f683c7864c849bda5424748fc5ef
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:
Anastasia V. Fokina, Hyun Ah Kang, Tatyana S. Kalebina, Tatyana A. Sabirzyanova, Azamat V. Karginov, Michael D. Ter-Avanesyan, Michael O. Agaphonov
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-11 (2018)
Scientific Reports
Scientific Reports
The closely related yeasts Ogataea polymorpha and O. parapolymorpha differ drastically from each other by sensitivity to the toxic phosphate analog vanadate. Search for genes underlying this difference revealed two genes, one designated as ABV1 (Alci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::004c968c935b3b43ec58e6a85f32378b
http://link.springer.com/article/10.1038/s41598-018-34888-5
http://link.springer.com/article/10.1038/s41598-018-34888-5
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
Autor:
Alexander A. Dergalev, Sergey V. Leonov, Vitaly V. Kushnirov, Alexander I. Alexandrov, Igor I. Kireev, Erika V. Grosfeld, Michael D. Ter-Avanesyan, Pyotr A. Tyurin-Kuzmin, Roman N. Chuprov-Netochin, Michael O. Agaphonov
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___::fc40268627b935a988ee35989b8b79d7
https://doi.org/10.1101/562728
https://doi.org/10.1101/562728
Publikováno v:
Prion. 10:221-227
Proteins with expanded polyglutamine (polyQ) regions are prone to form amyloids, which can cause diseases in humans and toxicity in yeast. Recently, we showed that in yeast non-toxic amyloids of Q-rich proteins can induce aggregation and toxicity of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70e2cca2ad85ff8b6838faaf27828aa8
https://doi.org/10.1080/19336896.2016.1176659
https://doi.org/10.1080/19336896.2016.1176659
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