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作者:... Ivannikov Roman I , Ter-Avanesyan Michael D , Kushnirov Vitaly V
来源:[J].International journal of molecular sciences(IF 2.464), 2019, Vol.20 (11)PubMed
摘要:The yeast [ PSI +] prion, formed by the Sup35 (eRF3) protein, has multiple structural variants differing in the strength of nonsense suppressor phenotype. Structure of [ PSI +] and its variation are characterized poorly. Here, we mapped Sup35 amyloid cores of 26 [ PSI +] ex vivo ...
作者:... Ivannikov Roman I , Ter-Avanesyan Michael D , Kushnirov Vitaly V
来源:[J].International journal of molecular sciences(IF 2.464), 2019, Vol.20 (11)PubMed
摘要:The yeast [ PSI +] prion, formed by the Sup35 (eRF3) protein, has multiple structural variants differing in the strength of nonsense suppressor phenotype. Structure of [ PSI +] and its variation are characterized poorly. Here, we mapped Sup35 amyloid cores of 26 [ PSI +] ex vivo ...
作者:Kushnirov Vitaly V , Chuprov-Netochin Roman N ...
来源:[J].Biology open, 2019, Vol.8 (7)PubMed
摘要: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 proteins form numerous foci with...
作者:Kushnirov Vitaly V , Dergalev Alexander A , Alexandrov Alexander I
来源:[J].Prion, 2020, Vol.14 (1), pp.11-19PubMed
摘要: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 resistant to treatment with protein...
作者:Kushnirov Vitaly V , Vishnevskaya Aleksandra B ...
来源:[J].Prion, 2007, Vol.1 (3), pp.179-84PubMed
摘要:Yeast prion determinants are related to polymerization of some proteins into amyloid-like fibers. The [PSI(+)] determinant reflects polymerization of the Sup35 protein. Fragmentation of prion polymers by the Hsp104 chaperone represents a key step of the prion replication cycle. T...
作者:Kushnirov Vitaly V , Smirnov Vladimir N
来源:[J].Prion, 2010, Vol.4 (1), pp.45-52PubMed
摘要:In eukaryotic cells amyloid aggregates may incorporate various functionally unrelated proteins. In mammalian diseases this may cause amyloid toxicity, while in yeast this could contribute to prion phenotypes. Insolubility of amyloids in the presence of strong ionic detergents, su...

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