Identification of New FG-Repeat Nucleoporins with Amyloid Properties

Autor: Lavrentii G. Danilov, Xenia V. Sukhanova, Tatiana M. Rogoza, Ekaterina Y. Antonova, Nina P. Trubitsina, Galina A. Zhouravleva, Stanislav A. Bondarev

Publikováno v: International Journal of Molecular Sciences; Volume 24; Issue 10; Pages: 8571

Amyloids are fibrillar protein aggregates with a cross-β structure. More than two hundred different proteins with amyloid or amyloid-like properties are already known. Functional amyloids with conservative amyloidogenic regions were found in differe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bedda4bb31b11bc9fc2ccc3b667cee85

Amyloid and Amyloid-Like Aggregates: Diversity and the Term Crisis

Autor: Stanislav A. Bondarev, Yury A. Barbitoff, Andrew G. Matveenko, Galina A. Zhouravleva, A B Matiiv, Nina P. Trubitsina

Publikováno v: Biochemistry (Moscow). 85:1011-1034

Abstract Active accumulation of the data on new amyloids continuing nowadays dissolves boundaries of the term “amyloid”. Currently, it is most often used to designate aggregates with cross-β structure. At the same time, amyloids also exhibit a n

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::43e2fdd62dd5bfbdf5fdf927081f906e
https://doi.org/10.1134/s0006297920090035

Nonsense Mutations in the Yeast SUP35 Gene Affect the [PSI+] Prion Propagation

Autor: Galina A. Zhouravleva, Nina P. Trubitsina, Stanislav A. Bondarev, Olga M. Zemlyanko

Publikováno v: International Journal of Molecular Sciences
Volume 21
Issue 5
International Journal of Molecular Sciences, Vol 21, Iss 5, p 1648 (2020)

The essential SUP35 gene encodes yeast translation termination factor eRF3. Previously, we isolated nonsense mutations sup35-n and proposed that the viability of such mutants can be explained by readthrough of the premature stop codon. Such mutations

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64d2cc1e495280df720e0205198b5afb

Point mutations affecting yeast prion propagation change the structure of its amyloid fibrils

Autor: Mikhail V. Belousov, Irina M. Kuznetsova, Nina P. Trubitsina, Anna I. Sulatskaya, Galina A. Zhouravleva, Maksim I. Sulatsky, Konstantin K. Turoverov, Manuel A. Llanos, Stanislav A. Bondarev, Andrey V. Kajava

Publikováno v: Journal of Molecular Liquids
Journal of Molecular Liquids, Elsevier, 2020, 314, pp.113618. ⟨10.1016/j.molliq.2020.113618⟩
SEDICI (UNLP)
Universidad Nacional de La Plata
instacron:UNLP

We investigated the effect of the point substitutions in the N-terminal domain of the yeast prion protein Sup35 (Sup35NMp) on the structure of its amyloid fibrils. As the objects of the study, proteins with mutations that have different influence on

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1efef5b42e593965472eb28d8ce04d82
https://doi.org/10.1016/j.molliq.2020.113618