Search Results - "Trubitsina, Nina P"

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  1. 1

    How Big Is the Yeast Prion Universe? by Zhouravleva, Galina A, Bondarev, Stanislav A, Trubitsina, Nina P

    “…The number of yeast prions and prion-like proteins described since 1994 has grown from two to nearly twenty. If in the early years most scientists working with…”
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    Journal Article
  2. 2

    Identification of New FG-Repeat Nucleoporins with Amyloid Properties by Danilov, Lavrentii G, Sukhanova, Xenia V, Rogoza, Tatiana M, Antonova, Ekaterina Y, Trubitsina, Nina P, Zhouravleva, Galina A, Bondarev, Stanislav A

    “…Amyloids are fibrillar protein aggregates with a cross-β structure. More than two hundred different proteins with amyloid or amyloid-like properties are…”
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  3. 3

    Nonsense Mutations in the Yeast SUP35 Gene Affect the [ PSI + ] Prion Propagation by Trubitsina, Nina P, Zemlyanko, Olga M, Bondarev, Stanislav A, Zhouravleva, Galina A

    “…The essential gene encodes yeast translation termination factor eRF3. Previously, we isolated nonsense mutations and proposed that the viability of such…”
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  4. 4

    Structure and Polymorphism of Amyloid and Amyloid-Like Aggregates by Matiiv, Anton B., Trubitsina, Nina P., Matveenko, Andrew G., Barbitoff, Yury A., Zhouravleva, Galina A., Bondarev, Stanislav A.

    Published in Biochemistry (Moscow) (01-05-2022)
    “…Amyloids are protein aggregates with the cross-β structure. The interest in amyloids is explained, on the one hand, by their role in the development of…”
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  5. 5

    Role of the Gut Microbiome and Bacterial Amyloids in the Development of Synucleinopathies by Trubitsina, Nina P., Matiiv, Anton B., Rogoza, Tatyana M., Zudilova, Anna A., Bezgina, Mariya D., Zhouravleva, Galina A., Bondarev, Stanislav A.

    Published in Biochemistry (Moscow) (01-03-2024)
    “…Less than ten years ago, evidence began to accumulate about association between the changes in the composition of gut microbiota and development of human…”
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  6. 6

    Point mutations affecting yeast prion propagation change the structure of its amyloid fibrils by Sulatskaya, Anna I., Bondarev, Stanislav A., Sulatsky, Maksim I., Trubitsina, Nina P., Belousov, Mikhail V., Zhouravleva, Galina A., Llanos, Manuel A., Kajava, Andrey V., Kuznetsova, Irina M., Turoverov, Konstantin K.

    Published in Journal of molecular liquids (15-09-2020)
    “…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…”
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