Prions and Non-infectious Amyloids of Mammals – Similarities and Differences

A. P. Galkin, M. E. Velizhanina, Yu V. Sopova, A. A. Shenfeld, S. P. Zadorsky

Результат исследований: Научные публикации в периодических изданияхОбзорная статьянаучнаярецензирование

Выдержка

Amyloids are highly ordered aggregates of protein fibrils exhibiting cross-β structure formed by intermolecular hydrogen bonds. Pathological amyloid deposition is associated with the development of several socially significant incurable human diseases. Of particular interest are infectious amyloids, or prions, that cause several lethal neurodegenerative diseases in humans and can be transmitted from one organism to another. Because of almost complete absence of criteria for infectious and non-infectious amyloids, there is a lack of consensus, especially, in the definition of similarities and differences between prions and non-infectious amyloids. In this review, we formulated contemporary molecular-biological criteria for identification of prions and non-infectious amyloids and focused on explaining the differences between these two types of molecules.

Язык оригиналаанглийский
Страницы (с-по)1184-1195
Число страниц12
ЖурналBiochemistry (Moscow)
Том83
Номер выпуска10
DOI
СостояниеОпубликовано - 2018

Ключевые слова

    Предметные области Scopus

    • Биохимия

    Цитировать

    Galkin, A. P. ; Velizhanina, M. E. ; Sopova, Yu V. ; Shenfeld, A. A. ; Zadorsky, S. P. / Prions and Non-infectious Amyloids of Mammals – Similarities and Differences. В: Biochemistry (Moscow). 2018 ; Том 83, № 10. стр. 1184-1195.
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    abstract = "Amyloids are highly ordered aggregates of protein fibrils exhibiting cross-β structure formed by intermolecular hydrogen bonds. Pathological amyloid deposition is associated with the development of several socially significant incurable human diseases. Of particular interest are infectious amyloids, or prions, that cause several lethal neurodegenerative diseases in humans and can be transmitted from one organism to another. Because of almost complete absence of criteria for infectious and non-infectious amyloids, there is a lack of consensus, especially, in the definition of similarities and differences between prions and non-infectious amyloids. In this review, we formulated contemporary molecular-biological criteria for identification of prions and non-infectious amyloids and focused on explaining the differences between these two types of molecules.",
    keywords = "amyloids, fibrils, infectivity, prions, protein aggregates",
    author = "Galkin, {A. P.} and Velizhanina, {M. E.} and Sopova, {Yu V.} and Shenfeld, {A. A.} and Zadorsky, {S. P.}",
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    Prions and Non-infectious Amyloids of Mammals – Similarities and Differences. / Galkin, A. P.; Velizhanina, M. E.; Sopova, Yu V.; Shenfeld, A. A.; Zadorsky, S. P.

    В: Biochemistry (Moscow), Том 83, № 10, 2018, стр. 1184-1195.

    Результат исследований: Научные публикации в периодических изданияхОбзорная статьянаучнаярецензирование

    TY - JOUR

    T1 - Prions and Non-infectious Amyloids of Mammals – Similarities and Differences

    AU - Galkin, A. P.

    AU - Velizhanina, M. E.

    AU - Sopova, Yu V.

    AU - Shenfeld, A. A.

    AU - Zadorsky, S. P.

    PY - 2018

    Y1 - 2018

    N2 - Amyloids are highly ordered aggregates of protein fibrils exhibiting cross-β structure formed by intermolecular hydrogen bonds. Pathological amyloid deposition is associated with the development of several socially significant incurable human diseases. Of particular interest are infectious amyloids, or prions, that cause several lethal neurodegenerative diseases in humans and can be transmitted from one organism to another. Because of almost complete absence of criteria for infectious and non-infectious amyloids, there is a lack of consensus, especially, in the definition of similarities and differences between prions and non-infectious amyloids. In this review, we formulated contemporary molecular-biological criteria for identification of prions and non-infectious amyloids and focused on explaining the differences between these two types of molecules.

    AB - Amyloids are highly ordered aggregates of protein fibrils exhibiting cross-β structure formed by intermolecular hydrogen bonds. Pathological amyloid deposition is associated with the development of several socially significant incurable human diseases. Of particular interest are infectious amyloids, or prions, that cause several lethal neurodegenerative diseases in humans and can be transmitted from one organism to another. Because of almost complete absence of criteria for infectious and non-infectious amyloids, there is a lack of consensus, especially, in the definition of similarities and differences between prions and non-infectious amyloids. In this review, we formulated contemporary molecular-biological criteria for identification of prions and non-infectious amyloids and focused on explaining the differences between these two types of molecules.

    KW - amyloids

    KW - fibrils

    KW - infectivity

    KW - prions

    KW - protein aggregates

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    U2 - 10.1134/S0006297918100048

    DO - 10.1134/S0006297918100048

    M3 - Review article

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    JO - Biochemistry (Moscow)

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