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Proteinase K resistant cores of prions and amyloids.
Kushnirov, Vitaly V; Dergalev, Alexander A; Alexandrov, Alexander I.
Afiliação
  • Kushnirov VV; Research Center of Biotechnology of Russian Academy of Sciences, A.N. Bach Institute of Biochemistry, Moscow, Russia.
  • Dergalev AA; Research Center of Biotechnology of Russian Academy of Sciences, A.N. Bach Institute of Biochemistry, Moscow, Russia.
  • Alexandrov AI; Research Center of Biotechnology of Russian Academy of Sciences, A.N. Bach Institute of Biochemistry, Moscow, Russia.
Prion ; 14(1): 11-19, 2020 12.
Article em En | MEDLINE | ID: mdl-31876447
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 proteinase K (PK). Amyloids can have structural variants, which can be distinguished by the patterns of their digestion by PK. In this review, we describe and compare studies of the resistant cores of various amyloids from different organisms. These data provide insight into the fine structure of amyloids and their variants as well as raise interesting questions, such as those concerning the differences between amyloids obtained ex vivo and in vitro, as well as the manner in which folding of one region of the amyloid can affect other regions.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Príons / Endopeptidase K / Amiloide Limite: Animals / Humans Idioma: En Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Príons / Endopeptidase K / Amiloide Limite: Animals / Humans Idioma: En Ano de publicação: 2020 Tipo de documento: Article