Conformational plasticity of recombinant bovine prion protein

Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a special class of neurodegenerative diseases occurring both in humans and animals. TSE pathogenesis is determined by the transition of the native spatial conformation of the cellular protein prion (PrPc), which consist primari...

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Veröffentlicht in:Doklady. Biochemistry and biophysics 2010-02, Vol.430 (1), p.17-19
Hauptverfasser: Grigoriev, V. B., Kalnov, S. L., Pokidyshev, A. N., Klimenko, S. M.
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Sprache:eng
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Zusammenfassung:Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a special class of neurodegenerative diseases occurring both in humans and animals. TSE pathogenesis is determined by the transition of the native spatial conformation of the cellular protein prion (PrPc), which consist primarily of helixes, into the conformation enriched in sheets (PrPsc, PrP). Progression of these diseases is accompanied by the formation of amyloid fibrils (the so called scrapie associated fibrils) in human and animal brain, which consist of PrP and are partially resistant to proteolysis.
ISSN:1607-6729
1608-3091
DOI:10.1134/S1607672910010060