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Familial prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM

2021-02-18

Abstract excerpt

Prion diseases are caused by the conformational conversion of prion protein (PrP) from its cellular form (PrP C ) into a protease-resistant, aggregated form (PrP Sc ). 42 different familial mutations were identified in human PrP, which lead to genetic prion diseases with distinct clinical syndromes. Here we report cryo-EM structure of an amyloid fibril formed by full-length human PrP with E196K mutation, a famil...

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Literature Corpus work
8c718d90-d9aa-5fe0-befd-f171a28b3538
DOI
10.1101/2021.02.18.431846
Open publication

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Familial prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EMDOI 10.1101/2021.02.18.431846
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