β-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptides.

Protein misfolding disorders are associated with conformational changes in specific proteins, leading to the formation of potentially neurotoxic amyloid fibrils. During pathogenesis of prion disease, the prion protein misfolds into β-sheet rich, protease-resistant isoforms. A key, hydrophobic domain...

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Auteur principal: Andrew C Gill
Format: article
Langue:EN
Publié: Public Library of Science (PLoS) 2014
Sujets:
R
Q
Accès en ligne:https://doaj.org/article/4034f86520c74aa2ba8344ed5fb3f26a
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