Post-translational modifications in PrP expand the conformational diversity of prions in vivo

Misfolded prion protein aggregates (PrP(Sc)) show remarkable structural diversity and are associated with highly variable disease phenotypes. Similarly, other proteins, including amyloid-β, tau, α-synuclein, and serum amyloid A, misfold into distinct conformers linked to different clinical diseases...

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Bibliographic Details
Published in:Sci Rep
Main Authors: Aguilar-Calvo, Patricia, Xiao, Xiangzhu, Bett, Cyrus, Eraña, Hasier, Soldau, Katrin, Castilla, Joaquin, Nilsson, K. Peter R., Surewicz, Witold K., Sigurdson, Christina J.
Format: Artigo
Language:Inglês
Published: Nature Publishing Group 2017
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Article
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC5341109/
https://ncbi.nlm.nih.gov/pubmed/28272426
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/srep43295
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