Article
Post-translational modifications in PrP expand the conformational diversity of prions in vivo.
Scientific reports - 8 Mar 2017
Aguilar-Calvo Patricia, Xiao Xiangzhu, Bett Cyrus, Eraña Hasier, Soldau Katrin, Castilla Joaquin, Nilsson K Peter R, Surewicz Witold K, Sigurdson Christina J
Abstract excerpt
Misfolded prion protein aggregates (PrPSc) 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 through poorly understood mechanisms. Here we use mice expressing glycophosphatidylinositol (GPI)-anchorless prion...
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