Substitutions of PrP N-terminal histidine residues modulate scrapie disease pathogenesis and incubation time in transgenic mice.

Substitutions of PrP N-terminal histidine residues modulate scrapie disease pathogenesis and incubation time in transgenic mice.

Prion diseases have been linked to impaired copper homeostasis and copper induced-oxidative damage to the brain. Divalent metal ions, such as Cu2+ and Zn2+, bind to cellular prion protein (PrPC) at octapeptide repeat (OR) and non-OR sites within the N-terminal half of the protein but information on...

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Bibliographic Details
Main Authors: Sabina Eigenbrod, Petra Frick, Uwe Bertsch, Gerda Mitteregger-Kretzschmar, Janina Mielke, Marko Maringer, Niklas Piening, Alexander Hepp, Nathalie Daude, Otto Windl, Johannes Levin, Armin Giese, Vignesh Sakthivelu, Jörg Tatzelt, Hans Kretzschmar, David Westaway
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2017-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC5722314?pdf=render

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http://europepmc.org/articles/PMC5722314?pdf=render

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