title: Molecular model of prion transmission to humans.
abstract: To assess interspecies barriers to transmission of transmissible spongiform encephalopathies, we investigated the ability of disease-associated prion proteins (PrPd) to initiate conversion of the human normal cellular form of prion protein of the 3 major PRNP polymorphic variants in vitro. Protein misfolding cyclic amplification showed that conformation of PrPd partly determines host susceptibility.
authors: National CJD Surveillance Unit, School of Molecular and Clinical Medicine, University of Edinburgh, Western General Hospital, Edinburgh, Scotland EH4 2XU, UK. mjones1@staffmail.ed.ac.uk
authors: Michael
authors: M
authors: Jones
authors: Darren
authors: D
authors: Wight
authors: Rona
authors: R
authors: Barron
authors: Martin
authors: M
authors: Jeffrey
authors: Jean
authors: J
authors: Manson
authors: Christopher
authors: C
authors: Prowse
authors: James W
authors: JW
authors: Ironside
authors: Mark W
authors: MW
authors: Head
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D004198:Disease Susceptibility; D006801:Humans; D051379:Mice; D017096:Prion Diseases / Q000635:transmission*; D011328:Prions / Q000737:chemistry*; D017510:Protein Folding; D020033:Protein Isoforms
chemical_list: D011328:Prions; D020033:Protein Isoforms