title: Folding and misfolding of the prion protein in the secretory pathway.
abstract: A hallmark of prion diseases in humans and animals is the conversion of the cellular prion protein PrPc to a pathogenic isoform, denoted PrPSc. PrPSc is characterized by distinct biochemical and biophysical properties; in addition, it is the major component of infectious prions. All available data indicate that the only difference between PrPc and PrPSc resides in their conformation, emphasizing a critical role of protein folding in the pathogenesis of prion diseases.
authors.affiliation: Department of Cellular Biochemistry, Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany. tatzelt@biochem.mpg.de
authors.forename: Jorg
authors.initials: J
authors.lastname: Tatzelt
authors.forename: Konstanze F
authors.initials: KF
authors.lastname: Winklhofer
mesh_terms: D000818:Animals; D006801:Humans; D018621:PrPC Proteins / Q000235:genetics / Q000378:metabolism*; D018620:PrPSc Proteins / Q000235:genetics / Q000378:metabolism*; D017096:Prion Diseases / Q000235:genetics / Q000378:metabolism / Q000473:pathology; D017510:Protein Folding; D021381:Protein Transport / Q000235:genetics / Q000502:physiology
chemical_list: D018621:PrPC Proteins; D018620:PrPSc Proteins