The Same Primary Structure of the Prion Protein Yields Two Distinct Self-propagating States
Open Access
- 1 June 2008
- journal article
- Published by Elsevier
- Vol. 283 (23) , 15988-15996
- https://doi.org/10.1074/jbc.m800562200
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Formation of native prions from minimal components in vitroProceedings of the National Academy of Sciences, 2007
- Nonpolar Substitution at the C-Terminus of the Prion Protein, a Mimic of the Glycosylphosphatidylinositol Anchor, Partially Impairs Amyloid Fibril FormationBiochemistry, 2006
- Dichotomous versus palm‐type mechanisms of lateral assembly of amyloid fibrilsProtein Science, 2006
- Polymorphism and Ultrastructural Organization of Prion Protein Amyloid Fibrils: An Insight from High Resolution Atomic Force MicroscopyJournal of Molecular Biology, 2006
- Search for a Prion-Specific Nucleic AcidJournal of Virology, 2005
- In vitro Conversion of Full-length Mammalian Prion Protein Produces Amyloid Form with Physical Properties of PrPScJournal of Molecular Biology, 2005
- Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid FibrilsScience, 2005
- A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform 1 1Edited by M. YanivJournal of Molecular Biology, 1997
- Evidence for the Conformation of the Pathologic Isoform of the Prion Protein Enciphering and Propagating Prion DiversityScience, 1996
- A 'unified theory' of prion propagationNature, 1991