Distinct Structures of Scrapie Prion Protein (PrPSc)-seeded Versus Spontaneous Recombinant Prion Protein Fibrils Revealed by Hydrogen/Deuterium Exchange
Open Access
- 1 September 2009
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 284 (36), 24233-24241
- https://doi.org/10.1074/jbc.m109.036558
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Getting a Grip on Prions: Oligomers, Amyloids, and Pathological Membrane InteractionsAnnual Review of Biochemistry, 2009
- Prion Diseases and Their Biochemical MechanismsBiochemistry, 2009
- Protein inheritance (prions) based on parallel in‐register β‐sheet amyloid structuresBioEssays, 2008
- Host PrP Glycosylation: A Major Factor Determining the Outcome of Prion InfectionPLoS Biology, 2008
- Mechanisms of prion protein assembly into amyloidProceedings of the National Academy of Sciences, 2008
- Molecular architecture of human prion protein amyloid: A parallel, in-register β-structureProceedings of the National Academy of Sciences, 2007
- Formation of native prions from minimal components in vitroProceedings of the National Academy of Sciences, 2007
- β-Sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchangeProceedings of the National Academy of Sciences, 2007
- Correlation of structural elements and infectivity of the HET-s prionNature, 2005
- Concentration and distribution of infectivity and PrPSc following partial denaturation of a mouse-adapted and a hamster-adapted scrapie strainArchiv für die gesamte Virusforschung, 1994