Conformational Stability of PrP Amyloid Fibrils Controls Their Smallest Possible Fragment Size
- 29 February 2008
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 376 (4) , 1155-1167
- https://doi.org/10.1016/j.jmb.2007.12.053
Abstract
No abstract availableKeywords
This publication has 79 references indexed in Scilit:
- A simplified recipe for prionsProceedings 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
- Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypesProceedings of the National Academy of Sciences, 2006
- Lipid-Induced β-Amyloid Peptide Assemblage FragmentationBiophysical Journal, 2006
- The physical basis of how prion conformations determine strain phenotypesNature, 2006
- Dichotomous versus palm‐type mechanisms of lateral assembly of amyloid fibrilsProtein Science, 2006
- The most infectious prion protein particlesNature, 2005
- Double-stranded siRNA targeted to the huntingtin gene does not induce DNA methylationBiochemical and Biophysical Research Communications, 2004
- Small heat shock proteins from extremophiles: a reviewExtremophiles, 2004
- The Chaperone Protein BiP Binds to a Mutant Prion Protein and Mediates Its Degradation by the ProteasomeJournal of Biological Chemistry, 2000