Conformational Plasticity of the Gerstmann–Sträussler–Scheinker Disease Peptide as Indicated by Its Multiple Aggregation Pathways
- 28 June 2008
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 381 (5) , 1349-1361
- https://doi.org/10.1016/j.jmb.2008.06.063
Abstract
No abstract availableKeywords
This publication has 60 references indexed in Scilit:
- Mechanisms of prion protein assembly into amyloidProceedings of the National Academy of Sciences, 2008
- Neurotoxic and Gliotrophic Activity of a Synthetic Peptide Homologous to Gerstmann–Sträussler–Scheinker Disease Amyloid ProteinJournal of Neuroscience, 2007
- Osmolyte Trimethylamine N-Oxide Converts Recombinant α-Helical Prion Protein to its Soluble β-Structured Form at High TemperatureJournal of Molecular Biology, 2006
- Aggregation/Fibrillogenesis of Recombinant Human Prion Protein and Gerstmann−Sträussler−Scheinker Disease Peptides in the Presence of Metal IonsBiochemistry, 2006
- Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopyBiochemical Journal, 2005
- Direct Observation of Aβ Amyloid Fibril Growth and InhibitionJournal of Molecular Biology, 2004
- Hierarchical Assembly of β2-Microglobulin Amyloid In Vitro Revealed by Atomic Force MicroscopyJournal of Molecular Biology, 2003
- α-Synuclein, Especially the Parkinson's Disease-associated Mutants, Forms Pore-like Annular and Tubular ProtofibrilsJournal of Molecular Biology, 2002
- Annular α-Synuclein Protofibrils Are Produced When Spherical Protofibrils Are Incubated in Solution or Bound to Brain-Derived MembranesBiochemistry, 2002
- Tetracycline affects abnormal properties of synthetic PrP peptides and PrPSc in vitro11Edited by J. KarnJournal of Molecular Biology, 2000