Structure of infectious prions: stabilization by domain swapping
Open Access
- 16 September 2005
- journal article
- Published by Wiley in The FASEB Journal
- Vol. 19 (13) , 1778-1782
- https://doi.org/10.1096/fj.05-4067hyp
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Synthetic Mammalian PrionsScience, 2004
- Prion Protein Interaction with the C-Terminal SH3 Domain of Grb2 Studied Using NMR and Optical SpectroscopyBiochemistry, 2004
- Molecular modeling of the core of Aβ amyloid fibrilsProteins-Structure Function and Bioinformatics, 2004
- β-Helix is a likely core structure of yeast prion Sup35 amyloid fibersBiochemical and Biophysical Research Communications, 2004
- Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation processNature Structural & Molecular Biology, 2003
- Formation of Monodispersed Nano‐ and Micro‐Particles Controlled in Size, Shape, and Internal StructureChemical Engineering & Technology, 2003
- Intramolecular VersusIntermolecular Disulfide Bonds in Prion ProteinsJournal of Biological Chemistry, 2002
- A proposed structural model for amyloid fibril elongation: domain swapping forms an interdigitating β-structure polymerProtein Engineering, Design and Selection, 2001
- 3D domain swapping: A mechanism for oligomer assemblyProtein Science, 1995
- AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of moleculesComputer Physics Communications, 1995