Amyloid Formation by Recombinant Full-length Prion Proteins in Phospholipid Bicelle Solutions
- 31 March 2006
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 357 (3) , 833-841
- https://doi.org/10.1016/j.jmb.2006.01.016
Abstract
No abstract availableKeywords
Funding Information
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
This publication has 53 references indexed in Scilit:
- NMR structure of the bovine prion protein isolated from healthy calf brainsEMBO Reports, 2004
- Short-chain phospholipids as detergentsBiochimica et Biophysica Acta (BBA) - Biomembranes, 2000
- Magnetically Oriented Phospholipid Bilayered Micelles for Structural Studies of Polypeptides. Does the Ideal Bicelle Exist?Journal of Magnetic Resonance, Series B, 1996
- [13] Gentle and fast transmembrane reconstitution of membrane proteinsPublished by Elsevier ,1989
- Spontaneous transmembrane insertion of membrane proteins into lipid vesicles facilitated by short-chain lecithinsBiochemistry, 1986
- Partial Copurification of Scrapie-Associated Fibrils and Scrapie InfectivityIntervirology, 1986
- Scrapie prions aggregate to form amyloid-like birefringent rodsCell, 1983
- A protease-resistant protein is a structural component of the Scrapie prionCell, 1983
- Ultrastructural morphology of amyloid fibrils from neuritic and amyloid plaquesActa Neuropathologica, 1983
- Abnormal fibrils from scrapie-infected brainActa Neuropathologica, 1981