Membrane perturbation effects of peptides derived from the N-termini of unprocessed prion proteins
- 21 September 2005
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Biomembranes
- Vol. 1716 (2), 126-136
- https://doi.org/10.1016/j.bbamem.2005.09.009
Abstract
No abstract availableKeywords
This publication has 54 references indexed in Scilit:
- Transmissible spongiform encephalopathiesThe Lancet, 2004
- PROTOFIBRILS, PORES, FIBRILS, AND NEURODEGENERATION: Separating the Responsible Protein Aggregates from The Innocent BystandersAnnual Review of Neuroscience, 2003
- Most Pathogenic Mutations Do Not Alter the Membrane Topology of the Prion ProteinPublished by Elsevier ,2001
- NMR structure of the bovine prion proteinProceedings of the National Academy of Sciences, 2000
- Transmissible and genetic prion diseases share a common pathway of neurodegenerationNature, 1999
- A Transmembrane Form of the Prion Protein in Neurodegenerative DiseaseScience, 1998
- Cell-free formation of protease-resistant prion proteinNature, 1994
- Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins.Proceedings of the National Academy of Sciences, 1993
- Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencingBiochemistry, 1993
- Molecular Biology of Prion DiseasesScience, 1991