Prion Proteins with Different Conformations Accumulate in Gerstmann-Sträussler-Scheinker Disease Caused by A117V and F198S Mutations
Open Access
- 1 June 2001
- journal article
- Published by Elsevier in The American Journal of Pathology
- Vol. 158 (6), 2201-2207
- https://doi.org/10.1016/s0002-9440(10)64692-5
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- A 7-kDa Prion Protein (PrP) Fragment, an Integral Component of the PrP Region Required for Infectivity, Is the Major Amyloid Protein in Gerstmann-Sträussler-Scheinker Disease A117VJournal of Biological Chemistry, 2001
- Prion Protein Selectively Binds Copper(II) IonsBiochemistry, 1998
- Physical Studies of Conformational Plasticity in a Recombinant Prion ProteinBiochemistry, 1997
- Metal‐dependent α‐helix formation promoted by the glycine‐rich octapeptide region of prion proteinFEBS Letters, 1996
- Molecular basis of phenotypic variability in sporadc creudeldt‐jakob diseaseAnnals of Neurology, 1996
- Prion Protein AmyloidosisBrain Pathology, 1996
- Copper Binding to the N-Terminal Tandem Repeat Region of Mammalian and Avian Prion Protein: Structural Studies Using Synthetic PeptidesBiochemical and Biophysical Research Communications, 1995
- Truncated Forms of the Human Prion Protein in Normal Brain and in Prion DiseasesJournal of Biological Chemistry, 1995
- Conformational Transformations in Peptides Containing Two Putative α-Helices of the Prion ProteinJournal of Molecular Biology, 1995
- Linkage of the Indiana kindred of Gerstmann-Sträussler-Scheinker disease to the prion protein geneNature Genetics, 1992