Direct visualisation of the β-sheet structure of synthetic Alzheimer’s amyloid
- 26 May 2000
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 299 (1), 225-231
- https://doi.org/10.1006/jmbi.2000.3650
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Propagating structure of Alzheimer’s β-amyloid (10–35) is parallel β-sheet with residues in exact registerProceedings of the National Academy of Sciences, 1998
- Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helixStructure, 1996
- MRC Image Processing ProgramsJournal of Structural Biology, 1996
- Conformation and Fibrillogenesis of Alzheimer Aβ Peptides with Selected Substitution of Charged ResiduesJournal of Molecular Biology, 1994
- Fibril formation by primate, rodent, and Dutch-hemorrhagic analogs of Alzheimer amyloid .beta.-proteinBiochemistry, 1992
- pH-dependent structural transitions of Alzheimer amyloid peptidesBiophysical Journal, 1991
- Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopyBiochemistry, 1991
- Resistance of Scrapie Infectivity to Steam Autoclaving after Formaldehyde Fixation and Limited Survival after Ashing at 360 C: Practical and Theoretical ImplicationsThe Journal of Infectious Diseases, 1990
- Conformation of twisted β-pleated sheets in proteinsJournal of Molecular Biology, 1973
- X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTSJournal of Histochemistry & Cytochemistry, 1968