Review: Model Peptides and the Physicochemical Approach to β-Amyloids
- 1 June 2000
- journal article
- review article
- Published by Elsevier in Journal of Structural Biology
- Vol. 130 (2-3) , 153-173
- https://doi.org/10.1006/jsbi.2000.4287
Abstract
No abstract availableKeywords
This publication has 172 references indexed in Scilit:
- Two-Dimensional Structure of β-Amyloid(10−35) FibrilsBiochemistry, 2000
- Nature disfavors sequences of alternating polar and non-polar amino acids: implications for amyloidogenesis 1 1Edited by F. E. CohenJournal of Molecular Biology, 2000
- 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
- Interaction between G-Actin and Various Types of Liposomes: A 19F, 31P, and 2H Nuclear Magnetic Resonance StudyBiochemistry, 1998
- Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helixStructure, 1996
- Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's diseaseJournal of Molecular Biology, 1992
- Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.Journal of Biological Chemistry, 1992
- Solution Structures of β Peptide and Its Constituent Fragments: Relation to Amyloid DepositionScience, 1991
- Cross-β protein structures. I. Insulin fibrilsBiochemistry, 1972
- Characterization of the Amyloid Fibril as a Cross- ProteinExperimental Biology and Medicine, 1969