Structures for amyloid fibrils
- 16 November 2005
- journal article
- review article
- Published by Wiley in The FEBS Journal
- Vol. 272 (23), 5950-5961
- https://doi.org/10.1111/j.1742-4658.2005.05025.x
Abstract
Alzheimer's disease and Creutzfeldt–Jakob disease are the best‐known examples of a group of diseases known as the amyloidoses. They are characterized by the extracellular deposition of toxic, insoluble amyloid fibrils. Knowledge of the structure of these fibrils is essential for understanding the process of pathology of the amyloidoses and for the rational design of drugs to inhibit or reverse amyloid formation. Structural models have been built using information from a wide variety of techniques, including X‐ray diffraction, electron microscopy, solid state NMR and EPR. Recent advances have been made in understanding the architecture of the amyloid fibril. Here, we describe and compare postulated structural models for the mature amyloid fibril and discuss how the ordered structure of amyloid contributes to its stability.Keywords
This publication has 103 references indexed in Scilit:
- Correlation of structural elements and infectivity of the HET-s prionNature, 2005
- Structure of the cross-β spine of amyloid-like fibrilsNature, 2005
- Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid FibrilsScience, 2005
- Mapping Aβ Amyloid Fibril Secondary Structure Using Scanning Proline MutagenesisJournal of Molecular Biology, 2004
- Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolutionJournal of Molecular Medicine, 2003
- Rationalization of the effects of mutations on peptide andprotein aggregation ratesNature, 2003
- Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopyJournal of Molecular Biology, 2001
- Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformationProceedings of the National Academy of Sciences, 2000
- Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packingThe EMBO Journal, 1999
- Examination of the Structure of the Transthyretin Amyloid Fibril by Image Reconstruction from Electron MicrographsJournal of Molecular Biology, 1995