Makin, O Sumner and Serpell, Louise C (2005) Structures for amyloid fibrils (mini-review). FEBS Journal, 272 (23). pp. 5950-5961. ISSN 1742-464X

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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

Item Type:	Article
Schools and Departments:	School of Life Sciences > Biochemistry
Depositing User:	Osmar Sumner Makin
Date Deposited:	06 Feb 2012 20:45
Last Modified:	22 Mar 2012 15:04
URI:	http://sro.sussex.ac.uk/id/eprint/27879

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