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Structures for amyloid fibrils (mini-review)

journal contribution
posted on 2023-06-08, 07:38 authored by O Sumner Makin, Louise SerpellLouise Serpell
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

History

Publication status

  • Published

Journal

FEBS Journal

ISSN

1742-464X

Issue

23

Volume

272

Page range

5950-5961

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

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