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The molecular basis of amyloidosis

journal contribution
posted on 2023-06-08, 09:56 authored by Louise SerpellLouise Serpell, C Blake, M Sunde
Amyloidoses are diseases, including some currently prominent such as Alzheimer's disease, bovine spongiform encephalophaty (BSE) and Type II diabetes, in which soluble proteins are deposited in a specific, highly stable, fibrillar form. The amyloid fibrils are made up of protofilaments whose molecular structure is composed of pairs of ß-sheets in a helical form that allows them to be continuously hydrogen-bonded along the length of the fibril. The observation that similar fibrils are generated from different proteins indicates that fibril formation is accompanied by structural conversion. The transmissible spongiform encephalopathies, such as BSE and kuru, involve an infectious agent identified with the prion protein. The properties of the agent are more consistent with prion amyloid than the protein itself suggesting infectivity in these diseases is equivalent to the 'seeding' of amyloid fibrils at a new site.

History

Publication status

  • Published

Journal

Cellular and Molecular Life Sciences

ISSN

1420-682X

Publisher

Springer Verlag

Issue

11-12

Volume

53

Page range

871-887

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

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