期刊
FEBS LETTERS
卷 582, 期 17, 页码 2537-2541出版社
WILEY
DOI: 10.1016/j.febslet.2008.06.021
关键词
oligomers; amyloid; serpin; Alzheimers; prions
资金
- British Heart Foundation Funding Source: Medline
- Wellcome Trust Funding Source: Medline
Many disorders, including Alzheimer's, the prion encephalopathies and other neurodegenerative diseases, result from aberrant protein aggregation. Surprisingly, cellular toxicity is often due not to the highly- ordered aggregates but to the oligomers that precede their formation. Using serpins as a paradigm, we show how the active and infective interface of oligomers is inherently toxic and can promiscuously bind to unrelated peptides, including neurotransmitters. Extension of the oligomer and its eventual sequestration as amyloid can thus be seen as a protective response to block the toxic interface. We illustrate how the preferential self- association that gives this protection has been selectively favoured. (c) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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