Abstract
Historically, amyloids were perceived as toxic/irreversible protein aggregates associated with neurodegenerative disorders including Alzheimer's and Parkinson's diseases. Recent papers are challenging this perception by uncovering widespread cellular roles for physiological amyloidogenesis. These findings suggest that the amyloid-fold should be considered, alongside the native-fold and unfolded configurations, as a physiological and reversible protein organization.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 465-467 |
| Number of pages | 3 |
| Journal | Trends in Cell Biology |
| Volume | 27 |
| Issue number | 7 |
| DOIs | |
| State | Published - Jul 2017 |
Keywords
- Alzheimer's
- amyloid
- dormancy
- phase transition
- protein folding
ASJC Scopus subject areas
- Cell Biology
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Wang, M., Audas, T. E., & Lee, S. (2017). Disentangling a Bad Reputation: Changing Perceptions of Amyloids. Trends in Cell Biology, 27(7), 465-467. https://doi.org/10.1016/j.tcb.2017.03.001