| Literature DB >> 28359692 |
Miling Wang1, Timothy E Audas2, Stephen Lee3.
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.Entities:
Keywords: Alzheimer’s; amyloid; dormancy; phase transition; protein folding
Mesh:
Substances:
Year: 2017 PMID: 28359692 PMCID: PMC5476492 DOI: 10.1016/j.tcb.2017.03.001
Source DB: PubMed Journal: Trends Cell Biol ISSN: 0962-8924 Impact factor: 20.808