title: Disentangling a Bad Reputation: Changing Perceptions of Amyloids.
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.
authors.affiliation: Department of Biochemistry and Molecular Biology, Miller School of Medicine, University of Miami, Miami, FL 31336, USA; Sylvester Comprehensive Cancer Center, Miller School of Medicine, University of Miami, Miami, FL 31336, USA.
authors.forename: Miling
authors.initials: M
authors.lastname: Wang
authors.affiliation: Department of Molecular Biology and Biochemistry, Simon Fraser University, 8888 University Drive, Burnaby, BC V5A 1S6, Canada.
authors.forename: Timothy E
authors.initials: TE
authors.lastname: Audas
authors.affiliation: Department of Biochemistry and Molecular Biology, Miller School of Medicine, University of Miami, Miami, FL 31336, USA; Sylvester Comprehensive Cancer Center, Miller School of Medicine, University of Miami, Miami, FL 31336, USA. Electronic address: stephenlee@med.miami.edu.
authors.forename: Stephen
authors.initials: S
authors.lastname: Lee
mesh_terms: D000682:Amyloid / Q000235:genetics / Q000378:metabolism*; D000686:Amyloidosis / Q000235:genetics; D006801:Humans; D019636:Neurodegenerative Diseases / Q000378:metabolism / Q000473:pathology; D066329:Protein Aggregates; D017510:Protein Folding
chemical_list: D000682:Amyloid; D066329:Protein Aggregates
keywords: Alzheimer’s; amyloid; dormancy; phase transition; protein folding