Disentangling a Bad Reputation

Changing Perceptions of Amyloids

Miling Wang, Timothy E. Audas, Stephen Lee

Research output: Contribution to journalArticle

6 Citations (Scopus)

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. Cells exploit the amyloid fibrillation propensity of proteins in physiology.Systemic physiological amyloidogenesis programs induce a state of dormancy.Amyloid-like assemblies exhibit properties of solid-state protein organization.Insights from physiological amyloidogenesis open potential novel avenues of investigation for amyloid pathogenesis.

Original languageEnglish (US)
JournalTrends in Cell Biology
DOIs
StateAccepted/In press - 2017

Fingerprint

Amyloid
Proteins
Poisons
Neurodegenerative Diseases
Parkinson Disease
Alzheimer Disease

Keywords

  • Alzheimer's
  • Amyloid
  • Dormancy
  • Phase transition
  • Protein folding

ASJC Scopus subject areas

  • Cell Biology

Cite this

Disentangling a Bad Reputation : Changing Perceptions of Amyloids. / Wang, Miling; Audas, Timothy E.; Lee, Stephen.

In: Trends in Cell Biology, 2017.

Research output: Contribution to journalArticle

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