Disentangling a Bad Reputation: Changing Perceptions of Amyloids

Miling Wang; Timothy E. Audas; Stephen Lee

doi:10.1016/j.tcb.2017.03.001

Disentangling a Bad Reputation: Changing Perceptions of Amyloids

Miling Wang, Timothy E. Audas, Stephen Lee

Biochemistry & Molecular Biology

Research output: Contribution to journal › Short survey › peer-review

10 Scopus citations

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	https://doi.org/10.1016/j.tcb.2017.03.001
State	Published - Jul 2017

Keywords

Alzheimer's
amyloid
dormancy
phase transition
protein folding

ASJC Scopus subject areas

Cell Biology

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10.1016/j.tcb.2017.03.001

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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.",

keywords = "Alzheimer's, amyloid, dormancy, phase transition, protein folding",

author = "Miling Wang and Audas, {Timothy E.} and Stephen Lee",

note = "Publisher Copyright: {\textcopyright} 2017 Elsevier Ltd",

year = "2017",

month = jul,

doi = "10.1016/j.tcb.2017.03.001",

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AU - Audas, Timothy E.

AU - Lee, Stephen

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AB - 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.

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KW - amyloid

KW - dormancy

KW - phase transition

KW - protein folding

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Disentangling a Bad Reputation: Changing Perceptions of Amyloids

Abstract

Keywords

ASJC Scopus subject areas

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