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

8 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

Access to Document

10.1016/j.tcb.2017.03.001

Cite this

@article{db2cbad919124d7991037ff57ae63333,

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",

language = "English (US)",

volume = "27",

pages = "465--467",

journal = "Trends in Cell Biology",

issn = "0962-8924",

publisher = "Elsevier Limited",

number = "7",

}

TY - JOUR

T1 - Disentangling a Bad Reputation

T2 - Changing Perceptions of Amyloids

AU - Wang, Miling

AU - Audas, Timothy E.

AU - Lee, Stephen

PY - 2017/7

Y1 - 2017/7

N2 - 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.

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.

KW - Alzheimer's

KW - amyloid

KW - dormancy

KW - phase transition

KW - protein folding

UR - http://www.scopus.com/inward/record.url?scp=85016221782&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85016221782&partnerID=8YFLogxK

U2 - 10.1016/j.tcb.2017.03.001

DO - 10.1016/j.tcb.2017.03.001

M3 - Short survey

C2 - 28359692

AN - SCOPUS:85016221782

VL - 27

SP - 465

EP - 467

JO - Trends in Cell Biology

JF - Trends in Cell Biology

SN - 0962-8924

IS - 7

ER -

Disentangling a Bad Reputation: Changing Perceptions of Amyloids

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this