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 language | English (US) |
|---|---|
| Journal | Trends in Cell Biology |
| DOIs | |
| State | Accepted/In press - 2017 |
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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 journal › Article
}
TY - JOUR
T1 - Disentangling a Bad Reputation
T2 - Changing Perceptions of Amyloids
AU - Wang, Miling
AU - Audas, Timothy E.
AU - Lee, Stephen
PY - 2017
Y1 - 2017
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. 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.
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. 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.
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 - Article
JO - Trends in Cell Biology
JF - Trends in Cell Biology
SN - 0962-8924
ER -