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Disentangling a Bad Reputation: Changing Perceptions of Amyloids
Miling Wang1, Timothy E Audas2, Stephen Lee1
1Department 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.
Trends in Cell Biology
|April 1, 2017
Summary
Amyloids, once thought toxic, are now understood to have vital physiological roles. This research redefines amyloid structures as reversible and essential for cellular functions, challenging previous disease-centric views.
Area of Science:
- Biochemistry
- Cell Biology
- Neuroscience
Background:
- Amyloid aggregates were historically linked to neurodegenerative diseases like Alzheimer's and Parkinson's, perceived as toxic and irreversible.
- This view is being challenged by emerging evidence of physiological roles for amyloid formation within cells.
Purpose of the Study:
- To re-evaluate the role of amyloid structures in cellular biology.
- To explore the concept of amyloidogenesis as a physiological and reversible process.
Main Methods:
- Review of recent scientific literature.
- Analysis of emerging data on amyloid structures in cellular contexts.
Main Results:
- Identified widespread cellular functions associated with physiological amyloidogenesis.
- Demonstrated that amyloid structures can be reversible, not just toxic aggregates.
Conclusions:
- The amyloid-fold represents a distinct, physiological, and reversible protein organization.
- Amyloid structures should be considered alongside native and unfolded protein states in biological systems.