Journal article
Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways
Prion, Vol.3(2), pp.51-58
2009
DOI: 10.4161/pri.3.2.8587
PMCID: PMC2712599
PMID: 19421006
Abstract
The self-association of misfolded or damaged proteins into ordered amyloid-like aggregates characterizes numerous neurodegenerative disorders. Insoluble amyloid plaques are diagnostic of many disease states. Yet soluble, oligomeric intermediates in the aggregation pathway appear to represent the toxic culprit. Molecular chaperones regulate the fate of misfolded proteins and thereby influence their aggregation state. Chaperones conventionally antagonize aggregation of misfolded, disease proteins and assist in refolding or degradation pathways. Recent work suggests that chaperones may also suppress neurotoxicity by converting toxic, soluble oligomers into benign aggregates. Chaperones can therefore suppress or promote aggregation of disease proteins to ameliorate the proteotoxic accumulation of soluble, assembly intermediates.
Details
- Title: Subtitle
- Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways
- Creators
- Peter M Douglas - Department of Cell and Developmental Biology; School of Medicine; University of North Carolina; Chapel Hill, NC USADaniel W Summers - Department of Cell and Developmental Biology; School of Medicine; University of North Carolina; Chapel Hill, NC USADouglas M Cyr - Department of Cell and Developmental Biology; School of Medicine; University of North Carolina; Chapel Hill, NC USA
- Resource Type
- Journal article
- Publication Details
- Prion, Vol.3(2), pp.51-58
- Publisher
- Landes Bioscience
- DOI
- 10.4161/pri.3.2.8587
- PMID
- 19421006
- PMCID
- PMC2712599
- ISSN
- 1933-6896
- eISSN
- 1933-690X
- Language
- English
- Date published
- 2009
- Academic Unit
- Iowa Neuroscience Institute; Biology
- Record Identifier
- 9984070459002771
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