The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
The therapeutic potential of chemical chaperones in protein folding diseases
Open accessAbstract
Several neurodegenerative diseases are caused by defects in protein folding, including Alzheimer, Parkinson, Huntington, and prion diseases. Once a disease-specific protein misfolds, it can then form toxic aggregates which accumulate in the brain, leading to neuronal dysfunction, cell death, and clinical symptoms. Although significant advances have been made toward understanding the mechanisms of protein aggregation, there are no curative treatments for any of these diseases. Since protein misfolding and the accumulation of aggregates are the most upstream events in the pathological cascade, rescuing or stabilizing the native conformations of proteins is an obvious therapeutic strategy. In recent years, small molecules known as chaperones have been shown to be effective in reducing levels of misfolded proteins, thus minimizing the accumulation of aggregates and their downstream pathological consequences. Chaperones are classified as molecular, pharmacological, or chemical. In this mini-review we summarize the modes of action of different chemical chaperones and discuss evidence for their efficacy in the treatment of protein folding diseases in vitro and in vivo.
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Metadata
- Authors
- Cortez, L., & Sim, V.
- Venue
- Prion
- Publisher
- Informa UK Limited
- Published
- 2014-03
- Volume
- 8
- Issue
- 2
- Pages
- 197-202
- ISSN
- 1933-6896 (ISSN-L)
- 1933-690X
- OpenAlex
- W2065631672
- Cited by
- 254
- References
- 62
- FWCI
- 5.23
- Type
- journal article
- Language
- en
- Open access
- bronze
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