The DOI matches its Crossref record; 174 of the 174 references it cites were found in a registry or an index.
Heat shock transcription factor 1 as a therapeutic target in neurodegenerative diseases
Open accessAbstract
Neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis and prion-based neurodegeneration are associated with the accumulation of misfolded proteins, resulting in neuronal dysfunction and cell death. However, current treatments for these diseases predominantly address disease symptoms, rather than the underlying protein misfolding and cell death, and are not able to halt or reverse the degenerative process. Studies in cell culture, fruitfly, worm and mouse models of protein misfolding-based neurodegenerative diseases indicate that enhancing the protein-folding capacity of cells, via elevated expression of chaperone proteins, has therapeutic potential. Here, we review advances in strategies to harness the power of the natural cellular protein-folding machinery through pharmacological activation of heat shock transcription factor 1 — the master activator of chaperone protein gene expression — to treat neurodegenerative diseases.
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Self-citationMolecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis
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Protein misfolding in neurodegenerative diseases: Implications and strategies
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Identifying phenotype-associated subpopulations by integrating bulk and single-cell sequencing data
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Metadata
- Authors
- Neef, D. W., Jaeger, A. M., & Thiele, D. J.
- Venue
- Nature Reviews Drug Discovery
- Published
- 2011-12
- Volume
- 10
- Issue
- 12
- Pages
- 930-944
- ISSN
- 1474-1776 (ISSN-L)
- 1474-1784
- OpenAlex
- W2014061195
- Cited by
- 307
- References
- 174
- FWCI
- 1.37
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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