The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Histone deacetylase inhibitors reduce polyglutamine toxicity
Open accessAbstract
Polyglutamine diseases include at least nine neurodegenerative disorders, each caused by a CAG repeat expansion in a different gene. Accumulation of mutant polyglutamine-containing proteins occurs in patients, and evidence from cell culture and animal experiments suggests the nucleus as a site of pathogenesis. To understand the consequences of nuclear accumulation, we created a cell culture system with nuclear-targeted polyglutamine. In our system, cell death can be mitigated by overexpression of full-length cAMP response element binding protein (CREB)-binding protein (CBP) or its amino-terminal portion alone. CBP is one of several histone acetyltransferases sequestered by polyglutamine inclusions. We found histone acetylation to be reduced in cells expressing mutant polyglutamine. Reversal of this hypoacetylation, which can be achieved either by overexpression of CBP or its amino terminus or by treatment with deacetylase inhibitors, reduced cell loss. These findings suggest that nuclear accumulation of polyglutamine can lead to altered protein acetylation in neurons and indicate a novel therapeutic strategy for polyglutamine disease.
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Expansion of an unstable trinucleotide CAG repeat in spinocerebellar ataxia type 1
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Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
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Self-citationA class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases
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CREB-binding protein in androgen receptor-mediated signaling
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Taylor, J. P., Hardy, J., & Fischbeck, K. H. (2002) · Science · doi:10.1126/science.1067122 · Cited by 1,251
Self-citationHuntington’s Disease: Mechanisms of Pathogenesis and Therapeutic Strategies
Jimenez-Sanchez, M., Licitra, F., Underwood, B. R., & Rubinsztein, D. C. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024240 · Cited by 507
HATs and HDACs in neurodegeneration: a tale of disconcerted acetylation homeostasis
Saha, R. N., & Pahan, K. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401769 · Cited by 441
Genome-wide expression profiling of human blood reveals biomarkers for Huntington's disease
Borovecki, F., Lovrecic, L., Zhou, J., Jeong, H., Then, F., Rosas, H. D., Hersch, S. M., Hogarth, P., Bouzou, B., Jensen, R. V., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504921102 · Cited by 414
Metadata
- Authors
- McCampbell, A., Taye, A. A., Whitty, L., Penney, E., Steffan, J. S., & Fischbeck, K. H.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2001-12-11
- Volume
- 98
- Issue
- 26
- Pages
- 15179-15184
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2122631256
- Cited by
- 239
- References
- 6
- FWCI
- 8.12
- Type
- journal article
- Language
- en
- Open access
- green
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- McCampbell, A., Taye, A. A., Whitty, L., Penney, E., Steffan, J. S., & Fischbeck, K. H. (2001). Histone deacetylase inhibitors reduce polyglutamine toxicity. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.261400698
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
