The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Green tea (−)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington's disease models
Open accessAbstract
Huntington's disease (HD) is a progressive neurodegenerative disorder for which only symptomatic treatments of limited effectiveness are available. Preventing early misfolding steps and thereby aggregation of the polyglutamine (polyQ)-containing protein huntingtin (htt) in neurons of patients may represent an attractive therapeutic strategy to postpone the onset and progression of HD. Here, we demonstrate that the green tea polyphenol (-)-epigallocatechin-3-gallate (EGCG) potently inhibits the aggregation of mutant htt exon 1 protein in a dose-dependent manner. Dot-blot assays and atomic force microscopy studies revealed that EGCG modulates misfolding and oligomerization of mutant htt exon 1 protein in vitro, indicating that it interferes with very early events in the aggregation process. Also, EGCG significantly reduced polyQ-mediated htt protein aggregation and cytotoxicity in an yeast model of HD. When EGCG was fed to transgenic HD flies overexpressing a pathogenic htt exon 1 protein, photoreceptor degeneration and motor function improved. These results indicate that modulators of htt exon 1 misfolding and oligomerization like EGCG are likely to reduce polyQ-mediated toxicity in vivo. Our studies may provide the basis for the development of a novel pharmacotherapy for HD and related polyQ disorders.
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Cites
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Aggregation of Huntingtin in Neuronal Intranuclear Inclusions and Dystrophic Neurites in Brain
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Neuropathological Classification of Huntingtonʼs Disease
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Self-citationReversal of Neuropathology and Motor Dysfunction in a Conditional Model of Huntington's Disease
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Self-citationNormal huntingtin function: an alternative approach to Huntington's disease
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Intake of flavonoids and risk of dementia
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The hunt for huntingtin function: interaction partners tell many different stories
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Self-citationRubinsztein, D. C., Leggo, J., Coles, R., Almqvist, E., Biancalana, V., Cassiman, J. J., Chotai, K. A., Connarty, M., Crauford, D., Curtis, A., et al. (1996) · PubMed Central · Cited by 525
Cited by
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers
Ehrnhoefer, D. E., Bieschke, J., Boeddrich, A., Herbst, M., Masino, L., Lurz, R., Engemann, S., Pastore, A., & Wanker, E. E. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1437 · Cited by 1,434
Self-citationEGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity
Bieschke, J., Russ, J., Friedrich, R. P., Ehrnhoefer, D. E., Wobst, H., Neugebauer, K., & Wanker, E. E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910723107 · Cited by 1,011
Self-citationAn integrative approach to ortholog prediction for disease-focused and other functional studies
Hu, Y., Flockhart, I., Vinayagam, A., Bergwitz, C., Berger, B., Perrimon, N., & Mohr, S. E. (2011) · BMC Bioinformatics · doi:10.1186/1471-2105-12-357 · Cited by 848
Molecular Mechanisms and Potential Therapeutical Targets in Huntington's Disease
Zuccato, C., Valenza, M., & Cattaneo, E. (2010) · Physiological Reviews · doi:10.1152/physrev.00041.2009 · Cited by 848
Manoharan, S., Guillemin, G. J., Abiramasundari, R. S., Essa, M. M., Akbar, M., & Akbar, M. D. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/8590578 · Cited by 523
Metadata
- Authors
- Ehrnhoefer, D. E., Duennwald, M., Markovic, P., Wacker, J. L., Engemann, S., Roark, M., Legleiter, J., Marsh, J. L., Thompson, L. M., Lindquist, S., Muchowski, P. J., & Wanker, E. E.
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2006-08-07
- Volume
- 15
- Issue
- 18
- Pages
- 2743-2751
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- OpenAlex
- W2147297400
- Cited by
- 414
- References
- 32
- FWCI
- 4.63
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Green tea (−)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington's disease models. https://app.cochat.ai/papers/10.1093/hmg/ddl210
- The paper
- Ehrnhoefer, D. E., Duennwald, M., Markovic, P., Wacker, J. L., Engemann, S., Roark, M., Legleiter, J., Marsh, J. L., Thompson, L. M., Lindquist, S., Muchowski, P. J., & Wanker, E. E. (2006). Green tea (−)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington's disease models. Human Molecular Genetics. https://doi.org/10.1093/hmg/ddl210
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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.
