The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
A bivalent Huntingtin binding peptide suppresses polyglutamine aggregation and pathogenesis in Drosophila
Open accessAbstract
Huntington disease is caused by the expansion of a polyglutamine repeat in the Huntingtin protein (Htt) that leads to degeneration of neurons in the central nervous system and the appearance of visible aggregates within neurons. We have developed and tested suppressor polypeptides that bind mutant Htt and interfere with the process of aggregation in cell culture. In a Drosophila model, the most potent suppressor inhibits both adult lethality and photoreceptor neuron degeneration. The appearance of aggregates in photoreceptor neurons correlates strongly with the occurrence of pathology, and expression of suppressor polypeptides delays and limits the appearance of aggregates and protects photoreceptor neurons. These results suggest that targeting the protein interactions leading to aggregate formation may be beneficial for the design and development of therapeutic agents for Huntington disease.
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Cites
MACDONALD, M. (1993) · Cell · doi:10.1016/0092-8674(93)90585-e · Cited by 8,366
Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
Steffan, J. S., Bodai, L., Pallos, J., Poelman, M., McCampbell, A., Apostol, B. L., Kazantsev, A., Schmidt, E., Zhu, Y.-Z., Greenwald, M., et al. (2001) · Nature · doi:10.1038/35099568 · Cited by 1,228
Self-citationNeuroprotective Effects of Creatine in a Transgenic Mouse Model of Huntington's Disease
Ferrante, R. J., Andreassen, O. A., Jenkins, B. G., Dedeoglu, A., Kuemmerle, S., Kubilus, J. K., Kaddurah-Daouk, R., Hersch, S. M., & Beal, M. F. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-12-04389.2000 · Cited by 522
Boutell, J. M., Thomas, P., Neal, J. W., Weston, V. J., Duce, J., Harper, P. S., & Lesley Jones, A. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.9.1647 · Cited by 310
Cited by
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
Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease
Tanaka, M., Machida, Y., Niu, S., Ikeda, T., Jana, N. R., Doi, H., Kurosawa, M., Nekooki, M., & Nukina, N. (2004) · Nature Medicine · doi:10.1038/nm985 · Cited by 782
Rapamycin alleviates toxicity of different aggregate-prone proteins
Berger, Z., Ravikumar, B., Menzies, F. M., Oroz, L. G., Underwood, B. R., Pangalos, M. N., Schmitt, I., Wullner, U., Evert, B. O., O'Kane, C. J., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddi458 · Cited by 657
Ehrnhoefer, D. E., Duennwald, M., Markovic, P., Wacker, J. L., Engemann, S., Roark, M., Legleiter, J., Marsh, J. L., Thompson, L. M., Lindquist, S., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl210 · Cited by 414
Self-citationChoosing an animal model for the study of Huntington's disease
Pouladi, M. A., Morton, A. J., & Hayden, M. R. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3570 · Cited by 356
Metadata
- Authors
- Kazantsev, A., Walker, H. A., Slepko, N., Bear, J. E., Preisinger, E., Steffan, J. S., Zhu, Y.-Z., Gertler, F. B., Housman, D. E., Marsh, J. L., & Thompson, L. M.
- Venue
- Nature Genetics
- Published
- 2002-03-25
- Volume
- 30
- Issue
- 4
- Pages
- 367-376
- ISSN
- 1061-4036 (ISSN-L)
- 1546-1718
- OpenAlex
- W2065310164
- Cited by
- 172
- References
- 4
- FWCI
- 8.39
- Type
- journal article
- Language
- en
- Open access
- green
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- Kazantsev, A., Walker, H. A., Slepko, N., Bear, J. E., Preisinger, E., Steffan, J. S., Zhu, Y.-Z., Gertler, F. B., Housman, D. E., Marsh, J. L., & Thompson, L. M. (2002). A bivalent Huntingtin binding peptide suppresses polyglutamine aggregation and pathogenesis in Drosophila. Nature Genetics. https://doi.org/10.1038/ng864
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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.