The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Pathogenesis of polyglutamine disorders: aggregation revisited
Open accessAbstract
Expansion of CAG trinucleotide repeats coding for polyglutamine in unrelated proteins causes at least nine late-onset progressive neurodegenerative disorders, including Huntington's disease and a number of spinocerebellar ataxias. Expanded polyglutamine provokes a dominant gain-of-function neurotoxicity, regardless of the specific protein context within which it resides. Nevertheless, the protein context does modulate polyglutamine toxicity, as evidenced by the distinct clinical and pathological features of the various disorders. Importantly, polyglutamine toxicity might derive from its ability to aggregate. Indeed, aggregation probably underlies some defining attributes of the polyglutamine disorders, such as their late onset, progressive nature, and the dependence of onset age on polyglutamine length. However, the central role of aggregation in polyglutamine pathogenesis has been challenged by several studies, which instead argued that the soluble form of the disease proteins is responsible for neuronal damage. Thus, the question whether polyglutamine aggregates are deleterious, harmless or protective remains the most passionately disputed issue in the study of these diseases. In this review, we attempt to reconcile some of these controversies.
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Cites
Aggresomes: A Cellular Response to Misfolded Proteins
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“The aggregates consist of b-sheet-rich fibrils aligned side-by-side to form ribbon-like structures, and exhibit several defining features of amyloid, such as binding of thioflavine T, congo red birefringence, and reactivity with a generic anti-amyloid antibody (11,14).”
BackgroundInfluentialHistone 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
Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines
Panov, A. V., Gutekunst, C.-A., Leavitt, B. R., Hayden, M. R., Burke, J. R., Strittmatter, W. J., & Greenamyre, J. T. (2002) · Nature Neuroscience · doi:10.1038/nn884 · Cited by 1,030
Disruption of CREB function in brain leads to neurodegeneration
Mantamadiotis, T., Lemberger, T., Bleckmann, S. C., Kern, H., Kretz, O., Villalba, A. M., Tronche, F., Kellendonk, C., Gau, D., Kapfhammer, J., et al. (2002) · Nature Genetics · doi:10.1038/ng882 · Cited by 684
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Cause of neural death in neurodegenerative diseases attributable to expansion of glutamine repeats
Perutz, M. F., & Windle, A. H. (2001) · Nature · doi:10.1038/35084141 · Cited by 199
Cited by
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
Mutant huntingtin impairs axonal trafficking in mammalian neurons in vivo and in vitro
Trushina, E., Dyer, R. B., Badger, J. D., Ure, D., Eide, L., Tran, D. D., Vrieze, B. T., Legendre-Guillemin, V., McPherson, P. S., Mandavilli, B. S., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.18.8195-8209.2004 · Cited by 520
Kell, D. B. (2010) · Archives of Toxicology · doi:10.1007/s00204-010-0577-x · Cited by 361
Role of mTOR in physiology and pathology of the nervous system
Swiech, L., Perycz, M., Malik, A., & Jaworski, J. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.08.015 · Cited by 338
HD CAG repeat implicates a dominant property of huntingtin in mitochondrial energy metabolism
Seong, I. S., Ivanova, E., Lee, J.-M., Choo, Y. S., Fossale, E., Anderson, M., Gusella, J. F., Laramie, J. M., Myers, R. H., Lesort, M., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi319 · Cited by 294
Metadata
- Authors
- Michalik, A., & Van Broeckhoven, C.
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2003-09-22
- Volume
- 12
- Issue
- suppl 2
- Pages
- R173-R186
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- OpenAlex
- W2106490406
- Cited by
- 232
- References
- 7
- FWCI
- 9.00
- Type
- journal article
- Language
- en
- Open access
- bronze
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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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