The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Aggregation promoting C-terminal truncation of α-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations
Open accessAbstract
Abnormal biology of α-synuclein (α-Syn) is directly implicated in the pathogenesis of Parkinson's disease and other α-synucleinopathies. Herein, we demonstrate that C-terminally truncated α-Syn (α-SynΔC), enriched in the pathological α-Syn aggregates, is normally generated from full-length α-Syn independent of α-Syn aggregation in brains and in cultured cells. The accumulation of α-SynΔC is enhanced in neuronal cells as compared with nonneuronal cells. Significantly, the expression of familial Parkinson's disease-linked mutant α-Syn is associated with the enhanced cellular accumulation of α-SynΔC. Moreover, substoichiometric amounts of α-SynΔC enhance the in vitro aggregation of the more abundant full-length α-Syn. Finally, cases of α-synucleinopathy exhibit increases in the total soluble α-Syn and a higher proportion of soluble α-SynΔC, a condition favoring the aggregation of α-Syn. Collectively, our results indicate that the biology behind the generation and accumulation of α-SynΔC is likely to have relevance for the initiation and the progression of α-Syn aggregation in vivo.
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Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
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Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
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AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
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Cited by
Volpicelli-Daley, L. A., Luk, K. C., Patel, T. P., Tanik, S. A., Riddle, D. M., Stieber, A., Meaney, D. F., Trojanowski, J. Q., & Lee, V. M.-Y. (2011) · Neuron · doi:10.1016/j.neuron.2011.08.033 · Cited by 1,569
-Synuclein in Parkinson's Disease
Stefanis, L. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009399 · Cited by 1,446
Luk, K. C., Song, C., O'Brien, P., Stieber, A., Branch, J. R., Brunden, K. R., Trojanowski, J. Q., & Lee, V. M.-Y. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908005106 · Cited by 938
Bendor, J. T., Logan, T. P., & Edwards, R. H. (2013) · Neuron · doi:10.1016/j.neuron.2013.09.004 · Cited by 825
T cells from patients with Parkinson’s disease recognize α-synuclein peptides
Sulzer, D., Alcalay, R. N., Garretti, F., Cote, L., Kanter, E., Agin-Liebes, J., Liong, C., McMurtrey, C., Hildebrand, W. H., Mao, X., et al. (2017) · Nature · doi:10.1038/nature22815 · Cited by 866
Self-citation
Metadata
- Authors
- Li, W., West, N., Colla, E., Pletnikova, O., Troncoso, J. C., Marsh, L., Dawson, T. M., Jäkälä, P., Hartmann, T., Price, D. L., & Lee, M. K.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-01-31
- Volume
- 102
- Issue
- 6
- Pages
- 2162-2167
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2011332000
- Cited by
- 472
- References
- 8
- FWCI
- 12.91
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Li, W., West, N., Colla, E., Pletnikova, O., Troncoso, J. C., Marsh, L., Dawson, T. M., Jäkälä, P., Hartmann, T., Price, D. L., & Lee, M. K. (2005). Aggregation promoting C-terminal truncation of α-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0406976102
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