The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Mitochondrial alpha-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo
Open accessAbstract
Alpha-synuclein is the major protein component of Lewy bodies, a cardinal pathological feature of the degenerating Parkinsonian brain. Alpha-synuclein has been reported to be able to intercalate into membranes via formation of an alpha-helical structure at its N-terminal end. Recent in vitro studies from various laboratories have demonstrated that alpha-synuclein can physically associate with mitochondria and interfere with mitochondrial function. α-Syn predominantly associates with the inner mitochondrial membrane, where it can apparently interact with complex I resulting in reduced mitochondrial complex I activity and increased free radical production. However, the effect of in vivo alpha-synuclein accumulation within dopaminergic neurons on mitochondrial function has not been thoroughly studied. Examination of transgenic animals which overexpress the familial mutant A53T form of the protein selectively within dopaminergic neurons reveals that A53T localizes to the mitochondrial membranes as monomers and oligomers particularly under conditions of proteasomal inhibitory stress, and that this localization coincides with a selective age-related mitochondrial complex I inhibition and decreased substrate-specific respiration along with increases in mitochondrial autophagy (mitophagy).
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Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
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AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
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“α-Syn has been reported to undergo degradation by the proteasome and by alternative pathways such as autophagy [7].”
Selective degradation of mitochondria by mitophagy
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Expanding insights of mitochondrial dysfunction in Parkinson's disease
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Cited by
The Role of Oxidative Stress in Parkinson's Disease
Dias, V., Junn, E., & Mouradian, M. M. (2013) · Journal of Parkinson’s Disease · doi:10.3233/jpd-130230 · Cited by 1,845
Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling.
Lee, J., Giordano, S., & Zhang, J. (2012) · Biochemical Journal · doi:10.1042/bj20111451 · Cited by 1,438
Mitochondria, oxidative stress and neurodegeneration
Federico, A., Cardaioli, E., Da Pozzo, P., Formichi, P., Gallus, G. N., & Radi, E. (2012) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2012.05.030 · Cited by 787
Mitochondrial Defects and Oxidative Stress in Alzheimer Disease and Parkinson Disease
Yan, M. H., Wang, X., & Zhu, X. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.11.014 · Cited by 718
Buendia, I., Michalska, P., Navarro, E., Gameiro, I., Egea, J., & León, R. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.11.003 · Cited by 678
Metadata
- Authors
- Chinta, S. J., Mallajosyula, J. K., Rane, A., & Andersen, J. K.
- Venue
- Neuroscience Letters
- Publisher
- Elsevier BV
- Published
- 2010-12
- Volume
- 486
- Issue
- 3
- Pages
- 235-239
- ISSN
- 0304-3940 (ISSN-L)
- OpenAlex
- W2055029031
- Cited by
- 449
- References
- 7
- FWCI
- 11.46
- Type
- journal article
- Language
- en
- Open access
- green
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- Chinta, S. J., Mallajosyula, J. K., Rane, A., & Andersen, J. K. (2010). Mitochondrial alpha-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo. Neuroscience Letters. https://doi.org/10.1016/j.neulet.2010.09.061
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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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