The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Optical Reporters for the Conformation of α-Synuclein Reveal a Specific Interaction with Mitochondria
Open accessAbstract
The aggregation of abnormally folded proteins is a defining feature of neurodegenerative disease, but it has not previously been possible to assess the conformation of these proteins in a physiologically relevant context, before they form morphologically recognizable aggregates. We now describe FRET-based reporters for the conformation of α-synuclein, a protein central to the pathogenesis of Parkinson's disease (PD). Characterization in vitro shows that α-synuclein adopts a relatively “closed” conformation in solution that converts to “open” on membrane binding. In living cells, the closed conformation predominates. In neurons, however, cell bodies contain a much larger proportion of the open conformation than synaptic boutons. To account for these differences, we also used the reporters to characterize the interaction with native membranes. We find that the conformation of α-synuclein responds selectively to mitochondria, indicating a direct link between α-synuclein and an organelle strongly implicated in the pathogenesis of PD.
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1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769 · cited 1×
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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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Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1
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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
-Synuclein in Parkinson's Disease
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Mitochondrial dysfunction and oxidative stress in Parkinson's disease
Subramaniam, S. R., & Chesselet, M.-F. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.04.004 · Cited by 913
Bendor, J. T., Logan, T. P., & Edwards, R. H. (2013) · Neuron · doi:10.1016/j.neuron.2013.09.004 · Cited by 825
Self-citationRole of mitochondrial ROS in the brain: from physiology to neurodegeneration
Angelova, P. R., & Abramov, A. Y. (2018) · FEBS Letters · doi:10.1002/1873-3468.12964 · Cited by 789
Metadata
- Authors
- Nakamura, K., Nemani, V. M., Wallender, E. K., Kaehlcke, K., Ott, M., & Edwards, R. H.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2008-11-19
- Volume
- 28
- Issue
- 47
- Pages
- 12305-12317
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- OpenAlex
- W2030715196
- Cited by
- 210
- References
- 15
- FWCI
- 6.09
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Nakamura, K., Nemani, V. M., Wallender, E. K., Kaehlcke, K., Ott, M., & Edwards, R. H. (2008). Optical Reporters for the Conformation of α-Synuclein Reveal a Specific Interaction with Mitochondria. The Journal of Neuroscience. https://doi.org/10.1523/jneurosci.3088-08.2008
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