The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Properties of native brain α-synuclein
Open accessAbstract
Arising from T. Bartels, J. G. Choi & D. J. Selkoe. 477, 107–110 (2011).10.1038/nature10324α-Synuclein is an abundant presynaptic protein that binds to negatively charged phospholipids, functions as a SNARE-complex chaperone and contributes to Parkinson’s disease pathogenesis. Recombinant α-synuclein in solution is largely unfolded and devoid of tertiary structure, but Bartels et al. have proposed that native α-synuclein purified from human erythrocytes forms a stably folded, soluble tetramer that resists aggregation. By contrast, we show here that native α-synuclein purified from mouse brain consists of a largely unstructured monomer, exhibits no stable tetramer formation, and is prone to aggregation. The native state of α-synuclein is important for understanding its pathological effects as a stably folded protein would be much less prone to aggregation than a conformationally labile protein. There is a Reply to this Brief Communication Arising by Bartels, T. & Selkoe, D. J. Nature 498, http://dx.doi.org/10.1038/nature12126 (2013).
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Cites
α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
Bartels, T., Choi, J. G., & Selkoe, D. J. (2011) · Nature · doi:10.1038/nature10324 · Cited by 1,263
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Bendor, J. T., Logan, T. P., & Edwards, R. H. (2013) · Neuron · doi:10.1016/j.neuron.2013.09.004 · Cited by 825
Structural disorder of monomeric α-synuclein persists in mammalian cells
Theillet, F.-X., Binolfi, A., Bekei, B., Martorana, A., Rose, H. M., Stuiver, M., Verzini, S., Lorenz, D., van Rossum, M., Goldfarb, D., et al. (2016) · Nature · doi:10.1038/nature16531 · Cited by 868
α‐Synuclein aggregation nucleates through liquid‐liquid phase separation
Ray, S., Singh, N., Kumar, R., Patel, K., Pandey, S., Datta, D., Mahato, J., Panigrahi, R., Navalkar, A., Mehra, S., et al. (2020) · Nature Chemistry · doi:10.1038/s41557-020-0465-9 · Cited by 863
Role 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
- Burré, J., Vivona, S., Diao, J., Sharma, M., Brunger, A. T., & Südhof, T. C.
- Venue
- Nature
- Published
- 2013-06-12
- Volume
- 498
- Issue
- 7453
- Pages
- E4-E6
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2076042026
- Cited by
- 339
- References
- 1
- FWCI
- 14.82
- Type
- journal article
- Language
- en
- Open access
- green
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- Burré, J., Vivona, S., Diao, J., Sharma, M., Brunger, A. T., & Südhof, T. C. (2013). Properties of native brain α-synuclein. Nature. https://doi.org/10.1038/nature12125
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