The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
Structural characterization of copper(II) binding to α-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease
Open accessAbstract
The aggregation of α-synuclein (AS) is characteristic of Parkinson's disease and other neurodegenerative synucleinopathies. We demonstrate here that Cu(II) ions are effective in accelerating AS aggregation at physiologically relevant concentrations without altering the resultant fibrillar structures. By using numerous spectroscopic techniques (absorption, CD, EPR, and NMR), we have located the primary binding for Cu(II) to a specific site in the N terminus, involving His-50 as the anchoring residue and other nitrogen/oxygen donor atoms in a square planar or distorted tetragonal geometry. The carboxylate-rich C terminus, originally thought to drive copper binding, is able to coordinate a second Cu(II) equivalent, albeit with a 300-fold reduced affinity. The NMR analysis of AS–Cu(II) complexes reveals the existence of conformational restrictions in the native state of the protein. The metallobiology of Cu(II) in Parkinson's disease is discussed by a comparative analysis with other Cu(II)-binding proteins involved in neurodegenerative disorders.
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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
Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 678
α-Synuclein misfolding and Parkinson's disease
Breydo, L., Wu, J. W., & Uversky, V. N. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.002 · Cited by 657
Metadata
- Authors
- Rasia, R. M., Bertoncini, C. W., Marsh, D., Hoyer, W., Cherny, D., Zweckstetter, M., Griesinger, C., Jovin, T. M., & Fernández, C. O.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-03-14
- Volume
- 102
- Issue
- 12
- Pages
- 4294-4299
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2148225540
- Cited by
- 408
- References
- 54
- FWCI
- 12.10
- Type
- journal article
- Language
- en
- Open access
- green
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- Rasia, R. M., Bertoncini, C. W., Marsh, D., Hoyer, W., Cherny, D., Zweckstetter, M., Griesinger, C., Jovin, T. M., & Fernández, C. O. (2005). Structural characterization of copper(II) binding to α-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0407881102
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