The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Inhibition and disaggregation of α-synuclein oligomers by natural polyphenolic compounds
Abstract
Aggregation of alpha-synuclein (αS) into oligomers is critically involved in the pathogenesis of Parkinson's disease (PD). Using confocal single-molecule fluorescence spectroscopy, we have studied the effects of 14 naturally-occurring polyphenolic compounds and black tea extract on αS oligomer formation. We found that a selected group of polyphenols exhibited potent dose-dependent inhibitory activity on αS aggregation. Moreover, they were also capable of robustly disaggregating pre-formed αS oligomers. Based upon structure-activity analysis, we propose that the key molecular scaffold most effective in inhibiting and destabilizing self-assembly by αS requires: (i) aromatic elements for binding to the αS monomer/oligomer and (ii) vicinal hydroxyl groups present on a single phenyl ring. These findings may guide the design of novel therapeutic drugs in PD.
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α-Synuclein is phosphorylated in synucleinopathy lesions
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Kinetic Stabilization of the α-Synuclein Protofibril by a Dopamine-α-Synuclein Adduct
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Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development
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Myricetin: A Dietary Molecule with Diverse Biological Activities
Semwal, D., Semwal, R., Combrinck, S., & Viljoen, A. (2016) · Nutrients · doi:10.3390/nu8020090 · Cited by 707
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Mehra, S., Sahay, S., & Maji, S. K. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.03.001 · Cited by 499
Pharmacological effects and mechanisms of tannic acid
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α‐Synuclein oligomers and clinical implications for Parkinson disease
Kalia, L. V., Kalia, S. K., McLean, P. J., Lozano, A. M., & Lang, A. E. (2013) · Annals of Neurology · doi:10.1002/ana.23746 · Cited by 292
Metadata
- Authors
- Caruana, M., Högen, T., Levin, J., Hillmer, A., Giese, A., & Vassallo, N.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2011-03-26
- Volume
- 585
- Issue
- 8
- Pages
- 1113-1120
- ISSN
- 0014-5793 (ISSN-L)
- OpenAlex
- W2038828761
- Cited by
- 273
- References
- 41
- FWCI
- 7.68
- Type
- journal article
- Language
- en
- Open access
- closed
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