The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity
Open accessAbstract
Significance: Parkinson’s disease is characterized by the presence in brain tissues of aberrant aggregates primarily formed by the protein α-synuclein. It has been difficult, however, to identify compounds capable of preventing the formation of such deposits because of the complexity of the aggregation process of α-synuclein. By exploiting recently developed highly quantitative in vitro assays, we identify a compound, squalamine, that blocks α-synuclein aggregation, and characterize its mode of action. Our results show that squalamine, by competing with α-synuclein for binding lipid membranes, specifically inhibits the initiation of the aggregation process of α-synuclein and abolishes the toxicity of α-synuclein oligomers in neuronal cells and in an animal model of Parkinson’s disease.
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Cites
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Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382
Self-citationMolecular anatomy of a trafficking organelle
Takamori, S., Holt, M., Stenius, K., Lemke, E. A., Grønborg, M., Riedel, D., Urlaub, H., Schenck, S., Brügger, B., Ringler, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.10.030 · Cited by 2,373
Unfolding the role of protein misfolding in neurodegenerative diseases
Soto, C. (2003) · Nature Reviews Neuroscience · doi:10.1038/nrn1007 · Cited by 1,506
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
Galvagnion, C., Buell, A. K., Meisl, G., Michaels, T. C. T., Vendruscolo, M., Knowles, T. P. J., & Dobson, C. M. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1750 · Cited by 661
Self-citationTARP Phosphorylation Regulates Synaptic AMPA Receptors through Lipid Bilayers
Sumioka, A., Yan, D., & Tomita, S. (2010) · Neuron · doi:10.1016/j.neuron.2010.04.035 · Cited by 167
Tóth, G., Gardai, S. J., Zago, W., Bertoncini, C. W., Cremades, N., Roy, S. L., Tambe, M. A., Rochet, J.-C., Galvagnion, C., Skibinski, G., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087133 · Cited by 151
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Cited by
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
Carroll, A. R., Copp, B. R., Davis, R. A., Keyzers, R. A., & Prinsep, M. R. (2019) · Natural Product Reports · doi:10.1039/c8np00092a · Cited by 518
The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson’s Disease
Galvagnion, C. (2017) · Journal of Parkinson's Disease · doi:10.3233/jpd-171103 · Cited by 258
Self-citationThe Role of α-Synuclein Oligomers in Parkinson’s Disease
Du, X.-Y., Xie, X.-X., & Liu, R.-T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228645 · Cited by 234
Parkinson disease and the gut: new insights into pathogenesis and clinical relevance
Travagli, R. A., Browning, K. N., & Camilleri, M. (2020) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-020-0339-z · Cited by 181
Metadata
- Authors
- Perni, M., Galvagnion, C., Maltsev, A., Meisl, G., Müller, M. B. D., Challa, P. K., Kirkegaard, J. B., Flagmeier, P., Cohen, S. I. A., Cascella, R., Chen, S. W., Limbocker, R., Sormanni, P., Heller, G. T., Aprile, F. A., Cremades, N., Cecchi, C., Chiti, F., Nollen, E. A. A., Knowles, T. P. J., Vendruscolo, M., Bax, A., Zasloff, M., & Dobson, C. M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2017-01-17
- Volume
- 114
- Issue
- 6
- Pages
- E1009-E1017
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2571594992
- Cited by
- 298
- References
- 6
- FWCI
- 20.34
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- The paper
- Perni, M., Galvagnion, C., Maltsev, A., Meisl, G., Müller, M. B. D., Challa, P. K., Kirkegaard, J. B., Flagmeier, P., Cohen, S. I. A., Cascella, R., Chen, S. W., Limbocker, R., Sormanni, P., Heller, G. T., Aprile, F. A., Cremades, N., Cecchi, C., Chiti, F., Nollen, E. A. A., . . . Dobson, C. M. (2017). A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1610586114
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
