The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation
Open accessAbstract
Significance: The deposition of α-synuclein as insoluble amyloid fibrils and the spreading of such species in the brain are two hallmarks of Parkinson disease. It is therefore of great importance to understand in detail the process of aggregation of this protein. We show by a series of in vitro measurements that amyloid fibrils of α-synuclein can grow under a wide range of solution conditions but that they can multiply rapidly only under a much more select set of solution conditions, mimicking those in endosomes and other organelles. The quantitative characterization of α-synuclein aggregation described here provides new insights into the microscopic mechanisms underlying α-synuclein aggregation in the context of Parkinson disease.
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Cites
Lewy body–like pathology in long-term embryonic nigral transplants in Parkinson's disease
Kordower, J. H., Chu, Y., Hauser, R. A., Freeman, T. B., & Olanow, C. W. (2008) · Nature Medicine · doi:10.1038/nm1747 · Cited by 1,722
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
Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide
Hu, X., Crick, S. L., Bu, G., Frieden, C., Pappu, R. V., & Lee, J.-M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911281106 · Cited by 426 · cited 1×
“It has been shown that the specific chemical microenvironments of cellular compartments, such as endosomes, can enhance protein aggregation by several orders of magnitude (41).”
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Cited by
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629
Self-citationα-Synuclein strains cause distinct synucleinopathies after local and systemic administration
Peelaerts, W., Bousset, L., Van der Perren, A., Moskalyuk, A., Pulizzi, R., Giugliano, M., Van den Haute, C., Melki, R., & Baekelandt, V. (2015) · Nature · doi:10.1038/nature14547 · Cited by 1,130
α-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies
Wong, Y. C., & Krainc, D. (2017) · Nature Medicine · doi:10.1038/nm.4269 · Cited by 897
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
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
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Metadata
- Authors
- Buell, A. K., Galvagnion, C., Gaspar, R., Sparr, E., Vendruscolo, M., Knowles, T. P. J., Linse, S., & Dobson, C. M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2014-05-09
- Volume
- 111
- Issue
- 21
- Pages
- 7671-7676
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2050375429
- Cited by
- 664
- References
- 3
- FWCI
- 23.28
- Type
- journal article
- Language
- en
- Open access
- bronze
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