The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
The Aggregation and Fibrillation of α-Synuclein
Abstract
alpha-Synuclein is a small (14 kDa), abundant, intrinsically disordered presynaptic protein, whose aggregation is believed to be a critical step in Parkinson's disease (PD). The kinetics of alpha-synuclein fibrillation are consistent with a nucleation-dependent mechanism, in which the critical early stage of the structural transformation involves a partially folded intermediate. Although the basis for the toxic effects of aggregated alpha-synuclein are unknown, it has been proposed that transient oligomers are responsible, possibly by forming pores in membranes. In this Account, I discuss our investigations into the molecular basis for alpha-synuclein aggregation/fibrillation, including factors that either accelerate or inhibit fibrillation, effects of molecular crowding, oxidation, point mutations, and lipid membranes, as well as the variety of conformational and oligomeric states that alpha-synuclein can adopt. It is apparent that neuronal cells must have a very fine balance of factors that control the levels and potential aggregation of alpha-synuclein.
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Cites
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240
AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
Krüger, R., Kuhn, W., Müller, T., Woitalla, D., Graeber, M., Kösel, S., Przuntek, H., Epplen, J. T., Schols, L., & Riess, O. (1998) · Nature Genetics · doi:10.1038/ng0298-106 · Cited by 3,836
Minton, A. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r100005200 · Cited by 1,474
β-Synuclein Inhibits α-Synuclein Aggregation
Hashimoto, M., Rockenstein, E., Mante, M., Mallory, M., & Masliah, E. (2001) · Neuron · doi:10.1016/s0896-6273(01)00462-7 · Cited by 398
Brain iron pathways and their relevance to Parkinson's disease
Berg, D., Gerlach, M., Youdim, M. B. H., Double, K. L., Zecca, L., Riederer, P., & Becker, G. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00608.x · Cited by 362
Norris, E. H., Giasson, B. I., Hodara, R., Xu, S., Trojanowski, J. Q., Ischiropoulos, H., & Lee, V. M.-Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412621200 · Cited by 273
Trimethylamine‐ N ‐oxide‐induced folding of α‐synuclein
Uversky, V. N., Li, J., & Fink, A. L. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03121-0 · Cited by 208
Cited by
Calderón-Garcidueñas, L., Solt, A. C., Henríquez-Roldán, C., Torres-Jardón, R., Nuse, B., Herritt, L., Villarreal-Calderón, R., Osnaya, N., Stone, I., García, R., et al. (2008) · Toxicologic Pathology · doi:10.1177/0192623307313011 · Cited by 937
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
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
Effects of Molecular Crowding on the Structures, Interactions, and Functions of Nucleic Acids
Nakano, S.-I., Miyoshi, D., & Sugimoto, N. (2014) · Chemical Reviews · doi:10.1021/cr400113m · Cited by 567
Dementia with Lewy bodies: an update and outlook
Outeiro, T. F., Koss, D. J., Erskine, D., Walker, L., Kurzawa-Akanbi, M., Burn, D., Donaghy, P., Morris, C., Taylor, J.-P., Thomas, A., et al. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0306-8 · Cited by 381
Metadata
- Authors
- Fink, A. L.
- Venue
- Accounts of Chemical Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2006-09-01
- Volume
- 39
- Issue
- 9
- Pages
- 628-634
- ISSN
- 0001-4842 (ISSN-L)
- 1520-4898
- OpenAlex
- W2158977717
- Cited by
- 501
- References
- 7
- FWCI
- 15.06
- Type
- journal article
- Language
- en
- Open access
- closed
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