The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Nitration inhibits fibrillation of human α‐synuclein in vitro by formation of soluble oligomers
Open accessAbstract
The aggregation of α‐synuclein in dopaminergic neurons is a critical factor in the etiology of Parkinson's disease (PD). Oxidative and nitrative stress is also implicated in PD. We examined the effect of nitration on the propensity of α‐synuclein to fibrillate in vitro. Fibril formation of α‐synuclein was completely inhibited by nitration, due to the formation of stable soluble oligomers (apparently octamers). More importantly the presence of sub‐stoichiometric concentrations of nitrated α‐synuclein led to inhibition of fibrillation of non‐modified α‐synuclein. These observations suggest that nitration of soluble α‐synuclein may be a protective factor in PD, rather than a causative one.
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AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
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Intrinsic Disorder and Protein Function
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Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation
Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010907200 · Cited by 1,096
Self-citationThe protein trinity—linking function and disorder
Dunker, A. K., & Obradovic, Z. (2001) · Nature Biotechnology · doi:10.1038/nbt0901-805 · Cited by 581
The importance of being unfolded
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Cited by
Conformational constraints for amyloid fibrillation: the importance of being unfolded
Uversky, V. N., & Fink, A. L. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.12.008 · Cited by 1,015
Self-citationα-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
Self-citationCell Biology and Pathophysiology of α-Synuclein
Burré, J., Sharma, M., & Südhof, T. C. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024091 · Cited by 579
The Synaptic Function of α-Synuclein
Burré, J. (2015) · Journal of Parkinson's Disease · doi:10.3233/jpd-150642 · Cited by 573
Neuropathology, biochemistry, and biophysics of α‐synuclein aggregation
Uversky, V. N. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04764.x · Cited by 567
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Metadata
- Authors
- Yamin, G., Uversky, V. N., & Fink, A. L.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2003-04-15
- Volume
- 542
- Issue
- 1-3
- Pages
- 147-152
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2079003999
- Cited by
- 167
- References
- 7
- FWCI
- 6.01
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Yamin, G., Uversky, V. N., & Fink, A. L. (2003). Nitration inhibits fibrillation of human α‐synuclein in vitro by formation of soluble oligomers. FEBS Letters. https://doi.org/10.1016/s0014-5793(03)00367-3
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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