The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Structural Organization of α-Synuclein Fibrils Studied by Site-directed Spin Labeling
Open accessAbstract
Despite its importance in Parkinson's disease, a detailed understanding of the structure and mechanism of alpha-synuclein fibril formation remains elusive. In this study, we used site-directed spin labeling and electron paramagnetic resonance spectroscopy to study the structural features of monomeric and fibrillar alpha-synuclein. Our results indicate that monomeric alpha-synuclein, in solution, has a highly dynamic structure, in agreement with the notion that alpha-synuclein is a natively unfolded protein. In contrast, fibrillar aggregates of alpha-synuclein exhibit a distinct domain organization. Our data identify a highly ordered and specifically folded central core region of approximately 70 amino acids, whereas the N terminus is structurally more heterogeneous and the C terminus ( approximately 40 amino acids) is completely unfolded. Interestingly, the central core region of alpha-synuclein exhibits several features reminiscent of those observed in the core region of fibrillar Alzheimer's amyloid beta peptide, including an in-register parallel structure. Although the lengths of the respective core regions differ, fibrils from different amyloid proteins nevertheless appear to be able to take up highly similar, and possibly conserved, structures.
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Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
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Protein aggregation and neurodegenerative disease
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Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
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Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development
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Metadata
- Authors
- Der-Sarkissian, A., Jao, C. C., Chen, J., & Langen, R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-09
- Volume
- 278
- Issue
- 39
- Pages
- 37530-37535
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2038729585
- Cited by
- 329
- References
- 47
- FWCI
- 13.67
- Type
- journal article
- Language
- en
- Open access
- hybrid
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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.
