The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
Open accessAbstract
Misfolded α-synuclein amyloid fibrils are the principal components of Lewy bodies and neurites, hallmarks of Parkinson's disease (PD). We present a high-resolution structure of an α-synuclein fibril, in a form that induces robust pathology in primary neuronal culture, determined by solid-state NMR spectroscopy and validated by EM and X-ray fiber diffraction. Over 200 unique long-range distance restraints define a consensus structure with common amyloid features including parallel, in-register β-sheets and hydrophobic-core residues, and with substantial complexity arising from diverse structural features including an intermolecular salt bridge, a glutamine ladder, close backbone interactions involving small residues, and several steric zippers stabilizing a new orthogonal Greek-key topology. These characteristics contribute to the robust propagation of this fibril form, as supported by the structural similarity of early-onset-PD mutants. The structure provides a framework for understanding the interactions of α-synuclein with other proteins and small molecules, to aid in PD diagnosis and treatment.
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Cites
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Self-citationMutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
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Cited by
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
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Cryo-EM structures of tau filaments from Alzheimer’s disease
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Discriminating α-synuclein strains in Parkinson’s disease and multiple system atrophy
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Structures of α-synuclein filaments from multiple system atrophy
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Metadata
- Authors
- Tuttle, M. D., Comellas, G., Nieuwkoop, A. J., Covell, D. J., Berthold, D. A., Kloepper, K. D., Courtney, J. M., Kim, J. K., Barclay, A. M., Kendall, A., Wan, W., Stubbs, G., Schwieters, C. D., Lee, V. M. Y., George, J. M., & Rienstra, C. M.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2016-03-28
- Volume
- 23
- Issue
- 5
- Pages
- 409-415
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2317462515
- Cited by
- 959
- References
- 62
- FWCI
- 74.66
- Type
- journal article
- Language
- en
- Open access
- green
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- Tuttle, M. D., Comellas, G., Nieuwkoop, A. J., Covell, D. J., Berthold, D. A., Kloepper, K. D., Courtney, J. M., Kim, J. K., Barclay, A. M., Kendall, A., Wan, W., Stubbs, G., Schwieters, C. D., Lee, V. M. Y., George, J. M., & Rienstra, C. M. (2016). Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.3194
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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.
