The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Mapping Long-Range Interactions in α-Synuclein using Spin-Label NMR and Ensemble Molecular Dynamics Simulations
Abstract
The intrinsically disordered protein alpha-synuclein plays a key role in the pathogenesis of Parkinson's disease (PD). We show here that the native state of alpha-synuclein consists of a broad distribution of conformers with an ensemble-averaged hydrodynamic radius significantly smaller than that expected for a random coil structure. This partial condensation is driven by interactions between the highly charged C-terminus and a large hydrophobic central region of the protein sequence. We suggest that this structure could inhibit the formation of alpha-synuclein aggregates, which are thought to be the cytotoxic species responsible for neurodegeneration in PD.
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Citations
Cites
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
Self-citationIntrinsic Disorder and Protein Function
Dunker, A. K., Brown, C. J., Lawson, J. D., Iakoucheva, L. M., & Obradović, Z. (2002) · Biochemistry · doi:10.1021/bi012159+ · Cited by 1,731
Cited by
The amyloid state and its association with protein misfolding diseases.
Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382
Self-citationNott, T. J., Petsalaki, E., Farber, P., Jervis, D., Fussner, E., Plochowietz, A., Craggs, T. D., Bazett-Jones, D. P., Pawson, T., Forman-Kay, J. D., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.013 · Cited by 1,803
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
Self-citationThe fold of α-synuclein fibrils
Vilar, M., Chou, H.-T., Lührs, T., Maji, S. K., Riek-Loher, D., Verel, R., Manning, G., Stahlberg, H., & Riek, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712179105 · Cited by 541
Metadata
- Authors
- Dedmon, M. M., Lindorff-Larsen, K., Christodoulou, J., Vendruscolo, M., & Dobson, C. M.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2004-12-21
- Volume
- 127
- Issue
- 2
- Pages
- 476-477
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2052660967
- Cited by
- 716
- References
- 2
- FWCI
- 5.90
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
