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A Broken α-Helix in Folded α-Synuclein
Open accessAbstract
alpha-Synuclein is a small cytosolic protein of presynaptic nerve terminals composed of seven 11-residue repeats and a hydrophilic tail. alpha-Synuclein misfolding and dysfunction may contribute to the pathogenesis of Parkinson's disease and neurodegenerative dementias, but its normal folding and function are unknown. In solution, alpha-synuclein is natively unstructured but assumes an alpha-helical conformation upon binding to phospholipid membranes. We now show that this conformation of alpha-synuclein consists of two alpha-helical regions that are interrupted by a short break. The structural organization of the alpha-helices of alpha-synuclein was not anticipated by sequence analyses and may be important for its pathogenic role.
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Cites
The rat brain synucleins; family of proteins transiently associated with neuronal membrane
Maroteaux, L., & Scheller, R. H. (1991) · Molecular Brain Research · doi:10.1016/0169-328x(91)90043-w · Cited by 334
Cited by
Gaggelli, E., Kozlowski, H., Valensin, D., & Valensin, G. (2006) · Chemical Reviews · doi:10.1021/cr040410w · Cited by 1,729
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
Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)
Theillet, F.-X., Binolfi, A., Frembgen-Kesner, T., Hingorani, K., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 503
A soluble α-synuclein construct forms a dynamic tetramer
Wang, W., Perovic, I., Chittuluru, J., Kaganovich, A., Nguyen, L. T. T., Liao, J., Auclair, J. R., Johnson, D., Landeru, A., Simorellis, A. K., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113260108 · Cited by 478
Alpha-synuclein structure and Parkinson’s disease – lessons and emerging principles
Meade, R. M., Fairlie, D. P., & Mason, J. M. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0329-1 · Cited by 404
Alpha-Synuclein Oligomers—Neurotoxic Molecules in Parkinson's Disease and Other Lewy Body Disorders
Ingelsson, M. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00408 · Cited by 344
The physiological role of α‐synuclein and its relationship to Parkinson’s Disease
Sulzer, D., & Edwards, R. H. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14810 · Cited by 312
Mutation E46K increases phospholipid binding and assembly into filaments of human α‐synuclein
Choi, W., Zibaee, S., Jakes, R., Serpell, L. C., Davletov, B., Anthony Crowther, R., & Goedert, M. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.09.038 · Cited by 286
Part II: α-synuclein and its molecular pathophysiological role in neurodegenerative disease
Dev, K. (2003) · Neuropharmacology · doi:10.1016/s0028-3908(03)00140-0 · Cited by 263
The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson’s Disease
Galvagnion, C. (2017) · Journal of Parkinson's Disease · doi:10.3233/jpd-171103 · Cited by 258
Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
Alderson, T. R., Pritišanac, I., Kolarić, Đ., Moses, A. M., & Forman-Kay, J. D. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2304302120 · Cited by 240
Mandal, P. K., Pettegrew, J. W., Masliah, E., Hamilton, R. L., & Mandal, R. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9140-9 · Cited by 219
Fluid Biomarkers for Synaptic Dysfunction and Loss
Camporesi, E., Nilsson, J., Brinkmalm, A., Becker, B., Ashton, N. J., Blennow, K., & Zetterberg, H. (2020) · Biomarker Insights · doi:10.1177/1177271920950319 · Cited by 165
Ben Gedalya, T., Loeb, V., Israeli, E., Altschuler, Y., Selkoe, D. J., & Sharon, R. (2009) · Traffic · doi:10.1111/j.1600-0854.2008.00853.x · Cited by 169
Dilsizoglu Senol, A., Samarani, M., Syan, S., Guardia, C. M., Nonaka, T., Liv, N., Latour-Lambert, P., Hasegawa, M., Klumperman, J., Bonifacino, J. S., et al. (2021) · PLOS Biology · doi:10.1371/journal.pbio.3001287 · Cited by 134
Alpha-Synuclein: Mechanisms of Release and Pathology Progression in Synucleinopathies
Brás, I. C., & Outeiro, T. F. (2021) · Cells · doi:10.3390/cells10020375 · Cited by 136
Defining α-synuclein species responsible for Parkinson’s disease phenotypes in mice
Froula, J. M., Castellana-Cruz, M., Anabtawi, N. M., Camino, J. D., Chen, S. W., Thrasher, D. R., Freire, J., Yazdi, A. A., Fleming, S., Dobson, C. M., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.007743 · Cited by 129
Amino acid sequence motifs and mechanistic features of the membrane translocation of α‐synuclein
Ahn, K. J., Paik, S. R., Chung, K. C., & Kim, J. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03731.x · Cited by 123
Intrinsically disordered proteins and membranes: a marriage of convenience for cell signalling?
Cornish, J., Chamberlain, S. G., Owen, D., & Mott, H. R. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200467 · Cited by 69
Increased Risk of Aging-Related Neurodegenerative Disease after Traumatic Brain Injury
Barker, S., Paul, B., & Pieper, A. (2023) · Biomedicines · doi:10.3390/biomedicines11041154 · Cited by 55
Extracellular Alpha-Synuclein: Mechanisms for Glial Cell Internalization and Activation
Chavarría, C., Ivagnes, R., & Souza, J. M. (2022) · Biomolecules · doi:10.3390/biom12050655 · Cited by 47
Genetic Defects and Pro-inflammatory Cytokines in Parkinson's Disease
Magnusen, A. F., Hatton, S. L., Rani, R., & Pandey, M. K. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.636139 · Cited by 47
Metadata
- Authors
- Chandra, S., Chen, X., Rizo, J., Jahn, R., & Südhof, T. C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-04
- Volume
- 278
- Issue
- 17
- Pages
- 15313-15318
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1844422703
- Cited by
- 540
- References
- 1
- FWCI
- 13.46
- Type
- journal article
- Language
- en
- Open access
- hybrid
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