The DOI matches its Crossref record; 106 of the 106 references it cites were found in a registry or an index.
The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson’s Disease
Open accessAbstract
α-synuclein is a small protein abundantly expressed in the brain and mainly located in synaptic terminals. The conversion of α-synuclein into oligomers and fibrils is the hallmark of a range of neurodegenerative disorders including Parkinson's disease and dementia with Lewy bodies. α-synuclein is disordered in solution but can adopt an α-helical conformation upon binding to lipid membranes. This lipid-protein interaction plays an important role in its proposed biological function, i.e., synaptic plasticity, but can also entail the aggregation of the protein. Both the chemical properties of the lipids and the lipid-to-protein-ratio have been reported to modulate the aggregation propensity of α-synuclein. In this review, the influence of changes in the nature and levels of lipids on the aggregation propensity of α-synuclein in vivo and in vitro will be discussed within a common general framework. In particular, while biophysical measurements and kinetic analyses of the time courses of α-synuclein aggregation in the presence of different types of lipid vesicles allow a mechanistic dissection of the influence of the lipids on α-synuclein aggregation, biological studies of cellular and animal models of Parkinson's disease allow the determination of changes in lipid levels and properties associated with the disease.
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2 retracted
Prasanthi, J. R. P., Feist, G., Thomasson, S., Thompson, A. J., Schommer, E., & Ghribi, O. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05736.x · Cited by 91
RetractedMarwarha, G., Rhen, T., Schommer, T., & Ghribi, O. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07497.x · Cited by 85
RetractedSpillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382
Membrane lipids: where they are and how they behave
van Meer, G., Voelker, D. R., & Feigenson, G. W. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2330 · Cited by 7,157
α-Synuclein Locus Triplication Causes Parkinson's Disease
Singleton, A. B., Farrer, M., Johnson, J., Singleton, A., Hague, S., Kachergus, J., Hulihan, M., Peuralinna, T., Dutra, A., Nussbaum, R., et al. (2003) · Science · doi:10.1126/science.1090278 · Cited by 4,383
Molecular anatomy of a trafficking organelle
Takamori, S., Holt, M., Stenius, K., Lemke, E. A., Grønborg, M., Riedel, D., Urlaub, H., Schenck, S., Brügger, B., Ringler, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.10.030 · Cited by 2,373
α-synuclein locus duplication as a cause of familial Parkinson's disease
Chartier-Harlin, M.-C., Kachergus, J., Roumier, C., Mouroux, V., Douay, X., Lincoln, S., Levecque, C., Larvor, L., Andrieux, J., Hulihan, M., et al. (2004) · The Lancet · doi:10.1016/s0140-6736(04)17103-1 · Cited by 2,029
The Role of Oxidative Stress in Parkinson's Disease
Dias, V., Junn, E., & Mouradian, M. M. (2013) · Journal of Parkinson’s Disease · doi:10.3233/jpd-130230 · Cited by 1,845
α-Synuclein Promotes SNARE-Complex Assembly in Vivo and in Vitro
Burré, J., Sharma, M., Tsetsenis, T., Buchman, V., Etherton, M. R., & Südhof, T. C. (2010) · Science · doi:10.1126/science.1195227 · Cited by 1,812
Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal
Maroteaux, L., Campanelli, J., & Scheller, R. (1988) · The Journal of Neuroscience · doi:10.1523/jneurosci.08-08-02804.1988 · Cited by 1,641
Cited by
Fanning, S., Haque, A., Imberdis, T., Baru, V., Barrasa, M. I., Nuber, S., Termine, D., Ramalingam, N., Ho, G. P. H., Noble, T., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.11.028 · Cited by 285
Probiotic Bacillus subtilis protects against α-synuclein aggregation in C. elegans
Goya, M. E., Xue, F., Sampedro-Torres-Quevedo, C., Arnaouteli, S., Riquelme-Dominguez, L., Romanowski, A., Brydon, J., Ball, K. L., Stanley-Wall, N. R., & Doitsidou, M. (2020) · Cell Reports · doi:10.1016/j.celrep.2019.12.078 · Cited by 205
Gut Microbial Ecosystem in Parkinson Disease: New Clinicobiological Insights from Multi‐Omics
Tan, A. H., Chong, C. W., Lim, S., Yap, I. K. S., Teh, C. S. J., Loke, M. F., Song, S., Tan, J. Y., Ang, B. H., Tan, Y. Q., et al. (2021) · Annals of Neurology · doi:10.1002/ana.25982 · Cited by 196
APOE4 exacerbates α-synuclein pathology and related toxicity independent of amyloid
Zhao, N., Attrebi, O. N., Ren, Y., Qiao, W., Sonustun, B., Martens, Y. A., Meneses, A. D., Li, F., Shue, F., Zheng, J., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aay1809 · Cited by 156
Exploring Sphingolipid Implications in Neurodegeneration
Alessenko, A. V., & Albi, E. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.00437 · Cited by 141
Metadata
- Authors
- Galvagnion, C.
- Venue
- Journal of Parkinson's Disease
- Publisher
- SAGE Publications
- Published
- 2017-08-08
- Volume
- 7
- Issue
- 3
- Pages
- 433-450
- ISSN
- 1877-7171 (ISSN-L)
- 1877-718X
- OpenAlex
- W2727376740
- Cited by
- 258
- References
- 106
- FWCI
- 12.37
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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