The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
GM1 Specifically Interacts with α-Synuclein and Inhibits Fibrillation
Abstract
The aggregation of alpha-synuclein is believed to be a key step in the etiology of Parkinson's disease. Alpha-synuclein is found in the cytosol and is associated with membranes in the presynaptic region of neurons and has recently been reported to be associated with lipid rafts and caveolae. We examined the interactions between several brain sphingolipids and alpha-synuclein and found that alpha-synuclein specifically binds to ganglioside GM1-containing small unilamellar vesicles (SUVs). This results in the induction of substantial alpha-helical structure and inhibition or elimination of alpha-synuclein fibril formation, depending on the amount of GM1 present. SUVs containing total brain gangliosides, gangliosides GM2 or GM3, or asialo-GM1 had weak inhibitory effects on alpha-synuclein fibrillation and induced some alpha-helical structure, while all other sphingolipids studied showed negligible interaction with alpha-synuclein. alpha-Synuclein binding to GM1-containing SUVs was accompanied by formation of oligomers of alpha-synuclein. The familial mutant A53T alpha-synuclein interacted with GM1-containing SUVs in an analogous manner to wild type, whereas the A30P mutant showed minimal interaction. This is the first detailed report showing a direct association between GM1 and alpha-synuclein, which is attributed to specific interaction between helical alpha-synuclein and both the sialic acid and carbohydrate moieties of GM1. The recruitment of alpha-synuclein by GM1 to caveolae and lipid raft regions in membranes could explain alpha-synuclein's localization to presynaptic membranes and raises the possibility that perturbation of GM1/raft association could induce changes in alpha-synuclein that contribute to the pathogenesis of PD.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
FUNCTIONS OF LIPID RAFTS IN BIOLOGICAL MEMBRANES
Brown, D. A., & London, E. (1998) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.14.1.111 · Cited by 2,948
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
Stabilization of α-Synuclein Secondary Structure upon Binding to Synthetic Membranes
Davidson, W. S., Jonas, A., Clayton, D. F., & George, J. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9443 · Cited by 1,585
Conway, K. A., Harper, J. D., & Lansbury, P. T. (1998) · Nature Medicine · doi:10.1038/3311 · Cited by 1,499
The State of Lipid Rafts: From Model Membranes to Cells
Edidin, M. (2003) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.32.110601.142439 · Cited by 1,341
Caveolae: From Cell Biology to Animal Physiology
Razani, B., Woodman, S. E., & Lisanti, M. P. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.431 · Cited by 987
Segrest, J., Jones, M., De Loof, H., Brouillette, C., Venkatachalapathi, Y., & Anantharamaiah, G. (1992) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)41536-6 · Cited by 866
Impey, S., Obrietan, K., & Storm, D. R. (1999) · Neuron · doi:10.1016/s0896-6273(00)80747-3 · Cited by 613
α-Synuclein Shares Physical and Functional Homology with 14-3-3 Proteins
Ostrerova, N., Petrucelli, L., Farrer, M., Mehta, N., Choi, P., Hardy, J., & Wolozin, B. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-14-05782.1999 · Cited by 564
Cited by
Mazzulli, J. R., Xu, Y.-H., Sun, Y., Knight, A. L., McLean, P. J., Caldwell, G. A., Sidransky, E., Grabowski, G. A., & Krainc, D. (2011) · Cell · doi:10.1016/j.cell.2011.06.001 · Cited by 1,341
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
Galvagnion, C., Brown, J. W. P., Ouberai, M. M., Flagmeier, P., Vendruscolo, M., Buell, A. K., Sparr, E., & Dobson, C. M. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1601899113 · Cited by 308
Sphingolipids and gangliosides of the nervous system in membrane function and dysfunction
Posse de Chaves, E., & Sipione, S. (2010) · FEBS Letters · doi:10.1016/j.febslet.2009.12.010 · Cited by 274
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
Metadata
- Authors
- Martinez, Z., Zhu, M., Han, S., & Fink, A. L.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2007-01-25
- Volume
- 46
- Issue
- 7
- Pages
- 1868-1877
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1981426567
- Cited by
- 260
- References
- 33
- FWCI
- 4.71
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: GM1 Specifically Interacts with α-Synuclein and Inhibits Fibrillation. https://app.cochat.ai/papers/10.1021/bi061749a
- The paper
- Martinez, Z., Zhu, M., Han, S., & Fink, A. L. (2007). GM1 Specifically Interacts with α-Synuclein and Inhibits Fibrillation. Biochemistry. https://doi.org/10.1021/bi061749a
Data sources
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).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
