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α-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells
Open accessAbstract
Post-mortem analyses of brains from patients with Parkinson disease who received fetal mesencephalic transplants show that α-synuclein-containing (α-syn-containing) Lewy bodies gradually appear in grafted neurons. Here, we explored whether intercellular transfer of α-syn from host to graft, followed by seeding of α-syn aggregation in recipient neurons, can contribute to this phenomenon. We assessed α-syn cell-to-cell transfer using microscopy, flow cytometry, and high-content screening in several coculture model systems. Coculturing cells engineered to express either GFP- or DsRed-tagged α-syn resulted in a gradual increase in double-labeled cells. Importantly, α-syn-GFP derived from 1 neuroblastoma cell line localized to red fluorescent aggregates in other cells expressing DsRed-α-syn, suggesting a seeding effect of transmitted α-syn. Extracellular α-syn was taken up by cells through endocytosis and interacted with intracellular α-syn. Next, following intracortical injection of recombinant α-syn in rats, we found neuronal uptake was attenuated by coinjection of an endocytosis inhibitor. Finally, we demonstrated in vivo transfer of α-syn between host cells and grafted dopaminergic neurons in mice overexpressing human α-syn. In summary, intercellularly transferred α-syn interacts with cytoplasmic α-syn and can propagate α-syn pathology. These results suggest that α-syn propagation is a key element in the progression of Parkinson disease pathology.
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“Particularly, the oligomeric α-Syn species appear to be prone to uptake and spread from cell-to-cell in a prion-like manner, leading to the templated misfolding of the native forms of α-Syn and formation of α-Syn aggregates throughout the brain, which are the defining pathological features of Parkinson’s disease (PD) and dementia with Lewy body (DLB) [12–19].”
From LRP1 is a neuronal receptor for α-synuclein uptake and spread (2022) · cites this paper as [18]
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“In cell culture, however, the prion-like propagation of α-synuclein lesions has been demonstrated80, 81”
From Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders (2011) · cites this paper as [81]
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Cites
Staging of brain pathology related to sporadic Parkinson’s disease
Braak, H., Tredici, K. D., Rüb, U., de Vos, R. A. I., Jansen Steur, E. N. H., & Braak, E. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00065-9 · Cited by 10,777
Spillantini, 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
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240
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
AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
Krüger, R., Kuhn, W., Müller, T., Woitalla, D., Graeber, M., Kösel, S., Przuntek, H., Epplen, J. T., Schols, L., & Riess, O. (1998) · Nature Genetics · doi:10.1038/ng0298-106 · Cited by 3,836
The new mutation, E46K, of α‐synuclein causes parkinson and Lewy body dementia
Zarranz, J. J., Alegre, J., Gómez‐Esteban, J. C., Lezcano, E., Ros, R., Ampuero, I., Vidal, L., Hoenicka, J., Rodriguez, O., Atarés, B., et al. (2004) · Annals of Neurology · doi:10.1002/ana.10795 · Cited by 2,737
Adapting Proteostasis for Disease Intervention
Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008) · Science · doi:10.1126/science.1141448 · Cited by 2,495
α-Synuclein Promotes SNARE-Complex Assembly in Vivo and in Vitro
Burré, J., Sharma, M., Tsetsenis, T., Buchman, V. L., Etherton, M. R., & Südhof, T. C. (2010) · Science · doi:10.1126/science.1195227 · Cited by 1,904
Li, J.-Y., Englund, E., Holton, J. L., Soulet, D., Hagell, P., Lees, A. J., Lashley, T., Quinn, N. P., Rehncrona, S., Björklund, A., et al. (2008) · Nature Medicine · doi:10.1038/nm1746 · Cited by 1,845
Self-citationTransmission and spreading of tauopathy in transgenic mouse brain
Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803
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Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563
Non-motor features of Parkinson disease
Schapira, A. H. V., Chaudhuri, K. R., & Jenner, P. (2017) · Nature Reviews Neuroscience · doi:10.1038/nrn.2017.62 · Cited by 2,053
Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663
Volpicelli-Daley, L. A., Luk, K. C., Patel, T. P., Tanik, S. A., Riddle, D. M., Stieber, A., Meaney, D. F., Trojanowski, J. Q., & Lee, V. M.-Y. (2011) · Neuron · doi:10.1016/j.neuron.2011.08.033 · Cited by 1,569
The Biology of Proteostasis in Aging and Disease
Labbadia, J., & Morimoto, R. I. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033955 · Cited by 1,472
-Synuclein in Parkinson's Disease
Stefanis, L. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009399 · Cited by 1,446
Goedert, M., Spillantini, M. G., Del Tredici, K., & Braak, H. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.242 · Cited by 1,190
Selective neuronal vulnerability in Parkinson disease
Surmeier, D. J., Obeso, J. A., & Halliday, G. M. (2017) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.178 · Cited by 1,116
Luk, K. C., Kehm, V. M., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M. ‐. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20112457 · Cited by 1,133
Direct evidence of Parkinson pathology spread from the gastrointestinal tract to the brain in rats
Holmqvist, S., Chutna, O., Bousset, L., Aldrin-Kirk, P., Li, W., Björklund, T., Wang, Z.-Y., Roybon, L., Melki, R., & Li, J.-Y. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1343-6 · Cited by 925
Self-citationStructural and functional characterization of two alpha-synuclein strains
Bousset, L., Pieri, L., Ruiz-Arlandis, G., Gath, J., Jensen, P. H., Habenstein, B., Madiona, K., Oliéric, V., Böckmann, A., Meier, B. H., et al. (2013) · Nature Communications · doi:10.1038/ncomms3575 · Cited by 925
Self-citationHeparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds
Holmes, B. B., DeVos, S. L., Kfoury, N., Li, M., Jacks, R., Yanamandra, K., Ouidja, M. O., Brodsky, F. M., Marasa, J., Bagchi, D. P., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301440110 · Cited by 859
Spreading of pathology in neurodegenerative diseases: a focus on human studies
Brettschneider, J., Tredici, K. D., Lee, V. M.-Y., & Trojanowski, J. Q. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3887 · Cited by 790
Human iPSC-based modeling of late-onset disease via progerin-induced aging
Miller, J. D., Ganat, Y. M., Kishinevsky, S., Bowman, R. L., Liu, B., Tu, E. Y., Mandal, P. K., Vera, E., Shim, J.-W., Kriks, S., et al. (2013) · Cell stem cell · doi:10.1016/j.stem.2013.11.006 · Cited by 777
Predicting Regional Neurodegeneration from the Healthy Brain Functional Connectome
Zhou, J., Gennatas, E. D., Kramer, J. H., Miller, B. L., & Seeley, W. W. (2012) · Neuron · doi:10.1016/j.neuron.2012.03.004 · Cited by 706
Plasma exosomal α-synuclein is likely CNS-derived and increased in Parkinson’s disease
Shi, M., Liu, C., Cook, T. J., Bullock, K. M., Zhao, Y., Ginghina, C., Li, Y., Aro, P., Dator, R., He, C., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1314-y · Cited by 676
Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
Lee, E. B., Lee, V. M.-Y., & Trojanowski, J. Q. (2012) · Nature Reviews Neuroscience · doi:10.1038/nrn3121 · Cited by 659
Exner, N., Lutz, A. K., Haass, C., & Winklhofer, K. F. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.170 · Cited by 675
Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases
Guo, J. L., & Lee, V. M. Y. (2014) · Nature Medicine · doi:10.1038/nm.3457 · Cited by 641
Recasens, A., Dehay, B., Bové, J., Carballo‐Carbajal, I., Doveró, S., Pérez‐Villalba, A., Fernagut, P., Blesa, J., Parent, A., Perier, C., et al. (2013) · Annals of Neurology · doi:10.1002/ana.24066 · Cited by 667
Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
Jucker, M., & Walker, L. C. (2011) · Annals of Neurology · doi:10.1002/ana.22615 · Cited by 622
Trans-cellular Propagation of Tau Aggregation by Fibrillar Species
Kfoury, N., Holmes, B. B., Jiang, H., Holtzman, D. M., & Diamond, M. I. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.346072 · Cited by 552
Mitochondrial dysfunction and mitophagy in Parkinson's: from familial to sporadic disease
Ryan, B. J., Hoek, S., Fon, E. A., & Wade-Martins, R. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.02.003 · Cited by 524
Microglial exosomes facilitate α-synuclein transmission in Parkinson’s disease
Guo, M., Wang, J., Zhao, Y., Feng, Y., Han, S., Dong, Q., Cui, M., & Tieu, K. (2020) · Brain · doi:10.1093/brain/awaa090 · Cited by 522
α-Synuclein misfolding and aggregation: Implications in Parkinson’s disease pathogenesis
Mehra, S., Sahay, S., & Maji, S. K. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.03.001 · Cited by 527
Dauvilliers, Y. A., Schenck, C. H., Postuma, R. B., Iranzo, Á., Luppi, P., Plazzi, G., Montplaisir, J. Y., & Boeve, B. F. (2018) · Nature Reviews Disease Primers · doi:10.1038/s41572-018-0016-5 · Cited by 516
Neuropathology of sporadic Parkinson's disease: Evaluation and changes of concepts
Jellinger, K. A. (2011) · Movement Disorders · doi:10.1002/mds.23795 · Cited by 480
Transmission of multiple system atrophy prions to transgenic mice
Watts, J. C., Giles, K., Oehler, A., Middleton, L. T., Dexter, D. T., Gentleman, S., DeArmond, S. J., & Prusiner, S. B. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318268110 · Cited by 454
Linking Neuroinflammation and Neurodegeneration in Parkinson's Disease
Gelders, G., Baekelandt, V., & Van der Perren, A. (2018) · Journal of Immunology Research · doi:10.1155/2018/4784268 · Cited by 430
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Abounit, S., Bousset, L., Loria, F., Zhu, S., de Chaumont, F., Pieri, L., Olivo‐Marin, J., Melki, R., & Zurzolo, C. (2016) · The EMBO Journal · doi:10.15252/embj.201593411 · Cited by 414
Self-citationProdromal Parkinson disease subtypes — key to understanding heterogeneity
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Bellingham, S. A., Guo, B. B., Coleman, B. M., & Hill, A. F. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00124 · Cited by 412
Review: Sporadic Parkinson's disease: development and distribution ofα‐synuclein pathology
Tredici, K. D., & Braak, H. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12298 · Cited by 414
Exploring Braak’s hypothesis of Parkinson’s disease
Rietdijk, C. D., Perez-Pardo, P., Garssen, J., van Wezel, R. J. A., & Kraneveld, A. D. (2017) · Frontiers in Neurology · doi:10.3389/fneur.2017.00037 · Cited by 395
Parkinson's Disease and Alpha Synuclein: Is Parkinson's Disease a Prion‐Like Disorder?
Olanow, C. W., & Brundin, P. (2013) · Movement Disorders · doi:10.1002/mds.25373 · Cited by 404
Self-citationMicroglia and astrocyte dysfunction in parkinson's disease
Kam, T., Hinkle, J. T., Dawson, T. M., & Dawson, V. L. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105028 · Cited by 414
Schapira, A. H. V., Olanow, C. W., Greenamyre, J. T., & Bézard, E. (2014) · The Lancet · doi:10.1016/s0140-6736(14)61010-2 · Cited by 399
Paumier, K. L., Luk, K. C., Manfredsson, F. P., Kanaan, N. M., Lipton, J. W., Collier, T. J., Steece‐Collier, K., Kemp, C. J., Celano, S. L., Schulz, E., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.06.003 · Cited by 411
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
Acceleration of α-Synuclein Aggregation by Exosomes
Grey, M., Dunning, C. J. R., Gaspar, R., Grey, C. E., Brundin, P., Sparr, E., & Linse, S. S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.585703 · Cited by 383
Self-citationThe Seeds of Neurodegeneration: Prion-like Spreading in ALS
Polymenidou, M., & Cleveland, D. W. (2011) · Cell · doi:10.1016/j.cell.2011.10.011 · Cited by 382
Alpha-synuclein biology in Lewy body diseases
Kim, W. S., Kågedal, K., & Halliday, G. M. (2014) · Alzheimer s Research & Therapy · doi:10.1186/s13195-014-0073-2 · Cited by 397
Neuron‐to‐neuron transmission of α‐synuclein fibrils through axonal transport
Freundt, E. C., Maynard, N., Clancy, E. K., Roy, S., Bousset, L., Sourigues, Y., Covert, M. W., Melki, R., Kirkegaard, K., & Brahic, M. (2012) · Annals of Neurology · doi:10.1002/ana.23747 · Cited by 394
Self-citationBraak, H., & Del Tredici, K. (2017) · Journal of Parkinson’s Disease · doi:10.3233/jpd-179001 · Cited by 372
Paillusson, S., Gómez‐Suaga, P., Stoica, R., Little, D., Gissen, P., Devine, M. J., Noble, W. J., Hanger, D. P., & Miller, C. C. J. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1704-z · Cited by 379
Astrocyte Heterogeneity: Impact to Brain Aging and Disease
Matias, I., Morgado, J., & Gomes, F. C. A. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00059 · Cited by 387
Scheiblich, H., Dansokho, C., Mercan, D., Schmidt, S. V., Bousset, L., Wischhof, L., Eikens, F., Odainic, A., Spitzer, J., Griep, A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.09.007 · Cited by 360
Self-citationAlzheimer’s pathogenesis: is there neuron-to-neuron propagation?
Braak, H., & Tredici, K. D. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0825-z · Cited by 375
Pathological roles of α-synuclein in neurological disorders
Vekrellis, K., Xilouri, M., Emmanouilidou, E., Rideout, H. J., & Stefanis, L. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70213-7 · Cited by 380
Alpha-synuclein oligomers: a new hope
Bengoa‐Vergniory, N., Roberts, R. F., Wade‐Martins, R., & Alegre‐Abarrategui, J. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1755-1 · Cited by 345
Human Astrocytes Transfer Aggregated Alpha-Synuclein via Tunneling Nanotubes
Rostami, J., Holmqvist, S., Lindström, V., Sigvardson, J., Westermark, G. T., Ingelsson, M., Bergström, J., Roybon, L., & Erlandsson, A. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.0983-17.2017 · Cited by 339
Antibody-Aided Clearance of Extracellular α-Synuclein Prevents Cell-to-Cell Aggregate Transmission
Bae, E.-J., Lee, H.-J., Rockenstein, E., Ho, D.-H., Park, E.-B., Yang, N.-Y., Desplats, P., Masliah, E., & Lee, S.-J. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.1292-12.2012 · Cited by 339
Exosomes: Mediators of Neurodegeneration, Neuroprotection and Therapeutics
Kalani, A., Tyagi, A. A., & Tyagi, N. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8544-1 · Cited by 339
Vagal neurocircuitry and its influence on gastric motility
Travagli, R. A., & Anselmi, L. (2016) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2016.76 · Cited by 323
Like prions: the propagation of aggregated tau and α-synuclein in neurodegeneration
Goedert, M., Masuda-Suzukake, M., & Falcon, B. (2017) · Brain · doi:10.1093/brain/aww230 · Cited by 323
Ferroptosis in Parkinson’s disease: glia–neuron crosstalk
Wang, Z.-L., Yuan, L., Li, W., & Li, J.-Y. (2022) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2022.02.003 · Cited by 319
Self-citationRole of Exosomes/Microvesicles in the Nervous System and Use in Emerging Therapies
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Propagation of Protein Aggregation in Neurodegenerative Diseases
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Extracellular α-synuclein—a novel and crucial factor in Lewy body diseases
Lee, H.-J., Bae, E.-J., & Lee, S. (2014) · Nature Reviews Neurology · doi:10.1038/nrneurol.2013.275 · Cited by 313
Exosomes: vesicular carriers for intercellular communication in neurodegenerative disorders
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Kalia, L. V., Kalia, S. K., McLean, P. J., Lozano, A. M., & Lang, A. E. (2012) · Annals of Neurology · doi:10.1002/ana.23746 · Cited by 309
α-Synuclein pathology in Parkinson’s disease and related α-synucleinopathies
Henderson, M. X., Trojanowski, J. Q., & Lee, V. M. ‐. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.134316 · Cited by 298
Loría, F., Vargas, J., Bousset, L., Syan, S., Salles, A., Melki, R., & Zurzolo, C. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1746-2 · Cited by 289
Self-citationFreeman, D., Cedillos, R., Choyke, S., Lukic, Z., McGuire, K., Marvin, S., Burrage, A. M., Sudholt, S., Rana, A., O'Connor, C., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062143 · Cited by 289
Alpha-synuclein: from secretion to dysfunction and death
Marques, O., & Outeiro, T. F. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.94 · Cited by 296
Self-citationThe prion hypothesis in Parkinson's disease: braak to the future
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Alpha‐synuclein transfers from neurons to oligodendrocytes
Reyes, J. F., Rey, N. L., Bousset, L., Melki, R., Brundin, P., & Angot, É. (2013) · Glia · doi:10.1002/glia.22611 · Cited by 278
Self-citationPrying into the Prion Hypothesis for Parkinson's Disease
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Self-citationVan der Perren, A., Gelders, G., Fenyi, A., Bousset, L., Brito, F., Peelaerts, W., Van den Haute, C., Gentleman, S., Melki, R., & Baekelandt, V. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02157-3 · Cited by 277
Self-citationRoberts, R. F., Wade‐Martins, R., & Alegre‐Abarrategui, J. (2015) · Brain · doi:10.1093/brain/awv040 · Cited by 280
Diógenes, M. J., Dias, R. B., Rombo, D. M., Miranda, H. V., Maiolino, F., Guerreiro, P. S., Näsström, T., Franquelim, H. G., Oliveira, L. M. A., Castanho, M. A. R. B., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0234-12.2012 · Cited by 272
Self-citationAlpha-synuclein cell-to-cell transfer and seeding in grafted dopaminergic neurons in vivo
Angot, E., Steiner, J. A., Lema Tomé, C. M., Ekström, P., Mattsson, B., Björklund, A., & Brundin, P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039465 · Cited by 270
Self-citationThe ongoing pursuit of neuroprotective therapies in Parkinson disease
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Rey, N. L., Petit, G. H., Bousset, L., Melki, R., & Brundin, P. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1160-3 · Cited by 267
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Self-citationProtein degradation pathways in Parkinson’s disease: curse or blessing
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Ulusoy, A., Rusconi, R., Pérez‐Revuelta, B. I., Musgrove, R. E., Helwig, M., Winzen‐Reichert, B., & Monte, D. A. D. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201302475 · Cited by 253
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Self-citationLindström, V., Gustafsson, G., Sanders, L. H., Howlett, E. H., Sigvardson, J., Kasrayan, A., Ingelsson, M., Bergström, J., & Erlandsson, A. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.04.009 · Cited by 233
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Nath, S., Agholme, L., Kurudenkandy, F. R., Granseth, B., Marcusson, J., & Hallbeck, M. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0615-12.2012 · Cited by 244
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Metadata
- Authors
- Hansen, C., Angot, E., Bergström, A.-L., Steiner, J. A., Pieri, L., Paul, G., Outeiro, T. F., Melki, R., Kallunki, P., Fog, K., Li, J.-Y., & Brundin, P.
- Affiliations
- Lund University (SE)
- Lundbeck (Denmark) (DK)
- Laboratoire d'Enzymologie et Biochimie Structurales (FR)
- University of Lisbon (PT)
- Corresponding author
- Brundin, Patrik
- ORCID
- Venue
- Journal of Clinical Investigation
- Published
- 2011-02-01
- Volume
- 121
- Issue
- 2
- Pages
- 715-725
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC3026723
- OpenAlex
- W2046885195
- Cited by
- 842
- References
- 42
- Citations by year
- 2026: 13 · 2025: 26 · 2024: 25 · 2023: 31 · 2022: 43 · 2021: 69 · 2020: 70 · 2019: 59 · 2018: 51 · 2017: 72 · 2016: 68 · 2015: 68 · 2014: 64 · 2013: 77 · 2012: 64
- FWCI
- 50.08
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- GoeScholar The Publication Server of the Georg-August-Universität Göttingen (Georg-August-Universität Göttingen) (submittedVersion, cc-by)
- Lund University Publications (Lund University) (submittedVersion, other-oa)
- Funders
- Michael J. Fox Foundation for Parkinson's Research
- Agence Nationale de la Recherche
- Knut och Alice Wallenbergs Stiftelse
- Vetenskapsrådet
- Stiftelsen Lars Hiertas Minne
- Centre National de la Recherche Scientifique
- Parkinsonfonden
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- alpha-synuclein, Parkinson's disease, Lewy bodies, intercellular transfer, endocytosis, neuroblastoma cells, intracortical injection
- MeSH terms
- Animals, Brain, Cells, Cultured, Dopamine, Humans, Neurons, Parkinson Disease, Recombinant Fusion Proteins, Lewy Bodies, Culture Media, Conditioned, Cell Transplantation, Coculture Techniques, Mice, Rats, alpha-Synuclein, HEK293 Cells
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