The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
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.
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
Experimental — accuracy not yet measuredIn the citing paper
“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]
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
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
Flagged first, then by citations
Cited by
Sorted by citations
Items 301–400 of 834
Generalization of the Prion Hypothesis to Other Neurodegenerative Diseases: An Imperfect Fit
Guest, W. C., Silverman, J. M., Pokrishevsky, E., O’Neill, M. A., Grad, L. I., & Cashman, N. R. (2011) · Journal of Toxicology and Environmental Health · doi:10.1080/15287394.2011.618967 · Cited by 67
Greene, J. G. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5859 · Cited by 69
Physiological and pathological roles of exosomes in the nervous system
Yuyama, K., & Igarashi, Y. (2016) · BioMolecular Concepts · doi:10.1515/bmc-2015-0033 · Cited by 66
Oh, S. H., Kim, H., Park, H.-J., Shin, J. Y., Kim, D. Y., & Lee, P. H. (2016) · Stem Cells Translational Medicine · doi:10.5966/sctm.2016-0111 · Cited by 68
Ageta, H., & Tsuchida, K. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03246-7 · Cited by 67
Luna, E., & Luk, K. C. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.10.023 · Cited by 67
Eisbach, S. E., & Outeiro, T. F. (2013) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1038-9 · Cited by 65
Self-citationα-Synuclein in Extracellular Vesicles: Functional Implications and Diagnostic Opportunities
Lööv, C., Scherzer, C. R., Hyman, B. T., Breakefield, X. O., & Ingelsson, M. (2016) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0317-0 · Cited by 68
Anti-aging treatments slow propagation of synucleinopathy by restoring lysosomal function
Kim, D., Lim, H.-S., Kawasaki, I., Shim, Y., Vaikath, N. N., El‐Agnaf, O. M. A., Lee, H.-J., & Lee, S. (2016) · Autophagy · doi:10.1080/15548627.2016.1207014 · Cited by 67
Rab GTPases: The Key Players in the Molecular Pathway of Parkinson’s Disease
Shi, M., Shi, C., & Xu, Y. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00081 · Cited by 66
Choi, Y. R., Cha, S., Kang, S., Kim, J.-B., Jou, I., & Park, S. M. (2018) · Cell Reports · doi:10.1016/j.celrep.2017.12.009 · Cited by 69
Pieri, L., Chafey, P., Gall, M. L., Clary, G., Melki, R., & Redeker, V. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.10.007 · Cited by 66
Self-citationRey, N. L., George, S., & Brundin, P. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12299 · Cited by 67
Self-citationZeineddine, R., & Yerbury, J. J. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00277 · Cited by 67
Pröschel, C., Stripay, J. L., Shih, C., Munger, J. C., & Noble, M. (2014) · EMBO Molecular Medicine · doi:10.1002/emmm.201302878 · Cited by 65
Beekes, M., Thomzig, A., Schulz‐Schaeffer, W., & Burger, R. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1324-9 · Cited by 67
Induced pluripotent stem cells in Parkinson's disease: scientific and clinical challenges
Xiao, B., Ng, H., Takahashi, R., & Tan, E.-K. (2016) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2015-312036 · Cited by 69
Fan, R. Z., Guo, M. A., Luo, S., Cui, M., & Tieu, K. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0821-4 · Cited by 63
Burbidge, K. J., Rademacher, D. J., Mattick, J., Zack, S. R., Grillini, A., Bousset, L., Kwon, O., Kubicki, K., Simon, A., Melki, R., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1967615 · Cited by 64
Self-citationGut-to-Brain α-Synuclein Transmission in Parkinson’s Disease: Evidence for Prion-like Mechanisms
Chen, M., & Mor, D. E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087205 · Cited by 65
Interaction between -Synuclein and Other Proteins in Neurodegenerative Disorders
Jellinger, K. A. (2011) · The Scientific World JOURNAL · doi:10.1100/2011/371893 · Cited by 64
Ottolini, D., Calí, T., Szabó, I., & Brini, M. (2016) · Biological Chemistry · doi:10.1515/hsz-2016-0201 · Cited by 65
Molecular mechanisms of proteinopathies across neurodegenerative disease: a review
Marsh, A. (2019) · Neurological Research and Practice · doi:10.1186/s42466-019-0039-8 · Cited by 64
Schaser, A. J., Stackhouse, T. L., Weston, L. J., Kerstein, P. C., Osterberg, V. R., López, C. S., Dickson, D. W., Luk, K. C., Meshul, C. K., Woltjer, R. L., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01026-0 · Cited by 63
Cellular Aspects of Prion Replication In Vitro
Grassmann, A., Wolf, H., Hofmann, J. P., Graham, J. F., & Vorberg, I. M. (2013) · Viruses · doi:10.3390/v5010374 · Cited by 62
Xiao, Y., Chen, X., Huang, S., Li, G., Mo, M., Zhang, L., Chen, C., Guo, W., Zhou, M., Wu, Z., et al. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14312 · Cited by 62
Thomsen, M. B., Ferreira, S. A., Schacht, A. C., Jacobsen, J., Simonsen, M., Betzer, C., Jensen, P. H., Brooks, D. J., Landau, A. M., & Romero‐Ramos, M. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105229 · Cited by 67
Nussbaum-Krammer, C. I., & Morimoto, R. I. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.013011 · Cited by 68
The Skin and Parkinson's Disease: Review of Clinical, Diagnostic, and Therapeutic Issues
Škorvánek, M., & Bhatia, K. P. (2016) · Movement Disorders Clinical Practice · doi:10.1002/mdc3.12425 · Cited by 62
Masnata, M., Sciacca, G., Maxan, A., Bousset, L., Denis, H. L., Lauruol, F., David, L. S., Saint‐Pierre, M., Kordower, J. H., Melki, R., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01973-6 · Cited by 64
Self-citationRadford, R. A. W., Rcom-H'cheo-Gauthier, A. N., Wong, M. B., Eaton, E. D., Quilty, M., Blizzard, C. A., Norazit, A., Meedeniya, A. C. B., Vickers, J. C., Gai, W., et al. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.02.015 · Cited by 60
Are rodent models of Parkinson’s disease behaving as they should?
Vingill, S., Connor‐Robson, N., & Wade‐Martins, R. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.10.021 · Cited by 63
Hoban, D. B., Shrigley, S., Mattsson, B., Breger, L. S., Jarl, U., Cardoso, T., Wahlestedt, J. N., Luk, K. C., Björklund, A., & Parmar, M. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2001305117 · Cited by 63
Barbuti, P. A., Barker, R. A., Brundin, P., Przedborski, S., Papa, S. M., Kalia, L. V., & Mochizuki, H. (2021) · Movement Disorders · doi:10.1002/mds.28628 · Cited by 60
Self-citationPyszko, J., & Strosznajder, J. B. (2014) · Folia Neuropathologica · doi:10.5114/fn.2014.45567 · Cited by 59
Topography of FUS pathology distinguishes late-onset BIBD from aFTLD-U
Lee, E. B., Russ, J., Jung, H., Elman, L. B., Chahine, L. M., Kremens, D. E., Miller, B. L., Coslett, H. B., Trojanowski, J. Q., Deerlin, V. M. V., et al. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-9 · Cited by 58
Emanuele, M., & Chieregatti, E. (2015) · Biomolecules · doi:10.3390/biom5020865 · Cited by 60
The Oligomer Hypothesis in α-Synucleinopathy
Ono, K. (2017) · Neurochemical Research · doi:10.1007/s11064-017-2382-x · Cited by 58
Lipids: Key Players That Modulate α-Synuclein Toxicity and Neurodegeneration in Parkinson’s Disease
Mori, A., Imai, Y., & Hattori, N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093301 · Cited by 60
Rapid macropinocytic transfer of α-synuclein to lysosomes
Bayati, A., Banks, E., Han, C., Luo, W., Reintsch, W. E., Zorca, C. E., Shlaifer, I., Del Cid Pellitero, E., Vanderperre, B., McBride, H. M., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111102 · Cited by 57
Cerebrospinal fluid–based kinetic biomarkers of axonal transport in monitoring neurodegeneration
Fanara, P., Wong, P. A., Husted, K. H., Liu, S., Liu, V. M., Kohlstaedt, L. A., Riiff, T. J., Protasio, J., Boban, D., Killion, S., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci64575 · Cited by 57
Intermediates of α-synuclein aggregation: Implications in Parkinson's disease pathogenesis
Gadhe, L. G., Sakunthala, A., Mukherjee, S., Gahlot, N., Bera, R., Sawner, A. S., Kadu, P., & Maji, S. K. (2021) · Biophysical Chemistry · doi:10.1016/j.bpc.2021.106736 · Cited by 56
Protein Transmission, Seeding and Degradation: Key Steps for α-Synuclein Prion-Like Propagation
Oueslati, A., Ximerakis, M., & Vekrellis, K. (2014) · Experimental Neurobiology · doi:10.5607/en.2014.23.4.324 · Cited by 58
Gene therapy for Parkinson's disease: Disease modification by GDNF family of ligands
Kirik, D., Cederfjäll, E. A., Halliday, G. M., & Petersén, Å. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.09.008 · Cited by 57
Borsarelli, C. D., Falomir‐Lockhart, L. J., Ostatná, V., Fauerbach, J. A., Hsiao, H., Urlaub, H., Paleček, E., Jares-Erijman, E. A., & Jovin, T. M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.06.035 · Cited by 55
Toni, M., Massimino, M. L., Mario, A. D., Angiulli, E., & Spisni, E. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00003 · Cited by 56
α-Synuclein liquid condensates fuel fibrillar α-synuclein growth
Piroska, L., Fenyi, A., Thomas, S., Plamont, M., Redeker, V., Melki, R., & Gueroui, Z. (2023) · Science Advances · doi:10.1126/sciadv.adg5663 · Cited by 55
Self-citationLindström, V., Ihse, E., Fagerqvist, T., Bergström, J. J. E., Nordström, E. K. L., Möller, C., Lannfelt, L., & Ingelsson, M. (2014) · Immunotherapy · doi:10.2217/imt.13.162 · Cited by 56
Yedlapudi, D., Joshi, G. S., Luo, D., Todi, S. V., & Dutta, A. K. (2016) · Scientific Reports · doi:10.1038/srep38510 · Cited by 55
Socías, S. B., González‐Lizárraga, F., Ávila, C. L., Vera, C., Acuña, L., Sepulveda-Diaz, J. E., Bel, E. A. D., Raisman‐Vozari, R., & Chehín, R. N. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.12.002 · Cited by 55
Regulation of α-synuclein homeostasis and inflammasome activation by microglial autophagy
Choi, I., Heaton, G. R., Lee, Y.-K., & Yue, Z. (2022) · Science Advances · doi:10.1126/sciadv.abn1298 · Cited by 54
Peña‐Díaz, S., García‐Pardo, J., & Ventura, S. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15030839 · Cited by 54
Extracellular vesicles and their synthetic analogues in aging and age-associated brain diseases
Smith, J. A., Leonardi, T., Huang, B., Iraci, N., Vega, B., & Pluchino, S. (2014) · Biogerontology · doi:10.1007/s10522-014-9510-7 · Cited by 55
Jackson, W. S., Borkowski, A. W., Watson, N., King, O. D., Faas, H., Jasanoff, A., & Lindquist, S. L. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1312006110 · Cited by 53
Activated microglia facilitate the transmission of α-synuclein in Parkinson's disease
Zheng, T., & Zhang, Z. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105094 · Cited by 57
Prion-Like Characteristics of Polyglutamine-Containing ProteinsPreprint
Pearce, M. M. P., & Kopito, R. R. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024257 · Cited by 53
Bousset, L., Brundin, P., Böckmann, A., Meier, B., & Melki, R. (2016) · Journal of Parkinson’s Disease · doi:10.3233/jpd-150691 · Cited by 53
Self-citationBrain clearance of protein aggregates: a close-up on astrocytes
Giusti, V., Kaur, G., Giusto, E., & Civiero, L. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00703-1 · Cited by 54
Kuo, G., Kumbhar, R., Blair, W., Dawson, V. L., Dawson, T. M., & Mao, X. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00797-1 · Cited by 55
Mechanism of Anti-α-Synuclein Immunotherapy
Lee, J. S., & Lee, S. (2016) · Journal of Movement Disorders · doi:10.14802/jmd.15059 · Cited by 53
Yacoubian, T. A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802810-0.00001-5 · Cited by 56
Degeneration of dopaminergic circuitry influences depressive symptoms in Lewy body disorders
Patterson, L., Rushton, S., Attems, J., Thomas, A. J., & Morris, C. M. (2018) · Brain Pathology · doi:10.1111/bpa.12697 · Cited by 53
Linking Parkinson's Disease and Melanoma: Interplay Between α‐Synuclein and Pmel17 Amyloid Formation
Dean, D. N., & Lee, J. C. (2021) · Movement Disorders · doi:10.1002/mds.28655 · Cited by 53
Neurons and Glia Interplay in α-Synucleinopathies
Mavroeidi, P., & Xilouri, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094994 · Cited by 55
Dilna, A., Deepak, K. V., Damodaran, N., Kielkopf, C. S., Kagedal, K., Ollinger, K., & Nath, S. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2021.166246 · Cited by 51
Manganese-Induced Parkinsonism: Evidence from Epidemiological and Experimental Studies
Lucchini, R. G., & Tieu, K. (2023) · Biomolecules · doi:10.3390/biom13081190 · Cited by 53
Neuropathology in transplants in Parkinson's disease
Brundin, P., & Kordower, J. H. (2012) · Progress in brain research · doi:10.1016/b978-0-444-59575-1.00010-7 · Cited by 55
Self-citationA nanobody-based fluorescent reporter reveals human α-synuclein in the cell cytosol
Gerdes, C., Waal, N., Offner, T., Fornasiero, E. F., Wender, N., Verbarg, H., Manzini, I., Trenkwalder, C., Mollenhauer, B., Strohäker, T., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16575-0 · Cited by 52
Gut Microbiota Approach—A New Strategy to Treat Parkinson’s Disease
Liu, J., Xu, F., Nie, Z., & Shao, L. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.570658 · Cited by 52
Redeker, V., Pemberton, S., Bienvenut, W. V., Bousset, L., & Melki, R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.387530 · Cited by 51
Self-citationAggregation of amyloids in a cellular context: modelling and experiment
Friedman, R. (2011) · Biochemical Journal · doi:10.1042/bj20110369 · Cited by 50
Coordination of Copper to the Membrane-Bound Form of α-Synuclein
Dudzik, C. G., Walter, É., Abrams, B. S., Jurica, M. S., & Millhauser, G. L. (2012) · Biochemistry · doi:10.1021/bi301475q · Cited by 50
Lysines, Achilles’ heel in alpha-synuclein conversion to a deadly neuronal endotoxin
Plotegher, N., & Bubacco, L. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.12.002 · Cited by 50
Pukaß, K., Goldbaum, O., & Richter‐Landsberg, C. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13256 · Cited by 49
Multiple system atrophy: α-Synuclein strains at the neuron-oligodendrocyte crossroad
Reddy, K., & Dieriks, B. V. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00579-z · Cited by 50
Yet another polymorph of α-synuclein: solid-state sequential assignments
Gath, J., Bousset, L., Habenstein, B., Melki, R., Meier, B. H., & Böckmann, A. (2013) · Biomolecular NMR Assignments · doi:10.1007/s12104-013-9526-y · Cited by 49
Self-citationAlpha-synuclein-based models of Parkinson's disease
Dehay, B., & Fernagut, P. (2016) · Revue Neurologique · doi:10.1016/j.neurol.2016.04.003 · Cited by 55
How the shapes of seeds can influence pathology
Melki, R. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.03.011 · Cited by 50
Self-citationPukaß, K., & Richter‐Landsberg, C. (2013) · Journal of Molecular Neuroscience · doi:10.1007/s12031-013-0154-x · Cited by 48
Ko, W. K. D., & Bézard, E. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.07.020 · Cited by 48
de Oliveira, G. A. P., Marques, M. A., Cruzeiro-Silva, C., Cordeiro, Y., Schuabb, C. M. P., Moraes, A. H., Winter, R., Oschkinat, H., Foguel, D., de Freitas, M. S., et al. (2016) · Scientific Reports · doi:10.1038/srep37990 · Cited by 47
Chi, L.-M., Wang, L., & Jiao, D. (2019) · Parkinson s Disease · doi:10.1155/2019/6078251 · Cited by 47
McAllister, B. B., Lacoursiere, S. G., Sutherland, R. J., & Mohajerani, M. H. (2020) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2020.01.026 · Cited by 48
Super-resolution imaging reveals α-synuclein seeded aggregation in SH-SY5Y cells
Sang, J. C., Hidari, E., Meisl, G., Ranasinghe, R. T., Spillantini, M. G., & Klenerman, D. (2021) · Communications Biology · doi:10.1038/s42003-021-02126-w · Cited by 48
Verasdonck, J., Bousset, L., Gath, J., Melki, R., Böckmann, A., & Meier, B. H. (2015) · Biomolecular NMR Assignments · doi:10.1007/s12104-015-9628-9 · Cited by 47
Self-citationBayati, A., & McPherson, P. S. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107742 · Cited by 47
Marxreiter, F., Ettle, B., May, V. E. L., Esmer, H., Patrick, C., Kragh, C. L., Klucken, J., Winner, B., Rieß, O., Winkler, J., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.07.004 · Cited by 46
Molecular events underlying the cell‐to‐cell transmission of α‐synuclein
Choi, Y. R., Park, S., & Park, S. M. (2020) · FEBS Journal · doi:10.1111/febs.15674 · Cited by 47
Song, L.-K., Ma, K., Yuan, Y., Mu, Z., Song, X., Niu, F., Han, N., & Chen, N. (2015) · PLoS ONE · doi:10.1371/journal.pone.0131281 · Cited by 45
The neural chaperone proSAAS blocks α-synuclein fibrillation and neurotoxicity
Jarvela, T. S., Lam, H. A., Helwig, M., Lorenzen, N., Otzen, D. E., McLean, P. J., Maidment, N. T., & Lindberg, I. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1601091113 · Cited by 46
Alpha-synuclein and the prion hypothesis in Parkinson's disease
Melki, R. (2018) · Revue Neurologique · doi:10.1016/j.neurol.2018.08.002 · Cited by 52
Self-citationProtein Quality Control Pathways at the Crossroad of Synucleinopathies
de Mattos, E. P., Wentink, A. S., Nussbaum-Krammer, C. I., Hansen, C., Bergink, S., Melki, R., & Kampinga, H. H. (2020) · Journal of Parkinson s Disease · doi:10.3233/jpd-191790 · Cited by 46
Self-citationConverging Patterns of α-Synuclein Pathology in Multiple System Atrophy
Brettschneider, J., Suh, E. R., Robinson, J. L., Fang, L., Lee, E. B., Irwin, D. J., Grossman, M., Deerlin, V. M. V., Lee, V. M. ‐., & Trojanowski, J. Q. (2018) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nly080 · Cited by 45
Ghochikyan, A., Petrushina, I., Davtyan, H., Hovakimyan, A., Saing, T., Davtyan, A., Cribbs, D. H., & Agadjanyan, M. G. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.12.028 · Cited by 44
Novel animal model defines genetic contributions for neuron-to-neuron transfer of α-synuclein
Tyson, T., Senchuk, M. M., Cooper, J. F., George, S., Raamsdonk, J. M. V., & Brundin, P. (2017) · Scientific Reports · doi:10.1038/s41598-017-07383-6 · Cited by 45
Self-citationRole of Ser129 phosphorylation of α-synuclein in melanoma cells
Lee, B. R., Matsuo, Y., Cashikar, A. G., & Kamitani, T. (2012) · Journal of Cell Science · doi:10.1242/jcs.122093 · Cited by 43
Pradhan, S., & Andreasson, K. I. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.12.008 · Cited by 43
Parkinson's disease, proteins, and prions: Milestones
Olanow, C. W., & McNaught, K. S. P. (2011) · Movement Disorders · doi:10.1002/mds.23767 · Cited by 43
Jia, C., Ma, X., Liu, Z., Gu, J., Zhang, X., Li, D., & Zhang, S. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01124 · Cited by 43
Biomarkers of Parkinson's disease and Dementia with Lewy bodies
Henchcliffe, C., Dodel, R. C., & Beal, M. F. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.09.002 · Cited by 42
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
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