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
Cited by
Sorted by citations
Items 201–300 of 834
α‐Synuclein: The Long Distance Runner
George, S., Rey, N. L., Reichenbach, N., Steiner, J. A., & Brundin, P. (2013) · Brain Pathology · doi:10.1111/bpa.12046 · Cited by 114
Self-citationAlpha-Synuclein Targeting Therapeutics for Parkinson's Disease and Related Synucleinopathies
Menon, S. A., Armstrong, S. E. M., Hamzeh, A. M., Visanji, N. P., Sardi, S. P., & Tandon, A. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.852003 · Cited by 108
Dysregulation of autophagy and mitochondrial function in Parkinson’s disease
Wang, B., Abraham, N. A., Gao, G., & Yang, Q. (2016) · Translational Neurodegeneration · doi:10.1186/s40035-016-0065-1 · Cited by 112
The prion-like spreading of α-synuclein: From in vitro to in vivo models of Parkinson’s disease
Vargas, J., Grudina, C., & Zurzolo, C. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.01.012 · Cited by 112
Prions and the Potential Transmissibility of Protein Misfolding Diseases
Kraus, A., Groveman, B. R., & Caughey, B. W. (2013) · Annual Review of Microbiology · doi:10.1146/annurev-micro-092412-155735 · Cited by 107
The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation
Aprile, F. A., Källstig, E., Limorenko, G., Vendruscolo, M., Ron, D., & Hansen, C. (2017) · Scientific Reports · doi:10.1038/s41598-017-08324-z · Cited by 105
Self-citationCan Parkinson's disease pathology be propagated from one neuron to another?
Dunning, C. J. R., Reyes, J. F., Steiner, J. A., & Brundin, P. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.11.003 · Cited by 111
Self-citationA Nigro−Vagal Pathway Controls Gastric Motility and Is Affected in a Rat Model of Parkinsonism
Anselmi, L., Toti, L., Bove, C., Hampton, J., & Travagli, R. A. (2017) · Gastroenterology · doi:10.1053/j.gastro.2017.08.069 · Cited by 105
Activity‐dependent secretion of alpha‐synuclein by enteric neurons
Paillusson, S., Clairembault, T., Biraud, M., Neunlist, M., & Derkinderen, P. (2012) · Journal of Neurochemistry · doi:10.1111/jnc.12131 · Cited by 108
Deubiquitinating enzymes (DUBs): decipher underlying basis of neurodegenerative diseases
Liu, B., Ruan, J., Chen, M., Li, Z., Manjengwa, G. M., Schlüter, D., Song, W., & Wang, X. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01233-8 · Cited by 107
Sorting out release, uptake and processing of alpha‐synuclein during prion‐like spread of pathology
Tyson, T., Steiner, J. A., & Brundin, P. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13449 · Cited by 110
Self-citationα-Synuclein: Multiple System Atrophy PrionsPreprint
Woerman, A. L., Watts, J. C., Aoyagi, A., Giles, K., Middleton, L. T., & Prusiner, S. B. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024588 · Cited by 104
The remarkable conformational plasticity of alpha-synuclein: blessing or curse?
Deleersnijder, A., Gérard, M., Debyser, Z., & Baekelandt, V. (2013) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2013.04.002 · Cited by 104
Doorn, K. J., Goudriaan, A., Blits‐Huizinga, C. T., Bol, J. G. J. M., Rozemüller, A. J. M., Hoogland, P. V. J. M., Lucassen, P. J., Drukarch, B., van de Berg, W. D. J., & van Dam, A. (2013) · Brain Pathology · doi:10.1111/bpa.12088 · Cited by 104
Loss of Functional Alpha-Synuclein: A Toxic Event in Parkinson's Disease?
Kanaan, N. M., & Manfredsson, F. P. (2012) · Journal of Parkinson s Disease · doi:10.3233/jpd-012138 · Cited by 104
Emerging roles of microglial activation and non-motor symptoms in Parkinson's disease
Doorn, K. J., Lucassen, P. J., Boddeke, H. W. G. M., Prins, M., Berendse, H. W., Drukarch, B., & van Dam, A. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.06.005 · Cited by 98
Nitrosative stress in Parkinson’s disease
Stykel, M. G., & Ryan, S. D. (2022) · npj Parkinson s Disease · doi:10.1038/s41531-022-00370-3 · Cited by 98
New insights into cellular α-synuclein homeostasis in health and disease
Dettmer, U., Selkoe, D. J., & Bartels, T. (2015) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2015.07.007 · Cited by 97
Prion-like propagation of pathology in Parkinson disease
Volpicelli‐Daley, L. A., & Brundin, P. (2018) · Handbook of clinical neurology · doi:10.1016/b978-0-444-63945-5.00017-9 · Cited by 103
Self-citationSmethurst, P., Sidle, K. C. L., & Hardy, J. (2014) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12206 · Cited by 99
Shrivastava, A. N., Aperia, A. C., Melki, R., & Triller, A. (2017) · Neuron · doi:10.1016/j.neuron.2017.05.026 · Cited by 96
Self-citationSecretion and Uptake of α-Synuclein Via Extracellular Vesicles in Cultured Cells
Gustafsson, G., Lööv, C., Persson, E., Lázaro, D. F., Takeda, S., Bergström, J. J. E., Erlandsson, A., Sehlin, D., Balaj, L., György, B., et al. (2018) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-018-0622-5 · Cited by 101
Self-citationQu, J. T., Ren, X., Xue, F., He, Y., Zhang, R., Zheng, Y., Huang, H., Wang, W., & Zhang, J. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.03.010 · Cited by 95
α-Synuclein and Lewy pathology in Parkinson's disease
Kalia, L. V., & Kalia, S. K. (2015) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000215 · Cited by 93
Multiple System Atrophy: Recent Developments and Future Perspectives
Meissner, W. G., Fernagut, P., Dehay, B., Péran, P., Traon, A. P., Foubert‐Samier, A., Cuina, M. L., Bézard, E., Tison, F., & Rascol, O. (2019) · Movement Disorders · doi:10.1002/mds.27894 · Cited by 96
Stem Cell-Based Therapies for Parkinson Disease
Liu, Z., & Cheung, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218060 · Cited by 98
Ugalde, C. L., Finkelstein, D. I., Lawson, V. A., & Hill, A. F. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13772 · Cited by 92
Neuron-to-neuron α-synuclein propagation in vivo is independent of neuronal injury
Ulusoy, A., Musgrove, R. E., Rusconi, R., Klinkenberg, M., Helwig, M., Schneider, A., & Monte, D. A. D. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0198-y · Cited by 91
Pathogenesis of α-Synuclein in Parkinson’s Disease: From a Neuron-Glia Crosstalk Perspective
Yi, S., Wang, L., Wang, H., Ho, M. S.-C., & Zhang, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314753 · Cited by 96
Visualization of cell-to-cell transmission of mutant huntingtin oligomers
Herrera, F., Tenreiro, S., Miller‐Fleming, L., & Outeiro, T. F. (2011) · PLoS Currents · doi:10.1371/currents.rrn1210 · Cited by 94
Self-citationKisos, H., Pukaß, K., Ben‐Hur, T., Richter‐Landsberg, C., & Sharon, R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046817 · Cited by 91
Development of P assive I mmunotherapies for S ynucleinopathies
Bergström, A., Kallunki, P., & Fog, K. (2015) · Movement Disorders · doi:10.1002/mds.26481 · Cited by 91
Self-citationSpencer, B. J., Valera, E., Rockenstein, E. M., Overk, C., Mante, M., Adame, A., Zago, W. M., Seubert, P. A., Barbour, R., Schenk, D., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0410-8 · Cited by 91
RetractedUnderstanding the pathogenesis of multiple system atrophy: state of the art and future perspectives
Compagnoni, G. M., & Fonzo, A. D. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0730-6 · Cited by 93
Manzanza, N. D. O., Sedlackova, L., & Kalaria, R. N. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.690293 · Cited by 98
Transmission of Systemic AA Amyloidosis in Animals
Murakami, T., Ishiguro, N., & Higuchi, K. (2013) · Veterinary Pathology · doi:10.1177/0300985813511128 · Cited by 89
ɑ‐Synuclein strains and the variable pathologies of synucleinopathies
Peelaerts, W., & Baekelandt, V. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13595 · Cited by 96
Chen, Y., Dolt, K. S., Kriek, M., BAKER, T. S., Downey, P. M., Drummond, N. J., Canham, M. A., Natalwala, A., Rosser, S. J., & Kunath, T. (2018) · European Journal of Neuroscience · doi:10.1111/ejn.14286 · Cited by 92
Villar‐Piqué, A., da Fonseca, T. L., Sant’Anna, R., Szegő, É. M., Fonseca‐Ornelas, L., Pinho, R., Čarija, A., Gerhardt, E., Masaracchia, C., Gonzalez, E. A., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1606791113 · Cited by 88
Self-citationPagano, G., Boess, F., Taylor, K. I., Ricci, B., Mollenhauer, B., Poewe, W. H., Boulay, A., Anzures‐Cabrera, J., Vogt, A., Marchesi, M., et al. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.705407 · Cited by 90
Limelight on Alpha-Synuclein: Pathological and Mechanistic Implications in Neurodegeneration
Wales, P., Pinho, R., Lázaro, D. F., & Outeiro, T. F. (2013) · Journal of Parkinson s Disease · doi:10.3233/jpd-130216 · Cited by 89
Self-citationα-Synuclein-carrying extracellular vesicles in Parkinson’s disease: deadly transmitters
Chistiakov, D. A., & Chistiakov, A. A. (2016) · Acta Neurologica Belgica · doi:10.1007/s13760-016-0679-1 · Cited by 87
Interaction between Parkin and α-Synuclein in PARK2-Mediated Parkinson’s Disease
Madsen, D. A., Schmidt, S. I., Blaabjerg, M., & Meyer, M. (2021) · Cells · doi:10.3390/cells10020283 · Cited by 85
Exosomes-associated neurodegeneration and progression of Parkinson's disease.
Russo, I., Bubacco, L., & Greggio, E. (2012) · Europe PMC (PubMed Central) · Cited by 85
Calcium dysregulation contributes to neurodegeneration in FTLD patient iPSC-derived neurons
Imamura, K., Sahara, N., Kanaan, N. M., Tsukita, K., Kondo, T., Kutoku, Y., Ohsawa, Y., Sunada, Y., Kawakami, K., Hotta, A., et al. (2016) · Scientific Reports · doi:10.1038/srep34904 · Cited by 88
Evidence of distinct α-synuclein strains underlying disease heterogeneity
Holec, S. A. M., & Woerman, A. L. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02163-5 · Cited by 91
LRRK2 and α-Synuclein: Distinct or Synergistic Players in Parkinson’s Disease?
O’Hara, D. M., Pawar, G. N., Kalia, S. K., & Kalia, L. V. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00577 · Cited by 89
α-Synuclein impairs oligodendrocyte progenitor maturation in multiple system atrophy
May, V. E. L., Ettle, B., Poehler, A.-M., Nuber, S., Ubhi, K. K., Rockenstein, E. M., Winner, B., Wegner, M., Masliah, E., & Winkler, J. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.02.028 · Cited by 85
A cell culture model for monitoring α-synuclein cell-to-cell transfer
Reyes, J. F., Olsson, T. T., Lamberts, J. T., Devine, M. J., Kunath, T., & Brundin, P. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.07.003 · Cited by 89
Self-citationMolecular Insights into Parkinson's Disease
Rochet, J., Hay, B. A., & Guo, M. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00011-4 · Cited by 87
Ghrelin is neuroprotective in Parkinson’s disease: molecular mechanisms of metabolic neuroprotection
Bayliss, J. A., & Andrews, Z. B. (2013) · Therapeutic Advances in Endocrinology and Metabolism · doi:10.1177/2042018813479645 · Cited by 86
Oh, S. H., Kim, H., Park, H. J., Shin, J. Y., Bae, E.-J., Sunwoo, M. K., Lee, S., & Lee, P. H. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.075 · Cited by 85
Beyond α-synuclein transfer: pathology propagation in Parkinson's disease
Hansen, C., & Li, J. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.03.002 · Cited by 85
Self-citationChutna, O., Gonçalves, S. A., Villar‐Piqué, A., Guerreiro, P. S., Marijanovic, Z., Mendes, T., Ramalho, J. S., Emmanouilidou, E., Ventura, S., Klucken, J., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu391 · Cited by 82
Self-citationLysosomes and α-synuclein form a dangerous duet leading to neuronal cell death
Bourdenx, M., Bézard, E., & Dehay, B. (2014) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2014.00083 · Cited by 88
γ-Synuclein: Seeding of α-Synuclein Aggregation and Transmission between Cells
Surgucheva, I. G., Sharov, V. S., & Surguchov, A. P. (2012) · Biochemistry · doi:10.1021/bi300478w · Cited by 86
The Contribution of α -Synuclein Spreading to Parkinson’s Disease Synaptopathy
Longhena, F., Faustini, G., Missale, C., Pizzi, M., Spano, P., & Bellucci, A. (2017) · Neural Plasticity · doi:10.1155/2017/5012129 · Cited by 82
Xhima, K., Nabbouh, F., Hynynen, K., Aubert, I., & Tandon, A. (2018) · Movement Disorders · doi:10.1002/mds.101 · Cited by 86
Studying neurodegenerative diseases in culture models
Schlachetzki, J. C. M., Saliba, S. W., & de Oliveira, A. C. P. (2013) · Brazilian Journal of Psychiatry · doi:10.1590/1516-4446-2013-1159 · Cited by 85
Gonçalves, S. A., Macedo, D., Raquel, H., Simões, P. D., Giorgini, F., Ramalho, J. S., Barral, D. C., Moita, L. F., & Outeiro, T. F. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1005995 · Cited by 81
Self-citationInterneurons, tau and amyloid-β in the piriform cortex in Alzheimer’s disease
Saiz-Sanchez, D., De la Rosa-Prieto, C., Ubeda-Banon, I., & Martinez-Marcos, A. (2015) · Brain Structure and Function · doi:10.1007/s00429-014-0771-3 · Cited by 79
Cellular mechanisms of protein aggregate propagation
Holmes, B. B., & Diamond, M. I. (2012) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32835a3ee0 · Cited by 80
Targeting α-Synuclein for PD Therapeutics: A Pursuit on All Fronts
Teil, M., Arotçarena, M.-L., Faggiani, E., Laferrière, F., Bézard, E., & Dehay, B. (2020) · Biomolecules · doi:10.3390/biom10030391 · Cited by 80
Valera, E., Ubhi, K. K., Mante, M., Rockenstein, E. M., & Masliah, E. (2013) · Glia · doi:10.1002/glia.22610 · Cited by 79
Alpha-Synuclein as a Prominent Actor in the Inflammatory Synaptopathy of Parkinson’s Disease
Cardinale, A., Calabrese, V., de Iure, A., & Picconi, B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126517 · Cited by 79
Proteolytic Cleavage of Extracellular α-Synuclein by Plasmin
Kim, K. S., Choi, Y. R., Park, J. Y., Lee, J.-H., Kim, D. K., Lee, S., Paik, S. R., Jou, I., & Park, S. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.348128 · Cited by 81
GABA transmission via ATP-dependent K + channels regulates α-synuclein secretion in mouse striatum
Emmanouilidou, E., Minakaki, G., Keramioti, M. V., Xylaki, M., Balafas, E., Chrysanthou‐Piterou, M., Kloukina, I., & Vekrellis, K. (2016) · Brain · doi:10.1093/brain/awv403 · Cited by 77
Nanomechanical properties of distinct fibrillar polymorphs of the protein α-synuclein
Makky, A., Bousset, L., Polesel‐Maris, J., & Melki, R. (2016) · Scientific Reports · doi:10.1038/srep37970 · Cited by 79
Self-citationDeveloping dopaminergic cell therapy for Parkinson's disease—give up or move forward?
Lindvall, O. (2013) · Movement Disorders · doi:10.1002/mds.25378 · Cited by 78
Selective neuronal vulnerability in Parkinson's disease
González‐Rodríguez, P., Zampese, E., & Surmeier, D. J. (2020) · Progress in brain research · doi:10.1016/bs.pbr.2020.02.005 · Cited by 80
Release and uptake of pathologic alpha-synuclein
Grozdanov, V., & Danzer, K. M. (2018) · Cell and Tissue Research · doi:10.1007/s00441-017-2775-9 · Cited by 75
Review: The future of cell therapies and brain repair: P arkinson's disease leads the way
Petit, G. H., Olsson, T. T., & Brundin, P. (2013) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12110 · Cited by 74
Self-citationSardi, S. P., Cheng, S. H., & Shihabuddin, L. S. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2014.12.001 · Cited by 75
Differential Membrane Binding and Seeding of Distinct α-Synuclein Fibrillar Polymorphs
Shrivastava, A. N., Bousset, L., Renner, M. L., Redeker, V., Savistchenko, J., Triller, A., & Melki, R. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.01.022 · Cited by 79
Self-citationChen, K., Wang, H., Ilyas, I., Mahmood, A., & Hou, L. (2023) · Brain Sciences · doi:10.3390/brainsci13040634 · Cited by 82
Lamberts, J. T., Hildebrandt, E. N., & Brundin, P. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.07.002 · Cited by 75
Self-citationCan infections trigger alpha-synucleinopathies?
Tulisiak, C. T., Mercado, G., Peelaerts, W., Brundin, L., & Brundin, P. (2019) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2019.06.002 · Cited by 76
Self-citationMechanisms of alpha-synuclein toxicity: An update and outlook
Brás, I. C., Xylaki, M., & Outeiro, T. F. (2019) · Progress in brain research · doi:10.1016/bs.pbr.2019.10.005 · Cited by 78
Self-citationIn vivo models of alpha-synuclein transmission and propagation
Recasens, A., Ulusoy, A., Kahle, P. J., Monte, D. A. D., & Dehay, B. (2017) · Cell and Tissue Research · doi:10.1007/s00441-017-2730-9 · Cited by 77
Prion-like seeding and nucleation of intracellular amyloid-β
Olsson, T. T., Klementieva, O. L., & Gouras, G. K. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.01.015 · Cited by 74
Corruption and Spread of Pathogenic Proteins in Neurodegenerative Diseases
Walker, L. C., & LeVine, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.399378 · Cited by 75
How strong is the evidence that Parkinson's disease is a prion disorder?
Brundin, P., Ma, J., & Kordower, J. H. (2016) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000349 · Cited by 76
Self-citationAngarica, V. E., Ventura, S., & Sancho, J. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-316 · Cited by 74
High-Throughput Screening Methodology to Identify Alpha-Synuclein Aggregation Inhibitors
Pujols, J., Peña‐Díaz, S., Conde-Giménez, M., Pinheiro, F., Navarro, S., Sancho, J., & Ventura, S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18030478 · Cited by 70
Cremades, N., & Dobson, C. M. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.07.009 · Cited by 72
Found in Translation: The Utility of C. elegans Alpha-Synuclein Models of Parkinson’s Disease
Gaeta, A. L., Caldwell, K. A., & Caldwell, G. A. (2019) · Brain Sciences · doi:10.3390/brainsci9040073 · Cited by 75
Stevenson, T. J., Murray, H. C., Turner, C. P., Faull, R. L. M., Dieriks, B. V., & Curtis, M. A. (2020) · Scientific Reports · doi:10.1038/s41598-020-63412-x · Cited by 70
Kumar, S. T., Donzelli, S., Chiki, A., Syed, M. M. K., & Lashuel, H. A. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.14955 · Cited by 69
Antibodies against Alpha-Synuclein Reduce Oligomerization in Living Cells
Näsström, T., Gonçalves, S. A., Sahlin, C., Nordström, E. K. L., Sundquist, V. S., Lannfelt, L., Bergström, J. J. E., Outeiro, T. F., & Ingelsson, M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027230 · Cited by 70
Self-citationHansen, C., Björklund, T., Petit, G. H., Lundblad, M., Nielsen, R. M., Brundin, P., & Li, J. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.04.017 · Cited by 69
Self-citationGoldberg, N. R. S., Caesar, J., Park, A., Sedgh, S., Finogenov, G., Masliah, E., Davis, J. L., & Blurton-Jones, M. M. (2015) · Stem Cell Reports · doi:10.1016/j.stemcr.2015.09.008 · Cited by 69
The Role of Glia in Alpha-Synucleinopathies
Fellner, L., & Stefanova, N. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8340-3 · Cited by 69
14-3-3 Proteins Reduce Cell-to-Cell Transfer and Propagation of Pathogenic α-Synuclein
Wang, B., Underwood, R., Kamath, A., Britain, C. M., McFerrin, M. B., McLean, P. J., Volpicelli‐Daley, L. A., Whitaker, R. H., Placzek, W. J., Becker, K., et al. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1134-18.2018 · Cited by 69
Regulation of neuronal autophagy and the implications in neurodegenerative diseases
Cai, Q., & Ganesan, D. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105582 · Cited by 70
The Hidden Cell-to-Cell Trail of α-Synuclein Aggregates
Neupane, S., Cecco, E. D., & Aguzzi, A. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167930 · Cited by 69
Solid-state NMR sequential assignments of α-synuclein
Gath, J., Habenstein, B., Bousset, L., Melki, R., Meier, B. H., & Böckmann, A. (2011) · Biomolecular NMR Assignments · doi:10.1007/s12104-011-9324-3 · Cited by 67
Self-citationVekrellis, K., & Stefanis, L. (2012) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2012.674111 · Cited by 68
Exogenous -Synuclein Decreases Raft Partitioning of Cav2.2 Channels Inducing Dopamine Release
Ronzitti, G., Bucci, G., Emanuele, M., Leo, D., Sotnikova, T. D., Mus, L., Soubrane, C., Dallas, M. L., Thalhammer, A., Cingolani, L. A., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.0608-14.2014 · Cited by 68
Cellular models as tools for the study of the role of alpha-synuclein in Parkinson's disease
Lázaro, D. F., Pavlou, M. A. S., & Outeiro, T. F. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.05.007 · Cited by 70
Self-citationCisbani, G., Maxan, A., Kordower, J. H., Planel, E., Freeman, T. B., & Cicchetti, F. (2017) · Brain · doi:10.1093/brain/awx255 · Cited by 67
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
