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 701–800 of 834
Perspective Chapter: Exosomes – The Surreptitious Intercellular Messengers in the Body
Soni, N., Jangra, J., Chaudhary, M., Nandi, G., & Bissa, B. (2023) · Physiology · doi:10.5772/intechopen.110779 · Cited by 2
Role of the Gut Microbiome and Bacterial Amyloids in the Development of Synucleinopathies
Trubitsina, N. P., Matiiv, A. B., Rogoza, T. M., Zudilova, A. A., Bezgina, M. D., Zhouravleva, G. A., & Bondarev, S. A. (2024) · Biochemistry (Moscow) · doi:10.1134/s0006297924030118 · Cited by 2
Biomarkers of Parkinson’s disease
Jin, H., Kanthasamy, A., Anantharam, V., & Kanthasamy, A. G. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-404630-6.00049-x · Cited by 2
Breid, S., Bernis, M. E., Babila, J. T., Garza, M. C., Wille, H., & Tamgüney, G. (2017) · Journal of Visualized Experiments · doi:10.3791/55503 · Cited by 2
Bentea, L., Ölveczky, P. C., & Bentea, E. (2014) · NORA - Norwegian Open Research Archives · Cited by 2
Is There Still Hope After Prions Have Spread Within the Brain?
Carnaud, C. (2011) · The Journal of Infectious Diseases · doi:10.1093/infdis/jir487 · Cited by 2
Investigating reach and grasp in Parkinson's disease cognitive impairment
Cosgrove, J. (2016) · Repository@Hull (Worktribe) (University of Hull) · Cited by 2
Malattie da prioni o encefalopatie spongiformi trasmissibili
Brandel, J., & Haı̈k, S. (2016) · EMC - Neurologia · doi:10.1016/s1634-7072(16)77562-3 · Cited by 1
Repairing the Aged Parkinsonian Striatum: Lessons from the Lab and Clinic
Mercado, N. M., & Collier, T. J. (2016) · Journal of Clinical & Cellular Immunology · doi:10.4172/2155-9899.1000476 · Cited by 1
Bioluminescence Imaging of Neuroinflammation in a Mouse Model of Parkinson’s Disease
Bernis, M. E., & Tamgüney, G. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9940-8_10 · Cited by 1
Cell Therapy for Neurodegenerative Disorders
Singeç, I. (2012) · Humana Press eBooks · doi:10.1007/978-1-62703-098-4_1 · Cited by 1
Chen, L., Yang, J., Xu, G., & Wu, Y. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3346-5_22 · Cited by 1
Pluripotent Stem Cell-Derived Dopaminergic Neurons As Models of Neurodegeneration
Watmuff, B., Hartley, B. J., Hunt, C. P. J., Pouton, C. W., & Haynes, J. M. (2013) · Future Neurology · doi:10.2217/fnl.13.50 · Cited by 1
Autophagy and Proteostasis: A Unifying Theory of Neurodegenerative Disease
Novack, J. P. (2017) · Journal of Restorative Medicine · doi:10.14200/jrm.2017.6.0102 · Cited by 1
Preclinical models based on endogenous neurotoxins
Segura‐Aguilar, J. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822120-4.00011-3 · Cited by 1
Muñoz, A. R., Fernández-Pérez, E. J., Olivos, N., Burgos, C. F., Boopathi, S., Armijo‐Weingart, L., Pacheco, C. R., González, W., & Aguayo, L. G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413253 · Cited by 1
Corradini, B. R. (2013) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.5.2013.tde-01082013-135108 · Cited by 1
Tsang, E. W. K. (2012) · TSpace (University of Toronto) · Cited by 1
Conformational changes and the self-assembly of alpha-synuclein
Mason, R. J. A. (2018) · Sheffield Hallam University · doi:10.7190/shu-thesis-00151 · Cited by 1
Enfermedad de Parkinson: Modificaciones oxidativas y su rol en la toxicidad de α-sinucleína
Giménez, E. (2022) · El Servicio de Difusión de la Creación Intelectual (National University of La Plata) · doi:10.35537/10915/138140 · Cited by 1
Prescott, E. E., Wei, J., Garland, E. F., Urbanek, A. N., Capriglia, F., Molenkamp, W. H., Rhodes, D. P., Heywood, L. D., Schwartzentruber, A., Stephen, E., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.17.676873 · Cited by 1
Yadav, A., Vacchi, E., Pinton, S., Lazzarini, E., Pecoraro, M., Raimondi, A., Barile, L., Kaelin‐Lang, A., & Melli, G. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.10.709299 · Cited by 1
Rôle des sphingolipides dans la cancérogenèse : l'exemple de la maladie de Gaucher
Astudillo, L. M. (2016) · theses.fr (ABES) · doi:10.70675/fa7a5078z1170z48a0z81a7z05c9d8e7a135 · Cited by 1
Effects of Alpha-Synuclein on Cellular Homeostasis
Vekrellis, K., Minakaki, G., & Emmanouilidou, E. (2011) · InTech eBooks · doi:10.5772/17637
Effects of Aggregated Alpha-Synuclein on Cultured Neuronal Cells
Freeman, D. W. (2015) · Loyola eCommons (Loyola University of Chicago)
Herrera, F., Gonçalves, S. A., Branco‐Santos, J., & Outeiro, T. F. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-394431-3.00012-2
Self-citationParkinson’s Disease and Stem Cells
Mochizuki, H., & Yasuda, T. (2012) · Springer eBooks · doi:10.1007/978-94-007-2993-3_35
Accumulating Evidence Suggests that Parkinson’s Disease Is a Prion-Like Disorder
Rey, N. L., Angot, É., Dunning, C. J. R., Steiner, J. A., & Brundin, P. (2013) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-35491-5_8
Self-citationImmunothérapie des maladies neurodégénératives: le temps est-il venu de changer de paradigme ?
Bachy, V. S., & Carnaud, C. (2011) · Bulletin de l Académie vétérinaire de France · doi:10.4267/2042/48075
Savolainen, M. H. (2015) · Työväentutkimus Vuosikirja
Utilizing Galectin 3 as a Marker of Ruptured Vesicles In Vivo
London, J. (2015) · Loyola eCommons (Loyola University of Chicago)
Role of Aberrant α-Synuclein–Membrane Interactions in Parkinson’s Disease
Griggs, A. M., Ysselstein, D., & Rochet, J. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-394431-3.00039-0
The role of alpha-synuclein phosphorylation in synucleinopathies
Basso, E. (2014) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
Extracellular vesicle release of α-Synuclein is mediated by SUMOylation
Kunadt, M. (2015) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-5371
Derkinderen, P., & Damier, P. (2015) · Elsevier eBooks · doi:10.1016/b978-2-294-74232-3.00003-9
Propagation and Replication of Misfolded SOD1: Implications for Amyotrophic Lateral Sclerosis
Bertolotti, A. (2013) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-35491-5_9
Extracellular α-Synuclein as a Target for Immunotherapy
Lee, J. S., & Lee, S. (2016) · Methods in pharmacology and toxicology · doi:10.1007/978-1-4939-3560-4_6
Renganathan, S. D. S., & Dushyaanthan, S. (2015) · TSpace (University of Toronto)
Pathogenic mechanisms in multiple system atrophy: a study of oligodendroglial pathology
Asi, Y. T. (2014) · UCL Discovery (University College London)
Alpha-synuclein expression influences the processing of the amyloid precursor protein
Hall‐Roberts, H. (2016) · The University of Bath Online Publications Store (The University of Bath)
Neural Substrates of Parkinson's Disease
Koshimori, Y. (2016) · TSpace (University of Toronto)
Basu, S. (2017) · Journal of International Crisis and Risk Communication Research
On a population dynamic model of active cells with direct interaction
Noussair, A. (2017) · Mathematical Modelling of Natural Phenomena · doi:10.1051/mmnp/2017077
Pathophysiological Roles of Brain Aquaporins in Parkinson’s Disease and Aging
Stahl, K. (2018) · NORA - Norwegian Open Research Archives
Defining the Role of Alpha-Synuclein in Enteric Dysfunction in Parkinsons Disease
Manfredsson, F. P. (2017)
Development and characterization of cell models of tau aggregation
Cavallini, A. (2018) · UCL Discovery (University College London)
IDENTIFICATION OF NOVEL SUBSTRATES OF LRRK2, A PARKINSON’S DISEASE ASSOCIATED KINASE
Lee, C. H. (2014) · OhioLink ETD Center (Ohio Library and Information Network)
Bäckström, D. C. (2019) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Sequence-Specific Extracellular MicroRNAs Activate TLR7
Wu, N. (2018) · DigitalCommons@UNMC
Parkinson's Disease Animal Models
Saxena, M. T. (2013) · Materials and Methods · doi:10.13070/mm.en.3.2843
Les protéinopathies infectieuses de Parkinson et d’Alzheimer
Melki, R. (2020) · Bulletin de l Académie Nationale de Médecine · doi:10.1016/j.banm.2019.12.019
Self-citationA toxic subset of soluble α-synuclein species in dementia with Lewy body
Castillo‐Carranza, D. L. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa016
Membrane Interaction of α-Synuclein in Different Aggregation States
Grey, M., Linse, S. S., Brundin, P., & Sparr, E. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2011.11.458
Self-citationDysbiosis Of The Gut Microbiome Associated With Parkinson’s Disease Pathophysiology
Mierau, P. C. (2019) · UA Campus Repository (The University of Arizona)
Studies on the Etiology of Parkinson's disease
Fardell, C. (2020) · Gothenburg University Publications Electronic Archive (Gothenburg University)
Alpha-synuclein as a regulator of synaptic signalling
Pelkonen, A. (2013) · UEF eRepo (University of Eastern Finland)
Biochemical Analysis of Strains of α-Synuclein Aggregates
Lau, A. (2018) · TSpace (University of Toronto)
Alpha-synuclein spreading mechanisms in Parkinson's disease: The role of membrane receptors
Brás, I. C., & Outeiro, T. F. (2021) · International review of movement disorders · doi:10.1016/bs.irmvd.2021.08.002
Self-citationBeckerman, M. (2015) · Biological and medical physics, biomedical engineering · doi:10.1007/978-3-319-22117-5_9
Biomarkers of Parkinson's Disease
Jin, H., Kanthasamy, A., Anantharam, V., & Kanthasamy, A. G. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814655-2.00050-5 · Cited by 1
Petersen, R. B. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734510478.793555621
Panoply of plant extracts in the treatment of prion diseases
Obulesu, M. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-95762-5.00002-3
Smimih, K., Azzouhri, C., Saad, F. E.-Z., Hamdan, Y. A., Laadraoui, J., Zouhairi, N., & Merzouki, M. (2023) · Advances in bioinformatics and biomedical engineering book series · doi:10.4018/978-1-6684-9675-6.ch005
Role of the Gut Microbiome and Bacterial Amyloids in the Development of Synucleinopathies (Review)
Trubitsina, N. P., Matiiv, A. B., Rogoza, T. M., Zudilova, A. A., Bezgina, M. D., Zhouravleva, G. A., & Bondarev, S. A. (2024) · Biochemistry (Moscow) · doi:10.31857/s0320972524030089
Pathophysiological Basis of Neurodegeneration in Parkinson’s Disease
Galindo, L. S. M., González‐Escamilla, G., & Groppa, S. (2024) · Neuromethods · doi:10.1007/978-1-0716-4083-8_1
The beta-sitosterol beta-D-glucoside (BSSG) rat model of Parkinson's disease
Soliman, R. I., Sultan, N. S., Lokman, H. M., Elkaramany, Y., Ibraheem, S. M., & Helmy, H. I. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-16128-5.00011-6
Magill, P. J., Schaffran, B., Wolff, A. R., Threlfell, S., Doig, N. M., Dinneen, D., Yona, G., Sharott, A., Luc, K. C., Cragg, S. J., et al. (2025) · Research Square · doi:10.21203/rs.3.rs-5931393/v1
Mao, H., Kuang, Y., Wang, Z., Lin, H., Dai, W., Lin, H., Gan, T., He, Z., Zou, W.-Q., Ma, C., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.26.645411
Liu, M., Zhu, J., Han, S., Zhu, S.-J., & Yang, D. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05014-0
Tullo, S., Park, J., Rahayel, S., Gallino, D., Park, M., Mar, K., Zheng, Y., del Cid‐Pellitero, E., Fon, E. A., Luo, W., et al. (2025) · eLife · doi:10.1101/2025.07.18.665565 · Cited by 1
Singh, K. V., Nimmagadda, S., Panda, A., Rarigela, R., Patel, T. J., Gopathoti, S., Patel, P. V., Parmar, M. P., & Mohammed, S. (2025) · Clinical Case Reports · doi:10.1002/ccr3.71529
., A., & Singh, K. P. (2025) · International Journal For Multidisciplinary Research · doi:10.36948/ijfmr.2025.v07i06.62469
Liu, Y., Kalpana, S., Baride, A., Romanova, S., Callegari, E., Huber, C. C., Wang, X., & Wang, H. (2021) · Figshare · doi:10.6084/m9.figshare.13620103
Liu, Y., Kalpana, S., Baride, A., Romanova, S., Callegari, E., Huber, C. C., Wang, X., & Wang, H. (2021) · Figshare · doi:10.6084/m9.figshare.13620088
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) · Figshare · doi:10.6084/m9.figshare.12891207
Liu, Y., Kalpana, S., Baride, A., Romanova, S., Callegari, E., Huber, C. C., Wang, X., & Wang, H. (2021) · Figshare · doi:10.6084/m9.figshare.13620100
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) · Figshare · doi:10.6084/m9.figshare.12891198
Liu, D., Guo, J.-J., Su, J.-H., Svanbergsson, A., Yuan, L., Haikal, C., Li, W., Gouras, G. K., & Li, J. (2021) · Figshare · doi:10.6084/m9.figshare.14813704
Self-citationLiu, X., Wang, Q., Yang, Y., Stewart, T., Shi, M., Soltys, D., Liu, G., Thorland, E., Cilento, E. M., Hou, Y., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14183759
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) · Figshare · doi:10.6084/m9.figshare.12891210
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) · Figshare · doi:10.6084/m9.figshare.12891222
Liu, Y., Kalpana, S., Baride, A., Romanova, S., Callegari, E., Huber, C. C., Wang, X., & Wang, H. (2021) · Figshare · doi:10.6084/m9.figshare.13620094
Additional file 1 of LRP1 is a neuronal receptor for α-synuclein uptake and spread
Chen, K., Martens, Y. A., Meneses, A. D., Ryu, D. H., Lü, W., Raulin, A. C., Li, F., Zhao, J., Chen, Y., Jin, Y., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20861097
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) · Figshare · doi:10.6084/m9.figshare.12891225
Liu, Y., Kalpana, S., Baride, A., Romanova, S., Callegari, E., Huber, C. C., Wang, X., & Wang, H. (2021) · Figshare · doi:10.6084/m9.figshare.13620082
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) · Figshare · doi:10.6084/m9.figshare.12891219
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) · Figshare · doi:10.6084/m9.figshare.12891201
Liu, Y., Kalpana, S., Baride, A., Romanova, S., Callegari, E., Huber, C. C., Wang, X., & Wang, H. (2021) · Figshare · doi:10.6084/m9.figshare.13620091
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) · Figshare · doi:10.6084/m9.figshare.12891213
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) · Figshare · doi:10.6084/m9.figshare.12891216
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) · Figshare · doi:10.6084/m9.figshare.12891204
Liu, Y., Kalpana, S., Baride, A., Romanova, S., Callegari, E., Huber, C. C., Wang, X., & Wang, H. (2021) · Figshare · doi:10.6084/m9.figshare.13620085
Liu, Y., Kalpana, S., Baride, A., Romanova, S., Callegari, E., Huber, C. C., Wang, X., & Wang, H. (2021) · Figshare · doi:10.6084/m9.figshare.13620097
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) · Figshare · doi:10.6084/m9.figshare.12891231
Ha, T.-Y., Choi, Y. R., Noh, H. R., Cha, S.-H., Kim, J.-B., & Park, S. M. (2021) · Figshare · doi:10.6084/m9.figshare.15071404
Bi, R. (2025) · International journal of high school research · doi:10.36838/v7i12.87
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