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 501–600 of 834
Protein aggregates stimulate macropinocytosis facilitating their propagation
Yerbury, J. J. (2016) · Prion · doi:10.1080/19336896.2016.1141860 · Cited by 26
Ahn, T. B., Langston, J. W., Aachi, V. R., & Dickson, D. W. (2012) · Europe PMC (PubMed Central) · Cited by 24
Disease-modifying therapeutic directions for Lewy-Body dementias
Zhang, Q., Kim, Y.-C., & Narayanan, N. S. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00293 · Cited by 26
The pallidopyramidal syndromes
Kara, E., Hardy, J., & Houlden, H. (2013) · Current Opinion in Neurology · doi:10.1097/wco.0b013e3283632e83 · Cited by 24
Novel therapeutic approaches in multiple system atrophy
Palma, J.-A., & Kaufmann, H. (2015) · Clinical Autonomic Research · doi:10.1007/s10286-014-0249-7 · Cited by 24
Hyun, C. H., Yoon, C. Y., Lee, H.-J., & Lee, S. (2013) · Experimental Neurobiology · doi:10.5607/en.2013.22.4.249 · Cited by 24
Andersen, M. A., Christensen, K. V., Badolo, L., Smith, G. P., Jeggo, R., Jensen, P. H., Andersen, K. J., & Sotty, F. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.04.011 · Cited by 24
Parkinson’s Disease: A Prionopathy?
Vascellari, S., & Manzin, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158022 · Cited by 26
Braidy, N., Gai, W.-P., Xu, Y. H., Sachdev, P. S., Guillemin, G. J., Jiang, X., Ballard, J. W. O., Horan, M. P., Fang, Z. M., Chong, B. H., et al. (2013) · Neurotoxicity Research · doi:10.1007/s12640-013-9420-5 · Cited by 24
Kaur, S., Sehrawat, A., Mastana, S. S., Kandimalla, R. J. L., Sharma, P. K., Bhatti, G. K., & Bhatti, J. S. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.121995 · Cited by 23
Woo, T., Yoon, M.-H., Kang, S., Park, S., Cho, J.-H., Hwang, Y. J., Ahn, J., Jang, H., Shin, Y.-J., Jung, E., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02862-z · Cited by 24
Park, S. M., & Kim, K. S. (2013) · Prion · doi:10.4161/pri.22850 · Cited by 23
Pemberton, S., & Melki, R. (2012) · Communicative & Integrative Biology · doi:10.4161/cib.18483 · Cited by 23
Self-citationSensing α‐Synuclein From the Outside via the Prion Protein: Implications for Neurodegeneration
Brás, I. C., Lopes, L. V., & Outeiro, T. F. (2018) · Movement Disorders · doi:10.1002/mds.27478 · Cited by 24
Self-citationPeña‐Díaz, S., Pujols, J., Pinheiro, F., Santos, J., Pallarès, I., Navarro, S., Conde-Giménez, M., García, J., Salvatella, X., Dalfó, E., et al. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.588947 · Cited by 22
Identification of Two Novel Peptides That Inhibit α-Synuclein Toxicity and Aggregation
Popova, B., Wang, D., Rajavel, A., Dhamotharan, K., Lázaro, D. F., Gerke, J., Uhrig, J. F., Hoppert, M., Outeiro, T. F., & Braus, G. H. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.659926 · Cited by 23
Self-citationChoi, J., Kim, S., Kwak, H., Park, D., Park, J., Ryu, J., Park, C., & Kang, J. (2017) · International Neurourology Journal · doi:10.5213/inj.1734961.458 · Cited by 22
Noradrenaline is crucial for the substantia nigra dopaminergic cell maintenance
af Bjerkén, S., Persson, R. S., Barkander, A., Karalija, N., Pelegrina‐Hidalgo, N., Gerhardt, G. A., Virel, A., & Strömberg, I. (2019) · Neurochemistry International · doi:10.1016/j.neuint.2019.104551 · Cited by 22
Neuroprotective approaches to halt Parkinson's disease progression
Sola, P., Krishnamurthy, P. T., Kumari, M., Byran, G., Gangadharappa, H. V., & Garikapati, K. K. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105380 · Cited by 21
Ito, N., Tsuji, M., Adachi, N., Nakamura, S., Sarkar, A. K., Ikenaka, K., Aguirre, C., Kimura, A., Kiuchi, Y., Mochizuki, H., et al. (2023) · npj Parkinson s Disease · doi:10.1038/s41531-023-00583-0 · Cited by 22
Calling α-synuclein a prion is scientifically justifiable
Watts, J. C. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02058-0 · Cited by 22
Raj, A. (2021) · Brain Connectivity · doi:10.1089/brain.2020.0905 · Cited by 21
Koh, Y. H., Tan, L. Y., & Ng, S. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00413 · Cited by 20
Amyloid accelerator polyphosphate fits as the mystery density in α-synuclein fibrils
Huettemann, P., Mahadevan, P., Lempart, J., Tse, E., Dehury, B., Edwards, B. F. P., Southworth, D. R., Sahoo, B. R., & Jakob, U. (2024) · PLoS Biology · doi:10.1371/journal.pbio.3002650 · Cited by 20
Jarras, H., Bourque, M., Poirier, A.-A., Morissette, M., Coulombe, K., Paolo, T. D., & Soulet, D. (2019) · Journal of Neuroendocrinology · doi:10.1111/jne.12782 · Cited by 20
Hadi, F., Akrami, H., Totonchi, M., Barzegar, A., Nabavi, S. M., & Shahpasand, K. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15257 · Cited by 22
Current Progress in the Development of Probes for Targeting α-Synuclein Aggregates
Zeng, Q., & Cui, M. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00877 · Cited by 19
Saturation mutagenesis of α-synuclein reveals monomer fold that modulates aggregation
Chlebowicz, J., Russ, W. P., Chen, D., Vega, A. R., Vernino, S. A., White, C. L., Rizo, J., Joachimiak, Ł. A., & Diamond, M. I. (2023) · Science Advances · doi:10.1126/sciadv.adh3457 · Cited by 19
Schorova, L., Bedard, N., Khayachi, A., Ho, H.-H., Bolivar-Pedroso, J., Huynh, J., Piccirelli, M., Wang, Y., Plourde, M., Luo, W., et al. (2023) · npj Parkinson s Disease · doi:10.1038/s41531-023-00601-1 · Cited by 20
The role of α-synuclein in neurodegeneration — An update
Jellinger, K. A. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0013-1 · Cited by 19
A note on testing hypotheses for stationary processes in the frequency domain
Holger Dette, A., & Hildebrandt, T. (2011) · Journal of Multivariate Analysis · doi:10.1016/j.jmva.2011.07.002 · Cited by 19
Ruiz-Arlandis, G., Pieri, L., Bousset, L., & Melki, R. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12258 · Cited by 21
Self-citationSmall molecules to prevent the neurodegeneration caused by α-synuclein aggregation
Peña‐Díaz, S., Pujols, J., & Ventura, S. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.284993 · Cited by 19
Models of Multiple System Atrophy
Fellner, L., Wenning, G. K., & Stefanova, N. (2013) · Current topics in behavioral neurosciences · doi:10.1007/7854_2013_269 · Cited by 19
Current Understanding of Protein Aggregation in Neurodegenerative Diseases
Hu, C., Lin, M., Wang, C., & Zhang, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110568 · Cited by 21
Rademacher, D. J. (2023) · Biomedicines · doi:10.3390/biomedicines11041187 · Cited by 18
Cell non‐autonomous functions of homeoproteins in neuroprotection in the brain
Joshi, R. L., Ibad, R. T., Rheey, J., Castagner, F., Prochiantz, A., & Moya, K. L. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.006 · Cited by 20
Chae, C. W., Lee, H. J., Choi, G. E., Jung, Y. H., Kim, J. S., Lim, J. R., Kim, S. Y., Hwang, I. K., Seong, J. K., & Han, H. J. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15131 · Cited by 18
Internalization of α-synuclein oligomers into SH-SY5Y cells
Shearer, L. J., Petersen, N. O., & Woodside, M. T. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2020.12.031 · Cited by 18
Raj, A., & Powell, F. (2021) · NeuroImage · doi:10.1016/j.neuroimage.2021.118008 · Cited by 18
Lau, D., Magnan, C., Hill, K. J., Cooper, A. A., Gambin, Y., & Sierecki, E. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00553 · Cited by 18
Spreading of alpha-synuclein between different cell types
Ruf, W. P., Meirelles, J. L., & Danzer, K. M. (2022) · Behavioural Brain Research · doi:10.1016/j.bbr.2022.114059 · Cited by 19
Amyotrophic lateral sclerosis and organ donation: Is there risk of disease transmission?
Holmes, B. B., & Diamond, M. I. (2012) · Annals of Neurology · doi:10.1002/ana.23684 · Cited by 18
Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion
Espargaró, A., Busquets, M. A., Estelrich, J., & Sabaté, R. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00029 · Cited by 18
Yan, M., Meng, L., Dai, L., Zhang, X., Chen, G., Zheng, Y., Zha, Y., Zeng, Y., & Zhang, Z. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.06.101 · Cited by 18
Palmas, M. F., Ena, A., Burgaletto, C., Casu, M. A., Cantarella, G., Carboni, E., Etzi, M., Simone, A. D., Fusco, G., Cardia, M. C., et al. (2022) · Neurotherapeutics · doi:10.1007/s13311-022-01182-2 · Cited by 18
Association between Parkinson’s Disease and Cancer: New Findings and Possible Mediators
Surguchov, A. P., & Surguchev, A. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25073899 · Cited by 17
Emerging role of microglia in inter-cellular transmission of α-synuclein in Parkinson’s disease
Zhang, X., Yu, H., & Feng, J. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1411104 · Cited by 17
Prions and Prion-Like Pathogens in Neurodegenerative Disorders
Peggion, C., Sorgato, M. C., & Bertoli, A. (2014) · Pathogens · doi:10.3390/pathogens3010149 · Cited by 17
Neurodegenerative disorders: Dysregulation of a carefully maintained balance?
Swart, C., Haylett, W. L., Kinnear, C. J., Johnson, G., Bardien, S., & Loos, B. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.09.003 · Cited by 19
A role for the proteasome in the turnover of S up35p and in [ PSI +] prion propagation
Kabani, M., Redeker, V., & Melki, R. (2014) · Molecular Microbiology · doi:10.1111/mmi.12572 · Cited by 17
Self-citationLi, Z.-F., Cui, L., Jin, M.-M., Hu, D., Hou, X.-G., Liu, S.-S., Zhang, X., & Zhu, J. (2022) · Disease Models & Mechanisms · doi:10.1242/dmm.049125 · Cited by 18
Allopregnanolone and neurogenesis in the nigrostriatal tract
Wang, J. M. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00224 · Cited by 17
Chen, S., Cai, F., Wang, J., Yang, Z., Gu, C., Wang, G., Mao, G., & Yan, J. (2019) · Molecular Medicine Reports · doi:10.3892/mmr.2019.10285 · Cited by 17
Direct Demonstration of Seed Size-Dependent α-Synuclein Amyloid Amplification
Sakunthala, A., Datta, D., Navalkar, A., Gadhe, L., Kadu, P., Patel, K., Mehra, S., Kumar, R., Chatterjee, D., Devi, J., et al. (2022) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.2c01650 · Cited by 16
Zheng, H., Shi, C., Luo, H., Fan, L., Yang, Z., Hu, X., Zhang, Z., Zhang, S., Hu, Z., Fan, Y., et al. (2020) · The Neuroscientist · doi:10.1177/1073858420943180 · Cited by 21
Environmental Epigenetics and Its Impacts on Disease Susceptibility: A Comprehensive Review
Ogunjobi, T. T., Gbayisomore, T. J., Nneji, P. O., Olofin, O. O., Olowe, E. N., Gigam-Ozuzu, C. D., Afolabi, J. I., Okwuokei, N. B., Boluwaji, V. A., Ojeniran, T. P., et al. (2024) · Medinformatics · doi:10.47852/bonviewmedin42022945 · Cited by 16
Preparation of α-Synuclein Amyloid Assemblies for Toxicity Experiments
Chen, S. W., & Cremades, N. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7816-8_4 · Cited by 16
The primary neuronal cells are more resistant than PC12 cells to α-synuclein toxic aggregates
Heravi, M., Dargahi, L., Parsafar, S., Marvian, A. T., Aliakbari, F., & Morshedi, D. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.01.055 · Cited by 16
Extracellular Alpha-Synuclein Promotes a Neuroinhibitory Secretory Phenotype in Astrocytes
Vieira, B. D. M., Radford, R. A. W., Hayashi, J., Eaton, E. D., Greenaway, B., Jambas, M., Petcu, E. B., Chung, R. S., & Pountney, D. L. (2020) · Life · doi:10.3390/life10090183 · Cited by 16
Macchi, F., Deleersnijder, A., den Haute, C. V., Munck, S., Pottel, H., Michiels, A., Debyser, Z., Gérard, M., & Baekelandt, V. (2015) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2015.11.009 · Cited by 16
Dadgar‐Kiani, E., Bieri, G., Melki, R., Gitler, A. D., & Lee, J. H. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111631 · Cited by 15
Self-citationSharma, S., & Deep, S. (2024) · Chemical Communications · doi:10.1039/d4cc00822g · Cited by 15
Zhu, Y., Wang, F., Xia, Y., Wang, L., Lin, H., Zhong, T., & Wang, X. (2024) · Reviews in the Neurosciences · doi:10.1515/revneuro-2024-0043 · Cited by 15
Role of Lipids in the Pathogenesis of Parkinson’s Disease
Kamano, S., Ozawa, D., Ikenaka, K., & Nagai, Y. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168935 · Cited by 15
Glucocerebrosidase, a new player changing the old rules in Lewy body diseases
Yang, N.-Y., Lee, Y.-N., Lee, H.-J., Kim, Y. S., & Lee, S. (2013) · Biological Chemistry · doi:10.1515/hsz-2012-0322 · Cited by 15
C. elegans Models to Study the Propagation of Prions and Prion-Like Proteins
Sandhof, C. A., Hoppe, S. O., Tittelmeier, J., & Nussbaum-Krammer, C. I. (2020) · Biomolecules · doi:10.3390/biom10081188 · Cited by 15
The effects of AQP4 rs162009 on resting‐state brain activity in Parkinson's disease
Jiang, M., Fang, Y., Dai, S., Si, X., Wang, Z., Tang, J., Gao, T., Liu, Y., Song, Z., Pu, J., et al. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14208 · Cited by 15
Review: The fate of cell grafts for the treatment of H untington's disease: the post‐mortem evidence
Cisbani, G., & Cicchetti, F. (2013) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12104 · Cited by 17
Stem cell pathologies and neurological disease
Steindler, D. A., Okun, M. S., & Scheffler, B. (2011) · Modern Pathology · doi:10.1038/modpathol.2011.165 · Cited by 16
Prognostic role of “prion-like propagation” in SOD1-linked familial ALS: an alternative view
Sugaya, K., & Nakano, I. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00359 · Cited by 16
Shen, Y., Guo, X., Han, C., Wan, F. J., Ma, K., Guo, S., Wang, L., Xia, Y. F., Liu, L., Lin, Z., et al. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2549-2 · Cited by 15
Menéndez‐González, M., Padilla-Zambrano, H., Tomás‐Zapico, C., & Fernández‐Garcia, B. (2018) · Brain Sciences · doi:10.3390/brainsci8040052 · Cited by 15
Prion-like propagation of α-synuclein in the gut-brain axis
Chen, Y., Shao, Q.-H., Yuan, Y., & Chen, N. (2018) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2018.06.002 · Cited by 15
Entropic Bristles Tune the Seeding Efficiency of Prion-Nucleating Fragments
Michiels, E., Liu, S., Gallardo, R. U., Louros, N. N., Mathelié‐Guinlet, M., Dufrêne, Y. F., Schymkowitz, J. W. H., Vorberg, I. M., & Rousseau, F. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.01.098 · Cited by 15
Bendifallah, M., Redeker, V., Monsellier, É., Bousset, L., Bellande, T., & Melki, R. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.04.091 · Cited by 15
Self-citationSmall molecule-based fluorescent probes for the detection of α-Synuclein aggregation states
Haque, R., & Maity, D. (2023) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2023.129257 · Cited by 15
The unique neuropathological vulnerability of the human brain to aging
Ferrer, I. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101916 · Cited by 15
Tullo, S., de Miranda, A. S., del Cid‐Pellitero, E., Lim, M. P., Gallino, D., Attaran, A., Patel, R., Novikov, V., Park, M., Beraldo, F. H., et al. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15967 · Cited by 17
Feng, M., Zou, Z., Shou, P., Peng, W., Liu, M., & Li, X. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1479343 · Cited by 14
Sirtuins and Proteolytic Systems: Implications for Pathogenesis of Synucleinopathies
Sampaio‐Marques, B., & Ludovico, P. (2015) · Biomolecules · doi:10.3390/biom5020735 · Cited by 15
In vitro models of multiple system atrophy from primary cells to induced pluripotent stem cells
Abati, E., Fonzo, A. D., & Corti, S. P. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13563 · Cited by 14
α -Synuclein Trafficking in Parkinson’s Disease: Insights From Fly and Mouse Models
Cheng, J., Lu, Q., Li, S., & Ho, M. S.-C. (2018) · ASN NEURO · doi:10.1177/1759091418812587 · Cited by 14
Cell-free amplification of prions: Where do we stand?
Cazzaniga, F. A., Luca, C. M. G. D., Bistaffa, E., Consonni, A., Legname, G., Giaccone, G., & Moda, F. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.08.005 · Cited by 14
Reduced erythrocytic CHCHD2 mRNA is associated with brain pathology of Parkinson’s disease
Liu, X., Wang, Q., Yang, Y., Stewart, T., Shi, M. Y., Soltys, D., Liu, G., Thorland, E., Cilento, E. M., Hou, Y., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01133-6 · Cited by 14
Structural and Biophysical Characterization of Stable Alpha-Synuclein Oligomers
Vaikath, N. N., Sudhakaran, I. P., Abdi, I. Y., Gupta, V. R., Majbour, N. K., Ghanem, S. S., Abdesselem, H., Vekrellis, K., & El‐Agnaf, O. M. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314630 · Cited by 14
Context dependence of protein misfolding and structural strains in neurodegenerative diseases
Mehta, A. K., Rosen, R. F., Childers, W. S., Gehman, J. D., Walker, L. C., & Lynn, D. G. (2013) · Biopolymers · doi:10.1002/bip.22283 · Cited by 14
Heat shock protein defenses in the neocortex and allocortex of the telencephalon
Posimo, J. M., Weilnau, J. N., Gleixner, A. M., Broeren, M. T., Weiland, N. L., Brodsky, J. L., Wipf, P., & Leak, R. K. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.02.011 · Cited by 14
Laumann, K., Boas, U., Larsen, H. M., Heegaard, P. M. H., & Bergström, A. (2014) · Biomacromolecules · doi:10.1021/bm501244m · Cited by 14
Self-citationLuo, H.-T., Zhang, J.-P., & Miao, F. (2016) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2016.3471 · Cited by 14
Fellner, L., Buchinger, E., Brück, D., Irschick, R., Wenning, G. K., & Stefanova, N. (2018) · BMC Neuroscience · doi:10.1186/s12868-018-0431-2 · Cited by 14
Veys, L., houcke, J. V., Aerts, J., Pottelberge, S. V., Mahieu, M., Coens, A., Melki, R., Moechars, D., Muynck, L. D., & Groef, L. D. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.614587 · Cited by 16
Self-citationMore than a Rumor Spreads in Parkinson's Disease
Prymaczok, N. C., Riek, R., & Gerez, J. (2016) · Frontiers in Human Neuroscience · doi:10.3389/fnhum.2016.00608 · Cited by 15
Neurodegenerative Disease Transmission and Transgenesis in MicePreprint
Dugger, B. N., Perl, D. P., & Carlson, G. A. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a023549 · Cited by 14
Abraham, J. N., Rawat, D., Srikanth, P., Sunny, L. P., & Abraham, N. M. (2025) · Mammalian Genome · doi:10.1007/s00335-025-10128-w · Cited by 13
Pratt, M. R., Abeywardana, T., & Marotta, N. P. (2015) · Biomolecules · doi:10.3390/biom5031210 · Cited by 14
Shrivastava, A. N., Redeker, V., Fritz, N., Pieri, L., Almeida, L. G., Spolidoro, M., Liebmann, T., Bousset, L., Renner, M. L., Léna, C., et al. (2016) · Data in Brief · doi:10.1016/j.dib.2016.02.018 · Cited by 13
Self-citationExperimental colitis drives enteric alpha-synuclein accumulation and Parkinson-like brain pathologyPreprint
Grathwohl, S. A., Quansah, E., Maroof, N., Steiner, J. A., Spycher, L., Benmansour, F., Durán-Pacheco, G., Siebourg‐Polster, J., Oroszlan‐Szovik, K., Remy, H., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/505164 · Cited by 13
Self-citationEtiology and Pathogenesis of Parkinson Disease
deSouza, R., & Schapira, A. H. V. (2017) · Neurodegeneration · doi:10.1002/9781118661895.ch5 · Cited by 13
The role of microglia in the prion-like transmission of protein aggregates in neurodegeneration
Öztürk, M. M., Emgård, J., García‐Revilla, J., Fernández‐Calle, R., Yang, Y., Deierborg, T., & Roos, T. T. (2025) · Brain Communications · doi:10.1093/braincomms/fcaf087 · Cited by 14
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
