Patient-Specific iPSC-Derived Astrocytes Contribute to Non-Cell-Autonomous Neurodegeneration in Parkinson's Disease
Open accessAbstract
Parkinson's disease (PD) is associated with the degeneration of ventral midbrain dopaminergic neurons (vmDAns) and the accumulation of toxic α-synuclein. A non-cell-autonomous contribution, in particular of astrocytes, during PD pathogenesis has been suggested by observational studies, but remains to be experimentally tested. Here, we generated induced pluripotent stem cell-derived astrocytes and neurons from familial mutant LRRK2 G2019S PD patients and healthy individuals. Upon co-culture on top of PD astrocytes, control vmDAns displayed morphological signs of neurodegeneration and abnormal, astrocyte-derived α-synuclein accumulation. Conversely, control astrocytes partially prevented the appearance of disease-related phenotypes in PD vmDAns. We additionally identified dysfunctional chaperone-mediated autophagy (CMA), impaired macroautophagy, and progressive α-synuclein accumulation in PD astrocytes. Finally, chemical enhancement of CMA protected PD astrocytes and vmDAns via the clearance of α-synuclein accumulation. Our findings unveil a crucial non-cell-autonomous contribution of astrocytes during PD pathogenesis, and open the path to exploring novel therapeutic strategies aimed at blocking the pathogenic cross talk between neurons and glial cells.
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Non-cell autonomous mechanisms can cause dysfunction across the entire substantia nigra pars compacta, leading to rapid dopaminergic neurodegeneration, in contrast to neuron-specific cell autonomous mechanisms.
“in contrast to neuron-specific cell autonomous mechanisms that affect individual DA neurons within the SNc, non-cell autonomous mechanisms can cause dysfunction across the entire SNc, thereby leading to rapid DA neurodegeneration”
From Mitochondrial DNA Damage in Substantia Nigra Pars Compacta Astrocytes Exacerbates Dopaminergic Neuron Loss in a 6-Hydroxydopamine Mouse Model of Parkinsonism (2026) · cites this paper as di Domenico et al. 2019
The Abstract and Discussion report that PD-derived astrocytes contribute to dopaminergic-neuron degeneration, including in co-culture with control neurons. The Introduction identifies the substantia nigra pars compacta as a site of dopaminergic-neuron loss, but the paper does not show dysfunction across the entire region, establish rapid degeneration, or make the stated comparison with neuron-specific mechanisms. Page numbers are unavailable in our copy. (LLM, conf=0.88)
Experimental — accuracy not yet measuredAstrocytes generated from hiPSC derived from fibroblasts of patients with CNS diseases show pathological phenotypes, including dysregulation of lipid metabolism, alteration in extracellular vesicles, reduced autophagy, or altered STAT3 signaling.
“Interestingly, astrocytes generated from hiPSC derived from fibroblasts obtained from patients with CNS diseases (usually with a genetic mutation causative of disease or a risk polymorphism) show pathological phenotypes, including dysregulation of lipid metabolism11, alteration in the contents of the extracellular vesicles released by astrocytes80, reduced autophagy81, or altered STAT3 signaling82”
From Reactive astrocyte nomenclature, definitions, and future directions (2021) · cites this paper as [81]
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Vos, T., Barber, R. M., Bell, B., Bertozzi-Villa, A., Biryukov, S., Bolliger, I., Charlson, F., Davis, A., Degenhardt, L., Dicker, D., et al. (2015) · The Lancet · doi:10.1016/s0140-6736(15)60692-4 · Cited by 6,414 · see citing works
Highly efficient neural conversion of human ES and iPS cells by dual inhibition of SMAD signaling
Chambers, S. M., Fasano, C. A., Papapetrou, E. P., Tomishima, M., Sadelain, M., & Studer, L. (2009) · Nature Biotechnology · doi:10.1038/nbt.1529 · Cited by 3,620 · see citing works
Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy
Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024 · cited 2× · see citing works
“…in a-syn turnover in these cells. a-syn has previously been shown to undergo degradation both by the ubiquitin/proteasome system and by autophagy (Cuervo et al., 2004; Webb et al., 2003); therefore a-syn flux in the presence of lysosomal and proteasome inhibitors (leupeptin and lactacystin,…”
BackgroundSelf-citationKriks, S., Shim, J., Piao, J., Ganat, Y. M., Wakeman, D. R., Xie, Z., Carrillo‐Reid, L., Auyeung, G., Antonacci, C. L., Buch, A., et al. (2011) · Nature · doi:10.1038/nature10648 · Cited by 1,912 · see citing works
α-Synuclein Is Degraded by Both Autophagy and the Proteasome
Webb, J. L., Ravikumar, B., Atkins, J., Skepper, J. N., & Rubinsztein, D. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300227200 · Cited by 1,429 · see citing works
Lee, H.-J., Suk, J.-E., Patrick, C., Bae, E.-J., Cho, J.-H., Rho, S., Hwang, D., Masliah, E., & Lee, S.-J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.081125 · Cited by 877 · see citing works
α-Synuclein impairs macroautophagy: implications for Parkinson’s disease
Winslow, A. R., Chen, C.-W., Corrochano, S., Acevedo-Arozena, A., Gordon, D. E., Peden, A. A., Lichtenberg, M., Menzies, F. M., Ravikumar, B., Imarisio, S., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201003122 · Cited by 825 · see citing works
A common LRRK2 mutation in idiopathic Parkinson's disease
Gilks, W. P., Abou-Sleiman, P. M., Gandhi, S., Jain, S., Singleton, A., Lees, A. J., Shaw, K., Bhatia, K. P., Bonifati, V., Quinn, N. P., et al. (2005) · The Lancet · doi:10.1016/s0140-6736(05)17830-1 · Cited by 774 · see citing works
LRRK2 Mutant iPSC-Derived DA Neurons Demonstrate Increased Susceptibility to Oxidative Stress
Nguyen, H. N., Byers, B., Cord, B. J., Shcheglovitov, A., Byrne, J., Gujar, P., Kee, K., Schüle, B., Dolmetsch, R. E., Langston, J. W., et al. (2011) · Cell stem cell · doi:10.1016/j.stem.2011.01.013 · Cited by 748 · see citing works
A novel TALE nuclease scaffold enables high genome editing activity in combination with low toxicity
Mussolino, C., Morbitzer, R., Lütge, F., Dannemann, N., Lahaye, T., & Cathomen, T. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr597 · Cited by 714 · see citing works
Dopamine-modified α-synuclein blocks chaperone-mediated autophagy
Martínez‐Vicente, M., Tallóczy, Z., Kaushik, S., Massey, A. C., Mazzulli, J. R., Mosharov, E. V., Hodara, R., Fredenburg, R. A., Wu, D.-C., Follenzi, A., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci32806 · Cited by 633 · see citing works
Self-citationThe Role of Astrocyte Dysfunction in Parkinson’s Disease Pathogenesis
Booth, H. D. E., Hirst, W. D., & Wade-Martins, R. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.04.001 · Cited by 633 · see citing works
Activation of Chaperone-mediated Autophagy during Oxidative Stress
Kiffin, R., Christian, C., Knecht, E., & Cuervo, A. M. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-06-0477 · Cited by 611 · see citing works
Self-citationInterplay of LRRK2 with chaperone-mediated autophagy
Orenstein, S. J., Kuo, S.-H., Tasset, I., Arias, E., Koga, H., Fernandez-Carasa, I., Cortes, E., Honig, L. S., Dauer, W., Consiglio, A., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3350 · Cited by 588 · see citing works
Self-citationSánchez‐Danés, A., Richaud‐Patín, Y., Carballo‐Carbajal, I., Jiménez‐Delgado, S., Caig, C., Mora, S., Guglielmo, C. D., Ezquerra, M., Patel, B., Giralt, A., et al. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201200215 · Cited by 557 · see citing works
Self-citationParkin Protects against the Toxicity Associated with Mutant α-Synuclein
Petrucelli, L., O’Farrell, C., Lockhart, P. J., Baptista, M. J., Kehoe, K. J., Vink, L., Choi, P., Wolozin, B. L., Farrer, M. J., Hardy, J., et al. (2002) · Neuron · doi:10.1016/s0896-6273(02)01125-x · Cited by 552 · see citing works
Consequences of the selective blockage of chaperone-mediated autophagy
Massey, A. C., Kaushik, S., Sovak, G., Kiffin, R., & Cuervo, A. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507436103 · Cited by 529 · see citing works
Self-citationTanaka, Y. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.9.919 · Cited by 497 · see citing works
Braak, H., Sastre, M., & Del Tredici, K. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0244-3 · Cited by 462 · see citing works
Defects in trafficking bridge Parkinson’s disease pathology and genetics
Abeliovich, A., & Gitler, A. D. (2016) · Nature · doi:10.1038/nature20414 · Cited by 462 · see citing works
Genetic screening for a single common LRRK2 mutation in familial Parkinson's disease
Nichols, W. C., Pankratz, N., Hernandez, D., Paisán-Ruíz, C., Jain, S., Halter, C. A., Michaels, V. E., Reed, T., Rudolph, A., Shults, C. W., et al. (2005) · The Lancet · doi:10.1016/s0140-6736(05)17828-3 · Cited by 457 · see citing works
Parkinson's--Divergent Causes, Convergent Mechanisms
Greenamyre, J. T., & Hastings, T. G. (2004) · Science · doi:10.1126/science.1098966 · Cited by 453 · see citing works
Wakabayashi, K., Hayashi, S., Yoshimoto, M., Kudo, H., & Takahashi, H. (2000) · Acta Neuropathologica · doi:10.1007/pl00007400 · Cited by 439 · see citing works
Genetics of Parkinson's disease
Lill, C. M. (2016) · Molecular and Cellular Probes · doi:10.1016/j.mcp.2016.11.001 · Cited by 362 · see citing works
Serio, A., Bilican, B., Barmada, S. J., Ando, D. M., Zhao, C., Siller, R., Burr, K., Haghi, G., Story, D., Nishimura, A. L., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300398110 · Cited by 345 · see citing works
Gu, X., Long, C.-X., Sun, L., Xie, C., Lin, X. Z., & Cai, H. (2010) · Molecular Brain · doi:10.1186/1756-6606-3-12 · Cited by 341 · see citing works
Kita‐Matsuo, H., Barcová, M., Prigozhina, N. L., Salomonis, N., Wei, K. A., Jacot, J. G., Nelson, B., Spiering, S., Haverslag, R. T., Kim, C., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005046 · Cited by 227 · see citing works
Chemical modulation of chaperone-mediated autophagy by retinoic acid derivatives
Anguiano, J., Garner, T. P., Mahalingam, M., Das, B. C., Gavathiotis, E., & Cuervo, A. M. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1230 · Cited by 226 · see citing works
Self-citationRegulated degradation of Chk1 by chaperone-mediated autophagy in response to DNA damage
Park, C., Suh, Y., & Cuervo, A. M. (2015) · Nature Communications · doi:10.1038/ncomms7823 · Cited by 224 · see citing works
Self-citationA photoconvertible fluorescent reporter to track chaperone-mediated autophagy
Koga, H., Martínez‐Vicente, M., Macián, F., Verkhusha, V. V., & Cuervo, A. M. (2011) · Nature Communications · doi:10.1038/ncomms1393 · Cited by 214 · see citing works
Self-citationLoss of hepatic chaperone‐mediated autophagy accelerates proteostasis failure in aging
Schneider, J. L., Villarroya, J., Díaz-Carretero, A. M., Patel, B., Urbanska, A. M., Thi, M. M., Villarroya, F., Santambrogio, L., & Cuervo, A. M. (2015) · Aging Cell · doi:10.1111/acel.12310 · Cited by 192 · see citing works
Self-citationCustom zinc-finger nucleases for use in human cells
Alwin, S., Gere, M. B., Guhl, E., Effertz, K., Barbas, C. F., Segal, D. J., Weitzman, M. D., & Cathomen, T. (2005) · Molecular Therapy · doi:10.1016/j.ymthe.2005.06.094 · Cited by 165 · see citing works
Heman-Ackah, S. M., Manzano, R., Hoozemans, J. J. M., Scheper, W., Flynn, R., Haerty, W., Cowley, S. A., Bassett, A. R., & Wood, M. J. A. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx331 · Cited by 155 · see citing works
“LRRK2: Autophagy and Lysosomal Activity”
Madureira, M., Connor‐Robson, N., & Wade‐Martins, R. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00498 · Cited by 141 · see citing works
Skibinski, G., Nakamura, K., Cookson, M., & Finkbeiner, S. M. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.2712-13.2014 · Cited by 138 · see citing works
Chang, C.-Y., Ting, H.-C., Liu, C.-A., Su, H., Chiou, T., Lin, S., Harn, H., & Ho, T. (2020) · Molecules · doi:10.3390/molecules25082000 · Cited by 133 · see citing works
Cavaliere, F., Cerf, L., Dehay, B., Ramos‐Gonzalez, P., Giorgi, F. D., Bourdenx, M., Bessede, A., Obeso, J. A., Matute, C., Ichas, F., et al. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.04.011 · Cited by 119 · see citing works
Nuclear Aggresomes Form by Fusion of PML-associated Aggregates
Fu, L., Gao, Y., Tousson, A., Shah, A., Chen, T.-L. L., Vertel, B. M., & Sztul, E. S. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-01-0019 · Cited by 72 · see citing works
Early cellular changes after blockage of chaperone-mediated autophagy
Massey, A. C., Follenzi, A., Kiffin, R., Zhang, C., & Cuervo, A. M. (2008) · Autophagy · doi:10.4161/auto.5654 · Cited by 70 · see citing works
Self-citationSu, Y.-C., Guo, X. L., & Qi, X. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.11.009 · Cited by 65 · see citing works
Pluripotent stem cell-based disease modeling: current hurdles and future promise
Zeltner, N., & Studer, L. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.10.008 · Cited by 65 · see citing works
Glutathione depletion and overproduction both initiate degeneration of nigral dopaminergic neurons
Garrido, M., Tereshchenko, Y., Zhevtsova, Z., Taschenberger, G., Bähr, M., & Kügler, S. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0791-x · Cited by 59 · see citing works
Cellular functions of LRRK2 implicate vesicular trafficking pathways in Parkinson's disease
Cookson, M. (2016) · Biochemical Society Transactions · doi:10.1042/bst20160228 · Cited by 51 · see citing works
Mechanisms of Mutant LRRK2 Neurodegeneration
Cookson, M. R. (2017) · Advances in neurobiology · doi:10.1007/978-3-319-49969-7_12 · Cited by 39 · see citing works
The Contribution of Astrocyte Autophagy to Systemic Metabolism
Ortiz‐Rodriguez, A., & Arévalo, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072479 · Cited by 36 · see citing works
Unprecedented Potential for Neural Drug Discovery Based on Self-Organizing hiPSC Platforms
Cota-Coronado, A., Durnall, J. C., Díaz, N. F., Thompson, L. H., & Díaz-Martínez, N. E. (2020) · Molecules · doi:10.3390/molecules25051150 · Cited by 10 · see citing works
CAV-2-Mediated GFP and LRRK2G2019S Expression in the Macaca fascicularis Brain
DiCaudo, C., Martínez-Valbuena, I., Mundiñano, I.-C., Gennetier, A., Hernández, M., Carmona‐Abellán, M., Marcilla, I., Kremer, E. J., & Luquín, M. R. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00049 · Cited by 4 · see citing works
Flagged first, then by citations
2 of the 49 references couldn’t be matched to a known paper.
Cited by
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Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,622 · see citing works
Self-citationReactive astrocyte nomenclature, definitions, and future directions
Escartin, C., Galea, E., Lakatos, A., O’Callaghan, J. P., Petzold, G. C., Serrano-Pozo, A., Steinhäuser, C., Volterra, A., Carmignoto, G., Agarwal, A., et al. (2021) · Nature Neuroscience · doi:10.1038/s41593-020-00783-4 · Cited by 2,533 · see citing works
Functional roles of reactive astrocytes in neuroinflammation and neurodegeneration
Patani, R., Hardingham, G. E., & Liddelow, S. A. (2023) · Nature Reviews Neurology · doi:10.1038/s41582-023-00822-1 · Cited by 531 · see citing works
The different autophagy degradation pathways and neurodegeneration
Fleming, A., Bourdenx, M., Fujimaki, M., Karabiyik, C., Krause, G. J., Lopez, A., Martín‐Segura, A., Puri, C., Scrivo, A., Skidmore, J., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.01.017 · Cited by 485 · see citing works
Self-citationCai, Y., Song, W., Li, J., Jing, Y., Liang, C., Zhang, L., Zhang, X., Zhang, W., Liu, B., An, Y., et al. (2022) · Science China Life Sciences · doi:10.1007/s11427-022-2161-3 · Cited by 436 · see citing works
Microglia and astrocyte dysfunction in parkinson's disease
Kam, T., Hinkle, J. T., Dawson, T. M., & Dawson, V. L. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105028 · Cited by 399 · see citing works
Glucocerebrosidase and its relevance to Parkinson disease
Do, J., McKinney, C. E., Sharma, P., & Sidransky, E. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0336-2 · Cited by 304 · see citing works
Autophagy and the hallmarks of aging
Kaushik, S., Tasset, I., Arias, E., Pampliega, O., Wong, E., Martinez-Vicente, M., & Cuervo, A. M. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101468 · Cited by 285 · see citing works
Self-citationLi, L., Acioglu, C., Heary, R. F., & Elkabes, S. (2021) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2020.10.007 · Cited by 283 · see citing works
The Contribution of Microglia to Neuroinflammation in Parkinson’s Disease
Badanjak, K., Fixemer, S., Smajić, S., Skupin, A., & Grünewald, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094676 · Cited by 281 · see citing works
LRRK2 mediates tubulation and vesicle sorting from lysosomes
Bonet-Ponce, L., Beilina, A., Williamson, C. D., Lindberg, E., Kluss, J. H., Saez-Atienzar, S., Landeck, N., Kumaran, R., Mamais, A., Bleck, C., et al. (2020) · Science Advances · doi:10.1126/sciadv.abb2454 · Cited by 230 · see citing works
Lysosomal dysfunction in neurodegeneration: emerging concepts and methods
Udayar, V., Chen, Y., Sidransky, E., & Jagasia, R. (2022) · Trends in Neurosciences · doi:10.1016/j.tins.2021.12.004 · Cited by 238 · see citing works
CD49f Is a Novel Marker of Functional and Reactive Human iPSC-Derived Astrocytes
Barbar, L., Jain, T., Zimmer, M., Kruglikov, I., Sadick, J. S., Wang, M., Kalpana, K., Rose, I. V. L., Burstein, S. R., Rusielewicz, T., et al. (2020) · Neuron · doi:10.1016/j.neuron.2020.05.014 · Cited by 206 · see citing works
Neuron-Astrocyte Interactions in Parkinson’s Disease
Miyazaki, I., & Asanuma, M. (2020) · Cells · doi:10.3390/cells9122623 · Cited by 186 · see citing works
Metabolic alterations in Parkinson’s disease astrocytes
Sonninen, T.-M., Hämäläinen, R. H., Koskuvi, M., Oksanen, M., Shakirzyanova, A., Wojciechowski, S., Puttonen, K. A., Naumenko, N. V., Goldsteins, G., Laham-Karam, N., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-71329-8 · Cited by 181 · see citing works
Copas, A. N. M., McComish, S. F., Fletcher, J. M., & Caldwell, M. A. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.666737 · Cited by 175 · see citing works
Melatonin and Autophagy in Aging-Related Neurodegenerative Diseases
Luo, F., Sandhu, A. F., Rungratanawanich, W., Williams, G. E., Akbar, M. D., Zhou, S., Song, B., & Wang, X. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197174 · Cited by 158 · see citing works
Dysfunction of Cellular Proteostasis in Parkinson’s Disease
Lehtonen, Š., Sonninen, T.-M., Wojciechowski, S., Goldsteins, G., & Koıstınaho, J. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00457 · Cited by 146 · see citing works
The immune system in Parkinson's disease: what we know so far
Roodveldt, C., Bernardino, L. I., Çakmak, Ö. Ö., Dragić, M., Fladmark, K. E., Ertan, S., Aktaş, B., Pita, C., Ciglar, L., Garraux, G., et al. (2024) · Brain · doi:10.1093/brain/awae177 · Cited by 148 · see citing works
“LRRK2: Autophagy and Lysosomal Activity”
Madureira, M., Connor‐Robson, N., & Wade‐Martins, R. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00498 · Cited by 141 · see citing works
Chang, C.-Y., Ting, H.-C., Liu, C.-A., Su, H., Chiou, T., Lin, S., Harn, H., & Ho, T. (2020) · Molecules · doi:10.3390/molecules25082000 · Cited by 133 · see citing works
The Emerging Role of the Lysosome in Parkinson’s Disease
Navarro-Romero, A., Montpeyó, M., & Martínez‐Vicente, M. (2020) · Cells · doi:10.3390/cells9112399 · Cited by 134 · see citing works
Jacquet, A. D. R., Alpaugh, M., Denis, H. L., Tancredi, J. L., Boutin, M., Decaestecker, J., Beauparlant, C., Herrmann, L., Saint-Pierre, M., Parent, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39038-8 · Cited by 114 · see citing works
Parkinson’s Disease–Associated LRRK2 Interferes with Astrocyte-Mediated Alpha-Synuclein Clearance
Streubel-Gallasch, L., Giusti, V., Sandre, M., Tessari, I., Plotegher, N., Giusto, E., Masato, A., Iovino, L., Battisti, I., Arrigoni, G., et al. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02327-8 · Cited by 123 · see citing works
Astrocytes Protect Human Dopaminergic Neurons from α-Synuclein Accumulation and Propagation
Tsunemi, T., Ishiguro, Y., Yoroisaka, A., Valdez, C., Miyamoto, K., Ishikawa, K., Saiki, S., Akamatsu, W., Hattori, N., & Krainc, D. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.0954-20.2020 · Cited by 115 · see citing works
Contribution of astrocytes to neuropathology of neurodegenerative diseases
Acıoğlu, Ç., Li, L., & Elkabes, S. (2021) · Brain Research · doi:10.1016/j.brainres.2021.147291 · Cited by 115 · see citing works
The Vicious Cycle Between α ‐Synuclein Aggregation and Autophagic‐Lysosomal Dysfunction
Bellomo, G., Paciotti, S., Gatticchi, L., & Parnetti, L. (2019) · Movement Disorders · doi:10.1002/mds.27895 · Cited by 114 · see citing works
Lysosome and Inflammatory Defects in GBA1‐Mutant Astrocytes Are Normalized by LRRK2 Inhibition
Sanyal, A., DeAndrade, M. P., Novis, H. S., Lin, S. C., Chang, J., Lengacher, N. A., Tomlinson, J. J., Tansey, M. G., & LaVoie, M. J. (2020) · Movement Disorders · doi:10.1002/mds.27994 · Cited by 114 · see citing works
Advances in microfluidic in vitro systems for neurological disease modeling
Holloway, P. M., Willaime‐Morawek, S., Siow, R. C. M., Barber, M., Owens, R. M., Sharma, A. D., Rowan, W. C., Hill, E. J., & Zagnoni, M. (2021) · Journal of Neuroscience Research · doi:10.1002/jnr.24794 · Cited by 101 · see citing works
Lee, J. H., Han, J., Kim, H., Park, S. M., Joe, E.-H., & Jou, I. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0716-4 · Cited by 105 · see citing works
The A1 astrocyte paradigm: New avenues for pharmacological intervention in neurodegeneration
Hinkle, J. T., Dawson, V. L., & Dawson, T. M. (2019) · Movement Disorders · doi:10.1002/mds.27718 · Cited by 98 · see citing works
Key genes and convergent pathogenic mechanisms in Parkinson disease
Coukos, R., & Krainc, D. (2024) · Nature reviews. Neuroscience · doi:10.1038/s41583-024-00812-2 · Cited by 102 · see citing works
Immune responses in the Parkinson's disease brain
Weiss, F. C., Labrador‐Garrido, A., Dzamko, N. L., & Halliday, G. M. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105700 · Cited by 97 · see citing works
Mitochondrial dysfunction in astrocytes: A role in Parkinson’s disease?
Bantle, C. M., Hirst, W. D., Weihofen, A., & Shlevkov, E. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.608026 · Cited by 95 · see citing works
Estes, R., Lin, B. C., Khera, A., & Davis, M. Y. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.788695 · Cited by 94 · see citing works
Boonpraman, N., Yoon, S., Kim, C. Y., Moon, J., & Yi, S. S. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102698 · Cited by 95 · see citing works
Wilson, H., Dervenoulas, G., Pagano, G., Tyacke, R. J., Polychronis, S., Myers, J., Gunn, R. N., Rabiner, E. A., Nutt, D., & Politis, M. (2019) · Brain · doi:10.1093/brain/awz260 · Cited by 93 · see citing works
Ordóñez, A. J. L., Fernández, B., Fdez, E., Romo-Lozano, M., Madero‐Pérez, J., Lobbestael, E., Baekelandt, V., Aiastui, A., de Munaín, A. L., Melrose, H. L., et al. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz201 · Cited by 90 · see citing works
Blood–Brain Barrier and Neurodegenerative Diseases—Modeling with iPSC-Derived Brain Cells
Wu, Y., Sonninen, T.-M., Peltonen, S., Koıstınaho, J., & Lehtonen, Š. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147710 · Cited by 88 · see citing works
Neuroinflammatory Responses and Parkinson’ Disease: Pathogenic Mechanisms and Therapeutic Targets
Yang, L., Mao, K., Yu, H., & Chen, J. (2020) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-020-09926-7 · Cited by 90 · see citing works
Jacquet, A. D. R., Tancredi, J. L., Lemire, A. L., DeSantis, M. C., Li, W., & O’Shea, E. K. (2021) · eLife · doi:10.7554/elife.73062 · Cited by 89 · see citing works
Arredondo, C., Cefaliello, C., Dyrda, A., Jury, N., Martínez, P., Díaz, I. D. P., Amaro, A., Tran, H., Morales, D., Pertusa, M., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.02.010 · Cited by 85 · see citing works
Pathogenesis of α-Synuclein in Parkinson’s Disease: From a Neuron-Glia Crosstalk Perspective
Yi, S., Wang, L.-F., Wang, H., Ho, M., & Zhang, S.-P. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314753 · Cited by 66 · see citing works
Wang, C., Yang, T., Liang, M., Xie, J., & Song, N. (2021) · Translational Neurodegeneration · doi:10.1186/s40035-021-00265-y · Cited by 85 · see citing works
A characterization of Gaucher iPS-derived astrocytes: Potential implications for Parkinson's disease
Aflaki, E., Stubblefield, B. K., McGlinchey, R. P., McMahon, B., Ory, D. S., & Sidransky, E. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104647 · Cited by 77 · see citing works
Astrocytic atrophy as a pathological feature of Parkinson’s disease with LRRK2 mutation
Ramos‐Gonzalez, P., Mato, S., Chara, J. C., Verkhratsky, A., Matute, C., & Cavaliere, F. (2021) · npj Parkinson s Disease · doi:10.1038/s41531-021-00175-w · Cited by 75 · see citing works
Autophagy in Astrocytes and its Implications in Neurodegeneration
Sung, K., & Jiménez-Sánchez, M. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.041 · Cited by 74 · see citing works
Towards Advanced iPSC-based Drug Development for Neurodegenerative Disease
Pasteuning-Vuhman, S., de Jongh, R., Timmers, A., & Pasterkamp, R. J. (2020) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2020.09.013 · Cited by 71 · see citing works
Boas, S. M., Joyce, K. L., & Cowell, R. M. (2021) · Antioxidants · doi:10.3390/antiox11010008 · Cited by 69 · see citing works
Ribarič, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23063245 · Cited by 72 · see citing works
Induced pluripotent stem cells: a tool for modeling Parkinson’s disease
Bose, A., Petsko, G. A., & Studer, L. (2022) · Trends in Neurosciences · doi:10.1016/j.tins.2022.05.001 · Cited by 70 · see citing works
Parfitt, G. M., Coccia, E., Goldman, C., Whitney, K. R., Reyes, R., Sarrafha, L., Nam, K. H., Sohail, S., Jones, D. R., Crary, J. F., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-44732-2 · Cited by 70 · see citing works
Insights into the pathogenesis of multiple system atrophy: focus on glial cytoplasmic inclusions
Kaji, S., Maki, T., Ishimoto, T., Yamakado, H., & Takahashi, R. (2020) · Translational Neurodegeneration · doi:10.1186/s40035-020-0185-5 · Cited by 68 · see citing works
Neuromodulation of Glial Function During Neurodegeneration
Stevenson, R., Samokhina, E., Rossetti, I., Morley, J. W., & Buskila, Y. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00278 · Cited by 68 · see citing works
An update on human astrocytes and their role in development and disease
de Majo, M., Koontz, M., Rowitch, D. H., & Ullian, E. M. (2020) · Glia · doi:10.1002/glia.23771 · Cited by 66 · see citing works
Astrocytes and microglia in neurodegenerative diseases: Lessons from human in vitro models
Franklin, H., Clarke, B. E., & Patani, R. (2021) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2020.101973 · Cited by 66 · see citing works
Smith, L. J., Lee, C., Menozzi, E., & Schapira, A. H. V. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.971252 · Cited by 65 · see citing works
Unique signatures of stress-induced senescent human astrocytes
Simmnacher, K., Krach, F., Schneider, Y., Alecu, J. E., Mautner, L., Klein, P., Roybon, L., Prots, I., Xiang, W., & Winner, B. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113466 · Cited by 63 · see citing works
Glia in Neurodegeneration: The Housekeeper, the Defender and the Perpetrator
Sheeler, C. A., Rosa, J. S., Ferro, A., McAdams, B. D., Borgenheimer, E., & Cvetanović, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239188 · Cited by 61 · see citing works
Pons‐Espinal, M., Blasco-Agell, L., Fernández‐Carasa, I., Andrés‐Benito, P., di Domenico, A., Richaud‐Patín, Y., Baruffi, V., Marruecos, L., Espinosa, L., Garrido, A., et al. (2024) · JCI Insight · doi:10.1172/jci.insight.163359 · Cited by 66 · see citing works
Self-citationWasielewska, J. M., & White, A. R. (2022) · Pharmaceutical Research · doi:10.1007/s11095-022-03185-2 · Cited by 63 · see citing works
Gatto, N., Dos Santos Souza, C., Shaw, A. C., Bell, S. M., Myszczynska, M. A., Powers, S., Meyer, K., Castelli, L. M., Karyka, E., Mortiboys, H., et al. (2021) · Aging Cell · doi:10.1111/acel.13281 · Cited by 58 · see citing works
Reduced astrocytic reactivity in human brains and midbrain organoids with PRKN mutations
Kano, M., Takanashi, M., Oyama, G., Yoritaka, A., Hatano, T., Shiba‐Fukushima, K., Nagai, M., Nishiyama, K., Hasegawa, K., Inoshita, T., et al. (2020) · npj Parkinson s Disease · doi:10.1038/s41531-020-00137-8 · Cited by 57 · see citing works
Single-cell brain atlas of Parkinson's disease mouse model
Zhong, J., Tang, G., Zhu, J., Wu, W., Li, G., Lin, X., Liang, L., Chai, C., Zeng, Y., Wang, F., et al. (2021) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2021.01.003 · Cited by 57 · see citing works
Bowles, K. R., Pugh, D. A., Liu, Y., Patel, T., Renton, A. E., Bandrés‐Ciga, S., Gan‐Or, Z., Heutink, P., Siitonen, A., Bertelsen, S. E., et al. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00551-x · Cited by 55 · see citing works
Dong, A.-Q., Yang, Y., Jiang, S.-M., Yao, X., Qi, D., Mao, C., Cheng, X.-Y., Wang, F., Hu, L., & Liu, C. (2022) · Acta Pharmacologica Sinica · doi:10.1038/s41401-022-00951-1 · Cited by 55 · see citing works
Bang, S., Lee, S., Choi, N., & Kim, H. N. (2021) · Advanced Healthcare Materials · doi:10.1002/adhm.202002119 · Cited by 55 · see citing works
3D hydrogel models of the neurovascular unit to investigate blood–brain barrier dysfunction
Potjewyd, G., Kellett, K. A. B., & Hooper, N. M. (2021) · Neuronal Signaling · doi:10.1042/ns20210027 · Cited by 54 · see citing works
Neurodegeneration cell per cell
Balusu, S., Praschberger, R., Lauwers, E., Strooper, B. D., & Verstreken, P. (2023) · Neuron · doi:10.1016/j.neuron.2023.01.016 · Cited by 51 · see citing works
Degl’Innocenti, E., & Dell’Anno, M. T. (2023) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2023.1130729 · Cited by 55 · see citing works
The Involvement of Neuroinflammation in the Onset and Progression of Parkinson’s Disease
Jurcău, A., Andronie-Cioară, F. L., Nistor-Cseppento, C. D., Pașcalău, N., Rus, M., Vasca, E., & Jurcău, M. C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914582 · Cited by 56 · see citing works
Jellinger, K. A. (2019) · Journal of Neural Transmission · doi:10.1007/s00702-019-02028-6 · Cited by 55 · see citing works
Astrocytic modulation of neuronal signalling
Purushotham, S. S., & Buskila, Y. (2023) · Frontiers in Network Physiology · doi:10.3389/fnetp.2023.1205544 · Cited by 54 · see citing works
Brain 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 52 · see citing works
The role of glia in protein aggregation
Li, Q., & Haney, M. S. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105015 · Cited by 51 · see citing works
Neurons and Glia Interplay in α-Synucleinopathies
Mavroeidi, P., & Xilouri, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094994 · Cited by 52 · see citing works
Role of SNAREs in Unconventional Secretion—Focus on the VAMP7-Dependent Secretion
Vats, S., & Galli, T. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.884020 · Cited by 51 · see citing works
Role of Astrocytes in Parkinson’s Disease Associated with Genetic Mutations and Neurotoxicants
Kim, S., Pajarillo, E. A. B., Nyarko‐Danquah, I., Aschner, M., & Lee, E.-S. (2023) · Cells · doi:10.3390/cells12040622 · Cited by 50 · see citing works
Extracellular clusterin limits the uptake of α‐synuclein fibrils by murine and human astrocytes
Filippini, A., Mutti, V., Faustini, G., Longhena, F., Ramazzina, I., Rizzi, F., Kaganovich, A., Roosen, D. A., Landeck, N., Duffy, M. F., et al. (2020) · Glia · doi:10.1002/glia.23920 · Cited by 48 · see citing works
Khawaja, R. R., Martín‐Segura, A., Santiago‐Fernández, O., Sereda, R., Lindenau, K. L., McCabe, M., Macho‐González, A., Jafari, M., Scrivo, A., Gómez‐Sintes, R., et al. (2025) · Nature Aging · doi:10.1038/s43587-024-00799-6 · Cited by 49 · see citing works
Self-citationPolychlorinated biphenyls induce oxidative stress and metabolic responses in astrocytes
McCann, M. S., Fernandez, H. R., Flowers, S. A., & Maguire‐Zeiss, K. A. (2021) · NeuroToxicology · doi:10.1016/j.neuro.2021.07.001 · Cited by 49 · see citing works
Human iPSC-Based Modeling of Central Nerve System Disorders for Drug Discovery
Lu, Q., & Julia, T. C. W. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031203 · Cited by 48 · see citing works
Neyrinck, K., Daele, J. V. D., Vervliet, T., Smedt, J. D., Wierda, K. D. B., Nijs, M., Vanbokhoven, T., D’hondt, A., Planque, M., Fendt, S., et al. (2021) · Stem Cell Reviews and Reports · doi:10.1007/s12015-021-10179-x · Cited by 46 · see citing works
Extracellular Alpha-Synuclein: Mechanisms for Glial Cell Internalization and Activation
Chavarría, C., Ivagnes, R., & Souza, J. M. (2022) · Biomolecules · doi:10.3390/biom12050655 · Cited by 47 · see citing works
Sen, T., & Thummer, R. P. (2022) · Neurotoxicity Research · doi:10.1007/s12640-022-00564-w · Cited by 50 · see citing works
Muddapu, V. R., & Chakravarthy, V. S. (2021) · Scientific Reports · doi:10.1038/s41598-021-81185-9 · Cited by 47 · see citing works
From cell lines to pluripotent stem cells for modelling Parkinson's Disease
Ferrari, E. S., Cardinale, A., Picconi, B., & Gardoni, F. (2020) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2020.108741 · Cited by 44 · see citing works
Impact of Chaperone-Mediated Autophagy in Brain Aging: Neurodegenerative Diseases and Glioblastoma
Auzmendi-Iriarte, J., & Matheu, A. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.630743 · Cited by 45 · see citing works
Alpha-Synuclein and the Endolysosomal System in Parkinson’s Disease: Guilty by Association
Teixeira, M., Sheta, R., Idi, W., & Oueslati, A. (2021) · Biomolecules · doi:10.3390/biom11091333 · Cited by 43 · see citing works
Raikwar, S. P., Kikkeri, N. S., Sakuru, R. C., Saeed, D., Zahoor, H., Premkumar, K., Mentor, S., Thangavel, R., Dubova, I., Ahmed, M. E., et al. (2019) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-019-09849-y · Cited by 47 · see citing works
Kanno, H., Handa, K., Murakami, T., Aizawa, T., & Ozawa, H. (2022) · Cells · doi:10.3390/cells11071205 · Cited by 44 · see citing works
Olsen, A. L., & Feany, M. Β. (2019) · Glia · doi:10.1002/glia.23671 · Cited by 42 · see citing works
Patient-Derived Midbrain Organoids to Explore the Molecular Basis of Parkinson's Disease
Galet, B., Cheval, H., & Ravassard, P. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.01005 · Cited by 45 · see citing works
Labib, D., Wang, Z., Prakash, P. S., Zimmer, M., Smith, M. D., Frazel, P. W., Barbar, L., Sapar, M. L., Calabresi, P. A., Peng, J., et al. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.870085 · Cited by 42 · see citing works
Jusop, A. S., Thanaskody, K., Tye, G. J., Dass, S. A., Zaman, W. S. W. K., & Nordin, F. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1173433 · Cited by 42 · see citing works
Novel human iPSC models of neuroinflammation in neurodegenerative disease and regenerative medicine
Summers, R. A., Fagiani, F., Rowitch, D. H., Absinta, M., & Reich, D. S. (2024) · Trends in Immunology · doi:10.1016/j.it.2024.08.004 · Cited by 39 · see citing works
Comprehensive Perspectives on Experimental Models for Parkinson’s Disease
Ke, M., Chong, C., Zhu, Q., Zhang, K., Cai, C.-Z., Lu, J., Qin, D., & Su, H. (2021) · Aging and Disease · doi:10.14336/ad.2020.0331 · Cited by 40 · see citing works
Utilising Induced Pluripotent Stem Cells in Neurodegenerative Disease Research: Focus on Glia
Albert, K., Niskanen, J., Kälvälä, S., & Lehtonen, Š. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094334 · Cited by 39 · see citing works
Therapeutic Potential of Astrocyte Transplantation
Hastings, N., Kuan, W., Osborne, A., & Kotter, M. (2022) · Cell Transplantation · doi:10.1177/09636897221105499 · Cited by 38 · see citing works
Vieira, R., Mariani, J. N., Huynh, N. P. T., Stephensen, H. J. T., Solly, R., Tate, A., Schanz, S. J., Cotrupi, N., Mousaei, M., Jon Sporring, A., et al. (2023) · Nature Biotechnology · doi:10.1038/s41587-023-01798-5 · Cited by 38 · see citing works
- Authors
- di Domenico, A., Carola, G., Calatayud, C., Pons-Espinal, M., Muñoz, J. P., Richaud-Patin, Y., Fernandez-Carasa, I., Gut, M., Faella, A., Parameswaran, J., Soriano, J., Ferrer, I., Tolosa, E., Zorzano, A., Cuervo, A. M., Raya, A., & Consiglio, A.
- Affiliations
- Bellvitge University Hospital (ES)
- Institute for Research in Biomedicine (ES)
- Centro Nacional de Análisis Genómico (ES)
- Universitat de Barcelona (ES)
- Biomedical Research Networking Center on Neurodegenerative Diseases (ES)
- Corresponding author
- Consiglio, Antonella
- ORCID
- Venue
- Stem Cell Reports
- Publisher
- Elsevier BV
- Published
- 2019-02
- Volume
- 12
- Issue
- 2
- Pages
- 213-229
- ISSN
- 2213-6711 (ISSN-L)
- PMC
- PMC6372974
- OpenAlex
- W2911036111
- Cited by
- 372
- References
- 49
- Citations by year
- 2026: 32 · 2025: 38 · 2024: 44 · 2023: 45 · 2022: 65 · 2021: 69 · 2020: 53 · 2019: 26
- FWCI
- 36.04
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Stem Cell Reports (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Dipòsit Digital de la Universitat de Barcelona (Universitat de Barcelona) (publishedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Institutional Research Information System (Università degli Studi di Brescia) (submittedVersion)
- Repositori digital de la UPF (Universitat Pompeu Fabra) (submittedVersion, cc-by)
- Funders
- Agència de Gestió d'Ajuts Universitaris i de Recerca (2014-SGR-878, 2017-SGR-899)
- Ministerio de Educación, Cultura y Deporte (BES-2014-069603, FPU12/03332)
- Ministerio de Economía y Competitividad (BFU2016-80870-P, FIS2016-78507-C2-2-P, SAF2015-69706-R)
- Instituto de Salud Carlos III
- European Regional Development Fund (RD16/0011/0024)
- Generalitat de Catalunya
- European Research Council (2012-StG-311736-PD-HUMMODEL)
- Topics
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Pluripotent Stem Cells Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Parkinson's disease, astrocytes, non-cell autonomous neurodegeneration, induced pluripotent stem cell-derived astrocytes, dopaminergic neurons, ventral midbrain, LRRK2 G2019S, familial Parkinson's disease, alpha-synuclein accumulation, chaperone-mediated autophagy, macroautophagy, neuron-glia interactions
- MeSH terms
- Leucine-Rich Repeat Serine-Threonine Protein Kinase-2, Astrocytes, Autophagy, Cell Differentiation, Cells, Cultured, Humans, Mesencephalon, Neuroglia, Parkinson Disease, Phenotype, Coculture Techniques, alpha-Synuclein, Induced Pluripotent Stem Cells, Dopaminergic Neurons
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