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Using Human iPSC-Derived Neurons to Model TAU Aggregation
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Alzheimer's disease and frontotemporal dementia are amongst the most common forms of dementia characterized by the formation and deposition of abnormal TAU in the brain. In order to develop a translational human TAU aggregation model suitable for screening, we transduced TAU harboring the pro-aggregating P301L mutation into control hiPSC-derived neural progenitor cells followed by differentiation into cortical neurons. TAU aggregation and phosphorylation was quantified using AlphaLISA technology. Although no spontaneous aggregation was observed upon expressing TAU-P301L in neurons, seeding with preformed aggregates consisting of the TAU-microtubule binding repeat domain triggered robust TAU aggregation and hyperphosphorylation already after 2 weeks, without affecting general cell health. To validate our model, activity of two autophagy inducers was tested. Both rapamycin and trehalose significantly reduced TAU aggregation levels suggesting that iPSC-derived neurons allow for the generation of a biologically relevant human Tauopathy model, highly suitable to screen for compounds that modulate TAU aggregation.
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iPSC-derived neurons or NGN2-induced neurons have been unable to produce the 4R Tau isoform found in adult human brains; only the fetal 0N3R splicing isoform is produced, even after one year of differentiation.
“One of the significant hurdles in modeling AD with iPSC-derived neurons or NGN2-induced neurons for the past decade has been their inability to produce the 4R Tau isoform found in adult human brains [19–22]; only the fetal 0N3R splicing isoform is produced, even after one year of differentiation [19].”
From Elevated SGK1 increases Tau phosphorylation and microtubule instability in Alzheimer’s patient-derived cortical neurons (2026) · cites this paper as [21]
The Results report that control iPSC-derived cortical neurons expressed only embryonic 0N3R TAU around day 90, and the Discussion says 4R TAU was undetectable after more than 90 days. The paper does not establish that this persists after one year or address NGN2-induced neurons; its Discussion instead notes reports of mature TAU isoforms after extended culture. Page numbers are unavailable in our copy. (LLM, conf=0.88)
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Cites
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676
Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498
Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492
Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders
Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174
Wittig, I., Braun, H., & Schägger, H. (2006) · Nature Protocols · doi:10.1038/nprot.2006.62 · Cited by 1,741
A three-dimensional human neural cell culture model of Alzheimer’s disease
Choi, S. H., Kim, Y. H., Hebisch, M., Sliwinski, C., Lee, S., D’Avanzo, C., Chen, H., Hooli, B., Asselin, C., Muffat, J., et al. (2014) · Nature · doi:10.1038/nature13800 · Cited by 1,195
Goedert, M., Spillantini, M. G., Cairns, N. J., & Crowther, R. A. (1992) · Neuron · doi:10.1016/0896-6273(92)90117-v · Cited by 1,122
Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau.
Drechsel, D. N., Hyman, A. A., Cobb, M. H., & Kirschner, M. W. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.10.1141 · Cited by 1,011
Shi, Y., Kirwan, P., & Livesey, F. J. (2012) · Nature Protocols · doi:10.1038/nprot.2012.116 · Cited by 972
Potential therapeutic applications of autophagy
Rubinsztein, D. C., Gestwicki, J. E., Murphy, L. O., & Klionsky, D. J. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2272 · Cited by 862
Alonso, A. D. C., Zaidi, T., Novak, M., Grundke-Iqbal, I., & Iqbal, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.121119298 · Cited by 827
Rapamycin alleviates toxicity of different aggregate-prone proteins
Berger, Z., Ravikumar, B., Menzies, F. M., Oroz, L. G., Underwood, B. R., Pangalos, M. N., Schmitt, I., Wullner, U., Evert, B. O., O'Kane, C. J., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddi458 · Cited by 657
Seeding of Normal Tau by Pathological Tau Conformers Drives Pathogenesis of Alzheimer-like Tangles
Guo, J. L., & Lee, V. M.-Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209296 · Cited by 636
Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205
Goedert, M., Jakes, R., & Vanmechelen, E. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)11484-e · Cited by 608
Developmentally regulated expression of specific tau sequences
Kosik, K. S., Orecchio, L. D., Bakalis, S., & Neve, R. L. (1989) · Neuron · doi:10.1016/0896-6273(89)90077-9 · Cited by 598
Trans-cellular Propagation of Tau Aggregation by Fibrillar Species
Kfoury, N., Holmes, B. B., Jiang, H., Holtzman, D. M., & Diamond, M. I. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.346072 · Cited by 552
Inducible Expression of Tau Repeat Domain in Cell Models of Tauopathy
Khlistunova, I., Biernat, J., Wang, Y., Pickhardt, M., von Bergen�, M., Gažová, Z., Mandelkow�, E., & Mandelkow, E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507753200 · Cited by 366
Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy
Schaeffer, V., Lavenir, I., Ozcelik, S., Tolnay, M., Winkler, D. T., & Goedert, M. (2012) · Brain · doi:10.1093/brain/aws143 · Cited by 343
Promotion of Hyperphosphorylation by Frontotemporal Dementia Tau Mutations
Alonso, A. D. C., Mederlyova, A., Novák, M., Grundke, I., & Iqbal, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405131200 · Cited by 330
Tau exon 10 alternative splicing and tauopathies
Liu, F., & Gong, C.-X. (2008) · Molecular Neurodegeneration · doi:10.1186/1750-1326-3-8 · Cited by 323
Autophagic degradation of tau in primary neurons and its enhancement by trehalose
Krüger, U., Wang, Y., Kumar, S., & Mandelkow, E.-M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.009 · Cited by 297
Synaptic Contacts Enhance Cell-to-Cell Tau Pathology Propagation
Calafate, S., Buist, A., Miśkiewicz, K., Vijayan, V. A., Daneels, G., Strooper, B. D., de Wit, J., Verstreken, P., & Moechars, D. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.043 · Cited by 277
Self-citationKanaan, N. M., Morfini, G. A., LaPointe, N. E., Pigino, G. F., Patterson, K. R., Song, Y., Andreadis, A., Fu, Y., Brady, S. T., & Binder, L. I. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0560-11.2011 · Cited by 273
Rapamycin attenuates the progression of tau pathology in P301S tau transgenic mice.
Ozcelik, S., Fraser, G., Castets, P., Schaeffer, V., Skachokova, Z., Breu, K., Clavaguera, F., Sinnreich, M., Kappos, L., Goedert, M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062459 · Cited by 226
Peeraer, E., Bottelbergs, A., Van Kolen, K., Stancu, I.-C., Vasconcelos, B., Mahieu, M., Duytschaever, H., Ver Donck, L., Torremans, A., Sluydts, E., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.08.032 · Cited by 214
Iovino, M., Agathou, S., González-Rueda, A., Del Castillo Velasco-Herrera, M., Borroni, B., Alberici, A., Lynch, T., O’Dowd, S., Geti, I., Gaffney, D., et al. (2015) · Brain · doi:10.1093/brain/awv222 · Cited by 155
Sposito, T., Preza, E., Mahoney, C. J., Setó-Salvia, N., Ryan, N. S., Morris, H. R., Arber, C., Devine, M. J., Houlden, H., Warner, T. T., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv246 · Cited by 148
AlphaLISA Immunoassay Platform— The “No-Wash” High-Throughput Alternative to ELISA
Bielefeld-Sévigny, M. (2009) · Assay and Drug Development Technologies · doi:10.1089/adt.2009.9996 · Cited by 143
Fong, H., Wang, C., Knoferle, J., Walker, D., Balestra, M. E., Tong, L. M., Leung, L., Ring, K. L., Seeley, W. W., Karydas, A., et al. (2013) · Stem Cell Reports · doi:10.1016/j.stemcr.2013.08.001 · Cited by 122
Guo, J., & Lee, V. M. ‐. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.051 · Cited by 117
Embryonic Stem Cell–Based Modeling of Tau Pathology in Human Neurons
Mertens, J., Stüber, K., Poppe, D., Doerr, J., Ladewig, J., Brüstle, O., & Koch, P. (2013) · American Journal Of Pathology · doi:10.1016/j.ajpath.2013.01.043 · Cited by 47
Human stem cell-derived neurons: a system to study human tau function and dysfunction
Iovino, M., Patani, R., Watts, C., Chandran, S., & Spillantini, M. G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013947 · Cited by 40
Szekeres, P. G., Leong, K., Day, T. A., Kingston, A. E., & Karran, E. H. (2008) · SLAS DISCOVERY · doi:10.1177/1087057107312778 · Cited by 32
Split GFP Complementation Assay for Quantitative Measurement of Tau Aggregation In Situ
Chun, W., Waldo, G. S., & Johnson, G. V. W. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-744-0_9 · Cited by 20
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Propagation of Tau aggregates and neurodegeneration
Goedert, M., Eisenberg, D. S., & Crowther, R. A. (2017) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-072116-031153 · Cited by 632
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TCW, J., Wang, M., Pimenova, A. A., Bowles, K. R., Hartley, B. J., Lacin, E., Machlovi, S. I., Abdelaal, R., Karch, C. M., Phatnani, H., et al. (2017) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.06.018 · Cited by 435
MAPT mutations, tauopathy, and mechanisms of neurodegeneration
Strang, K. H., Golde, T. E., & Giasson, B. I. (2019) · Laboratory Investigation · doi:10.1038/s41374-019-0197-x · Cited by 424
Like prions: the propagation of aggregated tau and α-synuclein in neurodegeneration
Goedert, M., Masuda-Suzukake, M., & Falcon, B. (2017) · Brain · doi:10.1093/brain/aww230 · Cited by 323
Stem cell models of Alzheimer’s disease: progress and challenges
Arber, C., Lovejoy, C., & Wray, S. (2017) · Alzheimer's Research & Therapy · doi:10.1186/s13195-017-0268-4 · Cited by 143
Galectin-8–mediated selective autophagy protects against seeded tau aggregation
Falcon, B., Noad, J., McMahon, H. T., Randow, F., & Goedert, M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.809293 · Cited by 119
Ercan-Herbst, E., Ehrig, J., Schöndorf, D. C., Behrendt, A., Klaus, B., Gomez Ramos, B., Prat Oriol, N., Weber, C., & Ehrnhoefer, D. E. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0823-2 · Cited by 101
Bell, M. J., & Zempel, H. (2021) · Reviews in the Neurosciences · doi:10.1515/revneuro-2020-0152 · Cited by 92
Hefti, M. M., Farrell, K. W., Kim, S., Bowles, K. R., Fowkes, M. E., Raj, T., & Crary, J. F. (2018) · PLoS ONE · doi:10.1371/journal.pone.0195771 · Cited by 94
Medda, X., Mertens, L., Versweyveld, S., Diels, A., Barnham, L., Bretteville, A., Buist, A., Verheyen, A., Royaux, I. E., Ebneth, A., et al. (2016) · SLAS DISCOVERY · doi:10.1177/1087057116638029 · Cited by 74
Self-citationLo, C. H., Lim, C. K., Ding, Z., Wickramasinghe, S. P., Braun, A. R., Ashe, K. H., Rhoades, E. R., Thomas, D. D., & Sachs, J. N. (2019) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2019.06.4954 · Cited by 65
Verheyen, A., Diels, A., Reumers, J., Hoorde, K. V., den Wyngaert, I. V., d’Ydewalle, C. V. O., Bondt, A. D., Kuijlaars, J., Muynck, L. D., Hoogt, R. D., et al. (2018) · Stem Cell Reports · doi:10.1016/j.stemcr.2018.06.022 · Cited by 67
Self-citationCapano, L. S., Sato, C., Ficulle, E., Yu, A., Horie, K., Kwon, J.-S., Burbach, K. F., Barthélemy, N. R., Fox, S. G., Karch, C. M., et al. (2022) · Cell Stem Cell · doi:10.1016/j.stem.2022.04.018 · Cited by 65
Novel human neuronal tau model exhibiting neurofibrillary tangles and transcellular propagation
Reilly, P., Winston, C. N., Baron, K. R., Trejo, M., Rockenstein, E. M., Akers, J. C., Kfoury, N., Diamond, M. I., Masliah, E., Rissman, R. A., et al. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.06.005 · Cited by 61
Katsinelos, T., Tuck, B. J., Mukadam, A. S., & McEwan, W. A. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01139 · Cited by 46
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Rickner, H., Jiang, L., Hong, R., O’Neill, N. K., Mojica, C. A., Snyder, B. J., Zhang, L., Shaw, D., Medalla, M., Wolozin, B. L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34005-1 · Cited by 43
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TCW, J. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.01.043 · Cited by 39
Gurwitz, D. (2016) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2016.18.3/dgurwitz · Cited by 39
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Carosi, J. M., Hein, L. K., van den Hurk, M., Adams, R., Milky, B., Singh, S., Bardy, C., Denton, D., Kumar, S., & Sargeant, T. J. (2020) · Autophagy · doi:10.1080/15548627.2020.1821545 · Cited by 41
Jacquet, A. D. R., Denis, H. L., Cicchetti, F., & Alpaugh, M. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-00999-7 · Cited by 36
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Shan, X., Zhang, A., Rezzonico, M. G., Tsai, M., Sánchez-Priego, C., Zhang, Y., Chen, M. B., Choi, M., López, J. M. A., Phu, L., et al. (2024) · Cell Reports Methods · doi:10.1016/j.crmeth.2024.100858 · Cited by 37
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Bell, M., Bachmann, S., Klimek, J., Langerscheidt, F., & Zempel, H. (2021) · Neuroscience · doi:10.1016/j.neuroscience.2021.01.041 · Cited by 34
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Manos, J. D., Preiss, C. N., Venkat, N., Tamm, J., Reinhardt, P., Kwon, T., Wu, J., Winter, A. D., Jahn, T. R., Yanamandra, K., et al. (2022) · iScience · doi:10.1016/j.isci.2021.103658 · Cited by 36
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Amin, N., Tan, X., Ren, Q., Zhu, N., Botchway, B. O. A., Hu, Z., & Fang, M. (2019) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2019.109674 · Cited by 36
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Sharma, N. S., Karan, A., Lee, D.-H., Yan, Z., & Xie, J. (2021) · Advanced NanoBiomed Research · doi:10.1002/anbr.202100097 · Cited by 31
Kopach, O., Esteras, N., Wray, S., Abramov, A. Y., & Rusakov, D. A. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04007-w · Cited by 25
Ritchie, L., Tate, R. J., Chamberlain, L. H., Robertson, G., Zagnoni, M., Sposito, T., Wray, S., Wright, J. A., Bryant, C. E., Gay, N. J., et al. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.02.025 · Cited by 25
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Jiménez-Moreno, N., Stathakos, P., Caldwell, M. A., & Lane, J. D. (2017) · Cells · doi:10.3390/cells6030024 · Cited by 22
Seranova, E., Palhegyi, A. M., Verma, S., Dimova, S., Lasry, R., Naama, M., Sun, C., Barrett, T. G., Rosenstock, T. R., Kumar, D., et al. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.024 · Cited by 20
Hromádková, L., Siddiqi, M. K., Liu, H., & Safar, J. (2022) · Cells · doi:10.3390/cells11192997 · Cited by 19
Virdee, J. K., Sarò, G., Fouillet, A., Findlay, J. D., Ferreira, F. M., Eversden, S., O’Neill, M. J., Wolak, J., & Ursu, D. (2017) · Scientific Reports · doi:10.1038/s41598-017-15171-5 · Cited by 19
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Hawkins, K., & Duchen, M. R. (2019) · World Journal of Stem Cells · doi:10.4252/wjsc.v11.i5.236 · Cited by 18
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Saleem, K., Xiao, Z., Zhu, B., Ren, Y., Yan, Z., & Feng, J. (2026) · Molecular Psychiatry · doi:10.1038/s41380-025-03225-4 · Cited by 10
Sala‐Jarque, J., Zimkowska, K., Ávila, J., Ferrer, I., & del Rı́o, J. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911527 · Cited by 11
Li, S., Roy, E. R., Wang, Y., Watkins, T. A., & Cao, W. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03720-1 · Cited by 14
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Labra, S. R., Compher, J., Prabhavalkar, A., Almaraz, M., Kwong, C. C., Baal, C., Talantova, M. V., Dolatabadi, N., Piña‐Sanz, J., Wang, Y., et al. (2026) · Advanced Science · doi:10.1002/advs.202514783 · Cited by 9
Jiang, H., Xiao, Z., Saleem, K., Zhong, P., Li, L., Chhetri, G., Li, P., Jiang, Z., Yan, Z., & Feng, J. (2025) · Journal of Alzheimer’s Disease · doi:10.1177/13872877251334831 · Cited by 6
Marreiro, A. F. D., Kolen, K. V., Sousa, C., Temmerman, L., Vasconcelos, B., Rodriguez, R. C., van Weering, J. R. T., Dam, D. V., Deyn, P. P. D., Apetri, A. C., et al. (2020) · BMC Molecular and Cell Biology · doi:10.1186/s12860-020-00320-y · Cited by 6
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Dannert, A., Schulz, N., Klimmt, J., Knez, L., Groschup, B., Gonçalves, C. C., Carraro, C., Schifferer, M., Brendel, M., & Paquet, D. (2026) · Science Translational Medicine · doi:10.1126/scitranslmed.adu9845 · Cited by 6
Bahnassawy, L., Nicolaisen, N., Untucht, C., Mielich‐Süss, B., Reinhardt, L., Ried, J. S., Morawe, M. P., Geist, D., Finck, A., Käfer, E., et al. (2023) · SLAS DISCOVERY · doi:10.1016/j.slasd.2023.12.009 · Cited by 5
Self-citationWauters, E., Sleegers, K., Cruts, M., & Broeckhoven, C. V. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805120-7.00009-9 · Cited by 6
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Hallinan, G. I., Pitera, A. P., Patel, P., West, J. J., & Deinhardt, K. (2018) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2018.09.032 · Cited by 4
Baud, A., Little, D., Teo, Q. W., Heywood, W., Gissen, P., & Mills, K. A. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00831 · Cited by 4
Li, S., Roy, E. R., Wang, Y., Watkins, T. A., & Cao, W. (2023) · Research Square · doi:10.21203/rs.3.rs-2617457/v1 · Cited by 3
Wasielewska, J. M., Bajracharya, R., Johnston, R. L., Chaves, J. C. S., Pébay, A., Oikari, L. E., Götz, J., Nisbet, R. M., & White, A. R. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.24.563706 · Cited by 2
Drug Discovery in Induced Pluripotent Stem Cell Models
Bourque, K., Mnasri, N., Jones-Tabah, J., Martins-Cannavino, K., & Hébert, T. E. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00049-9 · Cited by 1
Roose, S. K., Mizukami, Y., Muto, J., Okano, H., Nakamura, M., & Nagoshi, N. (2025) · Regenerative Therapy · doi:10.1016/j.reth.2025.06.012 · Cited by 2
Neurodegeneration and the Ordered Assembly of Tau
Goedert, M. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811304-2.00004-3 · Cited by 3
A Human Neuron/Astrocyte Co‐culture to Model Seeded and Spontaneous Intraneuronal Tau Aggregation
Batenburg, K. L., Rohde, S. K., Cornelissen‐Steijger, P., Breeuwsma, N., Heine, V. M., & Scheper, W. (2023) · Current Protocols · doi:10.1002/cpz1.900 · Cited by 2
Single cell transcriptomic profiling of tauopathy in a novel 3D neuron-astrocyte coculture modelPreprint
Rickner, H., Jiang, L., Hong, R., O’Neill, N. K., Mojica, C. A., Snyder, B. J., Zhang, L., Shaw, D., Medalla, M., Wolozin, B. L., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.05.03.490513 · Cited by 1
The endolysosomal system in neuronal physiology and pathology
Sanchez, S. V. (2019)
Modeling of Alzheimer’s Disease and Outlooks for its Therapy Using Induced Pluripotent Stem Cells
Хаспеков, Л. Г. (2019) · Neurochemical Journal · doi:10.1134/s181971241902003x
Brown, C. M., Brooks, J. K., Kelly, L., Vroom, M. M., Longo, M., Dodart, J., Carare, R. O., & Boyd, J. D. (2025) · Brain Pathology · doi:10.1111/bpa.70056
Marreiro, A. F. D., Kolen, K. V., Sousa, C., Temmerman, L., Vasconcelos, B., Rodriguez, R. C., van Weering, J. R. T., Dam, D. V., De Deyn, P. P., Apetri, A. C., et al. (2020) · Figshare · doi:10.6084/m9.figshare.13233265
Mothes, T., Portal, B., Konstantinidis, E., Eltom, K., Libard, S., Streubel-Gallasch, L., Ingelsson, M., Rostami, J., Lindskog, M., & Erlandsson, A. (2024) · Figshare · doi:10.6084/m9.figshare.26598035
Mothes, T., Portal, B., Konstantinidis, E., Eltom, K., Libard, S., Streubel-Gallasch, L., Ingelsson, M., Rostami, J., Lindskog, M., & Erlandsson, A. (2024) · Figshare · doi:10.6084/m9.figshare.26598053
Mothes, T., Portal, B., Konstantinidis, E., Eltom, K., Libard, S., Streubel-Gallasch, L., Ingelsson, M., Rostami, J., Lindskog, M., & Erlandsson, A. (2024) · Figshare · doi:10.6084/m9.figshare.26598050
Mothes, T., Portal, B., Konstantinidis, E., Eltom, K., Libard, S., Streubel-Gallasch, L., Ingelsson, M., Rostami, J., Lindskog, M., & Erlandsson, A. (2024) · Figshare · doi:10.6084/m9.figshare.26598032
Additional file 1 of A 3D human co-culture to model neuron-astrocyte interactions in tauopathies
Batenburg, K. L., Sestito, C., Cornelissen‐Steijger, P., van Weering, J. R. T., Price, L., Heine, V. M., & Scheper, W. (2024) · Figshare · doi:10.6084/m9.figshare.26570704
Marreiro, A. F. D., Kolen, K. V., Sousa, C., Temmerman, L., Vasconcelos, B., Rodriguez, R. C., van Weering, J. R. T., Dam, D. V., De Deyn, P. P., Apetri, A. C., et al. (2020) · Figshare · doi:10.6084/m9.figshare.13233262
Additional file 2 of A 3D human co-culture to model neuron-astrocyte interactions in tauopathies
Batenburg, K. L., Sestito, C., Cornelissen‐Steijger, P., van Weering, J. R. T., Price, L., Heine, V. M., & Scheper, W. (2024) · Figshare · doi:10.6084/m9.figshare.26570707
Mothes, T., Portal, B., Konstantinidis, E., Eltom, K., Libard, S., Streubel-Gallasch, L., Ingelsson, M., Rostami, J., Lindskog, M., & Erlandsson, A. (2024) · Figshare · doi:10.6084/m9.figshare.26598044
Mothes, T., Portal, B., Konstantinidis, E., Eltom, K., Libard, S., Streubel-Gallasch, L., Ingelsson, M., Rostami, J., Lindskog, M., & Erlandsson, A. (2024) · Figshare · doi:10.6084/m9.figshare.26598047
Mothes, T., Portal, B., Konstantinidis, E., Eltom, K., Libard, S., Streubel-Gallasch, L., Ingelsson, M., Rostami, J., Lindskog, M., & Erlandsson, A. (2024) · Figshare · doi:10.6084/m9.figshare.26598038
Mothes, T., Portal, B., Konstantinidis, E., Eltom, K., Libard, S., Streubel-Gallasch, L., Ingelsson, M., Rostami, J., Lindskog, M., & Erlandsson, A. (2024) · Figshare · doi:10.6084/m9.figshare.26598029
Mothes, T., Portal, B., Konstantinidis, E., Eltom, K., Libard, S., Streubel-Gallasch, L., Ingelsson, M., Rostami, J., Lindskog, M., & Erlandsson, A. (2024) · Figshare · doi:10.6084/m9.figshare.26598041
From mice to clinical relevance: humanizing neuroscience with human-based model systems
Bak, A., van Loo, K. M. J., Kronenberg‐Versteeg, D., & Koch, H. (2026) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2026.1776439
Siddique, I. A., Hong, M., & Bitan, G. (2026) · Topics in medicinal chemistry · doi:10.1007/7355_2026_189
Thakur, A., Sharma, R. R., Kumari, S., Prakash, D., & Devi, A. S. (2026) · Inflammopharmacology · doi:10.1007/s10787-026-02371-7
Lipka, J., Shan, X., Zhang, Q., Dutka, P., Phu, L., Johnson, M. C., Wendorff, T. J., Adrian, M., Biton, A., Sun, D., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.07.749799
Metadata
- Authors
- Verheyen, A., Diels, A., Dijkmans, J., Oyelami, T., Meneghello, G., Mertens, L., Versweyveld, S., Borgers, M., Buist, A., Peeters, P., & Cik, M.
- Affiliations
- Janssen (Belgium) (BE)
- Corresponding author
- Verheyen, An
- Venue
- PLOS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2015-12-31
- Volume
- 10
- Issue
- 12
- Pages
- e0146127
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC4697850
- OpenAlex
- W2201698544
- Cited by
- 86
- References
- 35
- Citations by year
- 2026: 7 · 2025: 5 · 2024: 14 · 2023: 9 · 2022: 6 · 2021: 9 · 2020: 7 · 2019: 10 · 2018: 7 · 2017: 9 · 2016: 3
- FWCI
- 4.67
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- European Federation of Pharmaceutical Industries and Associations (FP7/20072013)
- Alzheimer's Society
- Alzheimer Society
- National Institute for Health and Care Research (FP7/2007–2013)
- Newcastle University (G0400074)
- European Commission (2007–2013, FP7 2007-2013, 264872, 115439, FP7/2007)
- Innovative Medicines Initiative (115439, FP7/2007‐2013, n°115439)
- Vlaamse regering
- Medical Research Council (FP7/20072013, G0400074, MR/L016451/1)
- NIHR Newcastle Biomedical Research Centre
- Janssen Research and Development
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau aggregation, tauopathy, iPSC-derived neurons, P301L tau mutation, Alzheimer's disease, frontotemporal dementia, tau phosphorylation, cortical neurons, autophagy, rapamycin, trehalose, drug screening model
- MeSH terms
- Alzheimer Disease, Autophagy, Brain, Cells, Cultured, Humans, Models, Biological, Mutation, Neurons, Phosphorylation, Protein Binding, tau Proteins, Tauopathies, Neural Stem Cells, Protein Aggregation, Pathological
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