Insoluble tau aggregates induce neuronal death through modification of membrane ion conductance, activation of voltage‐gated calcium channels and NADPH oxidase

Mechanism of Oxidative Stress in Neurodegeneration

Gandhi, S., & Abramov, A. Y. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/428010 · Cited by 964 · see citing works

Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum.

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β-Amyloid Peptides Induce Mitochondrial Dysfunction and Oxidative Stress in Astrocytes and Death of Neurons through Activation of NADPH Oxidase

Abramov, A. Y., Canevari, L., & Duchen, M. R. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.4042-03.2004 · Cited by 587 · see citing works

α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease

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Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer’s and Pick’s diseases

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Proteomic and functional analyses reveal a mitochondrial dysfunction in P301L tau transgenic mice

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Alpha-Synuclein Oligomers Interact with Metal Ions to Induce Oxidative Stress and Neuronal Death in Parkinson's Disease

Deas, E., Cremades, N., Angelova, P. R., Ludtmann, M. H. R., Yao, Z., Chen, S. W., Horrocks, M. H., Banushi, B., Little, D., Devine, M. J., et al. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6343 · Cited by 360 · see citing works

Changes in Intracellular Calcium and Glutathione in Astrocytes as the Primary Mechanism of Amyloid Neurotoxicity

Abramov, A. Y., Canevari, L., & Duchen, M. R. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-12-05088.2003 · Cited by 337 · see citing works

Conformation Determines the Seeding Potencies of Native and Recombinant Tau Aggregates

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Expression and Modulation of an NADPH Oxidase in Mammalian Astrocytes

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Ca2+ is a key factor in α-synuclein-induced neurotoxicity

Angelova, P. R., Ludtmann, M. H. R., Horrocks, M. H., Negoda, A. E., Cremades, N., Klenerman, D., Dobson, C. M., Wood, N. W., Pavlov, E. V., Gandhi, S., et al. (2016) · Journal of Cell Science · doi:10.1242/jcs.180737 · Cited by 193 · see citing works

Tau Oligomers Impair Artificial Membrane Integrity and Cellular Viability

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Nrf2 activation in the treatment of neurodegenerative diseases: a focus on its role in mitochondrial bioenergetics and function

Esteras, N., Dinkova‐Kostova, A. T., & Abramov, A. Y. (2016) · Biological Chemistry · doi:10.1515/hsz-2015-0295 · Cited by 161 · see citing works

The role of an astrocytic NADPH oxidase in the neurotoxicity of amyloid beta peptides

Abramov, A. Y., & Duchen, M. R. (2005) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2005.1766 · Cited by 158 · see citing works

Helical α-Synuclein Forms Highly Conductive Ion Channels

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Hsp70 Inhibits the Nucleation and Elongation of Tau and Sequesters Tau Aggregates with High Affinity

Kundel, F., De, S., Flagmeier, P., Horrocks, M. H., Kjærgaard, M., Shammas, S. L., Jackson, S., Dobson, C. M., & Klenerman, D. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.7b01039 · Cited by 128 · see citing works

Mitochondrial dysfunction in Parkinsonian mesenchymal stem cells impairs differentiation

Angelova, P. R., Barilani, M., Lovejoy, C. E. J., Dossena, M., Viganò, M., Seresini, A., Piga, D., Gandhi, S., Pezzoli, G., Abramov, A. Y., et al. (2017) · Redox Biology · doi:10.1016/j.redox.2017.10.016 · Cited by 119 · see citing works

Mitochondrial hyperpolarization in iPSC-derived neurons from patients of FTDP-17 with 10+16 MAPT mutation leads to oxidative stress and neurodegeneration

Esteras, N., Rohrer, J. D., Hardy, J., Wray, S., & Abramov, A. Y. (2017) · Redox Biology · doi:10.1016/j.redox.2017.03.008 · Cited by 117 · see citing works

Rare Individual Amyloid-β Oligomers Act on Astrocytes to Initiate Neuronal Damage

Narayan, P. S., Holmström, K. M., Kim, D.-H., Whitcomb, D. J., Wilson, M. R., George‐Hyslop, P. S., Wood, N. W., Dobson, C. M., Cho, K., Abramov, A. Y., et al. (2014) · Biochemistry · doi:10.1021/bi401606f · Cited by 104 · see citing works

Tau inhibits mitochondrial calcium efflux and makes neurons vulnerable to calcium-induced cell death

Britti, E., Ros, J., Esteras, N., & Abramov, A. Y. (2019) · Cell Calcium · doi:10.1016/j.ceca.2019.102150 · Cited by 101 · see citing works

Alpha-synuclein and beta-amyloid – different targets, same players: calcium, free radicals and mitochondria in the mechanism of neurodegeneration

Angelova, P. R., & Abramov, A. Y. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.07.103 · Cited by 98 · see citing works

Membrane cholesterol content plays a key role in the neurotoxicity of β‐amyloid: implications for Alzheimer’s disease

Abramov, A. Y., Йонов, М., Pavlov, E. V., & Duchen, M. R. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00685.x · Cited by 96 · see citing works

Measurement of Tau Filament Fragmentation Provides Insights into Prion-like Spreading

Kundel, F., Hong, L., Falcon, B., McEwan, W. A., Michaels, T. C. T., Meisl, G., Esteras, N., Abramov, A. Y., Knowles, T. P. J., Goedert, M., et al. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00094 · Cited by 79 · see citing works

Ion Channel Formation by Tau Protein: Implications for Alzheimer’s Disease and Tauopathies

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Novel pathway for an old neurotransmitter: Dopamine-induced neuronal calcium signalling via receptor-independent mechanisms

Vaarmann, A., Gandhi, S., Gourine, A. V., & Abramov, A. Y. (2010) · Cell Calcium · doi:10.1016/j.ceca.2010.08.008 · Cited by 33 · see citing works

Inhibition of Tau Protein Aggregation by Rhodanine-based Compounds Solubilized Via Specific Formulation Additives to Improve Bioavailability and Cell Viability

Mandelkow�, E., Pickhardt, M., Lawatscheck, C., & Börner, H. G. (2017) · Current Alzheimer Research · doi:10.2174/1567205014666170202103136 · Cited by 9 · see citing works

ROS Generation in Microglia: Understanding Oxidative Stress and Inflammation in Neurodegenerative Disease

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Mitochondria and lipid peroxidation in the mechanism of neurodegeneration: Finding ways for prevention

Angelova, P. R., Esteras, N., & Abramov, A. Y. (2020) · Medicinal Research Reviews · doi:10.1002/med.21712 · Cited by 290 · see citing works

Mitochondria and Calcium in Alzheimer’s Disease: From Cell Signaling to Neuronal Cell Death

Calvo-Rodriguez, M., & Bacskai, B. J. (2021) · Trends in Neurosciences · doi:10.1016/j.tins.2020.10.004 · Cited by 254 · see citing works

Interaction of Mitochondrial Calcium and ROS in Neurodegeneration

Baev, A. Y., Vinokurov, A. Y., Novikova, I. N., Dremin, V. V., Potapova, E. V., & Abramov, A. Y. (2022) · Cells · doi:10.3390/cells11040706 · Cited by 162 · see citing works

NADPH oxidase family proteins: signaling dynamics to disease management

Begum, R., Thota, S., Abdulkadir, A. S., Kaur, G., Bagam, P., & Batra, S. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-022-00858-1 · Cited by 148 · see citing works

Linking Oxidative Stress and Proteinopathy in Alzheimer’s Disease

Sharma, C., & Kim, S. R. (2021) · Antioxidants · doi:10.3390/antiox10081231 · Cited by 136 · see citing works

Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases

Rinauro, D. J., Chiti, F., Vendruscolo, M., & Limbocker, R. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00651-2 · Cited by 132 · see citing works

Interaction of Oxidative Stress and Misfolded Proteins in the Mechanism of Neurodegeneration

Abramov, A. Y., Potapova, E., Владимирович, Д. В., & Dunaev, A. (2020) · Life · doi:10.3390/life10070101 · Cited by 125 · see citing works

Mitochondrial Calcium Deregulation in the Mechanism of Beta-Amyloid and Tau Pathology

Esteras, N., & Abramov, A. Y. (2020) · Cells · doi:10.3390/cells9092135 · Cited by 104 · see citing works

Oxygen metabolism abnormality and Alzheimer's disease: An update

Liu, G., Yang, C., Wang, X., Chen, X., Wang, Y., & Le, W. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102955 · Cited by 85 · see citing works

Therapeutic Insights on Ferroptosis in Parkinson's disease

Thapa, K., Khan, H., Kanojia, N., Singh, T. G., Kaur, A., & Kaur, G. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.175133 · Cited by 78 · see citing works

Ca2+ Dyshomeostasis Disrupts Neuronal and Synaptic Function in Alzheimer’s Disease

McDaid, J., Mustaly-Kalimi, S., & Stutzmann, G. E. (2020) · Cells · doi:10.3390/cells9122655 · Cited by 73 · see citing works

Nrf2 regulates glucose uptake and metabolism in neurons and astrocytes

Esteras, N., Blacker, T. S., Zherebtsov, E., Stelmashchuk, O. A., Zhang, Y., Wigley, W. C., Duchen, M. R., Dinkova‐Kostova, A. T., & Abramov, A. Y. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102672 · Cited by 65 · see citing works

Role of the Lipid Membrane and Membrane Proteins in Tau Pathology

Bok, E., Leem, E., Lee, B.-R., Lee, J. M., Yoo, C. J., Lee, E. M., & Kim, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.653815 · Cited by 61 · see citing works

Sources and triggers of oxidative damage in neurodegeneration

Angelova, P. R. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.07.003 · Cited by 64 · see citing works

Astroglial activation: Current concepts and future directions

Edison, P. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.13678 · Cited by 64 · see citing works

Tau and Membranes: Interactions That Promote Folding and Condensation

Sallaberry, C. A., Voss, B. J., Majewski, J. P., Biernat, J., Mandelkow�, E., Chi, E. Y., & Zanden, C. M. V. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.725241 · Cited by 60 · see citing works

Dysregulation of energy metabolism in Alzheimer's disease

Yuan, Y., Zhao, G., & Zhao, Y. (2024) · Journal of Neurology · doi:10.1007/s00415-024-12800-8 · Cited by 60 · see citing works

Therapeutic Strategies to Target Calcium Dysregulation in Alzheimer’s Disease

Calvo-Rodríguez, M., Kharitonova, E. K., & Bacskai, B. J. (2020) · Cells · doi:10.3390/cells9112513 · Cited by 59 · see citing works

Oxidative Stress in Tauopathies: From Cause to Therapy

Bartolomé, F. B., Carro, E., & Alquézar, C. (2022) · Antioxidants · doi:10.3390/antiox11081421 · Cited by 57 · see citing works

Alterations of the Endoplasmic Reticulum (ER) Calcium Signaling Molecular Components in Alzheimer’s Disease

Chami, M., & Checler, F. (2020) · Cells · doi:10.3390/cells9122577 · Cited by 53 · see citing works

Neurodegenerative disorders: Assessing the impact of natural vs drug‐induced treatment options

Mathur, S., Gawas, C. G., Ahmad, I. Z., Wani, M., & Tabassum, H. (2023) · Aging Medicine · doi:10.1002/agm2.12243 · Cited by 48 · see citing works

Cannabidiol Inhibits Tau Aggregation In Vitro

Alali, S., Riazi, G. H., Ashrafi-Kooshk, M. R., Meknatkhah, S., Ahmadian, S., Ardakani, M. H., & Hosseinkhani, B. (2021) · Cells · doi:10.3390/cells10123521 · Cited by 47 · see citing works

PINK1 overexpression prevents forskolin-induced tau hyperphosphorylation and oxidative stress in a rat model of Alzheimer’s disease

Wang, X., Qi, L., Cheng, Y.-F., Ji, X., Chi, T., Liu, P., & Zou, L. (2021) · Acta Pharmacologica Sinica · doi:10.1038/s41401-021-00810-5 · Cited by 43 · see citing works

Targeting tau only extracellularly is likely to be less efficacious than targeting it both intra- and extracellularly

Congdon, E. E., Jiang, Y., & Sigurdsson, E. M. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.12.002 · Cited by 37 · see citing works

P2X7 Receptor and Purinergic Signaling: Orchestrating Mitochondrial Dysfunction in Neurodegenerative Diseases

Zelentsova, A. S., Deykin, A. V., Soldatov, V. O., Ulezko, A. A., Borisova, A. Y., Belyaeva, V. S., Skorkina, M. Y., & Angelova, P. R. (2022) · eNeuro · doi:10.1523/eneuro.0092-22.2022 · Cited by 39 · see citing works

Astrocytes in Neurodegeneration: Inspiration From Genetics

Huang, J., Li, C., & Shang, H. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.882316 · Cited by 37 · see citing works

Do glutathione and copper interact to modify Alzheimer's disease pathogenesis?

Ho, T., Ahmadi, S., & Kerman, K. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.01.025 · Cited by 37 · see citing works

NOX-induced oxidative stress is a primary trigger of major neurodegenerative disorders

Zilberter, Y., Tabuena, D. R., & Zilberter, M. Y. (2023) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2023.102539 · Cited by 34 · see citing works

Intersection between Redox Homeostasis and Autophagy: Valuable Insights into Neurodegeneration

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Synaptic sabotage: How Tau and α-Synuclein undermine synaptic health

Uytterhoeven, V., Verstreken, P., & Nachman, E. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202409104 · Cited by 28 · see citing works

Microglial dysfunction in Alzheimer's disease: Mechanisms, emerging therapies, and future directions

Azmal, M., Paul, J. K., Prima, F. S., Haque, A. N. M. S. N. B., Meem, M., & Ghosh, A. (2025) · Experimental Neurology · doi:10.1016/j.expneurol.2025.115374 · Cited by 28 · see citing works

Friend or foe: role of pathological tau in neuronal death

Wu, M., Chen, Z., Jiang, M. H., Bao, B., Li, D., Yin, X., Wang, X., Liu, D., & Zhu, L. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02024-z · Cited by 28 · see citing works

N-Acetylcysteine Amide against Aβ-Induced Alzheimer’s-like Pathology in Rats

Alkandari, A. F., Madhyastha, S., & Rao, M. S. R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241612733 · Cited by 27 · see citing works

Genetically engineered MAPT 10+16 mutation causes pathophysiological excitability of human iPSC-derived neurons related to 4R tau-induced dementia

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 26 · see citing works

Structure-specific amyloid precipitation in biofluids

Rodrigues, M., Bhattacharjee, P., Brinkmalm, A., Do, D. T., Pearson, C. M., De, S., Ponjavic, A., Varela, J. A., Kulenkampff, K., Baudrexel, I., et al. (2022) · Nature Chemistry · doi:10.1038/s41557-022-00976-3 · Cited by 26 · see citing works

A comprehensive mechanism of biological and health effects of anthropogenic extremely low frequency and wireless communication electromagnetic fields

Panagopoulos, D. J., Yakymenko, I., Iuliis, G. N. D., & Chrousos, G. P. (2025) · Frontiers in Public Health · doi:10.3389/fpubh.2025.1585441 · Cited by 23 · see citing works

MAPT genotype-dependent mitochondrial aberration and ROS production trigger dysfunction and death in cortical neurons of patients with hereditary FTLD

Korn, L., Speicher, A. M., Schroeter, C. B., Gola, L., Kaehne, T., Engler, A., Disse, P., Fernández‐Orth, J., Csatári, J., Naumann, M., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102597 · Cited by 24 · see citing works

Exosomes: potential targets for the diagnosis and treatment of neuropsychiatric disorders

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Methionine-Mediated Protein Phosphatase 2A Catalytic Subunit (PP2Ac) Methylation Ameliorates the Tauopathy Induced by Manganese in Cell and Animal Models

Wu, B., Cai, H., Tang, S., Xu, Y., Shi, Q., Wei, L., Meng, L., Zhang, N., Wang, X., Xiao, D., et al. (2020) · Neurotherapeutics · doi:10.1007/s13311-020-00930-6 · Cited by 19 · see citing works

Lymphocyte‐Activation Gene 3 Facilitates Pathological Tau Neuron‐to‐Neuron Transmission

Chen, C., Kumbhar, R., Wang, H., Yang, X., Gadhave, K., Rastegar, C. T., Kimura, Y., Behensky, A. A., Kotha, S., Kuo, G., et al. (2024) · Advanced Science · doi:10.1002/advs.202303775 · Cited by 18 · see citing works

Mitochondrion-based organellar therapies for central nervous system diseases

Zhao, M., Wang, J., Zhu, S., Wang, M., Chen, C., Wang, L., & Liu, J. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01843-z · Cited by 20 · see citing works

Drug repurposing for neurodegenerative diseases using Zebrafish behavioral profiles

Hernández, T. D. R., Gore, S. V., Kreiling, J. A., & Créton, R. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.116096 · Cited by 18 · see citing works

Interaction of Tau construct K18 with model lipid membranes

Azouz, M., Feuillie, C., Lafleur, M., Molinari, M., & Lecomte, S. (2021) · Nanoscale Advances · doi:10.1039/d1na00055a · Cited by 16 · see citing works

Iron(ing) out parkinsonisms: The interplay of proteinopathy and ferroptosis in Parkinson's disease and tau-related parkinsonisms

Caiado, M. J. D. C., Dolga, A. M., & den Dunnen, W. F. A. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103478 · Cited by 16 · see citing works

Glaucoma as a Tauopathy—Is It the Missing Piece in the Glaucoma Puzzle?

Passaro, M. L., Matarazzo, F., Abbadessa, G., Pezone, A., Porcellini, A., Tranfa, F., Rinaldi, M., & Costagliola, C. (2023) · Journal of Clinical Medicine · doi:10.3390/jcm12216900 · Cited by 15 · see citing works

RT001 in Progressive Supranuclear Palsy—Clinical and In-Vitro Observations

Angelova, P. R., Andruska, K. M., Midei, M. G., Barilani, M., Atwal, P. S., Tucher, O., Milner, P., Heerinckx, F., & Shchepinov, M. S. (2021) · Antioxidants · doi:10.3390/antiox10071021 · Cited by 15 · see citing works

Neuroprotective Effects of Bromelain on the Common Neurodegenerative Diseases: A Systematic Review

Rostamian, S., Raeisi, E., Heidari-Soureshjani, S., & Sherwin, C. M. T. (2023) · Neurochemical Journal · doi:10.1134/s1819712423040256 · Cited by 12 · see citing works

Cellular Uptake of Tau Aggregates Triggers Disulfide Bond Formation in Four-Repeat Tau Monomers

Krzesinski, B. J., Holub, T. J., Gabani, Z. Y., & Margittai, M. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00607 · Cited by 11 · see citing works

Role of Oxygen Radicals in Alzheimer’s Disease: Focus on Tau Protein

Atlante, A., Valenti, D., Latina, V., & Amadoro, G. (2021) · Oxygen · doi:10.3390/oxygen1020010 · Cited by 11 · see citing works

Amyloids on Membrane Interfaces: Implications for Neurodegeneration

Mahakud, A. K., Shaikh, J., Iqbal, V. V. R., Gupta, A., Tiwari, A., & Saleem, M. (2022) · The Journal of Membrane Biology · doi:10.1007/s00232-022-00245-x · Cited by 8 · see citing works

Interaction Between a High-Fat Diet and Tau Pathology in Mice: Implications for Alzheimer’s Disease

Jang, Y. J., Choi, M. G., Yoo, B. J., Lee, K. J., Jung, W. B., Kim, S., & Park, S. A. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230927 · Cited by 9 · see citing works

Cell-Permeable HSP70 Protects Neurons and Astrocytes Against Cell Death in the Rotenone-Induced and Familial Models of Parkinson’s Disease

Vinokurov, A. Y., Palalov, A. A., Kritskaya, K. A., Demyanenko, S. V., Garbuz, D. G., Evgen’ev, M. B., Esteras, N., & Abramov, A. Y. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04077-9 · Cited by 9 · see citing works

Extracellular PHF-tau modulates astrocyte mitochondrial dynamics and mediates neuronal connectivity

Zufferey, V., Barve, A., Parietti, E., Belinga, L. N., Bringaud, A., Varisco, Y., Fabbri, K., Capotosti, F., Bezzi, P., Déglon, N., et al. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00474-9 · Cited by 10 · see citing works

Dysregulated calcium signaling in the aged primate association cortices: vulnerability to Alzheimer’s disease neuropathology

Arnsten, A. F. T., Perone, I., Wang, M., Yang, S., Uchendu, S., Bolat, D., & Datta, D. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1610350 · Cited by 7 · see citing works

Short-Term Inhibition of NOX2 Prevents the Development of Aβ-Induced Pathology in Mice

Mukhina, K. A., Kechko, O. I., Osypov, A. A., Petrushanko, I. Y., Makarov, A. А., Mitkevich, V. A., & Popova, I. Y. (2025) · Antioxidants · doi:10.3390/antiox14060663 · Cited by 7 · see citing works

Targeting NOX inhibitors in neurodegeneration: a therapeutic perspective

Kaur, S., Verma, R., Sharma, V., & Singh, T. G. (2025) · Metabolic Brain Disease · doi:10.1007/s11011-025-01644-4 · Cited by 6 · see citing works

Early mitophagy activation by Urolithin A prevents, but late activation does not reverse, age-related cognitive impairment

Jara, C., Venegas-Zamora, L., Park-Kang, H. S., Lira, M., Ricca, M., Valenzuela, S., & Tapia‐Rojas, C. (2026) · npj Aging · doi:10.1038/s41514-026-00351-3 · Cited by 6 · see citing works

Role of dysregulated calcium homeostasis in astrocytes in neurodegenerative disorders

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The Link between Exercise and Homocysteine in the Alzheimer’s Disease: A Bioinformatic Network Model

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Generation and characterization of two induced pluripotent stem cell lines (ICGi052-A and ICGi052-B) from a patient with frontotemporal dementia with parkinsonism-17 associated with the pathological variant c.2013T>G in the MAPT gene

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