Internalized Tau Oligomers Cause Neurodegeneration by Inducing Accumulation of Pathogenic Tau in Human Neurons Derived from Induced Pluripotent Stem Cells

LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.

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Induction of the Vitamin D Receptor Attenuates Autophagy Dysfunction-Mediated Cell Death Following Traumatic Brain Injury

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Guidelines for the use and interpretation of assays for monitoring autophagy

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Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease

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Staging of alzheimer's disease-related neurofibrillary changes

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Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model

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Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders

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Transmission and spreading of tauopathy in transgenic mouse brain

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Self-propagation of pathogenic protein aggregates in neurodegenerative diseases

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The Impact of the Cellular Environment and Aging on Modeling Alzheimer's Disease in 3D Cell Culture Models

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Expression and purification of tau protein and its frontotemporal dementia variants using a cleavable histidine tag

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A human induced pluripotent stem cell‐derived cortical neuron human‐on‐a chip system to study Aβ 42 and tau‐induced pathophysiological effects on long‐term potentiation

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Traumatic brain injury and the pathways to cerebral tau accumulation

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A framework for translating tauopathy therapeutics: Drug discovery to clinical trials

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Therapeutic Candidates for Alzheimer’s Disease: Saponins

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On the role of the cellular prion protein in the uptake and signaling of pathological aggregates in neurodegenerative diseases

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Clathrin mediated endocytosis in Alzheimer’s disease: cell type specific involvement in amyloid beta pathology

Jaye, S., Sandau, U. S., & Saugstad, J. A. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1378576 · Cited by 26

Distinct Neurotoxic Effects of Extracellular Tau Species in Primary Neuronal-Glial Cultures

Pampuščenko, K., Morkūnienė, R., Krasauskas, L., Smirnovas, V., Tomita, T., & Borutaitė, V. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02150-7 · Cited by 28

A gut–brain axis on-a-chip platform for drug testing challenged with donepezil

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Heterogeneous Tau Oligomers as Molecular Targets for Alzheimer’s Disease and Related Tauopathies

Lo, C. H. (2022) · Biophysica · doi:10.3390/biophysica2040039 · Cited by 24

Phospholipids and calmodulin modulate the inhibition of PMCA activity by tau

Berrocal, M., Corbacho‐Cuello, I., Sepúlveda, M. R., Gutiérrez‐Merino, C., & Mata, A. M. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.10.023 · Cited by 23

Binding and neurotoxicity mitigation of toxic tau oligomers by synthetic heparin like oligosaccharides

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Mechanisms of ubiquitin-independent proteasomal degradation and their roles in age-related neurodegenerative disease

Church, T. R., & Margolis, S. S. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1531797 · Cited by 25

Modeling neuroinflammatory interactions between microglia and astrocytes in a human iPSC-based coculture platform

Tujula, I., Hyvärinen, T., Lotila, J., Rogal, J., Voulgaris, D., Sukki, L., Tornberg, K., Korpela, K., Jäntti, H., Malm, T., et al. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02304-x · Cited by 22

Intraneuronal tau aggregation induces the integrated stress response in astrocytes

Batenburg, K. L., Kasri, N. N., Heine, V. M., & Scheper, W. (2022) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjac071 · Cited by 21

Pathological Impact of Tau Proteolytical Process on Neuronal and Mitochondrial Function: a Crucial Role in Alzheimer’s Disease

Olesen, M. A., & Quintanilla, R. A. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03434-4 · Cited by 23

Tau Secretion

Ruan, Z., & Ikezu, T. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_11 · Cited by 23

Cellular Models for the Study of PrionsPreprint

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The prion protein and its ligands: Insights into structure-function relationships

Shafiq, M., Vela, S. D., Amin, L., Younas, N., Harris, D. A., Zerr, I., Altmeppen, H. C., Svergun, D. I., & Glatzel, M. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119240 · Cited by 21

Hyperphosphorylated Tau Inflicts Intracellular Stress Responses that Are Mitigated by Apomorphine

Song, Z., Wang, K., Hagar, H. C., Chen, H., Kuan, C.-Y., Zhang, K., & Kuo, M. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03689-x · Cited by 23

The Neurotoxic Tau45-230 Fragment Accumulates in Upper and Lower Motor Neurons in Amyotrophic Lateral Sclerosis Subjects

Vintilescu, C. R., Afreen, S., Rubino, A. E., & Ferreira, A. (2016) · Molecular Medicine · doi:10.2119/molmed.2016.00095 · Cited by 20

Populations of Tau Conformers Drive Prion-like Strain Effects in Alzheimer’s Disease and Related Dementias

Hromádková, L., Siddiqi, M. K., Liu, H., & Safar, J. (2022) · Cells · doi:10.3390/cells11192997 · Cited by 19

A high-throughput model for investigating neuronal function and synaptic transmission in cultured neuronal networks

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 18

AD-Related N-Terminal Truncated Tau Is Sufficient to Recapitulate In Vivo the Early Perturbations of Human Neuropathology: Implications for Immunotherapy

Borreca, A., Latina, V., Corsetti, V., Middei, S., Piccinin, S., Valle, F. D., Bussani, R., Ammassari‐Teule, M., Nisticò, R., Calissano, P., et al. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0974-3 · Cited by 18

Synaptic oligomeric tau in Alzheimer’s disease – a potential culprit in the spread of tau pathology through the brainPreprint

Colom‐Cadena, M., Davies, C., Sirisi, S., Lee, J.-E., Simzer, E. M., Tzioras, M., Querol‐Vilaseca, M., Sánchez‐Aced, É., Chang, Y. Y., Holt, K., et al. (2023) · medRxiv · doi:10.1101/2023.03.15.23287268 · Cited by 19

Dementia Therapy Targeting Tau

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Nasal Rifampicin Halts the Progression of Tauopathy by Inhibiting Tau Oligomer Propagation in Alzheimer Brain Extract-Injected Mice

Umeda, T., Uekado, R., Shigemori, K., Eguchi, H., & Tomiyama, T. (2022) · Biomedicines · doi:10.3390/biomedicines10020297 · Cited by 18

Alzheimer proteopathic tau seeds are biochemically a forme fruste of mature paired helical filaments

Kumar, M., Quittot, N., Dujardin, S., Schlaffner, C. N., Viodé, A., Wiedmer, A. E., Beerepoot, P., Chun, J. E., Glynn, C. A., Fernandes, A. R., et al. (2024) · Brain · doi:10.1093/brain/awad378 · Cited by 20

Secretion of full-length Tau or Tau fragments in cell culture models. Propagation of Tau in vivo and in vitro

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Methylene Blue Blocks and Reverses the Inhibitory Effect of Tau on PMCA Function

Berrocal, M., Caballero-Bermejo, M., Gutierrez-Merino, C., & Mata, A. M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20143521 · Cited by 17

The use of human neurons for novel drug discovery in dementia research

Vargas‐Caballero, M., Willaime‐Morawek, S., Gómez‐Nicola, D., Perry, V. H., Bulters, D. O., & Mudher, A. K. (2016) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2016.1154528 · Cited by 15

The use of mouse models to study cell-to-cell transmission of pathological tau

Narasimhan, S., & Lee, V. M. ‐. (2017) · Methods in cell biology · doi:10.1016/bs.mcb.2017.06.009 · Cited by 16

Sorcin Activates the Brain PMCA and Blocks the Inhibitory Effects of Molecular Markers of Alzheimer’s Disease on the Pump Activity

Berrocal, M., Saez, L., & Mata, A. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22116055 · Cited by 16

Direct interaction between TDP-43 and Tau promotes their co-condensation, while suppressing Tau fibril formation and seeding

Simonetti, F., Zhong, W., Hutten, S., Uliana, F., Schifferer, M., Rezaei, A., Ramirez, L. M., Hochmair, J., Sankar, R., Gopalan, A. B., et al. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00590-2 · Cited by 22

Extracellular Tau Oligomers Damage the Axon Initial Segment

Best, M. N., Lim, Y., Ferenc, N. N., Kim, N., Min, L. Y., Wang, D. B., Sharifi, K., Wasserman, A. E., McTavish, S. A., Siller, K. H., et al. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-221284 · Cited by 15

Modeling of the brain-lung axis using organoids in traumatic brain injury: an updated review

Kim, J.-T., Song, K., Han, S. W., Youn, D. H., Jung, H., Kim, K., Lee, H., Hong, J. Y., Cho, Y.-J., Kang, S., et al. (2024) · Cell & Bioscience · doi:10.1186/s13578-024-01252-2 · Cited by 16

Cerium-doped Prussian blue biomimetic nanozyme as an amplified pyroptosis inhibitor mitigate Aβ oligomer-induced neurotoxicity in Alzheimer’s disease

Ma, J., Tian, Y., Du, C., Zhu, Y., Huang, W. C., Ding, C., Wei, P., Yi, X., Lin, Z., & Fang, W. (2025) · Journal of Nanobiotechnology · doi:10.1186/s12951-025-03263-8 · Cited by 15

Spreading of Pathology in Alzheimer’s Disease

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Neurodegeneration in a dish: advancing human stem-cell-based models of Alzheimer’s disease

Klimmt, J., Dannert, A., & Paquet, D. (2020) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2020.01.008 · Cited by 16

Altered Brain Leptin and Leptin Receptor Expression in the 5XFAD Mouse Model of Alzheimer’s Disease

Pratap, A. A., & Holsinger, R. M. D. (2020) · Pharmaceuticals · doi:10.3390/ph13110401 · Cited by 15

Pharmacotherapies for the Treatment of Progressive Supranuclear Palsy: A Narrative Review

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Internalization of extracellular Tau oligomers in Alzheimer’s disease

Chinnathambi, S., Rangappa, N., & Chandrashekar, M. (2025) · Advances in clinical chemistry · doi:10.1016/bs.acc.2025.01.005 · Cited by 14

Oxidative Stress Conditions Result in Trapping of PHF-Core Tau (297–391) Intermediates

Maina, M. B., Al‐Hilaly, Y. K., Burra, G., Rickard, J. E., Harrington, C. R., Wischik, C. M., & Serpell, L. C. (2021) · Cells · doi:10.3390/cells10030703 · Cited by 14

Targeted protein degradation with bifunctional molecules as a novel therapeutic modality for Alzheimer's disease & beyond

Sandhof, C. A., Murray, H. F. B., Silva, M. C., & Haggarty, S. J. (2024) · Neurotherapeutics · doi:10.1016/j.neurot.2024.e00499 · Cited by 14

Extracellular Tau Paired Helical Filaments Differentially Affect Tau Pathogenic Mechanisms in Mitotic and Post-Mitotic Cells: Implications for Mechanisms of Tau Propagation in the Brain

Varghese, M., Santa‐María, I., Ho, L., Ward, L. M., Yemul, S., Dubner, L., Ksiȩżak-Reding, H., & Pasinetti, G. M. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160166 · Cited by 14

Important advances in Alzheimer’s disease from the use of induced pluripotent stem cells

Majolo, F., Marinowic, D. R., Machado, D. C., & da Costa, J. C. (2019) · Journal of Biomedical Science · doi:10.1186/s12929-019-0501-5 · Cited by 15

Cornel iridoid glycoside induces autophagy to protect against tau oligomer neurotoxicity induced by the activation of glycogen synthase kinase-3β

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The role of wild-type tau in Alzheimer’s disease and related tauopathies

Lo, C. H., & Sachs, J. N. (2020) · JoLS Journal of Life Sciences · doi:10.36069/jols/20201201 · Cited by 15

Small molecules targeting molecular chaperones for tau regulation: Achievements and challenges

He, C., Gu, J., Wang, D., Wang, K., Wang, Y., You, Q., & Wang, L. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115859 · Cited by 12

The role of the cellular prion protein in the uptake and toxic signaling of pathological neurodegenerative aggregates

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Accumulation of C-terminal cleaved tau is distinctly associated with cognitive deficits, synaptic plasticity impairment, and neurodegeneration in aged mice

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Cromolyn platform suppresses fibrosis and inflammation, promotes microglial phagocytosis and neurite outgrowth

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Lipid role in synapse and nuclear envelope-associated endocytic pathways in Tauopathy

Chinnathambi, S., Adithyan, A., & Chandrashekar, M. (2024) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2024.08.002 · Cited by 11

The Fate of Tau Aggregates Between Clearance and Transmission

Seitkazina, A., Kim, K. H., Fagan, E., Sung, Y., Kim, Y. K., & Lim, S. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.932541 · Cited by 10

Towards a Mechanistic Model of Tau-Mediated Pathology in Tauopathies: What Can We Learn from Cell-Based In Vitro Assays?

Sala‐Jarque, J., Zimkowska, K., Ávila, J., Ferrer, I., & del Río, J. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911527 · Cited by 11

Review: Induced pluripotent stem cell models of frontotemporal dementia

Preza, E., Hardy, J., Warner, T. T., & Wray, S. (2016) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12334 · Cited by 10

MiR-219 deficiency in Alzheimer’s disease contributes to neurodegeneration and memory dysfunction through post-transcriptional regulation of tau-kinase networkPreprint

Arnés, M., Kim, Y. A., Lannes, J., Alaniz, M. E., Cho, J. D., McCabe, B. D., & Santa‐María, I. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/607176 · Cited by 11

Sex-specific hypothalamic neuropathology and glucose metabolism in an amyloidosis transgenic mouse model of Alzheimer’s disease

Qi, G., Tang, H., Gong, P., Liu, Y., He, C., Hu, J., Kang, S., Chen, L., & Qin, S. (2024) · Cell & Bioscience · doi:10.1186/s13578-024-01295-5 · Cited by 10

Novel regulators of heparan sulfate proteoglycans modulate cellular uptake of α-synuclein fibrils

Vanderperre, B., Muraleedharan, A., Dorion, M., Larroquette, F., del Cid‐Pellitero, E., Rajakulendran, N., Chen, C. X. ‐., Larivière, R., Michaud-Tardif, C., Goiran, T., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-08786-2 · Cited by 18

First dual binder of microRNA-146a and monomeric tau: a novel approach for multitargeted therapeutics for neurodegenerative diseases

Gabr, M. T., & Barbault, F. (2020) · Chemical Communications · doi:10.1039/d0cc04249h · Cited by 10

A Tau-Driven Adverse Outcome Pathway Blueprint Toward Memory Loss in Sporadic (Late-Onset) Alzheimer’s Disease with Plausible Molecular Initiating Event Plug-Ins for Environmental Neurotoxicants

Tsamou, M., Pistollato, F., & Roggen, E. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-201418 · Cited by 9

Potential of Microfluidics and Lab-on-Chip Platforms to Improve Understanding of “prion-like” Protein Assembly and Behavior

del Rı́o, J. A., & Ferrer, I. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.570692 · Cited by 8

Characterization of microtubule-associated protein tau isoforms and Alzheimer’s disease-like pathology in normal sheep (Ovis aries): relevance to their potential as a model of Alzheimer’s disease

Davies, E. S., Morphew, R. M., Cutress, D. J., Morton, A. J., & McBride, S. D. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04572-z · Cited by 9

Short-chain polyphosphates induce tau fibrillation and neurotoxicity in human iPSC-derived retinal neurons

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A Single-Chain Variable Fragment Antibody Inhibits Aggregation of Phosphorylated Tau and Ameliorates Tau Toxicity in vitro and in vivo

Li, S., Yi, Y., Cui, K., Zhang, Y., Chen, Y., Han, D., Sun, L. V., Zhang, X., Chen, F., Zhang, Y., et al. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-191266 · Cited by 9

Cellular Reprogramming and Its Potential Application in Alzheimer’s Disease

Zhou, C., Ni, W., Zhu, T., Dong, S., Sun, P., & Hua, F. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.884667 · Cited by 8

Editorial: Protein misfolding, altered mechanisms and neurodegeneration

Gogia, N., Tare, M., Kannan, R., & Singh, A. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1134855 · Cited by 8

Anterograde and Retrograde Propagation of Inoculated Human Tau Fibrils and Tau Oligomers in a Non-Transgenic Rat Tauopathy Model

Horvat, L. L., Španić, E., Leko, M. B., Zubčić, K., Horvat, L., Mustapić, M., Hof, P. R., & Šimić, G. (2023) · Biomedicines · doi:10.3390/biomedicines11041004 · Cited by 7

The evolution of microtubule associated proteins – a reference proteomic perspective

Gottschalk, A. C., & Hefti, M. M. (2022) · BMC Genomics · doi:10.1186/s12864-022-08502-y · Cited by 8

Research and progress of focused ultrasound in the treatment of Alzheimer’s disease

Ma, X., Li, T., Du, L., & Han, T. (2023) · Frontiers in Neurology · doi:10.3389/fneur.2023.1323386 · Cited by 7

Human iPSC Models in Drug Discovery: Opportunities and Challenges

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Mechanism of action deconvolution of the small-molecule pathological tau aggregation inhibitor Anle138b

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Sex-Specific Multiparameter Blood Test for the Early Diagnosis of Alzheimer’s Disease

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Disentangling tau, glymphatic dysfunction and astrocytic activation in amyloid-positive Alzheimer's disease

Chang, H., Chen, S.-W., Huang, S., Hsu, S., Lee, C.-C., Huang, C., Huang, C.-W., & Chang, C.-C. (2025) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2025.112113 · Cited by 5

Fas Apoptosis Inhibitory Molecule Blocks and Dissolves Pathological Amyloid-β Species

Kaku, H., Ludlow, A. V., Gutknecht, M. F., & Rothstein, T. L. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.750578 · Cited by 6

Targeted tau protein degradation: a promising therapeutic approach for tauopathies

Baazaoui, N., Alfaifi, M. Y., Shati, A. A., Saad, R. B., & Garzoli, S. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.11.041 · Cited by 5

Tau oligomers modulate synapse fate by eliciting progressive bipartite synapse dysregulation and synapse loss

Pareja-Navarro, K. A., King, C. D., Kauwe, G., Ngwala, Y. Y., Lokitiyakul, D., Wong, I., Vira, A., Liu, Y., Chen, J. H., Sharma, M., et al. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00928-2 · Cited by 6

Potential role of tanycyte-derived neurogenesis in Alzheimer’s disease

Qi, G., Tang, H., Hu, J., Kang, S., & Qin, S. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01865 · Cited by 7

Illuminating the Structural Basis of Tau Aggregation by Intramolecular Distance Tracking: A Perspective on Methods

Zeng, Z., Fichou, Y., Vigers, M. P., Tsay, K., & Han, S. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c02022 · Cited by 4

iPSC screening identifies CACNA2D2 as a potential therapeutic target for FTLD-Tau.

Imamura, K., Nagahashi, A., Okusa, A., Sakasai, T., Tsukita, K., Kutoku, Y., Ohsawa, Y., Sunada, Y., Sahara, N., Kanaan, N., et al. (2025) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2025.151484 · Cited by 4

A novel allosteric GCase modulator prevents Tau accumulation in GBA1WT and GBA1L444P/L444P cellular models

Ciccaldo, M., Pérez-Carmona, N., Piovesana, E., Cano-Crespo, S., Ruano, A., Delgado, A., Fregno, I., Guzmán, B. C.-F., Bellotto, M., Molinari, M., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-02346-8 · Cited by 4

Minimalistic in vitro systems for investigating tau pathology

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

Expression of the human herpesvirus 6A latency-associated transcript U94A impairs cytoskeletal functions in human neural cells

Hogestyn, J. M., Salois, G., Xie, L. H., Apa, C., Youngyunpipatkul, J., Pröschel, C., & Mayer-Pröschel, M. (2022) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2022.103770 · Cited by 3

A multiscale model to explain the spatiotemporal progression of amyloid beta and tau pathology in Alzheimer's disease

Xu, C., Xu, E., Xiao, Y., Yang, D., Guorong Wu, A., & Chen, M. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.142887 · Cited by 3

Small molecule modulation of the p75 neurotrophin receptor promotes dendritic spine resilience to pathogenic tau species and reduces their accumulation

Yang, T., Ay, Y. A., Kaur, S., Butler, R. R., Tran, K. C., Liu, H., Langness, V. F., Massa, S. M., & Longo, F. M. (2026) · Acta Neuropathologica Communications · doi:10.1186/s40478-026-02263-5 · Cited by 3

Microfluidic ‘Brain-on Chip’ Systems to Supplement Neurological Practice: Development, Applications and Considerations

Jarrah, R. M., Nathani, K. R., Bhandarkar, S., Ezeudu, C. S., Nguyen, R. T., Amare, A., Aljameey, U. A., Jarrah, S. I., Bhandarkar, A. R., & Fiani, B. (2023) · Regenerative Medicine · doi:10.2217/rme-2022-0212 · Cited by 3

Differential accumulation of human β-amyloid and tau from enriched extracts in neuronal and endothelial cells

Rabanal‐Ruiz, Y., Pedrero-Prieto, C. M., Rodríguez, L. S., Flores‐Cuadrado, A., Saiz‐Sánchez, D., Frontiñán-Rubio, J., Úbeda‐Bañón, I., Durán‐Prado, M., Martínez-Marcos, A., & Peinado, J. R. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167204 · Cited by 3

Regulation of presynaptic homeostatic plasticity by glial signalling in Alzheimer's disease

Cai, Y., & Wang, T. (2024) · The Journal of Physiology · doi:10.1113/jp286751 · Cited by 3

Abnormal Hyperphosphorylation of Tau in Canine Immune-mediated Meningoencephalitis

Son, M., Chae, Y., Kim, S., Yun, T., Koo, Y., Lee, D., Kim, H., Yang, M., Kang, B., & Kim, S. (2023) · In Vivo · doi:10.21873/invivo.13181 · Cited by 3

Seeding-competent early tau multimers are associated with cell type-specific transcriptional signatures

Feleke, R., Jogaudaite, S., Velentza‐Almpani, E., Yeung-Yeung, L., Clode, D., Ko, J. H., Shin, B., Matthews, S., Otero‐Jimenez, M., Wojewska, M. J., et al. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02869-4 · Cited by 4

A Combined Cell-Worm Approach to Search for Compounds Counteracting the Toxicity of Tau Oligomers In Vivo

Natale, C., Barzago, M. M., Colnaghi, L., Luigi, A. D., Orsini, F., Fioriti, L., & Diomede, L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911277 · Cited by 3

Mechanical stimulation prevents impairment of axon growth and overcompensates microtubule destabilization in cellular models of Alzheimer’s disease and related Tau pathologies

Galeotti, A. A., Santucci, L., Klimek, J., Kabbani, M. A. A., Zempel, H., & Raffa, V. (2025) · Frontiers in Medicine · doi:10.3389/fmed.2025.1519628 · Cited by 2

Morphological and Hyperphosphorylation Transitions of Nanoscale Tau Aggregates in Alzheimer's Disease

Santiago-Ruiz, A. N., Hugelier, S., Correa, G. L., Bond, C., Lee, E. B., & Lakadamyali, M. (2025) · Advanced Science · doi:10.1002/advs.202509773 · Cited by 3

Pyroptosis; igniting neuropsychiatric disorders from mild depression to aging-related neurodegeneration

Hushmandi, K., Reiter, R. J., Farahani, N., Cho, W. C. S., Alimohammadi, M., & Khoshnazar, S. M. (2025) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2025.111325 · 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

Selective vulnerability of human synapses to soluble tau oligomers

Kadamangudi, S., Sánchez-Sánchez, L., Kayed, R., Limón, A., & Taglialatela, G. (2026) · Journal of Alzheimer s Disease · doi:10.1177/13872877261416539 · Cited by 2

Apolipoprotein E ε4 and type 2 diabetes cooperatively accelerate amyloid beta and tau neurodegeneration

Chen, Y., Li, Z., Luo, S., Li, Z., Jiang, Y., Chen, K., Wang, J., Zhang, Z., & Initiative, A. D. N. (2026) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-026-08085-w · Cited by 1

Novel, Emerging Chip Models of the Blood-Brain Barrier and Future Directions

Holloway, P. M. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2289-6_11 · Cited by 1

Turmeric from Kitchen to Modern Medicine for Neurodegenerative Diseases

Bhattarai, S., Dhakal, M., & Pangeni, B. (2023) · Springer eBooks · doi:10.1007/978-981-99-7731-4_4 · Cited by 1

P3‐006: Models of tau pathology in induced pluripotent stem cell‐derived human neurons

Usenovic, M., Niroomand, S., Schachter, J. B., Zhou, H. H., Renger, J. J., & Parmentier‐Batteur, S. (2015) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2015.06.872

Extracellular Tau Oligomers Induce Disruption of Endogenous Tau Distribution, Invasion of Tau into the Somatodendritic Compartment and Axonal Transport Dysfunction

Swanson, E. C. (2017) · doi:10.18130/v3p643

Extracellular Tau Oligomers Induce Invasion of Endogenous Tau into the Somatodendritic Compartment and Axonal Transport Dysfunction

Swanson, E., Breckenridge, L., McMahon, L. P., Som, S., McConnell, I., & Bloom, G. S. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170168 · Cited by 76

Continuous Monitoring of Tau-Induced Neurotoxicity in Patient-Derived iPSC-Neurons

Oakley, D. H., Klickstein, N., Commins, C., Chung, M., Dujardin, S., Bennett, R. E., Hyman, B. T., & Frosch, M. P. (2021) · The Journal of Neuroscience · doi:10.1523/jneurosci.2590-20.2021 · Cited by 18

Dual Mechanism of Toxicity for Extracellular Injection of Tau Oligomers versus Monomers in Human Tau Mice

Manassero, G., Guglielmotto, M., Monteleone, D., Vasciaveo, V., Butenko, O., Tamagno, E., Arancio, O., & Tabaton, M. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170298 · Cited by 17