Tauopathies.

Neuropathological stageing of Alzheimer-related changes.

Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123

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

Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

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

Neurodegenerative Tauopathies

Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480

The spectrum of disease in chronic traumatic encephalopathy

McKee, A. C., Stein, T. D., Nowinski, C. J., Stern, R. A., Daneshvar, D. H., Alvarez, V. E., Lee, H.-S., Hall, G., Wojtowicz, S. M., Baugh, C. M., et al. (2013) · Brain · doi:10.1093/brain/aws307 · Cited by 2,098

Mutation in the tau gene in familial multiple system tauopathy with presenile dementia

Spillantini, M. G., Murrell, J. R., Goedert, M., Farlow, M. R., Klug, A., & Ghetti, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7737 · Cited by 1,474

Primary age-related tauopathy (PART): a common pathology associated with human aging

Crary, J. F., Trojanowski, J. Q., Schneider, J. A., Abisambra, J. F., Abner, E. L., Alafuzoff, I., Arnold, S. E., Attems, J., Beach, T. G., Bigio, E. H., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1349-0 · Cited by 1,467

Tau is a candidate gene for chromosome 17 frontotemporal dementia

Poorkaj, P., Bird, T. D., Wijsman, E., Nemens, E., Garruto, R. M., Anderson, L., Andreadis, A., Wiederholt, W. C., Raskind, M., & Schellenberg, G. D. (1998) · Annals of Neurology · doi:10.1002/ana.410430617 · Cited by 1,374

Frontotemporal dementia

Bang, J., Spina, S., & Miller, B. L. (2015) · The Lancet · doi:10.1016/s0140-6736(15)00461-4 · Cited by 1,144

Tau pathology and neurodegeneration

Spillantini, M. G., & Goedert, M. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70090-5 · Cited by 1,133

Preclinical characterization and IND‐enabling safety studies for PNT001, an antibody that recognizes cis‐pT231 tau

Foster, K., Manca, M., McClure, K. F., Koivula, P. P., Trojanowski, J. Q., Havas, D., Chancellor, S. E., Goldstein, L. E., Brunden, K. R., Kraus, A., et al. (2023) · Alzheimer s & Dementia · doi:10.1002/alz.13028 · Cited by 15

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 16

Zebrafish Models to Study New Pathways in Tauopathies

Barbereau, C., Cubedo, N., Maurice, T., & Rossel, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094626 · Cited by 14

Aging-Related Tau Astrogliopathy in Aging and Neurodegeneration

McCann, H., Durand, B., & Shepherd, C. E. (2021) · Brain Sciences · doi:10.3390/brainsci11070927 · Cited by 15

Histologic lesion type correlates of magnetic resonance imaging biomarkers in four-repeat tauopathies

Carlos, A. F., Tosakulwong, N., Weigand, S. D., Buciuc, M., Ali, F., Clark, H. M., Botha, H., Utianski, R. L., Machulda, M. M., Schwarz, C. G., et al. (2022) · Brain Communications · doi:10.1093/braincomms/fcac108 · Cited by 14

Lipid-Laden Microglia: Characterization and Roles in Diseases

Xing, J., McKenzie, T., & Hu, J. (2025) · Cells · doi:10.3390/cells14161281 · Cited by 13

ApoE-calypse tau: ApoE–tau synergy in Alzheimer’s disease

Lennol, M. P., Bordier, C., Kamelher, L., Ulrich, J. D., Holtzman, D. M., & Gratuze, M. (2025) · The Journal of Experimental Medicine · doi:10.1084/jem.20250965 · Cited by 14

Hyperphosphorylated Tau Relates to Improved Cognitive Performance and Reduced Hippocampal Excitability in the Young rTg4510 Mouse Model of Tauopathy

Xolalpa-Cueva, L., García-Carlos, C. A., Villaseñor-Zepeda, R., Orta-Salazar, E., Díaz-Miranda, S. Y., Peña‐Ortega, F., Perry, G., & Mondragón‐Rodríguez, S. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-215186 · Cited by 14

Phosphorylated Tau protein in the myenteric plexus of the ileum and colon of normothermic rats and during synthetic torpor

Chiocchetti, R., Hitrec, T., Giancola, F., Sadeghinezhad, J., Squarcio, F., Galiazzo, G., Piscitiello, E., Silva, M. D., Cerri, M., Amici, R., et al. (2021) · Cell and Tissue Research · doi:10.1007/s00441-020-03328-0 · Cited by 13

Astaxanthin inhibits apoptosis in a cell model of tauopathy by attenuating endoplasmic reticulum stress and unfolded protein response

Shi, H., & Zhao, Y. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176962 · Cited by 12

Novel Peptidomic Approach for Identification of Low and High Molecular Weight Tauopathy Peptides Following Calpain Digestion, and Primary Culture Neurotoxic Challenges

Yadikar, H., Johnson, C., Pafundi, N., Mouhawasse, E., Nguyen, L. T., Torres, I., Kurup, M., Yang, Z., Kobeissy, F. H., Yost, R. A., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20205213 · Cited by 12

Progress in the treatment of Parkinson-Plus syndromes

Olfati, N., Shoeibi, A., & Litvan, I. (2018) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2018.10.006 · Cited by 16

Endoplasmic Reticulum Stress in Tauopathies: Contrasting Human Brain Pathology with Cellular and Animal Models

Bocai, N. I., Marcora, M. S., Belfiori-Carrasco, L. F., Morelli, L., & Castaño, E. M. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-181021 · Cited by 12

Altered Brain Arginine Metabolism and Polyamine System in a P301S Tauopathy Mouse Model: A Time-Course Study

Mein, H., Yu, J., Ahmad, F., Zhang, H., & Liu, P. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116039 · Cited by 11

Induced pluripotent stem cell models as a tool to investigate and test fluid biomarkers in Alzheimer's disease and frontotemporal dementia

McInvale, J. J., Canoll, P., & Hargus, G. (2024) · Brain Pathology · doi:10.1111/bpa.13231 · Cited by 11

Genomic stress and impaired DNA repair in Alzheimer disease

Neven, J., Issayama, L. K., Dewachter, I., & Wilson, D. M. (2024) · DNA repair · doi:10.1016/j.dnarep.2024.103678 · Cited by 12

Retromer deficiency in Tauopathy models enhances the truncation and toxicity of Tau

Asadzadeh, J., Ruchti, E., Jiao, W., Limoni, G., MacLachlan, C., Small, S. A., Knott, G., Santa-Maria, I., & McCabe, B. D. (2022) · Nature Communications · doi:10.1038/s41467-022-32683-5 · Cited by 14

Exploring the significance of caspase-cleaved tau in tauopathies and as a complementary pathology to phospho-tau in Alzheimer’s disease: implications for biomarker development and therapeutic targeting

Rizzi, L., & Grinberg, L. T. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01744-9 · Cited by 12

MAPT mutations associated with familial tauopathies lead to formation of conformationally distinct oligomers that have cross‐seeding ability

Bhopatkar, A. A., Bhatt, N. N., Haque, M. A., Xavier, R., Fung, L., Jerez, C., & Kayed, R. (2024) · Protein Science · doi:10.1002/pro.5099 · Cited by 9

Tau immunotherapy in Alzheimer’s disease and progressive supranuclear palsy

Karimi, N., Catak, F. B., Arslan, E. O., Saghazadeh, A., & Rezaei, N. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109445 · Cited by 11

REMOVED: Nanodelivery of oxiracetam enhances memory, functional recovery and induces neuroprotection following concussive head injury

Niu, F., Sharma, A., Wang, Z., Feng, L., Muresanu, D. F., Sahib, S., Tian, Z. R., Lafuente, J. V., Buzoianu, A. D., Nozari, A., et al. (2021) · Progress in brain research · doi:10.1016/bs.pbr.2021.06.004 · Cited by 10

Aetiology and pathophysiology of neurodegenerative disorders

Sahoo, R. K., Gupta, T., Smily, Kumar, V., Rani, S., & Gupta, U. D. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85544-0.00006-x · Cited by 13

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

Novel insights into D-Pinitol based therapies: a link between tau hyperphosphorylation and insulin resistance

Vera, D. M., López-Gambero, A. J., Navarro, J. A., Sanjuan, C., Baixerás, E., Decara, J. M., & de Fonseca, F. R. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.379015 · Cited by 10

Interpretable Classification of Tauopathies with a Convolutional Neural Network Pipeline Using Transfer Learning and Validation against Post-Mortem Clinical Cases of Alzheimer’s Disease and Progressive Supranuclear Palsy

Diaz-Gomez, L., Gutierrez-Rodríguez, A. E., Martínez-Maldonado, A., Luna‐Muñoz, J., Cantoral-Ceballos, J. A., & Ontiveros‐Torres, M. Á. (2022) · Current Issues in Molecular Biology · doi:10.3390/cimb44120406 · Cited by 10

Reclassifying neurodegenerative diseases

Villoslada, P., Baeza-Yates, R. A., & Masdeu, J. C. (2020) · Nature Biomedical Engineering · doi:10.1038/s41551-020-0600-3 · Cited by 10

Downregulation of glob1 suppresses pathogenesis of human neuronal tauopathies in Drosophila by regulating tau phosphorylation and ROS generation

Nisha, N., & Sarkar, S. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105040 · Cited by 9

Methylation at a conserved lysine residue modulates tau assembly and cellular functions

Shams, H., Matsunaga, A., Ma, Q., Mofrad, M. R. K., & Didonna, A. (2022) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2022.103707 · Cited by 10

Benzothiazole Substitution Analogs of Rhodacyanine Hsp70 Inhibitors Modulate Tau Accumulation

Hill, S. E., Beaulieu‐Abdelahad, D., Lemus, A., Webster, J. M., Ospina, S. R., Darling, A. L., Martin, M. D., Patel, S., Bridenstine, L., Swonger, R., et al. (2023) · ACS Chemical Biology · doi:10.1021/acschembio.2c00919 · Cited by 9

GSK3β phosphorylation catalyzes the aggregation of Tau into Alzheimer’s disease-like amyloid strainPreprint

Chakraborty, P., de Opakua, A. I., Purslow, J. A., Fromm, S. A., Chatterjee, D., Zachrdla, M., Puri, S., Wolozin, B. L., & Zweckstetter, M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.19.572292 · Cited by 10

New Perspectives in Radiological and Radiopharmaceutical Hybrid Imaging in Progressive Supranuclear Palsy: A Systematic Review

Strobel, J., Müller, H.-P., Ludolph, A. C., Beer, A. J., Sollmann, N., & Kassubek, J. (2023) · Cells · doi:10.3390/cells12242776 · Cited by 10

SCRN1: A cerebrospinal fluid biomarker correlating with tau in Alzheimer's disease

Weiner, S., Sauer, M., Brinkmalm, G., Constantinescu, J., Constantinescu, R., Gomes, B. F., Becker, B., Nellgård, B., Dalla, K., Galasko, D. R., et al. (2023) · Alzheimer s & Dementia · doi:10.1002/alz.13042 · Cited by 9

Effect of Natural Osmolytes on Recombinant Tau Monomer: Propensity of Oligomerization and Aggregation

Arar, S. H., Haque, M. A., Bhatt, N. N., Zhao, Y., & Kayed, R. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00614 · Cited by 9

Stress Response Is the Main Trigger of Sporadic Amyloidoses

Galkin, A. P., & Sysoev, E. I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22084092 · Cited by 10

Brain Cell Type-Specific Nuclear Proteomics Is Imperative to Resolve Neurodegenerative Disease Mechanisms

Nelson, R. S., Dammer, E. B., Santiago, J. V., Seyfried, N. T., & Rangaraju, S. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.902146 · Cited by 10

Synthetic torpor triggers a regulated mechanism in the rat brain, favoring the reversibility of Tau protein hyperphosphorylation

Squarcio, F., Hitrec, T., Piscitiello, E., Cerri, M., Giovannini, C., Martelli, D., Occhinegro, A., Taddei, L., Tupone, D., Amici, R., et al. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1129278 · Cited by 7

Disentangling on and off-target binding in flortaucipir PET: a voxel-to-voxel P-tau, ferric iron, and MAO-B histology-to-flortaucipir PET comparison

Chen, Y., Joie, R. L., Pereira, F. L., Blazhenets, G., Zhu, L., Spina, S., Seeley, W. W., Heinsen, H., Ushizima, D. M., Tosun, D., et al. (2026) · Acta Neuropathologica · doi:10.1007/s00401-026-02983-x · Cited by 12

A Clinicopathologic Study of Movement Disorders in Frontotemporal Lobar Degeneration

Pablo‐Fernández, E. D., González‐Herrero, B., Santacruz, D. M. C., Rossor, M. N., Schott, J. M., Lashley, T., Holton, J. L., Fox, N. C., Révész, T., Warren, J. D., et al. (2020) · Movement Disorders · doi:10.1002/mds.28356 · Cited by 10

Blocking Site-Specific Cleavage of Human Tau Delays Progression of Disease-Related Phenotypes in Genetically Matched Tau-Transgenic Mice Modeling Frontotemporal Dementia

Steuer, E. L., Kemper, L. J., Hlynialuk, C. J. W., Leinonen-Wright, K., Montonye, M. L., Lapcinski, I. P., Forster, C. L., Ashe, K. H., & Liu, P. (2022) · Journal of Neuroscience · doi:10.1523/jneurosci.0543-22.2022 · Cited by 9

Mechanisms linking cerebrovascular dysfunction and tauopathy: Adding a layer of epiregulatory complexity

Kim, Y. A., Mellén, M., Kızıl, Ç., & Santa‐María, I. (2023) · British Journal of Pharmacology · doi:10.1111/bph.16280 · Cited by 9

DYRK1A in the physiology and pathology of the neuron-astrocyte axis

Cisternas, P., Kim, J.-Y., Ashfeld, B. L., & Zartman, J. J. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1626062 · Cited by 7

Disease-Associated Mutations in Tau Encode for Changes in Aggregate Structure Conformation

Sun, K. T., Patel, T., Kang, S., Yarahmady, A., Srinivasan, M., Julien, O., Heras, J., & Mok, S. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00422 · Cited by 7

SARS-CoV-2 Nucleocapsid Protein Induces Tau Pathological Changes That Can Be Counteracted by SUMO2

Orsini, F., Bosica, M., Martucci, A., Paola, M. D., Comolli, D., Pascente, R., Forloni, G., Fraser, P. E., Arancio, O., & Fioriti, L. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25137169 · Cited by 7

Discovery of Azaindolin-2-One as a Dual Inhibitor of GSK3β and Tau Aggregation with Potential Neuroprotective Activity

Ali, T. F. S., Ciftci, H. I., Radwan, M. O., Roshdy, E., Shawky, A. M., Abourehab, M. A. S., Tateishi, H., Otsuka, M., & Fujita, M. (2022) · Pharmaceuticals · doi:10.3390/ph15040426 · Cited by 7

Blood Biomarkers Predict Future Cognitive Decline after Military-Related Traumatic Brain Injury

Lippa, S. M., Gill, J., Brickell, T. A., Guedes, V. A., French, L. M., & Lange, R. T. (2022) · Current Alzheimer Research · doi:10.2174/1567205019666220330144432 · Cited by 8

Imaging of Tauopathies with PET Ligands: State of the Art and Future Outlook

Conte, M., Feo, M. S. D., Sidrak, M. M. A., Corica, F., Gorica, J., Granese, G. M., Filippi, L., Vincentis, G. D., & Frantellizzi, V. (2023) · Diagnostics · doi:10.3390/diagnostics13101682 · Cited by 8

Tau Fibrillation Induced by Heparin or a Lysophospholipid Show Different Initial Oligomer Formation

Rasmussen, H. Ø., Nielsen, J., de Poli, A., Otzen, D. E., & Pedersen, J. S. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168194 · Cited by 7

Tau Oligomers as Pathogenic Seeds: Preparation, Characterization, and Propagation In Vitro and In Vivo

Sengupta, U., & Kayed, R. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3629-9_9 · Cited by 8

Predictors of hippocampal tauopathy in people with and at risk for human immunodeficiency virus infection

Nader, S., Karlovich, E., Cortes, E. P., Insausti, R., Meloni, G., Jacobs, M. M., Crary, J. F., & Morgello, S. (2023) · Journal of NeuroVirology · doi:10.1007/s13365-023-01181-9 · Cited by 7

Time-Dependent Long-Term Effect of Memantine following Repetitive Mild Traumatic Brain Injury

Boucher, M. L., Conley, G. M., Morriss, N. J., Ospina-Mora, S., Qiu, J., Mannix, R., & Meehan, W. P., III (2024) · Journal of Neurotrauma · doi:10.1089/neu.2023.0423 · Cited by 6

Brain Drug Delivery: Overcoming the Blood-brain Barrier to Treat Tauopathies

Hanes, J., Dobáková, E., & Majerová, P. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200316130128 · Cited by 6

Contemporary approaches to clinical diagnosis and treatment of tau-protein accumulation related multisystem degenerations

Васенина, Е. Е., & Levin, O. S. (2020) · S S Korsakov Journal of Neurology and Psychiatry · doi:10.17116/jnevro202012010222 · Cited by 5

Interactions of Polyphenolic Gallotannins with Amyloidogenic Polypeptides Associated with Alzheimer’s Disease: From Molecular Insights to Physiological Significance

Khalifa, J., Bourgault, S., & Gaudreault, R. (2023) · Current Alzheimer Research · doi:10.2174/0115672050277001231213073043 · Cited by 6

Modulation of Primary and Secondary Processes in Tau Fibril Formation by Salt-Induced Dynamics

Vahid, A. A., Hassan, M. S. O., Sahayaraj, A. E., Babu, A. T., Kizhakkeduth, S. T., & Vijayan, V. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00852 · Cited by 6

Tau Protein Aggregation Inhibitors—Therapeutic Strategy for Concurrent Tau and Amyloid Aggregation Inhibition

Schreiner, T. G., Ciobanu, R. C., & Schreiner, O. D. (2026) · Biomedicines · doi:10.3390/biomedicines14030522 · Cited by 6

SUMO2 rescues neuronal and glial cells from the toxicity of P301L Tau mutant

Orsini, F., Pascente, R., Martucci, A., Palacino, S., Fraser, P. E., Arancio, O., & Fioriti, L. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1437995 · Cited by 5

Fluorescently-labelled amyloid paired helical filaments (PHF) in monitoring its fibrillation kinetics

Šmidlehner, T., Bonnet, H., Chierici, S., & Piantanida, I. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104196 · Cited by 5

Medial Temporal Lobe Involvement in Human Prion Diseases: Implications for the Study of Focal Non Prion Neurodegenerative Pathology

Rábano, A., Márquez, C. G., Juste, R. A., Geijó, M., & Calero, M. (2021) · Biomolecules · doi:10.3390/biom11030413 · Cited by 5

Sporadic Creutzfeldt–Jakob disease with extremely long 14‐year survival period

Zubizarreta, I. K., Onandi, R. R., Pereda, A., Vado, Y., González‐Chinchon, G., Eraña, H., de Nanclares, G. P., & Castilla, J. (2021) · European Journal of Neurology · doi:10.1111/ene.14946 · Cited by 8

The reverse transcriptase inhibitor 3TC modulates hippocampal transcriptome signatures of inflammation in tauopathy model mice

Wahl, D., Grant, R. A., & LaRocca, T. J. (2024) · Experimental Gerontology · doi:10.1016/j.exger.2024.112458 · Cited by 4

A Comprehensive Review on Preclinical Alzheimer's Disease Models: Evaluating their Clinical Relevance

Kushwaha, V., & Sahu, K. K. (2024) · Current Pharmaceutical Biotechnology · doi:10.2174/0113892010331845240802073645 · Cited by 5

Complement dysregulation in human tauopathies

Nimmo, J., Keat, S., Muynck, L. D., & Morgan, B. P. (2025) · Brain Pathology · doi:10.1111/bpa.70017 · Cited by 4

Tauopathies: Calmodulin Regulates Tau Hyperphosphorylation and Its Transformation into Disease-Specific Aggregates

O’Day, D. H. (2025) · Biomolecules · doi:10.3390/biom15081133 · Cited by 5

Sex differences for clinical presentations and co-pathologies in four-repeat tauopathies

Bayram, E., Carter, D. J., Aslam, S., Forbes, E. K., & Holden, S. K. (2026) · Biology of Sex Differences · doi:10.1186/s13293-026-00899-5 · Cited by 4

Immunotherapeutic Approaches for the Treatment of Neurodegenerative Diseases: Challenges and Outcomes

Mondal, A. C., & Sushma (2021) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527321666211228100955 · Cited by 4

Substituent Orchestration in Dimethylquinoxaline Derivatives: A Tool for Fishing Out Appropriate CDK5 Inhibitors as Potential Therapeutics for Alzheimer's

Jain, A. K., Gupta, A., Karthikeyan, C., Trivedi, P., & Konar, A. D. (2022) · Chemistry & Biodiversity · doi:10.1002/cbdv.202200116 · Cited by 4

Molecular Interactions between Tau Protein and TIA1: Distinguishing Physiological Condensates from Pathological Fibrils

Kizhakkeduth, S. T., Vahid, A. A., Hassan, M. S. O., Parambil, A. K., Jain, P., & Vijayan, V. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00456 · Cited by 3

Solubility and Metastability of the Amyloidogenic Core of Tau

Axell, E., Carlsson, A., Lindberg, M., Bernfur, K., Sparr, E., & Linse, S. S. (2026) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00784 · Cited by 3

Organoids, Biocybersecurity, and Cyberbiosecurity—A Light Exploration

Palmer, X., Akafia, C. S. K., Woodson, E., Woodson, A., & Potter, L. N. (2024) · Organoids · doi:10.3390/organoids3020007 · Cited by 3

Neurosteroids Alter p-ERK Levels and Tau Distribution, Restraining the Effects of High Extracellular Calcium

Konsta, V., Paschou, M., Koti, N., Vlachou, M. E., Livanos, P., Xilouri, M., & Papazafiri, P. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252111637 · Cited by 3

Role of non-neuronal cells in neurorepair: a focus on proteinopathy and neurodegeneration

Rodríguez-Carreiro, S., Nogales, M. D. C., Jiménez-Galán, D., Carmona-Lorenzo, S., Caro-Martín, A., Navarro, E., & Esteras, N. (2024) · Regenerative medicine reports . · doi:10.4103/regenmed.regenmed-d-24-00005 · Cited by 2

Computational Investigation of the Interaction Mechanism of Some anti-Alzheimer Drugs with the Acetylcholinesterase Enzyme

Çeli̇k, S., Demirağ, A. D., COŞGUN, A. O., Özel, A. E., & Akyüz, S. (2023) · Open Journal of Nano · doi:10.56171/ojn.1109606 · Cited by 3

Primary progressive freezing gait with impressive response to laser light visual cueing: a video case report

León‐Ruiz, M., García-Soldevilla, M. Á., & Ristol, E. G.-A. (2018) · Journal of Neurology · doi:10.1007/s00415-018-8966-9 · Cited by 3

Generation of 17q21.31 duplication iPSC-derived neurons as a model for primary tauopathies

Miguel, L., Rovelet‐Lecrux, A., Chambon, P., Joly‐Hélas, G., Rousseau, S., Wallon, D., Epelbaum, S., Frébourg, T., Campion, D., Nicolas, G., et al. (2022) · Stem Cell Research · doi:10.1016/j.scr.2022.102762 · Cited by 3

Abnormal Tau Protein Influences Intercellular Mitochondrial Transfer Between Astrocytic and Neuronal CellsPreprint

Riou, A., Broeglin, A., Papassotiropoulos, A., Eckert, A., & Grimm, A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.11.648113 · Cited by 3

Differential expression profiles of MAPT (TAU) gene isoforms in dry age-related macular degeneration

Lak, S. S., Kanavi, M. R., Bayat, K., Ahmadieh, H., Soheili, Z., & Suri, F. (2025) · Experimental Eye Research · doi:10.1016/j.exer.2025.110517 · Cited by 2

Selective reduction of KCNA4 in vulnerable glutamatergic–serotonin neurons of the dorsal raphe nucleus in Alzheimer's disease

Kolling, L. J., Balasubramanian, N., Ismail, S., Feller, A. J., Alberhasky, J. M. H., Wang, R., Jennings, L., Hefti, M. M., & Marcinkiewcz, C. A. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71317 · Cited by 2

rTg4510 Tauopathy Mice Exhibit Non-Spatial Memory Deficits Prevented by Doxycycline Treatment

Kishimoto, Y., Kubota, T., Nakashima, K., & Kirino, Y. (2025) · Brain Sciences · doi:10.3390/brainsci15111183 · Cited by 2

Deep Learning-Based Classification of Temporal Stages of AT8-Labeled Tau Pathology After Experimental Traumatic Brain Injury

Sousa, G. J. A., Sá, R. A., Gomes, M. A. S. M., Edwards, G. A., Moreno‐González, I., & de Sousa, R. J. A. (2026) · Neuroinformatics · doi:10.1007/s12021-025-09763-0 · Cited by 2

Sodium selenate as a therapeutic for tauopathies: A hypothesis paper

Dilcher, R., Malpas, C. B., Walterfang, M., Velakoulis, D., O'Brien, T. J., & Vivash, L. E. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.915460 · Cited by 2

Molecular mechanisms and biomarkers underlying the protective roles of the nutraceutical laminarin against ischaemic strokes

Luo, J., Lan, Y., Pan, W., Lai, K. P., & Kong, D. (2023) · Food and Agricultural Immunology · doi:10.1080/09540105.2023.2249265 · Cited by 2

The Possible Associations between Tauopathies and Atherosclerosis, Diabetes Mellitus, Dyslipidemias, Metabolic Syndrome and Niemann–Pick Disease

Fryncel, A., Madetko‐Alster, N., Krępa, Z., Kuch, M., & Alster, P. (2024) · Diagnostics · doi:10.3390/diagnostics14161831 · Cited by 2

Abnormal Structural–Functional Coupling and MRI Alterations of Brain Network Topology in Progressive Supranuclear Palsy

Qu, J., Zhu, R., Wu, Y., Xu, G., & Wang, D. (2024) · Journal of Magnetic Resonance Imaging · doi:10.1002/jmri.29620 · Cited by 2

ICAM-1 and IL-10 are associated with cognitive dysfunction using the MoCA test in glioma: Findings from the NCI Neuro-Oncology Branch Natural History Study

Slattery, K., Kauss, M. C., Raval, D., Hsieh, E., Choi, A., Davis, T. S., Robins, K. R., Miller, H., Vera, E. M., Wright, M. L., et al. (2025) · Neuro-Oncology Advances · doi:10.1093/noajnl/vdaf002 · Cited by 2

Nanotheranostic Approach for Targeting Tauopathies in Alzheimer's Disease: Mechanistic Insight and Recent Advances

Sahu, K. K., Chaudhary, R., Farooqi, M. A., & Kaurav, M. (2024) · Drug Delivery Letters · doi:10.2174/0122103031331346241122152643 · Cited by 1

Exploring the Biological Connection Between Tau and PrPC in Neuronal Cells: GSK3β as a Possible Key Player

Gavín, R., & del Río, J. A. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05163-2 · Cited by 2

Tau Oligomers in Alzheimer’s Disease: Modulation Effect of Osmolytes on Amplified Brain-Derived Tau Oligomers

Arar, S. H., Haque, M. A., Kayed, A., Khan, S., Bhatt, N. N., Zhao, Y., & Kayed, R. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00122 · Cited by 1

Clinicopathological features of primary tauopathies: a brain bank series

Ryan, B., Marriott, L., Murray, H. C., Faull, R. L. M., Turner, C. P., & Curtis, M. A. (2026) · Frontiers in Neurology · doi:10.3389/fneur.2026.1768959 · Cited by 1

Diagnostic accuracy of CSF and plasma pTau-181, pTau-217, and pTau-231 for Alzheimer’s disease: a diagnostic meta-analysis

Mohammed, H. E., Haseeb, M. E., Nasser, M., Hanen, G., Abdelkader, M., Yaser, H., Yaser, S., Samir, A., Arafeh, Y., Wagdy, M., et al. (2026) · Acta Neurologica Belgica · doi:10.1007/s13760-026-03107-8 · Cited by 1

Amylin at the crossroads of type 2 diabetes and neurodegenerative diseases

Castillo, I. L. D., Garcia-Martin, J., Gutiérrez, A., & Moreno‐González, I. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103226 · Cited by 1

Nanowired Delivery of Cerebrolysin Together with Antibodies to Amyloid Beta Peptide, Phosphorylated Tau, and Tumor Necrosis Factor Alpha Induces Superior Neuroprotection in Alzheimer’s Disease Brain Pathology Exacerbated by Sleep Deprivation

Sharma, A., Feng, L., Muresanu, D. F., Tian, Z. R., Lafuente, J. V., Buzoianu, A. D., Nozari, A., Bryukhovetskiy, I., Manzhulo, I., Wiklund, L., et al. (2023) · Advances in neurobiology · doi:10.1007/978-3-031-32997-5_1 · Cited by 1

Criterios diagnósticos en la enfermedad demencial ¿Qué hay de nuevo?

Labos, E., Bavec, C. V., Cristalli, D. O., Deschle, F., Isaac, C. F., Dorman, G. S., Ollari, J., Rubiño, V., & Russo, M. J. (2023) · Vertex Revista Argentina de Psiquiatría · doi:10.53680/vertex.v34i160.460 · Cited by 4

Modeling Taupathies in Zebrafish (Danio rerio)

Kotova, M. M., Kolesnikova, T. O., & Kalueff, A. V. (2023) · Российский физиологический журнал им И М Сеченова · doi:10.31857/s0869813923110067 · Cited by 1

Tau amyloid polymorphism is shaped by local structural propensities of its protein sequencePreprint

Louros, N. N., Wilkinson, M., Tsaka, G., Ramakers, M., Morelli, C., Garcia, T., Gallardo, R. U., D’Haeyer, S., Goossens, V., Audenaert, D., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.24.512987 · Cited by 1

α5-GABA-A Receptor Positive Allosteric Modulation prevents neuronal atrophy and cognitive decline independently of p-Tau accumulation in the PS19 mouse modelPreprint

Dharavath, R. N., Bernardo, A. M., Marceau-Linhares, C., Marcotte, M. D., Mezo‐González, C. E., Wong, K. D., Pina‐Leblanc, C., Bouchet, A., Sharmin, D., Pandey, K. P., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.07.611810 · Cited by 1

Post-Mortem 7.0-Tesla Magnetic Resonance Imaging of the Hippocampus in Progressive Supranuclear Palsy with and without Cerebral Amyloid Angiopathy

Reuck, J. D., Auger, F., Durieux, N., Maurage, C., Deramecourt, V., Cordonnier, C., Pasquier, F., Leys, D., & Bordet, R. (2020) · NeuroSci · doi:10.3390/neurosci1020011

CULTURE OF LEARNING AND PERFORMANCE GOALS IN THE UAE EDUCATION

Alkaabi, A. M. (2014) · ICERI proceedings

A Brief Overview of Pathological Tau and Inhibitors and Modifiers of Tau Aggregation for Treatment of Tauopathies

Manthapuri, S. S., & Davis, E. (2021) · Journal of Student Research · doi:10.47611/jsrhs.v10i4.2468

Aluminum-Induced AD-Like Pathological Features

Yang, J. (2023) · Springer eBooks · doi:10.1007/978-981-99-1592-7_8

Modeling Tauopathies in Zebrafish (Danio rerio)

Kotova, M. M., Kolesnikova, T. O., & Kalueff, A. V. (2023) · Journal of Evolutionary Biochemistry and Physiology · doi:10.1134/s0022093023060133

Invited review: Neuropathology of tauopathies: principles and practice

Kovacs, G. G. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12208 · Cited by 492

Tau Pathology in Neurodegenerative Diseases

Vogels, T., & Hromádka, T. (2021) · Neuromethods · doi:10.1007/978-1-0716-1712-0_4 · Cited by 2

The tauopathies

Devi, G. (2023) · Handbook of clinical neurology · doi:10.1016/b978-0-323-98817-9.00015-6 · Cited by 27

The Neuropathological Spectrum of Neurodegenerative Tauopathies

Tolnay, M., & Probst, A. (2003) · IUBMB Life · doi:10.1080/1521654032000114348 · Cited by 59

A peculiar constellation of tau pathology defines a subset of dementia in the elderly

Kovács, G. G., Molnár, K., László, L., Ströbel, T., Botond, G., Hönigschnabl, S., Reiner‐Concin, A., Palkovits, M., Fischer, P. A., & Budka, H. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0819-x · Cited by 90