Soluble hyper-phosphorylated tau causes microtubule breakdown and functionally compromises normal tau in vivo

Physical basis of cognitive alterations in alzheimer's disease: Synapse loss is the major correlate of cognitive impairment

Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.

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

Lithium inhibits glycogen synthase kinase-3 activity and mimics wingless signalling in intact cells

Stambolic, V., Ruel, L., & Woodgett, J. R. (1996) · Current Biology · doi:10.1016/s0960-9822(02)70790-2 · Cited by 1,321

Differential Regulation of Dynein and Kinesin Motor Proteins by Tau

Dixit, R., Ross, J. L., Goldman, Y. E., & Holzbaur, E. L. F. (2008) · Science · doi:10.1126/science.1152993 · Cited by 1,012

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

Tauopathy in Drosophila : Neurodegeneration Without Neurofibrillary Tangles

Wittmann, C. W., Wszolek, M. F., Shulman, J. M., Salvaterra, P. M., Lewis, J., Hutton, M., & Feany, M. B. (2001) · Science · doi:10.1126/science.1062382 · Cited by 939

Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding

Bramblett, G. T., Goedert, M., Jakes, R., Merrick, S. E., Trojanowski, J. Q., & Lee, V. M. Y. (1993) · Neuron · doi:10.1016/0896-6273(93)90057-x · Cited by 903

Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly

Cleveland, D. W., Hwo, S. Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90214-5 · Cited by 881

Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau)

Wood, J. G., Mirra, S. S., Pollock, N. J., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4040 · Cited by 763

Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease.

Alonso, A. C., Zaidi, T., Grundke-Iqbal, I., & Iqbal, K. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.12.5562 · Cited by 738

Microtubule disruption upon CNS damage triggers mitotic entry via TNF signaling activation

Barros, C. S., & Bossing, T. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109325 · Cited by 11

New perspective on neurodegenerative diseases: Focusing on the interaction between autophagy and oxidative stress and targeted strategies

Jin, J., Cen, Q., Wang, H., Xin, Y., Feng, J., Cui, Y., Li, J., You, Z., Jing, F., Yu, Y., et al. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107283 · Cited by 10

Histone deacetylase’s regulates Tau function in Alzheimer’s disease

Chinnathambi, S. (2024) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2024.09.008 · Cited by 9

Tau-mediated axonal degeneration is prevented by activation of the WldS pathway

Stubbs, K., Batchelor, B. G., Sivanantharajah, L., Sealey, M. A., Moreno, M. R., Ruiz, E., Richardson, B., Perry, V. H., Newman, T. A., & Mudher, A. K. (2023) · Brain Communications · doi:10.1093/braincomms/fcad052 · Cited by 9

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

The Role of Smad Proteins for Development, Differentiation and Dedifferentiation of Neurons

Ueberham, U., & Arendt, T. (2013) · InTech eBooks · doi:10.5772/54532 · Cited by 12

An Overview of Transgenic Mouse Models for the Study of Alzheimer’s Disease

Lopes, P. A., Pádua, M. S., & Guil‐Guerrero, J. L. (2025) · Journal of dementia and Alzheimer's disease · doi:10.3390/jdad2010002 · Cited by 9

Lysosome trafficking across intracellular and intercellular networks in the brain

Murphy, D. T., & Lo, C. H. (2026) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2026.1755292 · Cited by 8

Tau phosphorylation homeostasis: Mechanisms, targets, and therapeutic implications in Alzheimer’s disease

Lu, S., Qiu, S., Yu, G., Zhang, A., & Zhao, Q. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103097 · Cited by 8

What we can learn from animal models about cerebral multi-morbidity

Baker, S. L., & Götz, J. (2015) · Alzheimer s Research & Therapy · doi:10.1186/s13195-015-0097-2 · Cited by 8

Effects of obesity on hippocampus function: Synaptic plasticity hypothesis

Al-Dalaeen, A. M., Ahram, M. A., & Al-Domi, H. A. (2020) · Obesity Medicine · doi:10.1016/j.obmed.2020.100246 · Cited by 8

Tau Forms Oligomeric Complexes on Microtubules that are Distinct from Pathological Oligomers in Disease

Gyparaki, M. T., Arab, A., Sorokina, E. M., Santiago-Ruiz, A. N., Bohrer, C. H., Xiao, J., & Lakadamyali, M. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2020.11.442 · Cited by 8

The Role of Aβ and Tau Oligomers in the Pathogenesis of Alzheimer’s Disease

Bhaskar, K., & Lamb, B. T. (2011) · Springer eBooks · doi:10.1007/978-94-007-2774-8_5 · Cited by 8

Modeling neurodegenerative and neurodevelopmental disorders in theDrosophilamushroom bodyPreprint

Stahl, A., & Tomchik, S. M. (2024) · Learning & Memory · doi:10.1101/lm.053816.123 · Cited by 8

Torpor induces reversible tau hyperphosphorylation and accumulation in mice expressing human tau

Mestdagh, C. F. D. V., Witte, M. E., Scheper, W., Smit, A. B., Henning, R. H., & van Kesteren, R. E. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01800-4 · Cited by 7

Age dependent trans-cellular propagation of human tau aggregates in Drosophila disease models

Aqsa, A., & Sarkar, S. (2020) · Brain Research · doi:10.1016/j.brainres.2020.147207 · Cited by 7

Tau Phosphorylation and μ-Calpain Activation Mediate the Dexamethasone-Induced Inhibition on the Insulin-Stimulated Akt Phosphorylation

Liu, Y., Su, Y., Sun, S., Wang, T., Qiao, X., Run, X., & Liang, Z. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035783 · Cited by 6

Protein Phosphatase 5-Recruiting Chimeras for Accelerating Tau Dephosphorylation

Gu, J., He, C., Han, Z., Huang, Q., He, Y., Lu, Y., You, Q., Zhang, Q., & Wang, L. (2025) · ACS Chemical Biology · doi:10.1021/acschembio.5c00165 · Cited by 5

Dynamic 3D-Network Coating Composite Enables Global Isolation of Phosphopeptides, Stepwise Separation of Mono- and Multi-Phosphopeptides, and Phosphoproteomics of Human Lung Cells

Liu, L., Chen, Z., Wang, D., Liang, W., Wang, B., Xia, C., Yan, Y., Ding, C., Meng, X., & Liang, H. (2025) · Biomolecules · doi:10.3390/biom15060894 · Cited by 4

The Potential of Small Molecules in Preventing Tau Oligomer Formation and Toxicity

Gerson, J. E., Cascio, F. L., & Kayed, R. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803690-7.00006-5 · Cited by 4

Prefoldin 5 is a microtubule-associated protein that suppresses Tau aggregation and neurotoxicity

Bisht, A., Pippadpally, S., Majumder, S., Gopi, A. T., Das, A., Sahi, C., Ramaswami, M., & Kumar, V. (2024) · eLife · doi:10.7554/elife.104691.3 · Cited by 4

Is tau pathology a relevant factor in neuronal damage induced by alcohol and other drugs?

Olesen, M. A., Ancía, A., & Quintanilla, R. A. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.168059 · Cited by 3

The Insight into the Role of Protein Misfolding and Tau Oligomers in Alzheimer’s Disease

Pandey, P., Kumar, C., & Khandia, R. (2025) · Springer eBooks · doi:10.1007/978-981-96-6202-9_12 · Cited by 3

Examining the vulnerability of adult neuron subtypes to tau-mediated toxicity in Drosophila

Sivanantharajah, L., Mudher, A. K., & Shepherd, D. (2025) · Translational Psychiatry · doi:10.1038/s41398-025-03342-2 · Cited by 2

Drosophila wing is a high-throughput and versatile screening tool for Tau-mediated disease mechanisms and drug discovery

Moreno, M. R., Cooper, A. S., Lian, T., Liu, J., Abtahi, S., Skoulakis, E. M. C., Sivanantharajah, L., Allan, D. W., & Mudher, A. K. (2026) · Disease Models & Mechanisms · doi:10.1242/dmm.052492 · Cited by 2

Drosophila Models of Tauopathy

Ali, Y., Ruan, K., & Zhai, R. G. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405195-9.00054-8 · Cited by 2

Profiling Brain Trauma in Professional American-style Football and the Implications to Developing Neurological Injury

Karton, C. (2019) · uO Research (University of Ottawa) · doi:10.20381/ruor-24220 · Cited by 2

Stabilizing microtubules increases acute cellular injury at high strain rates

Kang, G., Webster, E., Delgado, D. D. S., Holahan, M. R., Banton, R. J., Petel, O. E., & Harris, A. R. (2025) · Biophysical Journal · doi:10.1016/j.bpj.2025.10.024 · Cited by 1

Tau-Centric Therapies for Treating Alzheimer’s Disease

Quraishe, S., Cowan, C. M., & Mudher, A. K. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803690-7.00005-3 · Cited by 1

Models of Alzheimer’s Disease

Chen, M., Kretzschmar, D., Verdile, G., & Lardelli, M. T. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-415894-8.00025-7 · Cited by 2

Cogs in the autophagic machine—equipped to combat dementia-prone neurodegenerative diseases

de Wet, S., Theart, R. P., & Loos, B. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1225227 · Cited by 1

Are we missing a trick by not exploiting fruit flies in inflammation-led drug discovery for neurodegeneration?

Price, R., Moreno, M. R., Cooper, A. S., Singh, R., Khaw, Y. M., Mhaka, A. M., Sivanantharajah, L., & Mudher, A. K. (2025) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2025.2498675 · Cited by 1

Cytoskeletal proteins regulates Tau protein in Alzheimer’s disease

Chinnathambi, S., & Adityan, A. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.029 · Cited by 1

NDUFA12L mitochondrial complex-I assembly factor: Implications for taupathies

Salama, M., & Mohamed, W. M. Y. (2015) · Applied & Translational Genomics · doi:10.1016/j.atg.2015.05.003 · Cited by 1

Aggregation promoting sequences rather than phosphorylation are essential for Tau-mediated toxicity in DrosophilaPreprint

Cooper, A. S., Richardson, B., Ruiz, E., Zhang, Y., Batchelor, B., Chithran, A. V., Liu, J., Lian, T., Moreno, M. R., Boehme, B., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.22.629946 · Cited by 1

Early memory deficits and extensive brain network disorganization in the AppNL-F/MAPT double knock-in mouse model of familial Alzheimer's disease

Borcuk, C. (2021) · theses.fr (ABES) · doi:10.70675/c316f2dcz54d3z41cfzb3f5z99c7b2d3cd95 · Cited by 1

Drosophila model of cognitive disorders: Focus on memory abnormality

Shao, L., & Zhong, Y. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9780511920585.013

A Genome-Wide Screen on Modifiers of Tau-Induced Neurodegeneration Using RNAi-Mediated Gene Silencing in Drosophila

Butzlaff, M. (2011) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-1007

Drosophila melanogaster as a Model System for the Study of Human Neuropathy and the Testing of Neuroprotectors

Matiytsiv, N. P., & Chernyk, Y. I. (2020) · Cytology and Genetics · doi:10.3103/s0095452720030081

Drug discovery in Alzheimer’s disease using metal chelators: Warning toward their usage

Mutoh, T. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-89906-2.00005-8

Happiness as a Local Invariant of Pain: A Perspective on Spontaneous and Induced Emotions

Dutta, T., & Bandyopadhyay, A. (2024) · Studies in Rhythm Engineering · doi:10.1007/978-981-99-9334-5_8

Prefoldin 5 is a microtubule-associated protein that suppresses Tau-aggregation and neurotoxicityPreprint

Bisht, A., Pippadpally, S., Majumder, S., Gopi, A. T., Das, A., Sahi, C., Ramaswami, M., & Kumar, V. (2025) · eLife · doi:10.7554/elife.104691.2

The Role of c-Abl in Alzheimer’s Disease: Guilty or not Guilty?

Li, W., Wang, X., Liu, J., & Chen, Y. (2025) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-025-01650-1

Additional file 1 of Torpor induces reversible tau hyperphosphorylation and accumulation in mice expressing human tau

Mestdagh, C. F. D. V., Witte, M. E., Scheper, W., Smit, A. B., Henning, R. H., & van Kesteren, R. E. (2024) · Figshare · doi:10.6084/m9.figshare.26729566

Implications of virus-induced stress granules in tauopathies

Sharma, S., Vandenakker, A., Cortes-Pérez, C. M., Milne, S., & Douville, R. N. (2026) · Translational Neurodegeneration · doi:10.1186/s40035-026-00538-4

Les nanotubes comme nouvelle voie de transfert et de propagation de la protéine Tau pathologique

Tardivel, M. (2017) · theses.fr (ABES) · doi:10.70675/0cfcd049z970ez4f2dz8417z195cfabdc00d

Inducing β-hairpin and α-helix folding in peptides : design, synthesis and evaluation of α-synuclein and tau aggregation inhibitors

Bisi, N. (2023) · theses.fr (ABES) · doi:10.70675/657635ccz1a16z4ba8za94ez401ac3bdaf48

The light at the end of the tunnel : study of early-stage brain dynamics alterations in Alzheimer’s disease and beneficial effects of light stimulation in the AppNL-F/MAPT mouse model

Aguilera, M. (2024) · theses.fr (ABES) · doi:10.70675/dc614591zf8f9z4a6dzb174za8a482fa3ece

Cytoskeletal Imbalance and Axonal Vulnerability in Sporadic PSP-RS: Early Changes in a Human iPSC-Derived Neuronal Model with Altered mTOR Signaling

Covello, R., Benedetto, G. L., Scalise, S., Gabriele, C., Valente, D., Zannino, C., Puccio, B., Quattrone, A., Guzzi, P. H., Gaspari, M., et al. (2026) · Cells · doi:10.3390/cells15090754

Evolution of the Neurometabolic Cascade of Traumatic Brain Injury

Flavin, W. P., Bickart, K. C., Belle, J. E. L., Babikian, T., Harris, M., Kamins, J., Pineda, J. A., Choe, M. C., Giza, C. C., & Prins, M. L. (2026) · Neurologic Clinics · doi:10.1016/j.ncl.2026.05.001

Small Molecules as Anti-Alzheimer’s Scaffolds

Hazra, R., Roy, S., Gayen, S., Parui, A., Arshad, A., Roy, N., & Sarkar, A. N. (2026) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9798898815646126010013

Cell-Based Tau Polymerization Assays

Horgan, N. G., Ibrahium, O. M. H., Ademoye, T. A., Fortin, J. S., & Ostafe, R. (2026) · Neuromethods · doi:10.1007/978-1-0716-5234-3_12

When myelin breaks, tau aggregates — a new perspective on Alzheimer's disease

Tiane, A., van den Hove, D., & Vanmierlo, T. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71774

A conserved serotonin receptor pathway is a druggable modifier of Tau pathology, neural circuit formation and neurodegenerationPreprint

Tsap, M. I., Navrotskaya, V., Labus, J., Ponimaskin, E. G., Yatsenko, A. S., & Shcherbata, H. R. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.24.746720

Steered molecular dynamics and free-energy analysis of withanolide unbinding from tau kinases TTBK1 and GSK-3β

Kavitha, J., S., S. K., George, M., Francis, D., & Abi, T. G. (2026) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2026.2736169

APH-1A and CDK5 Expression Correlates with Tau Hyperphosphorylation and Its Attenuation by Brahmi and Donep-M in STZ induced Alzheimer’s Disease ModelPreprint

Hathi, U. P. S., Kumar, A., Jyotsna, A., & Kateriya, S. (2026) · Research Square · doi:10.21203/rs.3.rs-11257702/v1

F1‐01‐06: Soluble hyper‐phosphorylated tau causes microtubule breakdown and poisons normal tau in vivo

Mudher, A. K. (2010) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2010.05.175

O3‐05‐04: Soluble hyper‐phosphorylated tau disrupts the microtubule‐binding function of normal tau in vivo

Cowan, C. M., & Mudher, A. K. (2009) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2009.05.460 · Cited by 1

Disruption of neuronal function by soluble hyperphosphorylated tau in a Drosophila model of tauopathy

Cowan, C. M., Chee, F. C., Shepherd, D., & Mudher, A. K. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380564 · Cited by 42

Drosophila models of human tauopathies indicate that Tau protein toxicity in vivo is mediated by soluble cytosolic phosphorylated forms of the protein

Feuillette, S., Miguel, L., Frébourg, T., Campion, D., & Lecourtois, M. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06663.x · Cited by 81

Important neuronal toxicity of microtubule-bound Tau in vivo in Drosophila

Talmat-Amar, Y., Arribat, Y., Redt‐Clouet, C., Feuillette, S., Bougé, A.-L., Lecourtois, M., & Parmentier, M. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr290 · Cited by 48