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Tau-Targeted Therapeutic Strategies: Mechanistic Targets, Clinical Pipelines, and Analysis of Failures

Shen, X., Li, H., Zhang, B., Li, Y., & Zhu, Z. (2025) · Cells · doi:10.3390/cells14191506 · Cited by 32 · see citing works

The misfolding mechanism of the key fragment R3 of tau protein: a combined molecular dynamics simulation and Markov state model study.

Liu, H.-L., Zhong, H., Xu, Z.-R., Zhang, Q., Shah, S. J. A., Liu, H.-X., & Yao, X.-J. (2020) · Physical Chemistry, Chemical Physics - PCCP · doi:10.1039/c9cp06954b · Cited by 17 · see citing works

Sleep Disruption Precedes Forebrain Synaptic Tau Burden and Contributes to Cognitive Decline in a Sex-Dependent Manner in the P301S Tau Transgenic Mouse Model

Martin, S. C., Joyce, K. K., Lord, J. S., Harper, K. M., Nikolova, V. D., Cohen, T. J., Moy, S. S., & Diering, G. H. (2024) · eNeuro · doi:10.1523/eneuro.0004-24.2024 · Cited by 22 · see citing works

Comprehensive Insights into Pathophysiology of Alzheimer's Disease: Herbal Approaches for Mitigating Neurodegeneration

Sen, D., Rathee, S., Pandey, V., Jain, S., & Patil, U. K. (2024) · Current Alzheimer Research · doi:10.2174/0115672050309057240404075003 · Cited by 19 · see citing works

Microtubule Stabilization Enhances the Chondrogenesis of Synovial Mesenchymal Stem Cells

Li, J., Sun, Z., Lv, Z., Jiang, H., Liu, A., Wang, M., Tan, G., Guo, H., Sun, H., Wu, R., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.748804 · Cited by 18 · see citing works

Prion-Like Propagation Mechanisms in Tauopathies and Traumatic Brain Injury: Challenges and Prospects

Alyenbaawi, H., Allison, W. T., & Mok, S. (2020) · Biomolecules · doi:10.3390/biom10111487 · Cited by 18 · see citing works

Multiple pathways promote microtubule stabilization in senescent intestinal epithelial cells

Chu, S., Moujaber, O., Lemay, S., & Stochaj, U. (2022) · npj Aging · doi:10.1038/s41514-022-00097-8 · Cited by 16 · see citing works

Beyond uniformity: Exploring the heterogeneous and dynamic nature of the microtubule lattice

Motta, M. R., Biswas, S., & Schaedel, L. (2023) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2023.151370 · Cited by 16 · see citing works

Microtubule-modulating Agents in the Fight Against Neurodegeneration: Will it ever Work?

Soliman, A., Bakota, L., & Brandt, R. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666211201101020 · Cited by 17 · see citing works

The RNA-binding protein EIF4A3 promotes axon development by direct control of the cytoskeleton

Alsina, F. C., Lupan, B. M., Lin, L. J., Musso, C. M., Mosti, F., Newman, C. R., Wood, L. M., Suzuki, A., Agostino, M., Moore, J. K., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114666 · Cited by 15 · see citing works

Dynamin 1 is important for microtubule organization and stabilization in glomerular podocytes

La, T. M., Tachibana, H., Li, S., Abe, T., Seiriki, S., Nagaoka, H., Takashima, E., Takeda, T., Ogawa, D., Makino, S., et al. (2020) · The FASEB Journal · doi:10.1096/fj.202001240rr · Cited by 15 · see citing works

Hibernation Impairs Odor Discrimination – Implications for Alzheimer’s Disease

Bullmann, T., Feneberg, E., Kretzschmann, T. P., Ogunlade, V., Holzer, M., & Arendt, T. (2019) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2019.00069 · Cited by 13 · see citing works

P301L tau mutation leads to alterations of cell cycle, DNA damage response and apoptosis: Evidence for a role of tau in cancer

Cimini, S., Giaccone, G., Tagliavini, F., Costantino, M., Perego, P., & Rossi, G. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115043 · Cited by 12 · see citing works

Microtubule assembly and disassembly dynamics model: Exploring dynamic instability and identifying features of Microtubules’ Growth, Catastrophe, Shortening, and Rescue

Kliuchnikov, E., Klyshko, E., Kelly, M. S., Zhmurov, A. A., Dima, R. I., Marx, K. A., & Barsegov, V. A. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.01.028 · Cited by 12 · see citing works

Microtubule-modulating Agents in the Fight Against Neurodegeneration: Will it ever Work?

Soliman, A., Bakota, L., & Brandt, R. (2022) · UCL Discovery (University College London) · Cited by 12 · see citing works

Are Hippocampal Hypoperfusion and ATP Depletion Prime Movers in the Genesis of Alzheimer’s Disease? A Review of Recent Pertinent Observations from Molecular Biology

Walker, V. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157328 · Cited by 11 · see citing works

Hydrolysis-deficient mosaic microtubules as faithful mimics of the GTP cap

Estévez-Gallego, J., Blum, T. B., Ruhnow, F., Gili, M., Speroni, S., García-Castellanos, R., Steinmetz, M. O., & Surrey, T. (2025) · Nature Communications · doi:10.1038/s41467-025-57555-6 · Cited by 17 · see citing works

Tau accelerates tubulin exchange in the microtubule lattice

Biswas, S., Grover, R., Reuther, C., Poojari, C., Shaebani, M. R., Nandakumar, S., Grünewald, M., Zablotsky, A., Hub, J. S., Diez, S., et al. (2025) · Nature Physics · doi:10.1038/s41567-025-03003-7 · Cited by 9 · see citing works

A Network of 17 Microtubule-Related Genes Highlights Functional Deregulations in Breast Cancer

Rodrigues-Ferreira, S., MORIN, M., Guichaoua, G., Moindjie, H., Haykal, M. M., Collier, O., Stoven, V., & Nahmias, C. (2023) · Cancers · doi:10.3390/cancers15194870 · Cited by 9 · see citing works

Positron Emission Tomography Molecular Imaging of the Major Neurodegenerative Disorders: Overview and Pictorial Essay, from a Nuclear Medicine Center's Perspective

Calabria, F. F., Leporace, M., Cimini, A., Ricci, M., Travascio, L., & Bagnato, A. (2023) · Journal of Integrative Neuroscience · doi:10.31083/j.jin2206172 · Cited by 8 · see citing works

The structure of a Tau fragment bound to tubulin prompts new hypotheses on Tau mechanism and oligomerization

Khodja, L. A., Campanacci, V., Lippens, G. M., & Gigant, B. (2024) · PNAS Nexus · doi:10.1093/pnasnexus/pgae487 · Cited by 7 · see citing works

Molecular dynamics simulations reveal the disruption mechanism of a 2,4‐thiazolidinedione derivative C30 against tau hexapeptide ( PHF6 ) oligomer

Liu, H., Zhong, H., Liu, H., & Yao, X. (2021) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26196 · Cited by 7 · see citing works

Studying Tau-Microtubule Interaction Using Single-Molecule TIRF Microscopy

Stoppin‐Mellet, V., Bagdadi, N., Saoudi, Y., & Arnal, I. (2019) · Methods in molecular biology · doi:10.1007/978-1-0716-0219-5_6 · Cited by 6 · see citing works

Microtubules composed of α4A undergo curved growth mainly mediated by its core structure

Diao, L., Liu, M., Liu, Y., Zhang, X., & Bao, L. (2023) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjad004 · Cited by 6 · see citing works

Advances in Understanding the Molecular Mechanisms of Neuronal Polarity

Gu, X., Jia, C., & Wang, J. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03242-w · Cited by 6 · see citing works

The role of intrinsic disorder in binding of plant microtubule‐associated proteins to the cytoskeleton

Gonzalez, J. P., Frandsen, K. E. H., & Kesten, C. (2023) · Cytoskeleton · doi:10.1002/cm.21773 · Cited by 6 · see citing works

The ataxia-telangiectasia disease protein ATM controls vesicular protein secretion via CHGA and microtubule dynamics via CRMP5

Reichlmeir, M., Duecker, R. P., Röhrich, H., Key, J., Schubert, R., Abell, K., Possemato, A. P., Stokes, M. P., & Auburger, G. W. J. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106756 · Cited by 5 · see citing works

Evaluation of the Potential Phosphorylation Effect on Isocitrate Dehydrogenases from Saccharomyces cerevisiae and Yarrowia lipolytica

Wang, P., Liu, T., Zhou, X., & Zhu, G. (2019) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-019-02974-7 · Cited by 5 · see citing works

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 4 · see citing works

Tau and Alzheimer’s Disease: Molecular Mechanisms and Treatment Approaches

Reiss, A. B., Muhieddine, D., Leon, A. Z. D., Voloshyna, I., Gomolin, I. H., & Pinkhasov, A. (2021) · SN Comprehensive Clinical Medicine · doi:10.1007/s42399-021-01092-y · Cited by 4 · see citing works

Dual Modification of Tau by Pseudophosphorylation and Glycation Does Not Enhance Amorphous Aggregation

Chinnathambi, S. (2024) · Cellular Physiology and Biochemistry · doi:10.33594/000000693 · Cited by 3 · see citing works

Controlled Tau Cleavage in Cells Reveals Abnormal Localizations of Tau Fragments

Fourest‐Lieuvin, A., Vinit, A., Blot, B., Perrot, A., Denarier, É., Saudou, F., & Arnal, I. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.08.016 · Cited by 3 · see citing works

Loss of Eml1 alters microtubule-associated protein networks in mouse brain heterotopia

Yiğit, B. N., Tufekci, D., Viola, V., Kirim, B. A., Zaidi, D., Francis, F., & Özlü, N. (2025) · Communications Biology · doi:10.1038/s42003-025-08394-0 · Cited by 3 · see citing works

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 · see citing works

Human spastin functions as an ATPase-independent microtubule nucleator via ring-stack formationPreprint

Liu, H., Matsumoto, N., Kaneshiro, T., Kato, T., Shigematsu, H., Kikkawa, S., Nitta, E., Imasaki, T., & Nitta, R. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.28.691112 · Cited by 2 · see citing works

Phospho-Tau Signature During Mitosis: AT8, p-T217 and p-S422 as Key Phospho-Epitopes

Goussard, M., Zarka, K., Denus, M., Curel, T., Claeysen, S., Lefebvre, B., Hamdane, M., Marin, P., Villeneuve, J., & Parmentier, M. (2025) · Cells · doi:10.3390/cells14201638 · Cited by 1 · see citing works

Eriocitrin and its derivatives against Alzheimer's disease: Cumulative accounts of in vitro and in vivo studies.

Kritika, Sanjay, & Lee, H. (2025) · Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · doi:10.1016/j.biopha.2025.118362 · Cited by 1 · see citing works

Munc 18–1 is a multifaceted therapeutic target for dementia

Singh, K. S., Rani, P., Arora, A., Verma, R., Gupta, A., & Singh, L. R. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102899 · Cited by 1 · see citing works

G-protein coupled receptor regulates cytoskeletal remodelling of extracellular Tau in Alzheimer’s disease

Chinnathambi, S., Rangappa, N., Velmurugan, G., & Chandrashekar, M. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.018 · Cited by 1 · see citing works

A coherent structural picture of the interaction of Tau with tubulin provides a link to its aggregation

Gigant, B., Khodja, L. A., Campanacci, V., & Lippens, G. M. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113086 · Cited by 1 · see citing works

The critical role of microglia in the stress response

Chen, K., Xuan, Z.-Y., Sun, B.-Y., Zhong, G.-N., Sun, X.-L., & Yan, J. (2026) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2026.106894 · Cited by 1 · see citing works

A molecular mechanism for salt stress-induced microtubule array formation in ArabidopsisPreprint

Kesten, C., Wallmann, A., Schneider, R., McFarlane, H. E., Diehl, A., Khan, G. A., van Rossum, B., Lampugnani, E. R., Cremer, N., Schmieder, P., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/431031 · Cited by 1 · see citing works

Tau-seed interactome analysis reveals distinct functional signatures in Alzheimer’s disease across model systemsPreprint

Martínez, P., Patel, H., You, Y., Lopes, D., Amaro, A., Jury, N., Min, Y., Redding‐Ochoa, J., Dutta, S., Rochet, J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.17.660179 · Cited by 2 · see citing works

The Role of DNA Damage-induced Cellular Senescence in the Pathophysiology of mTBI

Schwab, N. (2019) · TSpace (University of Toronto)

The N-terminal domain of COMPANION OF CELLULOSE SYNTHASE1 promotes microtubule array formation in Arabidopsis

Gurumoorthy, V., Hicks, A., Krishnan, S. T., Leite, W. C., Chodankar, S., Kolape, J., Smith, J. C., Lamichhane, R., & O’Neill, H. (2025) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiaf392

Chr:17q21.31 locus risk haplotype H1 susceptibility to ferroptosis is mediated by endolysosomal pathway

Sadikoglou, E., Domingo‐Fernándéz, D., Savytska, N., Fernandes, N., Rizzu, P., Illarionova, A., Strauß, T., Schwarz, S. C., Kodamullil, A. T., Höglinger, G. U., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08147-1 · Cited by 1 · see citing works

Biosimilars: Antibody and nanobody-based therapeutic approaches towards protein misfolding diseases

Chinnathambi, S., & Rangappa, N. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.014

SSNA1 mechanically reinforces the damaged microtubule latticePreprint

Richardson, L. B., Lawrence, E. J., Pinjakan, A., & Žanić, M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.16.699973

Reconstitution du réseau corticostriatal et cible thérapeutique dans la maladie de Huntington

Virlogeux, A. (2018) · doi:10.70675/92b9e042zfafcz42e8z890bz6c7ca43e2613

Exploration de nouveaux biomarqueurs plasmatiques pour le diagnostic de la maladie d’Alzheimer

Rossi, E. (2021) · doi:10.70675/71230be4z1955z4fafzb1b8z8ff71a4edaff

Mécanismes de stabilisation des microtubules : rôle du nucléotide lié à la tubuline et action des protéines associées aux microtubules

Bagdadi, N. (2021) · doi:10.70675/f5dafa48z046bz4f81z92e6zb415fb85d4f3

Caractérisation d'un nouveau mode de fixation de la protéine Tau aux microtubules

Khodja, L. A. (2022) · theses.fr (ABES) · doi:10.70675/d8b90a94z5fbdz4ca2za1edz18751d5575da

Myotoxin 3, a peptide from Crotalus oreganus rattlesnake venom as a microtubule targeting agent

García, M. C. G. (2022) · doi:10.70675/2f63b6fdz5c24z4369za50dz5b62780ae1e2

Targeting the cell cycle : A novel therapeutic strategy against ATIP3- deficient breast cancer

Haykal, M. M. (2023) · theses.fr (ABES) · doi:10.70675/03dee32bz395cz469ez9a0dzf4c5f2e84330

The Role of Tubulin Polyglutamylation in Controlling the Binding and Activity of Microtubule-Interacting Proteins

Genova, M. (2023) · theses.fr (ABES) · doi:10.70675/8bd8ddfeza950z4855z9c43zce2ac854ecf3

A framework for the organization of microtubules in developing neuronsPreprint

Nicolaou, K., Mulder, B. M., Kapitein, L. C., & Berger, F. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.15.732274

Microglial interactions of Tau in Alzheimer’s disease: Mechanisms of aggregation, propagation, and neurodegeneration

Muruagn, G. V., & Chinnathambi, S. (2026) · Advances in pharmacology · doi:10.1016/bs.apha.2026.06.002

Stress and dementia

Bhattacharya, H., Chakraborty, P., & Dewanjee, S. (2026) · International review of neurobiology · doi:10.1016/bs.irn.2026.08.022

Axonal Branch Points of Parvalbumin Interneurons are Focal Sites of Tau-Induced DegenerationPreprint

Feyen, P., Zhang, Y., Niedermeier, T., Landgraf, N. F., Bareyre, F. M., Vos, C., Paeger, L., & Herms, J. W. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.17.751394

Impact of tau and its pathological forms on microtubule network organization

Prezel, E. (2017) · theses.fr (ABES)

Structural Evolution of Energy-Consuming Tau Mediated Microtubule Bundles

Kohl, P. A., Fletcher, B. J., Song, C., Chung, P. J., Miller, H. P., Wilson, L., Feinstein, S. C., & Safinya, C. R. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2019.11.3242

Impact de tau et ses formes pathologiques sur l'organisation des réseaux microtubulaires

Prezel, E. (2017) · doi:10.70675/987befa8zdd9fz45ddzb329z3f59cbbbe887

Tau Organizes Distinct Lattice Confirmation-dependent Microtubule Networks Under Mechanical LoadPreprint

Hewes, K., Mitkoff, J., Dionisio, B., Henglein, A., & Forth, S. T. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.7004466

Tau protein induces bundling of microtubules in vitro: Comparison of different tau isoforms and a tau protein fragment

Scott, C. W., Klika, A. B., Lo, M. M. S., Norris, T. E., & Caputo, C. B. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490330104 · Cited by 65 · see citing works