Tau Structures

Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359

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

A protein factor essential for microtubule assembly

Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089

A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation

Patel, A., Lee, H. O., Jawerth, L. M., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 2,927

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

Tau in physiology and pathology

Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251

Paclitaxel (Taxol)

Rowinsky, E. K., & Donehower, R. C. (1995) · New England Journal of Medicine · doi:10.1056/nejm199504133321507 · Cited by 1,924

Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models

Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821

Transmission and spreading of tauopathy in transgenic mouse brain

Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803

Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.

Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780

Roles of tau protein in health and disease

Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003

Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease

Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994

MAPT mutations, tauopathy, and mechanisms of neurodegeneration

Strang, K. H., Golde, T. E., & Giasson, B. I. (2019) · Laboratory Investigation · doi:10.1038/s41374-019-0197-x · Cited by 424

Liquid-liquid phase separation induces pathogenic tau conformations in vitro

Kanaan, N. M., Hamel, C., Grabinski, T., & Combs, B. (2020) · Nature Communications · doi:10.1038/s41467-020-16580-3 · Cited by 397

Visualization of neurofibrillary tangle maturity in Alzheimer's disease: A clinicopathologic perspective for biomarker research

Moloney, C. M., Lowe, V. J., & Murray, M. E. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12321 · Cited by 358

Mechanisms of secretion and spreading of pathological tau protein

Brunello, C. A., Merezhko, M., Uronen, R.-L., & Huttunen, H. J. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03349-1 · Cited by 304

Mitochondrial dysfunction in Alzheimer’s disease

D’Alessandro, M. C. B., Kanaan, S., Geller, M., Praticò, D., & Daher, J. P. L. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102713 · Cited by 240

Oxidative Stress Occurs Prior to Amyloid Aβ Plaque Formation and Tau Phosphorylation in Alzheimer’s Disease: Role of Glutathione and Metal Ions

Roy, R. G., Mandal, P. K., & Maroon, J. C. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00486 · Cited by 194

Tau Proteolysis in the Pathogenesis of Tauopathies: Neurotoxic Fragments and Novel Biomarkers

Quinn, J. P., Corbett, N. J., Kellett, K. A. B., & Hooper, N. M. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-170959 · Cited by 170

Contribution of Tau Pathology to Mitochondrial Impairment in Neurodegeneration

Maria Jose Perez, J., Jara, C., & Quintanilla, R. A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00441 · Cited by 157

The role of amyloid oligomers in neurodegenerative pathologies

Wells, C., Brennan, S. E., Keon, M., & Ooi, L. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.03.113 · Cited by 131

The Role of Microglia in the Spread of Tau: Relevance for Tauopathies

Perea, J. R., Llorens-Martín, M., Ávila, J., & Bolós, M. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00172 · Cited by 129

Extracellular Monomeric Tau Is Internalized by Astrocytes

Perea, J. R., López, E., Díez-Ballesteros, J. C., Ávila, J., Hernández, F., & Bolós, M. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00442 · Cited by 114

Role of the Extracellular Matrix in Alzheimer’s Disease

Sun, Y., Xu, S., Jiang, M., Liu, X., Yang, L., Bai, Z., & Yang, Q. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.707466 · Cited by 119

The Role of Protein Misfolding and Tau Oligomers (TauOs) in Alzheimer′s Disease (AD)

Mroczko, B., Groblewska, M., & Litman‐Zawadzka, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194661 · Cited by 111

Baicalein inhibits heparin-induced Tau aggregation by initializing non-toxic Tau oligomer formation

Sonawane, S. K., Uversky, V. N., & Chinnathambi, S. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00704-3 · Cited by 95

Ten Years of Tau-Targeted Immunotherapy: The Path Walked and the Roads Ahead

Novak, P., Kontsekova, E., Zilka, N., & Novak, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00798 · Cited by 87

Genetic ablation of tau improves mitochondrial function and cognitive abilities in the hippocampus

Jara, C., Aránguiz, A., Cerpa, W. F., Tapia‐Rojas, C., & Quintanilla, R. A. (2018) · Redox Biology · doi:10.1016/j.redox.2018.07.010 · Cited by 85

Overview of tau PET molecular imaging

Petersen, G. C., Roytman, M., Chiang, G. C.-Y., Li, Y., Gordon, M. L., & Franceschi, A. M. (2022) · Current Opinion in Neurology · doi:10.1097/wco.0000000000001035 · Cited by 87

Regulation of neuronal microtubule dynamics by tau: Implications for tauopathies

Venkatramani, A., & Panda, D. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.04.120 · Cited by 84

Astrocyte senescence and SASP in neurodegeneration: tau joins the loop

Ungerleider, K., Beck, J. A., Lissa, D., Turnquist, C., Horikawa, I., Harris, B. T., & Harris, C. C. (2021) · Cell Cycle · doi:10.1080/15384101.2021.1909260 · Cited by 72

The Positive Side of the Alzheimer’s Disease Amyloid Cross-Interactions: The Case of the Aβ 1-42 Peptide with Tau, TTR, CysC, and ApoA1

Ciccone, L., Shi, C., di Lorenzo, D., Van Baelen, A.-C., & Tonali, N. (2020) · Molecules · doi:10.3390/molecules25102439 · Cited by 69

Prion and Prion-Like Protein Strains: Deciphering the Molecular Basis of Heterogeneity in Neurodegeneration

Scialò, C., Cecco, E. D., Manganotti, P., & Legname, G. (2019) · Viruses · doi:10.3390/v11030261 · Cited by 69

Impact of Tau on Neurovascular Pathology in Alzheimer's Disease

Canepa, E., & Fossati, S. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.573324 · Cited by 67

Novel Functions of the Neurodegenerative-Related Gene Tau in Cancer

Gargini, R., Segura‐Collar, B., & Sánchez‐Gómez, P. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00231 · Cited by 60

Biosensor approaches on the diagnosis of neurodegenerative diseases: Sensing the past to the future

Karaboğa, M. N. S., & Sezgintürk, M. K. (2021) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2021.114479 · Cited by 59

Screening of tau protein kinase inhibitors in a tauopathy-relevant cell-based model of tau hyperphosphorylation and oligomerization

Yadikar, H., Torres, I., Aiello, G., Kurup, M., Yang, Z., Lin, F. Y., Kobeissy, F. H., Yost, R. A., & Wang, K. (2020) · PLoS ONE · doi:10.1371/journal.pone.0224952 · Cited by 58

Glycogen Synthase Kinase 3β Involvement in Neuroinflammation and Neurodegenerative Diseases

Gianferrara, T., Cescon, E., Grieco, I., Spalluto, G., & Federico, S. (2022) · Current Medicinal Chemistry · doi:10.2174/0929867329666220216113517 · Cited by 58

The journey of boswellic acids from synthesis to pharmacological activities

Ragab, E. A., Abdelwahab, M. F., Doghish, A. S., Salama, R. M., Eissa, N., & Darwish, S. F. (2023) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-023-02725-w · Cited by 56

Dephosphorylated rather than hyperphosphorylated Tau triggers a pro-inflammatory profile in microglia through the p38 MAPK pathway

Perea, J. R., Ávila, J., & Bolós, M. (2018) · Experimental Neurology · doi:10.1016/j.expneurol.2018.08.007 · Cited by 54

Mechanistic role of boswellic acids in Alzheimer’s disease: Emphasis on anti-inflammatory properties

Siddiqui, A., Shah, Z., Jahan, R. N., Othman, I., & Kumari, Y. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112250 · Cited by 54

Tau Aggregation

Hernández, F., Ferrer, I., Pérez, M., Zabala, J. C., del Rı́o, J. A., & Ávila, J. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.04.024 · Cited by 49

Tau forms synaptic nano-biomolecular condensates controlling the dynamic clustering of recycling synaptic vesicles

Longfield, S. F., Mollazade, M., Wallis, T. P., Gormal, R. S., Joensuu, M., Wark, J. R., Waardenberg, A. J., Small, C., Graham, M. E., Meunier, F. A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43130-4 · Cited by 47

Cytoskeletal Proteins and Alzheimer’s Disease Pathogenesis: Focusing on the Interplay with Tau Pathology

Jiang, G., Xie, G., Li, X., & Xiong, J. (2025) · Biomolecules · doi:10.3390/biom15060831 · Cited by 48

Real-Time Quaking- Induced Conversion Assays for Prion Diseases, Synucleinopathies, and Tauopathies

Vascellari, S., Orru, C. D., & Caughey, B. W. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.853050 · Cited by 43

Passive immunotherapy for N-truncated tau ameliorates the cognitive deficits in two mouse Alzheimer’s disease models

Corsetti, V., Borreca, A., Latina, V., Giacovazzo, G., Pignataro, A., Krashia, P., Natale, F., Cocco, S., Rinaudo, M., Malerba, F., et al. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa039 · Cited by 42

14-3-3/Tau Interaction and Tau Amyloidogenesis

Chen, Y., Chen, X., Yao, Z., Shi, Y., Xiong, J., Zhou, J., Su, Z., & Huang, Y. (2019) · Journal of Molecular Neuroscience · doi:10.1007/s12031-019-01325-9 · Cited by 47

Phosphorylated tau targeted small-molecule PROTACs for the treatment of Alzheimer's disease and tauopathies

Pradeepkiran, J. A., & Reddy, P. H. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2021.166162 · Cited by 41

Role of Microglia in Regulating Cholesterol and Tau Pathology in Alzheimer’s Disease

Nanjundaiah, S., Chidambaram, H., Chandrashekar, M., & Chinnathambi, S. (2021) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00883-6 · Cited by 36

Noradrenergic neuromodulation in ageing and disease

Krohn, F., Lancini, E., Ludwig, M., Leiman, M., Guruprasath, G., Haag, L., Panczyszyn, J., Düzel, E., Hämmerer, D., & Betts, M. J. (2023) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2023.105311 · Cited by 41

Alterations in Tau Metabolism in ALS and ALS-FTSD

Strong, M. J., Donison, N. S., & Volkening, K. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.598907 · Cited by 37

Curcumin as Scaffold for Drug Discovery against Neurodegenerative Diseases

Cascio, F. L., Marzullo, P., Kayed, R., & Piccionello, A. P. (2021) · Biomedicines · doi:10.3390/biomedicines9020173 · Cited by 41

Aggregation, Transmission, and Toxicity of the Microtubule-Associated Protein Tau: A Complex Comprehension

Hu, J., Sha, W., Yuan, S., Wu, J., & Huang, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241915023 · Cited by 40

Electrostatics of Tau Protein by Molecular Dynamics

Castro, T. G., Munteanu, F., & Cavaco-Paulo, A. M. (2019) · Biomolecules · doi:10.3390/biom9030116 · Cited by 32

Differential binding affinity of tau repeat region R2 with neuronal-specific β-tubulin isotypes

Bhandare, V. V., Kumbhar, B. V., & Kunwar, A. (2019) · Scientific Reports · doi:10.1038/s41598-019-47249-7 · Cited by 30

Bioenergetic failure and oxidative stress: mitochondrial contributions to Alzheimer’s disease

Wasim, R. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01916-6 · Cited by 31

Harmonization of pipeline for preclinical multicenter plasma protein and miRNA biomarker discovery in a rat model of post-traumatic epileptogenesis

Kamnaksh, A., Puhakka, N., Ali, I. Y., Smith, G. S., Aniceto, R., McCullough, J., Gupta, S. D., Ndode‐Ekane, X. E., Brady, R. D., Casillas-Espinosa, P. M., et al. (2018) · Epilepsy Research · doi:10.1016/j.eplepsyres.2018.11.009 · Cited by 29

Activating autophagy to eliminate toxic protein aggregates with small molecules in neurodegenerative diseases

Fu, Y., Zhang, J., Qin, R., Ren, Y., Zhou, T., Han, B., & Liu, B. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100053 · Cited by 29

Macromolecular Structures and Proteins Interacting with the Microtubule Associated Tau Protein

Jiménez, J. S. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.05.023 · Cited by 28

GSKIP-Mediated Anchoring Increases Phosphorylation of Tau by PKA but Not by GSK3beta via cAMP/PKA/GSKIP/GSK3/Tau Axis Signaling in Cerebrospinal Fluid and iPS Cells in Alzheimer Disease

Ko, H.-J., Chiou, S.-J., Wong, Y., Wang, Y.-H., Lai, Y.-L., Chou, C., Wang, C., Loh, J., Lieu, A., Cheng, J., et al. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8101751 · Cited by 26

The Structure Biology of Tau and Clue for Aggregation Inhibitor Design

Wang, D., Huang, X., Yan, L., Zhou, L., Chang, Y., Wu, J., Su, Z., & Huang, Y. (2021) · The Protein Journal · doi:10.1007/s10930-021-10017-6 · Cited by 27

Tau/DDX6 interaction increases microRNA activity

Chauderlier, A., Gilles, M., Špolcová, A., Caillierez, R., Chwastyniak, M., Kress, M., Drobecq, H., Bonnefoy, E., Pinet, F., Barbieri-Weill, D., et al. (2018) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2018.06.006 · Cited by 26

Cyclic dipeptide‐based small molecules modulate zinc‐mediated liquid–liquid phase separation of tau

Ramesh, M., Balachandra, C., Baruah, P., & Govindaraju, T. (2022) · Journal of Peptide Science · doi:10.1002/psc.3465 · Cited by 25

Tau Protein as Therapeutic Target for Cancer? Focus on Glioblastoma

Hedna, R., Kovacic, H., Pagano, A., Peyrot, V., Robin, M., Devred, F., & Breuzard, G. (2022) · Cancers · doi:10.3390/cancers14215386 · Cited by 25

In Situ Raman Study of Neurodegenerated Human Neuroblastoma Cells Exposed to Outer-Membrane Vesicles Isolated from Porphyromonas gingivalis

Pezzotti, G., Adachi, T., Imamura, H., Redolfi‐Bristol, D., Adachi, K., Yamamoto, T., Kanamura, N., Marin, E., Zhu, W., Kawai, T., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713351 · Cited by 23

Protein aggregation and neurodegenerative disease: Structural outlook for the novel therapeutics

Arar, S. H., Haque, M. A., & Kayed, R. (2023) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26561 · Cited by 20

Targeted protein modification as a paradigm shift in drug discovery

Amirian, R., Azadi Badrbani, M., Izadi, Z., Samadian, H., Bahrami, G., Sarvari, S., Abdolmaleki, S., Nabavi, S. M., Derakhshankhah, H., & Jaymand, M. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115765 · Cited by 18

Inflammasome links traumatic brain injury, chronic traumatic encephalopathy, and Alzheimer’s disease

Seplovich, G., Bouchi, Y., Vaccari, J. P. D. R., Pareja, J. C. M., Reisner, A., Blackwell, L. S., Mechref, Y. S., Wang, K., Tyndall, J. A., Tharakan, B., et al. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-00107 · Cited by 21

Pilot Study for Deciphering Post-Translational Modifications and Proteoforms of Tau Protein by Capillary Electrophoresis-Mass Spectrometry

Fang, F., Xu, T., Hagar, H. C., Hovde, S., Kuo, M., & Sun, L. (2024) · Journal of Proteome Research · doi:10.1021/acs.jproteome.4c00587 · Cited by 18

Pathogenic Tau Protein Species: Promising Therapeutic Targets for Ocular Neurodegenerative Diseases

Mishan, M. A., Kanavi, M. R., Shahpasand, K., & Ahmadieh, H. (2019) · Journal of Ophthalmic and Vision Research · doi:10.18502/jovr.v14i4.5459 · Cited by 18

Tau protein structure and dynamics

Chinnathambi, S., Velmurugan, G., & Chandrashekar, M. (2024) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2024.09.002 · Cited by 18

Phosphorylation and Dephosphorylation of Tau Protein by the Catalytic Subunit of PKA, as Probed by Electrophoretic Mobility Retard

Benítez, M. J., Cuadros, R., & Jiménez, J. S. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-201077 · Cited by 19

Ethnobotanical significance of medicinal plants: Beta‐amyloid and tau aggregation inhibitors against Alzheimer's disease

Anand Ganapathy, A., Haripriya, V. M., Acharya, N. S., Somappa, S. B., & Kumaran, A. (2023) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23339 · Cited by 17

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 20

A theoretical study of polymorphism in VQIVYK fibrils

Yang, J., Agnihotri, M. V., Huseby, C. J., Kuret, J., & Singer, S. J. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.01.032 · Cited by 17

Production of Monoclonal Antibodies to Pathologic β-sheet Oligomeric Conformers in Neurodegenerative Diseases

Goñi, F., Martá-Ariza, M., Peyser, D. K., Herline, K., & Wısnıewskı, T. (2017) · Scientific Reports · doi:10.1038/s41598-017-10393-z · Cited by 16

Imaging Amyloid and Tau in the Retina: Current Research and Future Directions

Tang, M. Y., Blazes, M. S., & Lee, C. S. (2023) · Journal of Neuro-Ophthalmology · doi:10.1097/wno.0000000000001786 · Cited by 17

Reversible protein assemblies in the proteostasis network in health and disease

Kohler, V., & Andréasson, C. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1155521 · Cited by 17

Untangling Tau: Molecular Insights into Neuroinflammation, Pathophysiology, and Emerging Immunotherapies

Davidson, R., Krider, R. I., Borsellino, P., Noorda, K., Alhwayek, G., & Vida, T. A. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45110553 · Cited by 17

Realization of Amyloid-like Aggregation as a Common Cause for Pathogenesis in Diseases

Naskar, S., & Gour, N. (2023) · Life · doi:10.3390/life13071523 · Cited by 13

Boswellic Acids as Promising Leads in Drug Development against Alzheimer’s Disease

Haghaei, H., Soltani, S., Hosseini, S. R. A., Rashidi, M., & Karima, S. (2020) · Pharmaceutical Sciences · doi:10.34172/ps.2020.25 · Cited by 16

Molecular mechanism of amyloidogenicity and neurotoxicity of a pro-aggregated tau mutant in the presence of histidine tautomerism via replica-exchange simulation

Chatterjee, S., Salimi, A., & Lee, J. Y. (2021) · Physical Chemistry Chemical Physics · doi:10.1039/d1cp00105a · Cited by 15

Hiding in plain sight: Complex interaction patterns between Tau and 14-3-3ζ protein variants

Crha, R., Kozeleková, A., Hofrová, A., Iľkovičová, L., Gašparik, N., Kadeřávek, P., & Hritz, J. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.130802 · Cited by 15

4R Tau Modulates Cocaine-Associated Memory through Adult Dorsal Hippocampal Neurogenesis

Li, H.-C., Xu, W., Wang, D., Wang, L., Fang, Q., Wan, X., Zhang, J., Hu, Y.-M., Li, H.-F., Zhang, J., et al. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.2848-20.2021 · Cited by 11

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

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

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

Protein tau phosphorylation in the proline rich region and its implication in the progression of Alzheimer's disease

Merino‐Serrais, P., Soria, J. M., Arrabal, C. A., Ortigado-López, A., Esparza, M. Á. G., Muñoz, A., Hernández, F., Ávila, J., DeFelipe, J., & León‐Espinosa, G. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.115049 · Cited by 10

Targeting tau in Alzheimer’s Disease: rationale, approach and challenges

Aslanyan, A., Foiani, M. S., Giovannucci, T. A., McDade, E., Duff, K., Mummery, C. J., Schöll, M., Wildsmith, K. R., & Paterson, R. W. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00925-5 · Cited by 10

Unveiling the Metal-Dependent Aggregation Properties of the C-terminal Region of Amyloidogenic Intrinsically Disordered Protein Isoforms DPF3b and DPF3a

Leyder, T., Mignon, J., Mottet, D., & Michaux, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315291 · Cited by 9

Roles of Nucleic Acids in Protein Folding, Aggregation, and Disease

Litberg, T. J., & Horowitz, S. A. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.3c00695 · Cited by 10

Cell redistribution of G quadruplex‐structured DNA is associated with morphological changes of nuclei and nucleoli in neurons during tau pathology progression

Comptdaer, T., Tardivel, M., Schirmer, C., Buée, L., & Galas, M. (2024) · Brain Pathology · doi:10.1111/bpa.13262 · Cited by 8

Tau post-translational modifications in Alzheimer's disease: Insights into pathogenesis, therapeutic strategies, and diagnostic advances

Lei, H., Chen, X., Ruan, L., Liu, X., Ye, F., Li, K., Cheng, W., Yu, B., Di, C., & Di, C. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102927 · Cited by 7

Unravelling the Proteinopathic Engagement of α-Synuclein, Tau, and Amyloid Beta in Parkinson’s Disease: Mitochondrial Collapse as a Pivotal Driver of Neurodegeneration

Sahoo, T. A., Chand, J., Kandy, A. T., Shanish Antony, A., & Subramanian, G. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04399-7 · Cited by 9

Tau and tauopathies across primate species: implications for modeling neurodegenerative disorders

Colwell, J. C., & Emborg, M. E. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1598245 · Cited by 10

The sulfation pattern of glycosaminoglycans in human brain development and neurological disorders such as Alzheimer’s disease

Hirano, K., Egawa, H., & Nishihara, S. (2025) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00842.2024 · Cited by 6

Glycogen synthase kinase-3: the master switch driving neurodegeneration in Alzheimer’s disease and Parkinson’s disease

Liu, Y., Zhang, J., Tang, L., Yang, J., Hao, L., Lou, F., & Su, J. (2025) · Archives of Toxicology · doi:10.1007/s00204-025-04174-1 · Cited by 8

Oral Microbiome–Derived Proteins in Brain Extracellular Vesicles Circulate and Tie to Specific Dysbiotic and Neuropathological Profiles in Age-Related Dementias

Mulet, M., Milán, J. A. S., Lorca, C., Fernández‐Rhodes, M., Planell, A. A., Castillo, M. C. B., Saiz-Aúz, L., Mateos‐Moreno, M., Hase, Y., Mira, A., et al. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.101464 · Cited by 6

Intrinsic Disorder and Other Malleable Arsenals of Evolved Protein Multifunctionality

Aftab, A., Sil, S., Nath, S., Basu, A., & Basu, S. (2024) · Journal of Molecular Evolution · doi:10.1007/s00239-024-10196-7 · Cited by 7

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

Effect of cellular polyanion mimetics on tau peptide aggregation

Ismail, T., & Kanapathipillai, M. (2018) · Journal of Peptide Science · doi:10.1002/psc.3125 · Cited by 6

Rational Modulation of Liquid–Liquid Phase Separation Offers Novel Ways to Combat Tauopathies

Zhang, X., Wang, L., Lin, N., Gao, M. Y., & Huang, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146709 · Cited by 7

Unraveling Alzheimer’s: Exploring the Gut Microbiota–Brain Axis as a New Frontier in Understanding

Rashid, S. M., Razak, R., Tantray, A. K., James, A. W., Showkat, N., Shehjar, F., Jan, F., Ahmad, S. B., Khan, A., & Shah, Z. A. (2024) · Journal of dementia and Alzheimer's disease · doi:10.3390/jdad1010003 · Cited by 5

Proteolysis of tau by granzyme A in tauopathies generates fragments that are aggregation prone

Quinn, J. P., Fisher, K., Corbett, N. J., Warwood, S., Knight, D., Kellett, K. A. B., & Hooper, N. M. (2024) · Biochemical Journal · doi:10.1042/bcj20240007 · Cited by 5

Multimer Detection System: A Universal Assay System for Differentiating Protein Oligomers from Monomers

Jamerlan, A., Shim, K. H., Sharma, N., & An, S. S. A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26031199 · Cited by 5

A Specific Diplotype H1j/H2 of the MAPT Gene Could Be Responsible for Parkinson’s Disease with Dementia

Smaili, I., Hajjaj, I., Razıne, R., Tibar, H., Salmi, A., Bouslam, N., Moussa, A., Regragui, W., & Bouhouche, A. (2020) · Case Reports in Genetics · doi:10.1155/2020/8813344 · Cited by 5

Serine-404 Phosphorylation and the R406W Modification in Tau Stabilize the cis-Proline Amide Bond, via Phosphoserine-Proline C–H/O and Proline-Aromatic C–H/π InteractionsPreprint

Ganguly, H. K., Elbaum, M. B., & Zondlo, N. J. (2023) · ChemRxiv · doi:10.26434/chemrxiv-2023-w152b · Cited by 5

Intra-axonal Nanomagnetic Forces Differentially Impact hTau40 Transport Dynamics in Primary Cortical and Hippocampal Neurons

Landis, M. K., & Kunze, A. (2025) · ACS Nano · doi:10.1021/acsnano.4c14767 · Cited by 4

Role of Tau Protein Hyperphosphorylation in Diabetic Retinal Neurodegeneration

Mu, J., Zhang, Z., Jiang, C., Geng, H., & Duan, J. (2025) · Journal of Ophthalmology · doi:10.1155/joph/3278794 · Cited by 5

Tauopathy

Chi, H., Sang, T., & Chang, H.-Y. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.73198 · Cited by 5

Tau in physiology and pathology

Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251

It’s all about tau

Tapia‐Rojas, C., Cabezas-Opazo, F., Deaton, C. A., Vergara, E. H., Johnson, G. V. W., & Quintanilla, R. A. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.005 · Cited by 207

Probing forces generated and architectures mediated by Tau on microtubules

Chung, P. J. (2016) · eScholarship (California Digital Library)

Tau Protein Function in Axonal Formation

Paglini, M. G., Peris, L., Mascotti, F., Quiroga, S., & Cáceres, A. (2000) · Neurochemical Research · doi:10.1023/a:1007531230651 · Cited by 50

Tau: It’s Not What You Think

Baas, P. W., & Qiang, L. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.02.007 · Cited by 123