Tau; One Protein, So Many Diseases
Open accessAbstract
Tau, a member of the microtubule-associated proteins, is a known component of the neuronal cytoskeleton; however, in the brain tissue, it is involved in other vital functions beyond maintaining the cellular architecture. The pathologic tau forms aggregates inside the neurons and ultimately forms the neurofibrillary tangles. Intracellular and extracellular accumulation of different tau isoforms, including dimers, oligomers, paired helical filaments and tangles, lead to a highly heterogenous group of diseases named “Tauopathies”. About twenty-six different types of tauopathy diseases have been identified that have different clinical phenotypes or pathophysiological characteristics. Although all these diseases are identified by tau aggregation, they are distinguishable based on the specific tau isoforms, the affected cell types and the brain regions. The neuropathological and phenotypical heterogeneity of these diseases impose significant challenges for discovering new diagnostic and therapeutic strategies. Here, we review the recent literature on tau protein and the pathophysiological mechanisms of tauopathies. This article mainly focuses on physiologic and pathologic tau and aims to summarize the upstream and downstream events and discuss the current diagnostic approaches and therapeutic strategies.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Tau is predominantly expressed in cortical and hippocampal neurons, with expression also in oligodendrocytes and astrocytes.
“Tau is predominantly expressed in cortical and hippocampal neurons [5–7], although there is also expression in other cell types such as oligodendrocytes and astrocytes [8, 9].”
From Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease (2026) · cites this paper as [6]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
1 retracted
Zaki, M. O., El-Desouky, S., Elsherbiny, D. A., Salama, M., & Azab, S. S. (2022) · Inflammopharmacology · doi:10.1007/s10787-022-01023-w · Cited by 12 · see citing works
RetractedAmyloid 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 · see citing works
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 · see citing works
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 · see citing works
Tau in physiology and pathology
Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251 · see citing works
Buée, L., Bussière, T., Buée‐Scherrer, V., Delacourte, A., & Hof, P. R. (2000) · Brain Research Reviews · doi:10.1016/s0165-0173(00)00019-9 · Cited by 2,007 · see citing works
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 · see citing works
Donanemab in Early Alzheimer’s Disease
Mintun, M. A., Lo, A. C., Duggan Evans, C., Wessels, A. M., Ardayfio, P. A., Andersen, S. W., Shcherbinin, S., Sparks, J., Sims, J. R., Brys, M., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2100708 · Cited by 1,728 · cited 1× · see citing works
“Human AD patients Donanemab Slowing tau accumulation Tau accumulation [107,108]”
BackgroundDepletion of microglia and inhibition of exosome synthesis halt tau propagation
Asai, H., Ikezu, S., Tsunoda, S., Medalla, M., Luebke, J., Haydar, T., Wolozin, B., Butovsky, O., Kügler, S., & Ikezu, T. (2015) · Nature Neuroscience · doi:10.1038/nn.4132 · Cited by 1,591 · see citing works
An english translation of alzheimer’s 1907 paper, “über eine eigenartige erkankung der hirnrinde”
Stelzmann, R. A., Norman Schnitzlein, H., & Reed Murtagh, F. (1995) · Clinical Anatomy · doi:10.1002/ca.980080612 · Cited by 1,455 · see citing works
Hoover, B. R., Reed, M. N., Su, J., Penrod, R. D., Kotilinek, L. A., Grant, M. K., Pitstick, R., Carlson, G. A., Lanier, L. M., Yuan, L.-L., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.030 · Cited by 1,118 · see citing works
Tau-targeting therapies for Alzheimer disease
Congdon, E. E., & Sigurdsson, E. M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0013-z · Cited by 1,113 · cited 1× · see citing works
“Additional approaches include reducing the levels of plasma tau, inhibiting the aggregation of different forms of pathogenic tau such as PHFs, NFTs and small oligomeric tau aggregates, as well as enhancing tau clearance by active and passive tau immunization [90] (Figure 6).”
BackgroundTrans-Synaptic Spread of Tau Pathology In Vivo
Liu, L., Drouet, V., Wu, J., Witter, M. P., Small, S. A., Clelland, C. L. T., & Duff, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031302 · Cited by 994 · see citing works
Tau phosphorylation: the therapeutic challenge for neurodegenerative disease
Hanger, D. P., Anderton, B. H., & Noble, W. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.01.003 · Cited by 965 · see citing works
Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy
Min, S.-W., Cho, S.-H., Zhou, Y., Schroeder, S., Haroutunian, V., Seeley, W. W., Huang, E. J., Shen, Y., Masliah, E., Mukherjee, C., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.044 · Cited by 949 · see citing works
the TBI/CTE group, McKee, A. C., Cairns, N. J., Dickson, D. W., Folkerth, R. D., Dirk Keene, C., Litvan, I., Perl, D. P., Stein, T. D., Vonsattel, J.-P., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1515-z · Cited by 885 · see citing works
Molecular motors and mechanisms of directional transport in neurons
Hirokawa, N., & Takemura, R. (2005) · Nature reviews. Neuroscience · doi:10.1038/nrn1624 · Cited by 830 · see citing works
Blennow, K., Wallin, A., Ågren, H., Spenger, C., Siegfried, J., & Vanmechelen, E. (1995) · Molecular and Chemical Neuropathology · doi:10.1007/bf02815140 · Cited by 789 · see citing works
Structures of α-synuclein filaments from multiple system atrophy
Schweighauser, M., Shi, Y., Tarutani, A., Kametani, F., Murzin, A. G., Ghetti, B. F., Matsubara, T., Tomita, T., Ando, T., Hasegawa, K., et al. (2020) · Nature · doi:10.1038/s41586-020-2317-6 · Cited by 776 · see citing works
Tau protein function in living cells.
Drubin, D. G., & Kirschner, M. W. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.6.2739 · Cited by 745 · see citing works
Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609 · see citing works
Thijssen, E. H., La Joie, R., Strom, A., Fonseca, C., Iaccarino, L., Wolf, A., Spina, S., Allen, I. E., Cobigo, Y., Heuer, H., et al. (2021) · The Lancet Neurology · doi:10.1016/s1474-4422(21)00214-3 · Cited by 607 · see citing works
Dejanovic, B., Huntley, M. A., De Mazière, A., Meilandt, W. J., Wu, T., Srinivasan, K., Jiang, Z., Gandham, V., Friedman, B. A., Ngu, H., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.10.014 · Cited by 575 · see citing works
Neve, R. L., Harris, P. K. W., Kosik, K. S., Kurnit, D. M., & Donlon, T. A. (1986) · Molecular Brain Research · doi:10.1016/0169-328x(86)90033-1 · Cited by 565 · see citing works
Tau promotes neurodegeneration through global chromatin relaxation
Frost, B., Hemberg, M., Lewis, J., & Feany, M. B. (2014) · Nature Neuroscience · doi:10.1038/nn.3639 · Cited by 519 · see citing works
Zhang, W., Falcon, B., Murzin, A. G., Fan, J., Crowther, R. A., Goedert, M., & Scheres, S. H. W. (2019) · eLife · doi:10.7554/elife.43584 · Cited by 500 · see citing works
Tau Protein Disrupts Nucleocytoplasmic Transport in Alzheimer’s Disease
Eftekharzadeh, B., Daigle, J. G., Kapinos, L. E., Coyne, A., Schiantarelli, J., Carlomagno, Y., Cook, C., Miller, S. J., Dujardin, S., Amaral, A. S., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.07.039 · Cited by 460 · see citing works
Cerebrospinal fluid p-tau217 performs better than p-tau181 as a biomarker of Alzheimer's disease
Janelidze, S., Stomrud, E., Smith, R., Palmqvist, S., Mattsson, N., Airey, D. C., Proctor, N. K., Chai, X., Shcherbinin, S., Sims, J. R., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15436-0 · Cited by 450 · see citing works
c-Jun N-terminal Kinase (JNK) Signaling as a Therapeutic Target for Alzheimer’s Disease
Yarza, R., Vela, S., Solas, M., & Ramírez, M. J. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2015.00321 · Cited by 418 · see citing works
THE FINE STRUCTURE OF NEUROFIBRILLARY TANGLES IN ALZHEIMERʼS DISEASE
Terry, R. D. (1963) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-196310000-00005 · Cited by 403 · cited 1× · see citing works
“These studies showed that NFTs are predominantly composed of insoluble fibers called paired helical filaments (PHFs) [33].”
BackgroundLiu, Y., & Wang, M. (2002) · Circulation Research · doi:10.1161/01.res.0000022160.64355.62 · Cited by 388 · see citing works
Caccamo, A., Magrì, A., Medina, D. X., Wisely, E. V., López‐Aranda, M. F., Silva, A. J., & Oddo, S. (2013) · Aging Cell · doi:10.1111/acel.12057 · Cited by 362 · see citing works
Molecular neurobiology of mTOR.
Switon, K., Kotulska, K., Janusz-Kaminska, A., Zmorzyńska, J., & Jaworski, J. (2017) · Neuroscience · doi:10.1016/j.neuroscience.2016.11.017 · Cited by 352 · see citing works
Tauopathies: new perspectives and challenges
Zhang, Y., Wu, K.-M., Yang, L., Dong, Q., & Yu, J.-T. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00533-z · Cited by 323 · see citing works
Sun, W., Samimi, H., Gamez, M., Zare, H., & Frost, B. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0194-1 · Cited by 315 · see citing works
Tau Activates Transposable Elements in Alzheimer’s Disease
Guo, C., Jeong, H.-H., Hsieh, Y.-C., Klein, H.-U., Bennett, D. A., De Jager, P. L., Liu, Z., & Shulman, J. M. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.05.004 · Cited by 315 · see citing works
Protein phosphatase 2A dysfunction in Alzheimer’s disease
Sontag, J.-M., & Sontag, E. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00016 · Cited by 304 · see citing works
A walk through tau therapeutic strategies
Jadhav, S., Ávila, J., Schöll, M., Kovács, G. G., Kövari, E., Škrabana, R., Evans, L., Kontseková, E., Malawska, B., de Silva, R., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0664-z · Cited by 286 · see citing works
Rutin prevents tau pathology and neuroinflammation in a mouse model of Alzheimer’s disease
Sun, X., Li, L., Dong, Q.-X., Zhu, J., Huang, Y., Hou, S., Yu, X., & Liu, R. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02182-3 · Cited by 285 · see citing works
Zempel, H., Luedtke, J., Kumar, Y., Biernat, J., Dawson, H., Mandelkow, E., & Mandelkow, E. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.207 · Cited by 283 · see citing works
Tau PET imaging: present and future directions
Saint‐Aubert, L., Lemoine, L., Chiotis, K., Leuzy, A., Rodriguez‐Vieitez, E., & Nordberg, A. K. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0162-3 · Cited by 283 · see citing works
Tracy, T. E., Sohn, P. D., Minami, S. S., Wang, C., Min, S.-W., Li, Y., Zhou, Y., Le, D., Lo, I., Ponnusamy, R., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.005 · Cited by 277 · see citing works
Frandemiche, M. L., De Seranno, S., Rush, T., Borel, E., Elie, A., Arnal, I., Lanté, F., & Buisson, A. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.4261-13.2014 · Cited by 272 · see citing works
Glycogen Synthase Kinase 3β Phosphorylates Tau at Both Primed and Unprimed Sites
Cho, J.-H., & Johnson, G. V. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206236200 · Cited by 266 · see citing works
Immunotherapy for Alzheimer’s disease: targeting β-amyloid and beyond
Song, C., Shi, J., Zhang, P., Zhang, Y., Xu, J., Zhao, L., Zhang, R., Wang, H., & Chen, H. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00292-3 · Cited by 266 · see citing works
Liquid–liquid phase separation of tau protein: The crucial role of electrostatic interactions
Boyko, S., Qi, X., Chen, T., Surewicz, K. A., & Surewicz, W. K. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ac119.009198 · Cited by 255 · see citing works
Klein, C., Krämer, E.-M., Cardine, A.-M., Schraven, B., Brandt, R., & Trotter, J. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-03-00698.2002 · Cited by 250 · see citing works
Wang, W., Zhou, Q., Jiang, T., Li, S., Ye, J., Zheng, J., Wang, X., Liu, Y., Deng, M., Ke, D., et al. (2021) · Theranostics · doi:10.7150/thno.55680 · Cited by 242 · see citing works
A Brief Overview of Tauopathy: Causes, Consequences, and Therapeutic Strategies
Orr, M. E., Sullivan, A. C., & Frost, B. E. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.03.011 · Cited by 232 · see citing works
Barthélemy, N. R., Bateman, R. J., Hirtz, C., Marin, P., Becher, F., Sato, C., Gabelle, A., & Lehmann, S. (2020) · Alzheimer's Research & Therapy · doi:10.1186/s13195-020-00596-4 · Cited by 229 · see citing works
Rösler, T. W., Marvian, A. T., Brendel, M., Nykänen, N.-P., Höllerhage, M., Schwarz, S. C., Hopfner, F., Koeglsperger, T., Respondek, G., Schweyer, K., et al. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101644 · Cited by 219 · see citing works
Ectosomes: A New Mechanism for Non-Exosomal Secretion of Tau Protein
Dujardin, S., Bégard, S., Caillierez, R., Lachaud, C., Delattre, L., Carrier, S., Loyens, A., Galas, M., Bousset, L., Melki, R., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100760 · Cited by 215 · see citing works
Tau liquid‐liquid phase separation in neurodegenerative diseases
Boyko, S., & Surewicz, W. K. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2022.01.011 · Cited by 215 · see citing works
Shcherbinin, S., Evans, C. D., Lu, M., Andersen, S. W., Pontecorvo, M. J., Willis, B. A., Gueorguieva, I., Hauck, P. M., Brooks, D. A., Mintun, M. A., et al. (2022) · JAMA Neurology · doi:10.1001/jamaneurol.2022.2793 · Cited by 210 · see citing works
Safety and Efficacy of Semorinemab in Individuals With Prodromal to Mild Alzheimer Disease
Teng, E., Manser, P. T., Pickthorn, K., Brunstein, F., Blendstrup, M., Bohorquez, S. M. S., Wildsmith, K. R., Toth, B., Dolton, M. J., Ramakrishnan, V., et al. (2022) · JAMA Neurology · doi:10.1001/jamaneurol.2022.1375 · Cited by 204 · see citing works
Tau co-organizes dynamic microtubule and actin networks
Elie, A., Prezel, E., Guérin, C., Denarier, E., Ramirez-Rios, S., Serre, L., Andrieux, A., Fourest-Lieuvin, A., Blanchoin, L., & Arnal, I. (2015) · Scientific Reports · doi:10.1038/srep09964 · Cited by 200 · see citing works
Brelstaff, J., Tolkovsky, A. M., Ghetti, B., Goedert, M., & Spillantini, M. G. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.07.072 · Cited by 195 · see citing works
Tau oligomers and aggregation in Alzheimer’s disease
Meraz‐Ríos, M. A., León, K. I. L.-D., Campos‐Peña, V., Anda-Hernández, M. A. D., & Mena‐López, R. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06511.x · Cited by 193 · see citing works
Paonessa, F., Evans, L., Solanki, R., Larrieu, D., Wray, S., Hardy, J., Jackson, S. P., & Livesey, F. J. (2019) · Cell Reports · doi:10.1016/j.celrep.2018.12.085 · Cited by 189 · see citing works
From the prion-like propagation hypothesis to therapeutic strategies of anti-tau immunotherapy
Colin, M., Dujardin, S., Schraen-Maschke, S., Meno-Tetang, G., Duyckaerts, C., Courade, J.-P., & Buée, L. (2020) · Acta Neuropathologica · doi:10.1007/s00401-019-02087-9 · Cited by 187 · see citing works
Novak, P., Kovacech, B., Katina, S., Schmidt, R., Scheltens, P., Kontsekova, E., Ropele, S., Fialova, L., Kramberger, M., Paulenka-Ivanovova, N., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00070-2 · Cited by 187 · see citing works
Deregulated Cdk5 activity is involved in inducing Alzheimer's disease
Shukla, V., Skuntz, S., & Pant, H. C. (2012) · Archives of Medical Research · doi:10.1016/j.arcmed.2012.10.015 · Cited by 185 · see citing works
Developmental regulation of tau phosphorylation, tau kinases, and tau phosphatases
Yu, Y., Run, X., Liang, Z., Li, Y., Liu, F., Liu, Y. M., Iqbal, K., Grundke, I., & Gong, C. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05882.x · Cited by 177 · see citing works
Phosphorylation of tau regulates its axonal transport by controlling its binding to kinesin
Cuchillo‐Ibáñez, I., Seereeram, A., Byers, H. L., Leung, K., Ward, M. A., Anderton, B. H., & Hanger, D. P. (2008) · The FASEB Journal · doi:10.1096/fj.08-109181 · Cited by 170 · see citing works
Tau protein binds to pericentromeric DNA: a putative role for nuclear tau in nucleolar organization
Sjöberg, M. K., Shestakova, E., Mansuroglu, Z., Maccioni, R. B., & Bonnefoy, E. (2006) · Journal of Cell Science · doi:10.1242/jcs.02907 · Cited by 166 · see citing works
Ittner, L. M., Ke, Y. D., & Götz, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014472 · Cited by 156 · see citing works
Cabrales Fontela, Y., Kadavath, H., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017) · Nature Communications · doi:10.1038/s41467-017-02230-8 · Cited by 148 · see citing works
Retiring the term FTDP-17 as MAPT mutations are genetic forms of sporadic frontotemporal tauopathies
Forrest, S. L., Kril, J. J., Stevens, C. H., Kwok, J. B., Hallupp, M., Kim, W. S., Huang, Y. M., McGinley, C. V., Werka, H., Kiernan, M. C., et al. (2017) · Brain · doi:10.1093/brain/awx328 · Cited by 148 · see citing works
Dam, T., Boxer, A. L., Golbe, L. I., Höglinger, G. U., Morris, H. R., Litvan, I., Lang, A. E., Corvol, J., Aiba, I., Grundman, M., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01455-x · Cited by 146 · see citing works
Mansuroglu, Z., Benhelli-Mokrani, H., Marcato, V., Sultan, A., Violet, M., Chauderlier, A., Delattre, L., Loyens, A., Talahari, S., Bégard, S., et al. (2016) · Scientific Reports · doi:10.1038/srep33047 · Cited by 146 · see citing works
Correas, I., Padilla, R., & Avila, J. (1990) · Biochemical Journal · doi:10.1042/bj2690061 · Cited by 144 · see citing works
Tau protein diffuses along the microtubule lattice
Hinrichs, M. H., Jalal, A., Brenner, B., Mandelkow, E., Kumar, S., & Scholz, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.369785 · Cited by 141 · see citing works
Connecting the dots between tau dysfunction and neurodegeneration
Frost, B., Götz, J., & Feany, M. B. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.07.005 · Cited by 124 · see citing works
Reactive oxygen species regulate F‐actin dynamics in neuronal growth cones and neurite outgrowth
Munnamalai, V., & Suter, D. M. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05787.x · Cited by 123 · see citing works
Tau directs intracellular trafficking by regulating the forces exerted by kinesin and dynein teams
Chaudhary, A. R., Berger, F., Berger, C. L., & Hendricks, A. G. (2018) · Traffic · doi:10.1111/tra.12537 · Cited by 118 · see citing works
The involvement of tau in nucleolar transcription and the stress response
Maina, M. B., Bailey, L. J., Wagih, S., Biasetti, L., Pollack, S. J., Quinn, J. P., Thorpe, J. R., Doherty, A. J., & Serpell, L. C. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0565-6 · Cited by 109 · see citing works
Advances and considerations in AD tau-targeted immunotherapy
Bittar, A., Bhatt, N. N., & Kayed, R. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104707 · Cited by 105 · see citing works
Ercan-Herbst, E., Ehrig, J., Schöndorf, D. C., Behrendt, A., Klaus, B., Gomez Ramos, B., Prat Oriol, N., Weber, C., & Ehrnhoefer, D. E. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0823-2 · Cited by 101 · see citing works
Ou, W., Yang, J., Simanauskaite, J., Choi, M. K., Castellanos, D. M., Chang, R., Sun, J., Jagadeesan, N., Parfitt, K. D., Cribbs, D. H., et al. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02332-7 · Cited by 98 · see citing works
Kim, B., Sullivan, K. A., Backus, C., & Feldman, E. L. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3816 · Cited by 93 · see citing works
Recent developments of protein kinase inhibitors as potential AD therapeutics
Tell, V., & Hilgeroth, A. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00189 · Cited by 90 · see citing works
Hefti, M. M., Farrell, K. W., Kim, S., Bowles, K. R., Fowkes, M. E., Raj, T., & Crary, J. F. (2018) · PLoS ONE · doi:10.1371/journal.pone.0195771 · Cited by 86 · see citing works
Ramirez, P., Zuniga, G., Sun, W., Beckmann, A., Ochoa, E., DeVos, S. L., Hyman, B., Chiu, G., Roy, E. R., Cao, W., et al. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2021.102181 · Cited by 79 · see citing works
Current directions in tau research: Highlights from Tau 2020
Sexton, C. E., Snyder, H. M., Beher, D., Boxer, A. L., Brannelly, P., Brion, J., Buée, L., Cacace, A. M., Chételat, G., Citron, M., et al. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12452 · Cited by 78 · see citing works
Neves, A. F., Camargo, C. J., Premer, C., Hare, J. M., Baumel, B. S., & Pinto, M. (2021) · Experimental Neurology · doi:10.1016/j.expneurol.2021.113706 · Cited by 76 · see citing works
Partial rescue of memory deficits induced by calorie restriction in a mouse model of tau deposition
Brownlow, M. L., Joly‐Amado, A., Azam, S., Elza, M., Selenica, M. B., Pappas, C. A., Small, B. J., Engelman, R. W., Gordon, M. N., & Morgan, D. (2014) · Behavioural Brain Research · doi:10.1016/j.bbr.2014.06.001 · Cited by 73 · see citing works
Brandt, R., & Lee, G. S. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03613.x · Cited by 60 · see citing works
Distinct Conformers of Assembled Tau in Alzheimer's and Pick's DiseasesPreprint
Goedert, M., Falcon, B., Zhang, W., Ghetti, B. F., & Scheres, S. H. W. (2018) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2018.83.037580 · Cited by 56 · see citing works
A τ Fragment Containing a Repetitive Sequence Induces Bundling of Actin Filaments
Moraga, D. M., Nuñez, P., Garrido, J., & Maccioni, R. B. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03611.x · Cited by 56 · see citing works
Rühlmann, C., Wölk, T., Blümel, T., Stahn, L., Vollmar, B., & Kuhla, A. (2016) · Aging · doi:10.18632/aging.101086 · Cited by 55 · see citing works
Wischik, C. M., Bentham, P., Gauthier, S., Miller, S., Kook, K., & Schelter, B. O. (2022) · The Journal of Prevention of Alzheimer's Disease · doi:10.14283/jpad.2022.63 · Cited by 55 · see citing works
P‐tau235: a novel biomarker for staging preclinical Alzheimer’s disease
Lantero‐Rodriguez, J., Snellman, A., Benedet, A. L., Milà‐Alomà, M., Camporesi, E., Montoliu‐Gaya, L., Ashton, N. J., Vrillon, A., Karikari, T. K., Gispert, J. D., et al. (2021) · EMBO Molecular Medicine · doi:10.15252/emmm.202115098 · Cited by 54 · see citing works
Crary, J. F. (2016) · Journal of Neurology and Neuromedicine · doi:10.29245/2572.942x/2016/6.1059 · Cited by 52 · see citing works
Epigallocatechin-3-gallate modulates Tau Post-translational modifications and cytoskeletal network
Sonawane, S. K., & Chinnathambi, S. (2021) · Oncotarget · doi:10.18632/oncotarget.27963 · Cited by 51 · see citing works
Moscoso, A., Karikari, T. K., Grothe, M. J., Ashton, N. J., Lantero‐Rodriguez, J., Snellman, A., Zetterberg, H., Blennow, K., & Schöll, M. (2022) · Alzheimer s & Dementia · doi:10.1002/alz.12570 · Cited by 50 · see citing works
Tong, B. C., Huang, S., Wu, A. J., Iyaswamy, A., Ho, O. K.-Y., Kong, A. H.-Y., Sreenivasmurthy, S. G., Zhu, Z., Su, C.-F., Liu, J., et al. (2022) · Journal of Biomedical Science · doi:10.1186/s12929-022-00871-6 · Cited by 49 · see citing works
Closing the tau loop: the missing tau mutation
McCarthy, A. J., Lonergan, R. M., Olszewska, D. A., O’Dowd, S., Cummins, G. A., Magennis, B., Fallon, E., Pender, N. P., Huey, E. D., Cosentino, S., et al. (2015) · Brain · doi:10.1093/brain/awv234 · Cited by 41 · see citing works
Tauopathy and Movement Disorders—Unveiling the Chameleons and Mimics
Ganguly, J., & Jog, M. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.599384 · Cited by 38 · see citing works
Cousins, K. A. Q., Phillips, J. S., Irwin, D. J., Lee, E. B., Wolk, D. A., Shaw, L. M. J., Zetterberg, H., Blennow, K., Burke, S., Kinney, N. G., et al. (2020) · Alzheimer s & Dementia · doi:10.1002/alz.12233 · Cited by 36 · see citing works
Distribution of five clinically important neuroglial proteins in the human brain
Sjölin, K., Kultima, K., Larsson, A., Freyhult, E., Zjukovskaja, C., Alkass, K., & Burman, J. (2022) · Molecular Brain · doi:10.1186/s13041-022-00935-6 · Cited by 36 · see citing works
Interplay between Velocity and Travel Distance of Kinesin-based Transport in the Presence of Tau
Xu, J., King, S. J., Lapierre-Landry, M., & Nemec, B. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2013.10.006 · Cited by 32 · see citing works
Teng, E., Manser, P. T., Bohorquez, S. M. S., Wildsmith, K. R., Pickthorn, K., Baker, S. L., Ward, M. E., Kerchner, G. A., & Weimer, R. M. (2021) · Alzheimer s Research & Therapy · doi:10.1186/s13195-021-00937-x · Cited by 31 · see citing works
Preventing apoptosis with thioredoxin: ASK me how.
Bishopric, N., & Webster, K. (2002) · Circulation Research · doi:10.1161/01.res.0000025101.04065.83 · Cited by 30 · see citing works
Mignon, L., Kordasiewicz, H., Lane, R., Smith, A., Miller, T., Narayanan, P., Swayze, E., Norris, D., Fitzsimmons, B., & Bennett, F. (2018) · Neurology · doi:10.1212/wnl.90.15_supplement.s2.006 · Cited by 29 · see citing works
Easton, A. E., Jensen, M. L., Wang, C., Hagedorn, P., Li, Y.-W., Weed, M. R., Meredith, J. E., Guss, V. L., Jones, K. M., Gill, M. B., et al. (2022) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2022.07.027 · Cited by 27 · see citing works
Xia, L., Pang, Y., Li, J., Wu, B., Du, Y., Chen, Y., Luo, M., Wang, Y., & Dong, Z. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210643 · Cited by 25 · see citing works
Alvarez, X. A., Winston, C. N., Barlow, J. W., Sarsoza, F. M., Álvarez, I., Aleixandre, M., Linares, C., García-Fantini, M., Kastberger, B., Winter, S., et al. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220575 · Cited by 23 · see citing works
Genetic Architecture of Primary Tauopathies
Gallo, D., Ruiz, A., & Sánchez‐Juan, P. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.05.022 · Cited by 22 · see citing works
Maina, M. B., Al‐Hilaly, Y. K., Oakley, S. S., Burra, G., Khanom, T., Biasetti, L., Mengham, K., Marshall, K. E., Rickard, J. E., Harrington, C. R., et al. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167785 · Cited by 22 · see citing works
Bittar, A., Al-Lahham, R., Bhatt, N., Moore, K., Montalbano, M., Jerez, C., Fung, L., McAllen, S., Ellsworth, A., & Kayed, R. (2022) · Journal of Alzheimer's Disease · doi:10.3233/jad-220518 · Cited by 18 · see citing works
Polis, B., Squillario, M., Gurevich, V., Srikanth, K. D., Assa, M., & Samson, A. O. (2022) · Neurochemical Research · doi:10.1007/s11064-021-03519-3 · Cited by 15 · see citing works
Oxidative Stress Conditions Result in Trapping of PHF-Core Tau (297–391) Intermediates
Maina, M. B., Al‐Hilaly, Y. K., Burra, G., Rickard, J. E., Harrington, C. R., Wischik, C. M., & Serpell, L. C. (2021) · Cells · doi:10.3390/cells10030703 · Cited by 14 · see citing works
Propranolol Reduces p-tau Accumulation and Improves Behavior Outcomes in a Polytrauma Murine Model
Singer, K. E., McGlone, E., Collins, S. M., Wallen, T. E., Morris, M. C., Schuster, R. M., England, L. G., Robson, M. J., & Goodman, M. D. (2022) · Journal of Surgical Research · doi:10.1016/j.jss.2022.09.017 · Cited by 8 · see citing works
Anglada‐Huguet, M., Rodrigues, S., Hochgräfe, K., Mandelkow�, E., & Mandelkow, E. (2021) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.12170 · Cited by 6 · see citing works
Molecular imaging biomarkers in familial frontotemporal lobar degeneration: Progress and prospects
Wang, R., Gao, H., Xie, H., Jia, Z., & Chen, Q. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.933217 · Cited by 5 · see citing works
Flagged first, then by citations
2 of the 117 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Park, Y., Nirajan, K. C., Paneque, A., & Cole, P. D. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25126295 · Cited by 77 · see citing works
SIRT2 as a potential new therapeutic target for Alzheimer’s disease
Sola-Sevilla, N., & Puerta, E. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.375315 · Cited by 33 · see citing works
Chavoshinezhad, S., Beirami, E., Izadpanah, E., Feligioni, M., & Hassanzadeh, K. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115656 · Cited by 27 · see citing works
Nayak, V., Patra, S., Rout, S., Jena, A. B., Sharma, R., Pattanaik, K. P., Singh, J., Pandey, S. S., Singh, R. P., Majhi, S., et al. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.155150 · Cited by 25 · see citing works
Munteanu, C., Iordan, D. A., Hoteteu, M., Popescu, C., POSTOIU, R. L., Onu, I., & Onose, G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015481 · Cited by 23 · see citing works
Shared genetic architecture of COVID-19 and Alzheimer’s disease
Matveeva, N. A., Сергеевич, К. И., Baulina, N., Semina, E. V., Kakotkin, V. V., Агапов, М. А., Кулакова, О. Г., & Favorova, O. O. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1287322 · Cited by 19 · see citing works
Bisi, N., Pinzi, L., Rastelli, G., & Tonali, N. (2024) · Molecules · doi:10.3390/molecules29030722 · Cited by 13 · see citing works
Targeting Tau Protein with Proximity Inducing Modulators: A New Frontier to Combat Tauopathies
Uliassi, E., Bolognesi, M. L., & Milelli, A. (2025) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00733 · Cited by 13 · see citing works
Cai, H.-Y., Hou, F., Wang, Y., Wu, L.-H., Wang, Z.-J., Wu, M., Wang, X., & Hölscher, C. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.177347 · Cited by 7 · see citing works
Liu, Y.-F., Zhang, J., Tang, L., Yang, J.-Y., Hao, L., Lou, F., & Su, J.-Y. (2025) · Archives of Toxicology · doi:10.1007/s00204-025-04174-1 · Cited by 6 · see citing works
Illuminating Tau Aggregates: Multiscale Approaches for Detection, Imaging, and Understanding
Bhuskute, K. R., Fan, J., & Kaur, A. (2025) · Aggregate · doi:10.1002/agt2.70133 · Cited by 6 · see citing works
Potential Application of MicroRNAs and Some Other Molecular Biomarkers in Alzheimer’s Disease
Paprzycka, O., Wieczorek, J., Nowak, I., Madej, M., & Strzałka‐Mrozik, B. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46060304 · Cited by 6 · see citing works
Tau and MAP6 establish labile and stable domains on microtubules
Kirimtay, K., Huang, W., Sun, X., Qiang, L., Wang, D. V., Sprouse, F. C., Craig, E. M., & Baas, P. W. (2025) · iScience · doi:10.1016/j.isci.2025.111785 · Cited by 5 · see citing works
Suri, K., Ramesh, M., Bhandari, M., Gupta, V., Kumar, V., Govindaraju, T., & Murugan, N. A. (2024) · ChemBioChem · doi:10.1002/cbic.202400224 · Cited by 5 · see citing works
West, N. R., Lindberg, M. F., Dairou, J., MacGregor, S., Puthireddy, S., Meijer, L., & Bhattacharyya, A. (2026) · Disease Models & Mechanisms · doi:10.1242/dmm.052740 · Cited by 3 · see citing works
Negi, D., Shorter, S. A., Goodhall, I., Razansky, D., Shergill, S. S., & Ovsepian, S. V. (2025) · Scientific Reports · doi:10.1038/s41598-025-15561-0 · Cited by 3 · see citing works
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
Therapeutic Modalities Targeting Tau Protein in Alzheimer’s Disease
Schreiner, T. G., Iacob, L., Vasilache, C., & Schreiner, O. D. (2025) · Journal of dementia and Alzheimer's disease · doi:10.3390/jdad2030032 · Cited by 2 · see citing works
Amor-Guéret, M. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167213 · Cited by 1 · see citing works
Current Treatment Approaches for Alzheimer’s Disease and Possible Drug Targets
Ranjan, A., Shukla, S., & Singh, S. (2024) · Current Drug Therapy · doi:10.2174/0115748855307998240529063710 · Cited by 1 · see citing works
Caenorhabditis elegans as a Model Organism for Proteinopathies
Vimal, P., Verma, D., Bhunia, P. K., & Kasturi, P. (2026) · Springer eBooks · doi:10.1007/978-981-92-0038-2_9 · Cited by 1 · see citing works
Oxidative stress and inflammation in neurodegenerative disorders
Jomová, K., Alomar, S. Y., Valko, R., Nepovimová, E., Kuča, K., & Valko, M. (2026) · Archives of Toxicology · doi:10.1007/s00204-026-04518-5 · Cited by 1 · see citing works
Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease
Chimal-Juárez, E., Patel, H., Jury-Garfe, N., Dabin, L. C., Vidal, R., Kim, J., & Lasagna-Reeves, C. A. (2026) · bioRxiv · doi:10.64898/2026.05.12.724684
Parkinson's disease and related disorders
Agin‐Liebes, J., & Fahn, S. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-19176-3.00023-6
Sung, S.-H., Shin, S. H., Kim, Y., & Cho, S. (2025) · Journal of pharmacopuncture · doi:10.3831/kpi.2025.28.2.92
Hassan, M., Shahzadi, S., Moustafa, A. A., & Kloczkowski, A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262211021
Tau-Cytoskeleton and their interaction with other neurodegenerative proteins
Sahu, S., Rangappa, N., Chinnathambi, S., & Mishra, M. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.032
Chinnathambi, S., Suresh, S., Velmurugan, G., & Mishra, A. (2025) · Advances in immunology · doi:10.1016/bs.ai.2025.11.004
Leucettinib-21 decreases dosage effects of DYRK1A in human trisomy 21 iPSC-derived neural cellsPreprint
West, N. R., Lindberg, M. F., Dairou, J., MacGregor, S., Puthireddy, S., Meijer, L., & Bhattacharyya, A. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.05.704014
Connecting the Dots: Neurobiological Interplay Between Type 2 Diabetes and Alzheimer’s Disease
Foncea-Bitrán, A., Barros-Osorio, C., Arriaza, F., Ramírez-López, C., Ruíz, L. M., Barreto, M., Ortíz, F. C., Cornejo, F., & Gómez, G. I. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27073225
Clemente, E., Sivasubramanian, R., Kordes, S., Bhatia, P., Hans, R., Vogel, S., Baumann, M., Klebl, B., & Sterneckert, J. L. (2026) · Cells · doi:10.3390/cells15131228
Fischer, I. (2026) · Biomolecules · doi:10.3390/biom16081215
Otun, S., & Achilonu, I. (2026) · Exploration of neuroscience · doi:10.37349/en.2026.1006149
- Authors
- Tabeshmehr, P., & Eftekharpour, E.
- Affiliations
- University of Manitoba (CA)
- Corresponding author
- Eftekharpour, Eftekhar
- Venue
- Biology
- Publisher
- MDPI AG
- Published
- 2023-02-03
- Volume
- 12
- Issue
- 2
- Pages
- 244
- ISSN
- 2079-7737 (ISSN-L)
- PMC
- PMC9953016
- OpenAlex
- W4319316995
- Cited by
- 33
- References
- 117
- Citations by year
- 2026: 10 · 2025: 11 · 2024: 7 · 2023: 5
- FWCI
- 1.18
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Biology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- University of Manitoba Graduate Studentship Fund
- GETS (Graduate Enhancement of Tri-agency Stipends)
- Natural Sciences and Engineering Research Council of Canada
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Keywords
- tau protein, tauopathy, neurofibrillary tangles, tau aggregation, tau isoforms, paired helical filaments, microtubule-associated proteins, neuronal cytoskeleton, pathophysiological mechanisms, diagnostic approach, treatment options, Alzheimer's disease, frontotemporal lobar degeneration
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
