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The Many Faces of Tau
Open accessAbstract
While the microtubule-binding capacity of the protein tau has been known for many years, new functions of tau in signaling and cytoskeletal organization have recently emerged. In this review, we highlight these functions and the potential roles of tau in neurodegenerative disease. We also discuss the therapeutic potential of drugs targeting various aspects of tau biology.
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“markedly reduces amyloid 𝛃 and ApoE4 fragment-induced neuronal and cognitive impairments in vivo (34)”
From An Unbiased Approach to Identifying Tau Kinases That Phosphorylate Tau at Sites Associated with Alzheimer Disease (2013) · cites this paper as [34]
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“Reductions in tau levels have also been shown to prevent amyloid 𝛃 from causing neuronal deficits in cell culture and in transgenic mice expressing human amyloid precursor protein (34).”
From An Unbiased Approach to Identifying Tau Kinases That Phosphorylate Tau at Sites Associated with Alzheimer Disease (2013) · cites this paper as [34]
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“in mice a 50% reduction of endogenous tau is well tolerated”
From An Unbiased Approach to Identifying Tau Kinases That Phosphorylate Tau at Sites Associated with Alzheimer Disease (2013) · cites this paper as [34]
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“The interaction of tau with microtubules in neurons is well documented and more recent studies have proposed that tau also binds to actin34.”
From Tau co-organizes dynamic microtubule and actin networks (2015) · cites this paper as [34]
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“Tauopathies are neurodegenerative diseases characterized by aberrant forms of tau protein accumulation leading to neuronal death in focal brain areas.”
From Targeted degradation of aberrant tau in frontotemporal dementia patient-derived neuronal cell models (2019) · cites this paper as Morris et al., 2011
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Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
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
Mechanisms and Functional Implications of Adult Neurogenesis
Zhao, C., Deng, W., & Gage, F. H. (2008) · Cell · doi:10.1016/j.cell.2008.01.033 · Cited by 3,007
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
Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480
Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208
Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function
SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014
Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model
Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892
Self-citationDendritic 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
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Huang, Y., & Mucke, L. (2012) · Cell · doi:10.1016/j.cell.2012.02.040 · Cited by 1,758
Self-citationMechanisms of stress in the brain
McEwen, B. S., Bowles, N. P., Gray, J. D., Hill, M. N., Hunter, R. G., Karatsoreos, I. N., & Nasca, C. (2015) · Nature Neuroscience · doi:10.1038/nn.4086 · Cited by 1,386
Impairment of Glymphatic Pathway Function Promotes Tau Pathology after Traumatic Brain Injury
Iliff, J. J., Chen, M. J., Plog, B. A., Zeppenfeld, D. M., Soltero, M., Yang, L., Singh, I., Deane, R., & Nedergaard, M. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.3020-14.2014 · Cited by 1,159
Network abnormalities and interneuron dysfunction in Alzheimer disease
Palop, J. J., & Mucke, L. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.141 · Cited by 1,022
Self-citationRoles 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
Neurotoxicity of Amyloid -Protein: Synaptic and Network Dysfunction
Mucke, L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006338 · Cited by 1,000
Self-citationBiochemistry and Cell Biology of Tau Protein in Neurofibrillary DegenerationPreprint
Mandelkow, E., & Mandelkow, E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006247 · Cited by 897
Šimić, G., Leko, M. B., Wray, S., Harrington, C. R., Delalle, I., Milošević, N. J., Bažadona, D., Buée, L., de Silva, R., Giovanni, G. D., et al. (2016) · Biomolecules · doi:10.3390/biom6010006 · Cited by 730
Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609
Aβ induces astrocytic glutamate release, extrasynaptic NMDA receptor activation, and synaptic loss
Talantova, M., Sanz-Blasco, S., Zhang, X., Xia, P., Akhtar, M. W., Okamoto, S.-I., Dziewczapolski, G., Nakamura, T., Cao, G., Pratt, A. E., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1306832110 · Cited by 600
Maphis, N., Xu, G., Kokiko-Cochran, O. N., Jiang, S., Cardona, A., Ransohoff, R. M., Lamb, B. T., & Bhaskar, K. (2015) · Brain · doi:10.1093/brain/awv081 · Cited by 595
Suberbielle, E., Sanchez, P. E., Kravitz, A. V., Wang, X., Ho, K., Eilertson, K., Devidze, N., Kreitzer, A. C., & Mucke, L. (2013) · Nature Neuroscience · doi:10.1038/nn.3356 · Cited by 487
Self-citationMorris, M., Knudsen, G. M., Maeda, S., Trinidad, J. C., Ioanoviciu, A., Burlingame, A. L., & Mucke, L. (2015) · Nature Neuroscience · doi:10.1038/nn.4067 · Cited by 472
Self-citationTai, H.-C., Serrano-Pozo, A., Hashimoto, T., Frosch, M. P., Spires-Jones, T. L., & Hyman, B. T. (2012) · The American Journal of Pathology · doi:10.1016/j.ajpath.2012.06.033 · Cited by 443
The role of astrocytes in amyloid production and Alzheimer's disease
Frost, G. R., & Li, Y. (2017) · Open Biology · doi:10.1098/rsob.170228 · Cited by 448
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Zhou, L., McInnes, J., Wierda, K., Holt, M., Herrmann, A. G., Jackson, R. J., Wang, Y.-C., Swerts, J., Beyens, J., Miskiewicz, K., et al. (2017) · Nature Communications · doi:10.1038/ncomms15295 · Cited by 434
Olney, N. T., Spina, S., & Miller, B. L. (2017) · Neurologic Clinics · doi:10.1016/j.ncl.2017.01.008 · Cited by 419
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Mahley, R. W., & Huang, Y. (2012) · Neuron · doi:10.1016/j.neuron.2012.11.020 · Cited by 412
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Leyns, C. E. G., & Holtzman, D. M. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0192-x · Cited by 409
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Naseri, N. N., Wang, H., Guo, J. D., Sharma, M., & Luo, W. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.04.022 · Cited by 393
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
Tau interactome maps synaptic and mitochondrial processes associated with neurodegeneration
Tracy, T. E., Madero‐Pérez, J., Swaney, D. L., Chang, T. S., Moritz, M., Konràd, C., Ward, M. E., Stevenson, E. J., Hüttenhain, R., Kauwe, G., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.041 · Cited by 355
Michailidis, M., Moraitou, D., Tata, D. A., Kalinderi, K., Papamitsou, T., & Papaliagkas, V. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052687 · Cited by 330
Fluid biomarkers for mild traumatic brain injury and related conditions
Zetterberg, H., & Blennow, K. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2016.127 · Cited by 344
Lee, J. K., & Kim, N. (2017) · Molecules · doi:10.3390/molecules22081287 · Cited by 326
Mouse models of Alzheimer's disease
Hall, A. M., & Roberson, E. D. (2012) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2011.11.017 · Cited by 317
Role of Amyloid-β and Tau Proteins in Alzheimer’s Disease: Confuting the Amyloid Cascade
Gulisano, W., Maugeri, D., Baltrons, M. A., Fà, M., Amato, A., Palmeri, A., D’Adamio, L., Grassi, C., Devanand, D. P., Honig, L. S., et al. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179935 · Cited by 313
Microtubule-associated protein tau is essential for long-term depression in the hippocampus
Kimura, T., Whitcomb, D. J., Jo, J., Regan, P., Piers, T., Heo, S., Brown, C., Hashikawa, T., Murayama, M., Seok, H., et al. (2014) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2013.0144 · Cited by 307
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
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Kimura, T., Ishiguro, K., & Hisanaga, S. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00065 · Cited by 306
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Krüger, U., Wang, Y., Kumar, S., & Mandelkow, E.-M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.009 · Cited by 297
Neill, C. O. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2013.02.025 · Cited by 300
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
Targeted degradation of aberrant tau in frontotemporal dementia patient-derived neuronal cell models
Silva, M. C., Ferguson, F. M., Cai, Q., Donovan, K. A., Nandi, G., Patnaik, D., Zhang, T., Huang, H.-T., Lucente, D. E., Dickerson, B. C., et al. (2019) · eLife · doi:10.7554/elife.45457 · Cited by 283
Kopeikina, K. J., Carlson, G. A., Pitstick, R., Ludvigson, A. E., Peters, A., Luebke, J. I., Koffie, R. M., Frosch, M. P., Hyman, B. T., & Spires‐Jones, T. L. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.07.004 · Cited by 281
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Zhang, F., & Jiang, L. (2015) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s75546 · Cited by 276
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Schoch, K. M., & Miller, T. M. (2017) · Neuron · doi:10.1016/j.neuron.2017.04.010 · Cited by 274
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Fà, M., Puzzo, D., Piacentini, R., Staniszewski, A., Zhang, H., Baltrons, M. A., Puma, D. D. L., Chatterjee, I., Li, J., Saeed, F., et al. (2016) · Scientific Reports · doi:10.1038/srep19393 · Cited by 290
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
Tau-based therapies in neurodegeneration: opportunities and challenges
Li, C., & Götz, J. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.155 · Cited by 272
Inhibition of Amyloid Formation
Härd, T., & Lendel, C. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.062 · Cited by 277
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Busche, M. A., & Konnerth, A. (2015) · BioEssays · doi:10.1002/bies.201500004 · Cited by 266
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Chen, Y., Fu, A. K. Y., & Ip, N. Y. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.11.006 · Cited by 258
Models of β-amyloid induced Tau-pathology: The long and “folded” road to understand the mechanism
Stancu, I.-C., Vasconcelos, B., Terwel, D., & Dewachter, I. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-51 · Cited by 256
Benskey, M. J., Perez, R. G., & Manfredsson, F. P. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13570 · Cited by 257
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
The role of pathological tau in synaptic dysfunction in Alzheimer’s diseases
Wu, M., Zhang, M., Yin, X., Chen, K., Hu, Z., Zhou, Q., Cao, X., Chen, Z., & Liu, D. (2021) · Translational Neurodegeneration · doi:10.1186/s40035-021-00270-1 · Cited by 241
Pratt, W. B., Gestwicki, J. E., Osawa, Y., & Lieberman, A. P. (2014) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010814-124332 · Cited by 244
Holth, J. K., Bomben, V. C., Reed, J. G., Inoue, T., Younkin, L., Younkin, S. G., Pautler, R. G., Botas, J., & Noebels, J. L. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.3191-12.2013 · Cited by 238
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Kopeikina, K., Hyman, B., & Spires-Jones, T. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0032-y · Cited by 232
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Koutsodendris, N., Nelson, M. R., Rao, A., & Huang, Y. (2022) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-030421-112756 · Cited by 231
Randall, J., Mörtberg, E., Provuncher, G. K., Fournier, D. R., Duffy, D. C., Rubertsson, S., Blennow, K., Zetterberg, H., & Wilson, D. H. (2013) · Resuscitation · doi:10.1016/j.resuscitation.2012.07.027 · Cited by 230
Taniguchi, M., & Okazaki, T. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.12.003 · Cited by 229
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 231
Acetylated tau inhibits chaperone-mediated autophagy and promotes tau pathology propagation in mice
Caballero, B., Bourdenx, M., Luengo, E., Diaz, A., Sohn, P. D., Chen, X., Wang, C., Juste, Y. R., Wegmann, S., Patel, B., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22501-9 · Cited by 223
Tau in neurodegenerative disease
Gao, Y.-L., Wang, N., Sun, F.-R., Cao, X.-P., Zhang, W., & Yu, J.-T. (2018) · Annals of Translational Medicine · doi:10.21037/atm.2018.04.23 · Cited by 222
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Čulig, L., Chu, X., & Bohr, V. A. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101636 · Cited by 235
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Sinsky, J., Pichlerova, K., & Hanes, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179207 · Cited by 220
Lashley, T., Rohrer, J. D., Mead, S., & Révész, T. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12250 · Cited by 234
Kanaan, N. M., Pigino, G. F., Brady, S. T., Lazarov, O., Binder, L. I., & Morfini, G. A. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.06.003 · Cited by 215
Blalock, E. M., Buechel, H. M., Popovic, J., Geddes, J. W., & Landfield, P. W. (2011) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2011.06.007 · Cited by 211
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Sotiropoulos, I., Galas, M., Silva, J. M., Skoulakis, E. M. C., Wegmann, S., Maina, M. B., Blum, D. L., Sayas, C. L., Mandelkow, E., Mandelkow�, E., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0489-6 · Cited by 221
Updates in Alzheimer's disease: from basic research to diagnosis and therapies
Liu, E., Zhang, Y., & Wang, J. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00432-x · Cited by 241
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Marciniak, E., Leboucher, A., Caron, E., Ahmed, T., Tailleux, A., Dumont, J., Issad, T., Gerhardt, E., Pagesy, P., Vileno, M., et al. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20161731 · Cited by 205
Tau Phosphorylation at Serine 396 Residue Is Required for Hippocampal LTD
Regan, P., Piers, T., Yi, J.-H., Kim, D.-H., Huh, S., Park, S. J., Ryu, J. H., Whitcomb, D. J., & Cho, K. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.2842-14.2015 · Cited by 202
Fatouros, C., Pir, G. J., Biernat, J., Koushika, S. P., Mandelkow�, E., Mandelkow, E., Schmidt, E., & Baumeister, R. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds190 · Cited by 201
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
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Frozza, R. L., Lourenco, M. V., & Felice, F. G. D. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00037 · Cited by 213
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
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Bradley, C. A., Peineau, S., Taghibiglou, C., Nicolas, C. S., Whitcomb, D. J., Bortolotto, Z. A., Kaang, B., Cho, K., Wang, Y. T., & Collingridge, G. L. (2012) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2012.00013 · Cited by 202
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Siahaan, V., Krattenmacher, J., Hyman, A. A., Diez, S., Hernández-Vega, A., Lansky, Z., & Braun, M. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0374-6 · Cited by 169
Neurodegeneration and microtubule dynamics: death by a thousand cuts
Dubey, J., Ratnakaran, N., & Koushika, S. P. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00343 · Cited by 191
Cellular and molecular mechanisms underlying axon formation, growth, and branching
Lewis, T. L., Courchet, J., & Polleux, F. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201305098 · Cited by 195
Li, C., & Götz, J. (2017) · The EMBO Journal · doi:10.15252/embj.201797724 · Cited by 178
Fuego—An Open-Source Framework for Board Games and Go Engine Based on Monte Carlo Tree Search
Enzenberger, M., Müller, M., Arneson, B., & Segal, R. B. (2010) · IEEE Transactions on Computational Intelligence and AI in Games · doi:10.1109/tciaig.2010.2083662 · Cited by 176
Barten, D. M., Fanara, P., Andorfer, C. A., Hoque, N., Wong, P. A., Husted, K. H., Cadelina, G. W., DeCarr, L. B., Yang, L., Liu, V., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0188-12.2012 · Cited by 173
Janning, D., Igaev, M., Sündermann, F., Brühmann, J., Beutel, O., Heinisch, J. J., Bakota, L., Piehler, J., Junge, W., & Brandt, R. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-06-1099 · Cited by 181
Tapia‐Rojas, C., Aránguiz, F. C., Varela‐Nallar, L., & Inestrosa, N. C. (2015) · Brain Pathology · doi:10.1111/bpa.12255 · Cited by 176
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Vossel, K. A., Xu, J. C., Fomenko, V., Miyamoto, T., Suberbielle, E., Knox, J. A., Ho, K., Kim, D. H., Yu, G.-Q., & Mucke, L. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201407065 · Cited by 167
Self-citationLeroy, K., Ando, K., Laporte, V., Dedecker, R., Suain, V., Authelet, M., Héraud, C., Pierrot, N., Yilmaz, Z., Octave, J.-N., et al. (2012) · The American Journal of Pathology · doi:10.1016/j.ajpath.2012.08.012 · Cited by 161
The role of extracellular Tau in the spreading of neurofibrillary pathology
Medina, M., & Avila, J. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00113 · Cited by 161
Sohn, P. D., Tracy, T. E., Son, H.-I., Zhou, Y., Leite, R. E. P., Miller, B. L., Seeley, W. W., Grinberg, L. T., & Gan, L. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0109-0 · Cited by 160
The basis of cellular and regional vulnerability in Alzheimer’s disease
Mrdjen, D., Fox, E. J., Bukhari, S. A., Montine, K. S., Bendall, S. C., & Montine, T. J. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02054-4 · Cited by 162
Sodium selenate reduces hyperphosphorylated tau and improves outcomes after traumatic brain injury
Shultz, S. R., Wright, D. K., Zheng, P., Stuchbery, R., Liu, S.-J., Sashindranath, M., Medcalf, R. L., Johnston, L. A., Hovens, C. M., Jones, N. C., et al. (2015) · Brain · doi:10.1093/brain/awv053 · Cited by 159
GSK3β and tau protein in Alzheimer's disease and epilepsy
Toral-Rios, D., Pichardo-Rojas, P. S., Alonso-Vanegas, M., & Campos-Peña, V. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00019 · Cited by 158
Reduction of Nuak1 Decreases Tau and Reverses Phenotypes in a Tauopathy Mouse Model
Lasagna‐Reeves, C. A., de Haro, M., Hao, S., Park, J., Rousseaux, M. W. C., Al‐Ramahi, I., Jafar‐Nejad, P., Vilanova-Velez, L., See, L., Maio, A. D., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.022 · Cited by 154
Protein–Small Molecule Interactions in Native Mass Spectrometry
Bennett, J. L., Nguyen, G. T. H., & Donald, W. A. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00293 · Cited by 161
Discovering the landscape of protein modifications
Keenan, E. K., Zachman, D. K., & Hirschey, M. D. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.03.015 · Cited by 160
Man, V. H., Nguyen, P. H., & Derreumaux, P. (2017) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.7b04689 · Cited by 152
Boselli, M. G., Lee, B., Robert, J., Prado, M. A., Min, S., Cheng, C., Silva, M. C., Seong, C., Elsasser, S., Hatle, K. M., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.815126 · Cited by 151
Zucca, F. A., Vanna, R., Cupaioli, F. A., Bellei, C., Palma, A. D., Silvestre, D. D., Mauri, P., Grassi, S., Prinetti, A., Casella, L., et al. (2018) · npj Parkinson s Disease · doi:10.1038/s41531-018-0050-8 · Cited by 154
Guan, S., Price, J. C., Prusiner, S. B., Ghaemmaghami, S., & Burlingame, A. L. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.010728 · Cited by 148
Frontotemporal Dementia: Implications for Understanding Alzheimer DiseasePreprint
Goedert, M., Ghetti, B. F., & Spillantini, M. G. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006254 · Cited by 156
Verwilst, P., Kim, H. R., Seo, J., Sohn, N., Cha, S.-Y., Kim, Y., Maeng, S., Shin, J. W., Kwak, J. H., Kang, C., et al. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b05878 · Cited by 149
Pathogenic Tau Impairs Axon Initial Segment Plasticity and Excitability Homeostasis
Sohn, P. D., Huang, C. T.-L., Yan, R., Fan, L., Tracy, T. E., Camargo, C. M., Montgomery, K. M., Arhar, T., Mok, S.-A., Freilich, R., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.08.008 · Cited by 148
“However, the lack of microtubule perturbation and detrimental effects by tau reduction (Morris et al., 2011; Roberson et al., 2007) raised doubts about the essential role of microtubule destabilization in tau-dependent pathogenesis.”
BackgroundTau-mediated synaptic and neuronal dysfunction in neurodegenerative disease
Tracy, T. E., & Gan, L. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.04.027 · Cited by 155
Evans, C. E., Miners, J. S., Piva, G., Willis, C. L., Heard, D. M., Kidd, E. J., Good, M. A., & Kehoe, P. G. (2020) · Acta Neuropathologica · doi:10.1007/s00401-019-02098-6 · Cited by 145
Hyperphosphorylation and Cleavage at D421 Enhance Tau Secretion
Plouffe, V., Mohamed, N., Rivest‐McGraw, J., Bertrand, J., Lauzon, M., & Leclerc, N. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036873 · Cited by 159
Tau protein is essential for stress-induced brain pathology
Lopes, S., Vaz‐Silva, J., Pinto, V., Dalla, C., Kokras, N., Bedenk, B. T., Mack, N., Czisch, M., Almeida, O. F. X., Sousa, N., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1600953113 · Cited by 147
Metadata
- Authors
- Morris, M., Maeda, S., Vossel, K., & Mucke, L.
- Affiliations
- Gladstone Institutes (US)
- Corresponding author
- Mucke, Lennart
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2011-05
- Volume
- 70
- Issue
- 3
- Pages
- 410-426
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC3319390
- OpenAlex
- W2125985978
- Cited by
- 899
- References
- 196
- Citations by year
- 2026: 29 · 2025: 33 · 2024: 36 · 2023: 52 · 2022: 59 · 2021: 65 · 2020: 59 · 2019: 59 · 2018: 72 · 2017: 65 · 2016: 67 · 2015: 70 · 2014: 67 · 2013: 80 · 2012: 59
- FWCI
- 7.63
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 808 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (AG011385, NS041787)
- Tau Consortium
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- tau protein, microtubule binding, cytoskeletal organization, signaling, neurodegenerative diseases, tauopathy
- MeSH terms
- Animals, Humans, Microtubules, Models, Biological, Signal Transduction, tau Proteins, Neurodegenerative Diseases
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