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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]
In the citing paper
“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
Cited by
Sorted by citations
Items 201–300 of 900
Kondadi, A. K., Wang, S., Montagner, S., Kladt, N., Korwitz, A., Martinelli, P., Herholz, D., Baker, M. J., Schauss, A. C., Langer, T., et al. (2014) · The EMBO Journal · doi:10.1002/embj.201387009 · Cited by 83
Shekhar, S., Kumar, R. K., Rai, N., Kumar, V. L., Singh, K. K., Upadhyay, A. D., Tripathi, M., Dwivedi, S. N., Dey, A. B., & Dey, S. (2016) · PLoS ONE · doi:10.1371/journal.pone.0159099 · Cited by 80
Shimojo, M., Takuwa, H., Takado, Y., Tokunaga, M., Tsukamoto, S., Minatohara, K., Ono, M., Seki, C., Maeda, J., Urushihata, T., et al. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.2880-19.2020 · Cited by 81
Mueller, R. L., Combs, B., Alhadidy, M. M., Brady, S. T., Morfini, G. A., & Kanaan, N. M. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.647054 · Cited by 81
Mechanical Effects of Dynamic Binding between Tau Proteins on Microtubules during Axonal Injury
Ahmadzadeh, H., Smith, D. H., & Shenoy, V. B. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.09.010 · Cited by 78
Swanson, E., Breckenridge, L., McMahon, L. P., Som, S., McConnell, I., & Bloom, G. S. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170168 · Cited by 76
Links among glaucoma, neurodegenerative, and vascular diseases of the central nervous system
Nucci, C., Martucci, A., Cesareo, M., Garaci, F. G., Morrone, L. A., Russo, R., Corasaniti, M. T., Bagetta, G., & Mancino, R. (2015) · Progress in brain research · doi:10.1016/bs.pbr.2015.04.010 · Cited by 78
An evolutionary roadmap to the microtubule-associated protein MAP Tau
Sündermann, F., Fernández, M. P., & Morgan, R. O. (2016) · BMC Genomics · doi:10.1186/s12864-016-2590-9 · Cited by 79
α-Linolenic acid inhibits Tau aggregation and modulates Tau conformation
Desale, S. E., Dubey, T., & Chinnathambi, S. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.10.226 · Cited by 77
Arendt, T., & Bullmann, T. (2013) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00117.2013 · Cited by 77
Tau mutants bind tubulin heterodimers with enhanced affinity
Elbaum‐Garfinkle, S., Cobb, G., Compton, J. T., Li, X., & Rhoades, E. R. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315983111 · Cited by 76
Sontag, J., Nunbhakdi‐Craig, V., White, C. L., Halpain, S., & Sontag, E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.338681 · Cited by 79
In search of antiepileptogenic treatments for post-traumatic epilepsy
Saletti, P. G., Ali, I. Y., Casillas-Espinosa, P. M., Semple, B. D., Lisgaras, C. P., Moshé, S. L., & Galanopoulou, A. S. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.06.017 · Cited by 75
Zhang, S., Zhu, Q., Chen, J.-Y., OuYang, D., & Lu, J.-H. (2020) · Phytomedicine · doi:10.1016/j.phymed.2020.153316 · Cited by 74
A Novel Mechanism of Spine Damages in Stroke via DAPK1 and Tau
Pei, L., Wang, S., Jin, H., Bi, L., Wei, N., Yan, H., Yang, X., Yao, C., Xu, M., Shu, S., et al. (2015) · Cerebral Cortex · doi:10.1093/cercor/bhv096 · Cited by 74
Restricting HIV the SAMHD1 way: through nucleotide starvation
Ayinde, D., Casartelli, N., & Schwartz, O. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2862 · Cited by 73
Giustiniani, J., Chambraud, B., Sardin, E., Dounane, O., Guillemeau, K., Nakatani, H., Paquet, D., Kamah, A., Landrieu, I., Lippens, G. M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402645111 · Cited by 72
Anti-Tau Trials for Alzheimer's Disease: A Report from the EU/US/CTAD Task Force
Cummings, J. L., Blennow, K., Johnson, K. A., Keeley, M. B., Bateman, R. J., Molinuevo, J. L., Touchon, J., Aisen, P. S. S., & Vellas, B. J. (2019) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2019.14 · Cited by 72
Melchior, B., Mittapalli, G. K., Lai, C., Duong‐Polk, K., Stewart, J., Güner, B., Hofilena, B. J., Tjitro, A., Anderson, S., Herman, D. S., et al. (2019) · Aging Cell · doi:10.1111/acel.13000 · Cited by 73
Phage display derived peptides for Alzheimer's disease therapy and diagnosis
Zhang, X., Zhang, X., Gao, H., & Qing, G. (2022) · Theranostics · doi:10.7150/thno.68636 · Cited by 75
Membrane trafficking in neuronal maintenance and degeneration
Wang, D., Chan, C., Cherry, S., & Hiesinger, P. R. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1201-4 · Cited by 74
Microtubule dynamics in axon guidance
Liu, G., & Dwyer, T. A. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-014-1444-6 · Cited by 73
Hochgräfe, K., Sydow, A., & Mandelkow, E. (2013) · FEBS Journal · doi:10.1111/febs.12250 · Cited by 78
Guha, S. K., Johnson, G. V. W., & Nehrke, K. W. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02084-0 · Cited by 77
Ramser, E. M., Gan, K. J., Decker, H., Fan, E. Y., Suzuki, M. M., Ferreira, S. T., & Silverman, M. A. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-12-0858 · Cited by 74
Lee, I., Eriksson, P., Fredriksson, A., Buratovic, S., & Viberg, H. (2015) · Toxicology · doi:10.1016/j.tox.2015.06.010 · Cited by 75
Pathologies of axonal transport in neurodegenerative diseases
Liu, X.-A., Rizzo, V., & Puthanveettil, S. V. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0044-7 · Cited by 73
Woo, J. A., Boggess, T. C., Uhlar, C., Wang, X., Khan, H., Cappos, G., Joly‐Amado, A., Narvaez, E. D., Majid, S., Minamide, L. S., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.37 · Cited by 70
Linking pathways in the developing and aging brain with neurodegeneration
Kovács, G. G., Adle‐Biassette, H., Milenković, I., Cipriani, S., van Scheppingen, J., & Aronica, E. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.03.045 · Cited by 69
Physiological and Pathophysiological Implications of Synaptic Tau
Regan, P. L., Whitcomb, D. J., & Cho, K. (2016) · The Neuroscientist · doi:10.1177/1073858416633439 · Cited by 75
Interleukin-10 deficiency exacerbates inflammation-induced tau pathology
Weston, L. L., Jiang, S., Chisholm, D., Jantzie, L. L., & Bhaskar, K. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02211-1 · Cited by 69
Modeling the complex pathology of Alzheimer's disease in Drosophila
Fernandez-Funez, P., de Mena, L., & Rincon-Limas, D. E. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.05.013 · Cited by 69
MicroRNAs and the Regulation of Tau Metabolism
Hébert, S. S., Sergeant, N., & Buée, L. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/406561 · Cited by 72
Kulbe, J. R., & Hall, E. D. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.08.003 · Cited by 70
Xu, Y., Zhang, S., & Zheng, H. (2018) · Autophagy · doi:10.1080/15548627.2018.1532258 · Cited by 69
Tau-induced pathology in epilepsy and dementia: notions from patients and animal models.
Sánchez, M., García-Cabrero, A., Sánchez-Elexpuru, G., Burgos, D., & Serratosa, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19041092 · Cited by 68
Bassoon contributes to tau-seed propagation and neurotoxicity
Martinez, P., Patel, H., You, Y., Jury, N., Perkins, A., Lee-Gosselin, A., Taylor, X., You, Y., Viana Di Prisco, G., Huang, X., et al. (2022) · Nature Neuroscience · doi:10.1038/s41593-022-01191-6 · Cited by 68
McDonald, S. J., Shultz, S. R., & Agoston, D. V. (2021) · Journal of Neurotrauma · doi:10.1089/neu.2021.0011 · Cited by 70
Melatonin ameliorates tau-related pathology via the miR-504-3p and CDK5 axis in Alzheimer’s disease
Chen, D., Lan, G., Li, R., Mei, Y., Shui, X., Gu, X., Wang, L., Zhang, T., Gan, C., Xia, Y., et al. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00302-4 · Cited by 68
Cdk5 at crossroads of protein oligomerization in neurodegenerative diseases: facts and hypotheses
Wilkaniec, A., Czapski, G. A., & Adamczyk, A. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13365 · Cited by 69
Tan, X. L., Wright, D. K., Liu, S., Hovens, C. M., O'Brien, T. J., & Shultz, S. R. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.05.001 · Cited by 68
Activated cofilin exacerbates tau pathology by impairing tau-mediated microtubule dynamics
Woo, J. A., Liu, T., Fang, C. C., Cazzaro, S., Kee, T. R., LePochat, P., Yrigoin, K., Penn, C., Zhao, X., Wang, X., et al. (2019) · Communications Biology · doi:10.1038/s42003-019-0359-9 · Cited by 69
Lye, J. J., Latorre, E., Lee, B. P., Bandinelli, S., Holley, J. E., Gutowski, N. J., Ferrucci, L., & Harries, L. W. (2019) · GeroScience · doi:10.1007/s11357-019-00100-3 · Cited by 69
Ojeda-López, M. A., Needleman, D. J., Song, C., Ginsburg, A., Kohl, P. A., Li, Y., Miller, H. P., Wilson, L., Raviv, U., Choi, M. C., et al. (2014) · Nature Materials · doi:10.1038/nmat3858 · Cited by 67
Shukla, R., & Singh, T. R. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1571947 · Cited by 66
Mohammadzadeh, L., Abnous, K., Razavi, B. M., & Hosseinzadeh, H. (2019) · Nutritional Neuroscience · doi:10.1080/1028415x.2018.1492772 · Cited by 67
Lopes, S., Teplytska, L., Vaz-Silva, J., Dioli, C., Trindade, R., Morais, M., Webhofer, C., Maccarrone, G., Almeida, O. F. X., Turck, C. W., et al. (2016) · Cerebral Cortex · doi:10.1093/cercor/bhw057 · Cited by 66
Neuroepigenetic mechanisms in disease
Christopher, M. A., Kyle, S. M., & Katz, D. J. (2017) · Epigenetics & Chromatin · doi:10.1186/s13072-017-0150-4 · Cited by 69
Espíndola, S. L., Damianich, A., Alvarez, R. J., Sartor, M., Belforte, J. E., Ferrario, J. E., Gallo, J.-M., & Avale, M. E. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.03.079 · Cited by 65
Metformin prevents p-tau and amyloid plaque deposition and memory impairment in diabetic mice
Oliveira, W. H., Braga, C. F., Lós, D. B., Araújo, S. M. R., França, M. R., Duarte-Silva, E., Rodrigues, G. B., Rocha, S. W. S., & Peixoto, C. A. (2021) · Experimental Brain Research · doi:10.1007/s00221-021-06176-8 · Cited by 64
Alzheimer's Disease-Related Misfolded Proteins and Dysfunctional Organelles on Autophagy Menu
Correia, S. C., Resende, R., Moreira, P. I., & Pereira, C. (2015) · DNA and Cell Biology · doi:10.1089/dna.2014.2757 · Cited by 66
Protein Tau: Prime Cause of Synaptic and Neuronal Degeneration in Alzheimer's Disease
Crespo‐Biel, N., Theunis, C., & LEUVEN, F. V. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/251426 · Cited by 69
C-Glycosylflavones Alleviate Tau Phosphorylation and Amyloid Neurotoxicity through GSK3β Inhibition
Liang, Z., Zhang, B., Su, W., Williams, P. G., & Li, Q. X. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00059 · Cited by 65
Yang, J., Zhi, W., & Wang, L. (2024) · Molecules · doi:10.3390/molecules29122812 · Cited by 63
What is the pathological significance of tau oligomers?
Cowan, C. M., Quraishe, S., & Mudher, A. K. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120135 · Cited by 62
The dark sides of amyloid in Alzheimer's disease pathogenesis
Sorrentino, P., Iuliano, A., Polverino, A., Jacini, F., & Sorrentino, G. (2014) · FEBS Letters · doi:10.1016/j.febslet.2013.12.038 · Cited by 64
Zhao, Z., Li, P., Ye, S., Ning, Y., Wang, H., Peng, Y., Yang, N., Zhao, Y., Zhang, Z.-H., Chen, J., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-02505-6 · Cited by 66
Review: tauopathy in the retina and optic nerve: does it shadow pathological changes in the brain?
Ho, W.-L., Leung, Y., Tsang, A. W.-T., So, K., Chiu, K., & Chang, R. C. (2012) · Europe PMC (PubMed Central) · Cited by 62
Calpain Dysregulation in Alzheimer’s Disease
Ferreira, A. (2012) · ISRN Biochemistry · doi:10.5402/2012/728571 · Cited by 64
Crystal Structures of the S. cerevisiae Spt6 Core and C-Terminal Tandem SH2 Domain
Close, D. W., Johnson, S. J., Sdano, M. A., McDonald, S., Robinson, H. H., Formosa, T., & Hill, C. P. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.03.002 · Cited by 58
Role of the Lipid Membrane and Membrane Proteins in Tau Pathology
Bok, E., Leem, E., Lee, B.-R., Lee, J. M., Yoo, C. J., Lee, E. M., & Kim, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.653815 · Cited by 61
Impaired plasticity of cortical dendritic spines in P301S tau transgenic mice
Hoffmann, N. A., Dorostkar, M. M., Blumenstock, S., Goedert, M., & Herms, J. W. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-82 · Cited by 69
Tau neurotoxicity and rescue in animal models of human Tauopathies
Krüger, L., & Mandelkow, E. (2015) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2015.09.004 · Cited by 63
Cantrelle, F., Loyens, A., Trivelli, X., Reimann, O., Despres, C., Gandhi, N. S., Hackenberger, C. P. R., Landrieu, I., & Smet‐Nocca, C. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.661368 · Cited by 63
Tau and Membranes: Interactions That Promote Folding and Condensation
Sallaberry, C. A., Voss, B. J., Majewski, J. P., Biernat, J., Mandelkow�, E., Chi, E. Y., & Zanden, C. M. V. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.725241 · Cited by 64
Too close for comfort? Adult attachment and cuddling in romantic and parent–child relationships
Chopik, W. J., Edelstein, R. S., van Anders, S. M., Wardecker, B. M., Shipman, E. L., & Samples-Steele, C. R. (2014) · Personality and Individual Differences · doi:10.1016/j.paid.2014.05.035 · Cited by 61
Human tau expression reduces adult neurogenesis in a mouse model of tauopathy
Komuro, Y., Xu, G., Bhaskar, K., & Lamb, B. T. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.03.002 · Cited by 64
Trans-splicing correction of tau isoform imbalance in a mouse model of tau mis-splicing
Avale, M. E., Rodríguez-Martín, T., & Gallo, J. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt108 · Cited by 60
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Potts, L. F., Luzzio, F. A., Smith, S. C., Hetman, M., Champy, P., & Litvan, I. (2011) · NeuroToxicology · doi:10.1016/j.neuro.2011.10.009 · Cited by 61
Pir, G. J., Choudhary, B. C., Mandelkow�, E., & Mandelkow, E. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0096-1 · Cited by 65
Mishra, V., Karumuri, B. K., Gautier, N. M., Liu, R., Hutson, T. N., Vanhoof‐Villalba, S. L., VLACHOS, I. K., Iasemidis, L. D., & Glasscock, E. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx104 · Cited by 61
Cilento, E. M., Jin, L., Stewart, T., Shi, M., Sheng, L., & Zhang, J. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14635 · Cited by 60
Elevated MARK2-Dependent Phosphorylation of Tau in Alzheimer's Disease
Gu, G. J., Wu, D., Lund, H., Sunnemark, D., Kvist, A. J., Milner, R. D. B., Eckersley, S., Nilsson, L. N. G., Agerman, K., Landegren, U. D., et al. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121357 · Cited by 58
Protein with tau-like repeats regulates neuronal integrity and lifespan inC. elegans
Chew, Y. L., Fan, X., Götz, J., & Nicholas, H. (2013) · Journal of Cell Science · doi:10.1242/jcs.jcs124404 · Cited by 59
Lin, X., Duan, X., Jacobs, C. S., Ullmann, J. F. P., Chan, C.-Y., Chen, S., Cheng, S. H., Zhao, W.-N., Poduri, A., Wang, X., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07289-5 · Cited by 60
Amal, H., Gong, G., Gjoneska, E., Lewis, S. M., Wishnok, J. S., Tsai, L., & Tannenbaum, S. R. (2019) · Translational Psychiatry · doi:10.1038/s41398-019-0388-7 · Cited by 55
Rossi, G., & Tagliavini, F. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00192 · Cited by 62
Neurodegenerative pathways as targets for acquired epilepsy therapy development
Casillas-Espinosa, P. M., Ali, I. Y., & O'Brien, T. J. (2020) · Epilepsia Open · doi:10.1002/epi4.12386 · Cited by 59
Prokop, A., Beaven, R., Qu, Y., & Sánchez‐Soriano, N. (2013) · Journal of Cell Science · doi:10.1242/jcs.126912 · Cited by 58
Tau-dependent suppression of adult neurogenesis in the stressed hippocampus
Dioli, C., Patrício, P., Trindade, R., Pinto, L., Silva, J. M., Morais, M., Ferreiro, E. B., Borges, S., Mateus‐Pinheiro, A., Rodrigues, A. J., et al. (2017) · Molecular Psychiatry · doi:10.1038/mp.2017.103 · Cited by 59
Bernick, C. B., Zetterberg, H., Shan, G., Banks, S. J., & Blennow, K. (2018) · Journal of Neurotrauma · doi:10.1089/neu.2017.5553 · Cited by 57
Hsp90 Modulation for the Treatment of Alzheimer’s Disease
Zhao, H., Michaelis, M. L., & Blagg, B. S. J. (2012) · Advances in pharmacology · doi:10.1016/b978-0-12-394816-8.00001-5 · Cited by 59
Ramachandran, G., & Udgaonkar, J. B. (2013) · Biochemistry · doi:10.1021/bi400209z · Cited by 59
Dubal, D. B., Broestl, L., & Worden, K. (2012) · Biology of Sex Differences · doi:10.1186/2042-6410-3-24 · Cited by 62
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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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