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Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders
Abstract
Advances in our understanding of the mechanisms of tau-mediated neurodegeneration in Alzheimer's disease (AD) and related tauopathies, which are characterized by prominent CNS accumulations of fibrillar tau inclusions, are rapidly moving this previously underexplored disease pathway to centre stage for disease-modifying drug discovery efforts. However, controversies abound concerning whether or not the deleterious effects of tau pathologies result from toxic gains-of-function by pathological tau or from critical losses of normal tau function in the disease state. This Review summarizes the most recent advances in our knowledge of the mechanisms of tau-mediated neurodegeneration to forge an integrated concept of those tau-linked disease processes that drive the onset and progression of AD and related tauopathies.
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“WPC2 also contains numerous cytoskeletal proteins, as exemplified by tau that is hyperphosphorylated and aggregated to contribute to neurodegeneration (Ballatore et al., 2007).”
From Deep Multilayer Brain Proteomics Identifies Molecular Networks in Alzheimer’s Disease Progression (2020) · cites this paper as Ballatore et al., 2007
In the citing paper
“The most widely used transgenic models express mutant forms of the amyloid precursor protein (APP) gene, with or without presenilin-1/2 (PSEN1/2), which are associated with autosomal-dominant, early-onset AD, or, alternatively, MAPT mutations, which cause familial frontotemporal dementia (FTD).”
From Meta-Analysis of the Alzheimer’s Disease Human Brain Transcriptome and Functional Dissection in Mouse Models (2020) · cites this paper as Ballatore et al., 2007
In the citing paper
“These models recapitulate features of AD neuropathology, including plaques or tangles, along with variable degree of neuronal dysfunction or loss and progressive behavioral impairment (Ballatore et al., 2007; Esquerda-Canals et al., 2017).”
From Meta-Analysis of the Alzheimer’s Disease Human Brain Transcriptome and Functional Dissection in Mouse Models (2020) · cites this paper as Ballatore et al., 2007
In the citing paper
“Together, these studies indicate that chronic neuroinflammation could provoke tau pathology thereby worsening neuronal injury and long-term outcome.”
From The Inflammatory Continuum of Traumatic Brain Injury and Alzheimer’s Disease (2018) · cites this paper as [150]
In the citing paper
“A robust and persistent neuroinflammatory response may then be sufficient to promote phosphorylation, aggregation, and subsequent neurodegeneration; key features of AD (149–151).”
From The Inflammatory Continuum of Traumatic Brain Injury and Alzheimer’s Disease (2018) · cites this paper as [150]
Citations
Cites
Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126
Protein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454
The blood-brain barrier: Bottleneck in brain drug development
Pardridge, W. M. (2005) · NeuroRX · doi:10.1602/neurorx.2.1.3 · Cited by 2,798
Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.3.631 · Cited by 2,668
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
Self-citationBuée, 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 2,142
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
Oxidative stress in neurodegeneration: Cause or consequence?
Andersen, J. K. (2004) · Nature Medicine · doi:10.1038/nrn1434 · Cited by 1,869
The distribution of tau in the mammalian central nervous system.
Binder, L. I., Frankfurter, A., & Rebhun, L. I. (1985) · The Journal of cell biology · doi:10.1083/jcb.101.4.1371 · Cited by 1,588
Research works printed but not linked: 1
- Mailliot, C., Trojanowski, J. Q. & Lee, V. M. Impaired tau protein function following nitration-induced oxidative stress in vitro and in vivo. Neurobiol. Aging 23 (Suppl. 1), 415 (2002).
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Items 401–500 of 1,014
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Nam, E., Lee, Y., Moon, C., & Chang, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21145007 · Cited by 97
Aggregation of Disordered Proteins Associated with Neurodegeneration
Tsoi, P. S., Quan, M. D., Ferreon, J. C., & Ferreon, A. C. M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043380 · Cited by 103
Phospholipase D in brain function and Alzheimer's disease
Oliveira, T. G., & Paolo, G. D. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2010.04.004 · Cited by 99
Bibow, S., Ozenne, V., Biernat, J., Blackledge, M. J., Mandelkow�, E., & Zweckstetter, M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja205836j · Cited by 103
The Role of Tau in Neurodegenerative Diseases and Its Potential as a Therapeutic Target
Wolfe, M. S. (2012) · Scientifica · doi:10.6064/2012/796024 · Cited by 105
McAteer, K. M., Corrigan, F., Thornton, E., Turner, R. J., & Vink, R. (2016) · PLoS ONE · doi:10.1371/journal.pone.0160220 · Cited by 100
The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants
Kesten, C., Wallmann, A., Schneider, R., McFarlane, H. E., Diehl, A., Khan, G. A., van Rossum, B., Lampugnani, E. R., Szymanski, W. G., Cremer, N., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-08780-3 · Cited by 97
Arora, J., Hu, Y., Esfandiary, R., Sathish, H. A., Bishop, S. M., Joshi, S. B., Middaugh, C. R., Volkin, D. B., & Weis, D. D. (2016) · mAbs · doi:10.1080/19420862.2016.1222342 · Cited by 100
Small heat shock proteins in neurodegenerative diseases
Vendredy, L., Adriaenssens, E., & Timmerman, V. (2020) · Cell Stress and Chaperones · doi:10.1007/s12192-020-01101-4 · Cited by 99
Gene therapy in Alzheimer’s disease – potential for disease modification
Nilsson, P., Iwata, N., Muramatsu, S., Tjernberg, L. O., Winblad, B. G., & Saido, T. C. (2010) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2010.01038.x · Cited by 98
Iijima, K., Gatt, A., & Iijima-Ando, K. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq200 · Cited by 96
Advances in Alzheimer’s Disease Drug Development
Rafii, M. S., & Aisen, P. S. S. (2015) · BMC Medicine · doi:10.1186/s12916-015-0297-4 · Cited by 98
Torres, L., Robinson, S.-A., Kim, D.-G., Yan, A., Cleland, T. A., & Bynoe, M. S. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1086-8 · Cited by 97
Sun, Y., Wang, Y., Chen, S., Chen, Y., Shen, J., Yao, W., Gao, X., & Chen, S. (2020) · Theranostics · doi:10.7150/thno.44370 · Cited by 95
Collins-Praino, L. E., & Corrigan, F. (2017) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2016.09.027 · Cited by 95
Microtubule-stabilizing agents as potential therapeutics for neurodegenerative disease
Brunden, K. R., Trojanowski, J. Q., Smith, A. B., Lee, V. M. ‐., & Ballatore, C. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.12.046 · Cited by 97
Self-citationThe Dynamic Structure of Filamentous Tau
Bibow, S., Mukrasch, M. D., Chinnathambi, S., Biernat, J., Griesinger, C., Mandelkow�, E., & Zweckstetter, M. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201105493 · Cited by 99
Gibbons, G. S., Banks, R. A., Kim, B., Changolkar, L., Riddle, D. M., Leight, S. N., Irwin, D. J., Trojanowski, J. Q., & Lee, V. M. Y. (2018) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nly010 · Cited by 94
Self-citationBrunden, K. R., Ballatore, C., Crowe, A., Smith, Lee, V. M.-Y., & Trojanowski, J. Q. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2009.08.031 · Cited by 93
Self-citationLou, K., Yao, Y., Hoye, A. T., James, M. J., Cornec, A., Hyde, E. G., Gay, B. C., Lee, V. M. ‐., Trojanowski, J. Q., Smith, A. B., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm5005623 · Cited by 93
Self-citationA functional role for intrinsic disorder in the tau-tubulin complex
Melo, A. M., Coraor, J., Cobb, G., Elbaum‐Garfinkle, S., Nath, A., & Rhoades, E. R. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610137113 · Cited by 97
Du, F., Yu, Q., Kanaan, N. M., & Yan, S. S. (2022) · Human Molecular Genetics · doi:10.1093/hmg/ddab363 · Cited by 93
Selecting a Mouse Model of Alzheimer’s Disease
Chin, J. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-744-0_13 · Cited by 98
Chronic exercise ameliorates the neuroinflammation in mice carrying NSE/htau23
Leem, Y., Lee, Y.-I., Son, H.-J., & Lee, S. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.02.046 · Cited by 93
Nguyen, T. V., Shen, L., Griend, L. V., Quach, L. N., Belichenko, N. P., Saw, N. L., Yang, T., Shamloo, M., Wyss‐Coray, T., Massa, S. M., et al. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140036 · Cited by 93
Murugan, N. A., Nordberg, A., & Ågren, H. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00093 · Cited by 92
Liu, C., Sawaya, M. R., Cheng, P.-N., Zheng, J., Nowick, J. S., & Eisenberg, D. S. (2011) · Journal of the American Chemical Society · doi:10.1021/ja200222n · Cited by 98
p73 Regulates Neurodegeneration and Phospho-Tau Accumulation during Aging and Alzheimer's Disease
Wetzel, M. K., Naska, S., Laliberté, C. L., Rymar, V. V., Fujitani, M., Biernaskie, J., Cole, C. J., Lerch, J. P., Spring, S., Wang, S., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.07.021 · Cited by 97
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Medina, M., Hernández, F., & Ávila, J. (2016) · Biomolecules · doi:10.3390/biom6020021 · Cited by 103
Tau mis-splicing in the pathogenesis of neurodegenerative disorders
Park, S. A., Ahn, S. I., & Gallo, J. (2016) · BMB Reports · doi:10.5483/bmbrep.2016.49.8.084 · Cited by 100
Dasari, A. K. R., Kayed, R., Wi, S., & Lim, K. H. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00215 · Cited by 92
Khezri, M. R., Yousefi, K., Esmaeili, A., & Ghasemnejad‐Berenji, M. (2022) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-022-01191-x · Cited by 93
Effects of pH alterations on stress- and aging-induced protein phase separation
Jin, X., Zhou, M., Chen, S., Li, D., Cao, X., & Liu, B. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04393-0 · Cited by 94
Tran, H., Sanchez, L., & Brody, D. L. (2012) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182456aed · Cited by 93
Kuo, Y., & Tsao, C.-W. (2017) · International Journal of Nanomedicine · doi:10.2147/ijn.s132472 · Cited by 92
Kavungal, D., Magalhães, P., Kumar, S. T., Rajasekhar, K., Lashuel, H. A., & Altug, H. (2023) · Science Advances · doi:10.1126/sciadv.adg9644 · Cited by 95
Lonskaya, I., Shekoyan, A. R., Hebron, M. L., Desforges, N. M., Algarzae, N. K., & Moussa, C. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121141 · Cited by 93
Tau downregulates BDNF expression in animal and cellular models of Alzheimer's disease
Rosa, E., Mahendram, S., Ke, Y. D., Ittner, L. M., Ginsberg, S. D., & Fahnestock, M. L. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.08.020 · Cited by 92
Bundy, J. L., Vied, C., Badger, C., & Nowakowski, R. S. (2019) · Journal of Comparative Neurology · doi:10.1002/cne.24551 · Cited by 90
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Donnelly, M. P., Paschou, P., Grigorenko, E. L., Gurwitz, D., Mehdi, S. Q., Kajuna, S. L. B., Barta, C., Kungulilo, S., Karoma, N. J., Lu, R., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.01.007 · Cited by 91
Dissociable influences of APOE ε4 and polygenic risk of AD dementia on amyloid and cognition
Ge, T., Sabuncu, M. R., Smoller, J. W., Sperling, R. A., Mormino, E. C., & Initiative, A. D. N. (2018) · Neurology · doi:10.1212/wnl.0000000000005415 · Cited by 94
Crist, A. M., Hinkle, K. M., Wang, X., Moloney, C. M., Matchett, B. J., Labuzan, S. A., Frankenhauser, I., Azu, N. O., Liesinger, A. M., Lesser, E. R., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22399-3 · Cited by 93
Cornejo, A., Jiménez, J. M., Caballero, L., Melo, F., & Maccioni, R. B. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110623 · Cited by 89
Kwan, A. C., Duff, K., Gouras, G. K., & Webb, W. W. (2009) · Optics Express · doi:10.1364/oe.17.003679 · Cited by 90
Okadaic acid-induced Tau phosphorylation in rat brain: Role of NMDA receptor
Kamat, P., Rai, S., Swarnkar, S., Shukla, R., Ali, S., Najmi, A. K., & Nath, C. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.01.075 · Cited by 89
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van der Harg, J. M., Nölle, A., Zwart, R., Boerema, A. S., van Haastert, E. S., Strijkstra, A. M., Hoozemans, J. J. M., & Scheper, W. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.354 · Cited by 92
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The Parkinson Study Group DATATOP Investigators, Zhang, J., Mattison, H. A., Liu, C., Ginghină, C., Auinger, P., McDermott, M., Stewart, T., Kang, U. J., Cain, K. C., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1121-x · Cited by 90
HDAC6 mutations rescue human tau-induced microtubule defects in Drosophila
Xiong, Y., Zhao, K., Wu, J., Xu, Z., Jin, S., & Zhang, Y. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1207586110 · Cited by 90
Identifying dysfunctional crosstalk of pathways in various regions of Alzheimer's disease brains
Liu, Z.-P., Wang, Y., Zhang, X.-S., & Chen, L. (2010) · BMC Systems Biology · doi:10.1186/1752-0509-4-s2-s11 · Cited by 88
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Zhang, P.-L., Chen, Y., Zhang, C.-H., Wang, Y., & Fernández-Fúnez, P. (2017) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2017-105047 · Cited by 93
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Tau-induced neurodegeneration: mechanisms and targets
Beharry, C., Cohen, L. S., Di, J., Ibrahim, K., Briffa-Mirabella, S., & Alonso, A. D. C. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1414-z · Cited by 92
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Correia, S. C., Perry, G. L., & Moreira, P. I. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.07.010 · Cited by 92
Importance of Functional Loss of FUS in FTLD/ALS
Ishigaki, S., & Sobue, G. (2018) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2018.00044 · Cited by 97
Residue-specific identification of phase separation hot spots of Alzheimer's-related protein tau
Ambadipudi, S., Reddy, J. G., Biernat, J., Mandelkow�, E., & Zweckstetter, M. (2019) · Chemical Science · doi:10.1039/c9sc00531e · Cited by 88
Cornejo, A., Sandoval, F. A. A., Caballero, L., Machuca, L., Muñoz, P., Caballero, J., Perry, G. L., Ardiles, A., Areche, C., & Melo, F. (2017) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2017.1347783 · Cited by 87
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Shi, J., Qian, W., Yin, X., Iqbal, K., Grundke, I., Gu, X., Ding, F., Gong, C., & Liu, F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.204453 · Cited by 87
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Friedman, L. G., Qureshi, Y. H., & Yu, W. H. (2014) · Neurotherapeutics · doi:10.1007/s13311-014-0320-z · Cited by 89
Platelets, a reliable source for peripheral Alzheimer’s disease biomarkers?
Veitinger, M., Varga, B., Guterres, S. B., & Zellner, M. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-65 · Cited by 88
Vinepinsky, E., Cohen, L., Perchik, S., Ben-Shahar, O., Donchin, O., & Segev, R. (2020) · Scientific Reports · doi:10.1038/s41598-020-71217-1 · Cited by 87
Using Human iPSC-Derived Neurons to Model TAU Aggregation
Verheyen, A., Diels, A., Dijkmans, J., Oyelami, T., Meneghello, G., Mertens, L., Versweyveld, S., Borgers, M., Buist, A., Peeters, P., et al. (2015) · PLOS ONE · doi:10.1371/journal.pone.0146127 · Cited by 86
Al‐Hilaly, Y. K., Foster, B. E., Biasetti, L., Lutter, L., Pollack, S. J., Rickard, J. E., Storey, J. M. D., Harrington, C. R., Xue, W., Wischik, C. M., et al. (2019) · FEBS Letters · doi:10.1002/1873-3468.13675 · Cited by 86
Wren, M. C., Zhao, J., Liu, C., Murray, M. E., Atagi, Y., Davis, M. D., Fu, Y., Okano, H. J., Ogaki, K., Strongosky, A. J., et al. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0042-7 · Cited by 86
Kumar, S., Tepper, K., Kaniyappan, S., Biernat, J., Wegmann, S., Mandelkow, E., Müller, D. J., & Mandelkow�, E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.554725 · Cited by 88
Review: Modulating the unfolded protein response to prevent neurodegeneration and enhance memory
Halliday, M., & Mallucci, G. R. (2014) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12211 · Cited by 85
Gu, J., Chen, F., Iqbal, K., Gong, C., Wang, X., & Liu, F. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.783498 · Cited by 88
Combating deleterious phase transitions in neurodegenerative disease
Darling, A. L., & Shorter, J. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.118984 · Cited by 88
Yu, C.-H., Song, G. S., Yhee, J. Y., Kim, J. H., Im, K.-S., Nho, W.-G., Lee, J. H., & Sur, J. (2011) · Journal of Comparative Pathology · doi:10.1016/j.jcpa.2010.11.004 · Cited by 92
Neuropathogenic role of adenylate kinase-1 in Aβ-mediated tau phosphorylation via AMPK and GSK3β
Park, H., Kam, T., Kim, Y., Choi, H., Gwon, Y., Kim, C., Koh, J., & Jung, Y. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds100 · Cited by 89
Ruiz, E., Decrop, D., Ven, K., Tripodi, L., Leirs, K., Rosseels, J., de Wouwer, M. V., Geukens, N., Vos, A. D., Vanmechelen, E., et al. (2018) · Analytica Chimica Acta · doi:10.1016/j.aca.2018.02.011 · Cited by 85
Stabilizing the Hsp70-Tau Complex Promotes Turnover in Models of Tauopathy
Young, Z. T., Rauch, J. N., Assimon, V. A., Jinwal, U. K., Ahn, M., Li, X., Dunyak, B. M., Ahmad, A., Carlson, G. A., Srinivasan, S. R., et al. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.04.014 · Cited by 85
Usui, K., Hulleman, J. D., Paulsson, J. F., Siegel, S. J., Powers, E. T., & Kelly, J. W. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804758106 · Cited by 84
Adak, A., Das, G., Barman, S., Mohapatra, S., Bhunia, D., Jana, B., & Ghosh, S. (2017) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6b12114 · Cited by 84
Wang, X., Li, W., Marcus, J., Pearson, M. S., Song, L., Smith, K. D. B., Terracina, G., Lee, J. A., Hong, K.-L. K., Lu, S. X., et al. (2020) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.120.266122 · Cited by 85
Recent Advances in the Study of Bipolar/Rod-Shaped Microglia and their Roles in Neurodegeneration
Au, N. P. B., & Ma, C. H. E. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00128 · Cited by 87
Neuropathological assessment of the Alzheimer spectrum
Jellinger, K. A. (2020) · Journal of Neural Transmission · doi:10.1007/s00702-020-02232-9 · Cited by 85
SUMO and Its Role in Human Diseases
Sarge, K. D., & Park-Sarge, O.-K. (2011) · International review of cytology · doi:10.1016/b978-0-12-386041-5.00004-2 · Cited by 82
Begcevic, I., Brinc, D., Brown, M., Martinez-Morillo, E., Goldhardt, O., Grimmer, T., Magdolen, V., Batruch, I., & Diamandis, E. P. (2018) · Journal of Proteomics · doi:10.1016/j.jprot.2018.04.027 · Cited by 81
The Complex Role of Apolipoprotein E in Alzheimer’s Disease: an Overview and Update
Mahoney‐Sanchez, L., Belaidi, A. A., Bush, A. I., & Ayton, S. (2016) · Journal of Molecular Neuroscience · doi:10.1007/s12031-016-0839-z · Cited by 84
Lambeth, T. R., Riggs, D. L., Talbert, L. E., Tang, J. Y., Coburn, E., Kang, A. S., Noll, J. M., Augello, C. J., Ford, B. D., & Julian, R. R. (2019) · ACS Central Science · doi:10.1021/acscentsci.9b00369 · Cited by 82
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
Hu, J.-Y., Zhang, D.-L., Liu, X., Li, X.-S., Cheng, X., Chen, J., Du, H., & Liang, Y. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.022 · Cited by 81
Insights into brain microstructure from in vivo DW-MRS
Palombo, M., Shemesh, N., Ronen, I., & Valette, J. (2017) · NeuroImage · doi:10.1016/j.neuroimage.2017.11.028 · Cited by 81
Héraud, C., Goufak, D., Ando, K., Leroy, K., Suain, V., Yilmaz, Z., De Decker, R., Authelet, M., Laporte, V., Octave, J.-N., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.09.010 · Cited by 80
Xiong, R., Wang, X., Wu, J., Tang, Y., Qiu, W., Shen, X., Teng, J., Pan, R., Zhao, Y., Yu, L., et al. (2020) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.112548 · Cited by 81
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Ghimire, S., Subedi, L., Acharya, N., & Gaire, B. P. (2021) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c04581 · Cited by 80
Reifert, J. R., Hartung-Cranston, D., & Feinstein, S. C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.234674 · Cited by 83
Dammer, E. B., Lee, A. K., Duong, D. M., Gearing, M., Lah, J. J., Levey, A. I., & Seyfried, N. T. (2014) · PROTEOMICS · doi:10.1002/pmic.201400189 · Cited by 80
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Guo, J., Buist, A., Soares, A. C., Callaerts, K., Calafate, S., Stevenaert, F., Daniels, J. P., Zoll, B. E., Crowe, A., Brunden, K. R., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.712083 · Cited by 83
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Huan, T., Tran, T., Zheng, J., Sapkota, S., MacDonald, S. W. S., Camicioli, R. M., Dixon, R. A., & Li, L. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180711 · Cited by 81
Wu, X., Piña-Crespo, J., Zhang, Y., Chen, X., & Xu, H. (2017) · Chinese Medical Journal · doi:10.4103/0366-6999.220313 · Cited by 82
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Chen, L., Wei, Z., Chan, K. W. Y., Cai, S., Liu, G., Lu, H., Wong, P. C., van Zijl, P. C. M., Li, T., & Xu, J. (2018) · NeuroImage · doi:10.1016/j.neuroimage.2018.12.018 · Cited by 79
Li, X., Yu, Y., & Tu, Z. (2021) · Molecules · doi:10.3390/molecules26051202 · Cited by 80
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Portelius, E., Hansson, S., Tran, A. J., Zetterberg, H., Grognet, P., Vanmechelen, E., Höglund, K., Brinkmalm, G., Brinkmalm, A., Nordhoff, E., et al. (2008) · Journal of Proteome Research · doi:10.1021/pr7008669 · Cited by 79
Chang, C., Chen, S.-M., Lu, H.-E., Lai, S.-M., Lai, P., Shen, P.-W., Chen, P.-Y., Shen, C.-I., Harn, H., Lin, S., et al. (2015) · Scientific Reports · doi:10.1038/srep08744 · Cited by 79
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Götz, J., Gladbach, A., Pennanen, L., van Eersel, J., Schild, A., David, D. C., & Ittner, L. M. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.008 · Cited by 82
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Liu, X., Zhao, X., Zeng, X., Bossers, K., Swaab, D. F., Zhao, J., & Pei, G. (2012) · Cell Research · doi:10.1038/cr.2012.167 · Cited by 81
Dütting, S., Brachs, S., & Mielenz, D. (2011) · Cell Communication and Signaling · doi:10.1186/1478-811x-9-2 · Cited by 80
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Zhang, Z., & Simpkins, J. W. (2010) · Brain Research · doi:10.1016/j.brainres.2010.04.074 · Cited by 81
Metadata
- Authors
- Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q.
- Affiliations
- University of Pennsylvania (US)
- Corresponding author
- Trojanowski, John Q.
- Venue
- Nature Reviews Neuroscience
- Published
- 2007-09
- Volume
- 8
- Issue
- 9
- Pages
- 663-672
- ISSN
- 1471-003X (ISSN-L)
- 1471-0048
- OpenAlex
- W2034286717
- Cited by
- 2,174
- References
- 105
- Citations by year
- 2026: 70 · 2025: 94 · 2024: 113 · 2023: 108 · 2022: 129 · 2021: 117 · 2020: 161 · 2019: 138 · 2018: 135 · 2017: 139 · 2016: 137 · 2015: 117 · 2014: 123 · 2013: 102 · 2012: 104
- FWCI
- 9.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature reviews. Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute for Health and Care Research
- National Institutes of Health (5u01ag024904-10)
- National Institute on Aging (P01AG014382, P01AG011542, P01AG014449, U01AG24904, P30AG010124, P01AG009215, P01AG017586, P01AG019724)
- National Institute of Neurological Disorders and Stroke (P01NS044233)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau protein, Alzheimer's disease, tauopathy, neurofibrillary tangles, tau hyperphosphorylation, pathological tau
- MeSH terms
- Alzheimer Disease, Animals, Humans, Models, Biological, Nerve Degeneration, tau Proteins, Tauopathies
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