Cited by 2,174Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders

Ballatore, Carlo, Lee, Virginia M.-Y., Trojanowski, John Q.·2007·Nature Reviews Neuroscience

DOI 10.1038/nrn2194

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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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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-citation
Tau protein isoforms, phosphorylation and role in neurodegenerative disorders11These authors contributed equally to this work.
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 2,142
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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
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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
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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

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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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Function and regulation of tau conformations in the development and treatment of traumatic brain injury and neurodegeneration
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Correction of tau mis-splicing caused by FTDP-17 MAPT mutations by spliceosome-mediated RNA trans-splicing
Rodríguez-Martín, T., Anthony, K., García-Blanco, M. A., Mansfield, S. G., Anderton, B. H., & Gallo, J. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp264 · Cited by 57
Neurosentimentalism and Moral Agency
Gerrans, P., & Kennett, J. (2010) · Mind · doi:10.1093/mind/fzq037 · Cited by 56
Structure−Activity Relationship of Cyanine Tau Aggregation Inhibitors
Chang, E. S., Congdon, E. E., Honson, N. S., Duff, K., & Kuret, J. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900116d · Cited by 56
Heat shock protein 90: translation from cancer to Alzheimer's disease treatment?
Luo, W., Rodina, A., & Chiosis, G. (2008) · BMC Neuroscience · doi:10.1186/1471-2202-9-s2-s7 · Cited by 56
Enhancing CNS Repair in Neurological Disease
Xu, X., Warrington, A. E., Bieber, A. J., & Rodriguez, M. (2011) · CNS Drugs · doi:10.2165/11587830-000000000-00000 · Cited by 59
Lipid membrane templated misfolding and self-assembly of intrinsically disordered tau protein
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Control of HIF-1α Expression by eIF2α Phosphorylation–Mediated Translational Repression
Zhu, K., Chan, W., Heymach, J., Wilkinson, M., & McConkey, D. J. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4103 · Cited by 55
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Li, D., Li, Y., Li, Y., Zhu, X., Du, X., Zhou, M., Li, W., & Deng, H. (2018) · Chinese Medical Journal · doi:10.4103/0366-6999.240817 · Cited by 55
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Nam, H. (2015) · World Journal of Stem Cells · doi:10.4252/wjsc.v7.i1.126 · Cited by 59
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Crosstalk between Endoplasmic Reticulum Stress and Protein Misfolding in Neurodegenerative Diseases
Pereira, C. (2013) · ISRN Cell Biology · doi:10.1155/2013/256404 · Cited by 56
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Learning and memory deficits and alzheimer's disease-like changes in mice after chronic exposure to microcystin-LR
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P44, the ‘longevity‐assurance’ isoform of P53, regulates tau phosphorylation and is activated in an age‐dependent fashion
Pehar, M., Ko, M. H., Li, M., Scrable, H. J., & Puglielli, L. (2013) · Aging Cell · doi:10.1111/acel.12192 · Cited by 57
Molecular Pathogenesis of Alzheimer’s Disease: Reductionist versus Expansionist Approaches
Castellani, R. J., Zhu, X., Lee, H., Smith, M. A., & Perry, G. L. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10031386 · Cited by 57
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Attenuation of β‐amyloid‐induced tauopathy via activation of CK2α/SIRT1: Targeting for cilostazol
Lee, H. R., Shin, H. K., Park, S. Y., Kim, H. Y., Lee, W. S., Rhim, B. Y., Hong, K. W., & Kim, C. D. (2013) · Journal of Neuroscience Research · doi:10.1002/jnr.23310 · Cited by 53

Authors: Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q.
Affiliations: University of Pennsylvania (US)
Corresponding author: Trojanowski, John Q.
ORCID: Ballatore, Carlo
Lee, Virginia M.-Y.
Trojanowski, John Q.
Venue: Nature Reviews Neuroscience
Publisher: Springer Science and Business Media LLC
Published: 2007-09
Volume: 8
Issue: 9
Pages: 663-672
ISSN: 1471-003X (ISSN-L)
1471-0048
DOI: 10.1038/nrn2194
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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Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders

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