Dendritic Tau in Alzheimer’s Disease

Ittner, Arne; Ittner, Lars M.

doi:10.1016/j.neuron.2018.06.003

Cited by 280Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroscience and Neuropharmacology Research

Dendritic Tau in Alzheimer’s Disease

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Ittner, Arne, Ittner, Lars M.·2018·Neuron

DOI 10.1016/j.neuron.2018.06.003

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Abstract

The microtubule-associated protein tau and amyloid-β (Aβ) are key players in Alzheimer's disease (AD). Aβ and tau are linked in a molecular pathway at the post-synapse with tau-dependent synaptic dysfunction being a major pathomechanism in AD. Recent work on site-specific modification of dendritic and more specifically post-synaptic tau has revealed new endogenous functions of tau that limits synaptic Aβ toxicity. Thus, molecular studies opened a new perspective on tau, placing it at the center of neurotoxic and neuroprotective signaling at the post-synapse. Here, we review recent advances on tau in the dendritic compartments, with implications for understanding and treatment of AD and related neurological conditions.

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Tau is significantly elevated in the cerebrospinal fluid of AD patients, and its increase is an early event before the onset of clinical signs.
“Indeed, evidence shows that tau is significantly elevated in the cerebrospinal fluid (CSF) of AD patients, and its increase is an early event before the onset of the clinical signs [22].”
From Treatment of Alzheimer’s Disease: Beyond Symptomatic Therapies (2023) · cites this paper as [22]
Both total and phosphorylated tau are increased in the CSF of AD patients and can predict the progression of the disease.
“Furthermore, both total and phosphorylated tau (p-tau) are increased in the CSF of AD patients and can predict the progression of the disease [22,30,31].”
From Treatment of Alzheimer’s Disease: Beyond Symptomatic Therapies (2023) · cites this paper as [22]
These same mechanisms may render neurons vulnerable to excitotoxicity, as tau-dependent Fyn-PSD-95-NMDAR coupling amplifies glutamate receptor activation under pathological conditions.
“However, these same mechanisms may render neurons vulnerable to excitotoxicity, as tau-dependent Fyn-PSD-95-NMDAR coupling amplifies glutamate receptor activation under pathological conditions [52, 124].”
From Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease (2026) · cites this paper as [52]
Hyperphosphorylated tau spreads gradually from the post synaptic site to the dendrites and the cell body, and from the axon to other neurons by intra-axonal connections, resulting in synaptic dysfunction contributing to dementia and neurodegeneration.
“This hyperphosphorylated tau spreads gradually from the post synaptic site to the dendrites and the cell body, finally from the axon to other neurons by intra-axonal connections. This process results in synaptic dysfunction contributing to dementia and neurodegeneration [15].”
From Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease (2020) · cites this paper as [15]

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SynGAP regulates synaptic strength and mitogen-activated protein kinases in cultured neurons
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Tau protein is essential for stress-induced brain pathology
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Linking Amyloid-β and Tau: Amyloid-β Induced Synaptic Dysfunction via Local Wreckage of the Neuronal Cytoskeleton
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Pseudophosphorylation of Tau at distinct epitopes or the presence of the P301L mutation targets the microtubule-associated protein Tau to dendritic spines
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Tau‐targeting passive immunization modulates aspects of pathology in tau transgenic mice
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Phosphorylation of Human Tau Protein by Microtubule Affinity-Regulating Kinase 2
Schwalbe, M., Biernat, J., Bibow, S., Ozenne, V., Jensen, M. R., Kadavath, H., Blackledge, M., Mandelkow, E., & Zweckstetter, M. (2013) · Biochemistry · doi:10.1021/bi401266n · Cited by 78 · see citing works
p38 MAP kinase-mediated NMDA receptor-dependent suppression of hippocampal hypersynchronicity in a mouse model of Alzheimer’s disease
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Pro-aggregant Tau impairs mossy fiber plasticity due to structural changes and Ca++ dysregulation
Decker, J., Krüger, L., Sydow, A., Zhao, S., Frotscher, M., Mandelkow, E., & Mandelkow, E. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0193-3 · Cited by 77 · see citing works
Local Somatodendritic Translation and Hyperphosphorylation of Tau Protein Triggered by AMPA and NMDA Receptor Stimulation
Kobayashi, S., Tanaka, T., Soeda, Y., Almeida, O. F. X., & Takashima, A. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.05.012 · Cited by 74 · see citing works
Extracellular Tau Oligomers Induce Invasion of Endogenous Tau into the Somatodendritic Compartment and Axonal Transport Dysfunction
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 73 · see citing works
HDAC6 and RhoA are novel players in Abeta-driven disruption of neuronal polarity
Tsushima, H., Emanuele, M., Polenghi, A., Esposito, A., Vassalli, M., Barberis, A., Difato, F., & Chieregatti, E. (2015) · Nature Communications · doi:10.1038/ncomms8781 · Cited by 71 · see citing works
Amyloid-β plaques disrupt axon initial segments
Marin, M. A., Ziburkus, J., Jankowsky, J. L., & Rasband, M. N. (2016) · Experimental Neurology · doi:10.1016/j.expneurol.2016.04.018 · Cited by 67 · see citing works
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 64 · see citing works
An N-terminal motif unique to primate tau enables differential protein–protein interactions
Stefanoska, K., Volkerling, A. M., Bertz, J., Poljak, A., Ke, Y. D., Ittner, L. M., & Ittner, A. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001784 · Cited by 60 · see citing works
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Tau and spectraplakins promote synapse formation and maintenance through Jun kinase and neuronal trafficking
Voelzmann, A., Okenve-Ramos, P., Qu, Y., Chojnowska-Monga, M., del Caño-Espinel, M., Prokop, A., & Sánchez‐Soriano, N. (2016) · eLife · doi:10.7554/elife.14694 · Cited by 56 · see citing works
Altered hippocampal information coding and network synchrony in APP-PS1 mice
Cayzac, S., Mons, N. E., Ginguay, A., Allinquant, B., Jeantet, Y., & Cho, Y. H. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.08.023 · Cited by 51 · see citing works
NR2B Phosphorylation at Tyrosine 1472 Contributes to Brain Injury in a Rodent Model of Neonatal Hypoxia-Ischemia
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Loss of tau results in defects in photoreceptor development and progressive neuronal degeneration in Drosophila
Bolkan, B. J., & Kretzschmar, D. (2014) · Developmental Neurobiology · doi:10.1002/dneu.22199 · Cited by 47 · see citing works
Mobility and subcellular localization of endogenous, gene-edited Tau differs from that of over-expressed human wild-type and P301L mutant Tau
Xia, D., Gutmann, J. M., & Götz, J. (2016) · Scientific Reports · doi:10.1038/srep29074 · Cited by 47 · see citing works
Generation of a New Tau Knockout (tau Δex1 ) Line Using CRISPR/Cas9 Genome Editing in Mice
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No Overt Deficits in Aged Tau-Deficient C57Bl/6.Mapttm1(EGFP)Kit GFP Knockin Mice
van Hummel, A., Bi, M., Ippati, S., van der Hoven, J., Volkerling, A. M., Lee, W. S., Tan, D. C. S., Bongers, A., Ittner, A., Ke, Y. D., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0163236 · Cited by 40 · see citing works
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Accelerated kindling epileptogenesis in Tg4510 tau transgenic mice, but not in tau knockout mice
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Differential Phosphorylation of Human Tau Isoforms Containing Three Repeats by Several Protein Kinases
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PSD-93 deletion inhibits Fyn-mediated phosphorylation of NR2B and protects against focal cerebral ischemia
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Mice Devoid of Tau Have Increased Susceptibility to Neuronal Damage in Myelin Oligodendrocyte Glycoprotein-Induced Experimental Autoimmune Encephalomyelitis
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Selective impact of Tau loss on nociceptive primary afferents and pain sensation
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Evidence for trans-synaptic and exo-synaptic tau propagation in Alzheimer disease
Wood, H. B. (2015) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.205 · Cited by 17 · see citing works

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Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease
Khan, S., Barve, K. H., & Kumar, M. S. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200528142429 · Cited by 820 · see citing works
“synaptic dysfunction contributing to dementia and neurodegeneration [15].”
Background
Alzheimer's disease
López, J. A., González, H. M., & Léger, G. C. (2019) · Handbook of clinical neurology · doi:10.1016/b978-0-12-804766-8.00013-3 · Cited by 834 · see citing works
Complement C3 Is Activated in Human AD Brain and Is Required for Neurodegeneration in Mouse Models of Amyloidosis and Tauopathy
Wu, T., Dejanovic, B., Gandham, V. D., Gogineni, A., Edmonds, R., Schauer, S., Srinivasan, K., Huntley, M. A., Wang, Y., Wang, T.-M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.060 · Cited by 466 · see citing works
The complexity of tau in Alzheimer’s disease
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 374 · see citing works
The clinical promise of biomarkers of synapse damage or loss in Alzheimer’s disease
the Synaptic Health Endpoints Working Group, Colom-Cadena, M., Spires-Jones, T., Zetterberg, H., Blennow, K., Caggiano, A., DeKosky, S. T., Fillit, H., Harrison, J. E., Schneider, L. S., et al. (2020) · Alzheimer's Research & Therapy · doi:10.1186/s13195-020-00588-4 · Cited by 328 · 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
Tau: Enabler of diverse brain disorders and target of rapidly evolving therapeutic strategies
Chang, C.-W., Shao, E., & Mucke, L. (2021) · Science · doi:10.1126/science.abb8255 · Cited by 263 · see citing works
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 · see citing works
It’s all about tau
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 195 · see citing works
The Role of Glymphatic System in Alzheimer’s and Parkinson’s Disease Pathogenesis
Buccellato, F. R., D’Anca, M., Serpente, M., Arighi, A., & Galimberti, D. (2022) · Biomedicines · doi:10.3390/biomedicines10092261 · Cited by 184 · see citing works
Functions of p38 MAP Kinases in the Central Nervous System
Asih, P. R., Prikas, E., Stefanoska, K., Tan, A. R. P., Ahel, H. I., & Ittner, A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.570586 · Cited by 158 · see citing works
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Increased excitatory to inhibitory synaptic ratio in parietal cortex samples from individuals with Alzheimer’s disease
Lauterborn, J. C., Scaduto, P., Cox, C. D., Schulmann, A., LYNCH, G. S., Gall, C. M., Keene, C. D., & Limón, A. (2021) · Nature Communications · doi:10.1038/s41467-021-22742-8 · Cited by 146 · see citing works
The six brain‐specific TAU isoforms and their role in Alzheimer's disease and related neurodegenerative dementia syndromes
Buchholz, S., & Zempel, H. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.13784 · Cited by 145 · see citing works
Insulin Resistance at the Crossroad of Alzheimer Disease Pathology: A Review
Berlanga‐Acosta, J., Guillén, G. E., Rodríguez-Rodríguez, N., Bringas-Vega, M. L., García-del-Barco-Herrera, D., Berlanga-Saez, J. O., Ojalvo, A. G., Valdés-Sosa, M. J., & Valdes-Sosa, P. A. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.560375 · Cited by 139 · see citing works
New Insights Into Drug Discovery Targeting Tau Protein
Soeda, Y., & Takashima, A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.590896 · Cited by 133 · see citing works
Cognitive enhancement and neuroprotective effects of OABL, a sesquiterpene lactone in 5xFAD Alzheimer's disease mice model
Tang, J., Huang, L.-F., Deng, J., Wang, Y., Guo, C., Peng, X.-N., Liu, Z., & Gao, J. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102229 · Cited by 132 · see citing works
Alzheimer’s disease: Ablating single master site abolishes tau hyperphosphorylation
Stefanoska, K., Gajwani, M., Tan, A. R. P., Ahel, H. I., Asih, P. R., Volkerling, A., Poljak, A., & Ittner, A. (2022) · Science Advances · doi:10.1126/sciadv.abl8809 · Cited by 128 · see citing works
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Microglial phagocytosis in aging and Alzheimer's disease
Gabandé‐Rodríguez, E., Keane, L., & Capasso, M. (2020) · Journal of Neuroscience Research · doi:10.1002/jnr.24419 · Cited by 127 · see citing works
Tau induces PSD95–neuronal NOS uncoupling and neurovascular dysfunction independent of neurodegeneration
Park, L., Hochrainer, K., Hattori, Y., Ahn, S. J., Anfray, A., Wang, G., Uekawa, K., Seo, J., Palfini, V. L., Blanco, I., et al. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0686-7 · Cited by 123 · see citing works
Insights into Disease-Associated Tau Impact on Mitochondria
Szabo, L., Eckert, A., & Grimm, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176344 · Cited by 102 · see citing works
Cellular Prion Protein Mediates the Disruption of Hippocampal Synaptic Plasticity by Soluble TauIn Vivo
Ondrejčák, T., Klyubin, I. V., Corbett, G. T., Fraser, G. M., Hong, W., Mably, A. J., Gardener, M. J., Hammersley, J., Perkinton, M. S., Billinton, A., et al. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1700-18.2018 · Cited by 102 · see citing works
Current Concepts of Mixed Pathologies in Neurodegenerative Diseases
Forrest, S. L., & Kovács, G. G. (2022) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/cjn.2022.34 · Cited by 99 · see citing works
Tau in neurodegenerative diseases: molecular mechanisms, biomarkers, and therapeutic strategies
Zhang, X., Wang, J., Zhang, Z., & Ye, K. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00429-6 · Cited by 106 · see citing works
BAG3 and SYNPO (synaptopodin) facilitate phospho-MAPT/Tau degradation via autophagy in neuronal processes
Ji, C., Tang, M., Zeidler, C., Höhfeld, J., & Johnson, G. (2019) · bioRxiv · doi:10.1080/15548627.2019.1580096 · Cited by 89 · see citing works
Treatment of Alzheimer’s Disease: Beyond Symptomatic Therapies
Buccellato, F. R., D’Anca, M., Tartaglia, G. M., Del Fabbro, M., Scarpini, E., & Galimberti, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813900 · Cited by 94 · see citing works
“In this regard, experimental data supports a pathogenic mechanism in which AD neuropathology and Tau, a microtubule-associated protein, is highly expressed in neurons and has been implicated in the pathogenesis of AD and other neurodegenerative diseases called “tauopathies” [19,20,22–25].”
BackgroundInfluential
Ten Years of Tau-Targeted Immunotherapy: The Path Walked and the Roads Ahead
Novak, P., Kontsekova, E., Zilka, N., & Novak, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00798 · Cited by 87 · see citing works
“In comparison to immunotherapies targeting extracellular pathology, such as Aβ, tau-targeted immunotherapy faces an additional challenge: many types of tau are located intracellularly [whether axonal, dendritic (Ittner and Ittner, 2018), somatic, or nuclear (Paholikova et al.”
BackgroundInfluential
Proteotoxicity and Neurodegenerative Diseases
Ruz, C., Alcantud, J. L., Montero, F. V., Durán, R., & Bandrés‐Ciga, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165646 · Cited by 81 · see citing works
Protein kinases in neurodegenerative diseases: current understandings and implications for drug discovery
Wu, X., Yang, Z., Zou, J., Gao, H., Shao, Z., Li, C., & Lei, P. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02179-x · Cited by 88 · see citing works
Gut microbiota: A magical multifunctional target regulated by medicine food homology species
Zuo, W., Pang, Q., Yao, L.-P., Zhang, Y., Peng, C. Y., Huang, W., & Han, B. (2023) · Journal of Advanced Research · doi:10.1016/j.jare.2023.05.011 · Cited by 81 · see citing works
Selective Disruption of Inhibitory Synapses Leading to Neuronal Hyperexcitability at an Early Stage of Tau Pathogenesis in a Mouse Model
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 78 · see citing works
Flavonoids as an Intervention for Alzheimer’s Disease: Progress and Hurdles Towards Defining a Mechanism of Action
Hole, K. L., & Williams, R. J. (2020) · Brain Plasticity · doi:10.3233/bpl-200098 · Cited by 78 · see citing works
microRNAs as early biomarkers of Alzheimer’s disease: a synaptic perspective
Siedlecki-Wullich, D., Miñano-Molina, A. J., & Rodríguez-Álvarez, J. (2021) · Cells · doi:10.3390/cells10010113 · Cited by 76 · see citing works
Presynaptic failure in Alzheimer's disease
Barthet, G., & Mulle, C. (2020) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2020.101801 · Cited by 74 · see citing works
Cellular and regional vulnerability in frontotemporal tauopathies
Forrest, S. L., Kril, J. J., & Halliday, G. M. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02035-7 · Cited by 71 · see citing works
Cerebrospinal Fluid Biomarkers in Cerebral Amyloid Angiopathy
Banerjee, G., Ambler, G., Keshavan, A., Paterson, R. W., Foiani, M. S., Toombs, J., Heslegrave, A., Dickson, J. C., Fraioli, F., Groves, A. M., et al. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-191254 · Cited by 72 · see citing works
Significance of Blood and Cerebrospinal Fluid Biomarkers for Alzheimer’s Disease: Sensitivity, Specificity and Potential for Clinical Use
d’Abramo, C., D'adamio, L., & Giliberto, L. (2020) · Journal of Personalized Medicine · doi:10.3390/jpm10030116 · Cited by 68 · see citing works
Emerging role of AMPA receptor subunit GluA1 in synaptic plasticity: Implications for Alzheimer's disease
Qu, W., Yuan, B., Li, R., Liu, Q., Zhang, X., Cui, R., Yang, W., & Li, B. (2020) · Cell Proliferation · doi:10.1111/cpr.12959 · Cited by 64 · see citing works
Brain Ischemia as a Prelude to Alzheimer's Disease
Pluta, R. M., Januszewski, S., & Czuczwar, S. J. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.636653 · Cited by 67 · see citing works
The Enigma of Tau Protein Aggregation: Mechanistic Insights and Future Challenges
Zheng, H., Sun, H., Cai, Q., & Tai, H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25094969 · Cited by 65 · see citing works
The gut microbiota attenuate neuroinflammation in manganese exposure by inhibiting cerebral NLRP3 inflammasome
Wang, H., Yang, F., Xin, R., Cui, D., He, J., Zhang, S., & Sun, Y. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110449 · Cited by 63 · see citing works
Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review
Yang, J., Zhi, W., & Wang, L. (2024) · Molecules · doi:10.3390/molecules29122812 · Cited by 63 · see citing works
“Many of these sites are prominently phosphorylated in aggregated tau in neuroﬁbrillary tangles [62–66].”
Background
Functional Foods: An Approach to Modulate Molecular Mechanisms of Alzheimer’s Disease
Atlante, A., Amadoro, G., Bobba, A., & Latina, V. (2020) · Cells · doi:10.3390/cells9112347 · Cited by 64 · see citing works
Cerebrolysin in the therapy of mild cognitive impairment and dementia due to Alzheimer's disease: 30 years of clinical use
Si, G., & Álvarez, A. (2020) · Medicinal Research Reviews · doi:10.1002/med.21722 · Cited by 61 · see citing works
Super-resolution microscopy: a closer look at synaptic dysfunction in Alzheimer disease
Padmanabhan, P., Kneynsberg, A., & Götz, J. (2021) · Nature reviews. Neuroscience · doi:10.1038/s41583-021-00531-y · Cited by 55 · see citing works
Resveratrol Rescues Tau-Induced Cognitive Deficits and Neuropathology in a Mouse Model of Tauopathy
Sun, X., Dong, Q.-X., Zhu, J., Sun, X., Zhang, L., Qiu, M., Yu, X., & Liu, R. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666190801153751 · Cited by 58 · see citing works
Tau seeding and spreading in vivo is supported by both AD-derived fibrillar and oligomeric tau
de Gérando, A. M., Welikovitch, L. A., Khasnavis, A., Commins, C., Glynn, C. A., Chun, J. E., Perbet, R., & Hyman, B. T. (2023) · Acta Neuropathologica · doi:10.1007/s00401-023-02600-1 · Cited by 52 · see citing works
Dietary Polyphenols in Metabolic and Neurodegenerative Diseases: Molecular Targets in Autophagy and Biological Effects
García-Aguilar, A., Palomino, O. M., Benito, M., & Guillén, C. (2021) · Antioxidants · doi:10.3390/antiox10020142 · Cited by 52 · see citing works
Pharmacophore-based models for therapeutic drugs against phosphorylated tau in Alzheimer’s disease
Pradeepkiran, J. A., Reddy, A. P., & Reddy, P. H. (2018) · Drug Discovery Today · doi:10.1016/j.drudis.2018.11.005 · Cited by 52 · see citing works
Factors Regulating the Activity of LINE1 Retrotransposons
Protasova, M., Андреева, Т. В., & Rogaev, E. I. (2021) · Genes · doi:10.3390/genes12101562 · Cited by 51 · see citing works
Blood tau‐PT217 contributes to the anesthesia/surgery‐induced delirium‐like behavior in aged mice
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Key Peptides and Proteins in Alzheimer’s Disease
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Glutamatergic receptor expression changes in the Alzheimer's disease hippocampus and entorhinal cortex
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The Role of Amyloid-Beta and Tau in the Early Pathogenesis of Alzheimer’s Disease
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Phosphorylated tau as a toxic agent in synaptic mitochondria: implications in aging and Alzheimer’s disease
Tapia‐Rojas, C., Torres, A., Rivera, B., Polanco, C. M., & Jara, C. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.332125 · Cited by 48 · see citing works
Differential expression of tau species and the association with cognitive decline and synaptic loss in Alzheimer's disease
Saroja, S. R., Sharma, A., Hof, P. R., & Pereira, A. C. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12518 · Cited by 45 · see citing works
Phospho-Tau Changes in the Human CA1 During Alzheimer’s Disease Progression
Regalado-Reyes, M., Furcila, D., Hernández, F., Ávila, J., DeFelipe, J., & León‐Espinosa, G. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-181263 · Cited by 46 · see citing works
Tau is required for the function of extrasynaptic NMDA receptors
Pallas‐Bazarra, N., Draffin, J. E., Cuadros, R., Esteban, J. A., & Ávila, J. (2019) · Scientific Reports · doi:10.1038/s41598-019-45547-8 · Cited by 46 · see citing works
The multifaceted role of WNT signaling in Alzheimer’s disease onset and age-related progression.
Kostes, W. W., & Brafman, D. A. (2023) · Cells · doi:10.3390/cells12081204 · Cited by 43 · see citing works
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Authors: Ittner, A., & Ittner, L. M.
Affiliations: UNSW Sydney (AU)
Corresponding author: Ittner, Lars M.
ORCID: Ittner, Arne
Ittner, Lars M.
Venue: Neuron
Publisher: Elsevier BV
Published: 2018-07
Volume: 99
Issue: 1
Pages: 13-27
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/j.neuron.2018.06.003
OpenAlex: W2815697343
Cited by: 278
References: 179
Citations by year: 2026: 20 · 2025: 34 · 2024: 37 · 2023: 31 · 2022: 31 · 2021: 40 · 2020: 58 · 2019: 21 · 2018: 6
FWCI: 4.13
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, 375 d)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
Funders: National Health and Medical Research Council (1132524, 1136241, 1081916, 1143848, 1143978)
Australian Research Council (609-2015-07, DP170100781, DP170100843)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Keywords: tau protein, Alzheimer's disease, amyloid-beta, dendrites, synaptic dysfunction, neuroprotection, microtubule-associated proteins
MeSH terms: Alzheimer Disease, Dendrites, Humans, Neurons, Synapses, Amyloid beta-Peptides, Neurofibrillary Tangles, tau Proteins, Plaque, Amyloid

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Dendritic Tau in Alzheimer’s Disease

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