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Nuclear Tau, a Key Player in Neuronal DNA Protection
Open accessAbstract
Tau, a neuronal protein involved in neurodegenerative disorders such as Alzheimer disease, which is primarily described as a microtubule-associated protein, has also been observed in the nuclei of neuronal and non-neuronal cells. However, the function of the nuclear form of Tau in neurons has not yet been elucidated. In this work, we demonstrate that acute oxidative stress and mild heat stress (HS) induce the accumulation of dephosphorylated Tau in neuronal nuclei. Using chromatin immunoprecipitation assays, we demonstrate that the capacity of endogenous Tau to interact with neuronal DNA increased following HS. Comet assays performed on both wild-type and Tau-deficient neuronal cultures showed that Tau fully protected neuronal genomic DNA against HS-induced damage. Interestingly, HS-induced DNA damage observed in Tau-deficient cells was completely rescued after the overexpression of human Tau targeted to the nucleus. These results highlight a novel role for nuclear Tau as a key player in early stress response.
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“In particular, intranuclear tau is thought to bind to chromatin and stabilize it in response to cellular stressors such heat [149].”
From DNA repair deficiency and senescence in concussed professional athletes involved in contact sports (2019) · cites this paper as [149]
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“prevents DNA damage by oxidative stress 94, 106”
From Altered Machinery of Protein Synthesis in Alzheimer's: From the Nucleolus to the Ribosome (2016) · cites this paper as [94]
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Cites
Single cell gel/comet assay: Guidelines for in vitro and in vivo genetic toxicology testing
Tice, R. R., Agurell, E., Anderson, D. C., Burlinson, B., Hartmann, A., Kobayashi, H., Miyamae, Y., Rojas, E., Ryu, J., & Sasaki, Y. F. (2000) · Environmental and Molecular Mutagenesis · doi:10.1002/(sici)1098-2280(2000)35:3 · Cited by 4,885
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
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
Self-citationThe 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
Olive, P. L., Banáth, J. P., Durand, R. E., & Banáth, J. P. (1990) · Radiation Research · doi:10.2307/3577587 · Cited by 1,095
Olive, P. L., Banáth, J. P., & Durand, R. E. (2012) · Radiation Research · doi:10.1667/rrav04.1 · Cited by 1,031
Crossing the Nuclear Envelope: Hierarchical Regulation of Nucleocytoplasmic Transport
Terry, L. J., Shows, E. B., & Wente, S. R. (2007) · Science · doi:10.1126/science.1142204 · Cited by 543
I will survive: DNA protection in bacterial spores
Setlow, P. (2007) · Trends in Microbiology · doi:10.1016/j.tim.2007.02.004 · Cited by 466
Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules.
Trinczek, B., Biernat, J., Baumann, K., Mandelkow, E. M., & Mandelkow, E. (1995) · Molecular Biology of the Cell · doi:10.1091/mbc.6.12.1887 · Cited by 340
Heat-induced formation of reactive oxygen species and 8-oxoguanine, a biomarker of damage to DNA
Брусков, В. И. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.6.1354 · Cited by 307
Research works printed but not linked: 1
- Daniel, 2008, BBA, 1783, 1003
Cited by
Sorted by citations
Items 301–400 of 420
The mitotic tensegrity guardian tau protects mammary epithelia from katanin-like1-induced aneuploidy
Sudo, H., & Nakajima, K. (2016) · Oncotarget · doi:10.18632/oncotarget.10728 · Cited by 6
“Tau and a severing family protein are known to have functions not only via MT but also via their interactions with DNA [65, 66].”
BackgroundInfluentialLRP1 and SORL1 regulate tau internalization and degradation and enhance tau seedingPreprint
Cooper, J. M., Lathuilière, A., Migliorini, M. M., Arai, A. L., Wani, M. M., Dujardin, S., Muratoglu, S. C., Hyman, B. T., & Strickland, D. K. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.17.386581 · Cited by 6
“In addition, tau phosphorylation at specific residues regulates tau’s function, regulates its subcellular localization (Pooler et al., 2012; Sultan et al., 2011; Tang et al., 2015) and reduces its affinity for microtubules (Biernat et al., 1993; Jameson et al., 1980).”
BackgroundZimmer‐Bensch, G., & Zempel, H. (2021) · Preprints.org · doi:10.20944/preprints202105.0717.v1 · Cited by 6
Schreiner, T. G., Ciobanu, R. C., & Schreiner, O. D. (2026) · Biomedicines · doi:10.3390/biomedicines14030522 · Cited by 6
“In the nucleus, tau binds to DNA and protects genomic integrity under oxidative stress [26].”
Trichloroacetic acid treatment as a tricky way for rapid purification of 1N/4R tau protein
Asadollahi, K., Rafiee, S., Riazi, G. H., Pooyan, S., & Afrasiabi, A. (2015) · Protein Expression and Purification · doi:10.1016/j.pep.2015.10.007 · Cited by 5
Sturiale, V., Bruno, F., Brancato, D., D’Amico, A. G., Maugeri, G., D’Agata, V., Saccone, S., & Federico, C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241814373 · Cited by 5
Adenosine Receptors and Alzheimer’s Disease
Blum, D. L., Sandau, U. S., Laurent, C., Batalha, V. L., Leboucher, A., Hamdane, M., Pasquier, F., Boison, D., Buée, L., & Lopes, L. V. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3903-5_19 · Cited by 6
Self-citationMagrin, C., Bellafante, M., Sola, M., Piovesana, E., Bolis, M., Cascione, L., Napoli, S., Rinaldi, A., Papin, S., & Paganetti, P. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1232963 · Cited by 6
“Heat or oxidative stress cause nuclear translocation of Tau, which may favor its role in DNA protection (Sultan et al., 2011).”
BackgroundChronic exposure to ketamine induces neuronal lose and glial reaction in CA4 region of hippocampus
Ahmadpour, S., Foghi, K., & Behrad, A. G. M. (2016) · Journal of Morphological Sciences · doi:10.4322/jms.095115 · Cited by 5
The many connections of UFMylation with Alzheimer’s disease: a comprehensive review
Yan, T., Clarkson, B. D. S., Lou, Z., Springer, W., & Fiesel, F. C. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00855-8 · Cited by 4
“Tau translocates to the nucleus under heat or oxidative stress [106] and upon treatment with DNA damage-inducing agents such as etoposide [6].”
Targeted tau protein degradation: a promising therapeutic approach for tauopathies
Baazaoui, N., Alfaifi, M. Y., Shati, A. A., Saad, R. B., & Garzoli, S. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.11.041 · Cited by 5
Axonal tau reduction ameliorates tau and amyloid pathology in a mouse model of Alzheimer’s disease
Zare, A., Salehi, S., Bader, J. M., Wiessler, A.-L., Prokesch, M., Albrecht, V., Villmann, C., Mann, M., Briese, M., & Sendtner, M. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00499-0 · Cited by 4
“In addition, tau exerts functions in neuronal cell bodies, such as DNA damage protection [90], and these functions might be affected by complete tau removal.”
Lehmann, D. J., Elshorbagy, A. K., & Hurley, M. J. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230295 · Cited by 5
“This is not helped, though understandably so, by the way and clinical trials and to a lesser extent basic research are designed.”
Mohammadi, F., Takalloo, Z., Rahmani, H., Khalili, M. A. N., Khajeh, K., Riazi, G. H., & Sajedi, R. H. (2020) · The Journal of Biochemistry · doi:10.1093/jb/mvaa101 · Cited by 4
Shapeshifting tau: from intrinsically disordered to paired-helical filaments
Mengham, K., Al‐Hilaly, Y. K., Oakley, S. S., Kasbi, K., Maina, M. B., & Serpell, L. C. (2022) · Essays in Biochemistry · doi:10.1042/ebc20220150 · Cited by 4
Identification of Novel Kinases of Tau Using Fluorescence Complementation Mass Spectrometry (FCMS)
Kao, D., Du, Y., DeMarco, A. G., Min, S., Hall, M. C., Rochet, J., & Tao, W. A. (2022) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2022.100441 · Cited by 5
“The ampli fi ed cDNAs were then cloned in frame into the EcoRI/XhoI sites of pMyc-MCS-2(4G1S)Linker-VN155(I152L).”
InfluentialSubcellular functions of tau mediate repair response and synaptic homeostasis in injury
Thomas, R., Zhang, D., Cronkite, C. A., Thomas, R., Singh, S. K., Bronk, L. F., Morales, R., Duman, J. G., & Grosshans, D. R. (2025) · Molecular Psychiatry · doi:10.1038/s41380-025-03029-6 · Cited by 6
The Essentials of Biochemistry of the Proteins as Related to Alzheimer’s Disease: A Review
Prasad, A. (2020) · International Journal of Biochemistry Research & Review · doi:10.9734/ijbcrr/2020/v29i130163 · Cited by 4
Targeting pyroptosis in tauopathies: A redox-driven axis of neuroinflammation and neurodegeneration
López, E. A., Silva-Llanes, I., Diez-Tejedor, E., & Lastres‐Becker, I. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.04.029 · Cited by 4
Cho, H., Lee, J., Nho, H., Lee, K., Gim, B., Lee, J., Lee, J., Ewert, K. K., Li, Y., Feinstein, S. C., et al. (2023) · The European Physical Journal E · doi:10.1140/epje/s10189-023-00328-0 · Cited by 2
“The protein Tau is mostly localized in axons of neurons and plays a key role in neuronal development including cell polarity, outgrowth, dendrite pruning, and DNA protection [1–8].”
BackgroundHigh Tau expression correlates with reduced invasion and prolonged survival in Ewing sarcoma
Cidre‐Aranaz, F., Magrin, C., Zimmermann, M., Li, J., Baffa, A., Ciccaldo, M., Hartmann, W., Dirksen, U., Sola, M., Paganetti, P., et al. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02497-7 · Cited by 3
“For instance, Tau translocates to the cell nucleus upon heat or oxidative stress and protects DNA [7 – 11].”
Tau protein aggregation: A therapeutic target for neurodegenerative diseases
Duggal, A., Mahindru, D., Baghel, K., Mehrotra, S., & Prajapati, V. K. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2024.11.012 · Cited by 2
Loss of AT8 Nuclear Tau as a Marker of Neuronal Ageing and Alzheimer’s Disease Progression
Bruno, F., Gil, L., Sturiale, V., Guerrero, C., Poves, A. B. R., Brancato, D., Morales, J., Saccone, S., & Federico, C. (2025) · Biomedicines · doi:10.3390/biomedicines13112587 · Cited by 2
“Tau, encoded by the microtubule-associated protein tau (MAPT) gene, is known primarily for stabilising microtubules, but increasing evidence suggests that it also has nuclear functions in chromatin organisation and protection [14,19,58,63].”
Clinical and neuropathological variability in the rare IVS10 + 14 tau mutation
Maxwell, S. P., Cash, M. K., Rockwood, K. J., Fisk, J. D., & Darvesh, S. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.01.004 · Cited by 2
Gene-Environment Interactions in Progressive Supranuclear Palsy
Litvan, I., Proudfoot, J. A., Martin, E. R., Standaert, D. G., Riley, D. E., Hall, D. A., Marras, C., Bayram, E., Dubinsky, R., Bordelon, Y. M., et al. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.664796 · Cited by 2
“MAPT has been well-documented as a significant predisposing gene in PSP, and oxidative stress has been shown to cause tau accumulation (25).”
BackgroundGil, L., Capdeville, G., Rodríguez‐Leyva, I., Niño, S. A., & Jiménez-Capdeville, M. E. (2021) · Revista de Fomento Social · doi:10.24875/rmn.20000108 · Cited by 2
Ghalat, N. J., Shahpasand, K., & Javan, M. (2022) · Experimental Neurology · doi:10.1016/j.expneurol.2022.114262 · Cited by 2
Park, C., Jung, J., Hong, Y., Yoo, H., Yang, K., Shin, J., Kim, M., Lim, C. S., Jeong, A., Hong, S., et al. (2026) · Nature Communications · doi:10.1038/s41467-025-67888-x · Cited by 2
“One notable exception is tau ’ s role in the nucleus, where it has been proposed to protect the genome and in fl uence gene expression 26 – 28 .”
Vingtdeux, V., Buée, L., & Sergeant, N. (2011) · InTech eBooks · doi:10.5772/20567 · Cited by 1
“Tau is likely secreted and is also located into the nucleus following stress conditions (Sultan et al., 2011).”
Self-citationEffects of Formaldehyde on Protein (Tau) Aggregation and Cytotoxicity
He, R. (2017) · Springer eBooks · doi:10.1007/978-94-024-1177-5_7 · Cited by 2
Tau in Health and Neurodegenerative Diseases
Chu, D., & Liu, F. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.101299 · Cited by 2
Natural antioxidants in prevention and management of Alzheimer's disease
Zhao, Y. M. (2011) · Frontiers in Bioscience-Elite · doi:10.2741/516 · Cited by 2
Tau modulates nuclear integrity, chromatin, and cholesterol synthesis genes via the nuclear envelopePreprint
Diez, L., Ponce-Lina, R., Kilic, C., Sankar, R., Balduin, F., Wang, C., Grundschöttel, P., Sakurai, K., Askin, B., Bordier, C., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.05.692577 · Cited by 2
Federico, C., Bruno, F., Sturiale, V., D’Amico, A. G., Maugeri, G., D’Agata, V., Gil, L., & Saccone, S. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-817990-1.00007-x · Cited by 1
Mayeri, Z., Woods, G., Rane, A., Kifle, A., Chamoli, M., Shukla, S., Walton, C. C., & Andersen, J. K. (2026) · GeroScience · doi:10.1007/s11357-026-02139-5 · Cited by 2
Tau conformation, distribution and PET imaging correlations in progressive supranuclear palsy
Dong, C., Ma, J., Qiao, H., Tamagnan, G. D., Chan, P., & Liu, S. (2026) · Translational Neurodegeneration · doi:10.1186/s40035-026-00545-5 · Cited by 2
“Pathological tau is also associated with reduced nuclear tau, impairing the physiological role of tau in preventing DNA damage, thus contributing to genomic instability [43].”
Alonso-Estanillo, B., Ochoa, M., Gómez, L., Pin, X., López, A., & Vásquez, F. (2026) · Biology · doi:10.3390/biology15110845 · Cited by 1
“…tau translocation may represent an adaptive response to chronic oxidative stress and intermittent hypoxia in diving mammals, a “nuclear shield” hypothesis [17,44] that awaits direct empirical validation through measurements of oxidative stress markers and comparative studies in terrestrial mammals.”
Oosterlynck, M., Fichter, L., Leroux, É., Eddarkaoui, S., Bouillet, T., Lefebvre, C., Nguyen, M., Maurage, C., Accart, B., Dupré, E., et al. (2026) · Journal of Biomedical Science · doi:10.1186/s12929-026-01250-1 · Cited by 1
Self-citationTau protein as a regulator of mitochondrial function and dynamics
Tsakiri, E. N., Campos‐Marques, C., Ploumi, C., Skourti, K., Roussos, A., Mytilinaiou, E., Vamvaka-Iakovou, A., Ferreira, I. L., Dioli, C., Gianniou, D. D., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2521642123 · Cited by 1
From Protein Tangles to Genetic Variants: The Central Role of Tau in Neurodegenerative Disease
Julia, H., & Wade‐Martins, R. (2011) · InTech eBooks · doi:10.5772/29839 · Cited by 1
“Recently, it has been shown that nuclear tau interacts with neuronal DNA and protects DNA integrity against mild heat-stress induced damage (Sultan et al., 2011).”
Tau Phosphorylation as a Therapeutic Target in Alzheimer’s Disease
Medina, M., & Ávila, J. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00012-5 · Cited by 1
Risk Factors for Alzheimer’s Disease
Cai, D., & Gaamouch, F. E. (2016) · InTech eBooks · doi:10.5772/64270 · Cited by 1
“[45] Sultan A, Nesslany F, Violet M, Begard S, Loyens A, Talahari S, et al.”
BackgroundStephens, G. S., You, J. C., Fu, C.-H., & Chin, J. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809324-5.21126-7 · Cited by 1
Tau Phosphorylation and Amyloid-β Deposition in the Presence of Formaldehyde
Lü, J., & He, R. (2017) · Springer eBooks · doi:10.1007/978-94-024-1177-5_9 · Cited by 1
Martins, D. R., Vandermeeren, M., Kolen, K. V., Brepoels, E., Borgers, M., Wintmolders, C., Delay, C., Bottelbergs, A., Mercken, M. H., & Theunis, C. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-221266 · Cited by 1
Schneeweis, A. K., & Pak, D. T. S. (2023) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2023.106475 · Cited by 1
The potential of proteomics for in-depth molecular investigations of progressive supranuclear palsy
Romero-Murillo, S., Lee, S., Fernández‐Irigoyen, J., Martínez-Valbuena, I., & Santamaría, E. (2025) · Expert Review of Proteomics · doi:10.1080/14789450.2025.2519466 · Cited by 1
“…cytoplasmic tau stabilizes microtubules and supports axonal transport [6,7]; membrane-associated tau participates in neurite development and intracellular signaling [8– 10]; and nuclear tau contributes to gene regulation and DNA protection against oxidative and heat-induced damage [11– 13].”
Experimental Models of Tau Aggregation
Buck, K., Jahn, T. R., & Gasparini, L. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811353-0.00070-1 · Cited by 1
Bimonte, S., Barbieri, A., Nagoth, J. A., Cascella, M., Cuomo, A., & Arra, C. (2019) · Neuromethods · doi:10.1007/978-1-4939-9891-3_13 · Cited by 1
New Perspectives for Treatment in Alzheimer’s Disease
Loureiro, J. C., Silva, L. F. D. A. L. E., Pais, M. V., & Forlenza, O. V. (2022) · Springer eBooks · doi:10.1007/978-3-030-94383-7_10 · Cited by 1
Modeling Taupathies in Zebrafish (Danio rerio)
Kotova, M. M., Kolesnikova, T. O., & Kalueff, A. V. (2023) · Российский физиологический журнал им И М Сеченова · doi:10.31857/s0869813923110067 · Cited by 1
Investigating Tau pathology in an in vitro model for Alzheimer’s disease
Powrie, Y. S. L. (2016) · SUNScholar (Stellenbosch University) · Cited by 1
Mutant MAPT Induces rDNA Transcriptional Hyperactivation and Nucleolar Stress in Cellular ModelsPreprint
Muhammad, Z., Gu, Y., Kwairanga, S. H., Bailey, L. J., Khan, A., Nasser, M., Aljarrah, D., Arber, C., Wray, S., Serpell, L. C., et al. (2025) · Research Square · doi:10.21203/rs.3.rs-7713987/v1 · Cited by 1
The Microtubule-Dissociating Tau in Neurological Disorders
Jos, F., Schraen‐Maschke, S., & Buée, L. (2012) · InTech eBooks · doi:10.5772/30190
Self-citationFunctional implications of tau-fyn interactions in Alzheimer's disease
Lau, H. W. D. (2015)
Adenosine Receptors and Memory Disorders
de Mendonça, A., Blum, D. L., & Geiger, J. D. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803724-9.00009-0
Neurochemical Aspects of β-Amyloid Cascade Hypothesis for Alzheimer’s Disease
Farooqui, A. A. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809937-7.00001-x · Cited by 1
Functional Interactions of tau, Pin1, p53 and mRNA 3′ Processing Factors in Non-Neuronal Cells
Baquero, J. (2018) · CUNY Academic Works (City University of New York)
Single Molecule Imaging Reveals Tau Structure And Function On The Microtubule Surface
Stern, J. L. (2018) · ScholarWorks -A service of University of Vermont Libraries (University of Vermont)
Characterizing tau in the nucleus
Camphire, S. G., & Henwood, M. L. (2018) · JMU Scholoraly Commons (James Madison University)
Lee, Y. J. (2021) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/151287
Tau Protein Disrupts Nucleocytoplasmic Transport in Alzheimer’s DiseasePreprint
Eftekharzadeh, B., Daigle, J. G., Kapinos, L. E., Dujardin, S., Coyne, A. N., Miller, S., Cook, C. N., Grima, J. C., Bennett, R. E., Schiantarelli, J., et al. (2018) · SSRN Electronic Journal · doi:10.2139/ssrn.3155576
Molekularne podłoże proteinopatii: przyczyna zespołów otępiennych i zaburzeń motorycznych
Zgórzyńska, E., Krawczyk, K., Bełdzińska, P., & Walczewska, A. (2021) · Postępy Higieny i Medycyny Doświadczalnej · doi:10.5604/01.3001.0014.9513
THE ROLE OF MICROTUBULE-ASSOCIATED PROTEIN TAU IN NEURONAL EXCITABILITY AND EPILEPTOGENESIS
Cloyd, R. (2021) · UKnowledge (University of Kentucky) · doi:10.13023/etd.2021.271
Doersch, A. (2020) · University of Minnesota Digital Conservancy (University of Minnesota)
Marques, R. B. (2021) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.17.2021.tde-06122021-121359
Nanoskalauntersuchungen vom zellulären Metabolismus mittels Sekundärionen-Massenspektrometrie
Karsten, L. (2022) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9484
Tau’s function and dysfunction in the brain
Portillo, M., & Toiber, D. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.373682
“Among these stresses, Tau has been found to respond to oxidative stress, heat shock, glucose deprivation, loss of proteostasis, and genotoxic stress (Sultan et al., 2011; Ulrich et al., 2018; Asada-Utsugi et al., 2022).”
BackgroundTau Protein Modulates an Epigenetic Mechanism of Cellular SenescencePreprint
Magrin, C., Sola, M., Piovesana, E., Bolis, M., Rinaldi, A., Papin, S., & Paganetti, P. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.05.543662
Callari, M., Sola, M., Magrin, C., Rinaldi, A., Bolis, M., Paganetti, P., Colnaghi, L., & Papin, S. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.04.547660
“accumulation of DNA lesions in the brains of MAPT knock-out (MAPT KO) mice and primary neurons(7, 8).”
BackgroundHorta‐López, P. H., Říčný, J., Florán, B., & García‐Sierra, F. (2023) · Journal of Experimental Neurology · doi:10.33696/neurol.4.080
Modeling Tauopathies in Zebrafish (Danio rerio)
Kotova, M. M., Kolesnikova, T. O., & Kalueff, A. V. (2023) · Journal of Evolutionary Biochemistry and Physiology · doi:10.1134/s0022093023060133
“The first contains 2000 nucleotide pairs (n.p.) and encodes a nuclear tau protein, which is irrelevant to microtubule stabilization but partici(cid:2) pates in DNA protection [14].”
Amyloid β Deposition, Tau Phosphorylation, ApoE4 Dysfunction, and Formaldehyde
Lü, J., & He, R. (2025) · Springer eBooks · doi:10.1007/978-981-96-7281-3_10
Multifunctional Protein Tau Aggregation and Cytotoxicity
He, X., Lü, Y., & He, R.-Q. (2025) · Springer eBooks · doi:10.1007/978-981-96-7281-3_8
Ávila, J., Hernández, F., & Viña, J. (2025) · Geromedicine · doi:10.70401/geromedicine.2025.0006
Copsey, A. C., Oakley, S. S., Maina, M. B., Parker, R., Marshall, K. E., Harrington, C. R., Storey, J. M. D., Wischik, C. M., & Serpell, L. C. (2026) · Bioscience Reports · doi:10.1042/bsr20260349
“Both acute OS and heat stress increase the localisation of tau to the nucleus of neuronal cells, where it fully protectes the neuronal cells against heat-shock-induced DNA damage [3].”
InfluentialFrandemiche, M. (2013) · theses.fr (ABES) · doi:10.70675/260ed9c4zd958z47e0za418z0f324a1b102b
“Longtemps considérée comme une protéine exclusivement axonale, il est maintenant admis que la répartition de la protéine tau est plus étendue (Tashiro et al., 1997 ; Sultan et al., 2011) et que cette protéine possède diverses fonctions dont les mécanismes sous-jacents font actuellement l'objet d'intensives investigati…”
InfluentialFarmer, K. M., Ghag, G., Puangmalai, N., Montalbano, M., Bhatt, N. N., & Kayed, R. (2020) · Figshare · doi:10.6084/m9.figshare.12788590
Farmer, K. M., Ghag, G., Puangmalai, N., Montalbano, M., Bhatt, N. N., & Kayed, R. (2020) · Figshare · doi:10.6084/m9.figshare.12788593
Farmer, K. M., Ghag, G., Puangmalai, N., Montalbano, M., Bhatt, N. N., & Kayed, R. (2020) · Figshare · doi:10.6084/m9.figshare.12788602
Farmer, K. M., Ghag, G., Puangmalai, N., Montalbano, M., Bhatt, N. N., & Kayed, R. (2020) · Figshare · doi:10.6084/m9.figshare.12788596
Additional file 1 of Synaptic tau: A pathological or physiological phenomenon?
Robbins, M., Clayton, E. L., & Schierle, G. S. K. (2021) · Figshare · doi:10.6084/m9.figshare.16599510
Marie, O., Fichter, L., Leroux, É., Eddarkaoui, S., Thomas, B., Camille, L., Maurage, C., Bertrand, A., Nguyen, M., Dupré, E., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-8558884/v1
Self-citationImplications of virus-induced stress granules in tauopathies
Sharma, S., Vandenakker, A., Cortes-Pérez, C. M., Milne, S., & Douville, R. N. (2026) · Translational Neurodegeneration · doi:10.1186/s40035-026-00538-4
“Nuclear speckles of dephosphorylated tau are evident following heat shock and could bind genomic DNA [73], likely via its PRD and MTBD [74].”
Liquid–liquid phase separation of tau in Alzheimer’s disease
Rajkhowa, S., & Tripathi, T. (2026) · International review of neurobiology · doi:10.1016/bs.irn.2026.01.009
Spinal motor neuron degeneration after brachial plexus avulsion: mechanisms and therapeutic targets
Yang, J., Qin, B., Yang, Y., Fang, J., & He, W. (2026) · Frontiers in Neuroscience · doi:10.3389/fnins.2026.1778229
Expression of non-neuronal Tau in humans and micePreprint
Lekka, C., Ellis, M., Holden, K. L., Flaxman, C. S., Todd, J. A., Stefana, M. I., & Richardson, S. J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.27.708441
Sepulveda-Diaz, J. E. (2013) · theses.fr (ABES) · doi:10.70675/56c42bcbz41dfz432bzbb78z77110b373285
A Study of Striatal Markers as Disease Modifiers in Huntington's Disease
Francelle, L. (2014) · theses.fr (ABES) · doi:10.70675/ac372f63z7712z4632z8782z6b71a643add2
Les nanotubes comme nouvelle voie de transfert et de propagation de la protéine Tau pathologique
Tardivel, M. (2017) · theses.fr (ABES) · doi:10.70675/0cfcd049z970ez4f2dz8417z195cfabdc00d
Auboyer, L. (2018) · theses.fr (ABES) · doi:10.70675/07243ef7zb974z4ad8z97d9zd046801798b1
“La perte de la protéine pourrait également jouer un rôle dans la neurodégénérescence, de par son implication dans de nombreux processus vitaux pour les neurones tels que le transport de fer, la neurogenèse, la protection de l’ADN neuronal (Kimura et al., 2014; Lei et al., 2012; Sultan et al., 2011).”
BackgroundRôle des modifications post-traductionnelles dans le processus d’agrégation de la protéine Tau
Despres, C. (2017) · theses.fr (ABES) · doi:10.70675/de10f843z8572z4295zb672z763dbf30e2b5
Vautheny, A. (2019) · theses.fr (ABES) · doi:10.70675/1812d71aze8d9z48d6z87d1z5a23a4e81953
Study of the Neuron-Astrocyte Relationship in a Rodent Model of Tauopathy
de Gérando, A. M. (2019) · theses.fr (ABES) · doi:10.70675/04658671zaca3z4fefza24dz2f5a011bebfe
Metadata
- Authors
- Sultan, A., Nesslany, F., Violet, M., Bégard, S., Loyens, A., Talahari, S., Mansuroglu, Z., Marzin, D., Sergeant, N., Humez, S., Colin, M., Bonnefoy, E., Buée, L., & Galas, M.-C.
- Affiliations
- Inserm (FR)
- Institut Pasteur de Lille (FR)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Galas, Marie-Christine
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2011-02
- Volume
- 286
- Issue
- 6
- Pages
- 4566-4575
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3039398
- OpenAlex
- W2155048015
- Cited by
- 421
- References
- 54
- Citations by year
- 2026: 24 · 2025: 16 · 2024: 21 · 2023: 31 · 2022: 29 · 2021: 44 · 2020: 39 · 2019: 24 · 2018: 48 · 2017: 27 · 2016: 23 · 2015: 25 · 2014: 26 · 2013: 18 · 2012: 16
- FWCI
- 9.41
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Commission (200611)
- Agence Nationale de la Recherche
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Keywords
- heat stress, oxidative stress, DNA damage, neurodegeneration, Alzheimer's disease, microtubule-associated proteins, stress response
- MeSH terms
- Alzheimer Disease, Animals, Cell Nucleus, Cells, Cultured, DNA, Humans, Neurons, Phosphorylation, tau Proteins, Mice, Knockout, Heat-Shock Response, Mice
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