Loss of Tau protein affects the structure, transcription and repair of neuronal pericentromeric heterochromatin

A guided tour into subcellular colocalization analysis in light microscopy

Bolte, S., & Cordelières, F. (2006) · Journal of Microscopy · doi:10.1111/j.1365-2818.2006.01706.x · Cited by 5,238 · see citing works

The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics

Karran, E., Mercken, M., & Strooper, B. D. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3505 · Cited by 2,188 · see citing works

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 2,007 · see citing works

Hyperdynamic Plasticity of Chromatin Proteins in Pluripotent Embryonic Stem Cells

Meshorer, E., Yellajoshyula, D., George, E. M., Scambler, P. J., Brown, D. T., & Misteli, T. (2006) · Developmental Cell · doi:10.1016/j.devcel.2005.10.017 · Cited by 1,008 · see citing works

Epigenetic Codes for Heterochromatin Formation and Silencing

Richards, E. J., & Elgin, S. C. R. (2002) · Cell · doi:10.1016/s0092-8674(02)00644-x · Cited by 869 · see citing works

Constitutive heterochromatin formation and transcription in mammals

Saksouk, N., Simboeck, E., & Déjardin, J. (2015) · Epigenetics & Chromatin · doi:10.1186/1756-8935-8-3 · Cited by 543 · see citing works

Neurotrophins are required for nerve growth during development

Tucker, K. L., Meyer, M., & Barde, Y. (2001) · Nature Neuroscience · doi:10.1038/82868 · Cited by 526 · see citing works

Tau promotes neurodegeneration through global chromatin relaxation

Frost, B., Hemberg, M., Lewis, J., & Feany, M. B. (2014) · Nature Neuroscience · doi:10.1038/nn.3639 · Cited by 519 · see citing works

Mouse centric and pericentric satellite repeats form distinct functional heterochromatin

Guenatri, M., Bailly, D., Maison, C., & Almouzni, G. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200403109 · Cited by 498 · see citing works

Nuclear Tau, a Key Player in Neuronal DNA Protection

Sultan, A., Nesslany, F., Violet, M., Bégard, S., Loyens, A., Talahari, S., Mansuroglu, Z., Marzin, D., Sergeant, N., Humez, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.199976 · Cited by 421 · see citing works

Defects in Axonal Elongation and Neuronal Migration in Mice with Disrupted tau and map1b Genes

Takei, Y., Teng, J., Harada, A., & Hirokawa, N. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.5.989 · Cited by 408 · see citing works

Prime, Repair, Restore: The Active Role of Chromatin in the DNA Damage Response

Soria, G., Polo, S. E., & Almouzni, G. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.06.002 · Cited by 342 · see citing works

A Strand-Specific Burst in Transcription of Pericentric Satellites Is Required for Chromocenter Formation and Early Mouse Development

Probst, A. V., Okamoto, I., Casanova, M., Marjou, F. E., Baccon, P. L., & Almouzni, G. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.09.002 · Cited by 323 · see citing works

Stress-induced transcription of satellite III repeats

Jolly, C., Metz, A., Govin, J., Vigneron, M., Turner, B. M., Khochbin, S., & Vourc’h, C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200306104 · Cited by 314 · see citing works

DNA double-strand breaks in heterochromatin elicit fast repair protein recruitment, histone H2AX phosphorylation and relocation to euchromatin

Jakob, B., Splinter, J., Conrad, S., Voss, K., Zink, D., Durante, M., Löbrich, M., & Taucher-Scholz, G. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr230 · Cited by 312 · see citing works

Neuron-to-neuron wild-type Tau protein transfer through a trans-synaptic mechanism: relevance to sporadic tauopathies

Dujardin, S., Lécolle, K., Caillierez, R., Bégard, S., Zommer, N., Lachaud, C., Carrier, S., Dufour, N., Aurégan, G., Winderickx, J., et al. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-14 · Cited by 259 · see citing works

Protein phosphorylation in neurodegeneration: friend or foe?

Tenreiro, S., Eckermann, K., & Outeiro, T. F. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00042 · Cited by 252 · see citing works

A major role for Tau in neuronal DNA and RNA protection in vivo under physiological and hyperthermic conditions

Violet, M., Delattre, L., Tardivel, M., Sultan, A., Chauderlier, A., Caillierez, R., Talahari, S., Nesslany, F., Lefebvre, B., Bonnefoy, E., et al. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00084 · Cited by 251 · see citing works

A SAP30 Complex Inhibits IFN-β Expression in Rift Valley Fever Virus Infected Cells

May, N. L., Mansuroglu, Z., Léger, P., Josse, T., Blot, G., Billecocq, A., Flick, R., Jacob, Y., Bonnefoy, E., & Bouloy, M. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.0040013 · Cited by 219 · see citing works

SUMOylation promotes de novo targeting of HP1α to pericentric heterochromatin

Maison, C., Bailly, D., Roche, D. M. J., Oca, R. M. D., Probst, A. V., Vassias, I., Dingli, F., Lombard, B., Loew, D., Quivy, J., et al. (2011) · Nature Genetics · doi:10.1038/ng.765 · Cited by 211 · see citing works

Transcription of Satellite III non-coding RNAs is a general stress response in human cells

Valgardsdottir, R., Chiodi, I., Giordano, M., Rossi, A., Bazzini, S., Ghigna, C., Riva, S., & Biamonti, G. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm1056 · Cited by 209 · see citing works

Predictive Atomic Resolution Descriptions of Intrinsically Disordered hTau40 and α-Synuclein in Solution from NMR and Small Angle Scattering

Schwalbe, M., Ozenne, V., Bibow, S., Jaremko, M., Jaremko, Ł., Gajda, M. J., Jensen, M. R., Biernat, J., Becker, S., Mandelkow�, E., et al. (2013) · Structure · doi:10.1016/j.str.2013.10.020 · Cited by 192 · see citing works

Heterochromatic Genome Stability Requires Regulators of Histone H3 K9 Methylation

Peng, J. C., & Karpen, G. H. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000435 · Cited by 183 · see citing works

A transcription factor–based mechanism for mouse heterochromatin formation

Bulut-Karslıoğlu, A., Perrera, V., Scaranaro, M., Rosa-Velázquez, I. A. D. L., van de Nobelen, S., Shukeir, N., Popow, J., Mifsud, B., Opravil, S., Pagani, M., et al. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2382 · Cited by 180 · see citing works

Tau protein binds to pericentromeric DNA: a putative role for nuclear tau in nucleolar organization

Sjöberg, M. K., Shestakova, E., Mansuroglu, Z., Maccioni, R. B., & Bonnefoy, E. (2006) · Journal of Cell Science · doi:10.1242/jcs.02907 · Cited by 166 · see citing works

Beyond the walls of the nucleus: the role of histones in cellular signaling and innate immunityThis paper is one of a selection of papers published in this Special Issue, entitled 27th International West Coast Chromatin and Chromosome Conference, and has undergone the Journal's usual peer review process.

Parseghian, M. H., & Luhrs, K. A. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-082 · Cited by 162 · see citing works

Profiling Murine Tau with 0N, 1N and 2N Isoform-Specific Antibodies in Brain and Peripheral Organs Reveals Distinct Subcellular Localization, with the 1N Isoform Being Enriched in the Nucleus

Liu, C., & Götz, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0084849 · Cited by 155 · see citing works

The impact of heterochromatin on DSB repair

Goodarzi, A. A., Noon, A. T., & Jeggo, P. A. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370569 · Cited by 149 · see citing works

Expression of α- and β-globin genes occurs within different nuclear domains in haemopoietic cells

Brown, K. E., Amoils, S., Horn, J. M., Buckle, V. J., Higgs, D. R., Merkenschlager, M., & Fisher, A. G. (2001) · Nature Cell Biology · doi:10.1038/35078577 · Cited by 146 · see citing works

Proliferation-dependent and cell cycle–regulated transcription of mouse pericentric heterochromatin

Lu, J., & Gilbert, D. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200706176 · Cited by 145 · see citing works

Something Silent This Way Forms: The Functional Organization of the Repressive Nuclear Compartment

Politz, J. C. R., Scalzo, D., & Groudine, M. T. (2013) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101512-122317 · Cited by 132 · see citing works

Binding to the Minor Groove of the Double-Strand, Tau Protein Prevents DNA from Damage by Peroxidation

Wei, Y., Qu, M.-H., Wang, X.-S., Chen, L., Wang, D.-L., Liu, Y., Hua, Q., & He, R.-Q. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002600 · Cited by 129 · see citing works

Transcription of tandemly repetitive DNA: functional roles

Biscotti, M. A., Canapa, A., Forconi, M., Olmo, E., & Barucca, M. (2015) · Chromosome Research · doi:10.1007/s10577-015-9494-4 · Cited by 123 · see citing works

The secret message of heterochromatin: new insights into the mechanisms and function of centromeric and pericentric repeat sequence transcription.

Eymery, A., Callanan, M., & Vourc'h, C. (2009) · International Journal of Developmental Biology · doi:10.1387/ijdb.082673ae · Cited by 120 · see citing works

A transcriptomic analysis of human centromeric and pericentric sequences in normal and tumor cells

Eymery, A., Horard, B., Atifi, M. E., Fourel, G., Berger, F. R., Vitte, A.-L., Broeck, A. V. D., Brambilla, E. M., Fournier, A., Callanan, M. B., et al. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp639 · Cited by 114 · see citing works

Mammalian Su(var) Genes in Chromatin Control

Fodor, B. D., Shukeir, N., Reuter, G., & Jenuwein, T. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.042308.113225 · Cited by 105 · see citing works

Amyloid Precursor Protein (APP) Metabolites APP Intracellular Fragment (AICD), Aβ42, and Tau in Nuclear Roles

Multhaup, G., Huber, O., Buée, L., & Galas, M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.677211 · Cited by 101 · see citing works

Heterochromatin Reorganization during Early Mouse Development Requires a Single-Stranded Noncoding Transcript

Casanova, M., Pasternak, M., Marjou, F. E., Baccon, P. L., Probst, A. V., & Almouzni, G. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.015 · Cited by 98 · see citing works

The Peptidylprolyl cis/trans-Isomerase Pin1 Modulates Stress-induced Dephosphorylation of Tau in Neurons

Galas, M.-C., Dourlen, P., Bégard, S., Ando, K., Blum, D., Hamdane, M., & Buée, L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601849200 · Cited by 97 · see citing works

Specificity, propagation, and memory of pericentric heterochromatin

Müller‐Ott, K., Erdel, F., Matveeva, A., Mallm, J., Rademacher, A., Hahn, M., Bauer, C., Zhang, Q., Kaltofen, S., Schotta, G., et al. (2014) · Molecular Systems Biology · doi:10.15252/msb.20145377 · Cited by 96 · see citing works

The Carboxy-Terminal Acidic Domain of Rift Valley Fever Virus NSs Protein Is Essential for the Formation of Filamentous Structures but Not for the Nuclear Localization of the Protein

Yadani, F.-Z., Kohl, A., Prehaud, C. J. N., Billecocq, A., & Bouloy, M. (1999) · Journal of Virology · doi:10.1128/jvi.73.6.5018-5025.1999 · Cited by 86 · see citing works

Nuclear Magnetic Resonance Spectroscopy Characterization of Interaction of Tau with DNA and Its Regulation by Phosphorylation

Qi, H., Cantrelle, F., Benhelli‐Mokrani, H., Smet‐Nocca, C., Buée, L., Lippens, G. M., Bonnefoy, E., Galas, M., & Landrieu, I. (2015) · Biochemistry · doi:10.1021/bi5014613 · Cited by 83 · see citing works

Characterization and dynamics of pericentromere-associated domains in micePreprint

Wijchers, P. J., Geeven, G., Eyres, M., Bergsma, A. J., Janssen, M., Verstegen, M. J. A. M., Zhu, Y. K., Schell, Y., Vermeulen, C., de Wit, E., et al. (2015) · Genome Research · doi:10.1101/gr.186643.114 · Cited by 82 · see citing works

Diversity in the organization of centromeric chromatin

Steiner, F. A., & Henikoff, S. (2015) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2015.03.010 · Cited by 68 · see citing works

Nonstructural NSs Protein of Rift Valley Fever Virus Interacts with Pericentromeric DNA Sequences of the Host Cell, Inducing Chromosome Cohesion and Segregation Defects

Mansuroglu, Z., Josse, T., Gilleron, J., Billecocq, A., Léger, P., Bouloy, M., & Bonnefoy, E. (2009) · Journal of Virology · doi:10.1128/jvi.01165-09 · Cited by 66 · see citing works

Prefibrillar Tau oligomers alter the nucleic acid protective function of Tau in hippocampal neurons in vivo

Violet, M., Chauderlier, A., Delattre, L., Tardivel, M., Chouala, M. S., Sultan, A., Marciniak, E., Humez, S., Binder, L. I., Kayed, R., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.09.003 · Cited by 66 · see citing works

Nuclear dynamics of radiation-induced foci in euchromatin and heterochromatin

Chiolo, I., Tang, J., Georgescu, W., & Costes, S. V. (2013) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2013.08.001 · Cited by 64 · see citing works

Striatal NELF-mediated RNA polymerase II stalling controls l-dopa induced dyskinesia.

Bastide, M. F., Bido, S., Duteil, N., et al. (2015) · HAL (Le Centre pour la Communication Scientifique Directe) · doi:10.1016/j.nbd · Cited by 64 · see citing works

Aberrant intracellular localization of H3k4me3 demonstrates an early epigenetic phenomenon in Alzheimer's disease

Mastroeni, D., Delvaux, E., Nolz, J., Tan, Y., Grover, A., Oddo, S., & Coleman, P. D. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.08.017 · Cited by 62 · see citing works

Thermodynamics of the Interaction between Alzheimer's Disease Related Tau Protein and DNA

Camero, S., Benítez, M. J., Cuadros, R., Hernández, F., Ávila, J., & Jiménez, J. S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0104690 · Cited by 40 · see citing works

Pericentromeric Heterochromatin Domains Are Maintained without Accumulation of HP1

Langerak, J. M., Brink, M. C., Luijsterburg, M. S., van der Kraan, I., DRIEL, R. V., & Verschure, P. J. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-01-0025 · Cited by 40 · see citing works

Heterochromatin Controls γH2A Localization in Neurospora crassa

Sasaki, T., Lynch, K. L., Mueller, C. V., Friedman, S., Freitag, M., & Lewis, Z. (2014) · Eukaryotic Cell · doi:10.1128/ec.00117-14 · Cited by 32 · see citing works

Binding of YY1 to the Proximal Region of the Murine Beta Interferon Promoter Is Essential To Allow CBP Recruitment and K8H4/K14H3 Acetylation on the Promoter Region after Virus Infection

Benhelli‐Mokrani, H., Dein, O. S. E., Mansuroglu, Z., & Bonnefoy, E. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00420-06 · Cited by 26 · see citing works

Association of the interferon-β gene with pericentromeric heterochromatin is dynamically regulated during virus infection through a YY1-dependent mechanism

Josse, T., Benhelli‐Mokrani, H., Benferhat, R., Shestakova, E. A., Mansuroglu, Z., Kakanakou, H., Billecocq, A., Bouloy, M., & Bonnefoy, E. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks050 · Cited by 13 · see citing works

Transcriptional Activation of Mouse Major Satellite Regions during Neuronal Differentiation

Kishi, Y., Kondo, S., & Gotoh, Y. (2012) · Cell Structure and Function · doi:10.1247/csf.12009 · Cited by 9 · see citing works

Roles of tau protein in health and disease

Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003 · see citing works

The physiological roles of tau and Aβ: implications for Alzheimer’s disease pathology and therapeutics

Kent, S. A., Spires-Jones, T. L., & Durrant, C. S. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02196-w · Cited by 446 · see citing works

Amyloid-β and tau complexity — towards improved biomarkers and targeted therapies

Polanco, J. C., Li, C., Bodea, L., Martínez‐Mármol, R., Meunier, F. A., & Götz, J. (2017) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.162 · Cited by 374 · see citing works

Tau and neuroinflammation: what impact for Alzheimer's disease and tauopathies?

Laurent, C., Buée, L., & Blum, D. (2018) · Biomedical Journal · doi:10.1016/j.bj.2018.01.003 · Cited by 348 · see citing works

Epigenome-wide study uncovers large-scale changes in histone acetylation driven by tau pathology in aging and Alzheimer’s human brains

Klein, H., Aubin, C., Gjoneska, E., Sullivan, S. E., Kaskow, B. J., Tang, A. Y., Smith, R. V., Xu, J., Pfenning, A. R., Bernstein, B., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0291-1 · Cited by 267 · see citing works

A Brief Overview of Tauopathy: Causes, Consequences, and Therapeutic Strategies

Orr, M. E., Sullivan, A. C., & Frost, B. E. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.03.011 · Cited by 232 · see citing works

Loss of Nuclear TDP-43 Is Associated with Decondensation of LINE Retrotransposons

Liu, E. Y., Russ, J., Cali, C. P., Phan, J. M., Amlie-Wolf, A., & Lee, E. B. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.04.003 · Cited by 231 · see citing works

Tau Protein Interaction Partners and Their Roles in Alzheimer’s Disease and Other Tauopathies

Sinsky, J., Pichlerova, K., & Hanes, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179207 · Cited by 220 · see citing works

Atypical, non-standard functions of the microtubule associated Tau protein

Sotiropoulos, I., Galas, M., Silva, J. M., Skoulakis, E. M. C., Wegmann, S., Maina, M. B., Blum, D. L., Sayas, C. L., Mandelkow, E., Mandelkow�, E., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0489-6 · Cited by 207 · see citing works

From the prion-like propagation hypothesis to therapeutic strategies of anti-tau immunotherapy

Colin, M., Dujardin, S., Schraen-Maschke, S., Meno-Tetang, G., Duyckaerts, C., Courade, J.-P., & Buée, L. (2020) · Acta Neuropathologica · doi:10.1007/s00401-019-02087-9 · Cited by 187 · see citing works

Tau Oligomers Neurotoxicity

Niewiadomska, G., Niewiadomski, W., Steczkowska, M., & Gąsiorowska, A. (2021) · Life · doi:10.3390/life11010028 · Cited by 132 · see citing works

Mechanisms of DNA damage-mediated neurotoxicity in neurodegenerative disease

Welch, G., & Tsai, L. (2022) · The EMBO Reports · doi:10.15252/embr.202154217 · Cited by 129 · see citing works

Tau Isoforms: Gaining Insight into MAPT Alternative Splicing

Corsi, A., Bombieri, C., Valenti, M. T., & Romanelli, M. G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315383 · Cited by 118 · see citing works

Contributions of DNA Damage to Alzheimer’s Disease

Lin, X., Kapoor, A., Gu, Y., Chow, M. J., Peng, J., Zhao, K., & Tang, D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051666 · Cited by 117 · see citing works

Reduced repressive epigenetic marks, increased DNA damage and Alzheimer's disease hallmarks in the brain of humans and mice exposed to particulate urban air pollution

Calderón‐Garcidueñas, L., Herrera-Soto, A., Jury, N., Maher, B. A., González-Maciel, A., Reynoso-Robles, R., Ruiz-Rudolph, P., van Zundert, B., & Varela‐Nallar, L. (2020) · Environmental Research · doi:10.1016/j.envres.2020.109226 · Cited by 114 · see citing works

The involvement of tau in nucleolar transcription and the stress response

Maina, M. B., Bailey, L. J., Wagih, S., Biasetti, L., Pollack, S. J., Quinn, J. P., Thorpe, J. R., Doherty, A. J., & Serpell, L. C. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0565-6 · Cited by 109 · see citing works

The Role of Protein Misfolding and Tau Oligomers (TauOs) in Alzheimer′s Disease (AD)

Mroczko, B., Groblewska, M., & Litman‐Zawadzka, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194661 · Cited by 106 · see citing works

Reinstating plasticity and memory in a tauopathy mouse model with an acetyltransferase activator

Chatterjee, S., Cassel, R., Schneider‐Anthony, A., Mérienne, K., Cosquer, B., Tzeplaeff, L., Sinha, S. H., Kumar, M., Chaturbedy, P., Eswaramoorthy, M., et al. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201708587 · Cited by 95 · see citing works

Proteostasis and lysosomal repair deficits in transdifferentiated neurons of Alzheimer’s disease

Chou, C.-C., Vest, R., Prado, M. A., Wilson-Grady, J., Paulo, J. A., Shibuya, Y., Moran-Losada, P., Lee, T.-T., Luo, J., Gygi, S. P., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01623-y · Cited by 94 · see citing works

Alzheimer's Disease-like Paired Helical Filament Assembly from Truncated Tau Protein Is Independent of Disulfide Crosslinking

Al‐Hilaly, Y. K., Pollack, S. J., Vadukul, D. M., Citossi, F., Rickard, J. E., Simpson, M. C., Storey, J. M. D., Harrington, C. R., Wischik, C. M., & Serpell, L. C. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.09.007 · Cited by 91 · see citing works

Early Life Stress and Epigenetics in Late-onset Alzheimer’s Dementia: A Systematic Review

Lemche, E. (2018) · Current Genomics · doi:10.2174/1389202919666171229145156 · Cited by 82 · see citing works

Pathogenic tau accelerates aging-associated activation of transposable elements in the mouse central nervous system

Ramirez, P., Zuniga, G., Sun, W., Beckmann, A., Ochoa, E., DeVos, S. L., Hyman, B., Chiu, G., Roy, E. R., Cao, W., et al. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2021.102181 · Cited by 79 · see citing works

Tau: A Signaling Hub Protein

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 78 · see citing works

Current directions in tau research: Highlights from Tau 2020

Sexton, C. E., Snyder, H. M., Beher, D., Boxer, A. L., Brannelly, P., Brion, J., Buée, L., Cacace, A. M., Chételat, G., Citron, M., et al. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12452 · Cited by 78 · see citing works

Update on tauopathies

Lebouvier, T., Pasquier, F., & Buée, L. (2017) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000502 · Cited by 68 · see citing works

Transposable elements as new players in neurodegenerative diseases

Ravel‐Godreuil, C., Znaidi, R., Bonnifet, T., Joshi, R. L., & Fuchs, J. (2021) · FEBS Letters · doi:10.1002/1873-3468.14205 · Cited by 67 · see citing works

Tau, microtubule dynamics, and axonal transport: New paradigms for neurodegenerative disease

Cario, A., & Berger, C. L. (2023) · BioEssays · doi:10.1002/bies.202200138 · Cited by 64 · see citing works

Characterization of tau binding by gosuranemab

Sopko, R., Golonzhka, O., Arndt, J. W., Quan, C., Czerkowicz, J., Cameron, A., Smith, B., Yogapriya, M., Gibbons, G. S., Kim, S., et al. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105120 · Cited by 64 · see citing works

Phosphorylation and O-GlcNAcylation of the PHF-1 Epitope of Tau Protein Induce Local Conformational Changes of the C-Terminus and Modulate Tau Self-Assembly Into Fibrillar Aggregates

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 62 · see citing works

Alzheimer’s disease and related tauopathies: disorders of disrupted neuronal identity

Frost, B. E. (2023) · Trends in Neurosciences · doi:10.1016/j.tins.2023.07.006 · Cited by 56 · see citing works

The impact of histone post-translational modifications in neurodegenerative diseases

Cobos, S. N., Bennett, S. A., & Torrente, M. P. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.10.019 · Cited by 53 · see citing works

Phosphorylation regulates tau’s phase separation behavior and interactions with chromatin

Abasi, L. S., Elathram, N., Movva, M., Deep, A., Corbett, K. D., & Debelouchina, G. T. (2024) · Communications Biology · doi:10.1038/s42003-024-05920-4 · Cited by 52 · see citing works

Genome-wide identification of genic and intergenic neuronal DNA regions bound by Tau protein under physiological and stress conditions

Benhelli‐Mokrani, H., Mansuroglu, Z., Chauderlier, A., Albaud, B., Gentien, D., Sommer, S., Schirmer, C., Laqueuvre, L. M., Josse, T., Buée, L., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky929 · Cited by 52 · see citing works

Aging dependent effect of nuclear tau

Gil, L., Federico, C., Pinedo, F., Bruno, F., Poves, A. B. R., Montoya, J. J., Olazabal, I. M., Ferrer, I., & Saccone, S. (2017) · Brain Research · doi:10.1016/j.brainres.2017.09.030 · Cited by 50 · see citing works

Neuronal nuclear tau and neurodegeneration

Antón‐Fernández, A., Vallés‐Saiz, L., Ávila, J., & Hernández, F. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.07.015 · Cited by 44 · see citing works

Tau and DNA Damage in Neurodegeneration

Colnaghi, L., Rondelli, D., Muzi-Falconi, M., & Sertic, S. (2020) · Brain Sciences · doi:10.3390/brainsci10120946 · Cited by 42 · see citing works

Nuclear Transport Deficits in Tau-Related Neurodegenerative Diseases

Diez, L., & Wegmann, S. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.01056 · Cited by 40 · see citing works

Tau Modulates mRNA Transcription, Alternative Polyadenylation Profiles of hnRNPs, Chromatin Remodeling and Spliceosome Complexes

Montalbano, M., Jaworski, E. A., García, S., Ellsworth, A., McAllen, S., Routh, A. L., & Kayed, R. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.742790 · Cited by 39 · see citing works

Cellular Senescence as the Key Intermediate in Tau-Mediated Neurodegeneration

Mendelsohn, A. R., & Larrick, J. W. (2018) · Rejuvenation Research · doi:10.1089/rej.2018.2155 · Cited by 39 · see citing works

The Involvement of Aβ42 and Tau in Nucleolar and Protein Synthesis Machinery Dysfunction

Maina, M. B., Bailey, L. J., Doherty, A. J., & Serpell, L. C. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00220 · Cited by 38 · see citing works

Tau Mutations Serve as a Novel Risk Factor for Cancer

Rossi, G., Redaelli, V., Contiero, P., Fabiano, S., Tagliabue, G., Perego, P., Benussi, L., Bruni, A. C., Filippini, G., Farinotti, M., et al. (2018) · Cancer Research · doi:10.1158/0008-5472.can-17-3175 · Cited by 37 · see citing works

Monitoring Histone Methylation (H3K9me3) Changes in Live Cells

Sánchez, O. F., Mendonca, A., Min, A., Liu, J., & Yuan, C. (2019) · ACS Omega · doi:10.1021/acsomega.9b01413 · Cited by 37 · see citing works

What’s in a Gene? The Outstanding Diversity of MAPT

Ruiz-Gabarre, D., Carnero-Espejo, A., Ávila, J., & García‐Escudero, V. (2022) · Cells · doi:10.3390/cells11050840 · Cited by 37 · see citing works

Aggregation, Transmission, and Toxicity of the Microtubule-Associated Protein Tau: A Complex Comprehension

Hu, J., Sha, W., Yuan, S., Wu, J., & Huang, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241915023 · Cited by 35 · see citing works

Brain-derived tau oligomer polymorphs: distinct aggregations, stability profiles, and biological activities

Cascio, F. L., Park, S., Sengupta, U., Puangmalai, N., Bhatt, N. N., Shchankin, N., Jerez, C., Moreno, N., Bittar, A., Xavier, R., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-07499-w · Cited by 35 · see citing works

Neurodegenerative Disease-Related Proteins within the Epidermal Layer of the Human Skin

Åkerman, S., Hossain, S., Shobo, A., Zhong, Y., Jourdain, R., Hancock, M. A., George, K. M., Breton, L., & Multhaup, G. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-181191 · Cited by 35 · see citing works

Cancer-specific association between Tau (MAPT) and cellular pathways, clinical outcome, and drug response

Callari, M., Sola, M., Magrin, C., Rinaldi, A., Bolis, M., Paganetti, P., Colnaghi, L., & Papin, S. (2023) · Scientific Data · doi:10.1038/s41597-023-02543-y · Cited by 35 · see citing works

Perinuclear Lamin A and Nucleoplasmic Lamin B2 Characterize Two Types of Hippocampal Neurons through Alzheimer’s Disease Progression

Gil, L., Niño, S. A., Chi-Ahumada, É., Rodríguez‐Leyva, I., Guerrero, C., Poves, A. B. R., Navalón, J. A. A., & Jiménez-Capdeville, M. E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051841 · Cited by 34 · see citing works

Widespread loss of the silencing epigenetic mark H3K9me3 in astrocytes and neurons along with hippocampal-dependent cognitive impairment in C9orf72 BAC transgenic mice

Jury, N., Abarzúa, S., Díaz, I. D. P., Guerra, M. V., Ampuero, E., Cubillos, P., Martínez, P., Herrera-Soto, A., Arredondo, C., Rojas, F., et al. (2020) · Clinical Epigenetics · doi:10.1186/s13148-020-0816-9 · Cited by 34 · see citing works

Tau; One Protein, So Many Diseases

Tabeshmehr, P., & Eftekharpour, E. (2023) · Biology · doi:10.3390/biology12020244 · Cited by 33 · see citing works

Nuclear face of Tau: an inside player in neurodegeneration

Younas, N., Saleem, T., Younas, A., & Zerr, I. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01702-x · Cited by 33 · see citing works

Complicated Role of Post-translational Modification and Protease-Cleaved Fragments of Tau in Alzheimer’s Disease and Other Tauopathies

Yang, J., Shen, N., Shen, J., Yang, Y., & Li, H.-L. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03867-x · Cited by 32 · see citing works

Tau-Targeted Therapeutic Strategies: Mechanistic Targets, Clinical Pipelines, and Analysis of Failures

Shen, X., Li, H., Zhang, B., Li, Y., & Zhu, Z. (2025) · Cells · doi:10.3390/cells14191506 · Cited by 32 · see citing works

Phosphorylated tau exhibits antimicrobial activity capable of neutralizing herpes simplex virus 1 infectivity in human neurons

Eimer, W. A., Rodriguez, A. S., DeFao, M. T., Ehricke, S., Park, J., Kumar, D. K. V., Shanmugam, N. K. N., Singh, S., Sawhney, T., Moir, R. D., et al. (2025) · Nature Neuroscience · doi:10.1038/s41593-025-02157-0 · Cited by 29 · see citing works

Vascular and Nonvascular Mechanisms of Cognitive Impairment and Dementia

Kara, B., Gordon, M. N., Gifani, M., Dorrance, A. M., & Counts, S. (2022) · Clinics in Geriatric Medicine · doi:10.1016/j.cger.2022.07.006 · Cited by 29 · see citing works

Tau promotes oxidative stress-associated cycling neurons in S phase as a pro-survival mechanism: Possible implication for Alzheimer’s disease

Denéchaud, M., Geurs, S., Comptdaer, T., Bégard, S., García-Núñez, A., Pechereau, L.-A., Bouillet, T., Vermeiren, Y., Deyn, P. P. D., Perbet, R., et al. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102386 · Cited by 29 · see citing works

Aging and Alzheimer’s disease connection: Nuclear Tau and lamin A

Gil, L., Niño, S. A., Capdeville, G., & Jiménez-Capdeville, M. E. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.135741 · Cited by 29 · see citing works

Transcriptome analyses reveal tau isoform-driven changes in transposable element and gene expression

Grundman, J., Spencer, B., Sarsoza, F., & Rissman, R. A. (2021) · PLOS ONE · doi:10.1371/journal.pone.0251611 · Cited by 27 · see citing works

Neurodegeneration caused by S1P-lyase deficiency involves calcium-dependent tau pathology and abnormal histone acetylation

Alam, S., Piazzesi, A., Abd El Fatah, M., Raucamp, M., & van Echten-Deckert, G. (2020) · Cells · doi:10.3390/cells9102189 · Cited by 26 · see citing works

Tau Stabilizes Chromatin Compaction

Rico, T., Gilles, M., Chauderlier, A., Comptdaer, T., Magnez, R., Chwastyniak, M., Drobecq, H., Pinet, F., Thuru, X., Buée, L., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.740550 · Cited by 26 · see citing works

KDM6B cooperates with Tau and regulates synaptic plasticity and cognition via inducing VGLUT1/2

Wang, Y., Khandelwal, N., Liu, S., Zhou, M., Bao, L., Wang, J. E., Kumar, A., Xing, C., Gibson, J. R., & Wang, Y. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01750-0 · Cited by 25 · see citing works

Importin-Mediated Pathological Tau Nuclear Translocation Causes Disruption of the Nuclear Lamina, TDP-43 Mislocalization and Cell Death

Candia, R. F., Cohen, L. S., Morozova, V., Corbo, C. P., & Alonso, A. D. C. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.888420 · Cited by 24 · see citing works

Moesin is an effector of tau-induced actin overstabilization, cell cycle activation, and neurotoxicity in Alzheimer’s disease

Beckmann, A., Ramirez, P., Gamez, M., Gonzalez, E. M., Mange, J. D., Bieniek, K. F., Ray, W. J., & Frost, B. E. (2023) · iScience · doi:10.1016/j.isci.2023.106152 · Cited by 24 · see citing works

Tau/DDX6 interaction increases microRNA activity

Chauderlier, A., Gilles, M., Špolcová, A., Caillierez, R., Chwastyniak, M., Kress, M., Drobecq, H., Bonnefoy, E., Pinet, F., Barbieri-Weill, D., et al. (2018) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2018.06.006 · Cited by 24 · see citing works

Tau Interacting Proteins: Gaining Insight into the Roles of Tau in Health and Disease

Stancu, I., Ferraiolo, M., Terwel, D., & Dewachter, I. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_13 · Cited by 23 · see citing works

H3K9 Methyltransferases Suv39h1 and Suv39h2 Control the Differentiation of Neural Progenitor Cells in the Adult Hippocampus

Guerra, M. V., Cáceres, M. I., Herrera-Soto, A., Arredondo, S. B., Varas‐Godoy, M., van Zundert, B., & Varela‐Nallar, L. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.778345 · Cited by 23 · see citing works

Epigenetic mechanisms underlying enhancer modulation of neuronal identity, neuronal activity and neurodegeneration

Alcalá‐Vida, R., Awada, A., Boutillier, A., & Mérienne, K. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105155 · Cited by 22 · see citing works

Single‐Cell Patch‐Clamp/Proteomics of Human Alzheimer's Disease iPSC‐Derived Excitatory Neurons Versus Isogenic Wild‐Type Controls Suggests Novel Causation and Therapeutic Targets

Ghatak, S., Diedrich, J. K., Talantova, M. V., Bhadra, N., Scott, H. R., Sharma, M., Albertolle, M. E., Schork, N. J., Yates, J. R., & Lipton, S. A. (2024) · Advanced Science · doi:10.1002/advs.202400545 · Cited by 22 · see citing works

Epigenetic Changes and Chromatin Reorganization in Brain Function: Lessons from Fear Memory Ensemble and Alzheimer’s Disease

van Zundert, B., & Montecino, M. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012081 · Cited by 21 · see citing works

DNA repair deficiencies and neurodegeneration

Ropert, B., Gallrein, C., & Schumacher, B. (2024) · DNA repair · doi:10.1016/j.dnarep.2024.103679 · Cited by 21 · see citing works

Roles of Topoisomerases in Heterochromatin, Aging, and Diseases

Lee, S. K., & Wang, W. (2019) · Genes · doi:10.3390/genes10110884 · Cited by 20 · see citing works

Minding the Gap: Exploring Neuroinflammatory and Microglial Sex Differences in Alzheimer’s Disease

Reed-Geaghan, E. G., & Keller-Norrell, P. R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417377 · Cited by 19 · see citing works

Phosphorylated nucleolar Tau protein is related to the neuronal in vitro differentiation

Federico, C., Gil, L., Bruno, F., D’Amico, A. G., D’Agata, V., & Saccone, S. (2018) · Gene · doi:10.1016/j.gene.2018.04.051 · Cited by 19 · see citing works

Solid-state NMR of paired helical filaments formed by the core tau fragment tau(297-391)

Al‐Hilaly, Y. K., Hurt, C., Rickard, J. E., Harrington, C. R., Storey, J. M. D., Wischik, C. M., Serpell, L. C., & Siemer, A. B. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.988074 · Cited by 19 · see citing works

Epigenetics in Neurodegenerative Diseases

van Zundert, B., & Montecino, M. A. (2025) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-75980-2_3 · Cited by 18 · see citing works

Tau: More than a microtubule‐binding protein in neurons

Alonso, A. D. C., Idrissi, A. E., Candia, R. F., Morozova, V., & Kleiman, F. E. (2023) · Cytoskeleton · doi:10.1002/cm.21795 · Cited by 17 · see citing works

Genome anchoring to nuclear landmarks drives functional compartmentalization of the nuclear space

Canat, A., Veillet, A., Bonnet, A., & Therizols, P. (2020) · Briefings in Functional Genomics · doi:10.1093/bfgp/elz034 · Cited by 17 · see citing works

Phospho-Tau and Chromatin Landscapes in Early and Late Alzheimer’s Disease

Gil, L., Niño, S. A., Guerrero, C., & Jiménez-Capdeville, M. E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910283 · Cited by 15 · see citing works

Histone post-translational modification and heterochromatin alterations in neurodegeneration: revealing novel disease pathways and potential therapeutics

Fisher, R. M. A., & Torrente, M. P. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1456052 · Cited by 14 · see citing works

Pathogenesis of Alzheimer's disease and therapeutic strategies involving traditional Chinese medicine

Li, S., & Yang, J. (2024) · RSC Medicinal Chemistry · doi:10.1039/d4md00660g · Cited by 14 · see citing works

Tau oligomers accumulation sensitizes prostate cancer cells to docetaxel treatment

Martellucci, S., Clementi, L., Sabetta, S., Muzi, P., Mattei, V., Bologna, M., & Angelucci, A. (2021) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-021-03598-3 · Cited by 14 · see citing works

DNA Damage and Chromatin Rearrangement Work Together to Promote Neurodegeneration

Sharma, H., Koirala, S., Chew, Y. L., & Konopka, A. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04331-0 · Cited by 13 · see citing works

Emerging Connections Between Tau and Nucleic Acids

Galas, M., Bonnefoy, E., Buée, L., & Lefebvre, B. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_12 · Cited by 13 · see citing works

P301L tau mutation leads to alterations of cell cycle, DNA damage response and apoptosis: Evidence for a role of tau in cancer

Cimini, S., Giaccone, G., Tagliavini, F., Costantino, M., Perego, P., & Rossi, G. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115043 · Cited by 12 · see citing works

A Closer Look into the Role of Protein Tau in the Identification of Promising Therapeutic Targets for Alzheimer’s Disease

Khan, R. I., Nirzhor, S. S. R., & Rashid, B. (2018) · Brain Sciences · doi:10.3390/brainsci8090162 · Cited by 12 · see citing works

TDP-43 in Alzheimer's disease: Pathophysiology and therapeutic strategies

Zhou, X., Lin, X., He, Y., Huang, N., & Luo, Y. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.107977 · Cited by 11 · see citing works

Pathological Nuclear Hallmarks in Dentate Granule Cells of Alzheimer’s Patients: A Biphasic Regulation of Neurogenesis

Gil, L., Chi-Ahumada, É., Niño, S. A., Capdeville, G., Méndez-Torres, A. M., Guerrero, C., Poves, A. B. R., Olazabal, I. M., & Jiménez-Capdeville, M. E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112873 · Cited by 10 · see citing works

New approaches for understanding the potential role of microbes in Alzheimer's disease

Whitson, H. E., Banks, W. A., Diaz, M. M., Frost, B. E., Kellis, M., Lathe, R., Schmader, K. E., Spudich, S., Tanzi, R. E., & Garden, G. A. (2024) · Brain Behavior & Immunity - Health · doi:10.1016/j.bbih.2024.100743 · Cited by 8 · see citing works

The enigma of mitochondrial epigenetic alterations in air pollution-induced neurodegenerative diseases

Acharyya, S., Kumar, S. H., Chouksey, A., Soni, N., Nazeer, N., & Mishra, P. K. (2024) · NeuroToxicology · doi:10.1016/j.neuro.2024.10.002 · Cited by 8 · see citing works

Looking at Alzheimer’s Disease Pathogenesis from the Nuclear Side

D’Andrea, L., Stringhi, R., Luca, M. D., & Marcello, E. E. (2021) · Biomolecules · doi:10.3390/biom11091261 · Cited by 8 · see citing works

DAXX safeguards heterochromatin formation in embryonic stem cells

Canat, A., Veillet, A., Batrin, R., Dubourg, C., Lhoumaud, P., Arnau-Romero, P., Greenberg, M., Bonhomme, F., Arimondo, P. B., Illingworth, R. S., et al. (2023) · Journal of Cell Science · doi:10.1242/jcs.261092 · Cited by 7 · see citing works

Phosphorylated-tau associates with HSV-1 chromatin and correlates with nuclear speckles decondensation in low-density host chromatin regions

D’Aiuto, L., Caldwell, J. K., Edwards, T. G., Zhou, C., McDonald, M. L., Maio, R. D., Joel, W., Hyde, V. R., Wallace, C. T., Watkins, S. C., et al. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106804 · Cited by 7 · see citing works

Differential Epigenetic Changes in the Dorsal Hippocampus of Male and Female SAMP8 Mice: A Preliminary Study

Ravanelli, F., Musazzi, L., Barbieri, S. S., Rovati, G. E., Popoli, M., Barbon, A., & Ieraci, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713084 · Cited by 6 · see citing works

A novel derivative of evodiamine improves cognitive impairment and synaptic integrity in AD mice

Wan, Y.-C., Yang, Y., Pang, S., & Kong, Z. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117103 · Cited by 6 · see citing works

The role of non-enzymatic glycation on Tau-DNA interactions: Kinetic and mechanistic approaches

Yekta, R., Sadeghi, L., & Dehghan, G. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.02.178 · Cited by 6 · see citing works

Tau mediates the reshaping of the transcriptional landscape toward intermediate Alzheimer’s disease stages

Siano, G., Varisco, M., Terrigno, M., Wang, C., Scarlatti, A., Iannone, V., Groth, M., Galas, M., Hoozemans, J. J. M., Cellerino, A., et al. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1459573 · Cited by 5 · see citing works

Exploration of common pathogenic genes between cerebral amyloid angiopathy and insomnia based on bioinformatics and experimental validation

Li, X., Li, K., Wei, Y., Yu, W.-K., Wu, J., Gao, K., He, W., Niu, P., Zhang, C., Cheng, Y. B., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-12553-y · Cited by 5 · see citing works

Profiling inflammatory mechanisms, hyperphosphorylated tau of hippocampal tissue and spatial memory following vitamin D3 treatment in the mice model of vascular dementia

Sadeghzadeh, J., Jafarzadeh, J., Hadinezhad, P., Nazari, A., Sohrabi, S., Musazadeh, V., Barzegar, A., & Shahabi, P. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.110314 · Cited by 5 · see citing works

Cell Cycle Reactivation, at the Start of Neurodegeneration, Induced by Forskolin and Aniline in Differentiated Neuroblastoma Cells

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 · see citing works

Chromatin Changes Associated with Neuronal Maintenance and Their Pharmacological Application

Lee, J. H., Kim, J., Kim, S., Cho, K. S., & Lee, S. B. (2017) · Current Neuropharmacology · doi:10.2174/1570159x15666170601124220 · Cited by 5 · see citing works

Tau promotes neurodegeneration through global chromatin relaxation

Frost, B., Hemberg, M., Lewis, J., & Feany, M. B. (2014) · Nature Neuroscience · doi:10.1038/nn.3639 · Cited by 519 · see citing works

Tau protein binds to pericentromeric DNA: a putative role for nuclear tau in nucleolar organization

Sjöberg, M. K., Shestakova, E., Mansuroglu, Z., Maccioni, R. B., & Bonnefoy, E. (2006) · Journal of Cell Science · doi:10.1242/jcs.02907 · Cited by 166 · see citing works

Epigenome-wide study uncovers large-scale changes in histone acetylation driven by tau pathology in aging and Alzheimer’s human brains

Klein, H., Aubin, C., Gjoneska, E., Sullivan, S. E., Kaskow, B. J., Tang, A. Y., Smith, R. V., Xu, J., Pfenning, A. R., Bernstein, B., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0291-1 · Cited by 267 · see citing works

Phospho-Tau and Chromatin Landscapes in Early and Late Alzheimer’s Disease

Gil, L., Niño, S. A., Guerrero, C., & Jiménez-Capdeville, M. E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910283 · Cited by 15 · see citing works

P2–064: The tau protein: From physiological to pathological process in Alzheimer's disease

Flores, P., López, R. M., Florán, B., Segovia‐Vila, J., & Luna‐Muñoz, J. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.05.707