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Specific binding of Hsp27 and phosphorylated Tau mitigates abnormal Tau aggregation-induced pathology

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Tau phosphorylation in the mouse brain during aversive conditioning

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Phosphorylation of the tau protein sequence 199–205 in the hippocampal CA3 region of Syrian hamsters in adulthood and during aging

Härtig, W., Oklejewicz, M., Strijkstra, A. M., Boerema, A. S., Stieler, J., & Arendt, T. (2005) · Brain Research · doi:10.1016/j.brainres.2005.07.017 · Cited by 24

Pathogenic tau recruits wild-type tau into brain inclusions and induces gut degeneration in transgenic SPAM mice

Xia, Y., Prokop, S., Bell, B. M., Gorion, K.-M. M., Croft, C. L., Nasif, L. H., Xu, G. M., Riffe, C. J., Manaois, A. N., Strang, K. H., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03373-1 · Cited by 24

Postmortem Brain Imaging in Alzheimer’s Disease and Related Dementias: The South Texas Alzheimer’s Disease Research Center Repository

Li, K., Rashid, T., Li, J., Honnorat, N., Nirmala, A. B., Fadaee, E., Wang, D., Charisis, S., Liu, H., Franklin, C. G., et al. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230389 · Cited by 25

Involvement of Precerebellar Nuclei in Pick's Disease

Braak, H., & Braak, E. (1998) · Experimental Neurology · doi:10.1006/exnr.1998.6895 · Cited by 23

Physiologically relevant factors influence tau phosphorylation by leucine‐rich repeat kinase 2

Hamm, M. J., Bailey, R. M., Shaw, G., Yen, S.-H. C., Lewis, J. M., & Giasson, B. I. (2015) · Journal of Neuroscience Research · doi:10.1002/jnr.23614 · Cited by 23

Expression of Concern: High specificity of widely used phospho‐tau antibodies validated using a quantitative whole‐cell based assay

Li, D., & Cho, Y. K. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14830 · Cited by 23

Tau assemblies do not behave like independently acting prion-like particles in mouse neural tissue

Mukadam, A. S., Miller, L. V. C., Durrant, C. S., Vaysburd, M. J., Katsinelos, T., Tuck, B. J., Sanford, S., Sheppard, O., Knox, C., Cheng, S., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01141-6 · Cited by 23

Differential phosphorylation of tau proteins during kitten brain development and Alzheimer's disease

Riederer, B. M., Mourton-Gilles, C., Frey, P., Delacourte, A., & Probst, A. (2001) · Journal of Neurocytology · doi:10.1023/a:1011991207942 · Cited by 22

P301L tauopathy

Adamec, E., Murrell, J. R., Takao, M., Hobbs, W., Nixon, R. A., Ghetti, B. F., & Vonsattel, J. P. (2002) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(02)00150-8 · Cited by 22

Pathogenic tau modifications occur in axons before the somatodendritic compartment in mossy fiber and Schaffer collateral pathways

Christensen, K. R., Beach, T. G., Serrano, G. E., & Kanaan, N. M. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0675-9 · Cited by 23

Cyclin-dependent kinase 5 colocalizes with phosphorylated tau in human inclusion-body myositis paired-helical filaments and may play a role in tau phosphorylation

Wilczynski, G. M., Engel, W. K., & Askanas, V. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01485-3 · Cited by 21

Morphine and HIV-1 Tat interact to cause region-specific hyperphosphorylation of tau in transgenic mice

Ohene‐Nyako, M., Nass, S. R., Hahn, Y. K., Knapp, P. E., & Hauser, K. F. (2020) · Neuroscience Letters · doi:10.1016/j.neulet.2020.135502 · Cited by 20

Tau Protein Binding Modes in Alzheimer’s Disease for Cationic Luminescent Ligands

Todarwal, Y., Gustafsson, C., Minh, N. N. T., Ertzgaard, I., Klingstedt, T., Ghetti, B. F., Vidal, R., König, C., Lindgren, M., Nilsson, K. P. R., et al. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c06019 · Cited by 20

Brain vasculature accumulates tau and is spatially related to tau tangle pathology in Alzheimer’s disease

Hoglund, Z. T., Ruiz‐Uribe, N. E., del Sastre, E., Woost, B., Bader, E., Bailey, J. J., Hyman, B. T., Zwang, T. J., & Bennett, R. E. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02751-9 · Cited by 22

SAR110894, a potent histamine H3‐receptor antagonist, displays disease‐modifying activity in a transgenic mouse model of tauopathy

Delay‐Goyet, P., Blanchard, V., Schussler, N., Lopez‐Grancha, M., Ménager, J., Mary, V., Sultan, E., Buzy, A., Guillemot, J.-C., Stemmelin, J., et al. (2016) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2016.10.002 · Cited by 20

LRRK2, alpha-synuclein, and tau: partners in crime or unfortunate bystanders?

Outeiro, T. F., Harvey, K., Dominguez‐Meijide, A., & Gerhardt, E. (2019) · Biochemical Society Transactions · doi:10.1042/bst20180466 · Cited by 20

β-Protein/A4 deposits are not associated with hyperphosphorylated tau in somatostatin neurons in the hypothalamus of Alzheimer’s disease patients

van de Nes, J. A. P., Konermann, S., Nafe, R., & Swaab, D. F. (2006) · Acta Neuropathologica · doi:10.1007/s00401-005-0018-8 · Cited by 19

Tau phosphorylation in cells transfected with wild-type or an Alzheimer's disease mutant Presenilin 1

Irving, N. G., & Miller, C. C. J. (1997) · Neuroscience Letters · doi:10.1016/s0304-3940(97)13343-2 · Cited by 20

Pyramidal cell axon initial segment in Alzheimer´s disease

Antón‐Fernández, A., León‐Espinosa, G., DeFelipe, J., & Muñoz, A. (2022) · Scientific Reports · doi:10.1038/s41598-022-12700-9 · Cited by 21

Activation of TNF Receptor 2 Improves Synaptic Plasticity and Enhances Amyloid-β Clearance in an Alzheimer’s Disease Mouse Model with Humanized TNF Receptor 2

Ortí-Casañ, N., Wajant, H., Kuiperij, H. B., Hooijsma, A., Tromp, L., Poortman, I. L., Tadema, N., de Lange, J. H. E., Verbeek, M. M., Deyn, P. P. D., et al. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-221230 · Cited by 20

Modelling of amyloid β-peptide induced lesions using roller-drum incubation of hippocampal slice cultures from neonatal rats

Johansson, S. M., Radesäter, A., Cowburn, R. F., Thyberg, J., & Luthman, J. (2005) · Experimental Brain Research · doi:10.1007/s00221-005-0069-z · Cited by 19

Regional Analysis of Differently Phosphorylated Tau Proteins in Brains from Patients with Alzheimer’s Disease

Nakano, H., Kobayashi, K., Sugimori, K., Shimazaki, M., Miyazu, K., Hayashi, M., & Furuta, H. (2004) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000076344 · Cited by 19

Pharmacologic reversal of advanced Alzheimer’s disease in mice and identification of potential therapeutic nodes in human brain

Chaubey, K., Vázquez‐Rosa, E., Tripathi, S. J., Shin, M., Yu, Y., Dhar, M., Chakraborty, S., Yamakawa, M., Wang, X., Sridharan, P. S., et al. (2025) · Cell Reports Medicine · doi:10.1016/j.xcrm.2025.102535 · Cited by 21

Mutation ∆K281 in MAPT causes Pick’s disease

Schweighauser, M., Garringer, H. J., Klingstedt, T., Nilsson, K. P. R., Masuda‐Suzukake, M., Murrell, J. R., Risacher, S. L., Vidal, R., Scheres, S. H. W., Goedert, M., et al. (2023) · Acta Neuropathologica · doi:10.1007/s00401-023-02598-6 · Cited by 18

Sequence and trajectory of early Alzheimer’s disease-related tau inclusions in the hippocampal formation of cases without amyloid-β deposits

Braak, H., Mayer, B., Feldengut, S., Schön, M., & Tredici, K. D. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02862-x · Cited by 20

Peripheral nervous system effects in the PS19 tau transgenic mouse model of tauopathy

Merchán‐Rubira, J., Sebastián‐Serrano, Á., Dı́az-Hernández, M., Ávila, J., & Hernández, F. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.01.031 · Cited by 18

An autopsy report of three kindred in a Gerstmann–Sträussler–Scheinker disease P105L family with a special reference to prion protein, tau, and beta‐amyloid

Ishizawa, K., Mitsufuji, T., Shioda, K., Kobayashi, A., Komori, T., Nakazato, Y., Kitamoto, T., Araki, N., Yamamoto, T., & Sasaki, A. (2018) · Brain and Behavior · doi:10.1002/brb3.1117 · Cited by 17

Epitope mapping of mAbs AT8 and Tau5 directed against hyperphosphorylated regions of the human tau protein

Porzig, R., Singer, D. L., & Hoffmann, R. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.187 · Cited by 117

P2‐125: Characterization of phosphorylation‐dependent monoclonal anti‐tau antibodies

Porzig, R., Singer, D. L., & Hoffmann, R. (2008) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2008.05.1199

Epitope mapping and structural basis for the recognition of phosphorylated tau by the anti‐tau antibody AT8

Malia, T., Teplyakov, A., Ernst, R., Wu, S., Lacy, E. R., Liu, X., Vandermeeren, M., Mercken, M. H., Luo, J., Sweet, R. W., et al. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24988 · Cited by 144

The switch of tau protein to an Alzheimer‐like state includes the phosphorylation of two serine‐proline motifs upstream of the microtubule binding region.

Biernat, J., Mandelkow, E. M., Schröter, C., Lichtenberg‐Kraag, B., Steiner, B., Berling, B., Meyer, H., Mercken, M., Vandermeeren, A., & Goedert, M. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05204.x · Cited by 484

Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: identification of phosphorylation sites in tau protein

Goedert, M., Jakes, R., Crowther, R. A., Cohen, P., Vanmechelen, E., Vandermeeren, M., & Cras, P. (1994) · Biochemical Journal · doi:10.1042/bj3010871 · Cited by 375