Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205

Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492

A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau

Lee, V. M.-Y., Balin, B. J., Otvos, L., & Trojanowski, J. Q. (1991) · Science · doi:10.1126/science.1899488 · Cited by 1,418

Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization.

Goedert, M., & Jakes, R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07870.x · Cited by 929

Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding

Bramblett, G. T., Goedert, M., Jakes, R., Merrick, S. E., Trojanowski, J. Q., & Lee, V. M. Y. (1993) · Neuron · doi:10.1016/0896-6273(93)90057-x · Cited by 903

Inactivation of glycogen synthase kinase-3 β by phosphorylation: new kinase connections in insulin and growth-factor signalling

Sutherland, C., Leighton, I. A., & Cohen, P. (1993) · Biochemical Journal · doi:10.1042/bj2960015 · Cited by 903

A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads

Braak, F., Braak, H., & Mandelkow, E. (1994) · Acta Neuropathologica · doi:10.1007/bf00293315 · Cited by 769

Tau protein and the neurofibrillary pathology of Alzheimer's disease

Goedert, M. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90078-z · Cited by 721

Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau.

Matsuo, E. S., Shin, R., Billingsley, M., de Voorde, A. V., O'Connor, M., Trojanowski, J., & Lee, V. (1994) · Neuron · doi:10.1016/0896-6273(94)90264-x · Cited by 588

Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer‐like state.

Drewes, G., Lichtenberg‐Kraag, B., Döring, F., Mandelkow, E. M., Biernat, J., Goris, J., Dorée, M., & Mandelkow, E. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05272.x · Cited by 565

Glycogen synthase kinase‐3 and the Alzheimer‐like state of microtubule‐associated protein tau

Mandelkow, E.-M., Drewes, G., Biernat, J., Gustke, N., Van Lint, J., Vandenheede, J. R., & Mandelkow, E. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81496-9 · Cited by 515

Pathogenic Tau Protein Species: Promising Therapeutic Targets for Ocular Neurodegenerative Diseases

Mishan, M. A., Kanavi, M. R., Shahpasand, K., & Ahmadieh, H. (2019) · Journal of Ophthalmic and Vision Research · doi:10.18502/jovr.v14i4.5459 · Cited by 18

6-Hydroxydopamine-Induced Lesions of Dopaminergic Neurons Alter the Function of Postsynaptic Cholinergic Neurons without Changing Cytoskeletal Proteins

Muma, N. A., Lee, J. M., Gorman, L. K., Heidenreich, B. A., Mitrovic, I., & Napier, T. C. (2001) · Experimental Neurology · doi:10.1006/exnr.2000.7582 · Cited by 18

Phosphorylation and Dephosphorylation of Tau Protein by the Catalytic Subunit of PKA, as Probed by Electrophoretic Mobility Retard

Benítez, M. J., Cuadros, R., & Jiménez, J. S. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-201077 · Cited by 19

Prion-Like Propagation Mechanisms in Tauopathies and Traumatic Brain Injury: Challenges and Prospects

Alyenbaawi, H., Allison, W. T., & Mok, S. (2020) · Biomolecules · doi:10.3390/biom10111487 · Cited by 20

Racemization in Post-Translational Modifications Relevance to Protein Aging, Aggregation and Neurodegeneration: Tip of the Iceberg

Dyakin, V. V., Wısnıewskı, T., & Lajtha, Á. (2021) · Symmetry · doi:10.3390/sym13030455 · Cited by 20

Pick's disease: cytoskeletal changes in the hypothalamic lateral tuberal nucleus

Braak, H., & Braak, E. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00578-2 · Cited by 17

Functional screening in Drosophila reveals the conserved role of REEP1 in promoting stress resistance and preventing the formation of Tau aggregates

Appocher, C., Klima, R., & Feiguin, F. M. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu393 · Cited by 17

Comparative assessment of regional tau distribution by Tau-PET and Post-mortem neuropathology in a representative set of Alzheimer’s & frontotemporal lobar degeneration patients

Gatto, R. G., Carlos, A. F., Reichard, R. R., Lowe, V. J., Whitwell, J. L., & Josephs, K. A. (2023) · PLoS ONE · doi:10.1371/journal.pone.0284182 · Cited by 17

Characterization of neurofibrillary tangle immunophenotype signatures to classify tangle maturity in Alzheimer's disease

Hamlin, D., Ryall, C., Turner, C. P., Faull, R. L. M., Murray, H. C., & Curtis, M. A. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.13922 · Cited by 16

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 16

Phosphorylation Pattern of tau Associated with Distinct Changes of the Growth Cone Cytoskeleton

Šimić, G., Diana, A., & Hof, P. R. (2003) · Progress in molecular and subcellular biology · doi:10.1007/978-3-642-55557-2_2 · Cited by 17

Levels of soluble and insoluble tau reflect overall status of tau phosphorylation in vivo

Hirata‐Fukae, C., Li, H., Ma, L., Hoe, H., Rebeck, G. W., Aisen, P. S. S., & Matsuoka, Y. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.11.023 · Cited by 17

Tau proteins-enhanced Ca2+/calmodulin (CaM)-dependent phosphorylation by the brain supernatant of diisopropyl phosphorofluoridate (DFP)-treated hen: tau mutants indicate phosphorylation of more amino acids in tau by CaM kinase II

Gupta, R. P., & Abou-Donia, M. B. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00988-3 · Cited by 16

Induction of a specific tau Alzheimer epitope in SY-5Y neuroblastoma cells

Caillet‐Boudin, M., & Delacourte, A. (1996) · Neuroreport · doi:10.1097/00001756-199612200-00061 · Cited by 16

Tau hyperphosphorylation on T217 in cerebrospinal fluid is specifically associated to amyloid-β pathologyPreprint

Barthélemy, N. R., Bateman, R. J., Marin, P., Bécher, F., Sato, C., Lehmann, S., & Gabelle, A. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/226977 · Cited by 16

Arc mediates intercellular tau transmission via extracellular vesicles

Tyagi, M., de Hoog, E., Grega, M., Sullivan, K. R., Walker, A., Chadha, R., Northrop, A., Fábián, B., Hummer, G., Fuxreiter, M., et al. (2026) · Cell · doi:10.1016/j.cell.2026.06.008 · Cited by 19

Anti-tau antibodies targeting a conformation-dependent epitope selectively bind seeds

Hitt, B. D., Gupta, A., Singh, R., Yang, T., Beaver, J. D., Shang, P., White, C. L., Joachimiak, Ł. A., & Diamond, M. I. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105252 · Cited by 16

Some markers of neuronal damage in cerebrospinal fluid of multiple sclerosis patients in relapse.

Mitosek‐Szewczyk, K., Gordon‐Krajcer, W., Flis, D., & Stelmasiak, Z. (2011) · PubMed · Cited by 15

Genetic ablation of tau in postnatal neurons rescues decreased adult hippocampal neurogenesis in a tauopathy model

Houben, S., Leroy, K., Ando, K., Yilmaz, Z., Widomski, C., Buée, L., & Brion, J. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.02.021 · Cited by 16

Erythropoietin-derived peptide treatment reduced neurological deficit and neuropathological changes in a mouse model of tauopathy

Choi, Y., Dunn-Meynell, A. A., Marchese, M. E., Blumberg, B. M., Gaindh, D., Dowling, P. C., & Lü, W. (2021) · Alzheimer s Research & Therapy · doi:10.1186/s13195-020-00766-4 · Cited by 14

Olfactory Dysfunctions and Decreased Nitric Oxide Production in the Brain of Human P301L Tau Transgenic Mice

Hu, Y., Ding, W., Zhu, X., Chen, R., & Wang, X. (2015) · Neurochemical Research · doi:10.1007/s11064-015-1741-8 · Cited by 15

14‐3‐3 protein beta isoform is associated with 3‐repeat tau neurofibrillary tangles in Alzheimer's disease

Sugimori, K., Kobayashi, K., Kitamura, T., Sudo, S., & Koshino, Y. (2007) · Psychiatry and Clinical Neurosciences · doi:10.1111/j.1440-1819.2007.01631.x · Cited by 15

Possible Role of Tau in Mediating Pathological Effects of apoE4 in vivo prior to and following Activation of the Amyloid Cascade

Inbar, D., Belinson, H., Rosenmann, H., & Michaelson, D. M. (2010) · Neurodegenerative Diseases · doi:10.1159/000283477 · Cited by 14

AD molecular: Imaging tau aggregates with positron emissions tomography

Betthauser, T. J. (2019) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2019.07.007 · Cited by 14

Pathological and neurophysiological outcomes of seeding human-derived tau pathology in the APP-KI NL-G-F and NL-NL mouse models of Alzheimer’s Disease

Tok, S., Maurin, H., Delay, C., Crauwels, D., Manyakov, N. V., der Elst, W. V., Moechars, D., & Drinkenburg, W. H. I. M. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01393-w · Cited by 14

Pathological-Like Assembly of tau Induced by a Paired Helical Filament Core Expressed at the Plasma Membrane

Campos‐Peña, V., Tapia-Ramı́rez, J., Sánchez‐Torres, C., & Meraz‐Ríos, M. A. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1198 · Cited by 14

Tau Pathology in Neurons and Glial Cells of Aged Baboons

Schultz, C., Hubbard, G. B., Tredici, K. D., Braak, E., & Braak, H. (2001) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-1249-3_5 · Cited by 14

Tau accumulation in a patient with pallidonigroluysian atrophy

Mori, H., Motoi, Y., Kobayashi, T., Hasegawa, M., Yamamura, A., Iwatsubo, T., & Mizuno, Y. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)02034-1 · Cited by 14

Theoretical impact of the AT(N) framework on dementia using a community autopsy sample

Burke, B. T., Latimer, C., Keene, C. D., Sonnen, J. A., McCormick, W., Bowen, J. D., McCurry, S. M., Larson, E. B., & Crane, P. K. (2021) · Alzheimer's & Dementia · doi:10.1002/alz.12348 · Cited by 13

Identification of phosphorylated tau protein interactors in progressive supranuclear palsy ( PSP ) reveals networks involved in protein degradation, stress response, cytoskeletal dynamics, metabolic processes, and neurotransmission

Radford, R. A. W., Rayner, S. L., Szwaja, P., Morsch, M., Cheng, F., Zhu, T., Widagdo, J., Anggono, V., Pountney, D. L., Chung, R. S., et al. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15796 · Cited by 12

Early and selective localization of tau filaments to glutamatergic subcellular domains within the human anterodorsal thalamus

Sárkány, B., Dávid, C., Hortobágyi, T., Gombás, P., Somogyi, P., Acsády, L., & Viney, T. J. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02749-3 · Cited by 15

A Study of Aβ Oligomers in the Temporal Cortex and Cerebellum of Patients with Neuropathologically Confirmed Alzheimer's Disease Compared to Aged Controls

Savioz, A., Giannakopoulos, P., Herrmann, F. R., Klein, W. L., Kövari, E., Bouras, C., & Giacobini, E. (2016) · Neurodegenerative Diseases · doi:10.1159/000446283 · Cited by 14

Reduction of amyloid beta by Aβ3-10-KLH vaccine also decreases tau pathology in 3×Tg-AD mice

Zhang, H., Zhu, K., Meng, Y., Ding, L., Wang, J.-C., Yin, W., Yan, Y., & Cao, Y. (2018) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2018.07.019 · Cited by 13

Monoamine oxidase binding not expected to significantly affect [18F]flortaucipir PET interpretation

Wright, J. P., Goodman, J. R., Lin, Y., Lieberman, B. P., Clemens, J., Gomez, L. F., Liang, Q., Hoye, A. T., Pontecorvo, M. J., & Conway, K. A. (2022) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-022-05822-9 · Cited by 13

Acetaldehyde induces tau phosphorylation via activation of p38 MAPK/JNK and ROS production

Li, T., Shi, H., & Zhao, Y. (2021) · Molecular & Cellular Toxicology · doi:10.1007/s13273-021-00193-y · Cited by 13

Trans-Channel Fluorescence Learning Improves High-Content Screening for Alzheimer's Disease Therapeutics

Wong, D. R., Conrad, J. C., Johnson, N. R., Ayers, J. I., Laeremans, A., Lee, J. C., Lee, J., Prusiner, S. B., Bandyopadhyay, S., Butte, A. J., et al. (2021) · Nature Machine Intelligence · doi:10.1038/s42256-022-00490-8 · Cited by 13

Biochemical and pathological characterization of frontotemporal dementia due to a Leu266Val mutation in microtubule-associated protein tau in an African American individual

Deerlin, V. M. V., Forman, M. S., Farmer, J. M., Grossman, M., Joyce, S. C., Crowe, A., Trojanowski, J. Q., Lee, V. M. ‐., & Chatterjee, A. K. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0155-8 · Cited by 13

Detection, visualization and quantification of protein complexes in human Alzheimer’s disease brains using proximity ligation assay

Romero‐Fernandez, W., Carvajal‐Tapia, C., Prusky, A., Katdare, K. A., Wang, E., Shostak, A., Ventura‐Antunes, L., Harmsen, H. J., Lippmann, E. S., Fuxé, K., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-38000-4 · Cited by 11

Detecting the Undetectable: Advances in Methods for Identifying Small Tau Aggregates in Neurodegenerative Diseases

Böken, D., Wu, Y., Zhang, Z.-W., & Klenerman, D. (2024) · ChemBioChem · doi:10.1002/cbic.202400877 · Cited by 11

STOX1A induces phosphorylation of tau proteins at epitopes hyperphosphorylated in Alzheimer's disease

van Abel, D., Abdul-Hamid, O., Scheper, W., van Dijk, M., & Oudejans, C. B. M. (2012) · Neuroscience Letters · doi:10.1016/j.neulet.2012.09.017 · Cited by 13

Profiling the IgOme: Meeting the challenge

Weiss-Ottolenghi, Y., & Gershoni, J. M. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.11.005 · Cited by 11

Multisite chronic pain: association with cognitive decline and post-mortem Alzheimer’s biomarkers

Bell, T. R., Franz, C. E., Lerman, I. R., Williams, M. E., Fennema‐Notestine, C., Panizzon, M. S., Elman, J. A., Bennett, D. A., & Kremen, W. S. (2025) · Brain Communications · doi:10.1093/braincomms/fcaf208 · Cited by 12

Gene-environment interaction promotes Alzheimer's risk as revealed by synergy of repeated mild traumatic brain injury and mouse App knock-in

Chiasseu, M., Fesharaki‐Zadeh, A., Saito, T., Saido, T. C., & Strittmatter, S. M. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105059 · Cited by 11

Targeting of phosphorylated tau at threonine 181 by a Qβ virus‐like particle vaccine is safe, highly immunogenic, and reduces disease severity in mice and rhesus macaques

Maphis, N. M., Hulse, J. P., Peabody, J., Dadras, S., Whelpley, M. J., Kandath, M., Wilson, C. M., Hobson, S., Thompson, J., Poolsup, S., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70101 · Cited by 10

Arterial spin labeling demonstrates preserved regional cerebral blood flow in the P301L mouse model of tauopathy

Kindler, D., Maschio, C., Ni, R., Zerbi, V., Razansky, D., & Klohs, J. (2021) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x211062274 · Cited by 11

Sequence-Dependent Conformational Properties of PGGG Motif in Tau Repeats: Insights from Molecular Dynamics Simulations of Narrow Pick Filament

Sahayaraj, A. E., Viswanathan, R., Pinhero, F., Vahid, A. A., & Vijayan, V. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00602 · Cited by 11

Oligomeric, phosphorylated, and truncated tau and spliceosome pathology within the entorhinal–hippocampal connectome across stages of Alzheimer's disease

Mahady, L. J., Perez, S. E., Malek‐Ahmadi, M. H., & Mufson, E. J. (2023) · The Journal of Comparative Neurology · doi:10.1002/cne.25466 · Cited by 11

Behavioral and neuropathological characterization over the adult lifespan of the human tau knock-in mouse

Benskey, M. J., Panoushek, S., Saito, T., Saido, T. C., Grabinski, T. M., & Kanaan, N. M. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1265151 · Cited by 13

Pattern of tau hyperphosphorylation and neurotransmitter markers in the brainstem of senescent tau filament forming transgenic mice

Morcinek, K., Köhler, C. N., Götz, J., & Schröder, H. (2012) · Brain Research · doi:10.1016/j.brainres.2012.12.016 · Cited by 11

Generation and Characterization of Novel Monoclonal Antibodies Targeting p62/sequestosome-1 Across Human Neurodegenerative Diseases

Trejo‐Lopez, J. A., Sorrentino, Z. A., Riffe, C. J., Prokop, S., Dickson, D. W., Yachnis, A. T., & Giasson, B. I. (2020) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlaa007 · Cited by 12

Analysis of the cholinergic pathology in the P301L tau transgenic pR5 model of tauopathy

Köhler, C. N., Bista, P., Götz, J., & Schröder, H. C. (2010) · Brain Research · doi:10.1016/j.brainres.2010.05.076 · Cited by 11

Regenerating islet-derived 1α (REG-1α) protein increases tau phosphorylation in cell and animal models of tauopathies

Moussaed, M., Huc-Brandt, S., Cubedo, N., Silhol, M., Murat, S., Lebart, M., Kovács, G. G., Verdier, J., Trousse, F., Rossel, M., et al. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.07.029 · Cited by 11

Distribution of the hematopoietic growth factor G ‐ CSF and its receptor in the adult human brain with specific reference to A lzheimer's disease

Ridwan, S., Bauer, H., Frauenknecht, K. B. M., Hefti, K., von Pein, H., & Sommer, C. (2014) · Journal of Anatomy · doi:10.1111/joa.12154 · Cited by 11

Elevated SGK1 increases Tau phosphorylation and microtubule instability in Alzheimer’s patient-derived cortical neurons

Saleem, K., Xiao, Z., Zhu, B., Ren, Y., Yan, Z., & Feng, J. (2026) · Molecular Psychiatry · doi:10.1038/s41380-025-03225-4 · Cited by 10

Proteolytic Cleavage of Apolipoprotein E in the Down Syndrome Brain

Day, R. J., McCarty, K. L., Ockerse, K. E., Head, E., & Rohn, T. T. (2016) · Aging and Disease · doi:10.14336/ad.2015.1020 · Cited by 10

An adeno-associated virus-mediated immunotherapy for Alzheimer’s disease

Zhang, Y., Lin, Q., Kuang, Y., Liu, J., Wang, D., Xie, W., Zhang, L., & Fu, L. (2022) · Molecular Immunology · doi:10.1016/j.molimm.2022.02.006 · Cited by 9

Arterial spin labeling demonstrates preserved regional cerebral blood flow in the P301L mouse model of tauopathy

Kindler, D., Maschio, C., Ni, R., Zerbi, V., Razansky, D., & Klohs, J. (2022) · Zurich Open Repository and Archive (University of Zurich) · doi:10.3929/ethz-b-000520246 · Cited by 10

Alzheimer PHF-tau aggregates do not spread tau pathology to the brain via the Retino-tectal projection after intraocular injection in male mouse models

de Fisenne, M.-A., Yilmaz, Z., Decker, R. D., Suain, V., Buée, L., Ando, K., Brion, J., & Leroy, K. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105875 · Cited by 10

Achalasie de l’œsophage, troubles du sommeil et mouvements choréiques au cours d’une taupathie sans ophtalmoplégie, syndrome parkinsonien ni démence (paralysie supranucléaire progressive ?) : étude clinicopathologique

Kaphan, E., Pellissier, J., Rey, M. F., Robert, D., Auphan, M., & Chérif, A. (2008) · Revue Neurologique · doi:10.1016/j.neurol.2007.09.007 · Cited by 10

Phospho-Tau Accumulation and Structural Alterations of the Golgi Apparatus of Cortical Pyramidal Neurons in the P301S Tauopathy Mouse Model

Antón‐Fernández, A., Merchán‐Rubira, J., Ávila, J., Hernández, F., DeFelipe, J., & Muñoz, A. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170332 · Cited by 11

A 4R tauopathy develops without amyloid deposits in aged cat brains

Poncelet, L., Ando, K., Vergara, C., Mansour, S., Suain, V., Yilmaz, Z., Reygel, A., Gilissen, E., Brion, J., & Leroy, K. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.05.024 · Cited by 10

Uncovering the Effect of pS202/pT205/pS208 Triple Phosphorylations on the Conformational Features of the Key Fragment G192–T212 of Tau Protein

Liu, H., Li, Q., Xiong, C., Zhong, H., Zhang, Q., Liu, H., & Yao, X. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00058 · Cited by 10

The Brain of the Aging Baboon: A Nonhuman Primate Model for Neuronal and Glial Tau Pathology

Schultz, C., Tredici, K. D., R�b, U., Braak, E., Hubbard, G. B., & Braak, H. (2002) · KARGER eBooks · doi:10.1159/000061454 · Cited by 10

Die Silberkornkrankheit - Abgrenzung zur Alzheimer'schen Erkrankung

Tolnay, M., Monsch, A. U., Staehelin, H. B., & Probst, A. (1999) · Der Pathologe · doi:10.1007/s002920050339 · Cited by 10

Interaction Between a High-Fat Diet and Tau Pathology in Mice: Implications for Alzheimer’s Disease

Jang, Y. J., Choi, M. G., Yoo, B. J., Lee, K. J., Jung, W. B., Kim, S., & Park, S. A. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230927 · Cited by 8

Tau-mediated axonal degeneration is prevented by activation of the WldS pathway

Stubbs, K., Batchelor, B. G., Sivanantharajah, L., Sealey, M. A., Moreno, M. R., Ruiz, E., Richardson, B., Perry, V. H., Newman, T. A., & Mudher, A. K. (2023) · Brain Communications · doi:10.1093/braincomms/fcad052 · Cited by 9

Specific serum antibody binding to phosphorylated and non-phosphorylated tau in non-cognitively impaired, mildly cognitively impaired, and Alzheimer’s disease subjects: an exploratory study

Klaver, A. C., Coffey, M. P., Bennett, D. A., & Loeffler, D. A. (2017) · Translational Neurodegeneration · doi:10.1186/s40035-017-0100-x · Cited by 9

Sex-Related Motor Deficits in the Tau-P301L Mouse Model

Camargo, L. C., Honold, D., Bauer, R., Shah, N. J., Langen, K., Willbold, D., Kutzsche, J., Willuweit, A., & Schemmert, S. (2021) · Biomedicines · doi:10.3390/biomedicines9091160 · Cited by 9

Characterization of microtubule-associated protein tau isoforms and Alzheimer’s disease-like pathology in normal sheep (Ovis aries): relevance to their potential as a model of Alzheimer’s disease

Davies, E. S., Morphew, R. M., Cutress, D. J., Morton, A. J., & McBride, S. D. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04572-z · Cited by 9

Molecular Dynamics Simulation of Tau Peptides for the Investigation of Conformational Changes Induced by Specific Phosphorylation Patterns

Gandhi, N. S., Kukić, P., Lippens, G. M., & Mancera, R. L. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6598-4_3 · Cited by 9

Apolipoprotein E genotype in senile dementia with tangles differs from Alzheimer's disease

Tolnay, M., Villoz, N., Probst, A., & Miserez, A. R. (2003) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.2003.04032.x · Cited by 9

Developmental regulation and PKC dependence of Alzheimer's-type tau phosphorylations in cultured fetal rat hippocampal neurons

Combs, C. K., Coleman, P. D., & O’Banion, M. K. (1998) · Developmental Brain Research · doi:10.1016/s0165-3806(98)00019-4 · Cited by 9

NMDA antagonist blockade of AT8 tau immunoreactive changes in neuronal cultures

Couratier, P., Lesort, M. J., Terro, F., Dussartre, C., & Hugon, J. (1996) · Fundamental and Clinical Pharmacology · doi:10.1111/j.1472-8206.1996.tb00585.x · Cited by 9

Tau Filaments from Amyotrophic Lateral Sclerosis/Parkinsonism-Dementia Complex (ALS/PDC) adopt the CTE FoldPreprint

Qi, C., Verheijen, B. M., Kokubo, Y., Shi, Y., Tetter, S., Murzin, A. G., Nakahara, A., Morimoto, S., Vermulst, M., Sasaki, R., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.26.538417 · Cited by 9

Endogenous pathology in tauopathy mice progresses via brain networksPreprint

Ramirez, D. M. O., Whitesell, J. D., Bhagwat, N., Thomas, T. L., Ajay, A. D., Nawaby, A., Delatour, B., Bay, S., Lafaye, P. J., Knox, J. E., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.23.541792 · Cited by 9

Microscopy assessment of a fluorescence [ 18 F] flortaucipir analog (T726) shows neuropathological overlap with 3R and 4R tau lesions

Gatto, R. G., Youssef, H., Reichard, R. R., Lowe, V. J., Whitwell, J. L., & Josephs, K. A. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14330 · Cited by 8

pS396/pS404 (PHF1) tau vaccine outperforms pS199/pS202 (AT8) in rTg4510 tauopathy model

Hulse, J. P., Maphis, N. M., Peabody, J., Bondu, V., Chackerian, B., & Bhaskar, K. (2025) · npj Vaccines · doi:10.1038/s41541-025-01147-4 · Cited by 9

DAP12 deletion reduces neuronal SLIT2 and demyelination and enhances brain resilience in female tauopathy mice

Chen, H., Fan, L., Guo, Q., Wong, M. Y., Zhu, J., Foxe, N. R., Wang, W. T., Nessim, A., Carling, G., Liu, B., et al. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00903-3 · Cited by 10

Glutamate but not interleukin-6 influences the phosphorylation of tau in primary rat hippocampal neurons

Hüll, M., Eistetter, J., Fiebich, B. L., & Bauer, J. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(98)01003-9 · Cited by 8

Selection of lansoprazole from an FDA-approved drug library to inhibit the Alzheimer’s disease seed-dependent formation of tau aggregates

Ahmed, I., Shimonaka, S., Uddin, M. N., Elahi, M., Ishiguro, K., Hasegawa, M., Hattori, N., & Motoi, Y. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1368291 · Cited by 8

Severe tauopathy and axonopathy in the medulla oblongata in Alzheimer’s disease implicate the changes in autonomic nervous function

Tian, Y., Gao, G., & Dai, J. (2022) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2022.102105 · Cited by 9

Anterograde and Retrograde Propagation of Inoculated Human Tau Fibrils and Tau Oligomers in a Non-Transgenic Rat Tauopathy Model

Horvat, L. L., Španić, E., Leko, M. B., Zubčić, K., Horvat, L., Mustapić, M., Hof, P. R., & Šimić, G. (2023) · Biomedicines · doi:10.3390/biomedicines11041004 · Cited by 7

Assessing individual variability of the entorhinal subfields in health and disease

Oltmer, J., Greve, D. N., Cerri, S., Slepneva, N., Rodríguez, J. L., Iglesias, J. E., Leemput, K. V., Champion, S. N., Frosch, M. P., & Augustinack, J. C. (2023) · The Journal of Comparative Neurology · doi:10.1002/cne.25538 · Cited by 6

Hyperphosphorylated tau in Alzheimer's disease disseminates along pathways predicted by the Structural Model for Cortico‐cortical Connections

Uceda‐Heras, A., Aparicio‐Rodríguez, G., & García‐Cabezas, M. Á. (2024) · The Journal of Comparative Neurology · doi:10.1002/cne.25623 · Cited by 9

Torpor induces reversible tau hyperphosphorylation and accumulation in mice expressing human tau

Mestdagh, C. F. D. V., Witte, M. E., Scheper, W., Smit, A. B., Henning, R. H., & van Kesteren, R. E. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01800-4 · Cited by 7

Herpes Simplex Virus 1 Upregulates p35, Alters CDK-5 Localization, and Stimulates CDK-5 Kinase Activity during Acute Infection in Neurons

Mostafa, H. H., Sels, J. M. V. L., & Davido, D. J. (2015) · Journal of Virology · doi:10.1128/jvi.00106-15 · Cited by 7

Neurophysiological effects of human-derived pathological tau conformers in the APPKM670/671NL.PS1/L166P amyloid mouse model of Alzheimer’s disease

Tok, S., Maurin, H., Delay, C., Crauwels, D., Manyakov, N. V., der Elst, W. V., Moechars, D., & Drinkenburg, W. H. I. M. (2022) · Scientific Reports · doi:10.1038/s41598-022-11582-1 · Cited by 7

Laser-Induced Axotomy of Human iPSC-Derived and Murine Primary Neurons Decreases Somatic Tau and AT8 Tau Phosphorylation: A Single-Cell Approach to Study Effects of Acute Axonal Damage

Bell-Simons, M., Buchholz, S., Klimek, J., & Zempel, H. (2023) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-023-01359-z · Cited by 8

Individual variability in the structural properties of neurons in the human inferior olive

Baizer, J. S., Wong, K. M., Sherwood, C. C., Hof, P. R., & Witelson, S. F. (2017) · Brain Structure and Function · doi:10.1007/s00429-017-1580-2 · Cited by 7

Correspondence of mean apparent propagator MRI metrics with phosphorylated tau and astrogliosis in chronic traumatic encephalopathy

Gangolli, M., Pajevic, S., Kim, J. H., Hutchinson, E. B., Benjamini, D., & Basser, P. J. (2023) · Brain Communications · doi:10.1093/braincomms/fcad253 · Cited by 7

Differential effects of age and sex on tau pathology propagation in the htau mouse model: A neuropathological and proteomic study

Kosa, A., Lopez‐Gutierrez, L., Ando, K., Doeraene, E., Aydin, E., Lasri, H., Wathelet‐Depauw, A., Pieters, K., Morckhoven, D. V., Imbault, V., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70784 · Cited by 6

Evolving prion-like tau conformers differentially alter postsynaptic proteins in neurons inoculated with distinct isolates of Alzheimer’s disease tau

Hromádková, L., Kim, C., Haldiman, T., Peng, L., Zhu, X., Cohen, M. L., de Silva, R., & Safar, J. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-01133-0 · Cited by 6

Cytoskeletal Protection: Acting on Notch to Prevent Neuronal Dysfunction

Bonini, S. A., Ferrari‐Toninelli, G., Maccarinelli, G., Bettinsoli, P., Montinaro, M., & Memo, M. (2013) · Neurodegenerative Diseases · doi:10.1159/000354230 · Cited by 7

Protective Effect of Tat PTD-Hsp27 Fusion Protein on Tau Hyperphosphorylation Induced by Okadaic Acid in the Human Neuroblastoma Cell Line SH-SY5Y

Choi, S., Oh, J. H., Kim, H., Nam, S. H., Shin, J., & Park, J. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0199-1 · Cited by 6

Simultaneous detection of tau phospho-epitopes with haptenylated antibodies

Härtig, W., Lehmann, J., Stieler, J., Singer, D. L., Grosche, J., Arendt, T., & Hoffmann, R. (2006) · Neuroreport · doi:10.1097/01.wnr.0000215778.76602.da · Cited by 6

Novel cytoplasmic immunolocalization of RNA polymerase II in inclusion-body myositis muscle

Wilczynski, G. M., Engel, W. K., & Askanas, V. (2001) · Neuroreport · doi:10.1097/00001756-200107030-00010 · Cited by 6

Tau P301S Transgenic Mice Develop Gait and Eye Movement Impairments That Mimic Progressive Supranuclear PalsyPreprint

Creed, R. B., Harris, S. C., Sridhar, S., du Lac, S., Zee, D. S., Dunn, F. A., Bouvier, G., & Nelson, A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.20.614197 · Cited by 6

Spontaneous pathology in PS19 tauopathy mice progresses via brain networks

Ramirez, D. M. O., Whitesell, J. D., Bhagwat, N., Thomas, T. L., Ajay, A. D., Nawaby, A., Delatour, B., Bay, S., LaFaye, P., Harris, J. A., et al. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.107072 · Cited by 5

Telomere-driven senescence accelerates tau pathology, neuroinflammation and neurodegeneration in a tauopathy mouse model

Palomares, D., Vanparys, A., Jorgji, J., Paître, E., Kienlen‐Campard, P., & Suelves, N. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02118-5 · Cited by 7

Making tau amyloid models in vitro: a crucial and underestimated challenge

Broc, J., Piersson, C., & Fichou, Y. (2025) · FEBS Letters · doi:10.1002/1873-3468.70022 · Cited by 5

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