Localization, induction, and cellular effects of tau phosphorylated at threonine 2171

Research criteria for the diagnosis of Alzheimer's disease: revising the NINCDS–ADRDA criteria

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A protein factor essential for microtubule assembly

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Introduction to the recommendations from the National Institute on Aging‐Alzheimer's Association workgroups on diagnostic guidelines for Alzheimer's disease

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Discriminative accuracy of plasma phospho-tau217 for Alzheimer disease vs other neurodegenerative disorders

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Plasma P-tau181 in Alzheimer's disease: relationship to other biomarkers, differential diagnosis, neuropathology and longitudinal progression to Alzheimer's dementia

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Tau Mislocalization to Dendritic Spines Mediates Synaptic Dysfunction Independently of Neurodegeneration

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Assembly of τ protein into Alzheimer paired helical filaments depends on a local sequence motif ( ³⁰⁶ VQIVYK ³¹¹ ) forming β structure

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Hyperphosphorylation induces self-assembly of τ into tangles of paired helical filaments/straight filaments

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Plasma p-tau231: a new biomarker for incipient Alzheimer’s disease pathology.

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Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice

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Prediction of future Alzheimer’s disease dementia using plasma phospho-tau combined with other accessible measures

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The microtubule binding domain of tau protein

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Global Hairpin Folding of Tau in Solution

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Prion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-β

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Functional implications for the microtubule-associated protein tau: localization in oligodendrocytes.

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Phosphorylation of different tau sites during progression of Alzheimer’s disease

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Tau aggregation is driven by a transition from random coil to beta sheet structure.

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Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly.

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Long‐term culture of mouse cortical neurons as a model for neuronal development, aging, and death

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Cerebrospinal fluid phospho-tau T217 outperforms T181 as a biomarker for the differential diagnosis of Alzheimer's disease and PET amyloid-positive patient identification

Barthélemy, N. R., Bateman, R. J., Hirtz, C., Marin, P., Becher, F., Sato, C., Gabelle, A., & Lehmann, S. (2020) · Alzheimer's Research & Therapy · doi:10.1186/s13195-020-00596-4 · Cited by 229 · see citing works

Tau protein, the paired helical filament and Alzheimer's disease

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Progression of Amyloid Pathology to Alzheimer's Disease Pathology in an Amyloid Precursor Protein Transgenic Mouse Model by Removal of Nitric Oxide Synthase 2

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Tau Is Hyperphosphorylated at Multiple Sites in Mouse Brain In Vivo After Streptozotocin-Induced Insulin Deficiency

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Pseudophosphorylation of tau protein alters its ability for self‐aggregation

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CSF biomarkers for Alzheimer’s disease: use in early diagnosis and evaluation of drug treatment

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CSF biomarkers for Alzheimer's disease: current utility and potential future use

Holtzman, D. M. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.09.003 · Cited by 122 · see citing works

Alzheimer disease

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Structural and Functional Implications of Tau Hyperphosphorylation: Information from Phosphorylation-Mimicking Mutated Tau Proteins

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Phosphorylated tau sites that are elevated in Alzheimer's disease fluid biomarkers are visualized in early neurofibrillary tangle maturity levels in the post mortem brain

Moloney, C. M., Labuzan, S. A., Crook, J. E., Siddiqui, H., Castanedes‐Casey, M., Lachner, C., Petersen, R. C., Duara, R., Graff‐Radford, N. R., Dickson, D. W., et al. (2022) · Alzheimer s & Dementia · doi:10.1002/alz.12749 · Cited by 74 · see citing works

Extracellular Tau Oligomers Induce Invasion of Endogenous Tau into the Somatodendritic Compartment and Axonal Transport Dysfunction

Swanson, E., Breckenridge, L., McMahon, L. P., Som, S., McConnell, I., & Bloom, G. S. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170168 · Cited by 73 · see citing works

Cellular localization of p-tau217 in brain and its association with p-tau217 plasma levels

Wennström, M., Janelidze, S., Nilsson, K. P. R., Bank, T. N. B., Serrano, G. E., Beach, T. G., Dage, J. L., & Hansson, O. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01307-2 · Cited by 59 · see citing works

Intraneuronal Tau Misfolding Induced by Extracellular Amyloid-β Oligomers

Rudenko, L. K., Wallrabe, H. K., Periasamy, A., Siller, K. H., Švindrych, Z., Seward, M. E., Best, M. N., & Bloom, G. S. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190226 · Cited by 23 · see citing works

Clinical Neuropathology Practice News 3-2012: the ABC in AD revised and updated guideline for the neuropathologic assessment of Alzheimers disease

Kovács, G. G., & Gelpí, E. (2012) · Clinical Neuropathology · doi:10.5414/np300512 · Cited by 14 · see citing works

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

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The potential dual role of tau phosphorylation: plasma phosphorylated-tau217 in newborns and Alzheimer’s disease

González‐Ortiz, F., Vávra, J., Payne, E., Kirsebom, B., Sjöbom, U., dos Santos, C. P., Júlvez, J., Kramer, K., Zalcberg, D., Montoliu‐Gaya, L., et al. (2025) · Brain Communications · doi:10.1093/braincomms/fcaf221 · Cited by 34 · see citing works

Leucettinib-21, a DYRK1A Kinase Inhibitor as Clinical Drug Candidate for Alzheimer’s Disease and Down Syndrome

Meijer, L., Chrétien, E., & Ravel, D. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-240078 · Cited by 30 · see citing works

Nanoscale imaging of pT217‐tau in aged rhesus macaque entorhinal and dorsolateral prefrontal cortex: Evidence of interneuronal trafficking and early‐stage neurodegeneration

Datta, D., Perone, I., Wijegunawardana, D., Liang, F., Morozov, Y. M., Arellano, J. I., Duque, A., Xie, Z., van Dyck, C. H., Joyce, M. K. P., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.13737 · Cited by 28 · see citing works

Neuronal plasma biomarkers in acute ischemic stroke

Gundersen, J. K., González‐Ortiz, F., Karikari, T. K., Kirsebom, B., Mertes, K., Zetterberg, H., Kvartsberg, H., Rønning, O. M., Gísladóttir, B., Blennow, K., et al. (2024) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x241293537 · Cited by 16 · see citing works

Associations Between Changes in Levels of Phosphorylated Tau and Severity of Cognitive Impairment in Early Alzheimer Disease

González‐Ortiz, F., Kirsebom, B., Yakoub, Y., Gundersen, J. K., Pålhaugen, L., Waterloo, K. K., Selnes, P., Jarholm, J. A., Gísladóttir, B., Rongve, A., et al. (2025) · Neurology · doi:10.1212/wnl.0000000000213676 · Cited by 16 · see citing works

Dysregulation of mTOR by tau in Alzheimer's disease

Bloom, G. S., & Norambuena, A. (2023) · Cytoskeleton · doi:10.1002/cm.21782 · Cited by 15 · see citing works

Concussion-Related Biomarker Variations in Retired Rugby Players and Implications for Neurodegenerative Disease Risk: The UK Rugby Health Study

Alanazi, N., Fitzgerald, M., Hume, P. A., Hellewell, S. C., Horncastle, A., Anyaegbu, C. C., Papini, M. G., Hargreaves, N., Halicki, M., Entwistle, I. R., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25147811 · Cited by 13 · see citing works

Biomarker-related phospho-tau217 appears in synapses around Aβ plaques prior to tau tangle in cerebral cortex of preclinical Alzheimer’s disease

Hirota, Y., Sakakibara, Y., Morishima, M., Sano, T., Hara, M., Arakawa, A., Takao, M., Murayama, S., Saito, Y., Sekiya, M., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116203 · Cited by 13 · see citing works

The Relationship between p-tau217, p-tau231, and p-tau205 in the Human Brain Is Affected by the Cellular Environment and Alzheimer’s Disease Pathology

Wennström, M., Schultz, N., Gallardo, P. M., Bank, T. N. B., Serrano, G. E., Beach, T. G., Bose, S., & Hansson, O. (2024) · Cells · doi:10.3390/cells13040331 · Cited by 10 · see citing works

P-tau217 as a Biomarker in Alzheimer’s Disease: Applications in Latin American Populations

Varela-Vidales, C. A., Martínez-Hernández, A., Hernández-Castellanos, E., & Delgado-Lara, D. L. C. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146633 · Cited by 9 · see citing works

Gliosis, misfolded protein aggregation, and neuronal loss in a guinea pig model of pulmonary tuberculosis

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Does p-tau217 play a physiological reparative role in neonates and neurodegenerative diseases?

Daly, T. P., Pini, L., & Imbimbo, B. P. (2025) · Brain Communications · doi:10.1093/braincomms/fcaf321 · Cited by 3 · see citing works

Baseline plasma p-tau217/Aβ42 as a sensitive marker for the severity of Alzheimer’s disease continuum

Liu, W.-Z., Xue, M., Sheng, Z.-H., Wei, Y.-Q., Ma, Y., Li, J., Song, J., Chi, S., Ou, Y., & Initiative, A. D. N. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-07939-z · Cited by 3 · see citing works

Evolving alterations of structural organization and functional connectivity in feedforward neural networks after induced P301L tau mutation

Weir, J. S., Hanssen, K. S., Winter‐Hjelm, N., Sandvig, A., & Sandvig, I. (2024) · European Journal of Neuroscience · doi:10.1111/ejn.16625 · Cited by 3 · see citing works

Amyloid and tau pathologies cross-talk to promote Alzheimeŕs disease: novel mechanistic insights

Ávila, J., Hernández, F., & Perry, G. L. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.07.025 · Cited by 3 · see citing works

Paclitaxel compromises nuclear integrity in interphase through SUN2-mediated cytoskeletal coupling

Hale, T., Hale, V. L., Kolata, P., dos Santos, Á., & Allegretti, M. (2025) · Journal of Cell Science · doi:10.1242/jcs.264494 · Cited by 2 · see citing works

Tau proteoforms as plasma biomarkers in Alzheimer’s disease: mechanisms, measurement, and medicine

Kim, E., Lee, J. H., & Han, D. (2025) · Expert Review of Proteomics · doi:10.1080/14789450.2025.2611853 · Cited by 1 · see citing works

Association Between Alzheimer Pathology, Sleep, and Cognition in Patients With Late-Onset Unexplained Epilepsy

Sarkis, R. A., Yang, H., Liu, L., Lam, A. D., Pavlova, M., Lemus, H. N., Kozhemiako, N., Hankerson, A., Amariglio, R. E., Pennell, P. B., et al. (2026) · Neurology · doi:10.1212/wnl.0000000000218476 · Cited by 1 · see citing works

Impact of clinical severity on plasma p-tau performance in predementia Alzheimer’s diseasePreprint

González‐Ortiz, F., Kirsebom, B., Yakoub, Y., Gundersen, J. K., Pålhaugen, L., Waterloo, K. K., Selnes, P., Jarholm, J. A., Gísladóttir, B., Rongve, A., et al. (2024) · medRxiv · doi:10.1101/2024.08.06.24311532 · Cited by 1 · see citing works

Amyloid-Independent Elevation of Plasma phosphorylated tau-217 Tracks Neurodegenerative Risk in Tuberous Sclerosis Complex: Implications for mTOR-Targeted Intervention

Baumel, J., Lutz, M., Ding, C., Capal, J., Ritter, D., Krueger, D., Salter, A., Werner, K., & Liu, A. J. (2026) · medRxiv · doi:10.64898/2026.09.09.26362677

P-tau217 in Early Disease Detection: True Biomarker Value or Diagnostic Mirage?

Kaur, D., Khan, M. N., Agarwal, O. P., Kaur, J., Malik, S. A., & Kumar, A. (2026) · Pan-African Journal of Health and Psychological Sciences · doi:10.64261/ng288b81

Localization, induction, and cellular effects of tau-phospho-threonine 217Preprint

Rajbanshi, B., Mandell, J. W., & Bloom, G. S. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.18.488657

Localization, induction, and functional effects of tau phosphorylated at threonine 217

Bloom, G. S. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.089421

Effects of T217 Phosphorylation on Tau Localization and Microtubule Binding

Rajbanshi, B., Mandell, J. W., & Bloom, G. S. (2023) · Alzheimer s & Dementia · doi:10.1002/alz.066573

Localization and functional role of TaupT217 in Alzheimer's disease

Rajbanshi, B. (2022) · Libra · doi:10.18130/9jz9-j547

T217-Phosphorylation Exacerbates Tau Pathologies and Tau-Induced Cognitive Impairment

Wang, X., Liu, Q. R., Li, X., Zhou, Q., Wu, D., Li, S., Liu, Y., & Wang, J. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210297 · Cited by 17 · see citing works