Tau-targeting therapies for Alzheimer disease: Current status and future directions

Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works

Lecanemab in early Alzheimer's disease

van Dyck, C. H., Swanson, C. J., Aisen, P., Bateman, R. J., Chen, C., Gee, M., Kanekiyo, M., Li, D., Reyderman, L., Cohen, S., et al. (2023) · New England Journal of Medicine · doi:10.1056/nejmoa2212948 · Cited by 5,678 · see citing works

Estimation of the global prevalence of dementia in 2019 and forecasted prevalence in 2050: an analysis for the Global Burden of Disease Study 2019

Nichols, E., Steinmetz, J. D., Vollset, S. E., Fukutaki, K., Chalek, J., Abd-Allah, F., Abdoli, A., Abualhasan, A., Abu-Gharbieh, E., Akram, T. T., et al. (2022) · The Lancet Public Health · doi:10.1016/s2468-2667(21)00249-8 · Cited by 5,575 · see citing works

Neuroinflammation and microglial activation in Alzheimer disease: where do we go from here?

Leng, F., & Edison, P. (2021) · Nature Reviews Neurology · doi:10.1038/s41582-020-00435-y · Cited by 3,179 · see citing works

Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry

Braak, H., Alafuzoff, I., Arzberger, T., Kretzschmar, H., & Del Tredici, K. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0127-z · Cited by 3,172 · see citing works

Donanemab in Early Symptomatic Alzheimer Disease: The TRAILBLAZER-ALZ 2 Randomized Clinical Trial

Sims, J. R., Zimmer, J. A., Evans, C. D., Lu, M., Ardayfio, P., Sparks, J., Wessels, A. M., Shcherbinin, S., Wang, H., Monkul Nery, E. S., et al. (2023) · JAMA · doi:10.1001/jama.2023.13239 · Cited by 2,932 · see citing works

Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease

Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.3.631 · Cited by 2,668 · see citing works

2022 Alzheimer's disease facts and figures

Anonymous (2022) · Alzheimer s & Dementia · doi:10.1002/alz.12638 · Cited by 2,384 · see citing works

Curcumin as “Curecumin”: From kitchen to clinic

Goel, A., Kunnumakkara, A. B., & Aggarwal, B. B. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.08.016 · Cited by 2,220 · see citing works

Stages of the Pathologic Process in Alzheimer Disease: Age Categories From 1 to 100 Years

Braak, H., Thal, D. R., Ghebremedhin, E., & Del Tredici, K. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318232a379 · Cited by 2,194 · see citing works

Correlation of Alzheimer Disease Neuropathologic Changes With Cognitive Status: A Review of the Literature

Nelson, P. T., Alafuzoff, I., Bigio, E. H., Bouras, C., Braak, H., Cairns, N. J., Castellani, R. J., Crain, B. J., Davies, P., Tredici, K. D., et al. (2012) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31825018f7 · Cited by 2,050 · see citing works

CSF and blood biomarkers for the diagnosis of Alzheimer's disease: a systematic review and meta-analysis

Olsson, B., Lautner, R., Andreasson, U., Öhrfelt, A., Portelius, E., Bjerke, M., Hölttä, M., Rosén, C., Olsson, C., Strobel, G., et al. (2016) · The Lancet Neurology · doi:10.1016/s1474-4422(16)00070-3 · Cited by 2,049 · see citing works

Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration

Patrick, G. N., Zukerberg, L. R., Nikolić, M., de la Monte, S. M., Dikkes, P., & Tsai, L. (1999) · Nature · doi:10.1038/45159 · Cited by 1,541 · see citing works

Primary age-related tauopathy (PART): a common pathology associated with human aging

Crary, J. F., Trojanowski, J. Q., Schneider, J. A., Abisambra, J. F., Abner, E. L., Alafuzoff, I., Arnold, S. E., Attems, J., Beach, T. G., Bigio, E. H., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1349-0 · Cited by 1,467 · see citing works

Lysosomal Proteolysis and Autophagy Require Presenilin 1 and Are Disrupted by Alzheimer-Related PS1 Mutations

Lee, J.-H., Yu, W. H., Kumar, A., Lee, S., Mohan, P. S., Peterhoff, C. M., Wolfe, D. M., Martinez-Vicente, M., Massey, A. C., Sovak, G., et al. (2010) · Cell · doi:10.1016/j.cell.2010.05.008 · Cited by 1,212 · see citing works

Lysosome-targeting chimaeras for degradation of extracellular proteins

Banik, S. M., Pedram, K., Wisnovsky, S., Ahn, G., Riley, N. M., & Bertozzi, C. R. (2020) · Nature · doi:10.1038/s41586-020-2545-9 · Cited by 1,199 · see citing works

Tau PET patterns mirror clinical and neuroanatomical variability in Alzheimer’s disease

Ossenkoppele, R., Schonhaut, D. R., Schöll, M., Lockhart, S. N., Ayakta, N., Baker, S. L., O’Neil, J. P., Janabi, M., Lazaris, A., Cantwell, A., et al. (2016) · Brain · doi:10.1093/brain/aww027 · Cited by 1,185 · see citing works

Tau-targeting therapies for Alzheimer disease

Congdon, E. E., & Sigurdsson, E. M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0013-z · Cited by 1,113 · cited 7× · see citing works

Mannose 6-phosphate receptors: new twists in the tale

Ghosh, P., Dahms, N. M., & Kornfeld, S. A. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1050 · Cited by 1,086 · see citing works

Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease

Augustinack, J. C., Schneider, A., Mandelkow, E.-M., & Hyman, B. T. (2002) · Acta Neuropathologica · doi:10.1007/s004010100423 · Cited by 998 · see citing works

Distinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies

Sanders, D. W., Kaufman, S. K., DeVos, S. L., Sharma, A. M., Mirbaha, H., Li, A., Barker, S. J., Foley, A. C., Thorpe, J. R., Serpell, L. C., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.04.047 · Cited by 986 · see citing works

A critical appraisal of amyloid-β-targeting therapies for Alzheimer disease

Panza, F., Lozupone, M., Logroscino, G., & Imbimbo, B. P. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-018-0116-6 · Cited by 965 · see citing works

Impaired Proteasome Function in Alzheimer's Disease

Keller, J. N., Hanni, K. B., & Markesbery, W. R. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750436.x · Cited by 848 · see citing works

Ubiquitin Is a Component of Paired Helical Filaments in Alzheimer's Disease

Mori, H., Kondo, J., & Ihara, Y. (1987) · Science · doi:10.1126/science.3029875 · Cited by 843 · see citing works

Structures of filaments from Pick’s disease reveal a novel tau protein fold

Falcon, B., Zhang, W., Murzin, A. G., Murshudov, G. N., Garringer, H. J., Vidal, R., Crowther, R. A., Ghetti, B. F., Scheres, S. H. W., & Goedert, M. (2018) · Nature · doi:10.1038/s41586-018-0454-y · Cited by 837 · see citing works

O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease

Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W., & Gong, C.-X. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400348101 · Cited by 775 · see citing works

Brain homogenates from human tauopathies induce tau inclusions in mouse brain

Clavaguera, F., Akatsu, H., Fraser, G. M., Crowther, R. A., Frank, S., Hench, J., Probst, A., Winkler, D. T., Reichwald, J., Staufenbiel, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301175110 · Cited by 750 · see citing works

The therapeutic potential of nanobodies

Jovčevska, I., & Muyldermans, S. (2020) · BioDrugs · doi:10.1007/s40259-019-00392-z · Cited by 749 · see citing works

Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules

Falcon, B., Zivanov, J., Zhang, W., Murzin, A. G., Garringer, H. J., Vidal, R., Crowther, R. A., Newell, K. L., Ghetti, B. F., Goedert, M., et al. (2019) · Nature · doi:10.1038/s41586-019-1026-5 · Cited by 703 · see citing works

Tau PTM Profiles Identify Patient Heterogeneity and Stages of Alzheimer’s Disease

Wesseling, H., Mair, W., Kumar, M., Schlaffner, C. N., Tang, S., Beerepoot, P., Fatou, B., Guise, A. J., Cheng, L., Takeda, S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.029 · Cited by 688 · see citing works

AUTACs: Cargo-Specific Degraders Using Selective Autophagy

Takahashi, D., Moriyama, J., Nakamura, T., Miki, E., Takahashi, E., Sato, A., Akaike, T., Itto-Nakama, K., & Arimoto, H. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.009 · Cited by 675 · see citing works

LYTACs that engage the asialoglycoprotein receptor for targeted protein degradation

Ahn, G., Banik, S. M., Miller, C. L., Riley, N. M., Cochran, J. R., & Bertozzi, C. R. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00770-1 · Cited by 654 · see citing works

Distribution of Alzheimer-type pathologic changes in nondemented elderly individuals matches the pattern in Alzheimer’s disease

Arriagada, P. V., Marzloff, K., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.9.1681 · Cited by 638 · see citing works

Faulty autolysosome acidification in Alzheimer’s disease mouse models induces autophagic build-up of Aβ in neurons, yielding senile plaques

Lee, J.-H., Yang, D.-S., Goulbourne, C. N., Im, E., Stavrides, P., Pensalfini, A., Chan, H., Bouchet-Marquis, C., Bleiwas, C., Berg, M. J., et al. (2022) · Nature Neuroscience · doi:10.1038/s41593-022-01084-8 · Cited by 638 · see citing works

Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains.

Perry, G., Friedman, R., Shaw, G., & Chau, V (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.9.3033 · Cited by 623 · see citing works

Tau Kinetics in Neurons and the Human Central Nervous System

Sato, C., Barthélemy, N. R., Mawuenyega, K. G., Patterson, B. W., Gordon, B. A., Jockel-Balsarotti, J., Sullivan, M., Crisp, M. J., Kasten, T., Kirmess, K. M., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.02.015 · Cited by 586 · see citing works

Anti-Tau Antibodies that Block Tau Aggregate Seeding In Vitro Markedly Decrease Pathology and Improve Cognition In Vivo

Yanamandra, K., Kfoury, N., Jiang, H., Mahan, T. E., Ma, S., Maloney, S. E., Wozniak, D. F., Diamond, M. I., & Holtzman, D. M. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.046 · Cited by 574 · see citing works

Trans-cellular Propagation of Tau Aggregation by Fibrillar Species

Kfoury, N., Holmes, B. B., Jiang, H., Holtzman, D. M., & Diamond, M. I. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.346072 · Cited by 552 · see citing works

Development of Antibody-Based PROTACs for the Degradation of the Cell-Surface Immune Checkpoint Protein PD-L1

Cotton, A. D., Nguyen, D. P., Gramespacher, J. A., Seiple, I. B., & Wells, J. A. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.0c10008 · Cited by 551 · see citing works

Novel tau filament fold in corticobasal degeneration

Zhang, W., Tarutani, A., Newell, K. L., Murzin, A. G., Matsubara, T., Falcon, B., Vidal, R., Garringer, H. J., Shi, Y., Ikeuchi, T., et al. (2020) · Nature · doi:10.1038/s41586-020-2043-0 · Cited by 546 · see citing works

Effects of α-Synuclein Immunization in a Mouse Model of Parkinson’s Disease

Masliah, E., Rockenstein, E., Adame, A., Alford, M., Crews, L., Hashimoto, M., Seubert, P., Lee, M., Goldstein, J., Chilcote, T., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.05.010 · Cited by 542 · see citing works

-Amyloid Oligomers Induce Phosphorylation of Tau and Inactivation of Insulin Receptor Substrate via c-Jun N-Terminal Kinase Signaling: Suppression by Omega-3 Fatty Acids and Curcumin

Ma, Q.-L., Yang, F., Rosario, E. R., Ubeda, O. J., Beech, W., Gant, D. J., Chen, P. P., Hudspeth, B., Chen, C., Zhao, Y., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1071-09.2009 · Cited by 536 · see citing works

Protective effects of NSAIDs on the development of Alzheimer disease

Vlad, S. C., Miller, D. R., Kowall, N. W., & Felson, D. T. (2008) · Neurology · doi:10.1212/01.wnl.0000311269.57716.63 · Cited by 535 · see citing works

Metabolic properties of IgG subclasses in man

Morell, A., Terry, W. D., & Waldmann, T. A. (1970) · Journal of Clinical Investigation · doi:10.1172/jci106279 · Cited by 530 · see citing works

Early and protective microglial activation in Alzheimer’s disease: a prospective study using¹⁸F-DPA-714 PET imaging

Hamelin, L., Lagarde, J., Dorothée, G., Leroy, C., Labit, M., Comley, R. A., de Souza, L. C., Corne, H., Dauphinot, L., Bertoux, M., et al. (2016) · Brain · doi:10.1093/brain/aww017 · Cited by 519 · see citing works

Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits

Min, S.-W., Chen, X., Tracy, T. E., Li, Y., Zhou, Y., Wang, C., Shirakawa, K., Minami, S. S., Defensor, E., Mok, S. A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3951 · Cited by 516 · see citing works

Immunotherapy Targeting Pathological Tau Conformers in a Tangle Mouse Model Reduces Brain Pathology with Associated Functional Improvements

Asuni, A. A., Boutajangout, A., Quartermain, D., & Sigurdsson, E. M. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.2361-07.2007 · Cited by 506 · see citing works

Reactive Glia not only Associates with Plaques but also Parallels Tangles in Alzheimer’s Disease

Serrano-Pozo, A., Mielke, M. L., Gómez-Isla, T., Betensky, R. A., Growdon, J. H., Frosch, M. P., & Hyman, B. T. (2011) · The American Journal of Pathology · doi:10.1016/j.ajpath.2011.05.047 · Cited by 488 · see citing works

Alzheimer disease therapy—moving from amyloid-β to tau

Giacobini, E., & Gold, G. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2013.223 · Cited by 483 · see citing works

The importance of tau phosphorylation for neurodegenerative diseases

Noble, W., Hanger, D. P., Miller, C. C. J., & Lovestone, S. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00083 · Cited by 475 · see citing works

Accuracy of a Panel of 5 Cerebrospinal Fluid Biomarkers in the Differential Diagnosis of Patients With Dementia and/or Parkinsonian Disorders

Hall, S., Öhrfelt, A., Constantinescu, R., Andreasson, U., Surova, Y., Bostrom, F., Nilsson, C., Widner, H., Decraemer, H., Nägga, K., et al. (2012) · Archives of Neurology · doi:10.1001/archneurol.2012.1654 · Cited by 473 · see citing works

Tau prion strains dictate patterns of cell pathology, progression rate, and regional vulnerability in vivo

Kaufman, S. K., Sanders, D. W., Thomas, T. L., Ruchinskas, A. J., Vaquer-Alicea, J., Sharma, A. M., Miller, T. M., & Diamond, M. I. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.055 · Cited by 450 · see citing works

Antibody against early driver of neurodegeneration cis P-tau blocks brain injury and tauopathy

Kondo, A., Shahpasand, K., Mannix, R., Qiu, J., Moncaster, J., Chen, C.-H., Yao, Y., Lin, Y.-M., Driver, J. A., Sun, Y., et al. (2015) · Nature · doi:10.1038/nature14658 · Cited by 445 · see citing works

Efficacy and safety of tau-aggregation inhibitor therapy in patients with mild or moderate Alzheimer's disease: a randomised, controlled, double-blind, parallel-arm, phase 3 trial

Gauthier, S., Feldman, H. H., Schneider, L. S., Wilcock, G. K., Frisoni, G. B., Hardlund, J. H., Moebius, H. J., Bentham, P., Kook, K. A., Wischik, D. J., et al. (2016) · The Lancet · doi:10.1016/s0140-6736(16)31275-2 · Cited by 427 · cited 1× · see citing works

Biological subtypes of Alzheimer disease

Ferreira, D., Nordberg, A. K., & Westman, E. (2020) · Neurology · doi:10.1212/wnl.0000000000009058 · Cited by 427 · see citing works

Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses.

Mandelkow, E., Stamer, K., Vogel, R., Thies, E., & Mandelkow, E. (2003) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.04.007 · Cited by 422 · see citing works

An early and late peak in microglial activation in Alzheimer’s disease trajectory

Fan, Z., Brooks, D. J., Okello, A., & Edison, P. (2017) · Brain · doi:10.1093/brain/aww349 · Cited by 422 · see citing works

c-Jun N-terminal Kinase (JNK) Signaling as a Therapeutic Target for Alzheimer’s Disease

Yarza, R., Vela, S., Solas, M., & Ramírez, M. J. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2015.00321 · Cited by 418 · see citing works

Glial contributions to neurodegeneration in tauopathies

Leyns, C. E. G., & Holtzman, D. M. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0192-x · Cited by 409 · see citing works

Increased level of active GSK‐3β in Alzheimer’s disease and accumulation in argyrophilic grains and in neurones at different stages of neurofibrillary degeneration

Leroy, K., Yilmaz, Z., & Brion, J. ‐. (2007) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2006.00795.x · Cited by 404 · see citing works

Current Concepts of Antigen Cross-Presentation

Embgenbroich, M., & Burgdorf, S. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01643 · Cited by 403 · see citing works

Posttranslational Modifications Mediate the Structural Diversity of Tauopathy Strains

Arakhamia, T., Lee, C. E., Carlomagno, Y., Kumar, M., Duong, D. M., Wesseling, H., Kundinger, S. R., Wang, K., Williams, D., Deture, M. A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.01.027 · Cited by 400 · see citing works

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

Neddens, J., Temmel, M., Flunkert, S., Kerschbaumer, B., Hoeller, C., Loeffler, T., Niederkofler, V., Daum, G., Attems, J., & Hutter-Paier, B. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0557-6 · Cited by 384 · see citing works

Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation

Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367 · see citing works

Memory and Brain Amyloid and Tau Effects of a Bioavailable Form of Curcumin in Non-Demented Adults: A Double-Blind, Placebo-Controlled 18-Month Trial

Small, G. W., Siddarth, P., Li, Z., Miller, K. J., Ercoli, L. M., Emerson, N. D., Martinez, J., Wong, K. P., Liu, J., Merrill, D. A., et al. (2017) · American Journal of Geriatric Psychiatry · doi:10.1016/j.jagp.2017.10.010 · Cited by 357 · see citing works

The AUTOTAC chemical biology platform for targeted protein degradation via the autophagy-lysosome system

Ji, C. H., Kim, H. Y., Lee, M. J., Heo, A. J., Park, D. Y., Lim, S., Shin, S., Ganipisetti, S., Yang, W. S., Jung, C. A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28520-4 · Cited by 350 · see citing works

Tau-targeting antisense oligonucleotide MAPTRx in mild Alzheimer’s disease: a phase 1b, randomized, placebo-controlled trial

Mummery, C. J., Börjesson-Hanson, A., Blackburn, D. J., Vijverberg, E. G. B., De Deyn, P. P., Ducharme, S., Jonsson, M., Schneider, A., Rinne, J. O., Ludolph, A. C., et al. (2023) · Nature Medicine · doi:10.1038/s41591-023-02326-3 · Cited by 347 · see citing works

Passive Immunization with Anti-Tau Antibodies in Two Transgenic Models

Chai, X., Wu, S., Murray, T. K., Kinley, R. D., Cella, C. V., Sims, H., Buckner, N., Hanmer, J. M., Davies, P., O’Neill, M. J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.229633 · Cited by 346 · see citing works

Chaperone-mediated autophagy prevents collapse of the neuronal metastable proteome

Bourdenx, M., Martín-Segura, A., Scrivo, A., Rodriguez-Navarro, J. A., Kaushik, S., Tasset, I., Diaz, A., Storm, N. J., Xin, Q., Juste, Y. R., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.048 · Cited by 337 · see citing works

Tauopathies: new perspectives and challenges

Zhang, Y., Wu, K.-M., Yang, L., Dong, Q., & Yu, J.-T. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00533-z · Cited by 323 · see citing works

Tau Oligomers: Cytotoxicity, Propagation, and Mitochondrial Damage

Shafiei, S. S., Guerrero-Muñoz, M. J., & Castillo-Carranza, D. L. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00083 · Cited by 314 · see citing works

Discovery of a Keap1-dependent peptide PROTAC to knockdown Tau by ubiquitination-proteasome degradation pathway

Lu, M., Liu, T., Jiao, Q., Ji, J., Tao, M., Liu, Y., You, Q., & Jiang, Z. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.01.063 · Cited by 310 · see citing works

Passive immunization targeting pathological phospho‐tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain

Boutajangout, A., Ingadottir, J., Davies, P., & Sigurdsson, E. M. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07337.x · Cited by 306 · see citing works

Safety and immunogenicity of the tau vaccine AADvac1 in patients with Alzheimer's disease: a randomised, double-blind, placebo-controlled, phase 1 trial

Novák, P., Schmidt, R., Kontseková, E., Žilka, N., Kováčech, B., Škrabana, R., Kazmerova, Z., Katina, S., Fialová, Ľ., Prčina, M., et al. (2016) · The Lancet Neurology · doi:10.1016/s1474-4422(16)30331-3 · Cited by 306 · see citing works

Past, present and future of therapeutic strategies against amyloid-β peptides in Alzheimer’s disease: a systematic review

Jeremic, D., Jiménez-Díaz, L., & Navarro-López, J. D. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101496 · Cited by 306 · see citing works

Protein phosphatase 2A dysfunction in Alzheimer’s disease

Sontag, J.-M., & Sontag, E. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00016 · Cited by 304 · see citing works

Amyloid Activates GSK-3β to Aggravate Neuronal Tauopathy in Bigenic Mice

Terwel, D., Muyllaert, D., Dewachter, I., Borghgraef, P., Croes, S., Devijver, H., & Van Leuven, F. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.070904 · Cited by 300 · see citing works

Therapeutic IgG4 antibodies engage in Fab-arm exchange with endogenous human IgG4 in vivo

Labrijn, A. F., Buijsse, A. O., van den Bremer, E. T. J., Verwilligen, A., Bleeker, W. K., Thorpe, S. J., Killestein, J., Polman, C. H., Aalberse, R. C., Schuurman, J., et al. (2009) · Nature Biotechnology · doi:10.1038/nbt.1553 · Cited by 297 · see citing works

Caspase-1 inhibition alleviates cognitive impairment and neuropathology in an Alzheimer’s disease mouse model

Flores, J., Noël, A., Foveau, B., Lynham, J., Lecrux, C., & LeBlanc, A. C. (2018) · Nature Communications · doi:10.1038/s41467-018-06449-x · Cited by 288 · see citing works

A walk through tau therapeutic strategies

Jadhav, S., Ávila, J., Schöll, M., Kovács, G. G., Kövari, E., Škrabana, R., Evans, L., Kontseková, E., Malawska, B., de Silva, R., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0664-z · Cited by 286 · see citing works

Sodium selenate mitigates tau pathology, neurodegeneration, and functional deficits in Alzheimer’s disease models

van Eersel, J., Ke, Y. D., Liu, X., Delerue, F., Kril, J. J., Götz, J., & Ittner, L. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009038107 · Cited by 284 · see citing works

Targeted degradation of aberrant tau in frontotemporal dementia patient-derived neuronal cell models

Silva, M. C., Ferguson, F. M., Cai, Q., Donovan, K. A., Nandi, G., Patnaik, D., Zhang, T., Huang, H.-T., Lucente, D. E., Dickerson, B. C., et al. (2019) · eLife · doi:10.7554/elife.45457 · Cited by 283 · see citing works

Passive Immunization with Tau Oligomer Monoclonal Antibody Reverses Tauopathy Phenotypes without Affecting Hyperphosphorylated Neurofibrillary Tangles

Castillo-Carranza, D. L., Sengupta, U., Guerrero-Muñoz, M. J., Lasagna-Reeves, C. A., Gerson, J. E., Singh, G., Estes, D. M., Barrett, A. D. T., Dineley, K. T., Jackson, G. R., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.3192-13.2014 · Cited by 278 · cited 1× · see citing works

Protein S-guanylation by the biological signal 8-nitroguanosine 3′,5′-cyclic monophosphate

Sawa, T., Zaki, M. H., Okamoto, T., Akuta, T., Tokutomi, Y., Kim‐Mitsuyama, S., Ihara, H., Kobayashi, A., Yamamoto, M. P., Fujii, S., et al. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.33 · Cited by 273 · see citing works

Immunotherapy Targeting Pathological Tau Prevents Cognitive Decline in a New Tangle Mouse Model

Boutajangout, A., Quartermain, D., & Sigurdsson, E. M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4363-10.2010 · Cited by 272 · see citing works

Microglial activation correlates in vivo with both tau and amyloid in Alzheimer’s disease

Dani, M., Wood, M., Mizoguchi, R., Fan, Z., Walker, Z., Morgan, R., Hinz, R., Biju, M., Kuruvilla, T., Brooks, D. J., et al. (2018) · Brain · doi:10.1093/brain/awy188 · Cited by 270 · see citing works

Cryo-EM structures of tau filaments

Scheres, S. H. W., Zhang, W., Falcon, B., & Goedert, M. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.05.011 · Cited by 266 · see citing works

Loss of Bin1 Promotes the Propagation of Tau Pathology

Calafate, S., Flavin, W., Verstreken, P., & Moechars, D. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.063 · Cited by 265 · see citing works

Intraneuronal amyloid β oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo

Umeda, T., Tomiyama, T., Sakama, N., Tanaka, S., Lambert, M. P., Klein, W. L., & Mori, H. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22640 · Cited by 264 · see citing works

Molecular signatures underlying neurofibrillary tangle susceptibility in Alzheimer’s disease

Otero-Garcia, M., Mahajani, S. U., Wakhloo, D., Tang, W., Xue, Y.-Q., Morabito, S., Pan, J., Oberhauser, J., Madira, A. E., Shakouri, T., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.06.021 · Cited by 262 · see citing works

The relationships between neuroinflammation, beta-amyloid and tau deposition in Alzheimer’s disease: a longitudinal PET study

Ismail, R., Parbo, P., Madsen, L. S., Hansen, A. K., Hansen, K. V., Schaldemose, J. L., Kjeldsen, P. L., Stokholm, M. G., Gottrup, H., Eskildsen, S. F., et al. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01820-6 · Cited by 261 · see citing works

Exposure of rat hippocampal neurons to amyloid β peptide (25–35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3β

Takashima, A., Noguchi, K., Michel, G., Mercken, M., Hoshi, M., Ishiguro, K., & Imahori, K. (1996) · Neuroscience Letters · doi:10.1016/0304-3940(95)12257-5 · Cited by 260 · see citing works

Proline Isomer-Specific Antibodies Reveal the Early Pathogenic Tau Conformation in Alzheimer's Disease

Nakamura, K., Greenwood, A., Binder, L. I., Bigio, E. H., Denial, S., Nicholson, L. K., Zhou, X. Z., & Lu, K. P. (2012) · Cell · doi:10.1016/j.cell.2012.02.016 · Cited by 255 · see citing works

Effects of injected Alzheimer beta-amyloid cores in rat brain.

Frautschy, S. A., Baird, A., & Cole, G. M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.19.8362 · Cited by 254 · see citing works

Endocytic vesicle rupture is a conserved mechanism of cellular invasion by amyloid proteins

Flavin, W. P., Bousset, L., Green, Z. C., Chu, Y., Skarpathiotis, S., Chaney, M. J., Kordower, J. H., Melki, R., & Campbell, E. M. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1722-x · Cited by 254 · see citing works

CSF MTBR-tau243 is a specific biomarker of tau tangle pathology in Alzheimer’s disease

Horie, K., Salvadó, G., Barthélemy, N. R., Janelidze, S., Li, Y., He, Y., Saef, B., Chen, C. D., Jiang, H., Strandberg, O., et al. (2023) · Nature Medicine · doi:10.1038/s41591-023-02443-z · Cited by 249 · see citing works

First-in-man tau vaccine targeting structural determinants essential for pathological tau–tau interaction reduces tau oligomerisation and neurofibrillary degeneration in an Alzheimer’s disease model

Kontseková, E., Žilka, N., Kováčech, B., Novák, P., & Novák, M. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt278 · Cited by 248 · see citing works

Specific Knockdown of Endogenous Tau Protein by Peptide-Directed Ubiquitin-Proteasome Degradation

Chu, T.-T., Gao, N., Li, Q.-Q., Chen, P.-G., Yang, X.-F., Chen, Y.-X., Zhao, Y.-F., & Li, Y.-M. (2016) · Cell Chemical Biology · doi:10.1016/j.chembiol.2016.02.016 · Cited by 247 · see citing works

p62/SQSTM1/Sequestosome-1 is an N-recognin of the N-end rule pathway which modulates autophagosome biogenesis

Cha‐Molstad, H., Yu, J. E., Feng, Z., Lee, S. H., Kim, J. G., Yang, P., Han, B., Sung, K. W., Yoo, Y. D., Hwang, J., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00085-7 · Cited by 246 · see citing works

A novel small-molecule PROTAC selectively promotes tau clearance to improve cognitive functions in Alzheimer-like models

Wang, W., Zhou, Q., Jiang, T., Li, S., Ye, J., Zheng, J., Wang, X., Liu, Y., Deng, M., Ke, D., et al. (2021) · Theranostics · doi:10.7150/thno.55680 · Cited by 242 · see citing works

Microglial internalization and degradation of pathological tau is enhanced by an anti-tau monoclonal antibody

Luo, W., Liu, W., Hu, X., Hanna, M., Caravaca, A., & Paul, S. M. (2015) · Scientific Reports · doi:10.1038/srep11161 · Cited by 241 · see citing works

The Association of Tau With Mitochondrial Dysfunction in Alzheimer’s Disease

Cheng, Y., & Bai, F. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00163 · Cited by 239 · see citing works

Earliest Stages of Tau Conformational Changes are Related to the Appearance of a Sequence of Specific Phospho-Dependent Tau Epitopes in Alzheimer's Disease1

Luna-Muñoz, J., Chávez-Macías, L., García-Sierra, F., & Mena, R. (2007) · Journal of Alzheimer's Disease · doi:10.3233/jad-2007-12410 · Cited by 233 · see citing works

The non-fluent/agrammatic variant of primary progressive aphasia

Grossman, M. (2012) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70099-6 · Cited by 231 · see citing works

Human secreted tau increases amyloid-beta production

Bright, J., Hussain, S., Dang, V., Wright, S., Cooper, B., Byun, T., Ramos, C., Singh, A., Parry, G., Stagliano, N., et al. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.09.007 · Cited by 230 · see citing works

Cerebrospinal fluid profile in frontotemporal dementia and Alzheimer’s disease

Grossman, M., Farmer, J., Leight, S., Work, M., Moore, P., Van Deerlin, V., Pratico, D., Clark, C. M., Coslett, H. B., Chatterjee, A., et al. (2005) · Annals of Neurology · doi:10.1002/ana.20477 · Cited by 228 · see citing works

Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration

Pei, J.-J., Grundke-Iqbal, I., Iqbal, K., Bogdanovic, N., Winblad, B., & Cowburn, R. F. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00296-0 · Cited by 226 · see citing works

Reducing acetylated tau is neuroprotective in brain injury

Shin, M.-K., Vázquez-Rosa, E., Koh, Y., Dhar, M., Chaubey, K., Cintrón-Pérez, C. J., Barker, S., Miller, E., Franke, K., Noterman, M. F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.032 · Cited by 226 · see citing works

In vivo neurotoxicity of beta-amyloid [β(1–40)] and the β(25–35) fragment

Kowall, N. W., McKee, A. C., Yankner, B. A., & Beal, M. F. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90053-z · Cited by 224 · see citing works

Acetylated tau inhibits chaperone-mediated autophagy and promotes tau pathology propagation in mice

Caballero, B., Bourdenx, M., Luengo, E., Diaz, A., Sohn, P. D., Chen, X., Wang, C., Juste, Y. R., Wegmann, S., Patel, B., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22501-9 · Cited by 223 · see citing works

Potential of Low Dose Leuco-Methylthioninium Bis(Hydromethanesulphonate) (LMTM) Monotherapy for Treatment of Mild Alzheimer’s Disease: Cohort Analysis as Modified Primary Outcome in a Phase III Clinical Trial

Wilcock, G. K., Gauthier, S., Frisoni, G. B., Jia, J., Hardlund, J. H., Moebius, H. J., Bentham, P., Kook, K. A., Schelter, B. O., Wischik, D. J., et al. (2017) · Journal of Alzheimer's Disease · doi:10.3233/jad-170560 · Cited by 219 · see citing works

Cellular and pathological heterogeneity of primary tauopathies

Chung, D. C., Roemer, S. F., Petrucelli, L., & Dickson, D. W. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00476-x · Cited by 219 · see citing works

“Don’t Phos Over Tau”: recent developments in clinical biomarkers and therapies targeting tau phosphorylation in Alzheimer’s disease and other tauopathies

Xia, Y., Prokop, S., & Giasson, B. I. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00460-5 · Cited by 218 · see citing works

CSF biomarkers in frontotemporal lobar degeneration with known pathology

Bian, H., Van Swieten, J. C., Leight, S., Massimo, L., Wood, E., Forman, M., Moore, P., de Koning, I., Clark, C. M., Rosso, S., et al. (2008) · Neurology · doi:10.1212/01.wnl.0000311445.21321.fc · Cited by 216 · see citing works

Interplay of pathogenic forms of human tau with different autophagic pathways

Caballero, B., Wang, Y., Diaz, A., Tasset, I., Juste, Y. R., Stiller, B., Mandelkow, E., Mandelkow, E., & Cuervo, A. M. (2018) · Aging Cell · doi:10.1111/acel.12692 · Cited by 213 · see citing works

Curcumin Suppresses Soluble Tau Dimers and Corrects Molecular Chaperone, Synaptic, and Behavioral Deficits in Aged Human Tau Transgenic Mice

Ma, Q., Zuo, X., Yang, F., Ubeda, O. J., Gant, D. J., Alaverdyan, M., Teng, E., Hu, S., Chen, P., Maiti, P., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.393751 · Cited by 212 · see citing works

MAPT/Tau accumulation represses autophagy flux by disrupting IST1-regulated ESCRT-III complex formation: a vicious cycle in Alzheimer neurodegeneration

Feng, Q., Luo, Y., Zhang, X., Yang, X., Hong, X.-Y., Sun, D., Li, X., Hu, Y., Li, X., Zhang, J., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1633862 · Cited by 211 · see citing works

Activation of Ras-ERK Signaling and GSK-3 by Amyloid Precursor Protein and Amyloid Beta Facilitates Neurodegeneration in Alzheimer’s Disease

Kirouac, L., Rajic, A. J., Cribbs, D. H., & Padmanabhan, J. (2017) · eneuro · doi:10.1523/eneuro.0149-16.2017 · Cited by 207 · see citing works

Neuronal uptake of tau/pS422 antibody and reduced progression of tau pathology in a mouse model of Alzheimer‘s disease

Collin, L., Bohrmann, B., Göpfert, U., Oroszlan‐Szovik, K., Ozmen, L., & Grüninger, F. (2014) · Brain · doi:10.1093/brain/awu213 · Cited by 203 · see citing works

Charge-mediated influence of the antibody variable domain on FcRn-dependent pharmacokinetics

Schoch, A., Kettenberger, H., Mundigl, O., Winter, G., Engert, J., Heinrich, J., & Emrich, T. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1408766112 · Cited by 202 · see citing works

Cytosolic Fc receptor TRIM21 inhibits seeded tau aggregation

McEwan, W. A., Falcon, B., Vaysburd, M., Clift, D., Oblak, A. L., Ghetti, B., Goedert, M., & James, L. C. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1607215114 · Cited by 201 · see citing works

Antisense oligonucleotides

Scoles, D. R., Minikel, E. V., & Pulst, S. M. (2019) · Neurology Genetics · doi:10.1212/nxg.0000000000000323 · Cited by 201 · see citing works

A survey of Cdk5 activator p35 and p25 levels in Alzheimer's disease brains

Tseng, H.-C., Zhou, Y., Shen, Y., & Tsai, L.-H. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02934-4 · Cited by 198 · see citing works

Antibody Uptake into Neurons Occurs Primarily via Clathrin-dependent Fcγ Receptor Endocytosis and Is a Prerequisite for Acute Tau Protein Clearance

Congdon, E. E., Gu, J., Sait, H. B. R., & Sigurdsson, E. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.491001 · Cited by 195 · see citing works

Minocycline at 2 Different Dosages vs Placebo for Patients With Mild Alzheimer Disease: A Randomized Clinical Trial

Howard, R., Zubko, O., Bradley, R., Harper, E., Pank, L., O’Brien, J., Fox, C., Tabet, N., Livingston, G., Bentham, P., et al. (2020) · JAMA Neurology · doi:10.1001/jamaneurol.2019.3762 · Cited by 194 · see citing works

Combined effects of scanning ultrasound and a tau-specific single chain antibody in a tau transgenic mouse model

Nisbet, R. M., Van der Jeugd, A., Leinenga, G., Evans, H. T., Janowicz, P. W., & Götz, J. (2017) · Brain · doi:10.1093/brain/awx052 · Cited by 187 · 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

ADAMANT: a placebo-controlled randomized phase 2 study of AADvac1, an active immunotherapy against pathological tau in Alzheimer’s disease

Novak, P., Kovacech, B., Katina, S., Schmidt, R., Scheltens, P., Kontsekova, E., Ropele, S., Fialova, L., Kramberger, M., Paulenka-Ivanovova, N., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00070-2 · Cited by 187 · see citing works

Anti‐tau antibody reduces insoluble tau and decreases brain atrophy

Yanamandra, K., Jiang, H., Mahan, T. E., Maloney, S. E., Wozniak, D. F., Diamond, M. I., & Holtzman, D. M. (2015) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.176 · Cited by 185 · see citing works

Mannose 6-Phosphate Receptor Targeting and its Applications in Human Diseases

Gary‐Bobo, M., Nirdé, P., Jeanjean, A., Morère, A., & Garcia, M. (2007) · Current Medicinal Chemistry · doi:10.2174/092986707782794005 · Cited by 185 · see citing works

Tau – an inhibitor of deacetylase HDAC6 function

Perez, M., Santa‐Maria, I., De Barreda, E. G., Zhu, X., Cuadros, R., Cabrero, J. R., Sanchez‐Madrid, F., Dawson, H. N., Vitek, M. P., Perry, G., et al. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06102.x · Cited by 182 · see citing works

CSF tau microtubule binding region identifies tau tangle and clinical stages of Alzheimer’s disease

Horie, K., Barthélemy, N. R., Sato, C., & Bateman, R. J. (2021) · Brain · doi:10.1093/brain/awaa373 · Cited by 180 · see citing works

Tauopathy-like Abnormalities and Neurologic Deficits in Mice Immunized With Neuronal Tau Protein

Rosenmann, H., Grigoriadis, N., Karussis, D., Boimel, M., Touloumi, O., Ovadia, H., & Abramsky, O. (2006) · Archives of Neurology · doi:10.1001/archneur.63.10.1459 · Cited by 178 · see citing works

Distinct dynamic profiles of microglial activation are associated with progression of Alzheimer's disease

Hamelin, L., Lagarde, J., Dorothée, G., Potier, M. C., Corlier, F., Kuhnast, B., Caillé, F., Dubois, B., Fillon, L., Chupin, M., et al. (2018) · Brain · doi:10.1093/brain/awy079 · Cited by 177 · see citing works

Prevention of tau seeding and propagation by immunotherapy with a central tau epitope antibody

Albert, M., Mairet‐Coello, G., Danis, C., Lieger, S., Caillierez, R., Carrier, S., Skrobala, E., Landrieu, I., Michel, A., Schmitt, M., et al. (2019) · Brain · doi:10.1093/brain/awz100 · Cited by 177 · see citing works

Tau Proteolysis in the Pathogenesis of Tauopathies: Neurotoxic Fragments and Novel Biomarkers

Quinn, J. P., Corbett, N. J., Kellett, K. A. B., & Hooper, N. M. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-170959 · Cited by 170 · see citing works

Compromised function of the ESCRT pathway promotes endolysosomal escape of tau seeds and propagation of tau aggregation

Chen, J. J., Nathaniel, D. L., Raghavan, P., Nelson, M., Tian, R., Tse, E., Hong, J. Y., See, S. K., Mok, S.-A., Hein, M. Y., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009432 · Cited by 170 · see citing works

bioPROTACs as versatile modulators of intracellular therapeutic targets including proliferating cell nuclear antigen (PCNA)

Lim, S., Khoo, R., Peh, K. M., Teo, J., Chang, S. C., Ng, S., Beilhartz, G. L., Melnyk, R. A., Johannes, C. W., Brown, C. J., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1920251117 · Cited by 170 · see citing works

Sodium selenate specifically activates PP2A phosphatase, dephosphorylates tau and reverses memory deficits in an Alzheimer’s disease model

Corcoran, N. M., Martin, D., Hutter‐Paier, B., Windisch, M., Nguyen, T. T., Nheu, L., Sundström, L., Costello, A. J., & Hovens, C. M. (2010) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2010.04.020 · Cited by 168 · see citing works

Tau Oligomers: The Toxic Player at Synapses in Alzheimer’s Disease

Guerrero-Muñoz, M. J., Gerson, J., & Castillo-Carranza, D. L. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00464 · Cited by 168 · see citing works

Curcumin Inhibits Tau Aggregation and Disintegrates Preformed Tau Filaments in vitro

Rane, J. S., Bhaumik, P., & Panda, D. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170351 · Cited by 165 · see citing works

Effect of intraventricular injection of an anti-Purkinje cell antibody (anti-Yo) in a guinea pig model

Graus, F., Illa, I., Agustí, M., Ribalta, T., Cruz-Sánchez, F., & Juárez, C. (1991) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(91)90198-g · Cited by 164 · see citing works

Two Novel Tau Antibodies Targeting the 396/404 Region Are Primarily Taken Up by Neurons and Reduce Tau Protein Pathology

Gu, J., Congdon, E. E., & Sigurdsson, E. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.494922 · Cited by 163 · see citing works

The Translocon Protein Sec61 Mediates Antigen Transport from Endosomes in the Cytosol for Cross-Presentation to CD8+ T Cells

Zehner, M., Marschall, A. L. J., Bos, E., Schloetel, J.-G., Kreer, C., Fehrenschild, D., Limmer, A., OSSENDORP, F. A., Lang, T., Koster, A. J., et al. (2015) · Immunity · doi:10.1016/j.immuni.2015.04.008 · Cited by 160 · see citing works

Abeta42-Induced Neurodegeneration via an Age-Dependent Autophagic-Lysosomal Injury in Drosophila

Ling, D., Song, H., Garza, D., Neufeld, T. P., & Salvaterra, P. M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004201 · Cited by 160 · see citing works

C-Terminally Truncated Forms of Tau, But Not Full-Length Tau or Its C-Terminal Fragments, Are Released from Neurons Independently of Cell Death

Kanmert, D., Cantlon, A., Muratore, C., Jin, M., O’Malley, T. T., Lee, G. S., Young‐Pearse, T. L., Selkoe, D. J., & Walsh, D. M. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.0387-15.2015 · Cited by 159 · see citing works

Characterization of mAb AP422, a novel phosphorylation‐dependent monoclonal antibody against tau protein

Hasegawa, M., Jakes, R., Crowther, R. A., Lee, V. M.-Y., Ihara, Y., & Goedert, M. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00271-2 · Cited by 156 · see citing works

New roles for Fc receptors in neurodegeneration-the impact on Immunotherapy for Alzheimer's Disease

Fuller, J. P., Stavenhagen, J. B., & Teeling, J. L. (2014) · Frontiers in Neuroscience · doi:10.3389/fnins.2014.00235 · Cited by 154 · see citing works

Lipid peroxidation causes endosomal antigen release for cross-presentation

Dingjan, I., Verboogen, D. R. J., Paardekooper, L. M., Revelo, N. H., Sittig, S. P., Visser, L. J., von Mollard, G. F., Henriet, S., Figdor, C. G., ter Beest, M., et al. (2016) · Scientific Reports · doi:10.1038/srep22064 · Cited by 153 · see citing works

Cis P-tau is induced in clinical and preclinical brain injury and contributes to post-injury sequelae

Albayram, Ö., Kondo, A., Mannix, R., Smith, C., Tsai, C.-Y., Li, C., Herbert, M. K., Qiu, J., Monuteaux, M. C., Driver, J. A., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01068-4 · Cited by 152 · see citing works

Tau Phosphorylation Rates Measured by Mass Spectrometry Differ in the Intracellular Brain vs. Extracellular Cerebrospinal Fluid Compartments and Are Differentially Affected by Alzheimer’s Disease

Barthélemy, N. R., Mallipeddi, N., Moiseyev, P., Sato, C., & Bateman, R. J. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00121 · Cited by 152 · see citing works

The aging lysosome: An essential catalyst for late-onset neurodegenerative diseases

Nixon, R. A. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140443 · Cited by 149 · see citing works

Glial cells in Alzheimer’s disease: From neuropathological changes to therapeutic implications

Uddin, M. S., & Lim, L. W. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101622 · Cited by 149 · see citing works

FUNDAMANT: an interventional 72-week phase 1 follow-up study of AADvac1, an active immunotherapy against tau protein pathology in Alzheimer's disease

Novak, P., Schmidt, R., Kontsekova, E., Kovacech, B., Smolek, T., Katina, S., Fialova, L., Prcina, M., Parrak, V., Dal-Bianco, P., et al. (2018) · Alzheimer's Research & Therapy · doi:10.1186/s13195-018-0436-1 · Cited by 147 · see citing works

Hyperphosphorylation and Cleavage at D421 Enhance Tau Secretion

Plouffe, V., Mohamed, N., Rivest‐McGraw, J., Bertrand, J., Lauzon, M., & Leclerc, N. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036873 · Cited by 146 · see citing works

Safety and efficacy of tilavonemab in progressive supranuclear palsy: a phase 2, randomised, placebo-controlled trial

Höglinger, G. U., Litvan, I., Mendonça, N., Wang, D., Zheng, H., Rendenbach‐Mueller, B., Lon, H., Jin, Z., Fisseha, N., Budur, K. S., et al. (2021) · The Lancet Neurology · doi:10.1016/s1474-4422(20)30489-0 · Cited by 146 · see citing works

Safety and efficacy of anti-tau monoclonal antibody gosuranemab in progressive supranuclear palsy: a phase 2, randomized, placebo-controlled trial

Dam, T., Boxer, A. L., Golbe, L. I., Höglinger, G. U., Morris, H. R., Litvan, I., Lang, A. E., Corvol, J., Aiba, I., Grundman, M., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01455-x · Cited by 146 · see citing works

Interaction of Tau Protein with Model Lipid Membranes Induces Tau Structural Compaction and Membrane Disruption

Jones, E. M., Dubey, M. K., Camp, P. J., Vernon, B. C., Biernat, J., Mandelkow�, E., Majewski, J. P., & Chi, E. Y. (2012) · Biochemistry · doi:10.1021/bi201857v · Cited by 145 · see citing works

Tau Passive Immunotherapy in Mutant P301L Mice: Antibody Affinity versus Specificity

d’Abramo, C., Acker, C. M., Jimenez, H. T., & Davies, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062402 · Cited by 144 · see citing works

FLEXITau: Quantifying Post-translational Modifications of Tau Protein in Vitro and in Human Disease

Mair, W., Muntel, J., Tepper, K., Tang, S., Biernat, J., Seeley, W. W., Kosik, K. S., Mandelkow�, E., Steen, H., & Steen, J. A. J. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04509 · Cited by 144 · see citing works

Balancing charge in the complementarity-determining regions of humanized mAbs without affecting pI reduces non-specific binding and improves the pharmacokinetics

Datta‐Mannan, A., Thangaraju, A., Leung, D., Tang, Y., Witcher, D. R., Lu, J., & Wroblewski, V. J. (2015) · mAbs · doi:10.1080/19420862.2015.1016696 · Cited by 141 · see citing works

Differential Mass Spectrometry Profiles of Tau Protein in the Cerebrospinal Fluid of Patients with Alzheimer’s Disease, Progressive Supranuclear Palsy, and Dementia with Lewy Bodies

Barthélemy, N. R., Gabelle, A., Hirtz, C., Fenaille, F., Sergeant, N., Schraen-Maschke, S., Vialaret, J., Buée, L., Junot, C., Becher, F., et al. (2016) · Journal of Alzheimer’s Disease · doi:10.3233/jad-150962 · Cited by 139 · see citing works

Isotype modulates epitope specificity, affinity, and antiviral activities of anti–HIV-1 human broadly neutralizing 2F5 antibody

Tudor, D., Yu, H., Maupetit, J., Drillet, A.-S., Bouceba, T., Schwartz-Cornil, I., Lopalco, L., Tufféry, P., & Bomsel, M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1200024109 · Cited by 137 · see citing works

Preventive methylene blue treatment preserves cognition in mice expressing full-length pro-aggregant human Tau

Hochgräfe, K., Sydow, A., Matenia, D., Cadinu, D., Könen, S., Petrova, O. M., Pickhardt, M., Goll, P., Morellini, F., Mandelkow�, E., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0204-4 · Cited by 137 · see citing works

Tilavonemab in early Alzheimer’s disease: results from a phase 2, randomized, double-blind study

Florian, H., Wang, D., Arnold, S. E., Boada, M., Guo, Q., Jin, Z., Zheng, H., Fisseha, N., Kalluri, H. V., Rendenbach‐Mueller, B., et al. (2023) · Brain · doi:10.1093/brain/awad024 · Cited by 137 · see citing works

<i>In Vivo</i>Positron Emission Tomographic Imaging of Glial Responses to Amyloid-β and Tau Pathologies in Mouse Models of Alzheimer's Disease and Related Disorders

Maeda, J., Zhang, M.-R., Okauchi, T., Ji, B., Ono, M., Hattori, S., Kumata, K., Iwata, N., Saido, T. C., Trojanowski, J. Q., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3076-10.2011 · Cited by 136 · see citing works

Pre-clinical characterisation of E2814, a high-affinity antibody targeting the microtubule-binding repeat domain of tau for passive immunotherapy in Alzheimer’s disease

Roberts, M., Sevastou, I., Imaizumi, Y., Mistry, K., Talma, S., Dey, M., Gartlon, J., Ochiai, H., Zhou, Z., Akasofu, S., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-0884-2 · Cited by 135 · see citing works

Reactions to Multiple Ascending Doses of the Microtubule Stabilizer TPI-287 in Patients With Alzheimer Disease, Progressive Supranuclear Palsy, and Corticobasal Syndrome

Tsai, R. M., Miller, Z., KOESTLER, M. E., Rojas, J. C., Ljubenkov, P. A., Rosen, H. J., Rabinovici, G. D., Fagan, A. M., Cobigo, Y., Brown, J. A., et al. (2019) · JAMA Neurology · doi:10.1001/jamaneurol.2019.3812 · Cited by 134 · see citing works

Camelid single-domain antibodies: A versatile tool for in vivo imaging of extracellular and intracellular brain targets

Li, T., Vandesquille, M., Koukouli, F., Dudeffant, C., Youssef, I., Lenormand, P., Ganneau, C., Maskos, U., Czech, C., Grueninger, F., et al. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2016.09.019 · Cited by 133 · see citing works

The Immunoglobulin Heavy Chain Constant Region Affects Kinetic and Thermodynamic Parameters of Antibody Variable Region Interactions with Antigen

Torres, M., Fernaéndez-Fuentes, N., Fiser, A., & Casadevall, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700661200 · Cited by 132 · see citing works

Divergent CSF   alterations in two common tauopathies: Alzheimer's disease and progressive supranuclear palsy

Wagshal, D., Sankaranarayanan, S., Guss, V., Hall, T., Berisha, F., Lobach, I., Karydas, A., Voltarelli, L., Scherling, C., Heuer, H., et al. (2015) · Journal of Neurology, Neurosurgery &amp; Psychiatry · doi:10.1136/jnnp-2014-308004 · Cited by 132 · see citing works

Preclinical and Clinical Development of ABBV-8E12, a Humanized Anti-Tau Antibody, for Treatment of Alzheimer's Disease and Other Tauopathies.

West, T., Hu, Y., Verghese, P. B., Bateman, R. J., Braunstein, J. B., Fogelman, I., Budur, K., Florian, H., Mendonca, N., & Holtzman, D. M. (2017) · PubMed · doi:10.14283/jpad.2017.36 · Cited by 132 · 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

Exosomes induce endolysosomal permeabilization as a gateway by which exosomal tau seeds escape into the cytosol

Polanco, J. C., Hand, G. R., Briner, A., Li, C., & Götz, J. (2021) · Acta Neuropathologica · doi:10.1007/s00401-020-02254-3 · Cited by 132 · see citing works

Epitope determines efficacy of therapeutic anti-Tau antibodies in a functional assay with human Alzheimer Tau

Courade, J., Angers, R. C., Mairet‐Coello, G., Pacico, N., Tyson, K. L., Lightwood, D. J., Munro, R., McMillan, D., Griffin, R., BAKER, T. S., et al. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1911-2 · Cited by 131 · see citing works

Antibody-Mediated Targeting of Tau In Vivo Does Not Require Effector Function and Microglial Engagement

Lee, S.-H., Le Pichon, C. E., Adolfsson, O., Gafner, V., Pihlgren, M., Lin, H., Solanoy, H., Brendza, R., Ngu, H., Foreman, O., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.06.099 · Cited by 125 · see citing works

Granulovacuolar degeneration (GVD) bodies of Alzheimer's disease (AD) resemble late-stage autophagic organelles

Funk, K. E., Mrak, R. E., & Kuret, J. (2010) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2010.01135.x · Cited by 123 · see citing works

Minocycline reduces the development of abnormal tau species in models of Alzheimer's disease

Noble, W., Garwood, C., Stephenson, J., Kinsey, A. M., Hanger, D., & Anderton, B. (2009) · The FASEB Journal · doi:10.1096/fj.08-113795 · Cited by 123 · see citing works

Tau Protein Quantification in Human Cerebrospinal Fluid by Targeted Mass Spectrometry at High Sequence Coverage Provides Insights into Its Primary Structure Heterogeneity

Barthélemy, N. R., Fenaille, F., Hirtz, C., Sergeant, N., Schraen-Maschke, S., Vialaret, J., Buée, L., Gabelle, A., Junot, C., Lehmann, S., et al. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b01001 · Cited by 123 · see citing works

Framework selection can influence pharmacokinetics of a humanized therapeutic antibody through differences in molecule charge

Li, B., Tesar, D. B., Boswell, C. A., Cahaya, H. S., Wong, A., Zhang, J., Meng, Y. G., Eigenbrot, C. W., Pantua, H., Diao, J., et al. (2014) · mAbs · doi:10.4161/mabs.29809 · Cited by 122 · see citing works

Ceria Nanoparticles Stabilized by Organic Surface Coatings Activate the Lysosome-Autophagy System and Enhance Autophagic Clearance

Song, W., Lee, S. S., Savini, M., Popp, L., Colvin, V. L., & Segatori, L. (2014) · ACS Nano · doi:10.1021/nn505073u · Cited by 121 · see citing works

Involvement of in the abnormal hyperphosphorylation of tau and its reversal by Memantine

Chohan, M. O., Khatoon, S., Iqbal, I.-G., & Iqbal, K. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.06.021 · Cited by 120 · see citing works

The Role of Tau Oligomers in the Onset of Alzheimer's Disease Neuropathology

Cárdenas-Aguayo, M. D. C., Gómez-Virgilio, L., DeRosa, S., & Meraz-Ríos, M. A. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500148z · Cited by 120 · see citing works

Tau Antibody Targeting Pathological Species Blocks Neuronal Uptake and Interneuron Propagation of Tau in Vitro

Nobuhara, C. K., DeVos, S. L., Commins, C., Wegmann, S., Moore, B. D., Roe, A. D., Costantino, I., Frosch, M. P., Pitstick, R., Carlson, G. A., et al. (2017) · The American Journal of Pathology · doi:10.1016/j.ajpath.2017.01.022 · Cited by 120 · see citing works

AβPP induces cdk5-dependent tau hyperphosphorylation in transgenic mice Tg2576

Carola Otth, L., Concha, I. I., Arendt, T., Stieler, J., Schliebs, R., González-Billault, C. E., & Maccioni, R. B. (2002) · Journal of Alzheimer s Disease · doi:10.3233/jad-2002-4508 · Cited by 119 · see citing works

In vivo Patterns of Tau Pathology, Amyloid-β Burden, and Neuronal Dysfunction in Clinical Variants of Alzheimer’s Disease

Dronse, J., Fließbach, K., Bischof, G. N., von Reutern, B., Faber, J., Hammes, J., Kuhnert, G., Neumaier, B., Onur, O. A., Kukolja, J., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160316 · Cited by 118 · see citing works

A human single-chain Fv intrabody blocks aberrant cellular effects of overexpressed α-synuclein

Zhou, C., Emadi, S., Sierks, M. R., & Messer, A. C. (2004) · Molecular Therapy · doi:10.1016/j.ymthe.2004.08.019 · Cited by 117 · see citing works

Posttranslational modifications of α-tubulin in alzheimer disease

Zhang, F., Su, B., Wang, C., Siedlak, S. L., Mondragón‐Rodríguez, S., Lee, H., Wang, X., Perry, G. L., & Zhu, X. (2015) · Translational Neurodegeneration · doi:10.1186/s40035-015-0030-4 · Cited by 116 · see citing works

Safety of the tau-directed monoclonal antibody BIIB092 in progressive supranuclear palsy: a randomised, placebo-controlled, multiple ascending dose phase 1b trial.

Boxer, A., Qureshi, I., Ahlijanian, M., Grundman, M., Golbe, L., Litvan, I., Honig, L. S., Tuite, P., McFarland, N. R., O'Suilleabhain, P., et al. (2019) · Lancet Neurology · doi:10.1016/s1474-4422(19)30139-5 · Cited by 115 · see citing works

Randomized Phase II Study of the Safety and Efficacy of Semorinemab in Participants With Mild-to-Moderate Alzheimer Disease: Lauriet

Monteiro, C., Tóth, B. I., Brunstein, F., Bobbala, A., Datta, S., Ceniceros, R., Bohorquez, S. M. S., Anania, V. G., Wildsmith, K. R., Schauer, S. P., et al. (2023) · Neurology · doi:10.1212/wnl.0000000000207663 · Cited by 113 · see citing works

Distinct Therapeutic Mechanisms of Tau Antibodies

Funk, K. E., Mirbaha, H., Jiang, H., Holtzman, D. M., & Diamond, M. I. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.657924 · Cited by 111 · see citing works

Meta-analysis of nonsteroidal antiinflammatory drug use and risk of dementia.

de Craen, A. D., Gussekloo, J., Vrijsen, B., & Westendorp, R. (2005) · American Journal of Epidemiology · doi:10.1093/aje/kwi029 · Cited by 111 · see citing works

Glial Tau Pathology in Tauopathies: Functional Consequences

Kahlson, M. A., & Colodner, K. J. (2015) · Journal of Experimental Neuroscience · doi:10.4137/jen.s25515 · Cited by 110 · see citing works

Microglial activation in early Alzheimer trajectory is associated with higher gray matter volume

Femminella, G. D., Dani, M., Wood, M., Fan, Z., Calsolaro, V., Atkinson, R., Edginton, T. L., Hinz, R., Brooks, D. J., & Edison, P. (2019) · Neurology · doi:10.1212/wnl.0000000000007133 · Cited by 109 · see citing works

Human tau pathology transmits glial tau aggregates in the absence of neuronal tau

Narasimhan, S., Changolkar, L. N., Riddle, D. M., Kats, A. S., Stieber, A., Weitzman, S. A., Zhang, B., Li, Z., Roberson, E. D., Trojanowski, J. Q., et al. (2019) · The Journal of Experimental Medicine · doi:10.1084/jem.20190783 · Cited by 109 · see citing works

Antibody semorinemab reduces tau pathology in a transgenic mouse model and engages tau in patients with Alzheimer’s disease

Ayalon, G., Lee, S.-H., Adolfsson, O., Foo‐Atkins, C., Atwal, J. K., Blendstrup, M., Booler, H. S., Bravo, J., Brendza, R. P., Brunstein, F., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abb2639 · Cited by 108 · see citing works

Tau Phosphorylation by cdk5 and Fyn in Response to Amyloid Peptide Aβ25–35: Involvement of Lipid Rafts

Hernandez, P., Lee, G., Sjoberg, M., & Maccioni, R. B. (2009) · Journal of Alzheimer's Disease · doi:10.3233/jad-2009-0933 · Cited by 107 · see citing works

Truncation and activation of GSK-3β by calpain I: a molecular mechanism links to tau hyperphosphorylation in Alzheimer's disease

Jin, N., Yin, X., Yu, D., Cao, M., Gong, C., Iqbal, K., Ding, F., Gu, X., & Liu, F. (2015) · Scientific Reports · doi:10.1038/srep08187 · Cited by 107 · see citing works

Ultrastructural characteristics of tau filaments in tauopathies: Immuno‐electron microscopic demonstration of tau filaments in tauopathies

Arima, K. (2006) · Neuropathology · doi:10.1111/j.1440-1789.2006.00669.x · Cited by 106 · see citing works

Alzheimer’s disease: insights into pathology, molecular mechanisms, and therapy

Zheng, Q., & Wang, X. (2024) · Protein & Cell · doi:10.1093/procel/pwae026 · Cited by 454 · see citing works

Advance in peptide-based drug development: delivery platforms, therapeutics and vaccines

Xiao, W., Jiang, W., Chen, Z., Huang, Y., Mao, J., Zheng, W., Hu, Y., & Shi, J. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02107-5 · Cited by 449 · see citing works

Comparative efficacy, tolerability and acceptability of donanemab, lecanemab, aducanumab and lithium on cognitive function in mild cognitive impairment and Alzheimer's disease: A systematic review and network meta-analysis

Terao, I., & Kodama, W. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102203 · Cited by 134 · see citing works

Tau in neurodegenerative diseases: molecular mechanisms, biomarkers, and therapeutic strategies

Zhang, X., Wang, J., Zhang, Z., & Ye, K. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00429-6 · Cited by 106 · see citing works

Pathological mechanisms and treatment progression of Alzheimer’s disease

Zhang, J., Kong, G., Yang, J., Pang, L., & Li, X. (2025) · European journal of medical research · doi:10.1186/s40001-025-02886-9 · Cited by 94 · see citing works

Protein kinases in neurodegenerative diseases: current understandings and implications for drug discovery

Wu, X., Yang, Z., Zou, J., Gao, H., Shao, Z., Li, C., & Lei, P. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02179-x · Cited by 88 · see citing works

Membraneless organelles in health and disease: exploring the molecular basis, physiological roles and pathological implications

Li, Y., Liu, Y., Yu, X., Xu, Y., Pan, X., Sun, Y. E., Wang, Y., Song, Y.-H., & Shen, Z. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02013-w · Cited by 69 · see citing works

The Enigma of Tau Protein Aggregation: Mechanistic Insights and Future Challenges

Zheng, H., Sun, H., Cai, Q., & Tai, H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25094969 · Cited by 64 · see citing works

Alzheimer’s disease patient brain extracts induce multiple pathologies in novel vascularized neuroimmune organoids for disease modeling and drug discovery

Ji, Y., Chen, X., Wang, Z., Meek, C. J., McLean, J. L., Yang, Y., Yuan, C., Rochet, J., Liu, F., & Xu, R. (2025) · Molecular Psychiatry · doi:10.1038/s41380-025-03041-w · Cited by 65 · see citing works

Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review

Yang, J., Zhi, W., & Wang, L. (2024) · Molecules · doi:10.3390/molecules29122812 · Cited by 63 · see citing works

Insights into the use of biomarkers in clinical trials in Alzheimer's disease

Pascoal, T. A., Aguzzoli, C. S., Lussier, F. Z., Crivelli, L., Suemoto, C. K., Fortea, J., Rosa‐Neto, P., Zimmer, E. R., Ferreira, P. C. L., & Bellaver, B. (2024) · EBioMedicine · doi:10.1016/j.ebiom.2024.105322 · Cited by 55 · see citing works

Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease

Thawabteh, A. M., Ghanem, A. W., AbuMadi, S., Thaher, D., Jaghama, W., Karaman, D., & Karaman, R. (2024) · Molecules · doi:10.3390/molecules29215131 · Cited by 56 · see citing works

The evolving landscape of Alzheimer’s disease therapy: From Aβ to tau

Courade, J., Zetterberg, H., Höglinger, G. U., & Dewachter, I. (2025) · Cell · doi:10.1016/j.cell.2025.11.033 · Cited by 52 · see citing works

Tau-PET in early cortical Alzheimer brain regions in relation to mild behavioral impairment in older adults with either normal cognition or mild cognitive impairment

Naude, J., Wang, M., Leon, R., Smith, E. E., & Ismail, Z. (2024) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2024.02.006 · Cited by 49 · see citing works

Therapeutic Role of Heterocyclic Compounds in Neurodegenerative Diseases: Insights from Alzheimer’s and Parkinson’s Diseases

Puranik, N., & Song, M. (2025) · Neurology International · doi:10.3390/neurolint17020026 · Cited by 46 · see citing works

Photobiomodulation modulates mitochondrial energy metabolism and ameliorates neurological damage in an APP/PS1 mouse model of Alzheimer’s disease

Chen, H., Li, N., Liu, N., Zhu, H., Ma, C., Ye, Y., Shi, X., Luo, G., Dong, X., Tan, T., et al. (2025) · Alzheimer s Research & Therapy · doi:10.1186/s13195-025-01714-w · Cited by 49 · see citing works

Tau degradation in Alzheimer's disease: Mechanisms and therapeutic opportunities

Wang, L., Banesh, S., Kumar, R., Schedin‐Weiss, S., Tjernberg, L. O., & Winblad, B. G. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70048 · Cited by 45 · see citing works

A Nanozyme-Boosted MOF-CRISPR Platform for Treatment of Alzheimer’s Disease

Yang, J., Qin, G., Liu, Z., Zhang, H., Du, X., Ren, J., & Qu, X. (2024) · Nano Letters · doi:10.1021/acs.nanolett.4c02272 · Cited by 42 · see citing works

Myelin dysfunction in aging and brain disorders: mechanisms and therapeutic opportunities

Huang, Z., Zhang, Y., Zou, P., Zong, X., & Zhang, Q. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00861-w · Cited by 42 · see citing works

BACE1 Inhibitors for Alzheimer’s Disease: Current Challenges and Future Perspectives

Coimbra, J. R. M., Resende, R., Custódio, J. B., Salvador, J. A. R., & Santos, A. (2024) · Journal of Alzheimer's Disease · doi:10.3233/jad-240146 · Cited by 33 · see citing works

Roles of TREM2 in the Pathological Mechanism and the Therapeutic Strategies of Alzheimer's Disease

Lin, M., Yu, J., Zhang, W., Lao, F., & Huang, H. (2024) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2024.164 · Cited by 41 · see citing works

The Interplay of Protein Aggregation, Genetics, and Oxidative Stress in Alzheimer’s Disease: Role for Natural Antioxidants and Immunotherapeutics

Ali, J., Choe, K., Park, J. S., Park, H. Y., Kang, H., Park, T. J., & Kim, M.-O. (2024) · Antioxidants · doi:10.3390/antiox13070862 · Cited by 39 · see citing works

Ultrasmall iron-gallic acid coordination polymer nanoparticles for scavenging ROS and suppressing inflammation in tauopathy-induced Alzheimer's disease

Huang, J., Wu, F., Cao, W., Chen, Y., Yao, Q., Cen, P., Wang, J., Lu, H., Zhang, X. H., Zhou, R., et al. (2024) · Biomaterials · doi:10.1016/j.biomaterials.2024.123042 · Cited by 39 · see citing works

Biomarkers of synaptic degeneration in Alzheimer’s disease

Cheng, Q., Fan, Y., Zhang, P., Liu, H., Han, J., Yu, Q., Wang, X., Wu, S., & Lu, Z. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102642 · Cited by 37 · see citing works

Anti-amyloid-β Antibodies and Anti-tau Therapies for Alzheimer’s Disease: Recent Advances and Perspectives

Suzuki, N., Hatta, T., Ito, M., & Kusakabe, K. (2024) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c24-00069 · Cited by 39 · see citing works

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

Unlocking the secrets of aging: Epigenetic reader BRD4 as the target to combatting aging-related diseases

Sun, J., Gui, Y., Zhou, S., & Zheng, X. (2023) · Journal of Advanced Research · doi:10.1016/j.jare.2023.11.006 · Cited by 32 · see citing works

The roles of intrinsically disordered proteins in neurodegeneration

Utami, K. H., Morimoto, S., Mitsukura, Y., & Okano, H. (2025) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2025.130772 · Cited by 34 · see citing works

Chemical Synthesis Reveals Pathogenic Role of N-Glycosylation in Microtubule-Associated Protein Tau

Powell, W. C., Jing, R., Herlory, M., Holland, P., Poliyenko, D., Ebmeier, C. C., Stowell, M. H. B., & Walczak, M. A. A. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c17873 · Cited by 32 · see citing works

Exploring CAR-macrophages in non-tumor diseases: Therapeutic potential beyond cancer

Chen, Y., Xin, Q., Zhu, M., Qiu, J., Luo, Y., Li, R., Wei, W., & Tu, J. (2025) · Journal of Advanced Research · doi:10.1016/j.jare.2025.01.004 · Cited by 32 · see citing works

CRISPR/Cas9-Based therapeutics as a promising strategy for management of Alzheimer’s disease: progress and prospects

Khan, M. S., Qureshi, N., Khan, R., Son, Y., & Maqbool, T. (2025) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2025.1578138 · Cited by 33 · 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

Advancements and challenges in mouse models of Alzheimer’s disease

Qian, Z., Li, Y., & Ye, K. (2024) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2024.10.010 · Cited by 28 · see citing works

Advancements in Imaging Technologies and AI Integration for Neurodegenerative Disease Management: A Narrative Review

Xu, J., Gao, C., Zhang, J., Lu, J., Xuan, Y., Wang, S., & Bu, C. (2025) · Molecular Imaging · doi:10.1177/15353508251393056 · Cited by 31 · see citing works

Tau Immunotherapies for Alzheimer’s Disease and Related Tauopathies: Status of Trials and Insights from Preclinical Studies

Sigurdsson, E. M. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-231238 · Cited by 27 · see citing works

Targeted protein degradation in CNS disorders: a promising route to novel therapeutics?

Kuemper, S., Cairns, A. G., Birchall, K., Yao, Z., & Large, J. M. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1370509 · Cited by 27 · see citing works

Fecal Microbiota Transplantation in Alzheimer’s Disease: Mechanistic Insights Through the Microbiota–Gut–Brain Axis and Therapeutic Prospects

Ren, J., Wang, Q., Hong, H., & Tang, C. (2025) · Microorganisms · doi:10.3390/microorganisms13081956 · Cited by 27 · see citing works

CSF and plasma biomarkers in cerebral amyloid angiopathy: A single-center study and a systematic review/meta-analysis

Theodorou, A., Tsantzali, I., Stefanou, M., Sacco, S., Katsanos, A. H., Shoamanesh, A., Karapanayiotides, T., Koutroulou, I., Stamati, P., Werring, D. J., et al. (2024) · European Stroke Journal · doi:10.1177/23969873241260538 · Cited by 25 · see citing works

Alzheimer’s Disease Immunotherapy: Current Strategies and Future Prospects

Aljassabi, A., Zieneldien, T., Kim, J., Regmi, D., & Cao, C. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-231163 · Cited by 25 · see citing works

Microtubule-Targeting Agents: Advances in Tubulin Binding and Small Molecule Therapy for Gliomas and Neurodegenerative Diseases

Ezzo, M., & Etienne‐Manneville, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157652 · Cited by 24 · see citing works

Modulation of Tau Pathology in Alzheimer’s Disease by Dietary Bioactive Compounds

Shi, H., & Zhao, Y. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25020831 · Cited by 24 · see citing works

Enhancing Alzheimer's disease detection: An explainable machine learning approach with ensemble techniques

Mahamud, E., Assaduzzaman, M., Islam, J., Fahad, N., Hossen, M. J., & Ramanathan, T. (2025) · Intelligent Medicine · doi:10.1016/j.ibmed.2025.100240 · Cited by 26 · see citing works

Nrf2/Bach1 signaling axis: A promising multifaceted therapeutic strategy for Alzheimer's disease

Soni, P., Sharma, S. M., Pieper, A. A., Paul, B. D., & Thomas, B. (2025) · Neurotherapeutics · doi:10.1016/j.neurot.2025.e00586 · Cited by 22 · see citing works

Molecular Therapeutics in Development to Treat Alzheimer’s Disease

Tartaglia, M. C., & Ingelsson, M. (2024) · Molecular Diagnosis & Therapy · doi:10.1007/s40291-024-00738-6 · Cited by 22 · see citing works

An Anti-tau Therapeutic Antibody Etalanetug (E2814)

Rawal, S., Wildsmith, K. R., Aluri, J., Yagi, T., Chang, M., Niu, H., Zhou, J., Horie, K., Takahashi, E., Boyd, P., et al. (2025) · Alzheimer Disease & Associated Disorders · doi:10.1097/wad.0000000000000680 · Cited by 21 · see citing works

PROTAC: a revolutionary technology propelling small molecule drugs into the next golden age

Cai, J., Chen, C., Wang, J., Zhang, X., Cui, Y., Zhu, Q., & Sun, H. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1676414 · Cited by 21 · see citing works

Development of tau phosphorylation-targeting therapies for the treatment of neurodegenerative diseases

Su, J., Xiao, Y., Wang, X., Zheng, J., & Wang, J. (2024) · Medicine Plus · doi:10.1016/j.medp.2024.100060 · Cited by 21 · see citing works

Neuronal Vulnerability of the Entorhinal Cortex to Tau Pathology in Alzheimer’s Disease

Zhang, S., Crossley, C. A., & Yuan, Q. (2024) · British Journal of Biomedical Science · doi:10.3389/bjbs.2024.13169 · Cited by 20 · see citing works

Green-synthesized gold nanoparticles exhibit neuroprotective activity against oxidative stress-induced damage in SH-SY5Y cells

Nkentsha, Z., & Rambharose, S. (2025) · Journal of Nanoparticle Research · doi:10.1007/s11051-025-06387-y · Cited by 18 · see citing works

Rewired m6A of promoter antisense RNAs in Alzheimer’s disease regulates neuronal genes in 3D nucleome

Hu, B., Shi, Y., Xiong, F., Chen, Y.-T., Zhu, X., Carrillo, E. C., Wen, X., Drolet, N. A., Rajpurohit, C. S., Xu, X., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-60378-0 · Cited by 17 · see citing works

The Role of Amyloid-β and Tau PET in the New Era of Alzheimer Disease Therapies

Chiotis, K., Wang, Y.-B., Joie, R. L., & Rabinovici, G. (2025) · Journal of Nuclear Medicine · doi:10.2967/jnumed.124.268339 · Cited by 20 · see citing works

Immunological aspects of central neurodegeneration

Niso‐Santano, M., Fuentes, J. M., & Galluzzi, L. (2024) · Cell Discovery · doi:10.1038/s41421-024-00666-z · Cited by 16 · see citing works

Advancements in Pharmacological Treatment of Alzheimer’s Disease: The Advent of Disease-Modifying Therapies (DMTs)

Wang, Q., Chen, S., Wang, J., Shang, H., & Chen, X. (2024) · Brain Sciences · doi:10.3390/brainsci14100990 · Cited by 17 · see citing works

Peptide-based inhibitors and nanoparticles: Emerging therapeutics for Alzheimer’s disease

Mojarad-Jabali, S., & Roh, K. (2024) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2024.125055 · Cited by 17 · see citing works

Advancements in autophagy perturbations in Alzheimer’s disease: Molecular aspects and therapeutics

Dhapola, R., Kumari, S., Sharma, P., Vellingiri, B., & HariKrishnaReddy, D. (2025) · Brain Research · doi:10.1016/j.brainres.2025.149494 · Cited by 17 · see citing works

Identification of AS1842856 as a novel small‐molecule GSK3α/β inhibitor against Tauopathy by accelerating GSK3α/β exocytosis

He, D., Zhang, X., Su, J., Zhang, Q., Zhao, L., Wu, T., Hang, R., Jia, R., Lei, X., Hou, W., et al. (2024) · Aging Cell · doi:10.1111/acel.14336 · Cited by 16 · see citing works

Targeting USP11 regulation by a novel lithium-organic coordination compound improves neuropathologies and cognitive functions in Alzheimer transgenic mice

Guo, Y., Cai, C., Zhang, B., Tan, B., Tang, Q., Lei, Z., Qi, X., Chen, J., Zheng, X., Zi, D., et al. (2024) · EMBO Molecular Medicine · doi:10.1038/s44321-024-00146-7 · Cited by 16 · see citing works

Plasma phosphorylated-tau217 is increased in Niemann–Pick disease type C

González‐Ortiz, F., Karikari, T. K., Vruchte, D. T., Shepherd, D., Kirsebom, B., Fladby, T., Platt, F. M., & Blennow, K. (2024) · Brain Communications · doi:10.1093/braincomms/fcae375 · Cited by 15 · see citing works

Targeting ceramide-induced microglial pyroptosis: Icariin is a promising therapy for Alzheimer's disease

Li, H., Xiao, Q., Zhu, L., Kang, J. S., Zhan, Q., & Peng, W. (2024) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2024.101106 · Cited by 15 · see citing works

Advancements in Proteolysis Targeting Chimeras for Targeted Therapeutic Strategies in Alzheimer’s Disease

Zhou, Q., Wang, W., & Deng, C. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04838-0 · Cited by 15 · see citing works

Lysine lactylation in diseases: beyond histone lactylation

Liu, Y., Guo, X., Hu, X., Zhou, S., Yang, Q. E., Feng, P., & Zeng, L. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08223-6 · Cited by 15 · see citing works

Improvements in Exercise for Alzheimer’s Disease: Highlighting FGF21-Induced Cerebrovascular Protection

Wang, J., Meng, X., Jialun, Y., Tang, Y., Zeng, F., Wang, Y., Chen, Z., Chen, D., Zou, R., & Liu, W. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04350-w · Cited by 13 · see citing works

Immunization targeting diseased proteins in synucleinopathy and tauopathy: insights from clinical trials

Zhan, X., Wen, G., Wu, X., & Li, J. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00490-9 · Cited by 14 · see citing works

Nasal nanotherapeutics for central nervous system disorders: Bridging the translational gap in central nervous system drug delivery

Zhang, Y.-B., Liu, M., Wang, Y., Hu, D., Wu, S., Zhao, B., Zhou, B., & Yang, L. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.177958 · Cited by 13 · see citing works

Plant-Derived Exosome-Like Nanovesicles for CNS Drug Delivery and Gut–Brain Axis Modulation: A Narrative Review

Ding, L., Bian, Q., Mou, X., & Chang, X. (2025) · International Journal of Nanomedicine · doi:10.2147/ijn.s562305 · Cited by 13 · see citing works

Single-domain antibody-based protein degrader for synucleinopathies

Jiang, Y., Lin, Y., Tetlow, A. M., Pan, R., Ji, C., Kong, X., Congdon, E. E., & Sigurdsson, E. M. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00730-y · Cited by 13 · see citing works

Targeted protein degradation with bifunctional molecules as a novel therapeutic modality for Alzheimer's disease & beyond

Sandhof, C. A., Murray, H. F. B., Silva, M. C., & Haggarty, S. J. (2024) · Neurotherapeutics · doi:10.1016/j.neurot.2024.e00499 · Cited by 13 · see citing works

Protective Effects of Bifidobacterium Breve MCC1274 as a Novel Therapy for Alzheimer’s Disease

Abdelhamid, M., Counts, S., Zhou, C., Hida, H., Kim, J., Michikawa, M., & Jung, C. (2025) · Nutrients · doi:10.3390/nu17030558 · Cited by 16 · see citing works

A variant of the autophagic receptor NDP52 counteracts phospho-TAU accumulation and emerges as a protective factor for Alzheimer’s disease

Mattioni, A., Carsetti, C., Bruqi, K., Caputo, V., Cianfanelli, V., Bacalini, M. G., Casa, M., Gabelli, C., Giardina, E., Cestra, G., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07611-2 · Cited by 13 · see citing works

Tau in Alzheimer's disease: Shaping the future patient journey

Mummery, C. J., Li-Hsian, C. C., Lasagna‐Reeves, C. A., Ossenkoppele, R., Rowe, C. C., Scharre, D. W., Wang, H., Kyaga, S., & Cummings, J. L. (2026) · The Journal of Prevention of Alzheimer s Disease · doi:10.1016/j.tjpad.2025.100447 · Cited by 12 · see citing works

Diagnosing Alzheimer Disease

Day, G. S. (2024) · CONTINUUM Lifelong Learning in Neurology · doi:10.1212/con.0000000000001507 · Cited by 12 · see citing works

Application of the revised criteria for diagnosis and staging of Alzheimer's disease: Drug development and clinical practice

Jack, C. R., Graf, A., Burnham, S. C., Doty, E. G., Moebius, H. J., Montenigro, P. H., Siemers, E., Sink, K. M., Shaw, L. M. J., Hansen, C. T., et al. (2024) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.70013 · Cited by 13 · see citing works

Evolution of Alzheimer’s Disease Therapeutics: From Conventional Drugs to Medicinal Plants, Immunotherapy, Microbiotherapy and Nanotherapy

Ortiz-Islas, E., Montes, P., Rodríguez-Pérez, C. E., Ruiz-Sánchez, E., Sánchez-Barbosa, T., Pichardo-Rojas, D., Zavala‐Tecuapetla, C., Carvajal, K., & Campos‐Peña, V. (2025) · Pharmaceutics · doi:10.3390/pharmaceutics17010128 · Cited by 12 · see citing works

Design and synthesis of new 1,2,3-triazole-methoxyphenyl-1,3,4-oxadiazole derivatives: selective butyrylcholinesterase inhibitors against Alzheimer’s disease

Iraji, A., Hariri, R., Hashempur, M. H., Ghasemi, M., Pourtaher, H., Saeedi, M., & Akbarzadeh, T. (2025) · BMC Chemistry · doi:10.1186/s13065-025-01475-5 · Cited by 12 · see citing works

Glial phagocytosis for synapse and toxic proteins in neurodegenerative diseases

Choi, Y., & Chung, W. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00870-9 · Cited by 12 · see citing works

Design of Tau Aggregation Inhibitors Using Iterative Machine Learning and a Polymorph-Specific Brain-Seeded Fibril Amplification Assay

Santambrogio, A., Horne, R. I., Metrick, M. A., Gallagher, N. C. T., Brotzakis, Z. F., Rinauro, D. J., Vourkou, E., Papanikolopoulou, K., Skoulakis, E. M. C., Linse, S. S., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c12812 · Cited by 12 · see citing works

Systemic Treatment with siRNA Targeting Gamma-Secretase Activating Protein Inhibits Amyloid-β Accumulation in Alzheimer’s Disease

Kim, S., Ullah, I., Beloor, J., Chung, K., Kim, J.-K., Yi, Y., Kang, E., Yun, G., Heo, S., Pyun, S.-H., et al. (2024) · Biomaterials Research · doi:10.34133/bmr.0027 · Cited by 11 · see citing works

Dietary Flavonoid Chrysin Functions as a Dual Modulator to Attenuate Amyloid-β and Tau Pathology in the Models of Alzheimer’s Disease

Zhang, Z., Li, R., Zhou, Y., Huang, S., Hou, Y., & Pei, G. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04557-y · Cited by 11 · see citing works

O-GlcNAc modification differentially regulates microtubule binding and pathological conformations of tau isoforms in vitro

Alhadidy, M. M., Stemmer, P. M., & Kanaan, N. M. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108263 · Cited by 11 · see citing works

Overexpression of TGFBR3 Aggravates Cognitive Impairment and Neuroinflammation by Promoting Microglia M1 Polarization in the APP/PS1 Mouse Model of Alzheimer's Disease

Song, H., Xia, M., Zhao, P., Yang, J., & Yu, W. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04731-w · Cited by 11 · see citing works

Advancing Nanomaterial-Based Strategies for Alzheimer’s Disease: A Perspective

Zhou, H., Yin, X., Zhang, G., Yang, Z., & Zhou, R. (2025) · JACS Au · doi:10.1021/jacsau.5c00002 · Cited by 14 · see citing works

Clinical, imaging and blood biomarker outcomes in a Phase 3 clinical trial of tau aggregation inhibitor hydromethylthionine mesylate in mild cognitive impairment and mild to moderate dementia due to Alzheimer’s disease

Wischik, C. M., Stefanacci, R. G., Bentham, P., Gauthier, S. G., Zetterberg, H., Wilcock, G. K., Froelich, L., Burns, A. S., MacSweeney, E., Ballard, C. G., et al. (2026) · The Journal of Prevention of Alzheimer s Disease · doi:10.1016/j.tjpad.2026.100480 · Cited by 11 · see citing works

Leveraging Diverse Regulated Cell Death Patterns to Identify Diagnosis Biomarkers for Alzheimer's Disease

Ren, L., Zhang, Q., Zhou, J., Wang, X., Zhu, D., & Chen, X. (2024) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2024.119 · Cited by 10 · see citing works

Anti-tau single domain antibodies clear pathological tau and attenuate its toxicity and related functional defects

Nair, S., Jiang, Y., Marchal, I. S., Chernobelsky, E., Huang, H.-W., Suh, S., Pan, R., Kong, X., Ryoo, H. D., & Sigurdsson, E. M. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06927-9 · Cited by 10 · see citing works

Intrathecal Immunoselective Nanopheresis for Alzheimer’s Disease: What and How? Why and When?

Menéndez‐González, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910632 · Cited by 10 · see citing works

MAD—microbial (origin of) Alzheimer’s disease hypothesis: from infection and the antimicrobial response to disruption of key copper-based systems

Min, J.-H., Sarlus, H., & Harris, R. A. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1467333 · Cited by 11 · see citing works

Biomarkers for Alzheimer’s disease across diverse biological domains: an umbrella review and evidence map

Kang, J., Son, Y., Yim, Y., Cho, H., Kim, J., Lark, A. R. S., Mir, F. A., Kim, H. J., Park, J., Lee, H., et al. (2025) · Journal of Advanced Research · doi:10.1016/j.jare.2025.07.022 · Cited by 10 · see citing works

Biologics as Therapeutical Agents Under Perspective Clinical Studies for Alzheimer’s Disease

Li, H., Shen, X., Zhang, B., & Zhu, Z. (2025) · Molecules · doi:10.3390/molecules30173479 · Cited by 10 · see citing works

A Biomarker‐Based Classification of Corticobasal Syndrome

Palleis, C., Bernhardt, A. M., Weidinger, E., Fietzek, U. M., Jäck, A., Katzdobler, S., Gnörich, J. S., Bauer, T., Franzmeier, N., Perneczky, R., et al. (2025) · Movement Disorders · doi:10.1002/mds.70070 · Cited by 10 · see citing works

ROCK Inhibitor Fasudil Attenuates Neuroinflammation and Associated Metabolic Dysregulation in the Tau Transgenic Mouse Model of Alzheimer’s Disease

Ouyang, X., Collu, R., Benavides, G. A., Tian, R., Darley-Usmar, V. M., Xia, W., & Zhang, J. (2024) · Current Alzheimer Research · doi:10.2174/0115672050317608240531130204 · Cited by 9 · see citing works

Gene therapy in Aβ-induced cell and mouse models of Alzheimer’s disease through compensating defective mitochondrial complex I function

Li, H., Chen, Z., Shen, Y., Xiong, T., Chen, A., Chen, L., Ye, Y., Jiang, Q., Zhang, Y., Sun, J., et al. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05571-3 · Cited by 9 · see citing works

Diverse tau pathologies in late‐life mood disorders revealed by PET and autopsy assays

Kurose, S., Moriguchi, S., Kubota, M., Tagai, K., Momota, Y., Ichihashi, M., Sano, Y., Endo, H., Hirata, K., Kataoka, Y., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70195 · Cited by 9 · see citing works

Targeting tau in Alzheimer’s Disease: rationale, approach and challenges

Aslanyan, A., Foiani, M. S., Giovannucci, T. A., McDade, E., Duff, K., Mummery, C. J., Schöll, M., Wildsmith, K. R., & Paterson, R. W. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00925-5 · Cited by 10 · see citing works

Tubulin transforms Tau and α-synuclein condensates from pathological to physiological

Lucas, L., Tsoi, P. S., Quan, M. D., Choi, K., Ferreon, J. C., & Ferreon, A. C. M. (2026) · Nature Communications · doi:10.1038/s41467-026-69618-3 · Cited by 9 · see citing works

Targeting CB2 receptor with a novel antagonist reverses cognitive decline, neurodegeneration and pyroptosis in a TAU-dependent frontotemporal dementia mouse model

Silva-Llanes, I., Rodríguez-López, S., González-Naranjo, P., del Sastre, E., López, M. G., Paez, J. A., Campillo, N. E., & Lastres‐Becker, I. (2025) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2025.03.008 · Cited by 8 · see citing works

Biological Effects of Dietary Restriction on Alzheimer's Disease: Experimental and Clinical Investigations

Liu, Z., Zhang, J., Jiang, F., Liu, C., Shao, Y., & Le, W. (2025) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.70392 · Cited by 8 · see citing works

The Role of APOA-I in Alzheimer’s Disease: Bridging Peripheral Tissues and the Central Nervous System

Xie, G., Jiang, G., Huang, L., Sun, S., Wan, Y., Li, F., Wu, B., Zhang, Y., Li, X., Xiong, B., et al. (2025) · Pharmaceuticals · doi:10.3390/ph18060790 · Cited by 10 · see citing works

Tauopathies: Emerging discoveries on tau protein, with a special focus on Alzheimer's disease

Hattiholi, A., Hegde, H., & Shetty, S. K. (2025) · Neuropeptides · doi:10.1016/j.npep.2025.102536 · Cited by 10 · see citing works

Decoding tau acetylation in Alzheimer’s disease and tauopathies: from site-specific mechanisms to therapeutic horizons

Oh, Y. R., & Shin, M. (2025) · BMB Reports · doi:10.5483/bmbrep.2025-0077 · Cited by 9 · see citing works

Healthcare Complexities in Neurodegenerative Proteinopathies: A Narrative Review

Fereshtehnejad, S., & Lökk, J. (2025) · Healthcare · doi:10.3390/healthcare13151873 · Cited by 9 · see citing works

Tau-targeting therapies for Alzheimer disease

Congdon, E. E., & Sigurdsson, E. M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0013-z · Cited by 1,113 · see citing works

Tau-targeting therapy in Alzheimer’s disease: Critical advances and future opportunities

Guo, Y., Li, S., Zeng, L.-H., & Tan, J. (2022) · Ageing and Neurodegenerative Diseases · doi:10.20517/and.2022.16 · Cited by 61 · see citing works

Immunotherapy for the treatment of Alzheimer's disease: amyloid-β or tau, which is the right target?

Kayed, R., Castillo‐Carranza, D. L., & Guerrero‐Munoz, M. J. (2013) · ImmunoTargets and Therapy · doi:10.2147/itt.s40131 · Cited by 15 · see citing works

The evolving landscape of Alzheimer’s disease therapy: From Aβ to tau

Courade, J., Zetterberg, H., Höglinger, G. U., & Dewachter, I. (2025) · Cell · doi:10.1016/j.cell.2025.11.033 · Cited by 52 · see citing works

Tau-Based Therapeutic Approaches for Alzheimer's Disease - A Mini-Review

Boutajangout, A., & Wısnıewskı, T. (2014) · Gerontology · doi:10.1159/000358875 · Cited by 105 · see citing works