Tau filaments in neurodegenerative diseases

α-Synuclein in Lewy bodies

Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382

Imaging brain amyloid in Alzheimer's disease with Pittsburgh Compound‐B

Klunk, W. E., Engler, H., Nordberg, A., Wang, Y., Blomqvist, G., Holt, D. P., Bergström, M., Savitcheva, I., Huang, G., Estrada, S., et al. (2004) · Annals of Neurology · doi:10.1002/ana.20009 · Cited by 4,496

Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17

Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498

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

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

Cryo-EM structures of tau filaments from Alzheimer’s disease

Fitzpatrick, A. W. P., Falcon, B., He, S., Murzin, A. G., Murshudov, G., Garringer, H. J., Crowther, R. A., Ghetti, B., Goedert, M., & Scheres, S. H. W. (2017) · Nature · doi:10.1038/nature23002 · Cited by 2,061

Mutation in the tau gene in familial multiple system tauopathy with presenile dementia

Spillantini, M. G., Murrell, J. R., Goedert, M., Farlow, M. R., Klug, A., & Ghetti, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7737 · Cited by 1,474

Tau is a candidate gene for chromosome 17 frontotemporal dementia

Poorkaj, P., Bird, T. D., Wijsman, E., Nemens, E., Garruto, R. M., Anderson, L., Andreadis, A., Wiederholt, W. C., Raskind, M., & Schellenberg, G. D. (1998) · Annals of Neurology · doi:10.1002/ana.410430617 · Cited by 1,374

Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau

Goedert, M., Wischik, C. M., Crowther, R. A., Walker, J. E., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.4051 · Cited by 1,134

Tau proteins of alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms

Goedert, M., Spillantini, M. G., Cairns, N. J., & Crowther, R. A. (1992) · Neuron · doi:10.1016/0896-6273(92)90117-v · Cited by 1,122

Tau protein liquid–liquid phase separation can initiate tau aggregation

Wegmann, S., Eftekharzadeh, B., Tepper, K., Zoltowska, K. M., Bennett, R. E., Dujardin, S., Laskowski, P. R., MacKenzie, D., Kamath, T., Commins, C., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201798049 · Cited by 1,102

Genetic Correlates of Presenile Dementia and Cognitive Decline in the Armenian Population Following COVID-19: A Case-Control Study

Hovhannisyan, Y., Yeritsyan, H., Hakobjanyan, G., Petrosyan, G., Harutyunyan, H. A., Muradyan, A. A., Azizian, A., & Yenkoyan, K. B. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146965 · Cited by 4

Metformin, Microbiota and Health

Paz, G. S., & Fernandes, J. (2022) · Journal of Exploratory Research in Pharmacology · doi:10.14218/jerp.2022.00032 · Cited by 3

Advancing novel therapies for neurodegeneration through an innovative model for industry–academia collaborations: A decade of the Eisai–UCL experience

Atkinson, P. J., Swami, M., Ridgway, N., Roberts, M., Kinghorn, J., Warner, T. T., Staddon, J. M., & Takle, A. K. (2023) · Drug Discovery Today · doi:10.1016/j.drudis.2023.103732 · Cited by 3

A Review on the Correlation between the Pathology of Alzheimer's Disease and microRNA

Kim, S.-J., & Cho, H. (2021) · Journal of Experimental & Biomedical Sciences/Biomedical Science Letters · doi:10.15616/bsl.2021.27.4.208 · Cited by 2

Effects of All-Atom and Coarse-Grained Molecular Mechanics Force Fields on Amyloid Peptide Assembly: The Case of a Tau K18 Monomer

He, X., Man, V. H., Gao, J., & Wang, J. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c01448 · Cited by 2

PET Imaging of a Transgenic Tau Rat Model SHR24 with [18F]AV1451

Ramakrishnan, N. K., Zhao, A. Z., Thompson, S., Sephton, S. M., Williamson, D. J., Smolek, T., Žilka, N., & Aigbirhio, F. I. (2025) · Molecular Imaging and Biology · doi:10.1007/s11307-024-01972-4 · Cited by 2

Recently Progressed Postbiotics as Nutraceuticals

Jeong, G. (2021) · Food Supplements and Biomaterials for Health · doi:10.52361/fsbh.2021.1.e33 · Cited by 2

Structural exposure of different microtubule binding domains determines the propagation and toxicity of pathogenic tau conformers in Alzheimer’s disease

Hromádková, L., Kim, C., Haldiman, T., Siddiqi, M. K., Surewicz, K. A., Urquhart, K., Sadruddin, D.-E.-N., Peng, L., Zhu, X., Surewicz, W. K., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1012926 · Cited by 2

SKALE: An Interpretable Multiscale Machine Learning Model for Decoding Phase‐Specific Protein Aggregation in Neurodegenerative Proteinopathies

Loo, W. X. W., Sio, J. S., Yap, K., Loo, Y. S., Lim, H. X., Zhang, S., Liu, H., & Ng, C. S. (2026) · Aggregate · doi:10.1002/agt2.70280 · Cited by 1

Effect of Cosolutes on the Aggregation of a Tau Fragment: A Combined Experimental and Simulation Approach

Arsiccio, A., Liu, X., Ganguly, P., Buratto, S. K., Bowers, M. T., & Shea, J. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c00433 · Cited by 1

Effect of Scutellaria Baicalensis Georgi Stems and Leaves Flavonoids on Multisite Phosphorylation of tau Protein Induced by Composited Aβ in Rats

Liu, Q.-Q., Ding, S.-K., & Shang, Y. Z. (2020) · International Journal of Medicinal Plants and Natural Products · doi:10.20431/2454-7999.0604001 · Cited by 1

Phosphorylation of a Cleaved Tau Proteoform at a Single Residue Inhibits Binding to the E3 Ubiquitin Ligase, CHIPPreprint

Nadel, C. M., Wucherer, K., Oehler, A., Thwin, A. C., Basu, K., Callahan, M. D., Southworth, D. R., Mordes, D. A., Craik, C. S., & Gestwicki, J. E. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.16.553575 · Cited by 1

Tau proteolysis mechanisms and relevance for tauopathies

Quinn, J. P. (2019) · Research Explorer (The University of Manchester)

Perspective Chapter: Multiple Functions of Fukutin, the Gene Responsible for Fukuyama Congenital Muscular Dystrophy, Especially in the Central Nervous System

Yamamoto, T., Okamura, Y., Tsukui, R., Kato, Y., Onizuka, H., & Masui, K. (2022) · IntechOpen eBooks · doi:10.5772/intechopen.108063

Potential Therapeutic Strategies for Muscular Dystrophy

Gaina, G. (2022) · IntechOpen eBooks · doi:10.5772/intechopen.102255

Evidenced-based biological prevention and intervention strategies of dementia: a narrative review

Abukuri, D. N. (2023) · Current Psychology · doi:10.1007/s12144-023-05017-x

Analysis of genes associated with Alzheimer's disease and endoplasmic reticulum stressPreprint

Liu, Z., & Li, F. (2024) · Research Square · doi:10.21203/rs.3.rs-4334229/v1

Neurological Impact of Type I Interferon Dysregulation

Mylonas, A. (2024) · IntechOpen eBooks · doi:10.5772/intechopen.1006023

Inhibiting disulphide bonding in truncated tau297-391 results in enhanced self-assembly of tau into seed-competent assembliesPreprint

Oakley, S. S., Marshall, K. E., Meisl, G., Copsey, A. C., Maina, M. B., Milton, R., Vorley, T., Storey, J. M. D., Harrington, C. R., Wischik, C. M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.05.636249

Novel prostaglandin and isoprostane panel for evaluating Wilson’s Disease

Polat, M. Ç. A. Ü. L. T. İ. Ç. G., Durukan, B. M., İsrafilov, S., Çakmaklı, G. Y., İdilman, İ. S., Dağ, O., Karçaaltıncaba, M., Sökmensüer, C., Elibol, B., Balaban, Y. H., et al. (2025) · Turkish Journal of Biochemistry · doi:10.1515/tjb-2024-0330

Identification of common variants influencing risk of the three-repeat tauopathy Pick’s disease: a genome wide association studyPreprint

Scotton, W. J., Valentino, R. R., Martínez-Carrasco, A., Real, R., Macpherson, H. L., Tamvaka, N., Mok, K. Y., Heckman, M. G., Kobylecki, C., Escott‐Price, V., et al. (2025) · medRxiv · doi:10.64898/2025.12.21.25342758

Evaluating the Impact of Phosphorylation on the Dynamics of the Tau Protein Proline-Rich Region

Stöckelmaier, J., Polato, G., Hritz, J., & Oostenbrink, C. (2026) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5c02011

Inhomogeneous Tau polymerization, core–shell organization, and seed formation during Tau condensate agingPreprint

Franck, M., Biswas, A., Jiang, P., Fernández-Campo, M., Mohapatra, S., Sankar, R., Dominguez‐Baquero, A., Ravatt, L. M., Nagy-Herczeg, B. K., Kantar, O. E., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.18.711671

Développement d’une méthode de mesure et d’analyse du transport intraneuronal dans le cerveau de larve de poissons-zèbre par suivi de nanocristaux non-linéaires en microscopie de second-harmonique : application à l’étude d’anomalies de transport chez des poissons portant une mutation retrouvée dans des neuropathies humaines.

Terras, F. (2020) · doi:10.70675/872df6d1ze1b9z4a8dzb02dzad4656ff10f0

Early memory deficits and extensive brain network disorganization in the AppNL-F/MAPT double knock-in mouse model of familial Alzheimer's disease

Borcuk, C. (2021) · theses.fr (ABES) · doi:10.70675/c316f2dcz54d3z41cfzb3f5z99c7b2d3cd95 · Cited by 1

Rôle physiologique et pathologique de la kinésine Kif21b au cours de la migration neuronale

Alvarez, J. R. (2022) · theses.fr (ABES) · doi:10.70675/7fc29459z67a7z4bedzacbczf5ca6affb824

Novel therapeutic inhibitor targeting dysregulated kinase signaling in tau-mediated neurodegeneration

Sharma, S., & Singh, M. (2026) · BIO Web of Conferences · doi:10.1051/bioconf/202625201006

Neurodegeneration and the Ordered Assembly of Tau

Goedert, M. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811304-2.00004-3 · Cited by 3

Tau Protein and Neurodegeneratio

Goedert, M. (2025) · Alzheimer s & Dementia · doi:10.1002/alz70855_099770

Tau Protein and Neurodegeneration

Goedert, M. (2025) · Alzheimer s & Dementia · doi:10.1002/alz70855_098415 · Cited by 1

Tau and neurodegeneration

Goedert, M., Crowther, R. A., Scheres, S. H. W., & Spillantini, M. G. (2023) · Cytoskeleton · doi:10.1002/cm.21812 · Cited by 64

Ordered Assembly of Tau Protein and Neurodegeneration

Goedert, M., & Spillantini, M. G. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_1 · Cited by 74