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

Identification of two distinct synucleins from human brain

Jakes, R., Spillantini, M. G., & Goedert, M. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00395-5 · Cited by 1,080

Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans

Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., & Crowther, R. A. (1996) · Nature · doi:10.1038/383550a0 · Cited by 1,036

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

von Bergen, M., Friedhoff, P., Biernat, J., Heberle, J., Mandelkow, E.-M., & Mandelkow, E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.10.5129 · Cited by 1,021

Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy

Min, S.-W., Cho, S.-H., Zhou, Y., Schroeder, S., Haroutunian, V., Seeley, W. W., Huang, E. J., Shen, Y., Masliah, E., Mukherjee, C., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.044 · Cited by 949

Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.

Wischik, C. M., Novak, M., Thøgersen, H. C., Edwards, P. C., Runswick, M. J., Jakes, R., Walker, J. E., Milstein, C., Roth, M., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.12.4506 · Cited by 939

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

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

Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly

Cleveland, D. W., Hwo, S. Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90214-5 · Cited by 881

A common inversion under selection in Europeans

Stefánsson, H., Helgason, A., Þorleifsson, G., Steinthórsdóttir, V., Másson, G., Barnard, J., Baker, A., Jónasdóttir, Á., Ingason, A., Gudnadottir, V. G., et al. (2005) · Nature Genetics · doi:10.1038/ng1508 · Cited by 847

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

Tau and neurodegenerative disease: the story so far

Iqbal, K., Liu, F., & Gong, C.-X. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.225 · Cited by 806

Association of an Extended Haplotype in the Tau Gene with Progressive Supranuclear Palsy

Baker, M., Litvan, I., Houlden, H., Adamson, J., Dickson, D., Perez-Tur, J., Hardy, J., Lynch, T., Bigio, E., & Hutton, M. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.4.711 · Cited by 781

The acetylation of tau inhibits its function and promotes pathological tau aggregation

Cohen, T. J., Guo, J. L., Hurtado, D. E., Kwong, L. K., Mills, I. P., Trojanowski, J. Q., & Lee, V. M. Y. (2011) · Nature Communications · doi:10.1038/ncomms1255 · Cited by 724

Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain.

Brandt, R., Léger, J. G., & Lee, G. S. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.131.5.1327 · Cited by 663

Discovery of previously unidentified genomic disorders from the duplication architecture of the human genome

Sharp, A. J., Hansen, S., Selzer, R. R., Cheng, Z., Regan, R., Hurst, J. A., Stewart, H., Price, S. M., Blair, E., Hennekam, R. C., et al. (2006) · Nature Genetics · doi:10.1038/ng1862 · Cited by 658

Domains of tau Protein and Interactions with Microtubules

Gustke, N., Trinczek, B., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (1994) · Biochemistry · doi:10.1021/bi00198a017 · Cited by 655

Propagation of Tau aggregates and neurodegeneration

Goedert, M., Eisenberg, D. S., & Crowther, R. A. (2017) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-072116-031153 · Cited by 632

Structural characterization of the core of the paired helical filament of Alzheimer disease.

Wischik, C. M., Novák, M., Edwards, P. C., Klug, A., Tichelaar, W., & Crowther, R. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.13.4884 · Cited by 609

[ 18 F]T807, a novel tau positron emission tomography imaging agent for Alzheimer's disease

Xia, C., Arteaga, J., Chen, G., Gangadharmath, U., Gomez, L. F., Kasi, D., Lam, C., Liang, Q., Liu, C., Mocharla, V. P., et al. (2013) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2012.11.008 · Cited by 605

The Synucleinopathies: Twenty Years On

Goedert, M., Jakes, R., & Spillantini, M. G. (2017) · Journal of Parkinson s Disease · doi:10.3233/jpd-179005 · Cited by 590

Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice

Morris, M., Knudsen, G. M., Maeda, S., Trinidad, J. C., Ioanoviciu, A., Burlingame, A. L., & Mucke, L. (2015) · Nature Neuroscience · doi:10.1038/nn.4067 · Cited by 472

Tau interacts with src-family non-receptor tyrosine kinases

Lee, G. S., Newman, S. T., Gard, D. L., Band, H., & Panchamoorthy, G. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.21.3167 · Cited by 471

A new chromosome 17q21.31 microdeletion syndrome associated with a common inversion polymorphism

Koolen, D. A., Vissers, L. E. L. M., Pfundt, R., de Leeuw, N., Knight, S. J. L., Regan, R., Kooy, R. F., Reyniers, E., Romano, C., Fichera, M., et al. (2006) · Nature Genetics · doi:10.1038/ng1853 · Cited by 465

Global Hairpin Folding of Tau in Solution

Jeganathan, S., von Bergen, M., Brutlach, H., Steinhoff, H.-J., & Mandelkow, E. (2006) · Biochemistry · doi:10.1021/bi0521543 · Cited by 432

Regional profiles of the candidate tau PET ligand 18 F-AV-1451 recapitulate key features of Braak histopathological stages

Schwarz, A. J., Yu, P., Miller, B. B., Shcherbinin, S., Dickson, J., Navitsky, M., Joshi, A. D., Devous, M. D., & Mintun, M. S. (2016) · Brain · doi:10.1093/brain/aww023 · Cited by 425

Polymerization of τ into Filaments in the Presence of Heparin: The Minimal Sequence Required for τ ‐ τ Interaction

Pérez, M., Valpuesta, J., Medina, M., de Garcini, E. M., & Ávila, J. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67031183.x · Cited by 424

Near-atomic model of microtubule-tau interactions

Kellogg, E. H., Hejab, N. M. A., Poepsel, S., Downing, K. H., DiMaio, F., & Nogales, E. (2018) · Science · doi:10.1126/science.aat1780 · Cited by 416

Corticobasal degeneration and progressive supranuclear palsy share a common tau haplotype

Houlden, H., Baker, M., Morris, H. R., MacDonald, N., Pickering–Brown, S., Adamson, J., Lees, A. J., Rossor, M. N., Quinn, N. P., Kertesz, A., et al. (2001) · Neurology · doi:10.1212/wnl.56.12.1702 · Cited by 409

Genetic evidence for the involvement of τ in progressive supranuclear palsy

Conrad, C., Andreadis, A., Trojanowski, J. Q., Dickson, D. W., Kang, D. E., Chen, X., Wiederholt, W. C., Hansen, L., Masliah, E., Thal, L. J., et al. (1997) · Annals of Neurology · doi:10.1002/ana.410410222 · Cited by 388

Microdeletion encompassing MAPT at chromosome 17q21.3 is associated with developmental delay and learning disability

Shaw-Smith, C. J., Pittman, A. M., Willatt, L. R., Martin, H., Rickman, L., Gribble, S. M., Curley, R., Cumming, S., Dunn, C. A., Kalaitzopoulos, D. R., et al. (2006) · Nature Genetics · doi:10.1038/ng1858 · Cited by 377

Structure-based inhibitors of tau aggregation

Seidler, P. M., Boyer, D. R., Rodríguez, J. A., Sawaya, M. R., Cascio, D., Murray, K. A., Gonen, T., & Eisenberg, D. S. (2017) · Nature Chemistry · doi:10.1038/nchem.2889 · Cited by 346

MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments

Al-Bassam, J., Ozer, R. S., Safer, D., Halpain, S., & Milligan, R. A. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200201048 · Cited by 327

Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance

Cook, C. N., Carlomagno, Y., Gendron, T. F., Dunmore, J. H., Scheffel, K., Stetler, C. T., Davis, M., Dickson, D. W., Jarpe, M. B., Deture, M. A., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt402 · Cited by 325

RNA stores tau reversibly in complex coacervates

Zhang, X., Lin, Y., Eschmann, N. A., Zhou, H., Rauch, J. N., Hernández, I., Guzman, E., Kosik, K. S., & Han, S. (2017) · PLoS Biology · doi:10.1371/journal.pbio.2002183 · Cited by 312

Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-β structure

Berriman, J. A., Serpell, L. C., Oberg, K. A., Fink, A. L., Goedert, M., & Crowther, R. A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1530287100 · Cited by 288

Conformation Determines the Seeding Potencies of Native and Recombinant Tau Aggregates

Falcon, B., Cavallini, A., Angers, R. C., Glover, S. J., Murray, T. K., Barnham, L., Jackson, S., O'Neill, M. J., Isaacs, A. M., Hutton, M. L., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.589309 · Cited by 265

Identification of the Tau phosphorylation pattern that drives its aggregation

Despres, C., Byrne, C., Qi, H., Cantrelle, F., Huvent, I., Chambraud, B., Baulieu, É.-É., Jacquot, Y., Landrieu, I., Lippens, G. M., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708448114 · Cited by 263

Cloning of a big tau microtubule-associated protein characteristic of the peripheral nervous system.

Goedert, M., Spillantini, M. G., & Crowther, R. A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.5.1983 · Cited by 255

Primary structure of high molecular weight tau present in the peripheral nervous system.

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Mutations in the chromatin modifier gene KANSL1 cause the 17q21.31 microdeletion syndrome

Koolen, D. A., Kramer, J. M., Neveling, K., Nillesen, W. M., Moore-Barton, H. L., Elmslie, F. V., Toutain, A., Amiel, J., Malan, V., Tsai, A. C.-H., et al. (2012) · Nature Genetics · doi:10.1038/ng.2262 · Cited by 232

Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies

Ono, M., Sahara, N., Kumata, K., Ji, B., Ni, R., Koga, S., Dickson, D. W., Trojanowski, J. Q., Lee, V. M. ‐., Yoshida, M., et al. (2016) · Brain · doi:10.1093/brain/aww339 · Cited by 206

Single-molecule tracking of tau reveals fast kiss-and-hop interaction with microtubules in living neurons

Janning, D., Igaev, M., Sündermann, F., Brühmann, J., Beutel, O., Heinisch, J. J., Bakota, L., Piehler, J., Junge, W., & Brandt, R. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-06-1099 · Cited by 181

Mutations in KANSL1 cause the 17q21.31 microdeletion syndrome phenotype

Zollino, M., Orteschi, D., Murdolo, M., Lattante, S., Battaglia, D., Stefanini, C., Mercuri, E. M., Chiurazzi, P., Neri, G., & Marangi, G. (2012) · Nature Genetics · doi:10.1038/ng.2257 · Cited by 158

An acetylation–phosphorylation switch that regulates tau aggregation propensity and function

Carlomagno, Y., Chung, D.-E. C., Yue, M., Castanedes-Casey, M., Madden, B. J., Dunmore, J., Tong, J., DeTure, M., Dickson, D. W., Petrucelli, L., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.794602 · Cited by 143

Tau isoform composition influences rate and extent of filament formation

Zhong, Q., Congdon, E. E., Nagaraja, H. N., & Kuret, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.364067 · Cited by 122

Protein Semisynthesis Provides Access to Tau Disease-Associated Post-translational Modifications (PTMs) and Paves the Way to Deciphering the Tau PTM Code in Health and Diseased States

Haj‐Yahya, M., & Lashuel, H. A. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b02668 · Cited by 118

Heparin-induced tau filaments are structurally heterogeneous and differ from Alzheimer's disease filaments

Fichou, Y., Vigers, M., Goring, A. K., Eschmann, N. A., & Han, S. (2018) · Chemical Communications · doi:10.1039/c8cc01355a · Cited by 89

Haplotype-specific expression of the N-terminal exons 2 and 3 at the human MAPT locus

Caffrey, T. M., Joachim, C., & Wade-Martins, R. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.05.002 · Cited by 88

Annexins A2 and A6 interact with the extreme N terminus of tau and thereby contribute to tau's axonal localization

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Sequestration of tau by granulovacuolar degeneration in Alzheimer's disease.

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Presence of a carboxy-terminal pseudorepeat and disease-like pseudohyperphosphorylation critically influence tau’s interaction with microtubules in axon-like processes

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An N-terminal motif unique to primate tau enables differential protein–protein interactions

Stefanoska, K., Volkerling, A. M., Bertz, J., Poljak, A., Ke, Y. D., Ittner, L. M., & Ittner, A. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001784 · Cited by 60

Meta-analysis of the association between variants in MAPT and neurodegenerative diseases

Zhang, C., Zhu, J., Wan, Y., Tan, L., Wang, H.-F., Yu, J., & Tan, L. (2017) · Oncotarget · doi:10.18632/oncotarget.16690 · Cited by 57

Analysis of tau haplotypes in Pick’s disease

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Isoform-independent and -dependent phosphorylation of microtubule-associated protein tau in mouse brain during postnatal development

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Aβ deposition is associated with increases in soluble and phosphorylated tau that precede a positive tau PET in Alzheimer's disease

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Diagnostic Performance of RO948 F 18 Tau Positron Emission Tomography in the Differentiation of Alzheimer Disease From Other Neurodegenerative Disorders

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Enzymatic Noncovalent Synthesis

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Autophagic and endo-lysosomal dysfunction in neurodegenerative disease

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Roles and Mechanisms of Gut Microbiota in Patients With Alzheimer’s Disease

Wu, S., Liu, X., Jiang, R., Yan, X., & Ling, Z. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.650047 · Cited by 150

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

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