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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 1,114 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · 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

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 830 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 624 · see citing works

[ 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 · see citing works

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 597 · see citing works

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 566 · see citing works

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 · see citing works

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 458 · see citing works

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 445 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 368 · see citing works

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 355 · see citing works

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 338 · see citing works

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 · see citing works

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 309 · see citing works

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 308 · see citing works

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 · see citing works

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 · see citing works

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 252 · see citing works

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 246 · see citing works

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

Couchie, D., Mavilia, C., Georgieff, I. S., Liem, R. K. H., Shelanski, M. L., & Nunez, J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.10.4378 · Cited by 241 · see citing works

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 · see citing works

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 202 · see citing works

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 168 · see citing works

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 157 · see citing works

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 · see citing works

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 · see citing works

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 117 · see citing works

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 · see citing works

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 · see citing works

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

Gauthier‐Kemper, A., Alonso, M. S., Sündermann, F., Niewidok, B., Fernández, M. P., Bakota, L., Heinisch, J. J., & Brandt, R. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000490 · Cited by 84 · see citing works

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

Bondareff, W., Wischik, C. M., Novák, M., & Roth, M. (1991) · PubMed Central · Cited by 64 · see citing works

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

Niewidok, B., Igaev, M., Sündermann, F., Janning, D., Bakota, L., & Brandt, R. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-06-0402 · Cited by 60 · see citing works

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 · see citing works

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 53 · see citing works

Analysis of tau haplotypes in Pick’s disease

Morris, H. R., Baker, M., Yasojima, K., Houlden, H., Khan, M. N., Wood, N. W., Hardy, J., Grossman, M., Trojanowski, J. Q., Révész, T., et al. (2002) · Neurology · doi:10.1212/wnl.59.3.443 · Cited by 49 · see citing works

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

Tuerde, D., Kimura, T., Miyasaka, T., Furusawa, K., Shimozawa, A., Hasegawa, M., Ando, K., & Hisanaga, S. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.798918 · Cited by 47 · see citing works

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Solano (2000) · doi:10.1002/1531-8249(200002)47:2 · Cited by 3 · see citing works

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(1997) · doi:10.1002/(sici)1097-4547(19970415)48:2

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

Mattsson-Carlgren, N., Andersson, E., Janelidze, S., Ossenkoppele, R., Insel, P., Strandberg, O., Zetterberg, H., Rosen, H. J., Rabinovici, G., Chai, X., et al. (2020) · Science Advances · doi:10.1126/sciadv.aaz2387 · Cited by 359 · see citing works

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

Leuzy, A., Smith, R., Ossenkoppele, R., Santillo, A., Borroni, E., Klein, G., Ohlsson, T., Jögi, J., Palmqvist, S., Mattsson-Carlgren, N., et al. (2020) · JAMA Neurology · doi:10.1001/jamaneurol.2020.0989 · Cited by 222 · see citing works

Enzymatic Noncovalent Synthesis

He, H., Tan, W., Guo, J., Yi, M., Shy, A. N., & Xu, B. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00306 · Cited by 224 · see citing works

Autophagic and endo-lysosomal dysfunction in neurodegenerative disease

Malik, B. R., Maddison, D. C., Smith, G. A., & Peters, O. M. (2019) · Molecular Brain · doi:10.1186/s13041-019-0504-x · Cited by 180 · see citing works

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 146 · see citing works

Tau Isoforms: Gaining Insight into MAPT Alternative Splicing

Corsi, A., Bombieri, C., Valenti, M. T., & Romanelli, M. G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315383 · Cited by 118 · see citing works

Astroglia and Tau: New Perspectives

Kovacs, G. G. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00096 · Cited by 115 · see citing works

Oligomerization and Conformational Change Turn Monomeric β-Amyloid and Tau Proteins Toxic: Their Role in Alzheimer’s Pathogenesis

Penke, B., Szűcs, M., & Bogár, F. (2020) · Molecules · doi:10.3390/molecules25071659 · Cited by 115 · see citing works

Progressive supranuclear palsy: Advances in diagnosis and management

Coughlin, D. G., & Litvan, I. (2020) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2020.04.014 · Cited by 113 · see citing works

A novel tau‐based rhesus monkey model of Alzheimer's pathogenesis

Beckman, D., Chakrabarty, P., Ott, S. P., Dao, A., Zhou, E., Janssen, W. G. M., Donis‐Cox, K., Muller, S., Kordower, J. H., & Morrison, J. H. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12318 · Cited by 112 · see citing works

Insights into Disease-Associated Tau Impact on Mitochondria

Szabo, L., Eckert, A., & Grimm, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176344 · Cited by 102 · see citing works

PICALM and Alzheimer’s Disease: An Update and Perspectives

Ando, K., Nagaraj, S., Küçükali, F., de Fisenne, M.-A., Kosa, A.-C., Doeraene, E., Lopez Gutierrez, L., Brion, J.-P., & Leroy, K. (2022) · Cells · doi:10.3390/cells11243994 · Cited by 104 · see citing works

Specific post-translational modifications of soluble tau protein distinguishes Alzheimer’s disease and primary tauopathies

Zola, N. K. N., Balty, C., Ruys, S. P. D., Vanparys, A., Huyghe, N. D., Herinckx, G., Johanns, M., Boyer, E., Kienlen‐Campard, P., Rider, M. H., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39328-1 · Cited by 93 · see citing works

Cytosolic antibody receptor TRIM21 is required for effective tau immunotherapy in mouse models

Mukadam, A. S., Miller, L. V. C., Smith, A. E., Vaysburd, M., Sakya, S. A., Sanford, S., Keeling, S., Tuck, B. J., Katsinelos, T., Green, C., et al. (2023) · Science · doi:10.1126/science.abn1366 · Cited by 83 · see citing works

A multicenter comparison of [18F]flortaucipir, [18F]RO948, and [18F]MK6240 tau PET tracers to detect a common target ROI for differential diagnosis

Leuzy, A., Pascoal, T. A., Strandberg, O. T., Insel, P. S., Smith, R. A., Mattsson, N., Benedet, A. L., Cho, H., Lyoo, C. H., Joie, R. L., et al. (2021) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-021-05401-4 · Cited by 86 · see citing works

Tau and MAPT genetics in tauopathies and synucleinopathies

Léveillé, E., Ross, O. A., & Gan‐Or, Z. (2021) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2021.09.008 · Cited by 83 · see citing works

Lowering Synaptogyrin-3 expression rescues Tau-induced memory defects and synaptic loss in the presence of microglial activation

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Tau Protein Dysfunction after Brain Ischemia

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Insight into the Binding of First- and Second-Generation PET Tracers to 4R and 3R/4R Tau Protofibrils

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Systemic Immune Dyshomeostasis Model and Pathways in Alzheimer’s Disease

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CSF Diagnostics: A Potentially Valuable Tool in Neurodegenerative and Inflammatory Disorders Involving Motor Neurons: A Review

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Cathepsin D: A Candidate Link between Amyloid ?-protein and Tauopathy in Alzheimer Disease

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High-Dose Photodynamic Therapy Increases Tau Protein Signals in Drosophila

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Site-Specific C-Terminal Fluorescent Labeling of Tau Protein

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Mechanisms of Strain Diversity of Disease-Associated in-Register Parallel β-Sheet Amyloids and Implications About Prion Strains

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Lithium ions display weak interaction with amyloid-beta (Aβ) peptides and have minor effects on their aggregation

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Synaptic Plasticity in the Hippocampus

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Tau Protein and Neurodegeneratio

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Tau Protein and Neurodegeneration

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Ordered Assembly of Tau Protein and Neurodegeneration

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