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Cryo-EM structures of tau filaments from Alzheimer’s disease
Open accessAbstract
Alzheimer's disease is the most common neurodegenerative disease, and there are no mechanism-based therapies. The disease is defined by the presence of abundant neurofibrillary lesions and neuritic plaques in the cerebral cortex. Neurofibrillary lesions comprise paired helical and straight tau filaments, whereas tau filaments with different morphologies characterize other neurodegenerative diseases. No high-resolution structures of tau filaments are available. Here we present cryo-electron microscopy (cryo-EM) maps at 3.4-3.5 Å resolution and corresponding atomic models of paired helical and straight filaments from the brain of an individual with Alzheimer's disease. Filament cores are made of two identical protofilaments comprising residues 306-378 of tau protein, which adopt a combined cross-β/β-helix structure and define the seed for tau aggregation. Paired helical and straight filaments differ in their inter-protofilament packing, showing that they are ultrastructural polymorphs. These findings demonstrate that cryo-EM allows atomic characterization of amyloid filaments from patient-derived material, and pave the way for investigation of a range of neurodegenerative diseases.
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“ultra-structural analyses of tau filaments in brains from individuals with AD have shown that tau tangles contain both 3-repeat (3R)-tau and 4-repeat (4R)-tau isoforms (18)”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [18]
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“In AD, tau tangles contain a mixture of 3R- and 4R-tau isoforms to adopt an AD-characteristic topology (18, 19).”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [18]
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“In AD, tau filaments assume a cross-β/β-helical fold (10).”
From MAP2 caps tau fibrils and inhibits aggregation (2023) · cites this paper as [10]
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“Misfolding and aberrant accumulation of Tau is a pathological hallmark of Alzheimer’s disease (AD)18, 19.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [19]
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Citations
Cites
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796
Self-citationMolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Zheng, S. Q., Palovcak, E. J., Armache, J., Verba, K. A., Cheng, Y., & Agard, D. A. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,496
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,497
Gctf: Real-time CTF determination and correction
Zhang, K. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.11.003 · Cited by 3,417
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
Self-citationAtomic structures of amyloid cross-β spines reveal varied steric zippers
Sawaya, M. R., Sambashivan, S., Nelson, R. A., Ivanova, M. I., Sievers, S. A., Apostol, M. I., Thompson, M. J., Balbirnie, M., Wiltzius, J. J. W., McFarlane, H. T., et al. (2007) · Nature · doi:10.1038/nature05695 · Cited by 2,279
Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen
Sunde, M., Serpell, L. C., Bartlam, M. G., Fraser, P. E., Pepys, M. B., & Blake, C. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1348 · Cited by 1,735
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
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Flagged first, then by citations
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Items 401–500 of 1,003
Quantification of Tau Protein Lysine Methylation in Aging and Alzheimer’s Disease
Huseby, C. J., Hoffman, C. N., Cooper, G. L., Cocuron, J.-C., Alonso, A. P., Thomas, S. N., Yang, A. J., & Kuret, J. (2019) · Journal of Alzheimer’s Disease · doi:10.3233/jad-190604 · Cited by 54
Williams, T., Sorrentino, Z. A., Weinrich, M. J., Giasson, B. I., & Chakrabarty, P. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa090 · Cited by 56
“Several groups have hypothesized that such cross-seeded fibrils may form different conformational strains with unique properties that correspond with phenotypic diversity and clinical severity in Alzheimer’s disease and related dementias (Sanders et al., 2014; Fitzpatrick et al., 2017; Falcon et al., 2018).”
BackgroundAubrey, L. D., Blakeman, B. J. F., Lutter, L., Serpell, C. J., Tuite, M. F., Serpell, L. C., & Xue, W. (2020) · Communications Chemistry · doi:10.1038/s42004-020-00372-3 · Cited by 60
Malafaia, D., Albuquerque, H. M. T., & Silva, A. M. S. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113209 · Cited by 57
Xiao, S., Lu, Y.-F., Wu, Q., Yang, J., Chen, J., Zhong, S., Eliezer, D., Tan, Q., & Wu, C. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.02.210 · Cited by 56
Advances in Deep Neuropathological Phenotyping of Alzheimer Disease: Past, Present, and Future
Shakir, M., & Dugger, B. N. (2022) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlab122 · Cited by 58
van der Kant, R., Louros, N. N., Schymkowitz, J. W. H., & Rousseau, F. (2022) · Structure · doi:10.1016/j.str.2022.05.002 · Cited by 55
Protein–protein interactions regulating α-synuclein pathology
Wang, J., Dai, L., Chen, S., Zhang, Z., Fang, X., & Zhang, Z. (2024) · Trends in Neurosciences · doi:10.1016/j.tins.2024.01.002 · Cited by 58
Calpain-mediated tau fragmentation is altered in Alzheimer’s disease progression
Chen, H.-H., Liu, P., Auger, P., Lee, S.-H., Adolfsson, O., Rey-Bellet, L., Lafrance-Vanasse, J., Friedman, B. A., Pihlgren, M., Muhs, A., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-35130-y · Cited by 51
Losev, Y., Frenkel-Pinter, M., Abu-Hussien, M., Viswanathan, G. K., Elyashiv-Revivo, D., Geries, R., Khalaila, I., Gazit, E., & Segal, D. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03643-3 · Cited by 52
Integrative Structural Biology in the Era of Accurate Structure Prediction
Masrati, G., Landau, M., Ben-Tal, N., Lupas, A., Kosloff, M., & Kosinski, J. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167127 · Cited by 53
Liu, M., Dexheimer, T. S., Sui, D., Hovde, S., Deng, X., Kwok, R. P. S., Bochar, D. A., & Kuo, M. (2020) · Scientific Reports · doi:10.1038/s41598-020-73680-2 · Cited by 59
Zhang, M., & Bian, Z. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.687973 · Cited by 60
“A large number of specific miRNAs are reduced during AD development, which may be involved in the pathogenesis of AD by affecting the abnormal aggregation of tau protein (Fitzpatrick et al., 2017; Nisbet and Götz, 2018).”
BackgroundProtein amyloid aggregate: Structure and function
Xu, Q., Ma, Y., Sun, Y., Li, D., Zhang, X., & Liu, C. (2023) · Aggregate · doi:10.1002/agt2.333 · Cited by 57
Elucidating Tau function and dysfunction in the era of cryo-EM
Lippens, G. M., & Gigant, B. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.008031 · Cited by 56
“This same peptide motif is at the very beginning of the ordered structure of the brain-isolated AD fibrils (12).”
BackgroundInfluentialRelease of a disordered domain enhances HspB1 chaperone activity toward tau
Baughman, H. E. R., Pham, T.-H. T., Adams, C. S., Nath, A., & Klevit, R. E. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1915099117 · Cited by 55
Distinct Conformers of Assembled Tau in Alzheimer's and Pick's DiseasesPreprint
Goedert, M., Falcon, B., Zhang, W., Ghetti, B. F., & Scheres, S. H. W. (2018) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2018.83.037580 · Cited by 59
Self-citationOxidative Stress in Tauopathies: From Cause to Therapy
Bartolomé, F. B., Carro, E., & Alquézar, C. (2022) · Antioxidants · doi:10.3390/antiox11081421 · Cited by 59
Promoting Alzheimer’s disease research and therapy with stem cell technology
Cao, Z., Kong, F., Ding, J., Chen, C., He, F., & Deng, W. (2024) · Stem Cell Research & Therapy · doi:10.1186/s13287-024-03737-w · Cited by 60
The future of integrated structural biology
Schwalbe, H., Audergon, P. N. C. B., Haley, N., Amaro, C. A., Agirre, J., Baldus, M., Banci, L., Baumeister, W. P., Blackledge, M. J., Carazo, J. M., et al. (2024) · Structure · doi:10.1016/j.str.2024.08.014 · Cited by 57
Nam, Y., Shin, S. J., Kumar, V., Won, J., Kim, S., & Moon, M. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00479-4 · Cited by 62
Structural insight into microtubule stabilization and kinesin inhibition by Tau family MAPs
Shigematsu, H., Imasaki, T., Doki, C., Sumi, T., Aoki, M., Uchikubo-Kamo, T., Sakamoto, A., Tokuraku, K., Shirouzu, M., & Nitta, R. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201711182 · Cited by 54
“Tau is known to form filamentous aggregates called neurofibrillary tangles whose structure were recently reported by high-resolution cryo-EM study without microtubules (Fitzpatrick et al., 2017).”
BackgroundModulating disease-relevant tau oligomeric strains by small molecules
Cascio, F. L., García, S., Montalbano, M., Puangmalai, N., McAllen, S., Pace, A., Piccionello, A. P., & Kayed, R. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014630 · Cited by 53
Panda, C., Voelz, C., Habib, P., Mevissen, C., Pufe, T., Beyer, C., Gupta, S. K., & Slowik, A. (2021) · Cells · doi:10.3390/cells10071652 · Cited by 54
Alzheimer’s Disease: An Overview of Major Hypotheses and Therapeutic Options in Nanotechnology
Agarwal, M., Alam, R., Haider, M. K., Malik, M. Z., & Kim, D.-K. (2020) · Nanomaterials · doi:10.3390/nano11010059 · Cited by 59
“Over the years, the emergence of different events of the neurodegenerative triad may occur at different points of time with the progression of AD [57].”
BackgroundDnaJC7 binds natively folded structural elements in tau to inhibit amyloid formation
Hou, Z., Wydorski, P. M., Perez, V. A., Mendoza‐Oliva, A., Ryder, B. D., Mirbaha, H., Kashmer, O. M., & Joachimiak, Ł. A. (2021) · Nature Communications · doi:10.1038/s41467-021-25635-y · Cited by 53
Nisbet, R. M., & Götz, J. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-179907 · Cited by 57
Untangling the Tauopathy for Alzheimer’s disease and parkinsonism
Chang, H.-Y., Sang, T., & Chiang, A. (2018) · Journal of Biomedical Science · doi:10.1186/s12929-018-0457-x · Cited by 56
McKibben, K. M., & Rhoades, E. R. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010172 · Cited by 55
DeepTracer-ID: De novo protein identification from cryo-EM maps
Chang, L., Wang, F., Connolly, K., Meng, H., Su, Z., Cvirkaite-Krupovic, V., Krupovic, M., Egelman, E. H., & Si, D. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.06.025 · Cited by 50
Recent Advances in Understanding Mammalian Prion Structure: A Mini Review
Terry, C., & Wadsworth, J. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00169 · Cited by 31
Weisová, P., Cehlár, O., Škrabana, R., Žilková, M., Filipčík, P., Kováčech, B., Prčina, M., Wojčiaková, Ľ., Fialová, Ľ., Smolek, T., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0770-y · Cited by 53
On the Structural Diversity and Individuality of Polymorphic Amyloid Protein Assemblies
Lutter, L., Aubrey, L. D., & Xue, W. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167124 · Cited by 53
Maniv, I., Sarji, M., Bdarneh, A., Feldman, A., Ankawa, R., Koren, E., Magid-Gold, I., Reis, N., Soteriou, D., Salomon‐Zimri, S., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41545-7 · Cited by 54
HIV and Alzheimer’s disease: complex interactions of HIV-Tat with amyloid β peptide and Tau protein
Hategan, A. P., Masliah, E., & Nath, A. (2019) · Journal of NeuroVirology · doi:10.1007/s13365-019-00736-z · Cited by 52
Structural dissection of amyloid aggregates of TDP‐43 and its C‐terminal fragments TDP‐35 and TDP‐16
Shenoy, J., Mammeri, N. E., Dutour, A., Berbon, M., Saad, A., Lends, A., Morvan, E., Grélard, A., Lecomte, S., Kauffmann, B., et al. (2019) · FEBS Journal · doi:10.1111/febs.15159 · Cited by 52
Structural Diversity of Amyloid Fibrils and Advances in Their Structure Determination
Li, D., & Liu, C. (2020) · Biochemistry · doi:10.1021/acs.biochem.9b01069 · Cited by 52
Ferrie, J. J., Lengyel‐Zhand, Z., Janssen, B., Lougee, M. G., Giannakoulias, S. G., Hsieh, C., Pagar, V. V., Weng, C.-C., Xu, H. W., Graham, T. J. A., et al. (2020) · Chemical Science · doi:10.1039/d0sc02159h · Cited by 53
Dregni, A. J., Wang, H. K., Wu, H., Duan, P., Jin, J., DeGrado, W. F., & Hong, M. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c03314 · Cited by 50
He, H., Liu, Y., Sun, Y., & Ding, F. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00217 · Cited by 51
Carlson, G. A., & Prusiner, S. B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094861 · Cited by 51
Hernández, F., Ferrer, I., Pérez, M., Zabala, J. C., del Rı́o, J. A., & Ávila, J. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.04.024 · Cited by 49
Familial Parkinson’s point mutation abolishes multiple system atrophy prion replication
Woerman, A. L., Kazmi, S. A., Patel, S. S., Aoyagi, A., Oehler, A., Widjaja, K., Mordes, D. A., Olson, S. H., & Prusiner, S. B. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1719369115 · Cited by 51
Highly specific and selective anti‐pS396‐tau antibody C10.2 targets seeding‐competent tau
Rosenqvist, N., Asuni, A. A., Andersson, C. R., Christensen, S., Daechsel, J. C. A., Egebjerg, J., Falsig, J., Helboe, L., Jul, P., Kartberg, F., et al. (2018) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.09.005 · Cited by 52
Bourré, G., Cantrelle, F., Kamah, A., Chambraud, B., Landrieu, I., & Smet‐Nocca, C. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00595 · Cited by 57
“In AD, tau is hyperphosphorylated (it contains 9–10 moles of phosphate per mol of tau while normal tau contains 2– 3 moles of phosphate) (19, 20), undergoes conformational changes (21) and is converted into toxic oligomers and fibrillar aggregates, the straight (SFs) and paired helical filaments (PHFs) (22, 23).”
BackgroundBinding and Reactivity of Copper to R1 and R3 Fragments of tau Protein
Bacchella, C., Gentili, S., Bellotti, D., Quartieri, E., Draghi, S., Baratto, M. C., Remelli, M., Valensin, D., Monzani, E., Nicolis, S., et al. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b02266 · Cited by 51
Protofilament Structure and Supramolecular Polymorphism of Aggregated Mutant Huntingtin Exon 1
Boatz, J. C., Piretra, T., Lasorsa, A., Matlahov, I., Conway, J. F., & van der Wel, P. C. A. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.06.021 · Cited by 51
Emerging Roles of Functional Bacterial Amyloids in Gene Regulation, Toxicity, and Immunomodulation
Salinas, N., Povolotsky, T. L., Landau, M., & Kolodkin‐Gal, I. (2020) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00062-20 · Cited by 52
Vacchi, E., Kaelin‐Lang, A., & Melli, G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21145030 · Cited by 51
How do protein aggregates escape quality control in neurodegeneration?
Koopman, M. B., Ferrari, L., & Rüdiger, S. (2022) · Trends in Neurosciences · doi:10.1016/j.tins.2022.01.006 · Cited by 54
McDade, E. (2022) · CONTINUUM Lifelong Learning in Neurology · doi:10.1212/con.0000000000001131 · Cited by 56
Cryo-EM structures of amyloid-β and tau filaments in Down syndrome
Fernández, A., Hoq, M. R., Hallinan, G. I., Li, D., Bharath, S. R., Vago, F. S., Zhang, X., Ozcan, K. A., Newell, K. L., Garringer, H. J., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01252-3 · Cited by 50
“…that there is no variation in the structure of tau filaments between individuals with DS and sAD (and FAD), and tau in other brain amyloidosis 34–36 , further supporting the notion of a common mechanism through which different amyloids trigger aggregation of tau, resulting in tau filaments…”
Self-citationEnergetics Underlying Twist Polymorphisms in Amyloid Fibrils
Périole, X., Huber, T., Bonito-Oliva, A., Åberg, K. C., van der Wel, P. C. A., Sakmar, T. P., & Marrink, . J. (2017) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.7b10233 · Cited by 50
Ceska, T., Chung, C., Cooke, R., Phillips, C., & Williams, P. A. (2019) · Biochemical Society Transactions · doi:10.1042/bst20180267 · Cited by 50
Matlahov, I., & van der Wel, P. C. A. (2019) · Experimental Biology and Medicine · doi:10.1177/1535370219856620 · Cited by 45
Klingstedt, T., Ghetti, B. F., Holton, J. L., Ling, H., Nilsson, K. P. R., & Goedert, M. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0840-1 · Cited by 50
Self-citationWatanabe‐Nakayama, T., Sahoo, B. R., Ramamoorthy, A., & Ono, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124287 · Cited by 49
“Tau protein amyloid fibrils demonstrated different isoforms and structures between AD [3], Pick’s disease [4], progressive supranuclear palsy (PSP) [5], corticobasal degeneration (CBD) [5], and chronic traumatic encephalopathy (CTE) in tauopathy [6].”
BackgroundGao, Y., Zhong, T., Wang, L., Zhang, N., Zeng, Y., Hu, J.-Y., Dang, H.-B., Chen, J., & Liang, Y. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.04.034 · Cited by 48
Structure, dynamics and assembly of the ankyrin complex on human red blood cell membrane
Xia, X., Liu, S., & Zhou, Z. H. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00779-7 · Cited by 49
Suh, J., Kim, M., Yoo, J., Han, J., Paulina, C., & Lim, M. H. (2022) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2022.214978 · Cited by 49
Chemical Features of Polyanions Modulate Tau Aggregation and Conformational States
Montgomery, K. M., Carroll, E. C., Thwin, A. C., Quddus, A., Hodges, P., Southworth, D. R., & Gestwicki, J. E. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c08004 · Cited by 48
“Only a subset of these compounds ( 1 , 6 , 13 , 15 , and 31 ) had, to our knowledge, been previously tested for their effects on tau aggregation.”
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 57
Goto, Y., Adachi, M., Muta, H., & So, M. (2017) · Biophysical Reviews · doi:10.1007/s12551-017-0370-7 · Cited by 49
Ghetti, B. F., Piccardo, P., & Zanusso, G. (2018) · Handbook of clinical neurology · doi:10.1016/b978-0-444-63945-5.00014-3 · Cited by 49
Self-citationKey Peptides and Proteins in Alzheimer’s Disease
Penke, B., Bogár, F., Paragi, G., Gera, J., & Fülöp, L. (2019) · Current Protein and Peptide Science · doi:10.2174/1389203720666190103123434 · Cited by 51
Formation of functional, non‐amyloidogenic fibres by recombinant Bacillus subtilis TasA
Erskine, E., Morris, R. J., Schor, M., Earl, C., Gillespie, R. M. C., Bromley, K. M., Sukhodub, T., Clark, L., Fyfe, P. K., Serpell, L. C., et al. (2018) · Molecular Microbiology · doi:10.1111/mmi.13985 · Cited by 48
“Many amyloid-like fibres formed in vitro from proteins associated with disease show an in-register parallel cross-β arrangement (Margittai and Langen, 2008); recently however native Tau filaments extracted from the brain of an Alzheimer's Disease patient have been demonstrated to form an elaborate mixed β-helix/cross-…”
BackgroundIn vitro amplification of pathogenic tau conserves disease-specific bioactive characteristics
Xu, H. W., O’Reilly, M., Gibbons, G. S., Changolkar, L. N., McBride, J. D., Riddle, D. M., Zhang, B., Stieber, A., Nirschl, J., Kim, S., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-020-02253-4 · Cited by 52
Functional and pathological amyloid structures in the eyes of 2020 cryo-EM
Ragonis‐Bachar, P., & Landau, M. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2021.01.006 · Cited by 48
Tau Aggregation Inhibiting Peptides as Potential Therapeutics for Alzheimer Disease
Aillaud, I., & Funke, S. A. (2022) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-022-01230-7 · Cited by 51
Lutter, L., Serpell, C. J., Tuite, M. F., & Xue, W. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.07.010 · Cited by 48
“For instance, tau fibrils from an Alzheimer’s patient and a Pick’s disease patient have remarkably different core arrangements [72,73].”
BackgroundLedreux, A., Pryhoda, M. K., Gorgens, K. A., Shelburne, K. B., Gilmore, A., Linseman, D. A., Fleming, H., Koza, L. A., Campbell, J., Wolff, A., et al. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00761 · Cited by 53
“Notably, Tau filaments in AD and CTE assume different molecular structures (Fitzpatrick et al., 2017; Falcon et al., 2019).”
BackgroundTau Spreading Mechanisms; Implications for Dysfunctional Tauopathies
Fuster-Matanzo, A., Hernández, F., & Ávila, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030645 · Cited by 50
Watanabe‐Nakayama, T., Nawa, M., Konno, H., Kodera, N., Ando, T., Teplow, D. B., & Ono, K. (2020) · ACS Nano · doi:10.1021/acsnano.0c03074 · Cited by 48
Beveridge, R., & Calabrese, A. N. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.603639 · Cited by 49
Transient disorder along pathways to amyloid
Morgan, G. J. (2021) · Biophysical Chemistry · doi:10.1016/j.bpc.2021.106711 · Cited by 45
Abskharon, R. N. N., Pan, H., Sawaya, M. R., Seidler, P. M., Olivares, E. J., Chen, Y., Murray, K. A., Zhang, J., Lantz, C., Bentzel, M., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2300258120 · Cited by 50
“The structures of paired helical filaments (PHF) and straight filaments (SF) extracted from patients with AD reveal tau molecules in crossβ folds, which are stabilized by steric zippers (7, 14).”
BackgroundTau filaments from amyotrophic lateral sclerosis/parkinsonism-dementia complex adopt the CTE fold
Qi, C., Verheijen, B. M., Kokubo, Y., Shi, Y., Tetter, S., Murzin, A. G., Nakahara, A., Morimoto, S., Vermulst, M., Sasaki, R., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2306767120 · Cited by 51
“By cryo - EM, we have shown that tau filaments from AD and CTE each consist of two identical C - shaped protofilaments that comprise residues 306 to 378 (in the num bering of the 441 amino acid tau isoform) (28–30).”
Self-citationMammeri, N. E., Dregni, A. J., Duan, P., & Hong, M. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2316175121 · Cited by 54
Modeling Prion-Like Processing of Tau Protein in Alzheimer’s Disease for Pharmaceutical Development
Wischik, C. M., Schelter, B. O., Wischik, D., Storey, J. M. D., & Harrington, C. R. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170727 · Cited by 49
Lim, K. H. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00158 · Cited by 46
“Recently, near-atomic resolution structures of tau filaments were determined by cryo-EM (Fitzpatrick et al., 2017; Falcon et al., 2018; Zhang et al., 2019).”
BackgroundGaspar, R., Lund, M., Sparr, E., & Linse, S. S. (2020) · QRB Discovery · doi:10.1017/qrd.2020.7 · Cited by 46
“…the high-resolution structures of model peptide fibrils (Eisenberg and Sawaya, 2017), and as a consequence, α -syn fibrils rather resemble amyloid fibrils formed from long peptides and proteins such as those of the amyloid β peptide and protein tau (Colvin et al. , 2016; Fitzpatrick et al. , 2017).”
PHF-Core Tau as the Potential Initiating Event for Tau Pathology in Alzheimer’s Disease
Luna‐Viramontes, N. I., Campa-Córdoba, B. B., Ontiveros‐Torres, M. Á., Harrington, C. R., Villanueva‐Fierro, I., Guadarrama-Ortíz, P., Garcés‐Ramírez, L., de la Cruz, F., Hernándes‐Alejandro, M., Martínez-Robles, S., et al. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00247 · Cited by 47
Therapeutic Strategies to Reduce the Toxicity of Misfolded Protein Oligomers
Kreiser, R. P., Wright, A. K., Block, N. R., Hollows, J. E., Nguyen, L. T., LeForte, K., Mannini, B., Vendruscolo, M., & Limbocker, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228651 · Cited by 48
“Moreover, advances in cryo-electron microscopy have recently led to the characterization of patient-derived fibrils of the tau protein in AD [192], Pick’s disease [193], chronic traumatic encephalopathy [194], corticobasal degeneration [195,196], and αS filaments from multiple system atrophy [197].”
BackgroundThe association of lipids with amyloid fibrils
Sanderson, J. M. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102108 · Cited by 48
“Structural studies by cryo-EM of tau filaments extracted from the brains of patients with corticobasal degeneration (69) and AD (70) show the presence of regions weak density around the core β-structure that may reflect the presence of a more dynamic or transiently occupied structure than the rest of the core.”
BackgroundRational design of functional amyloid fibrillar assemblies
Wang, X., Zhang, S., Zhang, J., Wang, Y., Jiang, X., Tao, Y., Li, D., Zhong, C., & Liu, C. (2023) · Chemical Society Reviews · doi:10.1039/d2cs00756h · Cited by 48
Acetylation discriminates disease-specific tau deposition
Chakraborty, P., Rivière, G., Hebestreit, A., de Opakua, A. I., Vorberg, I. M., Andreas, L. B., & Zweckstetter, M. (2023) · Nature Communications · doi:10.1038/s41467-023-41672-1 · Cited by 52
Femtosecond X-ray coherent diffraction of aligned amyloid fibrils on low background graphene
Seuring, C., Ayyer, K., Filippaki, E., Barthelmeß, M., Longchamp, J.-N., Ringler, P., Pardini, T., Wojtas, D. H., Coleman, M. A., Dörner, K., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04116-9 · Cited by 46
Schelter, B. O., Shiells, H., Baddeley, T. C., Rubino, C. M., Ganesan, H., Hammel, J., Vuksanović, V., Staff, R. T., Murray, A. D., Bracoud, L., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190772 · Cited by 47
Modelling neurodegenerative disease using brain organoids
Wray, S. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.05.012 · Cited by 45
Mechanistic roles for altered O-GlcNAcylation in neurodegenerative disorders
Balana, A. T., & Pratt, M. R. (2021) · Biochemical Journal · doi:10.1042/bcj20200609 · Cited by 46
Shirani, H., Appelqvist, H., Bäck, M., Klingstedt, T., Cairns, N. J., & Nilsson, K. P. R. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201703846 · Cited by 45
Press‐Sandler, O., & Miller, Y. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.03.014 · Cited by 45
Phosphorylation of serine 305 in tau inhibits aggregation
Strang, K. H., Sorrentino, Z. A., Riffe, C. J., Gorion, K.-M. M., Vijayaraghavan, N., Golde, T. E., & Giasson, B. I. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.11.011 · Cited by 46
Aggregation of Microtubule Binding Repeats of Tau Protein is Promoted by Cu2+
Ahmadi, S., Zhu, S., Sharma, R., Wu, B. H., Soong, R., Majumdar, R. D., Wilson, D. J., Simpson, A. J., & Kraatz, H. (2019) · ACS Omega · doi:10.1021/acsomega.8b03595 · Cited by 45
“30,31 The presence of cysteine (Cys) in R2 and R3 (Scheme 1) is another feature that may contribute to aggregation by the formation of a disul fi de bond.”
Fibril Self-Assembly of Amyloid–Spider Silk Block Polypeptides
Dai, B., Sargent, C. J., Gui, X., Liu, C., & Zhang, F. (2019) · Biomacromolecules · doi:10.1021/acs.biomac.9b00218 · Cited by 45
Katsinelos, T., Tuck, B. J., Mukadam, A. S., & McEwan, W. A. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01139 · Cited by 46
“From cryoelectron microscopy structures, the EFE motif is hypothesized to interact with the core structure in the AD paired-helical and straight filaments (119).”
BackgroundDiverse Structural Conversion and Aggregation Pathways of Alzheimerʼs Amyloid-β (1–40)
Lin, Y., Sahoo, B. R., Ozawa, D., Kinoshita, M., Kang, J., Lim, M. H., Okumura, M., Huh, Y. H., Moon, E., Jang, J. H., et al. (2019) · ACS Nano · doi:10.1021/acsnano.9b01578 · Cited by 47
Derreumaux, P., Man, V. H., Wang, J., & Nguyen, P. H. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c00574 · Cited by 45
Advances in methods for atomic resolution macromolecular structure determination
Thompson, M. C., Yeates, T. O., & Rodríguez, J. A. (2020) · F1000Research · doi:10.12688/f1000research.25097.1 · Cited by 45
Expanding spectrum of prion diseases
Ayers, J. I., Paras, N. A., & Prusiner, S. B. (2020) · Emerging Topics in Life Sciences · doi:10.1042/etls20200037 · Cited by 45
Metadata
- Authors
- 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.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Indiana University Indianapolis (US)
- Corresponding author
- Goedert, Michel
- Scheres, Sjors H. W.
- ORCID
- Venue
- Nature
- Published
- 2017-07
- Volume
- 547
- Issue
- 7662
- Pages
- 185-190
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC5552202
- OpenAlex
- W2727929522
- Cited by
- 2,061
- References
- 58
- Citations by year
- 2026: 197 · 2025: 224 · 2024: 225 · 2023: 224 · 2022: 214 · 2021: 231 · 2020: 280 · 2019: 227 · 2018: 193 · 2017: 42
- FWCI
- 150.60
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- IUScholarWorks (Indiana University) (submittedVersion)
- Purdue University Indianapolis (Indiana University) (submittedVersion)
- PMC
- Funders
- Medical Research Council (MC_EX_MR/N027892/1)
- National Institute on Aging (P30AG010133)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, tau filaments, paired helical filaments, straight filaments, tau aggregation, protofilaments, tauopathy, neurodegenerative diseases
- MeSH terms
- Aged, Alzheimer Disease, Amino Acid Sequence, Amyloid, Brain, Female, Humans, tau Proteins, Cryoelectron Microscopy, Protein Aggregation, Pathological
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