Ultrasensitive tau biosensor cells detect no seeding in Alzheimer’s disease CSF
Open accessAbstract
Tau protein forms self-replicating assemblies (seeds) that may underlie progression of pathology in Alzheimer’s disease (AD) and related tauopathies. Seeding in recombinant protein preparations and brain homogenates has been quantified with “biosensor” cell lines that express tau with a disease-associated mutation (P301S) fused to complementary fluorescent proteins. Quantification of induced aggregation in cells that score positive by fluorescence resonance energy transfer (FRET) is accomplished by cell imaging or flow cytometry. Several groups have reported seeding activity in antemortem cerebrospinal fluid (CSF) using various methods, but these findings are not yet widely replicated. To address this question, we created two improved FRET-based biosensor cell lines based on tau expression, termed version 2 low (v2L) and version 2 high (v2H). We determined that v2H cells are ~ 100-fold more sensitive to AD-derived tau seeds than our original lines, and coupled with immunoprecipitation reliably detect seeding from samples containing as little as 100 attomoles of recombinant tau fibrils or ~ 32 pg of total protein from AD brain homogenate. We tested antemortem CSF from 11 subjects with a clinical diagnosis of AD, 9 confirmed by validated CSF biomarkers. We used immunoprecipitation coupled with seed detection in v2H cells and detected no tau seeding in any sample. Thus we cannot confirm prior reports of tau seeding activity in the CSF of AD patients. This next generation of ultra-sensitive tau biosensors may nonetheless be useful to the research community to quantify tau pathology as sensitively and specifically as possible.
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Tau FRET sensors composed of tau P301S-Ruby2 and -Clover reporters aggregate and transmit FRET signals in the presence of seed-competent tau species.
“These reporter proteins aggregate and transmit FRET signals in the presence of seed-competent tau species (44, 45).”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [44]
The Results section (‘Construction of tau RD(P301S) v2H biosensor cells’; page not available) reports that the biosensors aggregate and produce FRET upon exposure to tau seeds. But the Methods section (‘Generation of biosensor cell lines’; page not available) identifies the reporters as tau RD(P301S) fused to mClover3 and mCerulean3, not Ruby2 and Clover. (LLM, conf=0.90)
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Cites
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · see citing works
Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208 · 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
Propagation of Tau Misfolding from the Outside to the Inside of a Cell
Frost, B., Jacks, R. L., & Diamond, M. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808759200 · Cited by 1,252 · see citing works
Self-citationDistinct 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
Self-citationRapid protein-folding assay using green fluorescent protein
Waldo, G. S., Standish, B. M., Berendzen, J., & Terwilliger, T. C. (1999) · Nature Biotechnology · doi:10.1038/10904 · Cited by 906 · see citing works
Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds
Holmes, B. B., DeVos, S. L., Kfoury, N., Li, M., Jacks, R., Yanamandra, K., Ouidja, M. O., Brodsky, F. M., Marasa, J., Bagchi, D. P., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301440110 · Cited by 859 · see citing works
Self-citationNeuronal activity enhances tau propagation and tau pathology in vivo
Wu, J. W., Hussaini, S. A., Bastille, I. M., Rodriguez, G. A., Mrejeru, A., Rilett, K., Sanders, D. W., Cook, C., Fu, H., Boonen, R. A. C. M., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4328 · Cited by 820 · see citing works
Self-citationProteopathic tau seeding predicts tauopathy in vivo
Holmes, B. B., Furman, J. L., Mahan, T. E., Yamasaki, T. R., Mirbaha, H., Eades, W. C., Belaygorod, L., Cairns, N. J., Holtzman, D. M., & Diamond, M. I. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411649111 · Cited by 696 · see citing works
Self-citationPropagation 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
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
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
Self-citationTrans-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
Self-citationZhang, W., Falcon, B., Murzin, A. G., Fan, J., Crowther, R. A., Goedert, M., & Scheres, S. H. W. (2019) · eLife · doi:10.7554/elife.43584 · Cited by 500 · see citing works
Transient increase in total tau but not phospho-tau in human cerebrospinal fluid after acute stroke
Hesse, C., Rosengren, L., Andreasen, N., Davidsson, P., Vanderstichele, H., Vanmechelen, E., & Blennow, K. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01697-9 · Cited by 450 · see citing works
Bajar, B. T., Wang, E. S., Lam, A. J., Kim, B. B., Jacobs, C. L., Howe, E. S., Davidson, M. W., Lin, M. Z., & Chu, J. (2016) · Scientific Reports · doi:10.1038/srep20889 · Cited by 380 · 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
Synaptic Tau Seeding Precedes Tau Pathology in Human Alzheimer’s Disease Brain
DeVos, S. L., Corjuc, B. T., Oakley, D. H., Nobuhara, C. K., Bannon, R. N., Chase, A., Commins, C., Gonzalez, J. A., Dooley, P. M., Frosch, M. P., et al. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00267 · Cited by 285 · see citing works
Markwardt, M. L., Kremers, G., Kraft, C. A., Ray, K., Cranfill, P. J. C., Wilson, K. A., Day, R. N., Wachter, R. M., Davidson, M. W., & Rizzo, M. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017896 · Cited by 266 · see citing works
Kaufman, S. K., Del Tredici, K., Thomas, T. L., Braak, H., & Diamond, M. I. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1855-6 · Cited by 259 · see citing works
Self-citationMechanisms of Cell-to-Cell Transmission of Pathological Tau: A Review
Gibbons, G. S., Lee, V. M. Y., & Trojanowski, J. Q. (2019) · JAMA Neurology · doi:10.1001/jamaneurol.2018.2505 · Cited by 257 · see citing works
Enhanced tau aggregation in the presence of Amyloid β
Bennett, R. E., DeVos, S. L., Dujardin, S., Corjuc, B., Gor, R., Gonzalez, J., Roe, A. D., Frosch, M. P., Pitstick, R., Carlson, G. A., et al. (2017) · The American Journal of Pathology · doi:10.1016/j.ajpath.2017.03.011 · Cited by 245 · see citing works
Conformational Diversity of Wild-type Tau Fibrils Specified by Templated Conformation Change
Frost, B., Ollesch, J., Wille, H., & Diamond, M. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m805627200 · Cited by 224 · see citing works
Self-citationCSF 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
Saijo, E., Metrick, M. A., Koga, S., Parchi, P., Litvan, I., Spina, S., Boxer, A. L., Rojas, J. C., Galasko, D. R., Kraus, A., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02080-2 · Cited by 170 · see citing works
Cicognola, C., Brinkmalm, G., Wahlgren, J., Portelius, E., Gobom, J., Cullen, N. C., Hansson, O., Parnetti, L., Constantinescu, R., Wildsmith, K., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-018-1948-2 · Cited by 168 · 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.2018.04.035 · Cited by 154 · see citing works
Saijo, E., Ghetti, B. F., Zanusso, G., Oblak, A. L., Furman, J. L., Diamond, M. I., Kraus, A., & Caughey, B. W. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1692-z · Cited by 145 · see citing works
Self-citationSeeding selectivity and ultrasensitive detection of tau aggregate conformers of Alzheimer disease
Kraus, A., Saijo, E., Metrick, M. A., Newell, K., Sigurdson, C. J., Zanusso, G., Ghetti, B., & Caughey, B. (2019) · Acta Neuropathologica · doi:10.1007/s00401-018-1947-3 · Cited by 143 · see citing works
Widespread tau seeding activity at early Braak stages
Furman, J. L., Vaquer‐Alicea, J., White, C. L., Cairns, N. J., Nelson, P. T., & Diamond, M. I. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1644-z · Cited by 142 · see citing works
Self-citationBarthélemy, 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
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
CSF biomarkers for Alzheimer's disease: current utility and potential future use
Holtzman, D. M. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.09.003 · Cited by 122 · see citing works
Metrick, M. A., Ferreira, N., Saijo, E., Kraus, A., Newell, K. L., Zanusso, G., Vendruscolo, M., Ghetti, B. F., & Caughey, B. W. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-0887-z · Cited by 121 · see citing works
Takeda, S., Commins, C., DeVos, S. L., Nobuhara, C. K., Wegmann, S., Roe, A. D., Costantino, I., Fan, Z., Nicholls, S. B., Sherman, A. E., et al. (2016) · Annals of Neurology · doi:10.1002/ana.24716 · Cited by 113 · see citing works
Cerebrospinal fluid tau fragment correlates with tau PET: a candidate biomarker for tangle pathology
Blennow, K., Chen, C., Cicognola, C., Wildsmith, K. R., Manser, P. T., Bohorquez, S. M. S., Zhang, Z., Xie, B., Peng, J., Hansson, O., et al. (2020) · Brain · doi:10.1093/brain/awz346 · Cited by 105 · see citing works
Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry
Furman, J. L., Holmes, B. B., & Diamond, M. I. (2015) · Journal of Visualized Experiments · doi:10.3791/53205 · Cited by 101 · see citing works
Self-citationCrowther, T., Goedert, M., & Wischik, C. M. (1989) · Annals of Medicine · doi:10.3109/07853898909149199 · Cited by 100 · see citing works
Characterization of tau prion seeding activity and strains from formaldehyde-fixed tissue
Kaufman, S. K., Thomas, T. L., Tredici, K. D., Braak, H., & Diamond, M. I. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0442-8 · Cited by 97 · see citing works
Self-citationShin, W. S., Di, J., Cao, Q., Li, B., Seidler, P. M., Murray, K. A., Bitan, G., & Jiang, L. (2019) · Alzheimer s Research & Therapy · doi:10.1186/s13195-019-0541-9 · Cited by 94 · see citing works
Tariciotti, L., Casadei, M., Honig, L. S., Teich, A. F., McKhann, G. M., Tosto, G., & Mayeux, R. P. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180548 · Cited by 46 · see citing works
Tau exhibits unique seeding properties in globular glial tauopathy
Chung, D. C., Carlomagno, Y., Cook, C. N., Jansen‐West, K. R., Daughrity, L. M., Lewis‐Tuffin, L. J., Castanedes‐Casey, M., Deture, M. A., Dickson, D. W., & Petrucelli, L. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0691-9 · Cited by 37 · see citing works
Foiani, M. S., Cicognola, C., Ermann, N., Woollacott, I., Heller, C., Heslegrave, A., Keshavan, A., Paterson, R. W., Ye, K., Kornhuber, J., et al. (2019) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2018-319266 · Cited by 35 · see citing works
Cerebrospinal fluid from Alzheimer’s disease patients promotes tau aggregation in transgenic mice
Skachokova, Z. K., Martinisi, A., Flach, M., Sprenger, F., Naegelin, Y., Steiner-Monard, V., Sollberger, M. A., Monsch, A. U., Goedert, M., Tolnay, M., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0725-3 · Cited by 24 · see citing works
Tanaka, Y., Yamada, K., Satake, K., Nishida, I., Heuberger, M., Kuwahara, T., & Iwatsubo, T. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01258 · Cited by 22 · see citing works
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Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming
Sun, Z., Kwon, J.-S., Ren, Y., Chen, S., Walker, C. K., Lu, X., Cates, K., Karahan, H., Sviben, S., Fitzpatrick, J. A. J., et al. (2024) · Science · doi:10.1126/science.adl2992 · Cited by 77 · see citing works
“These reporter proteins aggregate and transmit FRET signals in the presence of seed-competent tau species (44, 45).”
Self-citationCo-opting templated aggregation to degrade pathogenic tau assemblies and improve motor function
Miller, L. V. C., Papa, G., Vaysburd, M., Cheng, S., Sweeney, P. W., Smith, A. N., Franco, C. D. M. F., Katsinelos, T., Huang, M., Sanford, S., et al. (2024) · Cell · doi:10.1016/j.cell.2024.08.024 · Cited by 58 · see citing works
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Zwierzchowski-Zarate, A. N., Mendoza‐Oliva, A., Kashmer, O. M., Collazo-Lopez, J. E., White, C. L., & Diamond, M. I. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102132 · Cited by 45 · see citing works
Self-citationDevelopmental neurotoxicity of PFOA exposure on hiPSC-derived cortical neurons
Wu, S., Xie, J., Zhao, H., Zhao, X., Sánchez, O. F., Rochet, J., Freeman, J. L., & Yuan, C. (2024) · Environment International · doi:10.1016/j.envint.2024.108914 · Cited by 42 · see citing works
Lorenzo, D. D. (2024) · ChemMedChem · doi:10.1002/cmdc.202400180 · Cited by 40 · see citing works
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Mac, K. D., & Su, J. (2025) · npj Biosensing · doi:10.1038/s44328-025-00040-3 · Cited by 38 · see citing works
Böken, D., Cox, D., Burke, M., Lam, J. Y. L., Katsinelos, T., Danial, J. S. H., Fertan, E., McEwan, W. A., Rowe, J. B., & Klenerman, D. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202317756 · Cited by 37 · see citing works
Manca, M., Standke, H. G., Browne, D. F., Huntley, M. L., Thomas, O. R., Orru, C. D., Hughson, A. G., Kim, Y., Zhang, J., Tatsuoka, C. M., et al. (2023) · Acta Neuropathologica · doi:10.1007/s00401-023-02574-0 · Cited by 34 · see citing works
Biophysical properties of a tau seed
Hou, Z., Chen, D., Ryder, B. D., & Joachimiak, Ł. A. (2021) · Scientific Reports · doi:10.1038/s41598-021-93093-z · Cited by 31 · see citing works
Aggidis, A., Devitt, G., Zhang, Y., Chatterjee, S., Townsend, D. J., Fullwood, N. J., Ruiz, E., Tarutani, A., Hasegawa, M., Cooper, A. S., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14246 · Cited by 31 · see citing works
Self-citationThe dual fates of exogenous tau seeds: Lysosomal clearance versus cytoplasmic amplification
Kolay, S., Vega, A. R., Dodd, D. A., Perez, V. A., Kashmer, O. M., White, C. L., & Diamond, M. I. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102014 · Cited by 29 · see citing works
Self-citationTau seeding in cases of multiple sclerosis
LaCroix, M., Mirbaha, H., Shang, P., Zandee, S., Foong, C., Prat, A., White, C. L., Stüve, O., & Diamond, M. I. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01444-2 · Cited by 27 · see citing works
Self-citationXie, J., Wu, S., Szadowski, H., Min, S., Yang, Y., Bowman, A. B., Rochet, J., Freeman, J. L., & Yuan, C. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105023 · Cited by 27 · see citing works
Frey, B., Holzinger, D., Taylor, K. C., Ehrnhoefer, D. E., Striebinger, A., Biesinger, S., Gasparini, L., O’Neill, M. J., Wegner, F., Barghorn, S., et al. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01676-w · Cited by 27 · see citing works
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Stopschinski, B. E., Del Tredici, K., Estill-Terpack, S.-J., Ghebremedhin, E., Yu, F. F., Braak, H., & Diamond, M. I. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01255-x · Cited by 26 · see citing works
Self-citationWater-directed pinning is key to tau prion formation
Vigers, M. P., Lobo, S., Najafi, S., DuBose, A., Tsay, K., Ganguly, P., Longhini, A. P., Jin, Y., Buratto, S. K., Kosik, K. S., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2421391122 · Cited by 24 · see citing works
DnaJC7 specifically regulates tau seeding
Perez, V. A., Sanders, D. W., Mendoza‐Oliva, A., Stopschinski, B. E., Mullapudi, V., White, C. L., Joachimiak, Ł. A., & Diamond, M. I. (2023) · eLife · doi:10.7554/elife.86936 · Cited by 24 · see citing works
Self-citationRyder, B. D., Ustyantseva, E., Boyer, D. R., Mendoza‐Oliva, A., Kuska, M. I., Wydorski, P. M., Macierzyńska, P., Morgan, N., Sawaya, M. R., Diamond, M. I., et al. (2024) · Structure · doi:10.1016/j.str.2024.02.015 · Cited by 24 · see citing works
Self-citationNeurodegeneration risk factor, EIF2AK3 (PERK), influences tau protein aggregation
Park, G., Xu, K., Chea, L., Kim, K., Safarta, L. A., Song, K., Wu, J., Park, S., Min, H., Hiramatsu, N., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102821 · Cited by 23 · see citing works
VCP regulates early tau seed amplification via specific cofactors
Batra, S., Vaquer‐Alicea, J., Valdez, C., Taylor, S. P., Manon, V. A., Vega, A. R., Kashmer, O. M., Kolay, S., Lemoff, A. S., Cairns, N. J., et al. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00783-z · Cited by 22 · see citing works
Self-citationCecon, E., Oishi, A., Luka, M., Ndiaye‐Lobry, D., François, A., Lescuyer, M., Panayi, F., Dam, J., Machado, P., & Jockers, R. (2023) · eLife · doi:10.7554/elife.78360 · Cited by 16 · see citing works
Anti-tau antibodies targeting a conformation-dependent epitope selectively bind seeds
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Self-citationFunctional classification of tauopathy strains reveals the role of protofilament core residues
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Self-citationPinzi, L., Conze, C., Bisi, N., Torre, G. D., Soliman, A., Monteiro-Abreu, N., Trushina, N. I., Krusenbaum, A., Dolouei, M. K., Hellwig, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45851-6 · Cited by 14 · see citing works
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Lathuilière, A., Jo, Y., Perbet, R., Donahue, C., Commins, C., Quittot, N., Fan, Z., Bennett, R. E., & Hyman, B. T. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00643-2 · Cited by 12 · see citing works
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Sala‐Jarque, J., Zimkowska, K., Ávila, J., Ferrer, I., & del Rı́o, J. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911527 · Cited by 10 · see citing works
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Jin, N., Gu, J., Wu, R., Chu, D., Tung, Y. C., Węgiel, J., Wısnıewskı, T., Gong, C., Iqbal, K., & Liu, F. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01436-2 · Cited by 8 · see citing works
Hromádková, L., Kim, C., Haldiman, T., Peng, L., Zhu, X., Cohen, M. L., de Silva, R., & Safar, J. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-01133-0 · Cited by 6 · see citing works
DnaJs are enriched in tau regulators
Esquivel, A. R., Hill, S. E., & Blair, L. J. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.127486 · Cited by 6 · see citing works
Tau in Multiple Sclerosis: A Review of Therapeutic Potential
Hoehne, C. L., Stüve, O., & Stopschinski, B. E. (2025) · Current Treatment Options in Neurology · doi:10.1007/s11940-024-00820-8 · Cited by 6 · see citing works
Diamond, M. I. (2023) · Cytoskeleton · doi:10.1002/cm.21806 · Cited by 5 · see citing works
Self-citationBöken, D., Cox, D., Burke, M., Lam, J. Y. L., Katsinelos, T., Danial, J. S. H., Fertan, E., McEwan, W. A., Rowe, J. B., & Klenerman, D. (2024) · Angewandte Chemie · doi:10.1002/ange.202317756 · Cited by 4 · see citing works
Zeng, Z., Fichou, Y., Vigers, M. P., Tsay, K., & Han, S. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c02022 · Cited by 4 · see citing works
Tau seeds translocate across the cell membrane to initiate aggregationPreprint
Dodd, D. A., LaCroix, M., Valdez, C., Knox, G. M., Vega, A. R., Kumar, A., Xing, C., White, C. L., & Diamond, M. I. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.05.10.491429 · Cited by 4 · see citing works
Self-citationZeng, Z., Tsay, K., Vijayan, V., Frost, M. P., Prakash, S., Quddus, A., Albert, A., Vigers, M. P., Srivastava, M., Woerman, A. L., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.19.549721 · Cited by 4 · see citing works
Houzé, L., Dhénain, M., Lam, S., Petit, F., Haı̈k, S., Mouton‐Liger, F., Hugon, J., Dam, J., Paquet, C., Jockers, R., et al. (2025) · Alzheimer s Research & Therapy · doi:10.1186/s13195-025-01792-w · Cited by 3 · see citing works
Discovery of penicillic acid as a chemical probe against tau aggregation in Alzheimer's disease
Shyong, J., Wang, J., Huynh, Q.-D. T., Fayzullina, M., Yuan, B., Lee, C., Minehan, T. G., Seidler, P. M., & Wang, C. C. C. (2024) · Chemical Science · doi:10.1039/d4sc05469e · Cited by 3 · see citing works
Amyloid-motif-dependent tau self-assembly is modulated by isoform sequence context
Bali, S., Wydorski, P. M., Singh, R., Nuland, N. E. V., Wosztyl, A., Morgan, N., Perez, V. A., Chen, D., Chen, J., Rizo, J., et al. (2025) · Structure · doi:10.1016/j.str.2025.11.009 · Cited by 3 · see citing works
Anti-tau antibodies targeting a conformation-dependent epitope selectively bind seeds
Hitt, B. D., Gupta, A., Singh, R., Yang, T., Beaver, J. D., Shang, P., White, C. L., Joachimiak, L. A., & Diamond, M. I. (2023) · doi:10.1101/2023.05.04.539475 · Cited by 15 · see citing works
Self-citationCerebellar contributions to tau-mediated cognitive and behavioral dysfunction
Angeles-Perez, L., Ren, C., Neniel, J., Widner, J., Yamashiro, K., Tak, Y., Batra, S., Tan, T., Nguyen, B., Diamond, M. I., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116036 · Cited by 2 · see citing works
Self-citationPredifferentiation Neurotoxicity of GenX Exposure on hiPSC-Derived Cortical Neurons
Wu, S., Xie, J., Zhao, X., Zhao, H., Sánchez, O. F., Yu, S., Rochet, J.-C., Freeman, J. L., & Yuan, C. (2026) · Environmental Science & Technology · doi:10.1021/acs.est.5c13193 · Cited by 2 · see citing works
In situ seeding assay: A novel technique for direct tissue localization of bioactive tau.
Perbet, R., de Gerando, A. M., Glynn, C., Donahue, C., Gaona, A., Taddei, R., Gómez-Isla, T., Lathuiliere, A., & Hyman, B. (2024) · Journal of Neuropathology and Experimental Neurology · doi:10.1093/jnen/nlae059 · Cited by 2 · see citing works
Tau in Health and Neurodegenerative Diseases
Chu, D., & Liu, F. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.101299 · Cited by 2 · see citing works
Preclinical Development of a Vectorized Artificial miRNA Gene Therapy for TauopathiesPreprint
Garza, I. T., Snyder, B., Holmes, S. K., Pearce, K. M., Knight, K. L., & Bailey, R. M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.12.681935 · Cited by 2 · see citing works
Chemical Approaches for Array Based Detection of Amyloids
Simon, P. M., Xu, Y., & Kaur, A. (2025) · Advanced Sensor Research · doi:10.1002/adsr.202500108 · Cited by 1 · see citing works
Alghamdi, H. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103322 · Cited by 1 · see citing works
Two simple assays for assessing the seeding activity of proteopathic tau
Liu, F., Wu, R., Jin, N., Chu, D., Gu, J., Tung, Y. C., Hu, Z., Gong, C., & Iqbal, K. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1073774 · Cited by 1 · see citing works
DnaJB1 chaperone inhibits tau aggregation by recognizing its N-terminusPreprint
Wydorski, P. M., Macierzyńska, P., Bali, S., Vaquer‐Alicea, J., & Joachimiak, Ł. A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.02.680111 · Cited by 1 · see citing works
Self-citationCysteines are critical determinants of spontaneous and seeded tau aggregation in cellsPreprint
Joachimiak, Ł. A., Jayan, P., Rastogi, S., Bommareddy, V., Dashnaw, C., Vaquer‐Alicea, J., Nguyen, B. A., Saelices, L., Shahmoradian, S. H., White, C. L., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-9217102/v1 · Cited by 1 · see citing works
Self-citationTau isoform imbalance and aggregation are pathological hallmarks of X-linked dystonia-parkinsonismPreprint
Reyes, C. J., Domingo, A., Penney, E. B., Norenberg, E. P., Han, J., Murcar, M. G., Vaine, C. A., Bravo‐Vasquez, N., Tran, H., Quittot, N., et al. (2026) · medRxiv · doi:10.64898/2026.07.23.26358614 · Cited by 1 · see citing works
Self-citationAndrés‐Benito, P., Carmona, M., Jordán, M., del Rı́o, J. A., & Ferrer, I. (2021) · Research Square · doi:10.21203/rs.3.rs-889543/v2
Editor's evaluation: DnaJC7 specifically regulates tau seeding
Dötsch, V. (2023) · eLife · doi:10.7554/elife.86936.sa0
Selective Targeting of Pathogenic Tau Seeds via a Novel VHHPreprint
Gupta, A., Liu, R., Keely, D., Sunderman, V., Tak, Y., Konstantoulea, K., Terpack, S. J., White, C. L., Russ, W. P., Rizo, J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.13.632833
Self-citationAmyloid- and Tau-Targeted Therapies in Alzheimer’s Disease
Rajic, A. J., Galasko, D. R., & Tuszynski, M. H. (2025) · Springer eBooks · doi:10.1007/978-3-031-89307-0_17
Conformation-based detection of tau seeds with a novel VHHPreprint
Gupta, A., Liu, R., Keely, D., Sunderman, V., Tak, Y., Konstantoulea, K., Terpack, S. J., White, C. L., Russ, W. P., Rizo, J., et al. (2025) · Research Square · doi:10.21203/rs.3.rs-8274351/v1
Self-citationLathuilière, A., Jo, Y., Perbet, R., Donahue, C., Commins, C., Quittot, N., Fan, Z., Bennett, R. E., & Hyman, B. T. (2023) · Figshare · doi:10.6084/m9.figshare.23908793
Frey, B., Holzinger, D., Taylor, K. C., Ehrnhoefer, D. E., Striebinger, A., Biesinger, S., Gasparini, L., O’Neill, M. J., Wegner, F., Barghorn, S., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26639710
Jin, N., 顾建兰, Wu, R., Chu, D., Tung, Y. C., Węgiel, J., Wisniewski, T., Gong, C.-X., Iqbal, K., & Liu, F. (2022) · Figshare · doi:10.6084/m9.figshare.20968215
Stopschinski, B. E., Tredici, K. D., Estill-Terpack, S.-J., Ghebremedhin, E., Yu, F. F., Braak, H., & Diamond, M. I. (2021) · Figshare · doi:10.6084/m9.figshare.16786942
Self-citationSiddique, I. A., Hong, M., & Bitan, G. (2026) · Topics in medicinal chemistry · doi:10.1007/7355_2026_189
Clemente, E., Sivasubramanian, R., Kordes, S., Bhatia, P., Hans, R., Vogel, S., Baumann, M., Klebl, B., & Sterneckert, J. L. (2026) · Cells · doi:10.3390/cells15131228
Generation of Stable Tau Biosensor Cell Lines
Vaquer‐Alicea, J., & Bommareddy, V. (2026) · Neuromethods · doi:10.1007/978-1-0716-5234-3_11
Self-citationEndolysosomal inhibition uncouples tau uptake from intracellular seeding
Dodd, D. A., LaCroix, M., Valdez, C., Mendoza‐Oliva, A., Beaver, J. D., Vega, A. R., Kumar, A., Xing, C., White, C. L., & Diamond, M. I. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113498
Self-citationDifferential aggregation and seeding of tau microtubule-binding region fragments in vitro
Kim, M.-S., Hwang, S.-J., Kim, D., & Yoon, S.-Y. (2026) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2026.154575
Yanamandra, K., Romanul, N., Patel, H., Sanders, H., Chang, R., Darcy, A., Brown, N., Kane, C. A., Wu, H.-Y., Jagtap, K., et al. (2026) · Molecular Neurodegeneration Advances · doi:10.1186/s44477-026-00049-6
Large-Scale Mutagenesis Identifies Sequence Changes That Bias Tau Toward CTE-like AggregationPreprint
Joachimiak, Ł. A., Dashnaw, C., Rastogi, S., Morgan, N., Memon, I., Jaczynska, K., Nguyen, B. A., Saelices, L., White, C. L., & Shahmoradian, S. H. (2026) · Research Square · doi:10.64898/2026.10.08.757173
- Authors
- Hitt, B. D., Vaquer-Alicea, J., Manon, V. A., Beaver, J. D., Kashmer, O. M., Garcia, J. N., & Diamond, M. I.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- Corresponding author
- Diamond, Marc I.
- Venue
- Acta Neuropathologica Communications
- Published
- 2021-05-26
- Volume
- 9
- Issue
- 1
- Pages
- 99-99
- ISSN
- 2051-5960 (ISSN-L)
- PMC
- PMC8152020
- OpenAlex
- W3165482231
- Cited by
- 71
- References
- 45
- Citations by year
- 2026: 11 · 2025: 14 · 2024: 12 · 2023: 18 · 2022: 10 · 2021: 6
- FWCI
- 7.23
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Acta Neuropathologica Communications (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institute of Neurological Disorders and Stroke (5R25NS098987)
- Alzheimer's Association (2018-AACSF-591977)
- Broughton Foundation
- National Institute on Aging (R01AG059689-01A1)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau seeding, Alzheimer's disease, cerebrospinal fluid, P301S tau, FRET biosensor, tau aggregation, tauopathy, cerebrospinal fluid biomarkers, immunoprecipitation, antemortem diagnosis
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Animals, Brain, Cells, Cultured, Female, Humans, Male, Mice, Inbred C57BL, Mice, Transgenic, Middle Aged, Biosensing Techniques, tau Proteins, Mice, HEK293 Cells
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