Unique pathological tau conformers from Alzheimer’s brains transmit tau pathology in nontransgenic mice

Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

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A protein factor essential for microtubule assembly

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A mesoscale connectome of the mouse brain

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Pathological α-Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice

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

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Neurodegenerative Tauopathies

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Transmission and spreading of tauopathy in transgenic mouse brain

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Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils

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Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP

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Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils

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The AD tau core spontaneously self-assembles and recruits full-length tau to filaments

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The anesthetic sevoflurane induces tau trafficking from neurons to microglia

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Tau Toxicity in Neurodegeneration

Liang, S., Wang, Z.-T., Tan, L., & Yu, J. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02809-3 · Cited by 61

The existence of Aβ strains and their potential for driving phenotypic heterogeneity in Alzheimer’s disease

Lau, H. H. C., Ingelsson, M., & Watts, J. C. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02201-2 · Cited by 57

Differential cross-seeding properties of tau and α-synuclein in mouse models of tauopathy and synucleinopathy

Williams, T., Sorrentino, Z. A., Weinrich, M. J., Giasson, B. I., & Chakrabarty, P. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa090 · Cited by 56

Clustering of Tau fibrils impairs the synaptic composition of α3‐Na+/K+‐ATPase and AMPA receptors

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Cholesterol determines the cytosolic entry and seeded aggregation of tau

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Tau seeding and spreading in vivo is supported by both AD-derived fibrillar and oligomeric tau

de Gérando, A. M., Welikovitch, L. A., Khasnavis, A., Commins, C., Glynn, C. A., Chun, J. E., Perbet, R., & Hyman, B. T. (2023) · Acta Neuropathologica · doi:10.1007/s00401-023-02600-1 · Cited by 54

GFP-Mutant Human Tau Transgenic Mice Develop Tauopathy Following CNS Injections of Alzheimer's Brain-Derived Pathological Tau or Synthetic Mutant Human Tau Fibrils

Gibbons, G. S., Banks, R. A., Kim, B., Xu, H., Changolkar, L., Leight, S. N., Riddle, D. M., Li, C., Gathagan, R. J., Brown, H. J., et al. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.2393-17.2017 · Cited by 53

Therapeutic antibody targeting microtubule-binding domain prevents neuronal internalization of extracellular tau via masking neuron surface proteoglycans

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

Tau Propagation as a Diagnostic and Therapeutic Target for Dementia: Potentials and Unanswered Questions

Takeda, S. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01274 · Cited by 53

Tau and Alpha Synuclein Synergistic Effect in Neurodegenerative Diseases: When the Periphery Is the Core

Vacchi, E., Kaelin‐Lang, A., & Melli, G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21145030 · Cited by 51

Catalytic Nanoparticles in Biomedical Applications: Exploiting Advanced Nanozymes for Therapeutics and Diagnostics

Manoharan, D., Wang, L., Chen, Y., Li, W., & Yeh, C. (2024) · Advanced Healthcare Materials · doi:10.1002/adhm.202400746 · Cited by 50

In 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

Novelty‐like activation of locus coeruleus protects against deleterious human pretangle tau effects while stress‐inducing activation worsens its effects

Omoluabi, T., Torraville, S. E., Maziar, A., Ghosh, A., Power, K. D., Reinhardt, C., Harley, C. W., & Yuan, Q. (2021) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.12231 · Cited by 53

Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain

Diner, I., Nguyen, T. T. H., & Seyfried, N. T. (2017) · Journal of Visualized Experiments · doi:10.3791/55835 · Cited by 52

Intracerebral seeding of amyloid-β and tau pathology in mice: Factors underlying prion-like spreading and comparisons with α-synuclein

McAllister, B. B., Lacoursiere, S. G., Sutherland, R. J., & Mohajerani, M. H. (2020) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2020.01.026 · Cited by 48

Cholesterol 25-hydroxylase mediates neuroinflammation and neurodegeneration in a mouse model of tauopathy

Toral-Rios, D., Long, J. M., Ulrich, J. D., Yu, J., Strickland, M. R., Han, X., Holtzman, D. M., Cashikar, A. G., & Paul, S. M. (2024) · Journal of Experimental Medicine · doi:10.1084/jem.20232000 · Cited by 47

Emerging Nanotechnology for Treatment of Alzheimer’s and Parkinson’s Disease

Li, A., Tyson, J., Patel, S. G., Patel, M., Katakam, S., Mao, X., & He, W. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.672594 · Cited by 48

Impaired tau–microtubule interactions are prevalent among pathogenic tau variants arising from missense mutations

Xia, Y., Sorrentino, Z. A., Kim, J. D., Strang, K. H., Riffe, C. J., & Giasson, B. I. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010178 · Cited by 48

Prevalence of Concomitant Pathologies in Parkinson’s Disease: Implications for Prognosis, Diagnosis, and Insights into Common Pathogenic Mechanisms

Walker, L., & Attems, J. (2023) · Journal of Parkinson s Disease · doi:10.3233/jpd-230154 · Cited by 48

Delta-secretase cleavage of Tau mediates its pathology and propagation in Alzheimer’s disease

Kang, S. S., Ahn, E. H., & Ye, K. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-00494-7 · Cited by 46

Functional Neurophysiological Biomarkers of Early-Stage Alzheimer’s Disease: A Perspective of Network Hyperexcitability in Disease Progression

Tok, S., Ahnaou, A., & Drinkenburg, W. H. I. M. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210397 · Cited by 45

Real-time mechanisms of exacerbated synaptic remodeling by microglia in acute models of systemic inflammation and tauopathy

Cangalaya, C., Wegmann, S., Sun, W., Diez, L., Gottfried, A., Richter, K., Stoyanov, S., Pakan, J. M. P., Fischer, K., & Dityatev, A. E. (2023) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2023.02.023 · Cited by 48

Tau follows principal axes of functional and structural brain organization in Alzheimer’s disease

Ottoy, J., Kang, M. S., Tan, J. X. M., Boone, L., de Wael, R. V., Park, B., Bezgin, G., Lussier, F. Z., Pascoal, T. A., Rahmouni, N., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49300-2 · Cited by 56

Structural disorder in four-repeat Tau fibrils reveals a new mechanism for barriers to cross-seeding of Tau isoforms

Weismiller, H. A., Murphy, R., Wei, G., Ma, B., Nussinov, R., & Margittai, M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005316 · Cited by 44

Detection of Alzheimer’s disease (AD) specific tau pathology with conformation-selective anti-tau monoclonal antibody in co-morbid frontotemporal lobar degeneration-tau (FTLD-tau)

Gibbons, G. S., Kim, S., Robinson, J. L., Changolkar, L. N., Irwin, D. J., Shaw, L. M. J., Lee, V. M. ‐., & Trojanowski, J. Q. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0687-5 · Cited by 44

Anti-tau scFvs Targeted to the Cytoplasm or Secretory Pathway Variably Modify Pathology and Neurodegenerative Phenotypes

Goodwin, M. S., Sinyavskaya, O., Burg, F., O’Neal, V., Ceballos‐Diaz, C., Cruz, P. E., Lewis, J. M., Giasson, B. I., Davies, P., Golde, T. E., et al. (2020) · Molecular Therapy · doi:10.1016/j.ymthe.2020.10.007 · Cited by 46

The multifaceted role of WNT signaling in Alzheimer’s disease onset and age-related progression.

Kostes, W. W., & Brafman, D. A. (2023) · Cells · doi:10.3390/cells12081204 · Cited by 43

Conformation-selective tau monoclonal antibodies inhibit tau pathology in primary neurons and a mouse model of Alzheimer’s disease

Gibbons, G. S., Kim, S., Wu, Q., Riddle, D. M., Leight, S. N., Changolkar, L. N., Xu, H. W., Meymand, E. S., O’Reilly, M., Zhang, B., et al. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00404-5 · Cited by 45

Pharmacogenetic neuronal stimulation increases human tau pathology and trans-synaptic spread of tau to distal brain regions in mice

Schultz, M. K., Gentzel, R. C., Usenovic, M., Gretzula, C. A., Ware, C., Parmentier‐Batteur, S., Schachter, J. B., & Zariwala, H. A. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.07.003 · Cited by 45

PAC1 receptor–mediated clearance of tau in postsynaptic compartments attenuates tau pathology in mouse brain

Schaler, A. W., Runyan, A. M., Clelland, C. L. T., Sydney, E. J., Fowler, S. L., Figueroa, H. Y., Shioda, S., Santa‐María, I., Duff, K., & Myeku, N. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.aba7394 · Cited by 41

Chaperoning shape-shifting tau in disease

Ryder, B. D., Wydorski, P. M., Hou, Z., & Joachimiak, Ł. A. (2022) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.12.009 · Cited by 44

Tau–RNA complexes inhibit microtubule polymerization and drive disease-relevant conformation change

McMillan, P. J., Benbow, S. J., Uhrich, R. L., Saxton, A. D., Baum, M., Strovas, T. J., Wheeler, J. M., Baker, J. D., Liachko, N. F., Keene, C. D., et al. (2023) · Brain · doi:10.1093/brain/awad032 · Cited by 43

Aβ Seeding as a Tool to Study Cerebral Amyloidosis and Associated Pathology

Friesen, M., & Meyer‐Luehmann, M. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00233 · Cited by 41

To target Tau pathologies, we must embrace and reconstruct their complexities

Limorenko, G., & Lashuel, H. A. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105536 · Cited by 41

Tau secretion and propagation: Perspectives for potential preventive interventions in Alzheimer's disease and other tauopathies

Annadurai, N., Sanctis, J. B. D., Hajdúch, M., & Das, V. (2021) · Experimental Neurology · doi:10.1016/j.expneurol.2021.113756 · Cited by 41

APOE Antibody Inhibits Aβ‐Associated Tau Seeding and Spreading in a Mouse Model

Gratuze, M., Jiang, H., Wang, C., Xiong, M., Bao, X., & Holtzman, D. M. (2022) · Annals of Neurology · doi:10.1002/ana.26351 · Cited by 41

Seizures are a druggable mechanistic link between TBI and subsequent tauopathy.

Alyenbaawi, H., Kanyo, R., Locskai, L. F., Kamali-Jamil, R., DuVal, M. G., Bai, Q., Wille, H., Burton, E. A., & Allison, W. T. (2021) · eLife · doi:10.7554/elife.58744 · Cited by 40

Regional vulnerability and spreading of hyperphosphorylated tau in seeded mouse brain

Detrez, J. R., Maurin, H., Van Kolen, K., Willems, R., Colombelli, J., Lechat, B., Roucourt, B., Van Leuven, F., Baatout, S., Larsen, P., et al. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.03.010 · Cited by 39

Anti-Tau Monoclonal Antibodies Derived from Soluble and Filamentous Tau Show Diverse Functional Properties in vitro and in vivo

Vandermeeren, M., Borgers, M., Kolen, K. V., Theunis, C., Vasconcelos, B., Bottelbergs, A., Wintmolders, C., Daneels, G., Willems, R., Dockx, K., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180404 · Cited by 40

The ‘a, b, c’s of pretangle tau and their relation to aging and the risk of Alzheimer’s Disease

Harley, C. W., Walling, S. G., Yuan, Q., & Martin, G. M. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.12.010 · Cited by 41

Neuroprotective effects of berberine on recognition memory impairment, oxidative stress, and damage to the purinergic system in rats submitted to intracerebroventricular injection of streptozotocin

de Oliveira, J. S., Abdalla, F. H., Dornelles, G. L., Palma, T. V., Signor, C., Bernardi, J., Baldissarelli, J., Lenz, L. S., de Oliveira, V. A., Schetinger, M. R. C., et al. (2018) · Psychopharmacology · doi:10.1007/s00213-018-5090-6 · Cited by 38

Human tauopathy-derived tau strains determine the substrates recruited for templated amplification

Tarutani, A., Miyata, H., Nonaka, T., Hasegawa, K., Yoshida, M., Saito, Y., Murayama, S., Robinson, A., Mann, D. M. A., Tomita, T., et al. (2021) · Brain · doi:10.1093/brain/awab091 · Cited by 37

PIKfyve activity is required for lysosomal trafficking of tau aggregates and tau seeding

Soares, A. C., Ferreira, A., Mariën, J., Delay, C., Lee, E. B., Trojanowski, J. Q., Moechars, D., Annaert, W. G., & Muynck, L. D. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100636 · Cited by 43

Wolframin is a novel regulator of tau pathology and neurodegeneration

Chen, S., Acosta, D. M., Li, L., Liang, J., Chang, Y., Wang, C., Fitzgerald, J., Morrison, C. T., Goulbourne, C. N., Nakano, Y., et al. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02417-4 · Cited by 40

Infections and immunity: associations with obesity and related metabolic disorders

Ray, A., Bonorden, M. J. L., Pandit, R., Nkhata, K. J., & Bishayee, A. (2023) · Journal of Pathology and Translational Medicine · doi:10.4132/jptm.2022.11.14 · Cited by 37

Sevoflurane anaesthesia induces cognitive impairment in young mice through sequential tau phosphorylation

Liang, F., Li, M., Xu, M., Zhang, Y., Dong, Y., Soriano, S. G., McCann, M. E., Yang, G., & Xie, Z. (2023) · British Journal of Anaesthesia · doi:10.1016/j.bja.2023.06.059 · Cited by 36

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 38

Prion Diseases: A Unique Transmissible Agent or a Model for Neurodegenerative Diseases?

Ritchie, D. L., & Barria, M. A. (2021) · Biomolecules · doi:10.3390/biom11020207 · Cited by 41

Conformational fingerprinting of tau variants and strains by Raman spectroscopy

Devitt, G., Crisford, A., Rice, W., Weismiller, H. A., Fan, Z., Commins, C., Hyman, B. T., Margittai, M., Mahajan, S., & Mudher, A. K. (2021) · RSC Advances · doi:10.1039/d1ra00870f · Cited by 34

Cryo-EM structures of pathogenic fibrils and their impact on neurodegenerative disease research

Todd, T. W., Islam, N. N., Cook, C. N., Caulfield, T. R., & Petrucelli, L. (2024) · Neuron · doi:10.1016/j.neuron.2024.05.012 · Cited by 37

Assessment of the efficacy of different procedures that remove and disassemble alpha-synuclein, tau and A-beta fibrils from laboratory material and surfaces

Fenyi, A., Coens, A., Bellande, T., Melki, R., & Bousset, L. (2018) · Scientific Reports · doi:10.1038/s41598-018-28856-2 · Cited by 34

Relevance of host tau in tau seeding and spreading in tauopathies

Ferrer, I., Zelaya, M. V., Aguiló, M., Carmona, M., López‐González, I., Andrés‐Benito, P., Lidón, L., Gavı́n, R., Garcia‐Esparcia, P., & del Rı́o, J. A. (2019) · Brain Pathology · doi:10.1111/bpa.12778 · Cited by 37

Quantitative propagation of assembled human Tau from Alzheimer's disease brain in microfluidic neuronal cultures

Katsikoudi, A., Ficulle, E., Cavallini, A., Sharman, G. J., Guyot, A., Zagnoni, M., Eastwood, B. J., Hutton, M. L., & Bose, S. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013325 · Cited by 37

Tau Seeding Mouse Models with Patient Brain-Derived Aggregates

Robert, A., Schöll, M., & Vogels, T. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22116132 · Cited by 37

Uncovering specificity of endogenous TAU aggregation in a human iPSC-neuron TAU seeding model

Manos, J. D., Preiss, C. N., Venkat, N., Tamm, J., Reinhardt, P., Kwon, T., Wu, J., Winter, A. D., Jahn, T. R., Yanamandra, K., et al. (2022) · iScience · doi:10.1016/j.isci.2021.103658 · Cited by 36

Latest Perspectives on Alzheimer’s Disease Treatment: The Role of Blood-Brain Barrier and Antioxidant-Based Drug Delivery Systems

Daraban, B. S., Popa, A. S., & Stan, M. S. (2024) · Molecules · doi:10.3390/molecules29174056 · Cited by 37

RNA G-quadruplexes and calcium ions synergistically induce Tau phase transition in vitro

Yabuki, Y., Matsuo, K., Komiya, G., Kudo, K., Hori, K., Ikenoshita, S., Kawata, Y., Mizobata, T., & Shioda, N. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107971 · Cited by 33

Conformational Evolution of Molecular Signatures during Amyloidogenic Protein Aggregation

Devitt, G., Rice, W., Crisford, A., Nandhakumar, I. S., Mudher, A. K., & Mahajan, S. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00451 · Cited by 33

Lymphoid gene expression supports neuroprotective microglia function

Ayata, P., Crowley, J. M., Challman, M. F., Sahasrabuddhe, V., Gratuze, M., Werneburg, S., Ribeiro, D., Hays, E. C., Durán-Laforet, V., Faust, T. E., et al. (2025) · Nature · doi:10.1038/s41586-025-09662-z · Cited by 32

Learning interpretable dynamics of stochastic complex systems from experimental data

Gao, T.-T., Barzel, B., & Yan, G. F. (2024) · Nature Communications · doi:10.1038/s41467-024-50378-x · Cited by 32

Prion-like properties of Tau assemblies

Clavaguera, F., Duyckaerts, C. J., & Haı̈k, S. (2020) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2019.11.022 · Cited by 32

Tau seeds from patients induce progressive supranuclear palsy pathology and symptoms in primates

Darricau, M., Katsinelos, T., Raschellà, F., Milekovic, T., Crochemore, L., Li, Q., Courtine, G., McEwan, W. A., Dehay, B., Bézard, E., et al. (2022) · Brain · doi:10.1093/brain/awac428 · Cited by 32

Reduced progranulin increases tau and α-synuclein inclusions and alters mouse tauopathy phenotypes via glucocerebrosidase

Takahashi, H., Bhagwagar, S. Z., Nies, S. H., Ye, H., Han, X., Chiasseu, M., Wang, G., Mackenzie, I. R., & Strittmatter, S. M. (2024) · Nature Communications · doi:10.1038/s41467-024-45692-3 · Cited by 32

Inhibition of an Alzheimer’s disease–associated form of necroptosis rescues neuronal death in mouse models

Koper, M. J., Moonen, S., Ronisz, A., Ospitalieri, S., Callaerts‐Vegh, Z., T’Syen, D., Rabe, S., Staufenbiel, M., Strooper, B. D., Balusu, S., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.adf5128 · Cited by 32

Discontinued disease-modifying therapies for Alzheimer’s disease: status and future perspectives

Imbimbo, B. P., Lozupone, M., Watling, M., & Panza, F. (2020) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2020.1795127 · Cited by 31

SETD7-mediated monomethylation is enriched on soluble Tau in Alzheimer’s disease

Bichmann, M., Oriol, N. P., Ercan-Herbst, E., Schöndorf, D. C., Ramos, B. G., Schwärzler, V., Neu, M., Schlüter, A., Wang, X., Jin, L., et al. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00468-x · Cited by 31

Genome-wide CRISPR screen identifies protein pathways modulating tau protein levels in neurons

Sanchez, C. G., Acker, C. M., Gray, A. J., Varadarajan, M., Song, C., Cochran, N. R., Paula, S., Lindeman, A., An, S., McAllister, G., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02272-1 · Cited by 37

Development of a novel tau propagation mouse model endogenously expressing 3 and 4 repeat tau isoforms

Hosokawa, M., Masuda‐Suzukake, M., Shitara, H., Shimozawa, A., Suzuki, G., Kondo, H., Nonaka, T., Campbell, W. D., Arai, T., & Hasegawa, M. (2021) · Brain · doi:10.1093/brain/awab289 · Cited by 30

A microtubule stabilizer ameliorates protein pathogenesis and neurodegeneration in mouse models of repetitive traumatic brain injury

Zhao, X., Zeng, W., Xu, H. W., Sun, Z., Hu, Y., Peng, B., McBride, J. D., Duan, J., Deng, J., Zhang, B., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abo6889 · Cited by 31

Preserving cognitive function in patients with Alzheimer's disease: The Alzheimer's disease neuroprotection research initiative (ADNRI)

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Alzheimer’s disease seeded tau forms paired helical filaments yet lacks seeding potential

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Photodynamic studies reveal rapid formation and appreciable turnover of tau inclusions

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