Tau filaments in neurodegenerative diseases

α-Synuclein in Lewy bodies

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Imaging brain amyloid in Alzheimer's disease with Pittsburgh Compound‐B

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Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17

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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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Cryo-EM structures of tau filaments from Alzheimer’s disease

Fitzpatrick, A. W. P., Falcon, B., He, S., Murzin, A. G., Murshudov, G., Garringer, H. J., Crowther, R. A., Ghetti, B., Goedert, M., & Scheres, S. H. W. (2017) · Nature · doi:10.1038/nature23002 · Cited by 2,061

Mutation in the tau gene in familial multiple system tauopathy with presenile dementia

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Tau is a candidate gene for chromosome 17 frontotemporal dementia

Poorkaj, P., Bird, T. D., Wijsman, E., Nemens, E., Garruto, R. M., Anderson, L., Andreadis, A., Wiederholt, W. C., Raskind, M., & Schellenberg, G. D. (1998) · Annals of Neurology · doi:10.1002/ana.410430617 · Cited by 1,374

Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau

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Tau proteins of alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms

Goedert, M., Spillantini, M. G., Cairns, N. J., & Crowther, R. A. (1992) · Neuron · doi:10.1016/0896-6273(92)90117-v · Cited by 1,122

Tau protein liquid–liquid phase separation can initiate tau aggregation

Wegmann, S., Eftekharzadeh, B., Tepper, K., Zoltowska, K. M., Bennett, R. E., Dujardin, S., Laskowski, P. R., MacKenzie, D., Kamath, T., Commins, C., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201798049 · Cited by 1,102

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

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

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 225

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 187

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

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

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

Astroglia and Tau: New Perspectives

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

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 119

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 118

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

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 107

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

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 103

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 84

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 89

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 87

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

Largo‐Barrientos, P., Apóstolo, N., Creemers, E., Callaerts‐Vegh, Z., Swerts, J., Davies, C., McInnes, J., Wierda, K. D. B., Strooper, B. D., Spires‐Jones, T. L., et al. (2021) · Neuron · doi:10.1016/j.neuron.2020.12.016 · Cited by 80

Tau Protein Dysfunction after Brain Ischemia

Pluta, R. M., Ułamek-Kozioł, M., Januszewski, S., & Czuczwar, S. J. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180772 · Cited by 73

Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences

Melková, K., Zapletal, V., Narasimhan, S., Jansen, S., Hritz, J., Škrabana, R., Zweckstetter, M., Jensen, M. R., Blackledge, M. J., & Žídek, L. (2019) · Biomolecules · doi:10.3390/biom9030105 · Cited by 78

Alzheimer’s Disease and Green Tea: Epigallocatechin-3-Gallate as a Modulator of Inflammation and Oxidative Stress

Valverde-Salazar, V., Ruiz-Gabarre, D., & García‐Escudero, V. (2023) · Antioxidants · doi:10.3390/antiox12071460 · Cited by 76

Glycan biomarkers for Alzheimer disease correlate with T‐tau and P‐tau in cerebrospinal fluid in subjective cognitive impairment

Schedin‐Weiss, S., Gaunitz, S., Sui, P., Chen, Q., Haslam, S. M., Blennow, K., Winblad, B. G., Dell, A., & Tjernberg, L. O. (2019) · FEBS Journal · doi:10.1111/febs.15197 · Cited by 55

Dissecting Alzheimer's disease pathogenesis in human 2D and 3D models

Cenini, G., Hebisch, M., Iefremova, V., Flitsch, L. J., Breitkreuz, Y., Tanzi, R. E., Kim, D. Y., Peitz, M., & Brüstle, O. (2020) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2020.103568 · Cited by 60

Distinct populations of highly potent TAU seed conformers in rapidly progressing Alzheimer’s disease

Kim, C., Haldiman, T., Kang, S.-G., Hromadkova, L., Han, Z. Z., Chen, W., Lissemore, F., Lerner, A., de Silva, R., Cohen, M. L., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abg0253 · Cited by 55

Cholesterol determines the cytosolic entry and seeded aggregation of tau

Tuck, B. J., Miller, L. V. C., Katsinelos, T., Smith, A. E., Wilson, E. L., Keeling, S., Cheng, S., Vaysburd, M. J., Knox, C., Tredgett, L., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110776 · Cited by 57

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

Corticobasal degeneration

Saranza, G., Whitwell, J. L., Kovács, G. G., & Lang, A. E. (2019) · International review of neurobiology · doi:10.1016/bs.irn.2019.10.014 · Cited by 52

Biomarker discovery and development for frontotemporal dementia and amyotrophic lateral sclerosis

Katzeff, J. S., Bright, F., Phan, K., Kril, J. J., Ittner, L. M., Kassiou, M., Hodges, J. R., Piguet, O., Kiernan, M. C., Halliday, G. M., et al. (2022) · Brain · doi:10.1093/brain/awac077 · Cited by 48

Tau as a potential therapeutic target for ischemic stroke

Chen, X., & Jiang, H. (2019) · Aging · doi:10.18632/aging.102547 · Cited by 45

Tau and DNA Damage in Neurodegeneration

Colnaghi, L., Rondelli, D., Muzi-Falconi, M., & Sertic, S. (2020) · Brain Sciences · doi:10.3390/brainsci10120946 · Cited by 42

The common marmoset as a model of neurodegeneration

Perez‐Cruz, C., & Rodríguez-Callejas, J. D. (2023) · Trends in Neurosciences · doi:10.1016/j.tins.2023.02.002 · Cited by 39

Review: Fluid biomarkers in the human prion diseases

Thompson, A. G. B., & Mead, S. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.12.003 · Cited by 42

Nuclear Transport Deficits in Tau-Related Neurodegenerative Diseases

Diez, L., & Wegmann, S. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.01056 · Cited by 40

MECP2 and the biology of MECP2 duplication syndrome

D’Mello, S. R. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15331 · Cited by 42

C1 Inhibits Liquid–Liquid Phase Separation and Oligomerization of Tau and Protects Neuroblastoma Cells against Toxic Tau Oligomers

Pradhan, A., Mishra, S., Surolia, A., & Panda, D. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00098 · Cited by 41

Type-I Interferons in Alzheimer's Disease and Other Tauopathies

Sanford, S., & McEwan, W. A. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.949340 · Cited by 42

Secernin-1 is a novel phosphorylated tau binding protein that accumulates in Alzheimer’s disease and not in other tauopathies

Pires, G., McElligott, S., Drusinsky, S., Halliday, G. M., Potier, M., Wısnıewskı, T., & Drummond, E. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0848-6 · Cited by 41

Mercury and Alzheimer’s Disease: Hg(II) Ions Display Specific Binding to the Amyloid-β Peptide and Hinder Its Fibrillization

Wallin, C., Friedemann, M., Sholts, S. B., Noormägi, A., Svantesson, T., Jarvet, J., Roos, P. M., Palumaa, P., Gräslund, A., & Wärmländer, S. K. T. S. (2019) · Biomolecules · doi:10.3390/biom10010044 · Cited by 36

The molecular processes underpinning prion-like spreading and seed amplification in protein aggregation

Meisl, G., Knowles, T. P. J., & Klenerman, D. (2020) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2020.01.010 · Cited by 37

Application of yeast to studying amyloid and prion diseases

Chernoff, Y. O., Grizel, A. V., Rubel, A. A., Zelinsky, A. А., Chandramowlishwaran, P., & Chernova, T. A. (2020) · Advances in genetics · doi:10.1016/bs.adgen.2020.01.002 · Cited by 41

What’s in a Gene? The Outstanding Diversity of MAPT

Ruiz-Gabarre, D., Carnero-Espejo, A., Ávila, J., & García‐Escudero, V. (2022) · Cells · doi:10.3390/cells11050840 · Cited by 39

Gut-brain axis and Alzheimer's disease: Therapeutic interventions and strategies

Singh, H., Chopra, C., Singh, H., Malgotra, V., Wani, A. K., Dhanjal, D. S., Sharma, I., Nepovimová, E., Alomar, S. Y., Singh, R., et al. (2023) · Journal of Functional Foods · doi:10.1016/j.jff.2023.105915 · Cited by 43

Tau Post-Translational Modifications: Potentiators of Selective Vulnerability in Sporadic Alzheimer’s Disease

Carroll, T., Guha, S. K., Nehrke, K. W., & Johnson, G. V. W. (2021) · Biology · doi:10.3390/biology10101047 · Cited by 39

Opportunities and challenges in delivering biologics for Alzheimer’s disease by low-intensity ultrasound

Chen, L., Cruz, E., Oikari, L. E., Padmanabhan, P., Song, J. H., & Götz, J. (2022) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2022.114517 · Cited by 35

Single-domain antibody–based noninvasive in vivo imaging of α-synuclein or tau pathology

Jiang, Y., Lin, Y., Krishnaswamy, S., Pan, R., Wu, Q., Sandusky‐Beltran, L. A., Liu, M., Kuo, M., Kong, X., Congdon, E. E., et al. (2023) · Science Advances · doi:10.1126/sciadv.adf3775 · Cited by 29

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

Potential benefit of manipulating protein quality control systems in neurodegenerative diseases

Luh, L. M., & Bertolotti, A. (2020) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2020.02.009 · Cited by 31

Subtle change of fibrillation condition leads to substantial alteration of recombinant Tau fibril structure

Li, X., Zhang, S., Liu, Z., Tao, Y., Xia, W., Sun, Y., Liu, C., Le, W., Sun, B., & Li, D. (2022) · iScience · doi:10.1016/j.isci.2022.105645 · Cited by 32

Transcellular Spreading of Tau in Tauopathies

Demaegd, K. C., Schymkowitz, J. W. H., & Rousseau, F. (2018) · ChemBioChem · doi:10.1002/cbic.201800288 · Cited by 32

Phosphorylation of tau at a single residue inhibits binding to the E3 ubiquitin ligase, CHIP

Nadel, C. M., Pokhrel, S., Wucherer, K., Oehler, A., Thwin, A. C., Basu, K., Callahan, M. D., Southworth, D. R., Mordes, D. A., Craik, C. S., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52075-1 · Cited by 36

Blood based biomarkers for movement disorders

Morris, H. R. (2022) · Acta Neurologica Scandinavica · doi:10.1111/ane.13700 · Cited by 29

Molecular hydrogen attenuates sepsis-induced cognitive dysfunction through regulation of tau phosphorylation

Qi, B., Song, Y., Chen, C., Zhao, L., Ma, W., Meng, S., Zhuang, X., Lin, H., Liang, J., Cui, Y., et al. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109603 · Cited by 28

The type‐I interferon response potentiates seeded tau aggregation and exacerbates tau pathology

Sanford, S. A. I., Miller, L. V. C., Vaysburd, M., Keeling, S., Tuck, B. J., Clark, J., Neumann, M., Syanda, V., James, L. C., & McEwan, W. A. (2024) · Alzheimer's & Dementia · doi:10.1002/alz.13493 · Cited by 26

Terminal Capping of an Amyloidogenic Tau Fragment Modulates Its Fibrillation Propensity

Arya, S., Ganguly, P., Arsiccio, A., Claud, S. L., Trapp, B., Schonfeld, G. E., Liu, X., Cantrell, K. L., Shea, J., & Bowers, M. T. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c05768 · Cited by 30

Cellular Biology of Tau Diversity and Pathogenic Conformers

Kang, S., Eskandari‐Sedighi, G., Hromádková, L., Safar, J., & Westaway, D. A. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.590199 · Cited by 29

Cerebrospinal fluid: A specific biofluid for the biosensing of Alzheimer's diseases biomarkers

Mirzaie, A., Nasrollahpour, H., Khalilzadeh, B., Jamali, A. A., Spiteri, R. J., Yousefi, H., Işıldak, İ., & Rahbarghazi‬, R. (2023) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2023.117174 · Cited by 28

Stoichiometric 14-3-3ζ binding promotes phospho-Tau microtubule dissociation and reduces aggregation and condensation

Hochmair, J., van den Oetelaar, M. C. M., Ravatt, L. M., Diez, L., Lemmens, L. J. M., Ponce-Lina, R., Sankar, R., Franck, M., Nolte, G., Semenova, E., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-08548-0 · Cited by 26

Cyclosporine A (CsA) prevents synaptic impairment caused by truncated tau by caspase-3

Tapia-Monsalves, C., Olesen, M. A., Villavicencio-Tejo, F., & Quintanilla, R. A. (2023) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2023.103861 · Cited by 24

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

Li, J., Kumar, A., Långström, B., Nordberg, A. K., & Ågren, H. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00437 · Cited by 25

Insights into the Structural Conformations of the Tau Protein in Different Aggregation Status

Pinzi, L., Bisi, N., Sorbi, C., Franchini, S., Tonali, N., & Rastelli, G. (2023) · Molecules · doi:10.3390/molecules28114544 · Cited by 20

Tau repeat regions contain conserved histidine residues that modulate microtubule-binding in response to changes in pH

Charafeddine, R. A., Cortopassi, W. A., Lak, P., Tan, R., McKenney, R. J., Jacobson, M. P., Barber, D. L., & Wittmann, T. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007004 · Cited by 24

Structure of NFT: Biochemical Approach

Hasegawa, M. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_2 · Cited by 22

Targeting tau in Alzheimer’s and beyond: Insights into pathology and therapeutic strategies

Singh, S., Khan, S., Shahid, M., Sardar, M., Hassan, M. I., & Islam, A. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102639 · Cited by 19

Populations of Tau Conformers Drive Prion-like Strain Effects in Alzheimer’s Disease and Related Dementias

Hromádková, L., Siddiqi, M. K., Liu, H., & Safar, J. (2022) · Cells · doi:10.3390/cells11192997 · Cited by 19

Alzheimer proteopathic tau seeds are biochemically a forme fruste of mature paired helical filaments

Kumar, M., Quittot, N., Dujardin, S., Schlaffner, C. N., Viodé, A., Wiedmer, A. E., Beerepoot, P., Chun, J. E., Glynn, C. A., Fernandes, A. R., et al. (2024) · Brain · doi:10.1093/brain/awad378 · Cited by 20

Blood Based Biomarkers of Central Nervous System Involvement in Wilson’s Disease

Antos, A., Członkowska, A., Bembenek, J. P., Skowrońska, M., Kurkowska‐Jastrzębska, I., & Litwin, T. (2023) · Diagnostics · doi:10.3390/diagnostics13091554 · Cited by 18

Somatic Mutations and Alzheimer’s Disease

Downey, J., Lam, J. C. K., Li, V. O. K., & Gozes, I. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220643 · Cited by 18

Systemic Immune Dyshomeostasis Model and Pathways in Alzheimer’s Disease

Talwar, P., Kushwaha, S. S., Gupta, R., & Agarwal, R. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00290 · Cited by 18

Synthesis and Assessment of Novel Probes for Imaging Tau Pathology in Transgenic Mouse and Rat Models

McMurray, L., Macdonald, J. A., Ramakrishnan, N. K., Zhao, Y., Williamson, D. W., Tietz, O., Zhou, X., Kealey, S., Fagan, S. G., Smolek, T., et al. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00790 · Cited by 17

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

Krause, K., Wulf, M., Sommer, P., Barkovits, K., Vorgerd, M., Marcus, K., & Eggers, B. (2021) · Diagnostics · doi:10.3390/diagnostics11091522 · Cited by 17

Tau, RNA, and RNA-Binding Proteins: Complex Interactions in Health and Neurodegenerative Diseases

Lester, E., & Parker, R. (2023) · The Neuroscientist · doi:10.1177/10738584231154551 · Cited by 16

Deconstructing Alzheimer’s Disease: How to Bridge the Gap between Experimental Models and the Human Pathology?

Vignon, A., Salvador-Prince, L., Lehmann, S., Perrier, V., & Torrent, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168769 · Cited by 17

Novel aspects of the phosphorylation and structure of pathological tau: implications for tauopathy biomarkers

Kimura, T., Sato, H., Kano, M., Tatsumi, L., & Tomita, T. (2023) · FEBS Open Bio · doi:10.1002/2211-5463.13667 · Cited by 15

Directly Reprogrammed Neurons Express MAPT and APP Splice Variants Pertinent to Ageing and Neurodegeneration

Habekost, M., Qvist, P., Denham, M., Holm, I. E., & Jørgensen, A. L. (2021) · Molecular Neurobiology · doi:10.1007/s12035-020-02258-w · Cited by 14

Novel Phosphorylation-State Specific Antibodies Reveal Differential Deposition of Ser26 Phosphorylated Aβ Species in a Mouse Model of Alzheimer’s Disease

Kumar, S., Kapadia, A., Theil, S., Joshi, P., Riffel, F., Heneka, M. T., & Walter, J. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.619639 · Cited by 16

Hyperphosphorylated Tau Relates to Improved Cognitive Performance and Reduced Hippocampal Excitability in the Young rTg4510 Mouse Model of Tauopathy

Xolalpa-Cueva, L., García-Carlos, C. A., Villaseñor-Zepeda, R., Orta-Salazar, E., Díaz-Miranda, S. Y., Peña‐Ortega, F., Perry, G., & Mondragón‐Rodríguez, S. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-215186 · Cited by 14

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

Suire, C. N., & Leissring, M. A. (2021) · Journal of Experimental Neurology · doi:10.33696/neurol.2.029 · Cited by 15

Oligodendrocyte Dysfunction in Tauopathy: A Less Explored Area in Tau-Mediated Neurodegeneration

Majumder, M., & Dutta, D. (2024) · Cells · doi:10.3390/cells13131112 · Cited by 14

Intron retention as a productive mechanism in human MAPT: RNA species generated by retention of intron 3

Ruiz-Gabarre, D., Vallés‐Saiz, L., Carnero-Espejo, A., Ferrer, I., Hernández, F., García‐Escudero, R., Ávila, J., & García‐Escudero, V. (2024) · EBioMedicine · doi:10.1016/j.ebiom.2023.104953 · Cited by 11

Tau biomarkers for neurodegenerative diseases: Current state and perspectives

Vacchi, E., Ruíz‐Barrio, I., & Melli, G. (2025) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2025.107772 · Cited by 11

Microtubule and auditory function – an underestimated connection

Bieniussa, L., Jain, I., Bosch, M., Juergens, L., Hagen, R., Janke, C., & ten Rak, K. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.02.004 · Cited by 11

Structural characterization of monoclonal antibodies targeting C-terminal Ser404 region of phosphorylated tau protein

Chukwu, J. E., Congdon, E. E., Sigurdsson, E. M., & Kong, X. (2019) · mAbs · doi:10.1080/19420862.2019.1574530 · Cited by 12

Neuronal Trafficking of the Amyloid Precursor Protein—What Do We Really Know?

Lin, T., Tjernberg, L. O., & Schedin‐Weiss, S. (2021) · Biomedicines · doi:10.3390/biomedicines9070801 · Cited by 13

On the Microtubule-Stabilizing Properties of a Tau Oligopeptide

Jiménez, V. A. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00955 · Cited by 9

The Diagnostic Potential of Amyloidogenic Proteins

Jin, Y., Vadukul, D. M., Gialama, D., Ge, Y., Thrush, R. J., White, J. T., & Aprile, F. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22084128 · Cited by 9

Short-chain polyphosphates induce tau fibrillation and neurotoxicity in human iPSC-derived retinal neurons

(2025) · doi:10.1038/s41419-025-07662-5 · Cited by 8

High-Dose Photodynamic Therapy Increases Tau Protein Signals in Drosophila

Willis, J. A., Cheburkanov, V. D., & Yakovlev, V. V. (2023) · IEEE Journal of Selected Topics in Quantum Electronics · doi:10.1109/jstqe.2023.3270403 · Cited by 9

Regulation of Neurodegeneration-associated Protein Fragments by the N-degron Pathways

Eldeeb, M. A., Ragheb, M. A., Soliman, M. H., & Fahlman, R. P. (2022) · Neurotoxicity Research · doi:10.1007/s12640-021-00396-0 · Cited by 9

Site-Specific C-Terminal Fluorescent Labeling of Tau Protein

Bryan, L. C., Awasthi, S., Li, Y., Nirmalraj, P. N., Balog, S., Yang, J., & Mayer, M. (2022) · ACS Omega · doi:10.1021/acsomega.2c06139 · Cited by 7

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

Taguchi, Y., Otaki, H., & Nishida, N. (2019) · Viruses · doi:10.3390/v11020110 · Cited by 7

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

Berntsson, E., Paul, S., Vosough, F., Sholts, S. B., Jarvet, J., Roos, P. M., Barth, A., Gräslund, A., & Wärmländer, S. K. T. S. (2021) · Acta Biochimica Polonica · doi:10.18388/abp.2020_5493 · Cited by 7

FibrilPaint to determine the length of Tau amyloids in fluids

Pedrola, J. A., Dekker, F. A., Garfagnini, T., Mayer, G., Koopman, M. B., Bergmeijer, M., Heesink, G., Rots, I., Claessens, M. M. A. E., Förster, F. G., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2502847122 · Cited by 6

Molecular dynamics of amyloid-β transport in Alzheimer's disease: Exploring therapeutic plasma exchange with albumin replacement – Current insights and future perspectives

Mondal, R., Deb, S., Shome, G., Sarkar, V., Lahiri, D., Datta, S. S., & Benito‐León, J. (2024) · Neurología · doi:10.1016/j.nrl.2023.11.005 · Cited by 6

NMR Relaxation Experiments Probe Monomer–Fibril Interaction and Identify Critical Interacting Residues Responsible for Distinct Tau Fibril Morphologies

Hassan, M. S. O., Vahid, A. A., Sahayaraj, A. E., Viswanathan, R., & Vijayan, V. (2023) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.3c00912 · Cited by 5

Adding the Topographical Information from Tau-PET to the A/T/(N) Framework: Steps Towards Staging AD in Vivo

Therriault, J., Gauthier, S. G., & Rosa‐Neto, P. (2023) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2023.52 · Cited by 4

Synaptic Plasticity in the Hippocampus

Bliss, T., Collingridge, G. L., Cooke, S. F., Georgiou, J., & Morris, R. (2025) · Oxford University Press eBooks · doi:10.1093/med/9780190065324.003.0010 · Cited by 4

Structure–Activity Relationships and Evaluation of 2-(Heteroaryl-cycloalkyl)-1H-indoles as Tauopathy Positron Emission Tomography Radiotracers

Stehouwer, J. S., Huang, G., Guarino, D. S., Debnath, M. L., Polu, A., Geib, S. J., Lopresti, B. J., Ikonomović, M. D., Mason, N. S., Mach, R. H., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02988 · Cited by 4

Passaging Human Tauopathy Patient Samples in Cells Generates Heterogeneous Fibrils with a Subpopulation Adopting Disease FoldsPreprint

Zeng, 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

Inhibiting Disulfide Bonding in Truncated Tau297–391 Results in Enhanced Self-Assembly of Tau into Seed-Competent Assemblies

Oakley, S. S., Marshall, K. E., Meisl, G., Copsey, A. C., Maina, M. B., Milton, R., Vorley, T., Storey, J. M. D., Harrington, C. R., Wischik, C. M., et al. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00639 · Cited by 3

Molecular dynamics of amyloid-β transport in Alzheimer's disease: Exploring therapeutic plasma exchange with albumin replacement – Current insights and future perspectives

Mondal, R., Deb, S., Shome, G., Sarkar, V., Lahiri, D., Datta, S. S., & Benito‐León, J. (2025) · Neurología (English Edition) · doi:10.1016/j.nrleng.2025.03.008 · Cited by 3

Neurodegeneration and the Ordered Assembly of Tau

Goedert, M. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811304-2.00004-3 · Cited by 3

Tau Protein and Neurodegeneratio

Goedert, M. (2025) · Alzheimer s & Dementia · doi:10.1002/alz70855_099770

Tau Protein and Neurodegeneration

Goedert, M. (2025) · Alzheimer s & Dementia · doi:10.1002/alz70855_098415 · Cited by 1

Tau and neurodegeneration

Goedert, M., Crowther, R. A., Scheres, S. H. W., & Spillantini, M. G. (2023) · Cytoskeleton · doi:10.1002/cm.21812 · Cited by 64

Ordered Assembly of Tau Protein and Neurodegeneration

Goedert, M., & Spillantini, M. G. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_1 · Cited by 74