Prion-like Properties of Tau Protein: The Importance of Extracellular Tau as a Therapeutic Target

Neuropathological stageing of Alzheimer-related changes.

Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123

2013 Alzheimer's disease facts and figures

Thies, W. H., & Bleiler, L. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.02.003 · Cited by 3,372

Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse

Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160

TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis

Sreedharan, J., Blair, I. P., Tripathi, V. B., Hu, X., Vance, C., Rogelj, B., Ackerley, S., Durnall, J. C., Williams, K. L., Buratti, E., et al. (2008) · Science · doi:10.1126/science.1154584 · Cited by 2,630

Neurodegenerative Diseases Target Large-Scale Human Brain Networks

Seeley, W. W., Crawford, R. K., Zhou, J., Miller, B. L., & Greicius, M. D. (2009) · Neuron · doi:10.1016/j.neuron.2009.03.024 · Cited by 2,350

Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model

Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892

Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation

Li, J.-Y., Englund, E., Holton, J. L., Soulet, D., Hagell, P., Lees, A. J., Lashley, T., Quinn, N. P., Rehncrona, S., Björklund, A., et al. (2008) · Nature Medicine · doi:10.1038/nm1746 · Cited by 1,845

Lewy body–like pathology in long-term embryonic nigral transplants in Parkinson's disease

Kordower, J. H., Chu, Y., Hauser, R. A., Freeman, T. B., & Olanow, C. W. (2008) · Nature Medicine · doi:10.1038/nm1747 · Cited by 1,722

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

Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687

Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death

Volpicelli-Daley, L. A., Luk, K. C., Patel, T. P., Tanik, S. A., Riddle, D. M., Stieber, A., Meaney, D. F., Trojanowski, J. Q., & Lee, V. M.-Y. (2011) · Neuron · doi:10.1016/j.neuron.2011.08.033 · Cited by 1,569

Reassessment of Neuronal Tau Distribution in Adult Human Brain and Implications for Tau Pathobiology

Paterno, G., Bell, B. M., Gorion, K.-M. M., Prokop, S., & Giasson, B. I. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01394-9 · Cited by 30

Cognitive Enhancers (Nootropics). Part 3: Drugs Interacting with Targets other than Receptors or Enzymes. Disease-modifying Drugs

Froestl, W., Pfeifer, A., & Muhs, A. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-121729 · Cited by 27

Alzheimer’s Disease: From Amyloid to Autoimmune Hypothesis

Arshavsky, Y. I. (2020) · The Neuroscientist · doi:10.1177/1073858420908189 · Cited by 28

The Distance between N and C Termini of Tau and of FTDP-17 Mutants Is Modulated by Microtubule Interactions in Living Cells

Primio, C. D., Quercioli, V., Siano, G., Rovere, M., Kováčech, B., Novák, M., & Cattaneo, A. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00210 · Cited by 30

Tau in the brain interstitial fluid is fragmented and seeding–competent

Barini, E., Plotzky, G., Mordashova, Y., Hoppe, J., Rodriguez-Correa, E., Julier, S., Prieult, F. L., Mairhofer, I., Mezler, M., Biesinger, S., et al. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.09.013 · Cited by 28

Astrogliopathy in Tauopathies

Ferrer, I. (2018) · Neuroglia · doi:10.3390/neuroglia1010010 · Cited by 27

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

Promising therapies for the treatment of frontotemporal dementia clinical phenotypes: from symptomatic to disease-modifying drugs

Logroscino, G., Imbimbo, B. P., Lozupone, M., Sardone, R., Capozzo, R., Battista, P., Zecca, C., Dibello, V., Giannelli, G., Bellomo, A., et al. (2019) · Expert Opinion on Pharmacotherapy · doi:10.1080/14656566.2019.1598377 · Cited by 30

Monoclonal antibody Y01 prevents tauopathy progression induced by lysine 280–acetylated tau in cell and mouse models

Song, H.-L., Kim, N.-Y., Park, J., Kim, M. I., Jeon, Y.-N., Lee, S.-J., Cho, K., Shim, Y.-L., Lee, K.-H., Mun, Y.-S., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci156537 · Cited by 26

Heparan Sulfate Proteoglycans (HSPGs) Serve as the Mediator Between Monomeric Tau and Its Subsequent Intracellular ERK1/2 Pathway Activation

Song, L., Oseid, D. E., Wells, E. A., Coaston, T. N., & Robinson, A. S. (2022) · Journal of Molecular Neuroscience · doi:10.1007/s12031-021-01943-2 · Cited by 28

Cerebrospinal Fluid Biomarkers in Alzheimer’s Disease—From Brain Starch to Bench and Bedside

Pawlowski, M., Meuth, S., & Duning, T. (2017) · Diagnostics · doi:10.3390/diagnostics7030042 · Cited by 25

Tau mRNA 3′UTR-to-CDS ratio is increased in Alzheimer disease

García‐Escudero, V., Gargini, R., Martín-Maestro, P., García, E., García‐Escudero, R., & Ávila, J. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.07.007 · Cited by 25

Mechanistic and Structural Origins of the Asymmetric Barrier to Prion-like Cross-Seeding between Tau-3R and Tau-4R

Kumar, H., & Udgaonkar, J. B. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.09.010 · Cited by 25

Tau Interacting Proteins: Gaining Insight into the Roles of Tau in Health and Disease

Stancu, I., Ferraiolo, M., Terwel, D., & Dewachter, I. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_13 · Cited by 23

The Interplay between GSK3β and Tau Ser262 Phosphorylation during the Progression of Tau Pathology

Song, L., Oseid, D. E., Wells, E. A., & Robinson, A. S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911610 · Cited by 25

Molecular drug targets and therapies for Alzheimer’s disease

Singh, D. B., Gupta, M., Kesharwani, R. K., Sagar, M., Dwivedi, S., & Misra, K. (2014) · Translational Neuroscience · doi:10.2478/s13380-014-0222-x · Cited by 25

Mosaic Somatic Gene Recombination as a Potentially Unifying Hypothesis for Alzheimer’s Disease

Kaeser, G. E., & Chun, J. J. M. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00390 · Cited by 23

Clinical development of passive tau-based immunotherapeutics for treating primary and secondary tauopathies

Panza, F., Dibello, V., Sardone, R., Castellana, F., Zupo, R., Lampignano, L., Bortone, I., Stallone, R., Cirillo, N., Damiani, C., et al. (2023) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2023.2233892 · Cited by 22

Preclinical, phase I, and phase II investigational clinical trials for treatment of progressive supranuclear palsy

Shoeibi, A., Olfati, N., & Litvan, I. (2018) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2018.1460356 · Cited by 23

Self‐Therapeutic Nanoparticle That Alters Tau Protein and Ameliorates Tauopathy Toward a Functional Nanomedicine to Tackle Alzheimer's

Vimal, S. K., Zuo, H., Wang, Z., Wang, H., Long, Z., & Bhattacharyya, S. (2020) · Small · doi:10.1002/smll.201906861 · Cited by 22

Peripheral Pathways to Neurovascular Unit Dysfunction, Cognitive Impairment, and Alzheimer’s Disease

Nelson, A. R. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.858429 · Cited by 24

Glymphatic system impairment in corticobasal syndrome: diffusion tensor image analysis along the perivascular space (DTI-ALPS)

Saito, Y., Kamagata, K., Andica, C., Uchida, W., Takabayashi, K., Yoshida, S., Nakaya, M., Tanaka, Y., Kamio, S., Sato, K., et al. (2023) · Japanese Journal of Radiology · doi:10.1007/s11604-023-01454-7 · Cited by 20

Endocytic pathways of pathogenic protein aggregates in neurodegenerative diseases

Hivare, P., Mujmer, K., Swarup, G., Gupta, S. K., & Bhatia, D. D. (2023) · Traffic · doi:10.1111/tra.12906 · Cited by 24

The 3-O sulfation of heparan sulfate proteoglycans contributes to the cellular internalization of tau aggregates

Ferreira, A., Royaux, I. E., Liu, J., Wang, Z., Su, G., Moechars, D., Callewaert, N., & Muynck, L. D. (2022) · BMC Molecular and Cell Biology · doi:10.1186/s12860-022-00462-1 · Cited by 24

Function and regulation of cis P‐tau in the pathogenesis and treatment of conventional and nonconventional tauopathies

Wang, R., Lu, K. P., & Zhou, X. Z. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15909 · Cited by 20

Disease-modifying therapies for tauopathies: agents in the pipeline

Panza, F., Imbimbo, B. P., Lozupone, M., Greco, A., Seripa, D., Logroscino, G., Daniele, A., & Colosimo, C. (2019) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2019.1606715 · Cited by 20

Dynamics of Internalization and Intracellular Interaction of Tau Antibodies and Human Pathological Tau Protein in a Human Neuron-Like Model

Shamir, D. B., Deng, Y., Wu, Q., Modak, S., Congdon, E. E., & Sigurdsson, E. M. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.602292 · Cited by 19

Passive Immunotherapy Targeting Tau Oligomeric Strains Reverses Tauopathy Phenotypes in Aged Human-Tau Mice in a Mouse Model-Specific Manner

Bittar, A., Al-Lahham, R., Bhatt, N., Moore, K., Montalbano, M., Jerez, C., Fung, L., McAllen, S., Ellsworth, A., & Kayed, R. (2022) · Journal of Alzheimer's Disease · doi:10.3233/jad-220518 · Cited by 18

Inflammasome links traumatic brain injury, chronic traumatic encephalopathy, and Alzheimer’s disease

Seplovich, G., Bouchi, Y., Vaccari, J. P. D. R., Pareja, J. C. M., Reisner, A., Blackwell, L. S., Mechref, Y. S., Wang, K., Tyndall, J. A., Tharakan, B., et al. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-00107 · Cited by 21

The development of peptide- and oligonucleotide-based drugs to prevent the formation of abnormal tau in tauopathies

Lozupone, M., Dibello, V., Sardone, R., Castellana, F., Zupo, R., Lampignano, L., Bortone, I., Stallone, R., Altamura, M., Bellomo, A., et al. (2023) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2023.2200245 · Cited by 21

Heparan sulfate proteoglycans and heparanases in Alzheimer's disease: current outlook and potential therapeutic targets

Fernández‐Vega, I., Lorente-Gea, L., García, B., Martín, C., & Quirós, L. M. (2017) · Neural Regeneration Research · doi:10.4103/1673-5374.208571 · Cited by 18

Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion

Espargaró, A., Busquets, M. A., Estelrich, J., & Sabaté, R. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00029 · Cited by 18

Passive tau-based immunotherapy for tauopathies

Panza, F., Solfrizzi, V., Daniele, A., & Lozupone, M. (2023) · Handbook of clinical neurology · doi:10.1016/b978-0-323-98817-9.00029-6 · Cited by 18

Neuro‐HIV —New insights into pathogenesis and emerging therapeutic targets

Sviridov, D., & Bukrinsky, M. (2023) · The FASEB Journal · doi:10.1096/fj.202301239rr · Cited by 17

Large-scale network analysis of the cerebrospinal fluid proteome identifies molecular signatures of frontotemporal lobar degeneration

Saloner, R., Staffaroni, A. M., Dammer, E. B., Johnson, E. C. B., Paolillo, E. W., Wise, A. B., Heuer, H. W., Forsberg, L. K., Lario‐Lago, A., Webb, J. D., et al. (2025) · Nature Aging · doi:10.1038/s43587-025-00878-2 · Cited by 21

Prion-Like Propagation Mechanisms in Tauopathies and Traumatic Brain Injury: Challenges and Prospects

Alyenbaawi, H., Allison, W. T., & Mok, S. (2020) · Biomolecules · doi:10.3390/biom10111487 · Cited by 20

Dose-dependent phosphorylation of endogenous Tau by intermittent hypoxia in rat brain

Marciante, A. B., Howard, J. C., Kelly, M. N., Santiago‐Moreno, J., Allen, L. L., Gonzalez‐Rothi, E. J., & Mitchell, G. S. (2022) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00332.2022 · Cited by 15

Extracellular Tau Oligomers Damage the Axon Initial Segment

Best, M. N., Lim, Y., Ferenc, N. N., Kim, N., Min, L. Y., Wang, D. B., Sharifi, K., Wasserman, A. E., McTavish, S. A., Siller, K. H., et al. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-221284 · Cited by 15

Impact of Phosphorylation and Pseudophosphorylation on the Early Stages of Aggregation of the Microtubule-Associated Protein Tau

Prokopovich, D., Whittaker, J. W., Muthee, M. M., Ahmed, A., & Larini, L. (2017) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.7b00194 · Cited by 15

Cell-free amplification of prions: Where do we stand?

Cazzaniga, F. A., Luca, C. M. G. D., Bistaffa, E., Consonni, A., Legname, G., Giaccone, G., & Moda, F. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.08.005 · Cited by 14

Immunization targeting diseased proteins in synucleinopathy and tauopathy: insights from clinical trials

Zhan, X., Wen, G., Wu, X., & Li, J. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00490-9 · Cited by 14

ApoE-calypse tau: ApoE–tau synergy in Alzheimer’s disease

Lennol, M. P., Bordier, C., Kamelher, L., Ulrich, J. D., Holtzman, D. M., & Gratuze, M. (2025) · The Journal of Experimental Medicine · doi:10.1084/jem.20250965 · Cited by 14

Targeted clearance of extracellular Tau using aptamer-armed monocytes alleviates neuroinflammation in mice with Alzheimer’s disease

Zhuo, Y., Yao, L., Zhu, Y., Wen, N., Zou, G.-J., Lu, H., Pei, X., Zhang, Y., Zhang, Q., Wang, X., et al. (2025) · Nature Biomedical Engineering · doi:10.1038/s41551-025-01525-2 · Cited by 15

Role of posttranslational modifications in memory and cognitive impairments caused by neonatal sevoflurane exposure

Jiang, Y., Zhou, Y. X., Tan, S., Xu, C., & Ma, J. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1113345 · Cited by 11

The structural line between prion and “prion-like”: Insights from prion protein and tau

Glynn, C. A., Rodríguez, J. A., & Hyman, B. T. (2024) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2024.102857 · Cited by 13

Quantitative detection of grey and white matter amyloid pathology using a combination of K114 and CRANAD-3 fluorescence

Stepanchuk, A. A., Barber, P. A., Lashley, T., Joseph, J. T., & Stys, P. K. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105540 · Cited by 13

A feature analysis of lower solubility proteins in three eukaryotic systems

Albu, R. F., Chan, G. T., Zhu, M., Wong, E. T. C., Taghizadeh, F., Hu, X., Mehran, A. E., Johnson, J. D., Gsponer, J. A., & Mayor, T. (2014) · Journal of Proteomics · doi:10.1016/j.jprot.2014.10.011 · Cited by 14

Sequence-dependent abnormal aggregation of human Tau fragment in an inducible cell model

Liu, X., Hu, J.-Y., Hu, M.-Y., Zhang, Y., Hong, Z., Cheng, X., Chen, J., Pang, D., & Liang, Y. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.04.015 · Cited by 13

Progress in the treatment of Parkinson-Plus syndromes

Olfati, N., Shoeibi, A., & Litvan, I. (2018) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2018.10.006 · Cited by 16

Mechanistic approaches to understand the prion-like propagation of aggregates of the human tau protein

Kumar, H., & Udgaonkar, J. B. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.04.004 · Cited by 12

Resting-State Functional MRI

Greicius, M. D. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-800105-9.00016-0 · Cited by 14

Development of preclinical diagnosis and preventive treatment of neurodegenerative diseases

Ugrumov, M. V. (2015) · S S Korsakov Journal of Neurology and Psychiatry · doi:10.17116/jnevro20151151114-14 · Cited by 11

Development of tau-directed Small Molecule Modulators for Alzheimer’s Disease: a Recent Patent Review (2014–2018)

Lee, H. E., Lim, D., Lee, J. Y., Lim, S. M., & Pae, A. N. (2019) · Pharmaceutical Patent Analyst · doi:10.4155/ppa-2019-0003 · Cited by 11

Inefficient induction and spread of seeded tau pathology in P301L mouse model of tauopathy suggests inherent physiological barriers to transmission

Chakrabarty, P., Hudson, V. J., Sacino, A. N., Brooks, M., D’Alton, S., Lewis, J. M., Golde, T. E., & Giasson, B. I. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1444-x · Cited by 10

The Way of Tau: Secretion and Synaptic Dysfunction

Dubal, D. B. (2018) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2018.05.006 · Cited by 10

Amyloid binding and beyond: a new approach for Alzheimer's disease drug discovery targeting Aβo–PrP C binding and downstream pathways

Grayson, J. D., Baumgartner, M. P., Souza, C. D. S., Dawes, S. J., Idrissi, I. G. E., Louth, J. C., Stimpson, S., Mead, E., Dunbar, C., Wolak, J., et al. (2021) · Chemical Science · doi:10.1039/d0sc04769d · Cited by 10

Tau-based therapies for Alzheimer’s disease: Promising novel neuroprotective approaches

Sayas, C. L. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814037-6.00005-7 · Cited by 9

Neurophysiological effects of human-derived pathological tau conformers in the APPKM670/671NL.PS1/L166P amyloid mouse model of Alzheimer’s disease

Tok, S., Maurin, H., Delay, C., Crauwels, D., Manyakov, N. V., der Elst, W. V., Moechars, D., & Drinkenburg, W. H. I. M. (2022) · Scientific Reports · doi:10.1038/s41598-022-11582-1 · Cited by 7

Remodeling Tau and Prion Proteins Using Nanochaperons

Bhattacharyya, S., Kim, K., & Teizer, W. (2017) · Advanced Biosystems · doi:10.1002/adbi.201700108 · Cited by 7

Acetylation Mimetic and Null Mutations Within the Filament Core of P301L Tau Have Varied Effects on Susceptibility to Seeding and Aggregation

Smith, E. D., Torrellas, J., McKenna, R., Vo, Q., Mietzsch, M., Borchelt, D., Prokop, S., & Chakrabarty, P. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70221 · Cited by 6

Cell-based Assay to Study Antibody-mediated Tau Clearance by Microglia

Marco, D. D., Taggenbrock, R. L. R. E., Crespo, R., Koudstaal, W., Ramsburg, E. A., & Apetri, A. C. (2018) · Journal of Visualized Experiments · doi:10.3791/58576 · Cited by 6

Polypeptides derived from α-Synuclein binding partners to prevent α-Synuclein fibrils interaction with and take-up by cells

Monsellier, É., Bendifallah, M., Redeker, V., & Melki, R. (2020) · PLoS ONE · doi:10.1371/journal.pone.0237328 · Cited by 5

Live Imaging of Pathological Tau Protein and Tau Antibodies in a Neuron-Like Cellular Model

Shamir, D. B., Deng, Y., & Sigurdsson, E. M. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7816-8_22 · Cited by 5

How can we manage progressive supranuclear palsy syndrome with pharmacotherapy?

Lozupone, M., Dibello, V., Daniele, A., Solfrizzi, V., Resta, E., & Panza, F. (2024) · Expert Opinion on Pharmacotherapy · doi:10.1080/14656566.2024.2345734 · Cited by 5

Conformational dynamics of Tau in the cell quantified by an intramolecular FRET biosensor in physiological and pathological contextPreprint

Primio, C. D., Quercioli, V., Siano, G., Kováčech, B., Novák, M., & Cattaneo, A. (2016) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/041756 · Cited by 4

Brain and immune system: KURU disease a toxicological process?

Luisetto, M., Nili-Ahmadabadi, B., Mashori, G. R., Yesvi, A., Sahu, R. K., Nasser, H., Luca, C., & Khan, F. A. (2018) · Journal of Neuroscience and Neurological Disorders · doi:10.29328/journal.jnnd.1001010 · Cited by 3

The effects of social environment on AD-related pathology in hAPP-J20 mice and tau-P301L mice

Lanooij, S. D., Drinkenburg, W. H. I. M., Eisel, U. L. M., van der Zee, E. A., & Kas, M. J. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106309 · Cited by 4

A role for the autophagy receptor NBR1 in the degradation of tau aggregates

Neu, M., Parfentev, I., Potts, G. K., Stöberl, N., Korffmann, J., Striebinger, A., Geist, D., Papageorgiou, D. N., Tarhonskaya, H., McKitterick, N., et al. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.107060 · Cited by 4

A coupled mathematical and numerical model for protein spreading and tissue atrophy applied to Alzheimer’s disease

Pederzoli, V., Corti, M., Riccobelli, D., & Antonietti, P. F. (2025) · Computer Methods in Applied Mechanics and Engineering · doi:10.1016/j.cma.2025.118118 · Cited by 2

Molecular and environmental drivers of tau post-translational modifications and tau pathology

Price, T. M., Tucker, A. E., & Funk, K. E. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103223 · Cited by 2

Heparan Sulfate Proteoglycans: Master Regulators of Cellular Signaling, Tissue Development, and Neural Function

Melrose, J. (2026) · Journal of Neuroscience Research · doi:10.1002/jnr.70151 · Cited by 2

A Phase 1 Study of the Pharmacokinetics, Safety, and Tolerability of Posdinemab (JNJ‐63733657) in Healthy Chinese Adults

Wang, F., Liu, J., Bai, D., Li, L., Fedgchin, M. M., Henley, D. B., Li, H., & Zhang, F. (2025) · The Journal of Clinical Pharmacology · doi:10.1002/jcph.70116 · Cited by 2

Prion Protein and Genetic Susceptibility to Diseases Caused by Its Misfolding

Carlson, G. A. (2017) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.06.007 · Cited by 2

Preclinical models of Alzheimer’s disease for identification and preclinical validation of therapeutic targets: from fine-tuning strategies for validated targets to new venues for therapy

Vasconcelos, B., Bird, M., Stancu, I., Terwel, D., & Dewachter, I. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805120-7.00006-3 · Cited by 2

Glymphatic Inhibition Exacerbates Tau Propagation in an Alzheimer’s Disease ModelPreprint

Lopes, D. M., Wells, J. A., Ma, D., Wallis, L., Park, D., Llewellyn, S. K., Ahmed, Z., Lythgoe, M. F., & Harrison, I. F. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.25.554601 · Cited by 2

PAR-1 in Alzheimer’s Disease: Pathophysiological Insights and Mechanistic Perspectives

Neha, Mandal, S., Sharma, V., Dhindsa, J., & Aran, K. R. (2026) · Current Medical Science · doi:10.1007/s11596-026-00175-y · Cited by 1

Extracellular Diffusion of Tau Protein Is Slower Than Similar‐Sized IgG Protein and Dextran Polysaccharide in Entorhinal Cortex but Not in Prefrontal Cortex

Rubin, M., Naik‐Talapadatur, A., Majerová, P., Hrabě, J., Kováč, A., & Hrabětová, S. (2026) · European Journal of Neuroscience · doi:10.1111/ejn.70460 · Cited by 1

Tau conformation, distribution and PET imaging correlations in progressive supranuclear palsy

Dong, C., Ma, J., Qiao, H., Tamagnan, G. D., Chan, P., & Liu, S. (2026) · Translational Neurodegeneration · doi:10.1186/s40035-026-00545-5 · Cited by 2

Tau Phosphorylation as a Therapeutic Target in Alzheimer’s Disease

Medina, M., & Ávila, J. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00012-5 · Cited by 1

Heparan sulfate proteoglycans as possible diagnostic molecular tools with therapeutic potential in Alzheimer´s disease

Fernández‐Vega, I., Lorente-Gea, L., Martín, C., & Quirós, L. M. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.301056 · Cited by 1

Prion Diseases of Humans

Ritchie, D. L., Peden, A., Urwin, P. J., & Ironside, J. W. (2015) · Wiley eBooks · doi:10.1002/9780470015902.a0000426 · Cited by 1

Inhibition of Alzheimer’s type toxic aggregates of tau with fungal secondary metabolites

Paranjape, S. R. (2015) · KU ScholarWorks (University of Kansas)

Engineering antibody therapeutics and cell culture models for neurodegenerative diseases

McHugh, K. P. (2016) · Library, Museums and Press - UDSpace (University of Delaware) · doi:10.58088/9ar9-m703

PRECLINICAL DIAGNOSIS OF NEURODEGENERATIVE DISEASES: PAST, PRESENT AND FUTURE

Киркина, Н., Kirkina, N., & Golovanov, A. V. (2018) · Clinical Medicine and Pharmacology · doi:10.12737/article_5b5ade3b251746.79381949

Intracellular Responses of Glial Cells To Monomeric Tau Protein Are Closely Mediated By Heparan Sulfate Proteoglycans (HSPGs)Preprint

Song, L., Oseid, D. E., Wells, E. A., Coaston, T. N., & Robinson, A. S. (2021) · Research Square · doi:10.21203/rs.3.rs-647000/v1

The Role of Microglial-Triggering Receptor Expressed on Myeloid Cells 2 (TREM2) in Neuronal Homeostasis and Tau Pathogenesis

Jadhav, V. (2021) · IUScholarWorks (Indiana University) · doi:10.7912/c2/2086

Quantification and Analysis of Tau Protein Effects on Microtubule Dynamics in Mammalian (LLC-PK1) Cells

Doersch, A. (2020) · University of Minnesota Digital Conservancy (University of Minnesota)

Extracellular Tau Oligomers Induce Disruption of Endogenous Tau Distribution, Invasion of Tau into the Somatodendritic Compartment and Axonal Transport Dysfunction

Swanson, E. C. (2017) · doi:10.18130/v3p643

Ensemble-based design of tau to inhibit aggregation while preserving biological activityPreprint

Joachimiak, Ł. A., Bali, S., Singh, R., Wydorski, P. M., Wosztyl, A., Perez, V., Chen, D., & Rizo, J. (2024) · Research Square · doi:10.21203/rs.3.rs-3796916/v1

New Frontiers in Animal Prion Diseases

Abdul, H., Konold, T., Spiropoulos, J., & Lewis, P. A. (2025) · Annual Review of Animal Biosciences · doi:10.1146/annurev-animal-111523-102335

Additional file 1 of The 3-O sulfation of heparan sulfate proteoglycans contributes to the cellular internalization of tau aggregates

Ferreira, A., Royaux, I. E., Liu, J., Wang, Z., Su, G., Moechars, D., Callewaert, N., & Muynck, L. D. (2024) · Figshare · doi:10.6084/m9.figshare.26557271

Additional file 1 of Reassessment of Neuronal Tau Distribution in Adult Human Brain and Implications for Tau Pathobiology

Paterno, G., Bell, B. M., Gorion, K.-M. M., Prokop, S., & Giasson, B. I. (2022) · Figshare · doi:10.6084/m9.figshare.20176025

Development of Inhibitors of Amyloid Fibril Propagation

Bendifallah, M. (2019) · theses.fr (ABES) · doi:10.70675/a872e5bdzc153z41f4z9472z725fd78aab48

Rôle de la dérégulation neuronale de la protéine kinase activée par l’AMP (AMPK) dans la pathologie tau, l’intégrité des synapses et le métabolisme énergétique : relevance pour la maladie d’Alzheimer

Domise, M. (2018) · theses.fr (ABES) · doi:10.70675/43c1f12fze623z41e8z970fz64a5de94a299

Prévention du phénomène de nucléation et de la propagation des tauopathies par immunothérapie passive utilisant un anticorps ciblant une région centrale de la protéine tau

Albert, M. (2018) · theses.fr (ABES) · doi:10.70675/7563255bz78adz4fe1zb0e6zc298f8457886

3S-HS et HS3ST2 dans les macrophages humains : implication dans le diagnostic de la maladie d'Alzheimer

Abdelouahab, O. B. (2021) · theses.fr (ABES) · doi:10.70675/97f4885fz3f5cz4234zb8e2ze3fa7c4e3d41

Caractérisation d'anticorps à domaine unique dirigés contre la protéine Tau

Danis, C. (2018) · theses.fr (ABES) · doi:10.70675/c783a062zb57bz4024z85d0z509baaed8a1b

Engineering artificial biomolecular condensates to study the aggregation of α-Synuclein

Piroska, M.-L. (2023) · theses.fr (ABES) · doi:10.70675/1d15bb63z3f2fz4a91z80f1z5086a39a5087

Tau physiology and pathology: impacts on cellular structures and neurodegenerative diseases

Akbari, V., & Bahramikia, S. (2026) · Inflammopharmacology · doi:10.1007/s10787-026-02328-w

Chemokine receptor CX3CR1 interacts with Tau and regulates its microglial activity in Alzheimer’s disease

Chinnathambi, S., Baisya, U., & Ananthanarayana, V. (2026) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2026.07.004

Is tau ready for admission to the prion club?

Hall, G. F., & Patuto, B. A. (2012) · Prion · doi:10.4161/pri.19912 · Cited by 43

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

Prion-like Mechanisms in the Pathogenesis of Tauopathies and Synucleinopathies

Goedert, M., Falcon, B., Clavaguera, F., & Tolnay, M. (2014) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-014-0495-z · Cited by 152

Prion-like properties of assembled TDP-43

Nonaka, T., & Hasegawa, M. (2019) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2019.11.018 · Cited by 28

Neurodegeneration‐related amyloids interact with the prion protein

Cecco, E. D., Narkiewicz, J., Grandolfo, M., Parisse, P., & Legname, G. (2019) · The FASEB Journal · doi:10.1096/fasebj.2019.33.1_supplement.464.3