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

Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359

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

Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563

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

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Neurodegenerative Tauopathies

Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480

Transmission and spreading of tauopathy in transgenic mouse brain

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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

Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP

Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611

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

Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526

The CNS in inbred transgenic models of 4-repeat Tauopathy develops consistent tau seeding capacity yet focal and diverse patterns of protein deposition

Eskandari-Sedighi, G., Daude, N., Gapeshina, H., Sanders, D. W., Kamali-Jamil, R., Yang, J., Shi, B., Wille, H., Ghetti, B., Diamond, M. I., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0215-7 · Cited by 22

LRRK2 kinase inhibition reverses G2019S mutation-dependent effects on tau pathology progression

Lubben, N., Brynildsen, J. K., Webb, C. M., Li, H. L., Leyns, C. E. G., Changolkar, L. N., Zhang, B., Meymand, E. S., O’Reilly, M., Madaj, Z. B., et al. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00403-2 · Cited by 22

Compound screening in cell-based models of tau inclusion formation: Comparison of primary neuron and HEK293 cell assays

Crowe, A., Henderson, M. J., Anderson, J. D., Titus, S. A., Zakharov, A. V., Simeonov, A. M., Buist, A., Delay, C., Moechars, D., Trojanowski, J. Q., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010532 · Cited by 23

Spreading of Alzheimer tau seeds is enhanced by aging and template matching with limited impact of amyloid-β

Nies, S. H., Takahashi, H., Herber, C. S., Huttner, A. J., Chase, A., & Strittmatter, S. M. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101159 · Cited by 25

Intraneuronal tau aggregation induces the integrated stress response in astrocytes

Batenburg, K. L., Kasri, N. N., Heine, V. M., & Scheper, W. (2022) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjac071 · Cited by 21

Connections between ApoE, sleep, and Aβ and tau pathologies in Alzheimer’s disease

Sadleir, K. R., & Vassar, R. J. (2023) · Journal of Clinical Investigation · doi:10.1172/jci171838 · Cited by 22

Enhancement of therapeutic potential of a naturally occurring human antibody targeting a phosphorylated Ser422 containing epitope on pathological tau

van Ameijde, J., Crespo, R., Janson, R., Juraszek, J., Siregar, B., Verveen, H., Sprengers, I., Nahar, T., Hoozemans, J. J. M., Steinbacher, S., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0562-9 · Cited by 21

Tau Secretion

Ruan, Z., & Ikezu, T. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_11 · Cited by 23

Pathogenic Role of RAGE in Tau Transmission and Memory Deficits

Kim, Y., Park, H., Kim, Y., Kim, S., Lee, J., Yang, H., Kim, S. J., Li, C. M., Lee, H., Na, D.-H., et al. (2022) · Biological Psychiatry · doi:10.1016/j.biopsych.2022.10.015 · Cited by 23

Alzheimer’s disease is an inherent, natural part of human brain aging: an integrated perspective

Ferrer, I. (2022) · Free Neuropathology · doi:10.17879/freeneuropathology-2022-3806 · Cited by 25

PM2.5 triggers tau aggregation in a mouse model of tauopathy

Liu, C., Meng, L., Gao, Y., Chen, J., Zhu, M., Xiong, M., Xiao, T., Gu, X., Liu, C., Li, T., et al. (2024) · JCI Insight · doi:10.1172/jci.insight.176703 · Cited by 22

Mitochondrial Dynamics Impairment in Dexamethasone-Treated Neuronal Cells

Suwanjang, W., Wu, K. L. H., Prachayasittikul, S., Chetsawang, B., & Charngkaew, K. (2019) · Neurochemical Research · doi:10.1007/s11064-019-02779-4 · Cited by 20

Discovery and Functional Characterization of hPT3, a Humanized Anti-Phospho Tau Selective Monoclonal Antibody

Kolen, K. V., Malia, T., Theunis, C., Nanjunda, R. K., Teplyakov, A., Ernst, R., Wu, S., Luo, J., Borgers, M., Vandermeeren, M., et al. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200544 · Cited by 21

TREM2-Deficient Microglia Attenuate Tau Spreading In Vivo

Lee-Gosselin, A., Jury-Garfe, N., You, Y., Dabin, L., Soni, D., Dutta, S., Rochet, J.-C., Kim, J., Oblak, A. L., & Lasagna-Reeves, C. A. (2023) · Cells · doi:10.3390/cells12121597 · 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

Relevance of plasma biomarkers to pathologies in Alzheimer’s disease, Parkinson’s disease and frontotemporal dementia

Chiu, P., Yang, F., Chiu, M., Lin, W.-C., Lu, C., & Yang, S. (2022) · Scientific Reports · doi:10.1038/s41598-022-22647-6 · Cited by 20

Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates

Limorenko, G., Tatlı, M., Rajasekhar, K., Nazarov, S., Weil, M., Schöndorf, D. C., Geist, D., Reinhardt, P., Ehrnhoefer, D. E., Stahlberg, H., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39314-7 · Cited by 22

Lymphocyte‐Activation Gene 3 Facilitates Pathological Tau Neuron‐to‐Neuron Transmission

Chen, C., Kumbhar, R., Wang, H., Yang, X., Gadhave, K., Rastegar, C. T., Kimura, Y., Behensky, A. A., Kotha, S., Kuo, G., et al. (2024) · Advanced Science · doi:10.1002/advs.202303775 · Cited by 18

Secretion of full-length Tau or Tau fragments in cell culture models. Propagation of Tau in vivo and in vitro

Pérez, M., Medina, M., Hernández, F., & Ávila, J. (2018) · BioMolecular Concepts · doi:10.1515/bmc-2018-0001 · Cited by 20

Is multiple system atrophy an infectious disease?

Wenning, G. K., Trojanowski, J. Q., Kaufmann, H., Wısnıewskı, T., Rocca, W. A., & Low, P. A. (2018) · Annals of Neurology · doi:10.1002/ana.25132 · Cited by 17

Temporal and Sex-Linked Protein Expression Dynamics in a Familial Model of Alzheimer’s Disease

Lopes, F. B. T. P., Schlatzer, D., Wang, R., Li, X., Feng, E., Koyutürk, M., Qi, X., & Chance, M. R. (2022) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2022.100280 · Cited by 17

Tau antibody 77G7 targeting microtubule binding domain suppresses proteopathic tau to seed tau aggregation

Li, L., Miao, J., Chu, D., Jin, N., Tung, Y. C., Dai, C., Hu, W. H., Gong, C., Iqbal, K., & Liu, F. (2022) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13970 · Cited by 17

Interaction of Proteins Involved in Neuronal Proteinopathies

Kulichikhin, K. Y., Malikova, O. A., Zobnina, A. E., Zalutskaya, N. M., & Rubel, A. A. (2023) · Life · doi:10.3390/life13101954 · Cited by 17

Traumatic brain injury derived pathological tau polymorphs induce the distinct propagation pattern and neuroinflammatory response in wild type mice

Puangmalai, N., Bhatt, N. N., Bittar, A., Jerez, C., Shchankin, N., & Kayed, R. (2023) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2023.102562 · Cited by 17

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

Coconut (Cocos nucifera) Ethanolic Leaf Extract Reduces Amyloid-β (1-42) Aggregation and Paralysis Prevalence in Transgenic Caenorhabditis elegans Independently of Free Radical Scavenging and Acetylcholinesterase Inhibition

Manalo, R. V. M., Silvestre, M., Barbosa, A., & Medina, P. M. B. (2017) · Biomedicines · doi:10.3390/biomedicines5020017 · Cited by 17

The big tau splice isoform resists Alzheimer’s-related pathological changesPreprint

Chung, D. C., Deng, X., Yalamanchili, H. K., Revelli, J., Han, A. L., Tadros, B., Richman, R., Dias, M., Naini, F. A., Boeynaems, S., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.30.605685 · Cited by 16

Dextran sulphate-induced tau assemblies cause endogenous tau aggregation and propagation in wild-type mice

Masuda‐Suzukake, M., Suzuki, G., Hosokawa, M., Nonaka, T., Goedert, M., & Hasegawa, M. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa091 · Cited by 16

A human tau seeded neuronal cell model recapitulates molecular responses associated with Alzheimer’s disease

Ficulle, E., Kananathan, S., Airey, D., Gharbi, S., Humphryes-Kirilov, N., Scherschel, J., Dunbar, C., Eastwood, B. J., Laing, E., Collier, D. A., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-06411-4 · Cited by 18

The use of mouse models to study cell-to-cell transmission of pathological tau

Narasimhan, S., & Lee, V. M. ‐. (2017) · Methods in cell biology · doi:10.1016/bs.mcb.2017.06.009 · Cited by 16

Tau Acetylation in Entorhinal Cortex Induces its Chronic Hippocampal Propagation and Cognitive Deficits in Mice

Wang, X., Liu, E.-J., Liu, Q. R., Li, S., Li, T., Zhou, Q., Liu, Y., Zhang, H., & Wang, J. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200529 · Cited by 16

Preclinical characterization and IND‐enabling safety studies for PNT001, an antibody that recognizes cis‐pT231 tau

Foster, K., Manca, M., McClure, K. F., Koivula, P. P., Trojanowski, J. Q., Havas, D., Chancellor, S. E., Goldstein, L. E., Brunden, K. R., Kraus, A., et al. (2023) · Alzheimer s & Dementia · doi:10.1002/alz.13028 · Cited by 15

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

Influence of Tau on Neurotoxicity and Cerebral Vasculature Impairment Associated with Alzheimer’s Disease

Rather, M. A., Khan, A., Jahan, S., Siddiqui, A. J., & Wang, L. (2024) · Neuroscience · doi:10.1016/j.neuroscience.2024.05.042 · Cited by 18

Conformation-based assay of tau protein aggregation

Fichou, Y., Eschmann, N. A., Keller, T. J., & Han, S. (2017) · Methods in cell biology · doi:10.1016/bs.mcb.2017.06.008 · Cited by 15

Thiophene‐Based Optical Ligands That Selectively Detect Aβ Pathology in Alzheimer's Disease

Klingstedt, T., Shirani, H., Ghetti, B. F., Vidal, R., & Nilsson, K. P. R. (2021) · ChemBioChem · doi:10.1002/cbic.202100199 · Cited by 14

Host Tau Genotype Specifically Designs and Regulates Tau Seeding and Spreading and Host Tau Transformation Following Intrahippocampal Injection of Identical Tau AD Inoculum

Andrés‐Benito, P., Carmona, M., Jordán, M., Fernández‐Irigoyen, J., Santamaría, E., del Rı́o, J. A., & Ferrer, I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23020718 · Cited by 14

Capacity for Seeding and Spreading of Argyrophilic Grain Disease in a Wild-Type Murine Model; Comparisons With Primary Age-Related Tauopathy

Ferrer, I., Andrés‐Benito, P., Sala‐Jarque, J., Gil, V., & del Rı́o, J. A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00101 · Cited by 14

Insoluble Tau From Human FTDP-17 Cases Exhibit Unique Transmission Properties In Vivo

Weitzman, S. A., Narasimhan, S., He, Z., Changolkar, L. N., McBride, J. D., Zhang, B., Schellenberg, G. D., Trojanowski, J. Q., & Lee, V. M. ‐. (2020) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlaa086 · Cited by 14

Absence of Uptake and Prion-Like Spreading of Alpha-Synuclein and Tau After Intravitreal Injection of Preformed Fibrils

Veys, L., houcke, J. V., Aerts, J., Pottelberge, S. V., Mahieu, M., Coens, A., Melki, R., Moechars, D., Muynck, L. D., & Groef, L. D. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.614587 · Cited by 16

Tau Isoform-Driven CBD Pathology Transmission in Oligodendrocytes in Humanized Tau Mice

Zarȩba-Pasławska, J., Patra, K., Kluzer, L., Révész, T., & Svenningsson, P. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.589471 · Cited by 14

The unique neuropathological vulnerability of the human brain to aging

Ferrer, I. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101916 · Cited by 15

A seeding-based neuronal model of tau aggregation for use in drug discovery

Amorim, I. S., Challal, S., Cistarelli, L., Dorval, T., Abjean, L., Touzard, M., Arbez, N., François, A., Panayi, F., Jeggo, R., et al. (2023) · PLoS ONE · doi:10.1371/journal.pone.0283941 · Cited by 14

Molecular Links Between Alzheimer's Disease and Gastrointestinal Microbiota: Emphasis on Helicobacter pylori Infection Involvement

Katsinelos, P., Doulberis, M., Pοlyzos, S. A., Papaefthymiou, A., Katsinelos, P., & Kountouras, J. (2019) · Current Molecular Medicine · doi:10.2174/1566524019666190917125917 · Cited by 13

The role of wild-type tau in Alzheimer’s disease and related tauopathies

Lo, C. H., & Sachs, J. N. (2020) · JoLS Journal of Life Sciences · doi:10.36069/jols/20201201 · Cited by 15

Seed structure and phosphorylation in the fuzzy coat impact tau seeding competency

Kasen, A., Lövestam, S., Breton, E., Meyerdirk, L. K., McPhail, J. A., Piché, K., Louwrier, A., Capan, C. D., Lee, H., Scheres, S. H. W., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-64312-2 · Cited by 17

Apolipoprotein E isoform does not influence trans-synaptic spread of tau pathology in a mouse model

Davies, C., Tulloch, J., Yip, E., Currie, L., Colom‐Cadena, M., Wegmann, S., Hyman, B. T., Wilkins, L., Hooley, M., Tzioras, M., et al. (2023) · Brain and Neuroscience Advances · doi:10.1177/23982128231191046 · Cited by 11

In vitro generation of tau aggregates conformationally distinct from parent tau seeds of Alzheimer’s brain

Nam, W., & Choi, Y. P. (2018) · Prion · doi:10.1080/19336896.2018.1545524 · Cited by 13

Strain-specific clearance of seed-dependent tau aggregation by lithium-induced autophagy

Uddin, M. N., Elahi, M., Shimonaka, S., Kakuta, S., Ishiguro, K., Motoi, Y., & Hattori, N. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.12.113 · Cited by 12

Generation and characterization of a humanized ACE2 mouse model to study long‐term impacts of SARS‐CoV‐2 infection

Choi, C., Gadhave, K., Villano, J., Pekosz, A. S., Mao, X., & Jia, H. (2024) · Journal of Medical Virology · doi:10.1002/jmv.29349 · Cited by 14

Shaping the future of preclinical development of successful disease-modifying drugs against Alzheimer's disease: a systematic review of tau propagation models

Basheer, N., Buée, L., Brion, J., Smolek, T., Muhammadi, M. K., Hritz, J., Hromádka, T., Dewachter, I., Wegmann, S., Landrieu, I., et al. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01748-5 · Cited by 12

Amyloid-β-activated microglia can induce compound proteinopathies

Lee, S. H., Bae, E.-J., Pérez-Acuña, D., Jung, M. K., Han, J. W., Mook‐Jung, I., & Lee, S. (2024) · Brain · doi:10.1093/brain/awae221 · Cited by 11

Tau Accumulation Induces Microglial State Alterations in Alzheimer's Disease Model Mice

Nagata, K., Hashimoto, S., Joho, D., Fujioka, R., Matsuba, Y., Sekiguchi, M., Mihira, N., Motooka, D., Liu, Y., Okuzaki, D., et al. (2024) · eNeuro · doi:10.1523/eneuro.0260-24.2024 · Cited by 11

Extensive Plasmid Library to Prepare Tau Protein Variants and Study Their Functional Biochemistry

Karikari, T. K., Keeling, S., Hill, E., Lantero‐Rodriguez, J., Nagel, D. A., Becker, B., Höglund, K., Zetterberg, H., Blennow, K., Hill, E. J., et al. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00469 · Cited by 11

Hexameric Aggregation Nucleation Core Sequences and Diversity of Pathogenic Tau Strains

Wu, L., Madhavan, S. S., Tan, C., & Xu, B. (2022) · Pathogens · doi:10.3390/pathogens11121559 · Cited by 9

Oligomeric, phosphorylated, and truncated tau and spliceosome pathology within the entorhinal–hippocampal connectome across stages of Alzheimer's disease

Mahady, L. J., Perez, S. E., Malek‐Ahmadi, M. H., & Mufson, E. J. (2023) · The Journal of Comparative Neurology · doi:10.1002/cne.25466 · Cited by 11

Behavioral and neuropathological characterization over the adult lifespan of the human tau knock-in mouse

Benskey, M. J., Panoushek, S., Saito, T., Saido, T. C., Grabinski, T. M., & Kanaan, N. M. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1265151 · Cited by 13

Brain aging and Alzheimer’s disease, a perspective from non-human primates

Ferrer, I. (2024) · Aging · doi:10.18632/aging.206143 · Cited by 10

Inducers and modulators of protein aggregation in Alzheimer's disease - Critical tools for understanding the foundations of aggregate structures

Sun, K. T., & Mok, S. (2025) · Neurotherapeutics · doi:10.1016/j.neurot.2024.e00512 · Cited by 12

Strain-Distinct α-Synuclein and Tau Cross-Seeding Uncovered by Correlative Approach with Optical Photothermal Infrared Sub-Micron Imaging

Zhan, X., Li, W., Hatterer, E., Courade, J., Piché, K., Klementieva, O. L., & Li, J. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c02811 · Cited by 12

Common and Specific Marks of Different Tau Strains Following Intra-Hippocampal Injection of AD, PiD, and GGT Inoculum in hTau Transgenic Mice

Ferrer, I., Andrés‐Benito, P., Carmona, M., & del Rı́o, J. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415940 · Cited by 10

Progressive tau aggregation does not alter functional brain network connectivity in seeded hTau.P301L mice

Detrez, J. R., Ben-Nejma, I. R. H., Kolen, K. V., Dam, D. V., Deyn, P. P. D., Fransén, E., Verhoye, M., Timmermans, J., Nuydens, R., der Linden, A. V., et al. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105011 · Cited by 10

Structural mapping techniques distinguish the surfaces of fibrillar 1N3R and 1N4R human tau

Caroux, E., Redeker, V., Madiona, K., & Melki, R. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101252 · Cited by 9

Strains of Pathological Protein Aggregates in Neurodegenerative Diseases

Wang, X., Noroozian, Z., Lynch, M., Armstrong, N., Schneider, R., Liu, M., Ghodrati, F., Zhang, A. B., Yang, Y. J., Hall, A. C., et al. (2017) · Discoveries · doi:10.15190/d.2017.8 · Cited by 11

Dysregulation of neuroproteasomes by ApoE isoforms drives endogenous Tau aggregationPreprint

Paradise, V., Sabu, M., Bafia, J., Sharif, N., Nguyen, C., Konrad-Vicario, K., Mukim, R. D., Wang, X., Corjuc, B., Fu, J. M., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.29.518293 · Cited by 10

Extracellular PHF-tau modulates astrocyte mitochondrial dynamics and mediates neuronal connectivity

Zufferey, V., Barve, A., Parietti, E., Belinga, L. N., Bringaud, A., Varisco, Y., Fabbri, K., Capotosti, F., Bezzi, P., Déglon, N., et al. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00474-9 · Cited by 11

Targeting tau in Alzheimer’s Disease: rationale, approach and challenges

Aslanyan, A., Foiani, M. S., Giovannucci, T. A., McDade, E., Duff, K., Mummery, C. J., Schöll, M., Wildsmith, K. R., & Paterson, R. W. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00925-5 · Cited by 10

A pathogenic Tau mutation drives autophagy-lysosome dysfunction that limits Tau degradation in a model of frontotemporal dementia

Mirfakhar, F. S., Marsh, J. A., Sato, C., Schache, K. J., Minaya, M., Dolle, R. E., Pak, S. C., Silverman, G. A., Perlmutter, D. H., Macauley, S. L., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-70473-5 · Cited by 9

Computational modelling of pathogenic protein spread in neurodegenerative diseases

Georgiadis, K. L., Wray, S., Sebastien Ourselin, A., Warren, J. D., & Marc Modat, A. (2018) · PLoS ONE · doi:10.1371/journal.pone.0192518 · Cited by 9

An early proinflammatory transcriptional response to tau pathology is age‐specific and foreshadows reduced tau burden

Rasmussen, J., Ewing, A. D., Bodea, L., Bodea, G. O., Gearing, M., & Faulkner, G. J. (2021) · Brain Pathology · doi:10.1111/bpa.13018 · Cited by 10

Limitations and Applications of Rodent Models in Tauopathy and Synucleinopathy Research

Szegvari, E., Holec, S. A. M., & Woerman, A. L. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70021 · Cited by 8

Tracking tau and cellular responses in human iPSC‐microglia: from uptake to seedable secretion, including in extracellular vesicles

Karabova, M. K., del Ser‐Badia, A., Hedegaard, A., Washer, S. J., Baykam, Z., O'Brien, D. P., Vendrell, I., Hester, S., Fischer, R., Johnson, E., et al. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71337 · Cited by 10

The role of prion strain diversity in the development of successful therapeutic treatments

Holec, S. A. M., Block, A. J., & Bartz, J. C. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.07.001 · Cited by 8

The Adult Neurogenesis Theory of Alzheimer’s Disease

Abbate, C. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-221279 · Cited by 11

A Next-Generation Sequencing Study in a Cohort of Sicilian Patients with Parkinson’s Disease

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MSUT2 regulates tau spreading via adenosinergic signaling mediated ASAP1 pathway in neurons

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Mouse serum albumin induces neuronal apoptosis and tauopathies

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The importance of prion research

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Spreading of P301S Aggregated Tau Investigated in Organotypic Mouse Brain Slice Cultures

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Learning Deficits Accompanied by Microglial Proliferation After the Long-Term Post-Injection of Alzheimer’s Disease Brain Extract in Mouse Brains

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LRRK2 Kinase Activity Does Not Alter Cell-Autonomous Tau Pathology Development in Primary Neurons

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Sarkosyl differentially solubilizes patient-derived alpha-synuclein fibril strains

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Selection of lansoprazole from an FDA-approved drug library to inhibit the Alzheimer’s disease seed-dependent formation of tau aggregates

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Animal models of tau propagation in Alzheimer's disease

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Anterograde and Retrograde Propagation of Inoculated Human Tau Fibrils and Tau Oligomers in a Non-Transgenic Rat Tauopathy Model

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Disease-Associated Mutations in Tau Encode for Changes in Aggregate Structure Conformation

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Severe neurodegeneration in brains of transgenic rats producing human tau prions

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

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Hyperactive neuronal networks enhance tau spread in an Alzheimer’s disease mouse modelPreprint

Barbour, A. J., Hoag, K., Cornblath, E. J., Chavez, A., Lucas, A., Li, X., Zebrowitz, S. E., Hassman, C., Vazquez, O., Xie, S. X., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.01.625514 · Cited by 6

Aqueous extractable nonfibrillar and sarkosyl extractable fibrillar Alzheimer’s disease tau seeds have distinct properties

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Divergent disruptive effects of soluble recombinant tau assemblies on synaptic plasticity in vivo

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Evolving prion-like tau conformers differentially alter postsynaptic proteins in neurons inoculated with distinct isolates of Alzheimer’s disease tau

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Human tauopathy strains defined by phosphorylation in R1-R2 repeat domains of tau

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Comparison of size distribution and (Pro249-Ser258) epitope exposure in in vitro and in vivo derived Tau fibrils

Marreiro, A. F. D., Kolen, K. V., Sousa, C., Temmerman, L., Vasconcelos, B., Rodriguez, R. C., van Weering, J. R. T., Dam, D. V., Deyn, P. P. D., Apetri, A. C., et al. (2020) · BMC Molecular and Cell Biology · doi:10.1186/s12860-020-00320-y · Cited by 6

Abundant copathologies of polyglucosan bodies, frontotemporal lobar degeneration with TDP‐43 inclusions and ageing‐related tau astrogliopathy in a family with a GBE1 mutation

Uemura, M. T., Suh, E. R., Robinson, J. L., Brunden, K. R., Grossman, M., Irwin, D. J., Lee, V. M. ‐., Trojanowski, J. Q., Lee, E. B., & Deerlin, V. M. V. (2022) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12865 · Cited by 6

Digital imaging software versus the “eyeball” method in quantifying steatosis in a liver biopsy

Long, J. J., Nijhar, K., Jenkins, R. T., Yassine, A., Motter, J. D., Jackson, K. R., Jerman, S., Besharati, S., Anders, R. A., Dunn, T. B., et al. (2023) · Liver Transplantation · doi:10.1097/lvt.0000000000000064 · Cited by 6

Seeding-Competent Tau in Gray Matter Versus White Matter of Alzheimer’s Disease Brain

Wu, R., Gu, J., Zhou, D., Tung, Y. C., Jin, N., Chu, D., Hu, W. H., Węgiel, J., Gong, C., Iqbal, K., et al. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-201290 · Cited by 5

Human Tau Isoform Aggregation and Selective Detection of Misfolded Tau from Post-Mortem Alzheimer’s Disease BrainsPreprint

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Additive effect of distant Lewy bodies and tau seeds injections on nigral degeneration in macaques

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A human iPSC model of tauopathies engineered for 4R tau isoform expression endogenously develops late-stage neuronal tau pathology

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The use of mouse models to study cell-to-cell transmission of pathological tau

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Synthetic Tau Fibrils Mediate Transmission of Neurofibrillary Tangles in a Transgenic Mouse Model of Alzheimer's-Like Tauopathy

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Pathological Tau Strains from Human Brains Recapitulate the Diversity of Tauopathies in Nontransgenic Mouse Brain

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Intracerebral injection of preformed synthetic tau fibrils initiates widespread tauopathy and neuronal loss in the brains of tau transgenic mice

Peeraer, E., Bottelbergs, A., Van Kolen, K., Stancu, I.-C., Vasconcelos, B., Mahieu, M., Duytschaever, H., Ver Donck, L., Torremans, A., Sluydts, E., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.08.032 · Cited by 214

Mechanisms of Cell-to-Cell Transmission of Pathological Tau: A Review

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