Microglia: Friend and foe in tauopathy
Open accessAbstract
Aggregation of misfolded microtubule associated protein tau into abnormal intracellular inclusions defines a class of neurodegenerative diseases known as tauopathies. The consistent spatiotemporal progression of tau pathology in Alzheimer's disease (AD) led to the hypothesis that tau aggregates spread in the brain via bioactive tau "seeds" underlying advancing disease course. Recent studies implicate microglia, the resident immune cells of the central nervous system, in both negative and positive regulation of tau pathology. Polymorphisms in genes that alter microglial function are associated with the development of AD and other tauopathies. Experimental manipulation of microglia function can alter tau pathology and microglia-mediated neuroinflammatory cascades can exacerbate tau pathology. Microglia also exert protective functions by mitigating tau spread: microglia internalize tau seeds and have the capacity to degrade them. However, when microglia fail to degrade these tau seeds there are deleterious consequences, including secretion of exosomes containing tau that can spread to neurons. This review explores the intersection of microglia and tau from the perspective of neuropathology, neuroimaging, genetics, transcriptomics, and molecular biology. As tau-targeted therapies such as anti-tau antibodies advance through clinical trials, it is critical to understand the interaction between tau and microglia.
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The phagocytic activity of microglia is crucial for the removal of Aβ, tau, and α-synuclein.
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From Microbiota–gut–brain axis and its therapeutic applications in neurodegenerative diseases (2024) · cites this paper as [95]
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Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · see citing works
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 · see citing works
Polazzi, E., Mengoni, I., Caprini, M., Peña‐Altamira, E., Kurtys, E., & Monti, B. (2012) · Neurosignals · doi:10.1159/000337115 · Cited by 9,023 · see citing works
The serial cultivation of human diploid cell strains
Hayflick, L., & Moorhead, P. S. (1961) · Experimental Cell Research · doi:10.1016/0014-4827(61)90192-6 · Cited by 8,508 · see citing works
Biogenesis, Secretion, and Intercellular Interactions of Exosomes and Other Extracellular Vesicles
Colombo, M., Raposo, G., & Théry, C. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101512-122326 · Cited by 6,186 · see citing works
Resting microglial cells are highly dynamic surveillants of brain parenchyma in vivo
Nimmerjahn, A., Kirchhoff, F., & Helmchen, F. (2005) · Science · doi:10.1126/science.1110647 · Cited by 5,827 · see citing works
A Unique Microglia Type Associated with Restricting Development of Alzheimer’s Disease
Keren-Shaul, H., Spinrad, A., Weiner, A., Matcovitch-Natan, O., Dvir-Szternfeld, R., Ulland, T. K., David, E., Baruch, K., Lara-Astaiso, D., Toth, B., et al. (2017) · Cell · doi:10.1016/j.cell.2017.05.018 · Cited by 5,493 · see citing works
Fate Mapping Analysis Reveals That Adult Microglia Derive from Primitive Macrophages
Ginhoux, F., Greter, M., Leboeuf, M., Nandi, S., See, P., Gokhan, S., Mehler, M. F., Conway, S. J., Ng, L. G., Stanley, E. R., et al. (2010) · Science · doi:10.1126/science.1194637 · Cited by 5,175 · see citing works
Zhang, Y., Chen, K., Sloan, S. A., Bennett, M. L., Scholze, A. R., O'Keeffe, S., Phatnani, H. P., Guarnieri, P., Caneda, C., Ruderisch, N., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.1860-14.2014 · Cited by 4,875 · see citing works
Synaptic Pruning by Microglia Is Necessary for Normal Brain Development
Paolicelli, R. C., Bolasco, G., Pagani, F., Maggi, L., Scianni, M., Panzanelli, P., Giustetto, M., Ferreira, T. A., Guiducci, E., Dumas, L., et al. (2011) · Science · doi:10.1126/science.1202529 · Cited by 4,244 · see citing works
Microglia: Active sensor and versatile effector cells in the normal and pathologic brain
Hanisch, U.-K., & Kettenmann, H. (2007) · Nature Neuroscience · doi:10.1038/nn1997 · Cited by 3,676 · see citing works
Kettenmann, H., Hanisch, U.-K., Noda, M., & Verkhratsky, A. (2011) · Physiological Reviews · doi:10.1152/physrev.00011.2010 · Cited by 3,547 · see citing works
<i>TREM2</i> Variants in Alzheimer's Disease
Guerreiro, R., Wojtas, A., Bras, J., Carrasquillo, M., Rogaeva, E., Majounie, E., Cruchaga, C., Sassi, C., Kauwe, J. S. K., Younkin, S., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1211851 · Cited by 3,020 · see citing works
Krasemann, S., Madore, C., Cialic, R., Baufeld, C., Calcagno, N., El Fatimy, R., Beckers, L., O’Loughlin, E., Xu, Y., Fanek, Z., et al. (2017) · Immunity · doi:10.1016/j.immuni.2017.08.008 · Cited by 2,979 · see citing works
Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.3.631 · Cited by 2,668 · see citing works
IgG Subclasses and Allotypes: From Structure to Effector Functions
Vidarsson, G., Dekkers, G., & Rispens, T. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00520 · Cited by 2,667 · see citing works
Identification of a unique TGF-β–dependent molecular and functional signature in microglia
Butovsky, O., Jedrychowski, M. P., Moore, C. S., Cialic, R., Lanser, A. J., Gabriely, G., Koeglsperger, T., Dake, B., Wu, P. M., Doykan, C. E., et al. (2014) · Nature Neuroscience · doi:10.1038/nn.3599 · Cited by 2,543 · see citing works
The NALP3 inflammasome is involved in the innate immune response to amyloid-β
Halle, A., Hornung, V., Petzold, G. C., Stewart, C. R., Monks, B. G., Reinheckel, T., Fitzgerald, K. A., Latz, E., Moore, K. J., & Golenbock, D. T. (2008) · Nature Immunology · doi:10.1038/ni.1636 · Cited by 2,441 · see citing works
Tjäderhane, L., Buzalaf, M. A. R., Carrilho, M., & Chaussain, C. (2015) · Caries Research · doi:10.1159/000363582 · Cited by 2,306 · see citing works
Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208 · see citing works
Nelson, P. T., Alafuzoff, I., Bigio, E. H., Bouras, C., Braak, H., Cairns, N. J., Castellani, R. J., Crain, B. J., Davies, P., Tredici, K. D., et al. (2012) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31825018f7 · Cited by 2,050 · see citing works
Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function
SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014 · see citing works
Elmore, M. R. P., Najafi, A. R., Koike, M. A., Dagher, N. N., Spangenberg, E. E., Rice, R. A., Kitazawa, M., Matusow, B., Nguyen, H., West, B. L., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.02.040 · Cited by 1,968 · see citing works
Transmission and spreading of tauopathy in transgenic mouse brain
Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803 · see citing works
Alzheimer’s disease drug-development pipeline: Few candidates, frequent failures
Cummings, J. L., Morstorf, T., & Zhong, K. (2014) · Alzheimer's Research & Therapy · doi:10.1186/alzrt269 · Cited by 1,744 · see citing works
DeNardo, D. G., Brennan, D. J., Rexhepaj, E., Ruffell, B., Shiao, S. L., Madden, S. F., Gallagher, W. M., Wadhwani, N., Keil, S. D., Junaid, S. A., et al. (2011) · Cancer Discovery · doi:10.1158/2159-8274.cd-10-0028 · Cited by 1,715 · see citing works
Depletion of microglia and inhibition of exosome synthesis halt tau propagation
Asai, H., Ikezu, S., Tsunoda, S., Medalla, M., Luebke, J., Haydar, T., Wolozin, B., Butovsky, O., Kügler, S., & Ikezu, T. (2015) · Nature Neuroscience · doi:10.1038/nn.4132 · Cited by 1,591 · see citing works
Heparan Sulfate ProteoglycansPreprint
Sarrazin, S., Lamanna, W. C., & Esko, J. D. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004952 · Cited by 1,524 · see citing works
Impairment of paravascular clearance pathways in the aging brain
Kress, B. T., Iliff, J. J., Xia, M., Wang, M., Wei, H. S., Zeppenfeld, D., Xie, L., Kang, H., Xu, Q., Liew, J. A., et al. (2014) · Annals of Neurology · doi:10.1002/ana.24271 · Cited by 1,521 · see citing works
Disease-Associated Microglia: A Universal Immune Sensor of Neurodegeneration
Deczkowska, A., Keren-Shaul, H., Weiner, A., Colonna, M., Schwartz, M., & Amit, I. (2018) · Cell · doi:10.1016/j.cell.2018.05.003 · Cited by 1,474 · see citing works
Propagation of Tau Pathology in a Model of Early Alzheimer's Disease
de Calignon, A., Polydoro, M., Suárez-Calvet, M., William, C., Adamowicz, D. H., Kopeikina, K. J., Pitstick, R., Sahara, N., Ashe, K. H., Carlson, G. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.033 · Cited by 1,427 · see citing works
Cysteine cathepsins: From structure, function and regulation to new frontiers
Turk, V., Stoka, V., Vasiljeva, O., Renko, M., Sun, T., Turk, B., & Turk, D. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.10.002 · Cited by 1,377 · see citing works
Alzheimer’s Disease Risk Genes and Mechanisms of Disease Pathogenesis
Karch, C. M., & Goate, A. M. (2015) · Biological Psychiatry · doi:10.1016/j.biopsych.2014.05.006 · Cited by 1,357 · see citing works
Microglial Dysfunction and Defective β-Amyloid Clearance Pathways in Aging Alzheimer's Disease Mice
Hickman, S. E., Allison, E. K., & El Khoury, J. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.0616-08.2008 · Cited by 1,329 · see citing works
Clearance of senescent glial cells prevents tau-dependent pathology and cognitive decline
Bussian, T. J., Aziz, A., Meyer, C. F., Swenson, B. L., van Deursen, J. M., & Baker, D. J. (2018) · Nature · doi:10.1038/s41586-018-0543-y · Cited by 1,289 · see citing works
Propagation of Tau Misfolding from the Outside to the Inside of a Cell
Frost, B., Jacks, R. L., & Diamond, M. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808759200 · Cited by 1,252 · see citing works
Iversen, T., Skotland, T., & Sandvig, K. (2011) · Nano Today · doi:10.1016/j.nantod.2011.02.003 · Cited by 1,235 · see citing works
Genome-wide Analysis of Genetic Loci Associated With Alzheimer Disease
Seshadri, S. (2010) · JAMA · doi:10.1001/jama.2010.574 · Cited by 1,219 · see citing works
PET Imaging of Tau Deposition in the Aging Human Brain
Schöll, M., Lockhart, S. N., Schonhaut, D. R., O’Neil, J. P., Janabi, M., Ossenkoppele, R., Baker, S. L., Vogel, J. W., Faria, J., Schwimmer, H. D., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.01.028 · Cited by 1,214 · see citing works
Impairment of Glymphatic Pathway Function Promotes Tau Pathology after Traumatic Brain Injury
Iliff, J. J., Chen, M. J., Plog, B. A., Zeppenfeld, D. M., Soltero, M., Yang, L., Singh, I., Deane, R., & Nedergaard, M. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.3020-14.2014 · Cited by 1,159 · see citing works
ARUK Consortium, Sims, R., GERAD/PERADES, C., van der Lee, S. J., Naj, A. C., Bellenguez, C., Badarinarayan, N., Jakobsdottir, J., Kunkle, B. W., Boland, A., et al. (2017) · Nature Genetics · doi:10.1038/ng.3916 · Cited by 1,126 · see citing works
The Complement System: An Unexpected Role in Synaptic Pruning During Development and Disease
Stephan, A. H., Barres, B. A., & Stevens, B. (2012) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-061010-113810 · Cited by 1,113 · see citing works
In-vivo measurement of activated microglia in dementia
Cagnin, A., Brooks, D. J., Kennedy, A. M., Gunn, R. N., Myers, R., Turkheimer, F. E., Jones, T., & Banati, R. B. (2001) · The Lancet · doi:10.1016/s0140-6736(01)05625-2 · Cited by 1,054 · see citing works
Banati, R. B., Gehrmann, J., Schubert, P., & Kreutzberg, G. W. (1993) · Glia · doi:10.1002/glia.440070117 · Cited by 1,020 · see citing works
The Cell Biology of Phagocytosis
Flannagan, R. S., Jaumouillé, V., & Grinstein, S. (2011) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-011811-132445 · Cited by 1,018 · see citing works
Regulatory evolution of innate immunity through co-option of endogenous retroviruses
Chuong, E. B., Elde, N. C., & Feschotte, C. (2016) · Science · doi:10.1126/science.aad5497 · Cited by 1,008 · see citing works
Trans-Synaptic Spread of Tau Pathology In Vivo
Liu, L., Drouet, V., Wu, J., Witter, M. P., Small, S. A., Clelland, C. L. T., & Duff, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031302 · Cited by 994 · see citing works
Spangenberg, E., Severson, P. L., Hohsfield, L. A., Crapser, J., Zhang, J., Burton, E. A., Zhang, Y., Spevak, W., Lin, J., Phan, N. Y., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11674-z · Cited by 939 · see citing works
Role of Particle Size in Phagocytosis of Polymeric Microspheres
Champion, J. A., Walker, A. H., & Mitragotri, S. (2008) · Pharmaceutical Research · doi:10.1007/s11095-008-9562-y · Cited by 887 · see citing works
Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds
Holmes, B. B., DeVos, S. L., Kfoury, N., Li, M., Jacks, R., Yanamandra, K., Ouidja, M. O., Brodsky, F. M., Marasa, J., Bagchi, D. P., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301440110 · Cited by 859 · see citing works
TREM2-mediated early microglial response limits diffusion and toxicity of amyloid plaques
Wang, Y., Ulland, T. K., Ulrich, J. D., Song, W., Tzaferis, J. A., Hole, J. T., Yuan, P., Mahan, T. E., Shi, Y., Gilfillan, S., et al. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20151948 · Cited by 840 · see citing works
Neuronal activity enhances tau propagation and tau pathology in vivo
Wu, J. W., Hussaini, S. A., Bastille, I. M., Rodriguez, G. A., Mrejeru, A., Rilett, K., Sanders, D. W., Cook, C., Fu, H., Boonen, R. A. C. M., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4328 · Cited by 820 · see citing works
Yuan, P., Condello, C., Keene, C. D., Wang, Y., Bird, T. D., Paul, S. M., Luo, W., Colonna, M., Baddeley, D., & Grutzendler, J. (2016) · Neuron · doi:10.1016/j.neuron.2016.05.003 · Cited by 817 · see citing works
Neuronal ‘On’ and ‘Off’ signals control microglia
Biber, K., Neumann, H., Inoue, K., & Boddeke, H. W. G. M. (2007) · Trends in Neurosciences · doi:10.1016/j.tins.2007.08.007 · Cited by 787 · see citing works
Tau pathology and neurodegeneration contribute to cognitive impairment in Alzheimer’s disease
Bejanin, A., Schonhaut, D. R., La Joie, R., Kramer, J. H., Baker, S. L., Sosa, N., Ayakta, N., Cantwell, A., Janabi, M., Lauriola, M., et al. (2017) · Brain · doi:10.1093/brain/awx243 · Cited by 778 · see citing works
Selective transfer of exosomes from oligodendrocytes to microglia by macropinocytosis
Fitzner, D., Schnaars, M., van Rossum, D., Krishnamoorthy, G., Dibaj, P., Bakhti, M., Regen, T., Hanisch, U.-K., & Simons, M. (2011) · Journal of Cell Science · doi:10.1242/jcs.074088 · Cited by 775 · see citing works
Brain homogenates from human tauopathies induce tau inclusions in mouse brain
Clavaguera, F., Akatsu, H., Fraser, G. M., Crowther, R. A., Frank, S., Hench, J., Probst, A., Winkler, D. T., Reichwald, J., Staufenbiel, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301175110 · Cited by 750 · see citing works
Streit, W. J., Braak, H., Xue, Q.-S., & Bechmann, I. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0556-6 · Cited by 727 · see citing works
Macropinocytosis: an endocytic pathway for internalising large gulps
Lim, J. P., & Gleeson, P. A. (2011) · Immunology and Cell Biology · doi:10.1038/icb.2011.20 · Cited by 705 · see citing works
Kitazawa, M., Oddo, S., Yamasaki, T. R., Green, K. N., & LaFerla, F. M. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2868-05.2005 · Cited by 697 · see citing works
Proteopathic tau seeding predicts tauopathy in vivo
Holmes, B. B., Furman, J. L., Mahan, T. E., Yamasaki, T. R., Mirbaha, H., Eades, W. C., Belaygorod, L., Cairns, N. J., Holtzman, D. M., & Diamond, M. I. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411649111 · Cited by 696 · see citing works
Iba, M., Guo, J. L., McBride, J. D., Zhang, B., Trojanowski, J. Q., & Lee, V. M.-Y. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.2642-12.2013 · Cited by 664 · see citing works
Friedman, B. A., Srinivasan, K., Ayalon, G., Meilandt, W. J., Lin, H., Huntley, M. A., Cao, Y., Lee, S.-H., Haddick, P. C. G., Ngu, H., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2017.12.066 · Cited by 662 · see citing works
Membrane flow during pinocytosis. A stereologic analysis.
Steinman, R. M., Brodie, S. E., & Cohn, Z. A. (1976) · The Journal of Cell Biology · doi:10.1083/jcb.68.3.665 · Cited by 644 · see citing works
Regulation of Tau Pathology by the Microglial Fractalkine Receptor
Bhaskar, K., Konerth, M., Kokiko-Cochran, O. N., Cardona, A., Ransohoff, R. M., & Lamb, B. T. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.023 · Cited by 639 · see citing works
Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice
Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Sengupta, U., Clos, A. L., Jackson, G. R., & Kayed, R. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-39 · Cited by 633 · see citing works
Holtman, I. R., Raj, D. D., Miller, J. A., Schaafsma, W., Yin, Z., Brouwer, N., Wes, P. D., Möller, T., Orre, M., Kamphuis, W., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0203-5 · Cited by 619 · see citing works
Maphis, N., Xu, G., Kokiko-Cochran, O. N., Jiang, S., Cardona, A., Ransohoff, R. M., Lamb, B. T., & Bhaskar, K. (2015) · Brain · doi:10.1093/brain/awv081 · Cited by 595 · see citing works
Tau protein aggregation is associated with cellular senescence in the brain
Musi, N., Valentine, J. M., Sickora, K. R., Baeuerle, E., Thompson, C. S., Shen, Q., & Orr, M. E. (2018) · Aging Cell · doi:10.1111/acel.12840 · Cited by 595 · see citing works
Interplay between innate immunity and Alzheimer disease: APOE and TREM2 in the spotlight
Shi, Y., & Holtzman, D. M. (2018) · Nature Reviews Immunology · doi:10.1038/s41577-018-0051-1 · Cited by 595 · see citing works
Suppression of glymphatic fluid transport in a mouse model of Alzheimer's disease
Peng, W., Achariyar, T. M., Li, B., Liao, Y., Mestre, H., Hitomi, E., Regan, S., Kasper, T., Peng, S., Ding, F., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.05.015 · Cited by 580 · see citing works
Yanamandra, K., Kfoury, N., Jiang, H., Mahan, T. E., Ma, S., Maloney, S. E., Wozniak, D. F., Diamond, M. I., & Holtzman, D. M. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.046 · Cited by 574 · see citing works
Li, Y., Liu, L., Barger, S. W., & Griffin, W. S. T. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-05-01605.2003 · Cited by 563 · see citing works
Late onset Alzheimer’s disease genetics implicates microglial pathways in disease risk
Efthymiou, A. G., & Goate, A. M. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0184-x · Cited by 562 · see citing works
Phagocytosis: A Fundamental Process in Immunity
Rosales, C., & Uribe‐Querol, E. (2017) · BioMed Research International · doi:10.1155/2017/9042851 · Cited by 562 · see citing works
LRP1 is a master regulator of tau uptake and spread
Rauch, J. N., Luna, G., Guzman, E., Audouard, M., Challis, C., Sibih, Y. E., Leshuk, C., Hernandez, I., Wegmann, S., Hyman, B. T., et al. (2020) · Nature · doi:10.1038/s41586-020-2156-5 · Cited by 541 · see citing works
Tau promotes neurodegeneration through global chromatin relaxation
Frost, B., Hemberg, M., Lewis, J., & Feany, M. B. (2014) · Nature Neuroscience · doi:10.1038/nn.3639 · Cited by 519 · see citing works
Leyns, C. E. G., Ulrich, J. D., Finn, M. B., Stewart, F. R., Koscal, L. J., Remolina Serrano, J., Robinson, G. O., Anderson, E., Colonna, M., & Holtzman, D. M. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1710311114 · Cited by 517 · see citing works
DeVos, S. L., Miller, R. L., Schoch, K. M., Holmes, B. B., Kebodeaux, C. S., Wegener, A. J., Chen, G., Shen, T., Tran, H., Nichols, B., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aag0481 · Cited by 516 · see citing works
Edison, P., Archer, H. A., Gerhard, A., Hinz, R., Pavese, N., Turkheimer, F. E., Hammers, A., Tai, Y. F., Fox, N., Kennedy, A., et al. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.08.001 · Cited by 513 · see citing works
Zhang, Z., Song, M., Liu, X., Kang, S. S., Kwon, I.-S., Duong, D. M., Seyfried, N. T., Hu, W. T., Liu, Z., Wang, J.-Z., et al. (2014) · Nature Medicine · doi:10.1038/nm.3700 · Cited by 494 · see citing works
Invited review: Neuropathology of tauopathies: principles and practice
Kovacs, G. G. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12208 · Cited by 492 · see citing works
Microglial activation and tau propagate jointly across Braak stages
Pascoal, T. A., Benedet, A. L., Ashton, N. J., Kang, M. S., Therriault, J., Chamoun, M., Savard, M., Lussier, F. Z., Tissot, C., Karikari, T. K., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01456-w · Cited by 490 · see citing works
Bratton, D. L., Fadok, V. A., Richter, D., Kailey, J. M., Guthrie, L. A., & Henson, P. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.42.26159 · Cited by 485 · see citing works
Distribution patterns of tau pathology in progressive supranuclear palsy
Kovacs, G. G., Lukic, M. J., Irwin, D. J., Arzberger, T., Respondek, G., Lee, E. B., Coughlin, D., Giese, A., Grossman, M., Kurz, C., et al. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02158-2 · Cited by 483 · see citing works
Kitazawa, M., Cheng, D., Tsukamoto, M. R., Koike, M. A., Wes, P. D., Vasilevko, V., Cribbs, D. H., & LaFerla, F. M. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100620 · Cited by 473 · see citing works
CHIP-Hsc70 Complex Ubiquitinates Phosphorylated Tau and Enhances Cell Survival
Shimura, H., Schwartz, D., Gygi, S. P., & Kosik, K. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m305838200 · Cited by 469 · see citing works
Disease Progression-Dependent Effects of TREM2 Deficiency in a Mouse Model of Alzheimer's Disease
Jay, T. R., Hirsch, A. M., Broihier, M. L., Miller, C. M., Neilson, L. E., Ransohoff, R. M., Lamb, B. T., & Landreth, G. E. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.2110-16.2016 · Cited by 457 · see citing works
Quintanilla, R. A., Orellana, D. I., González-Billault, C., & Maccioni, R. B. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.01.002 · Cited by 455 · see citing works
Zhou, Y., Lu, M., Du, R.-H., Qiao, C., Jiang, C.-Y., Zhang, K.-Z., Ding, J.-H., & Hu, G. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0094-3 · Cited by 455 · see citing works
Developmental Control of Endocytosis in Dendritic Cells by Cdc42
Garrett, W. S., Chen, L.-M., Kroschewski, R., Ebersold, M. W., Turley, S. J., Trombetta, S., Galán, J. E., & Mellman, I. (2000) · Cell · doi:10.1016/s0092-8674(00)00038-6 · Cited by 452 · see citing works
Kaufman, S. K., Sanders, D. W., Thomas, T. L., Ruchinskas, A. J., Vaquer-Alicea, J., Sharma, A. M., Miller, T. M., & Diamond, M. I. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.055 · Cited by 450 · see citing works
Microglia drive APOE-dependent neurodegeneration in a tauopathy mouse model
Shi, Y., Manis, M., Long, J., Wang, K., Sullivan, P. M., Remolina Serrano, J., Hoyle, R., & Holtzman, D. M. (2019) · Journal of Experimental Medicine · doi:10.1084/jem.20190980 · Cited by 448 · see citing works
Stancu, I.-C., Cremers, N., Vanrusselt, H., Couturier, J., Vanoosthuyse, A., Kessels, S., Lodder, C., Brône, B., Huaux, F., Octave, J.-N., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-018-01957-y · Cited by 447 · see citing works
Inflammation, microglia, and alzheimer's disease
Cameron, B., & Landreth, G. E. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.10.006 · Cited by 440 · see citing works
Guo, J. L., Narasimhan, S., Changolkar, L., He, Z., Stieber, A., Zhang, B., Gathagan, R. J., Iba, M., McBride, J. D., Trojanowski, J. Q., et al. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20160833 · Cited by 440 · see citing works
Tau molecular diversity contributes to clinical heterogeneity in Alzheimer’s disease
Dujardin, S., Commins, C., Lathuiliere, A., Beerepoot, P., Fernandes, A. R., Kamath, T. V., De Los Santos, M. B., Klickstein, N., Corjuc, D. L., Corjuc, B. T., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0938-9 · Cited by 438 · see citing works
Rangaraju, S., Dammer, E. B., Raza, S. A., Rathakrishnan, P., Xiao, H., Gao, T., Duong, D. M., Pennington, M. W., Lah, J. J., Seyfried, N. T., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0254-8 · Cited by 430 · see citing works
Microglia Mediate the Clearance of Soluble Aβ through Fluid Phase Macropinocytosis
Mandrekar, S., Jiang, Q., Lee, C. Y. D., Koenigsknecht-Talboo, J., Holtzman, D. M., & Landreth, G. E. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.5572-08.2009 · Cited by 415 · see citing works
Ghosh, S., Wu, M. D., Shaftel, S. S., Kyrkanides, S., LaFerla, F. M., Olschowka, J. A., & O'Banion, M. K. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.4361-12.2013 · Cited by 390 · see citing works
Liu, Y., Ying, Y., Li, Y., Eyo, U. B., Chen, T., Zheng, J., Umpierre, A. D., Zhu, J., Bosco, D. B., Dong, H., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0511-3 · Cited by 389 · see citing works
Dissecting phenotypic traits linked to human resilience to Alzheimer’s pathology
Perez-Nievas, B. G., Stein, T. D., Tai, H.-C., Dols-Icardo, O., Scotton, T. C., Barroeta-Espar, I., Fernandez-Carballo, L., de Munain, E. L., Perez, J., Marquie, M., et al. (2013) · Brain · doi:10.1093/brain/awt171 · Cited by 387 · see citing works
What is the evidence that tau pathology spreads through prion-like propagation?
Mudher, A., Colin, M., Dujardin, S., Medina, M., Dewachter, I., Alavi Naini, S. M., Mandelkow, E.-M., Mandelkow, E., Buée, L., Goedert, M., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0488-7 · Cited by 384 · see citing works
Takeda, S., Wegmann, S., Cho, H., DeVos, S. L., Commins, C., Roe, A. D., Nicholls, S. B., Carlson, G. A., Pitstick, R., Nobuhara, C. K., et al. (2015) · Nature Communications · doi:10.1038/ncomms9490 · Cited by 371 · see citing works
Butovsky, O., Jedrychowski, M. P., Cialic, R., Krasemann, S., Murugaiyan, G., Fanek, Z., Greco, D. J., Wu, P. M., Doykan, C. E., Kiner, O., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24304 · Cited by 358 · see citing works
Norbury, C. C., Chambers, B. J., Prescott, A. R., Ljunggren, H., & Watts, C. K. W. (1997) · European Journal of Immunology · doi:10.1002/eji.1830270141 · Cited by 350 · see citing works
TREM2 function impedes tau seeding in neuritic plaques
Leyns, C. E. G., Gratuze, M., Narasimhan, S., Jain, N., Koscal, L. J., Jiang, H., Manis, M., Colonna, M., Lee, V. M. Y., Ulrich, J. D., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0433-0 · Cited by 332 · see citing works
Single-Nucleus RNA-Seq Is Not Suitable for Detection of Microglial Activation Genes in Humans
Thrupp, N., Sala Frigerio, C., Wolfs, L., Skene, N. G., Fattorelli, N., Poovathingal, S., Fourne, Y., Matthews, P. M., Theys, T., Mancuso, R., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108189 · Cited by 329 · see citing works
Proteasomal degradation of tau protein
David, D. C., Layfield, R., Serpell, L., Narain, Y., Goedert, M., & Spillantini, M. G. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01137.x · Cited by 327 · see citing works
Streit, W. J., Xue, Q.-S., Tischer, J., & Bechmann, I. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0142-6 · Cited by 317 · see citing works
Sun, W., Samimi, H., Gamez, M., Zare, H., & Frost, B. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0194-1 · Cited by 315 · see citing works
Tau Activates Transposable Elements in Alzheimer’s Disease
Guo, C., Jeong, H.-H., Hsieh, Y.-C., Klein, H.-U., Bennett, D. A., De Jager, P. L., Liu, Z., & Shulman, J. M. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.05.004 · Cited by 315 · see citing works
Mechanisms of secretion and spreading of pathological tau protein
Brunello, C. A., Merezhko, M., Uronen, R.-L., & Huttunen, H. J. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03349-1 · Cited by 304 · see citing works
Coppé, J.-P., Patil, C. K., Rodier, F., Sun, Y., Muñoz, D. P., Goldstein, J., Nelson, P. S., Desprez, P.-Y., & Campisi, J. (2008) · PLoS Biology · doi:10.1371/journal.pbio.0060301 · Cited by 302 · see citing works
Altered microglial response to Aβ plaques in APPPS1-21 mice heterozygous for TREM2
Ulrich, J. D., Finn, M. B., Wang, Y., Shen, A., Mahan, T. E., Jiang, H., Stewart, F. R., Piccio, L., Colonna, M., & Holtzman, D. M. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-20 · Cited by 302 · see citing works
Spiller, K. J., Restrepo, C. R., Khan, T., Dominique, M. A., Fang, T. C., Canter, R. G., Roberts, C. J., Miller, K. R., Ransohoff, R. M., Trojanowski, J. Q., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0083-7 · Cited by 301 · see citing works
Bennett, R. E., Robbins, A. B., Hu, M., Cao, X., Betensky, R. A., Clark, T., Das, S., & Hyman, B. T. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1710329115 · Cited by 299 · see citing works
Bemiller, S. M., McCray, T. J., Allan, K., Formica, S. V., Xu, G., Wilson, G., Kokiko-Cochran, O. N., Crish, S. D., Lasagna-Reeves, C. A., Ransohoff, R. M., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0216-6 · Cited by 299 · see citing works
The role of microglia in processing and spreading of bioactive tau seeds in Alzheimer’s disease
Hopp, S. C., Lin, Y., Oakley, D., Roe, A. D., DeVos, S. L., Hanlon, D., & Hyman, B. T. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1309-z · Cited by 286 · see citing works
Self-citationSynaptic Tau Seeding Precedes Tau Pathology in Human Alzheimer’s Disease Brain
DeVos, S. L., Corjuc, B. T., Oakley, D. H., Nobuhara, C. K., Bannon, R. N., Chase, A., Commins, C., Gonzalez, J. A., Dooley, P. M., Frosch, M. P., et al. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00267 · Cited by 285 · see citing works
Activation of Microglia Acidifies Lysosomes and Leads to Degradation of Alzheimer Amyloid Fibrils
Majumdar, A., Cruz, D., Asamoah, N., Buxbaum, A., Sohar, I., Lobel, P., & Maxfield, F. R. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-10-0975 · Cited by 271 · see citing works
Microglial activation correlates in vivo with both tau and amyloid in Alzheimer’s disease
Dani, M., Wood, M., Mizoguchi, R., Fan, Z., Walker, Z., Morgan, R., Hinz, R., Biju, M., Kuruvilla, T., Brooks, D. J., et al. (2018) · Brain · doi:10.1093/brain/awy188 · Cited by 270 · see citing works
Microglial neuroinflammation contributes to tau accumulation in chronic traumatic encephalopathy
Cherry, J. D., Tripodis, Y., Alvarez, V. E., Huber, B., Kiernan, P. T., Daneshvar, D., Mez, J., Montenigro, P., Solomon, T. M., Alosco, M., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0382-8 · Cited by 267 · see citing works
Amphiphysin Heterodimers: Potential Role in Clathrin-mediated Endocytosis
Wigge, P., Köhler, K., Vallis, Y., Doyle, C. A., Owen, D. J., Hunt, S. P., & McMahon, H. T. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.10.2003 · Cited by 266 · see citing works
Loss of Bin1 Promotes the Propagation of Tau Pathology
Calafate, S., Flavin, W., Verstreken, P., & Moechars, D. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.063 · Cited by 265 · see citing works
Microglia and the aging brain: are senescent microglia the key to neurodegeneration?
Angelova, D. M., & Brown, D. R. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14860 · Cited by 262 · see citing works
Endocytic vesicle rupture is a conserved mechanism of cellular invasion by amyloid proteins
Flavin, W. P., Bousset, L., Green, Z. C., Chu, Y., Skarpathiotis, S., Chaney, M. J., Kordower, J. H., Melki, R., & Campbell, E. M. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1722-x · Cited by 254 · see citing works
TFEB enhances astroglial uptake of extracellular tau species and reduces tau spreading
Martini-Stoica, H., Cole, A. L., Swartzlander, D. B., Chen, F., Wan, Y.-W., Bajaj, L., Bader, D. A., Lee, V. M. Y., Trojanowski, J. Q., Liu, Z., et al. (2018) · Journal of Experimental Medicine · doi:10.1084/jem.20172158 · Cited by 253 · see citing works
Impact of TREM2R47H variant on tau pathology–induced gliosis and neurodegeneration
Gratuze, M., Leyns, C. E. G., Sauerbeck, A. D., St-Pierre, M.-K., Xiong, M., Kim, N., Serrano, J. R., Tremblay, M.-È., Kummer, T. T., Colonna, M., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci138179 · Cited by 252 · see citing works
Conformation Determines the Seeding Potencies of Native and Recombinant Tau Aggregates
Falcon, B., Cavallini, A., Angers, R. C., Glover, S. J., Murray, T. K., Barnham, L., Jackson, S., O'Neill, M. J., Isaacs, A. M., Hutton, M. L., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.589309 · Cited by 252 · see citing works
Siklos, M. I., BenAissa, M., & Thatcher, G. R. J. (2015) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2015.08.001 · Cited by 248 · see citing works
Clayton, K., Delpech, J. C., Herron, S., Iwahara, N., Ericsson, M., Saito, T., Saido, T. C., Ikezu, S., & Ikezu, T. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00440-9 · Cited by 245 · see citing works
Luo, W., Liu, W., Hu, X., Hanna, M., Caravaca, A., & Paul, S. M. (2015) · Scientific Reports · doi:10.1038/srep11161 · Cited by 241 · see citing works
Direct Evidence of Internalization of Tau by Microglia In Vitro and In Vivo
Bolós, M., Llorens-Martín, M., Jurado-Arjona, J., Hernández, F., Rábano, A., & Avila, J. (2016) · Journal of Alzheimer's Disease · doi:10.3233/jad-150704 · Cited by 234 · see citing works
Glymphatic system, AQP4, and their implications in Alzheimer’s disease
Silva, I., Silva, J., Ferreira, R., & Trigo, D. (2021) · Neurological Research and Practice · doi:10.1186/s42466-021-00102-7 · Cited by 234 · see citing works
Andreone, B. J., Przybyla, L., Llapashtica, C., Rana, A., Davis, S. S., van Lengerich, B., Lin, K., Shi, J., Mei, Y., Astarita, G., et al. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0650-6 · Cited by 233 · see citing works
A Brief Overview of Tauopathy: Causes, Consequences, and Therapeutic Strategies
Orr, M. E., Sullivan, A. C., & Frost, B. E. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.03.011 · Cited by 232 · see citing works
Absence of CX3CR1 impairs the internalization of Tau by microglia
Bolós, M., Llorens-Martín, M., Perea, J. R., Jurado-Arjona, J., Rábano, A., Hernández, F., & Avila, J. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0200-1 · Cited by 231 · see citing works
Sayed, F. A., Telpoukhovskaia, M., Kodama, L., Li, Y., Zhou, Y., Le, D., Hauduc, A., Ludwig, C., Gao, F., Clelland, C., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1811411115 · Cited by 229 · see citing works
Untangling Genetic Risk for Alzheimer’s Disease
Pimenova, A. A., Raj, T., & Goate, A. M. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.05.014 · Cited by 223 · see citing works
Iba, M., McBride, J. D., Guo, J. L., Zhang, B., Trojanowski, J. Q., & Lee, V. M.-Y. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1458-4 · Cited by 223 · see citing works
Microglial immunophenotype in dementia with Alzheimer’s pathology
CFAS, M., Minett, T., Classey, J., Matthews, F. E., Fahrenhold, M., Taga, M., Brayne, C., Ince, P. G., Nicoll, J. A. R., & Boche, D. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0601-z · Cited by 219 · see citing works
Activated microglia mitigate Aβ-associated tau seeding and spreading
Gratuze, M., Chen, Y., Parhizkar, S., Jain, N., Strickland, M. R., Serrano, J. R., Colonna, M., Ulrich, J. D., & Holtzman, D. M. (2021) · Journal of Experimental Medicine · doi:10.1084/jem.20210542 · Cited by 215 · see citing works
Dural lymphatics regulate clearance of extracellular tau from the CNS
Patel, T. K., Habimana-Griffin, L., Gao, X., Xu, B. J., Achilefu, S., Alitalo, K. K., McKee, C. A., Sheehan, P. W., Musiek, E. S., Xiong, C., et al. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0312-x · Cited by 215 · see citing works
Surface Functionality of Nanoparticles Determines Cellular Uptake Mechanisms in Mammalian Cells
Saha, K., Kim, S. T., Yan, B., Miranda, O. R., Alfonso, F. S., Shlosman, D., & Rotello, V. M. (2012) · Small · doi:10.1002/smll.201201129 · Cited by 214 · see citing works
Microglial calcium signaling is attuned to neuronal activity in awake mice
Umpierre, A. D., Bystrom, L. L., Ying, Y., Liu, Y., Worrell, G. A., & Wu, L. (2020) · eLife · doi:10.7554/elife.56502 · Cited by 208 · see citing works
Inflammatory changes parallel the early stages of Alzheimer disease
Parachikova, A., Agadjanyan, M. G., Cribbs, D. H., Blurton-Jones, M., Perreau, V., Rogers, J., Beach, T. G., & Cotman, C. W. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.08.014 · Cited by 203 · see citing works
Tauopathies as clinicopathological entities
Irwin, D. J. (2015) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2015.09.020 · Cited by 200 · see citing works
Anti-inflammatory Mechanisms Triggered by Apoptotic Cells during Their Clearance
Szondy, Z., Sarang, Z., Kiss, B., Garabuczi, É., & Köröskényi, K. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00909 · Cited by 195 · see citing works
Brelstaff, J., Tolkovsky, A. M., Ghetti, B., Goedert, M., & Spillantini, M. G. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.07.072 · Cited by 195 · see citing works
Congdon, E. E., Gu, J., Sait, H. B. R., & Sigurdsson, E. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.491001 · Cited by 195 · see citing works
P2X7 receptor regulation of non-classical secretion from immune effector cells
Dubyak, G. (2012) · Cellular Microbiology · doi:10.1111/cmi.12001 · Cited by 189 · see citing works
Tau Oligomers Impair Artificial Membrane Integrity and Cellular Viability
Flach, K., Hilbrich, I., Schiffmann, A., Gärtner, U., Krüger, M., Leonhardt, M., Waschipky, H., Wick, L., Arendt, T., & Holzer, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.396176 · Cited by 188 · see citing works
Ramjaun, A. R., & McPherson, P. S. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70062369.x · Cited by 183 · see citing works
Beta-amyloid activates NLRP3 inflammasome via TLR4 in mouse microglia
Liu, Y., Dai, Y., Li, Q., Chen, C., Chen, H., Song, Y., Hua, F., & Zhang, Z. (2020) · Neuroscience Letters · doi:10.1016/j.neulet.2020.135279 · Cited by 183 · see citing works
Insights into TREM2 biology by network analysis of human brain gene expression data
Forabosco, P., Ramasamy, A., Trabzuni, D., Walker, R., Smith, C., Bras, J., Levine, A. P., Hardy, J., Pocock, J. M., Guerreiro, R., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.05.001 · Cited by 180 · see citing works
Castillo‐Carranza, D. L., Gerson, J. E., Sengupta, U., Guerrero‐Munoz, M. J., Lasagna‐Reeves, C. A., & Kayed, R. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132477 · Cited by 180 · see citing works
TREM2 modifies microglial phenotype and provides neuroprotection in P301S tau transgenic mice
Jiang, T., Zhang, Y.-D., Chen, Q., Gao, Q., Zhu, X.-C., Zhou, J.-S., Shi, J.-Q., Lu, H., Tan, L., & Yu, J.-T. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.01.028 · Cited by 176 · see citing works
Soluble phospho-tau from Alzheimer’s disease hippocampus drives microglial degeneration
Sanchez-Mejias, E., Navarro, V., Jimenez, S., Sanchez-Mico, M., Sanchez-Varo, R., Nuñez-Diaz, C., Trujillo-Estrada, L., Davila, J. C., Vizuete, M., Gutierrez, A., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1630-5 · Cited by 175 · see citing works
Gerhard, A., Trender‐Gerhard, I., Turkheimer, F., Quinn, N. P., Bhatia, K. P., & Brooks, D. J. (2006) · Movement Disorders · doi:10.1002/mds.20668 · Cited by 171 · see citing works
BIN1 favors the spreading of Tau via extracellular vesicles
Crotti, A., Sait, H. R., McAvoy, K. M., Estrada, K., Ergun, A., Szak, S., Marsh, G., Jandreski, L., Peterson, M., Reynolds, T. L., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-45676-0 · Cited by 171 · see citing works
Profiling senescent cells in human brains reveals neurons with CDKN2D/p19 and tau neuropathology
Dehkordi, S. K., Walker, J., Sah, E., Bennett, E., Atrian, F., Frost, B., Woost, B., Bennett, R. E., Orr, T. C., Zhou, Y., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00142-3 · Cited by 169 · see citing works
Microglial secreted cathepsin B induces neuronal apoptosis
Kingham, P. J., & Pocock, J. M. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00146.x · Cited by 168 · see citing works
Grommes, C., Lee, C. Y. D., Wilkinson, B. L., Jiang, Q., Koenigsknecht-Talboo, J. L., Varnum, B., & Landreth, G. E. (2008) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-007-9090-2 · Cited by 162 · see citing works
Tau Oligomers and Fibrils Induce Activation of Microglial Cells
Morales, I., Jiménez, J. M., Mancilla, M., & Maccioni, R. B. (2013) · Journal of Alzheimer’s Disease · doi:10.3233/jad-131843 · Cited by 160 · see citing works
Accumulation of tau induced in neurites by microglial proinflammatory mediators
Gorlovoy, P., Larionov, S., Pham, T. T. H., & Neumann, H. (2009) · The FASEB Journal · doi:10.1096/fj.08-123877 · Cited by 156 · see citing works
Sayed, F. A., Kodama, L., Fan, L., Carling, G. K., Udeochu, J. C., Le, D., Li, Q., Zhou, L., Wong, M. Y., Horowitz, R., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abe3947 · Cited by 155 · see citing works
Bendiske, J., & Bahr, B. A. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.5.451 · Cited by 153 · see citing works
Feng, W., Zhang, Y., Wang, Z., Xu, H., Wu, T., Marshall, C., Gao, J., & Xiao, M. (2020) · Alzheimer's Research & Therapy · doi:10.1186/s13195-020-00688-1 · Cited by 150 · see citing works
Canton, J., Schlam, D., Breuer, C., Gütschow, M., Glogauer, M., & Grinstein, S. (2016) · Nature Communications · doi:10.1038/ncomms11284 · Cited by 148 · see citing works
In vivo imaging of microglial activation with [11C](R)‐PK11195 PET in corticobasal degeneration
Gerhard, A., Watts, J., Trender‐Gerhard, I., Turkheimer, F., Banati, R. B., Bhatia, K. P., & Brooks, D. J. (2004) · Movement Disorders · doi:10.1002/mds.20162 · Cited by 145 · see citing works
Selective suppression of the α isoform of p38 MAPK rescues late-stage tau pathology
Maphis, N., Jiang, S., Xu, G., Kokiko-Cochran, O. N., Roy, S. M., Van Eldik, L. J., Watterson, D. M., Lamb, B. T., & Bhaskar, K. (2016) · Alzheimer's Research & Therapy · doi:10.1186/s13195-016-0221-y · Cited by 144 · see citing works
Physical Constraints and Forces Involved in Phagocytosis
Jaumouillé, V., & Waterman, C. M. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01097 · Cited by 144 · see citing works
Slepnev, V. I., Ochoa, G.-C., Butler, M. H., & Camilli, P. V. D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910430199 · Cited by 142 · see citing works
Macropinocytosis: New Insights Into Its Underappreciated Role in Innate Immune Cell Surveillance
Canton, J. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02286 · Cited by 138 · see citing works
Ando, K., Brion, J.-P., Stygelbout, V., Suain, V., Authelet, M., Dedecker, R., Chanut, A., Lacor, P., Lavaur, J., Sazdovitch, V., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1111-z · Cited by 136 · see citing works
Brelstaff, J. H., Mason, M., Katsinelos, T., McEwan, W. A., Ghetti, B., Tolkovsky, A. M., & Spillantini, M. G. (2021) · Science Advances · doi:10.1126/sciadv.abg4980 · Cited by 135 · see citing works
The endocytic pathway in microglia during health, aging and Alzheimer’s disease
Solé-Domènech, S., Cruz, D. L., Capetillo-Zarate, E., & Maxfield, F. R. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.07.002 · Cited by 133 · see citing works
Removing endogenous tau does not prevent tau propagation yet reduces its neurotoxicity
Wegmann, S., Maury, E. A., Kirk, M. J., Saqran, L., Roe, A., DeVos, S. L., Nicholls, S., Fan, Z., Takeda, S., Cagsal‐Getkin, O., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201592748 · Cited by 132 · see citing works
Niewiadomska, G., Niewiadomski, W., Steczkowska, M., & Gąsiorowska, A. (2021) · Life · doi:10.3390/life11010028 · Cited by 132 · see citing works
Polanco, J. C., Hand, G. R., Briner, A., Li, C., & Götz, J. (2021) · Acta Neuropathologica · doi:10.1007/s00401-020-02254-3 · Cited by 132 · see citing works
Phagocytosis of full-length Tau oligomers by Actin-remodeling of activated microglia
Das, R. R., Balmik, A. A., & Chinnathambi, S. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-019-1694-y · Cited by 129 · see citing works
In vivo rate-determining steps of tau seed accumulation in Alzheimer’s disease
Meisl, G., Hidari, E., Allinson, K., Rittman, T., DeVos, S. L., Sanchez, J. S., Xu, C. K., Duff, K. E., Johnson, K. A., Rowe, J. B., et al. (2021) · Science Advances · doi:10.1126/sciadv.abh1448 · Cited by 127 · see citing works
Lee, S.-H., Le Pichon, C. E., Adolfsson, O., Gafner, V., Pihlgren, M., Lin, H., Solanoy, H., Brendza, R., Ngu, H., Foreman, O., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.06.099 · Cited by 125 · see citing works
Neuroinflammatory Signals in Alzheimer Disease and APP/PS1 Transgenic Mice
López‐González, I., Schlüter, A., Aso, E., Garcia‐Esparcia, P., Ansoleaga, B., Llorens, F., Carmona, M., Moreno, J. R., Fuso, A., Portero‐Otín, M., et al. (2015) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000176 · Cited by 125 · see citing works
Tse, S. M. L., Furuya, W., Gold, E., Schreiber, A. D., Sandvig, K., Inman, R. D., & Grinstein, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207966200 · Cited by 124 · see citing works
Schuh, C., Wimmer, I., Hametner, S., Haider, L., van Dam, A., Liblau, R., Smith, K. J., Probert, L., Binder, C., Bauer, J., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1263-5 · Cited by 123 · see citing works
Phosphatidic acid is required for the constitutive ruffling and macropinocytosis of phagocytes
Bohdanowicz, M., Schlam, D., Hermansson, M., Rizzuti, D., Fairn, G. D., Ueyama, T., Somerharju, P. J., Du, G., & Grinstein, S. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-11-0789 · Cited by 119 · see citing works
Ni, J., Wu, Z., Peterts, C., Yamamoto, K., Qing, H., & Nakanishi, H. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.1599-15.2015 · Cited by 118 · see citing works
Jaworski, T., Lechat, B., Demedts, D., Gielis, L., Devijver, H., Borghgraef, P., Duimel, H., Verheyen, F., Kügler, S., & LEUVEN, F. V. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.06.025 · Cited by 116 · see citing works
Conway, O. J., Carrasquillo, M. M., Wang, X., Bredenberg, J. M., Reddy, J. S., Strickland, S. L., Younkin, C. S., Burgess, J. D., Allen, M., Lincoln, S. J., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0289-x · Cited by 112 · see citing works
Jiang, T., Tan, L., Zhu, X.-C., Zhou, J.-S., Cao, L., Tan, M.-S., Wang, H.-F., Chen, Q., Zhang, Y.-D., & Yu, J.-T. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.08.019 · Cited by 111 · see citing works
Distinct Therapeutic Mechanisms of Tau Antibodies
Funk, K. E., Mirbaha, H., Jiang, H., Holtzman, D. M., & Diamond, M. I. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.657924 · Cited by 111 · see citing works
Cytosolic Proteolysis of τ by Cathepsin D in Hippocampus Following Suppression of Cathepsins B and L
Bednarski, E., & LYNCH, G. S. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67051846.x · Cited by 110 · see citing works
Ayalon, G., Lee, S.-H., Adolfsson, O., Foo‐Atkins, C., Atwal, J. K., Blendstrup, M., Booler, H. S., Bravo, J., Brendza, R. P., Brunstein, F., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abb2639 · Cited by 108 · see citing works
Tau reduction in the presence of amyloid-β prevents tau pathology and neuronal death in vivo
DeVos, S. L., Corjuc, B. T., Commins, C., Dujardin, S., Bannon, R. N., Corjuc, D., Moore, B. D., Bennett, R. E., Jorfi, M., Gonzales, J. A., et al. (2018) · Brain · doi:10.1093/brain/awy117 · Cited by 106 · see citing works
Corticobasal degeneration and corticobasal syndrome: A review
Constantinides, V. C., Paraskevas, G. P., Paraskevas, P. G., Stefanis, L., & Kapaki, E. N. (2019) · Clinical Parkinsonism & Related Disorders · doi:10.1016/j.prdoa.2019.08.005 · Cited by 99 · see citing works
Tau‐66: evidence for a novel tau conformation in Alzheimer's disease
Ghoshal, N., García‐Sierra, F., Fu, Y., Beckett, L. A., Mufson, E. J., Kuret, J., Berry, R. W., & Binder, L. I. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00346.x · Cited by 97 · see citing works
Rexach, J. E., Polioudakis, D., Yin, A., Swarup, V., Chang, T. S., Nguyen, T., Sarkar, A., Chen, L., Huang, J., Lin, L.-C., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108398 · Cited by 94 · see citing works
Filamentous recombinant human Tau activates primary astrocytes via an integrin receptor complex
Wang, P., & Ye, Y. (2021) · Nature Communications · doi:10.1038/s41467-020-20322-w · Cited by 93 · see citing works
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Microbiota–gut–brain axis and its therapeutic applications in neurodegenerative diseases
Loh, J. S., Mak, W. Q., Tan, L. K. S., Ng, C. X., Chan, H. H., Yeow, S. H., Foo, J. B., Ong, Y. S., How, C. W., & Khaw, K. Y. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01743-1 · Cited by 1,193 · see citing works
Neuroinflammation across neurological diseases
Shi, F., & Yong, V. W. (2025) · Science · doi:10.1126/science.adx0043 · Cited by 312 · see citing works
Quick, J. D., Silva, C., Wong, J. H., Lim, K. L., Reynolds, R., Barron, A. M., Zeng, J., & Lo, C. H. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02866-y · Cited by 203 · see citing works
Tau in neurodegenerative diseases: molecular mechanisms, biomarkers, and therapeutic strategies
Zhang, X., Wang, J., Zhang, Z., & Ye, K. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00429-6 · Cited by 106 · see citing works
The Yin and Yang of Microglia-Derived Extracellular Vesicles in CNS Injury and Diseases
Ghosh, M., & Pearse, D. D. (2024) · Cells · doi:10.3390/cells13221834 · Cited by 65 · see citing works
Beyond Amyloid and Tau: The Critical Role of Microglia in Alzheimer’s Disease Therapeutics
Dias, D., & Socodato, R. (2025) · Biomedicines · doi:10.3390/biomedicines13020279 · Cited by 57 · see citing works
Appleton, J., Finn, Q., Zanotti-Fregonara, P., Yu, M., Faridar, A., Nakawah, M. O., Zarate, C., Carrillo, M. C., Dickerson, B. C., Rabinovici, G. D., et al. (2025) · Brain · doi:10.1093/brain/awae234 · Cited by 58 · see citing works
Tau induces inflammasome activation and microgliosis through acetylating NLRP3
Zhang, L., Gai, Y., Liu, Y., Meng, D., Zeng, Y., Luo, Y., Zhang, H., Wang, Z., Yang, M., Li, Y., et al. (2024) · Clinical and Translational Medicine · doi:10.1002/ctm2.1623 · Cited by 50 · see citing works
Granzyme K+ CD8 T cells slow tauopathy progression by targeting microglia
Mason, H. D., Latour, Y. L., Boughter, C. T., Johnson, K. R., Maric, D., Dorrier, C., Guedes, V. A., Lai, C., Duncker, P. C., Johnson, A. M., et al. (2025) · Nature Immunology · doi:10.1038/s41590-025-02198-4 · Cited by 44 · see citing works
Kim, S., Sharma, C., Jung, U. J., & Kim, S. R. (2023) · Biomedicines · doi:10.3390/biomedicines11051383 · Cited by 40 · see citing works
Post-mortem validation of in vivo TSPO PET as a microglial biomarker
Wijesinghe, S. S., Rowe, J. B., Mason, H. D., Allinson, K. S. J., Thomas, R., Vontobel, D. S., Fryer, T. D., Hong, Y. T., Bacioglu, M., Spillantini, M. G., et al. (2025) · Brain · doi:10.1093/brain/awaf078 · Cited by 37 · see citing works
Donison, N. S., Palik, J., Volkening, K., & Strong, M. J. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00842-z · Cited by 39 · see citing works
Tubulin Cytoskeleton in Neurodegenerative Diseases–not Only Primary Tubulinopathies
Cyske, Z., Gaffke, L., Pierzynowska, K., & Węgrzyn, G. (2022) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-022-01304-6 · Cited by 32 · see citing works
Ghimire, A., Rehman, S. A., Subhani, A., Khan, M. A., Rahman, Z., Iqubal, M. K., & Iqubal, A. (2025) · hLife · doi:10.1016/j.hlife.2024.11.006 · Cited by 30 · see citing works
Shen, X., Li, H., Zhang, B., Li, Y., & Zhu, Z. (2025) · Cells · doi:10.3390/cells14191506 · Cited by 32 · see citing works
Yue, W., Deng, X., Wang, Z., Jiang, M., Hu, R., Duan, Y., Wang, Q., Cui, J., & Fang, Y. (2023) · Immunity & Ageing · doi:10.1186/s12979-023-00354-8 · Cited by 26 · see citing works
Microglia internalize tau monomers and fibrils using distinct receptors but similar mechanisms
Falkon, K. F., Danford, L., Kuri, E. G., Esquinca‐Moreno, P., Señeriz, Y. L. P., Smith, S. A., Wickline, J. L., Louwrier, A., McPhail, J. A., Sayre, N. L., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14418 · Cited by 25 · see citing works
Self-citationAmyloid beta and tau are associated with the dual effect of neuroinflammation on neurodegeneration
Povala, G., Bellaver, B., Bastiani, M. A. D., Ferrari‐Souza, J. P., Aguzzoli, C. S., Leffa, D. T., Ferreira, P. C. L., Lussier, F. Z., da Rocha, A. S., Zalzale, H., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70746 · Cited by 24 · see citing works
Hromádková, L., Siddiqi, M. K., Liu, H., & Safar, J. (2022) · Cells · doi:10.3390/cells11192997 · Cited by 19 · see citing works
Halicki, M. J., Hind, K., & Chazot, P. L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241612556 · Cited by 18 · see citing works
Complement receptor 4 mediates the clearance of extracellular tau fibrils by microglia
Yoo, C. J., Choi, Y., Bok, E., Lin, Y., Cheon, M., Lee, Y., & Kim, J. (2024) · FEBS Journal · doi:10.1111/febs.17150 · Cited by 15 · see citing works
Internalization of extracellular Tau oligomers in Alzheimer’s disease
Chinnathambi, S., Rangappa, N., & Chandrashekar, M. (2025) · Advances in clinical chemistry · doi:10.1016/bs.acc.2025.01.005 · Cited by 14 · see citing works
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 14 · see citing works
Shultz, A., Vincze, A., Yau, T. T., Poirier, E. L., Demanche, H., & Rauch, J. N. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.107058 · Cited by 12 · see citing works
Singhaarachchi, P. H., Antal, P., Calon, F., Culmsee, C., Delpech, J.-C., Feldotto, M., Geertsema, J., Hoeksema, E. E., Kőrösi, A., Layé, S., et al. (2025) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2025.102821 · Cited by 11 · see citing works
Proteostasis and Neuroinflammation in Alzheimer’s Disease
Potokiri, A., & Wang, H. (2025) · Journal of Integrative Neuroscience · doi:10.31083/jin39826 · Cited by 9 · see citing works
Diverse influences on tau aggregation and implications for disease progressionPreprint
Alstyne, M. V., Pratt, J., & Parker, R. (2025) · Genes & Development · doi:10.1101/gad.352551.124 · Cited by 10 · see citing works
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 9 · see citing works
The Adult Neurogenesis Theory of Alzheimer’s Disease
Abbate, C. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-221279 · Cited by 8 · see citing works
Schreiner, T. G., Ciobanu, R. C., & Schreiner, O. D. (2026) · Biomedicines · doi:10.3390/biomedicines14030522 · Cited by 6 · see citing works
Recent insights from non-mammalian models of brain injuries: an emerging literature
Katchur, N. J., & Notterman, D. A. (2024) · Frontiers in Neurology · doi:10.3389/fneur.2024.1378620 · Cited by 6 · see citing works
Zhang, W., Xu, J., Dong, J., Huang, Z., & Cao, L. (2022) · Neuroscience Bulletin · doi:10.1007/s12264-022-01002-9 · Cited by 4 · see citing works
Neuroimmune Dysfunction in Alzheimer’s Disease and Other Forms of Dementia
Yamane, T., Yoshioka, T., & Shimo, Y. (2024) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c23-00464 · Cited by 4 · see citing works
Zhang, D.-Q., Yang, X., Niu, H.-B., Sun, X.-C., Cao, D., Li, A., Yue, J., Li, X.-L., & Zhang, Q. (2025) · Current Alzheimer Research · doi:10.2174/0115672050351995241223065923 · Cited by 3 · see citing works
King, K. E., Haeri, M., Swerdlow, R. H., & Wozniak, A. L. (2025) · Molecular Biology of the Cell · doi:10.1091/mbc.e24-04-0182 · Cited by 3 · see citing works
Xing, L., Liu, A., Gao, W., Li, J., Yao, M., Song, J., Duan, P., & Li, H. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71330 · Cited by 3 · see citing works
Role of non-neuronal cells in neurorepair: a focus on proteinopathy and neurodegeneration
Rodríguez-Carreiro, S., Nogales, M. D. C., Jiménez-Galán, D., Carmona-Lorenzo, S., Caro-Martín, A., Navarro, E., & Esteras, N. (2024) · Regenerative medicine reports . · doi:10.4103/regenmed.regenmed-d-24-00005 · Cited by 3 · see citing works
Hydromethylthionine sustains truncated tau‐dependent inflammation‐lowering effects in mouse brain
Santos, R. X., Lee, S. H., Lofthouse, R. A., Melis, V., Robinson, L., Leith, M., Dreesen, E., Armstrong, P., Vorley, T., Goatman, E. A., et al. (2025) · FEBS Journal · doi:10.1111/febs.70021 · Cited by 3 · see citing works
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 · see citing works
Amyloid and tau pathologies cross-talk to promote Alzheimeŕs disease: novel mechanistic insights
Ávila, J., Hernández, F., & Perry, G. L. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.07.025 · Cited by 3 · see citing works
Laloli, K. J., Rentsch, P., Stayte, S., & Vissel, B. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1682979 · Cited by 2 · see citing works
Gautam, A. S., Anju, K., & Singh, R. K. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.150856 · Cited by 2 · see citing works
Wang, D., Zhao, D., & Li, X. (2026) · International Journal of General Medicine · doi:10.2147/ijgm.s600123 · Cited by 1 · see citing works
Microglial state transitions are constrained by developmental and metabolic checkpoints
Mesaoudi, A. E., & Kim, D. W. (2026) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2026.1852176 · Cited by 1 · see citing works
TLR4-mediated chronic neuroinflammation has no effect on tangle pathology in a tauopathy mouse model
Basheer, N., Muhammadi, M. K., Freites, C. L., Avila, M., Momand, M. U. D., Hryntsova, N. B., Smolek, T., Katina, S., & Žilka, N. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1468602 · Cited by 1 · see citing works
Yue, W., Deng, X., Wang, Z., Jiang, M., Hu, R., Duan, Y., Wang, Q., Cui, J., & Fang, Y. (2023) · Figshare · doi:10.6084/m9.figshare.23550334
Molecular Modeling Insights on the Pharmaceuticals and Hypotheses of Alzheimer’s Disease
de Castro, A. A., Silva, H. F., Garcia, M. V. F. P., Homem‐de‐Mello, P., & Ramalho, T. C. (2024) · Current Medicinal Chemistry · doi:10.2174/0109298673318143240823064403
Amyloid-Beta, Tau, and Microglial Activation in Aged Felid Brains
Kulik, V., Edler, M., Raghanti, M., Imam, A., & Sherwood, C. (2024) · The Journal of comparative neurology · doi:10.1002/cne.25679 · Cited by 1 · see citing works
Protein kinase CK2α’ as a dual modulator of immune signaling and synaptic dysfunction in TauopathyPreprint
White, A., Gavrilyuk, P., Gu, P., Moya, R. F., Thurston, R., Fickak, A., Rozema, N. B., Keshavaram, P., Vermilyea, S., Schlichte, R., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.24.661391
White, A., Gavrilyuk, P., Gu, P., Moya, R. F., Thurston, R. H., Fickak, A., Rozema, N. B., Keshavaram, P., Vermilyea, S., Schlichte, R., et al. (2026) · Translational Neurodegeneration · doi:10.1186/s40035-026-00563-3
Yue, W., Deng, X., Wang, Z., Jiang, M., Hu, R., Duan, Y., Wang, Q., Cui, J., & Fang, Y. (2023) · Figshare · doi:10.6084/m9.figshare.23550331
Extracellular Protein Quality Control in Tau Pathology
Bhunia, P. K., Verma, D., Vimal, P., & Kasturi, P. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05834-8
Actin cytoskeletal pathology in Alzheimer’s disease
Chinnathambi, S., Malik, S., Chandrashekar, M., & Rangappa, N. (2026) · Advances in pharmacology · doi:10.1016/bs.apha.2025.12.003
Jia, H., 孟永海, Zhao, N., & Liu, Y. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-11780-4
Lucy, T. T., Mamun-Or-Rashid, A. N. M., Lee, D. C., Lefterov, I. M., Koldamova, R. P., & Fitz, N. F. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27115050
Neuroinflammation and Tauopathies
Zeenny, M.-N., Salame, I., Maatouk, L., & Akoury, E. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-12253-4
Chinnathambi, S., Baisya, U., & Ananthanarayana, V. (2026) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2026.07.004
Tau-mediated Mechanisms in Alzheimerʼs Disease Pathogenesis
Narayanappa, T. S., Ananthanarayana, V., & Chinnathambi, S. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-06057-7
Therapeutic targeting of tauopathies: From druggable biology to precision intervention
Zhang, C., Ma, J., Wu, X., Wang, X., Huang, X., Zheng, H., & Zhao, Y. (2026) · Pharmacological Research · doi:10.1016/j.phrs.2026.108432
Wang, H., Fan, X., Ping, J., Shao, Q., Cai, W., Wang, H., Ji, Q., Su, M., & Qian, W. (2026) · Translational Neurodegeneration · doi:10.1186/s40035-026-00590-0
Microglial regulation of extracellular Tau dynamics in Alzheimer’s disease
Narayanappa, T. S., & Chinnathambi, S. (2026) · Advances in pharmacology · doi:10.1016/bs.apha.2026.08.006
- Authors
- Odfalk, K. F., Bieniek, K. F., & Hopp, S. C.
- Affiliations
- The University of Texas at San Antonio Health Science Center (US)
- Corresponding author
- Hopp, Sarah C.
- Venue
- Progress in Neurobiology
- Publisher
- Elsevier BV
- Published
- 2022-09
- Volume
- 216
- Pages
- 102306
- ISSN
- 0301-0082 (ISSN-L)
- PMC
- PMC9378545
- OpenAlex
- W4282841274
- Cited by
- 60
- References
- 265
- Citations by year
- 2026: 17 · 2025: 19 · 2024: 13 · 2023: 8 · 2022: 3
- FWCI
- 1.51
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (am, 480 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Progress in Neurobiology (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (K01AG066747, R21AG072423, R01AG062348, R01AG070214, P30AG066546)
- National Institute of Neurological Disorders and Stroke (T32NS082145, R01NS017950)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Neuroscience › Neurology › Neurological Disease Mechanisms and Treatments
- Keywords
- microglia, tauopathy, tau aggregation, Alzheimer's disease, tau seeding, neuroinflammation, tau spread, exosomes, anti-tau antibodies, tau-targeted therapy
- MeSH terms
- Alzheimer Disease, Brain, Humans, Neurons, tau Proteins, Microglia, Tauopathies
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