Microglia modulate neurodegeneration in Alzheimer’s and Parkinson’s diseases

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

Microglia Sculpt Postnatal Neural Circuits in an Activity and Complement-Dependent Manner

Schafer, D. P., Lehrman, E. K., Kautzman, A. G., Koyama, R., Mardinly, A. R., Yamasaki, R., Ransohoff, R. M., Greenberg, M. E., Barres, B. A., & Stevens, B. (2012) · Neuron · doi:10.1016/j.neuron.2012.03.026 · Cited by 4,089

Cognitive reserve in ageing and Alzheimer's disease

Stern, Y. (2012) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70191-6 · Cited by 3,557

Complement and microglia mediate early synapse loss in Alzheimer mouse models

Hong, S., Beja-Glasser, V. F., Nfonoyim, B. M., Frouin, A., Li, S., Ramakrishnan, S., Merry, K. M., Shi, Q., Rosenthal, A., Barres, B. A., et al. (2016) · Science · doi:10.1126/science.aad8373 · Cited by 3,343

Genetic meta-analysis of diagnosed Alzheimer’s disease identifies new risk loci and implicates Aβ, tau, immunity and lipid processing

Alzheimer Disease Genetics Consortium (ADGC), Kunkle, B. W., The European Alzheimer’s Disease Initiative (EADI), Cohorts for Heart and Aging Research in Genomic Epidemiology Consortium (CHARGE), Genetic and Environmental Risk in AD/Defining Genetic, P. A. E. R. F. A. D. C. (., Grenier-Boley, B., Sims, R., Bis, J. C., Damotte, V., Naj, A. C., et al. (2019) · Nature Genetics · doi:10.1038/s41588-019-0358-2 · Cited by 2,946

Microglia promote learning-dependent synapse formation through brain-derived neurotrophic factor

Parkhurst, C. N., Yang, G., Ninan, I., Savas, J. N., Yates, J. R., Lafaille, J. J., Hempstead, B. L., Littman, D. R., & Gan, W.-B. (2013) · Cell · doi:10.1016/j.cell.2013.11.030 · Cited by 2,599

Multicenter Analysis of Glucocerebrosidase Mutations in Parkinson's Disease

Sidransky, E., Nalls, M. A., Aasly, J. O., Aharon-Peretz, J., Annesi, G., Barbosa, E. R., Bar-Shira, A., Berg, D., Bras, J., Brice, A., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0901281 · Cited by 2,135

TREM2 Lipid Sensing Sustains the Microglial Response in an Alzheimer’s Disease Model

Wang, Y., Cella, M., Mallinson, K., Ulrich, J. D., Young, K. L., Robinette, M. L., Gilfillan, S., Krishnan, G. M., Sudhakar, S., Zinselmeyer, B. H., et al. (2015) · Cell · doi:10.1016/j.cell.2015.01.049 · Cited by 1,736

Molecular diversity and specializations among the cells of the adult mouse brain

Saunders, A., Macosko, E. Z., Wysoker, A., Goldman, M., Krienen, F. M., de Rivera, H., Bien, E., Baum, M., Bortolin, L., Wang, S., et al. (2018) · Cell · doi:10.1016/j.cell.2018.07.028 · Cited by 1,531

Transneuronal Propagation of Pathologic α-Synuclein from the Gut to the Brain Models Parkinson’s Disease

Kim, S., Kwon, S.-H., Kam, T.-I., Panicker, N., Karuppagounder, S. S., Lee, S., Lee, J. H., Kim, W. R., Kook, M., Foss, C. A., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.05.035 · Cited by 1,397

Lipid-droplet-accumulating microglia represent a dysfunctional and proinflammatory state in the aging brain

Marschallinger, J., Iram, T., Zardeneta, M., Lee, S. E., Lehallier, B., Haney, M. S., Pluvinage, J. V., Mathur, V., Hahn, O., Morgens, D. W., et al. (2020) · Nature Neuroscience · doi:10.1038/s41593-019-0566-1 · Cited by 1,384

Gaucher disease glucocerebrosidase and α-synuclein form a bidirectional pathogenic loop in synucleinopathies

Mazzulli, J. R., Xu, Y.-H., Sun, Y., Knight, A. L., McLean, P. J., Caldwell, G. A., Sidransky, E., Grabowski, G. A., & Krainc, D. (2011) · Cell · doi:10.1016/j.cell.2011.06.001 · Cited by 1,341

TREM2 Maintains Microglial Metabolic Fitness in Alzheimer’s Disease

Ulland, T. K., Song, W. M., Huang, S. C.-C., Ulrich, J. D., Sergushichev, A., Beatty, W. L., Loboda, A. A., Zhou, Y., Cairns, N. J., Kambal, A., et al. (2017) · Cell · doi:10.1016/j.cell.2017.07.023 · Cited by 1,263

Inhibitory Interneuron Deficit Links Altered Network Activity and Cognitive Dysfunction in Alzheimer Model

Verret, L., Mann, E. O., Hang, G. B., Barth, A. M. I., Cobos, I., Ho, K., Devidze, N., Masliah, E., Kreitzer, A. C., Mody, I., et al. (2012) · Cell · doi:10.1016/j.cell.2012.02.046 · Cited by 1,216

Block of A1 astrocyte conversion by microglia is neuroprotective in models of Parkinson’s disease

Yun, S. P., Kam, T.-I., Panicker, N., Kim, S., Oh, Y., Park, J.-S., Kwon, S.-H., Park, Y. J., Karuppagounder, S. S., Park, H., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0051-5 · Cited by 1,123

Hippocampal synaptic loss in early Alzheimer's disease and mild cognitive impairment

Scheff, S. W., Price, D. A., Schmitt, F. A., & Mufson, E. J. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.09.012 · Cited by 1,017

Glial Lipid Droplets and ROS Induced by Mitochondrial Defects Promote Neurodegeneration

Liu, L., Zhang, K., Sandoval, H., Yamamoto, S., Jaiswal, M., Sanz, E., Li, Z., Hui, J., Graham, B. H., Quintana, A., et al. (2015) · Cell · doi:10.1016/j.cell.2014.12.019 · Cited by 876

Oxidant stress evoked by pacemaking in dopaminergic neurons is attenuated by DJ-1

Guzmán, J. N., Sánchez-Padilla, J., Wokosin, D. L., Kondapalli, J., Ilijić, E., Schumacker, P. T., & Surmeier, D. J. (2010) · Nature · doi:10.1038/nature09536 · Cited by 864

Parkinson's Disease and Parkinsonism: Neuropathology

Dickson, D. W. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009258 · Cited by 847

Neuron-Astrocyte Metabolic Coupling Protects against Activity-Induced Fatty Acid Toxicity

Ioannou, M. S., Jackson, J., Sheu, S.-H., Chang, C.-L., Weigel, A. V., Liu, H., Pasolli, H. A., Xu, C. S., Pang, S., Matthies, D., et al. (2019) · Cell · doi:10.1016/j.cell.2019.04.001 · Cited by 760

TREM2 regulates microglial cholesterol metabolism upon chronic phagocytic challenge

Nugent, A. A., Lin, K., van Lengerich, B., Lianoglou, S., Przybyla, L., Davis, S. S., Llapashtica, C., Wang, J., Kim, D. J., Xia, D., et al. (2020) · Neuron · doi:10.1016/j.neuron.2019.12.007 · Cited by 745

Brain cell type–specific enhancer–promoter interactome maps and disease - risk association

Nott, A., Holtman, I. R., Coufal, N. G., Schlachetzki, J. C. M., Yu, M., Hu, R., Han, C. Z., Pena, M., Xiao, J., Wu, Y., et al. (2019) · Science · doi:10.1126/science.aay0793 · Cited by 699

The Microglial Innate Immune Receptor TREM2 Is Required for Synapse Elimination and Normal Brain Connectivity

Filipello, F., Morini, R., Corradini, I., Zerbi, V., Canzi, A., Michalski, B., Erreni, M., Markicevic, M., Starvaggi-Cucuzza, C., Otero, K., et al. (2018) · Immunity · doi:10.1016/j.immuni.2018.04.016 · Cited by 695

Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3

Mao, X., Ou, M. T., Karuppagounder, S. S., Kam, T.-I., Yin, X., Xiong, Y., Ge, P., Umanah, G. E., Brahmachari, S., Shin, J.-H., et al. (2016) · Science · doi:10.1126/science.aah3374 · Cited by 690

Microglia monitor and protect neuronal function through specialized somatic purinergic junctions

Cserép, C., Pósfai, B., Lénárt, N., Fekete, R., László, Z. I., Lele, Z., Orsolits, B., Molnár, G., Heindl, S., Schwarcz, A. D., et al. (2020) · Science · doi:10.1126/science.aax6752 · Cited by 684

A vicious cycle of β amyloid−dependent neuronal hyperactivation

Zott, B., Simon, M. M., Hong, W., Unger, F., Chen-Engerer, H.-J., Frosch, M. P., Sakmann, B., Walsh, D. M., & Konnerth, A. (2019) · Science · doi:10.1126/science.aay0198 · Cited by 640

Microglia mediate forgetting via complement-dependent synaptic elimination

Wang, C., Yue, H., Hu, Z., Shen, Y., Ma, J., Li, J., Wang, X.-D., Wang, L., Sun, B., Shi, P., et al. (2020) · Science · doi:10.1126/science.aaz2288 · Cited by 629

Microglial Remodeling of the Extracellular Matrix Promotes Synapse Plasticity

Nguyen, P. T., Dorman, L. C., Pan, S., Vainchtein, I. D., Han, R. T., Nakao-Inoue, H., Taloma, S. E., Barron, J. J., Molofsky, A. B., Kheirbek, M. A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.050 · Cited by 615

Cellular milieu imparts distinct pathological α-synuclein strains in α-synucleinopathies

Peng, C., Gathagan, R. J., Covell, D. J., Medellin, C., Stieber, A., Robinson, J. L., Zhang, B., Pitkin, R. M., Olufemi, M. F., Luk, K. C., et al. (2018) · Nature · doi:10.1038/s41586-018-0104-4 · Cited by 605

Self-Maintaining Gut Macrophages Are Essential for Intestinal Homeostasis

Schepper, S. D., Verheijden, S., Aguilera‐Lizarraga, J., Viola, M. F., Boesmans, W., Stakenborg, N., Voytyuk, I., Schmidt, I., Boeckx, B., de Casterlé, I. D., et al. (2018) · Cell · doi:10.1016/j.cell.2018.07.048 · Cited by 602

Pathogenesis of Parkinson disease—the gut–brain axis and environmental factors

Klingelhoefer, L., & Reichmann, H. (2015) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.197 · Cited by 598

Complement C3 deficiency protects against neurodegeneration in aged plaque-rich APP/PS1 mice

Shi, Q., Chowdhury, S., Ma, R., Le, K. X., Hong, S., Caldarone, B. J., Stevens, B., & Lemere, C. A. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf6295 · Cited by 593

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

Microglia clear neuron-released α-synuclein via selective autophagy and prevent neurodegeneration

Choi, I., Zhang, Y., Seegobin, S. P., Pruvost, M., Wang, Q., Purtell, K., Zhang, B., & Yue, Z. (2020) · Nature Communications · doi:10.1038/s41467-020-15119-w · Cited by 549

GM1 ganglioside–bound amyloid β–protein (Aβ): A possible form of preamyloid in Alzheimer's disease

Yanagisawa, K., Odaka, A., Suzuki, N., & Ihara, Y. (1995) · Nature Medicine · doi:10.1038/nm1095-1062 · Cited by 544

Complement C3aR Inactivation Attenuates Tau Pathology and Reverses an Immune Network Deregulated in Tauopathy Models and Alzheimer’s Disease

Litvinchuk, A., Wan, Y.-W., Swartzlander, D. B., Chen, F., Cole, A., Propson, N. E., Wang, Q., Zhang, B., Liu, Z., & Zheng, H. (2018) · Neuron · doi:10.1016/j.neuron.2018.10.031 · Cited by 523

Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies

Dejanovic, B., Huntley, M. A., De Mazière, A., Meilandt, W. J., Wu, T., Srinivasan, K., Jiang, Z., Gandham, V., Friedman, B. A., Ngu, H., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.10.014 · Cited by 517

Complement C3 Is Activated in Human AD Brain and Is Required for Neurodegeneration in Mouse Models of Amyloidosis and Tauopathy

Wu, T., Dejanovic, B., Gandham, V. D., Gogineni, A., Edmonds, R., Schauer, S., Srinivasan, K., Huntley, M. A., Wang, Y., Wang, T.-M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.060 · Cited by 466

How macrophages deal with death

Lemke, G. (2019) · Nature reviews. Immunology · doi:10.1038/s41577-019-0167-y · Cited by 446

Local externalization of phosphatidylserine mediates developmental synaptic pruning by microglia

Scott‐Hewitt, N., Perrucci, F., Morini, R., Erreni, M., Mahoney, M., Witkowska, A., Carey, A. E., Faggiani, E., Schuetz, L. T., Mason, S., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2020105380 · Cited by 436

Tau association with synaptic vesicles causes presynaptic dysfunction

Zhou, L., McInnes, J., Wierda, K., Holt, M., Herrmann, A. G., Jackson, R. J., Wang, Y.-C., Swerts, J., Beyens, J., Miskiewicz, K., et al. (2017) · Nature Communications · doi:10.1038/ncomms15295 · Cited by 434

Excessive burden of lysosomal storage disorder gene variants in Parkinson’s disease

Robak, L. A., Jansen, I. E., van Rooij, J., Uitterlinden, A. G., Kraaij, R., Jankovic, J., Heutink, P., Shulman, J. M., International Parkinson’s Disease Genomics Consortium (IPDGC), Nalls, M. A., et al. (2017) · Brain · doi:10.1093/brain/awx285 · Cited by 433

Tau impairs neural circuits, dominating amyloid-β effects, in Alzheimer models in vivo

Busche, M. A., Wegmann, S., Dujardin, S., Commins, C., Schiantarelli, J., Klickstein, N., Kamath, T. V., Carlson, G. A., Nelken, I., & Hyman, B. T. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0289-8 · Cited by 413

Gut-seeded α-synuclein fibrils promote gut dysfunction and brain pathology specifically in aged mice

Challis, C., Hori, A., Sampson, T. R., Yoo, B. B., Challis, R. C., Hamilton, A. M., Mazmanian, S. K., Volpicelli-Daley, L. A., & Gradinaru, V. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0589-7 · Cited by 405

Neuronal network activity controls microglial process surveillance in awake mice via norepinephrine signaling

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 401

LRRK2 kinase in Parkinson's disease

Alessi, D. R., & Sammler, E. (2018) · Science · doi:10.1126/science.aar5683 · Cited by 345

A single-cell atlas of the human substantia nigra reveals cell-specific pathways associated with neurological disorders

Agarwal, D., Sandor, C., Volpato, V., Caffrey, T. M., Monzón‐Sandoval, J., Bowden, R. J., Alegre‐Abarrategui, J., Wade‐Martins, R., & Webber, C. (2020) · Nature Communications · doi:10.1038/s41467-020-17876-0 · Cited by 328

Apolipoprotein E4 effects in Alzheimer’s disease are mediated by synaptotoxic oligomeric amyloid-β

Koffie, R. M., Hashimoto, T., Tai, H.-C., Kay, K. R., Serrano-Pozo, A., Joyner, D., Hou, S., Kopeikina, K. J., Frosch, M. P., Lee, V. M., et al. (2012) · Brain · doi:10.1093/brain/aws127 · Cited by 327

Increased soluble TREM2 in cerebrospinal fluid is associated with reduced cognitive and clinical decline in Alzheimer’s disease

Ewers, M., Franzmeier, N., Suárez-Calvet, M., Morenas-Rodriguez, E., Caballero, M. A. A., Kleinberger, G., Piccio, L., Cruchaga, C., Deming, Y., Dichgans, M., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aav6221 · Cited by 327

Microglial metabolic flexibility supports immune surveillance of the brain parenchyma

Bernier, L., York, E. M., Kamyabi, A., Choi, H. B., Weilinger, N. L., & MacVicar, B. A. (2020) · Nature Communications · doi:10.1038/s41467-020-15267-z · Cited by 323

Noradrenergic signaling in the wakeful state inhibits microglial surveillance and synaptic plasticity in the mouse visual cortex

Stowell, R. D., Sipe, G. O., Dawes, R. P., Batchelor, H. N., Lordy, K. A., Whitelaw, B. S., Stoessel, M. B., Bidlack, J. M., Brown, E., Sur, M., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0514-0 · Cited by 321

ApoE attenuates unresolvable inflammation by complex formation with activated C1q

Yin, C., Ackermann, S., Ma, Z., Mohanta, S. K., Zhang, C., Li, Y., Nietzsche, S., Westermann, M., Peng, L., Hu, D., et al. (2019) · Nature Medicine · doi:10.1038/s41591-018-0336-8 · Cited by 305

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

Parkinson’s disease: proteinopathy or lipidopathy?

Fanning, S., Selkoe, D. J., & Dettmer, U. (2020) · npj Parkinson s Disease · doi:10.1038/s41531-019-0103-7 · Cited by 251

Novel allele-dependent role for APOE in controlling the rate of synapse pruning by astrocytes

Chung, W.-S., Verghese, P. B., Chakraborty, C., Joung, J., Hyman, B. T., Ulrich, J. D., Holtzman, D. M., & Barres, B. A. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1609896113 · Cited by 242

Synaptogyrin-3 Mediates Presynaptic Dysfunction Induced by Tau

McInnes, J., Wierda, K., Snellinx, A., Bounti, L., Wang, Y.-C., Stancu, I.-C., Apóstolo, N., Gevaert, K., Dewachter, I., Spires-Jones, T. L., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.01.022 · Cited by 242

Soluble Aβ Oligomers Are Rapidly Sequestered from Brain ISF In Vivo and Bind GM1 Ganglioside on Cellular Membranes

Hong, S., Ostaszewski, B. L., Yang, T., O’Malley, T. T., Jin, M., Yanagisawa, K., Li, S., Bartels, T., & Selkoe, D. J. (2014) · Neuron · doi:10.1016/j.neuron.2014.02.027 · Cited by 213

Local apoptotic-like mechanisms underlie complement-mediated synaptic pruning

Györffy, B. A., Kun, J., Török, G., Bulyáki, É., Borhegyi, Z., Gulyássy, P., Kis, V., Szocsics, P., Micsonai, A., Matkó, J., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1722613115 · Cited by 188

LRRK2 is a negative regulator of Mycobacterium tuberculosis phagosome maturation in macrophages

Härtlová, A., Herbst, S., Peltier, J., Rodgers, A., Bilkei‐Gorzo, O., Fearns, A., Dill, B. D., Lee, H., Flynn, R., Cowley, S. A., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201798694 · Cited by 177

Synaptic phosphorylated α-synuclein in dementia with Lewy bodies

Colom‐Cadena, M., Pegueroles, J., Herrmann, A. G., Henstridge, C. M., Muñoz, L., Querol‐Vilaseca, M., Martín-Paniello, C. S., Luque-Cabecerans, J., Clarimón, J., Belbin, O., et al. (2017) · Brain · doi:10.1093/brain/awx275 · Cited by 130

Regulation of myeloid cell phagocytosis by LRRK2 via WAVE2 complex stabilization is altered in Parkinson’s disease

Kim, K. S., Marcogliese, P. C., Yang, J., Callaghan, S. M., Resende, V., Abdel-Messih, E., Marras, C., Visanji, N. P., Huang, J., Schlossmacher, M. G., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1718946115 · Cited by 111

Comparative profiling of the synaptic proteome from Alzheimer’s disease patients with focus on the APOE genotype

Hesse, R., Hurtado, M. L., Jackson, R. J., Eaton, S. L., Herrmann, A. G., Colom-Cadena, M., Tzioras, M., King, D., Rose, J., Tulloch, J., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0847-7 · Cited by 107

Selective vulnerability in α-synucleinopathies

Alegre‐Abarrategui, J., Brimblecombe, K. R., Roberts, R. F., Velentza‐Almpani, E., Tilley, B. S., Bengoa‐Vergniory, N., & Proukakis, C. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02010-2 · Cited by 90

C1q-targeted inhibition of the classical complement pathway prevents injury in a novel mouse model of acute motor axonal neuropathy

McGonigal, R., Cunningham, M. E., Yao, D., Barrie, J. A., Sankaranarayanan, S., Fewou, S. N., Furukawa, K., Yednock, T. A., & Willison, H. J. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0291-x · Cited by 74

Neuropathology and cognitive performance in self-reported cognitively healthy centenarians

Ganz, A. B., Beker, N., Hulsman, M., Sikkes, S. A. M., NBB, Scheltens, P., Smit, A. B., Rozemüller, A. J. M., Hoozemans, J. J. M., & Holstege, H. H. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0558-5 · Cited by 69

Synaptic mitochondrial dysfunction and septin accumulation are linked to complement-mediated synapse loss in an Alzheimer’s disease animal model

Györffy, B. A., Tóth, V., Török, G., Gulyássy, P., Kovács, R. Á., Vadászi, H., Micsonai, A., Tóth, M. E., Sántha, M., Homolya, L., et al. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03468-0 · Cited by 65

Understanding microglial diversity and implications for neuronal function in health and disease

Schepper, S. D., Crowley, G., & Hong, S. Y. (2020) · Developmental Neurobiology · doi:10.1002/dneu.22777 · Cited by 54

Prominent microglial inclusions in transgenic mouse models of α-synucleinopathy that are distinct from neuronal lesions

Tanriöver, G., Bacioglu, M., Schweighauser, M., Mahler, J., Wegenast‐Braun, B. M., Skodras, A., Obermüller, U., Barth, M., Kronenberg‐Versteeg, D., Nilsson, K. P. R., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00993-8 · Cited by 50

Analysis of α-synuclein species enriched from cerebral cortex of humans with sporadic dementia with Lewy bodies

Sanderson, J. B., De, S., Jiang, H., Rovere, M., Jin, M., Zaccagnini, L., Watson, A. H., de Boni, L., Lagomarsino, V. N., Young‐Pearse, T. L., et al. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa010 · Cited by 41

Progress in the genetic analysis of Parkinson’s disease

Singleton, A., & Hardy, J. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz183 · Cited by 33

Microglia in neurodegenerative diseases: mechanism and potential therapeutic targets

Gao, C., Jiang, J., Tan, Y., & Chen, S. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01588-0 · Cited by 1,616

The neuroimmune axis of Alzheimer’s disease

Jorfi, M., Maaser‐Hecker, A., & Tanzi, R. E. (2023) · Genome Medicine · doi:10.1186/s13073-023-01155-w · Cited by 313

Blood–Brain Barrier Breakdown: An Emerging Biomarker of Cognitive Impairment in Normal Aging and Dementia

Hussain, B., Fang, C., & Chang, J. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.688090 · Cited by 255

Extracellular protein components of amyloid plaques and their roles in Alzheimer’s disease pathology

Rahman, M. M., & Lendel, C. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00465-0 · Cited by 260

Alzheimer’s disease as a synaptopathy: Evidence for dysfunction of synapses during disease progression

Meftah, S., & Gan, J. (2023) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2023.1129036 · Cited by 205

Neuroimmune Interactions in Neurodegeneration: The Role of Microglia in Alzheimer’s and Parkinson’s Disease Pathogenesis

Goyal, P., Baldaniya, L. H., Tyagi, L. K., Joshi, K. K., Ballal, S., Sabarivani, A., Ray, S., Nathiya, D., Chauhan, A. S., Gulati, M., et al. (2026) · Brain Sciences · doi:10.3390/brainsci16020154 · Cited by 13

Microglia-Neuron Interactions in Alzheimer’s Disease

Ma, Y., Wang, X., Gao, M., Lin, Y., Chen, Q., Yang, H., Yang, C., & Wang, Q. (2025) · Current Neuropharmacology · doi:10.2174/011570159x379539250807114252 · Cited by 1

The Evolving Dialogue of Microglia and Neurons in Alzheimer’s Disease: Microglia as Necessary Transducers of Pathology

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