The endocytic pathway in microglia during health, aging and Alzheimer’s disease
Open accessAbstract
Microglia, the main phagocytes of the central nervous system (CNS), are involved in the surveillance and maintenance of nervous tissue. During normal tissue homeostasis, microglia migrates within the CNS, phagocytose dead cells and tissue debris, and modulate synapse pruning and spine formation via controlled phagocytosis. In the event of an invasion by a foreign body, microglia are able to phagocytose the invading pathogen and process it proteolytically for antigen presentation. Internalized substrates are incorporated and sorted within the endocytic pathway and thereafter transported via complex vesicular routes. When targeted for degradation, substrates are delivered to acidic late endosomes and lysosomes. In these, the enzymatic degradation relies on pH and enzyme content. Endocytosis, sorting, transport, compartment acidification and degradation are regulated by complex signaling mechanisms, and these may be altered during aging and pathology. In this review, we discuss the endocytic pathway in microglia, with insight into the mechanisms controlling lysosomal biogenesis and pH regulation. We also discuss microglial lysosome function associated with Alzheimer's disease (AD) and the mechanisms of amyloid-beta (Aβ) internalization and degradation. Finally, we explore some therapies currently being investigated to treat AD and their effects on microglial response to Aβ, with insight in those involving enhancement of lysosomal function.
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The endosome/lysosome system is involved in microglia-mediated degradation of internalized Aβ.
“The endosome/lysosome system is involved in microglia-mediated degradation of internalized Aβ [32, 33]”
From Microglia specific deletion of miR-155 in Alzheimer’s disease mouse models reduces amyloid-β pathology but causes hyperexcitability and seizures (2023) · cites this paper as [33]
Microglial phagocytosis of Aβ deposits in Alzheimer disease models requires the autophagy-related factors BECN1, ATG7 and LC3.
“microglial phagocytosis of Aβ deposits in Alzheimer disease models [430,431] requires the autophagy-related factors BECN1, ATG7 and LC3 [432,433].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [431]
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Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351 · see citing works
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · 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
Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429 · see citing works
Neuroinflammation in Alzheimer's disease
Heneka, M. T., Carson, M. J., Khoury, J. E., Landreth, G. E., Brosseron, F., Feinstein, D. L., Jacobs, A. H., Wyss-Coray, T., Vitorica, J., Ransohoff, R. M., et al. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(15)70016-5 · Cited by 6,226 · see citing works
Cui, C., Cui, J., Jin, F., Cui, Y., Li, R., Jiang, X., Tian, Y., Wang, R. C., Jiang, P., & Gao, J. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479571 · Cited by 5,214 · 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
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · see citing works
Immunobiology: the immune system in health and disease
(1995) · Choice Reviews Online · doi:10.5860/choice.32-3876 · Cited by 4,110 · see citing works
Apolipoprotein E and Alzheimer disease: risk, mechanisms and therapy
Liu, C.-C., Kanekiyo, T., Xu, H., & Bu, G. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.263 · Cited by 3,459 · see citing works
TFEB Links Autophagy to Lysosomal Biogenesis
Settembre, C., Di Malta, C., Polito, V. A., Arencibia, M. G., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Medina, D., Colella, P., et al. (2011) · Science · doi:10.1126/science.1204592 · Cited by 3,365 · see citing works
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160 · 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
A Gene Network Regulating Lysosomal Biogenesis and Function
Sardiello, M., Palmieri, M., di Ronza, A., Medina, D. L., Valenza, M., Gennarino, V. A., Di Malta, C., Donaudy, F., Embrione, V., Polishchuk, R. S., et al. (2009) · Science · doi:10.1126/science.1174447 · Cited by 2,543 · see citing works
Sallusto, F., Cella, M., Danieli, C., & Lanzavecchia, A. (1995) · The Journal of Experimental Medicine · doi:10.1084/jem.182.2.389 · Cited by 2,501 · see citing works
Tissue-resident macrophages originate from yolk-sac-derived erythro-myeloid progenitors
Gomez Perdiguero, E., Klapproth, K., Schulz, C., Busch, K., Azzoni, E., Crozet, L., Garner, H., Trouillet, C., de Bruijn, M. F., Geissmann, F., et al. (2015) · Nature · doi:10.1038/nature13989 · Cited by 2,339 · see citing works
Molecular mechanism and physiological functions of clathrin-mediated endocytosis
McMahon, H. T., & Boucrot, E. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3151 · Cited by 2,223 · see citing works
Davies, L. C., Jenkins, S. J., Allen, J. E., & Taylor, P. R. (2013) · Nature Immunology · doi:10.1038/ni.2705 · Cited by 2,096 · see citing works
The role of autophagy in neurodegenerative disease
Nixon, R. A. (2013) · Nature Medicine · doi:10.1038/nm.3232 · Cited by 2,059 · see citing works
Bard, F., Cannon, C., Barbour, R., Burke, R.-L., Games, D., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., et al. (2000) · Nature Medicine · doi:10.1038/78682 · Cited by 2,012 · see citing works
the Immunological Genome Consortium, Gautier, E. L., Shay, T., Miller, J., Greter, M., Jakubzick, C., Ivanov, S., Helft, J., Chow, A., Elpek, K. G., et al. (2012) · Nature Immunology · doi:10.1038/ni.2419 · Cited by 1,972 · 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
A lysosome‐to‐nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB
Settembre, C., Zoncu, R., Medina, D. L., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Ferron, M., Karsenty, G., Vellard, M. C., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.32 · Cited by 1,932 · see citing works
Amyloid β-peptide is produced by cultured cells during normal metabolism
Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921 · see citing works
Apolipoprotein E: Far More Than a Lipid Transport Protein
Mahley, R. W., & Rall, S. C. (2000) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.1.1.507 · Cited by 1,836 · see citing works
IMMUNOBIOLOGY : the immunesystem in health and disease
Janeway, C. A. (1994) · Cited by 1,757 · see citing works
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 · see citing works
Maxfield, F. R., & McGraw, T. E. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1315 · Cited by 1,716 · see citing works
Self-citationSignals from the lysosome: a control centre for cellular clearance and energy metabolism
Settembre, C., Fraldi, A., Medina, D. L., & Ballabio, A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3565 · Cited by 1,689 · see citing works
Microglial interactions with synapses are modulated by visual experience
Tremblay, M.-È., Lowery, R. L., & Majewska, A. K. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000527 · Cited by 1,542 · see citing works
The P2Y12 receptor regulates microglial activation by extracellular nucleotides
Haynes, S. E., Hollopeter, G., Yang, G., Kurpius, D., Dailey, M. E., Gan, W.-B., & Julius, D. (2006) · Nature Neuroscience · doi:10.1038/nn1805 · Cited by 1,542 · see citing works
Schmechel, D. E., Saunders, A. M., Strittmatter, W. J., Crain, B. J., Hulette, C. M., Joo, S. H., Pericak-Vance, M. A., Goldgaber, D., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.20.9649 · Cited by 1,525 · see citing works
Stewart, C. R., Stuart, L. M., Wilkinson, K., van Gils, J. M., Deng, J., Halle, A., Rayner, K. J., Boyer, L., Zhong, R., Frazier, W. A., et al. (2010) · Nature Immunology · doi:10.1038/ni.1836 · Cited by 1,513 · see citing works
Henne, W. M., Buchkovich, N. J., & Emr, S. D. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.05.015 · Cited by 1,505 · see citing works
Holmes, C., Boche, D., Wilkinson, D., Yadegarfar, G., Hopkins, V., Bayer, A., Jones, R. W., Bullock, R., Love, S., Neal, J. W., et al. (2008) · The Lancet · doi:10.1016/s0140-6736(08)61075-2 · Cited by 1,416 · see citing works
Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: a case report
Nicoll, J. A. R., Wilkinson, D., Holmes, C., Steart, P., Markham, H., & Weller, R. O. (2003) · Nature Medicine · doi:10.1038/nm840 · Cited by 1,397 · see citing works
MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB
Martina, J. A., Chen, Y., Guček, M., & Puertollano, R. (2012) · Autophagy · doi:10.4161/auto.19653 · Cited by 1,360 · see citing works
Roczniak-Ferguson, A., Petit, C. S. V., Froehlich, F., Qian, S., Ky, J., Angarola, B. L., Walther, T. C., & Ferguson, S. M. (2012) · Science Signaling · doi:10.1126/scisignal.2002790 · Cited by 1,358 · see citing works
A PPARγ-LXR-ABCA1 Pathway in Macrophages Is Involved in Cholesterol Efflux and Atherogenesis
Chawla, A., Boisvert, W. A., Lee, C.-H., Laffitte, B. A., Barak, Y., Joseph, S. B., Liao, D., Nagy, L., Edwards, P. A., Curtiss, L. K., et al. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00164-2 · Cited by 1,347 · 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
Mukherjee, S., Ghosh, R. K., & Maxfield, F. R. (1997) · Physiological Reviews · doi:10.1152/physrev.1997.77.3.759 · Cited by 1,299 · see citing works
Self-citationLysosomal acidification mechanisms
Mindell, J. A. (2012) · Annual Review of Physiology · doi:10.1146/annurev-physiol-012110-142317 · Cited by 1,258 · see citing works
Inflammation in Neurodegenerative Disease—A Double-Edged Sword
Wyss-Coray, T., & Mucke, L. (2002) · Neuron · doi:10.1016/s0896-6273(02)00794-8 · Cited by 1,235 · see citing works
Human ApoE isoforms differentially regulate brain amyloid-β peptide clearance
Castellano, J. M., Kim, J., Stewart, F. R., Jiang, H., DeMattos, R. B., Patterson, B. W., Fagan, A. M., Morris, J. C., Mawuenyega, K. G., Cruchaga, C., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002156 · Cited by 1,227 · see citing works
Vanier, M. T. (2010) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-5-16 · Cited by 1,222 · see citing works
Dai, X.-M., Ryan, G. R., Hapel, A. J., Dominguez, M. G., Russell, R. G., Kapp, S., Sylvestre, V., & Stanley, E. R. (2002) · Blood · doi:10.1182/blood.v99.1.111 · Cited by 1,184 · see citing works
Trophic macrophages in development and disease
Pollard, J. W. (2009) · Nature Reviews Immunology · doi:10.1038/nri2528 · Cited by 1,178 · see citing works
Namba, Y., Tomonaga, M., Kawasaki, H., Otomo, E., & Ikeda, K. (1991) · Brain Research · doi:10.1016/0006-8993(91)91092-f · Cited by 1,157 · see citing works
Takahashi, K., Rochford, C. D. P., & Neumann, H. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20041611 · Cited by 1,124 · see citing works
Microglial cell origin and phenotypes in health and disease
Saijo, K., & Glass, C. K. (2011) · Nature Reviews Immunology · doi:10.1038/nri3086 · Cited by 1,100 · see citing works
Trafficking and Proteolytic Processing of APP
Haass, C., Kaether, C., Thinakaran, G., & Sisodia, S. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006270 · Cited by 1,075 · see citing works
Classification and prediction of clinical Alzheimer's diagnosis based on plasma signaling proteins
Ray, S., Britschgi, M., Herbert, C., Takeda-Uchimura, Y., Boxer, A., Blennow, K., Friedman, L. F., Galasko, D. R., Jutel, M., Karydas, A., et al. (2007) · Nature Medicine · doi:10.1038/nm1653 · Cited by 1,048 · see citing works
TFEB controls cellular lipid metabolism through a starvation-induced autoregulatory loop
Settembre, C., De Cegli, R., Mansueto, G., Saha, P. K., Vetrini, F., Visvikis, O., Huynh, T., Carissimo, A., Palmer, D., Jürgen Klisch, T., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2718 · Cited by 1,022 · 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
In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
Stine, W. B., Dahlgren, K. N., Krafft, G. A., & LaDu, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210207200 · Cited by 1,015 · see citing works
Wang, Y., Szretter, K. J., Vermi, W., Gilfillan, S., Rossini, C., Cella, M., Barrow, A. D., Diamond, M. S., & Colonna, M. (2012) · Nature Immunology · doi:10.1038/ni.2360 · Cited by 1,011 · see citing works
Inflammation in Alzheimer Disease--A Brief Review of the Basic Science and Clinical Literature
Wyss-Coray, T., & Rogers, J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006346 · Cited by 975 · see citing works
Linking lipids to Alzheimer's disease: cholesterol and beyond
Di Paolo, G., & Kim, T.-W. (2011) · Nature Reviews Neuroscience · doi:10.1038/nrn3012 · Cited by 972 · see citing works
Phagocytosis of apoptotic cells in homeostasis
Arandjelovic, S., & Ravichandran, K. S. (2015) · Nature Immunology · doi:10.1038/ni.3253 · Cited by 959 · see citing works
Chishti, M. A., Yang, D.-S., Janus, C., Phinney, A. L., Horne, P., Pearson, J., Strome, R., Zuker, N., Loukides, J., French, J., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100710200 · Cited by 955 · see citing works
Phagocytosis: An Immunobiologic Process
Gordon, S. (2016) · Immunity · doi:10.1016/j.immuni.2016.02.026 · Cited by 902 · see citing works
Kaushik, S., & Cuervo, A. M. (2015) · Nature Medicine · doi:10.1038/nm.4001 · Cited by 899 · see citing works
ApoE Promotes the Proteolytic Degradation of Aβ
Jiang, Q., Lee, C. Y. D., Mandrekar, S., Wilkinson, B., Cramer, P., Zelcer, N., Mann, K., Lamb, B., Willson, T. M., Collins, J. L., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.04.010 · Cited by 876 · see citing works
Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling
Roy, C. L., & Wrana, J. L. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1571 · Cited by 862 · see citing works
Microglial Phagocytosis of Live Neurons
Brown, G. C., & Neher, J. J. (2014) · Nature Reviews Neuroscience · doi:10.1038/nrn3710 · Cited by 853 · see citing works
Discovery of a Cytokine and Its Receptor by Functional Screening of the Extracellular Proteome
Lin, H., Lee, E., Hestir, K., Leo, C., Huang, M., Bosch, E., Halenbeck, R., Wu, G., Zhou, A. J., Behrens, D., et al. (2008) · Science · doi:10.1126/science.1154370 · Cited by 815 · see citing works
The myeloid cells of the central nervous system parenchyma
Ransohoff, R. M., & Cardona, A. E. (2010) · Nature · doi:10.1038/nature09615 · Cited by 804 · see citing works
UDP acting at P2Y6 receptors is a mediator of microglial phagocytosis
Koizumi, S., Shigemoto-Mogami, Y., Nasu-Tada, K., Shinozaki, Y., Ohsawa, K., Tsuda, M., Joshi, B. V., Jacobson, K. A., Kohsaka, S., & Inoue, K. (2007) · Nature · doi:10.1038/nature05704 · Cited by 802 · see citing works
Review: microglia of the aged brain: primed to be activated and resistant to regulation
Norden, D. M., & Godbout, J. P. (2013) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2012.01306.x · Cited by 792 · 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
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 716 · see citing works
Extracellular vesicles round off communication in the nervous system
Budnik, V., Ruiz-Cañada, C., & Wendler, F. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.29 · Cited by 712 · see citing works
Takahashi, R. H., Milner, T. A., Li, F., Nam, E. E., Edgar, M. A., Yamaguchi, H., Beal, M. F., Xu, H., Greengard, P., & Gouras, G. K. (2002) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64463-x · Cited by 706 · see citing works
Spangenberg, E. E., Lee, R. J., Najafi, A. R., Rice, R. A., Elmore, M. R. P., Blurton-Jones, M., West, B. L., & Green, K. N. (2016) · Brain · doi:10.1093/brain/aww016 · Cited by 695 · see citing works
Astrocytes synthesize apolipoprotein E and metabolize apolipoprotein E-containing lipoproteins
Pitas, R. E., Boyles, J. K., Lee, S. H., Foss, D., & Mahley, R. W. (1987) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(87)90295-5 · Cited by 693 · see citing works
Garin, J., Diez, R., Kieffer‐Jaquinod, S., Dermine, J.-F., Duclos, S., Gagnon, É., Sadoul, R., Rondeau, C., & Desjardins, M. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.1.165 · Cited by 686 · see citing works
The role of protein clearance mechanisms in organismal ageing and age-related diseases
Vı́lchez, D., Sáez, I., & Dillin, A. G. (2014) · Nature Communications · doi:10.1038/ncomms6659 · Cited by 684 · see citing works
Immune activation in brain aging and neurodegeneration: too much or too little?
Lucin, K. M., & Wyss-Coray, T. (2009) · Neuron · doi:10.1016/j.neuron.2009.08.039 · Cited by 679 · see citing works
Hurley, J. H. (2015) · The EMBO Journal · doi:10.15252/embj.201592484 · Cited by 668 · see citing works
Paresce, D. M., Ghosh, R. N., & Maxfield, F. R. (1996) · Neuron · doi:10.1016/s0896-6273(00)80187-7 · Cited by 663 · see citing works
Self-citationMembrane 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
Endocytosis Is Required for Synaptic Activity-Dependent Release of Amyloid-β In Vivo
Cirrito, J. R., Kang, J.-E., Lee, J., Stewart, F. R., Verges, D. K., Silverio, L. M., Bu, G., Mennerick, S., & Holtzman, D. M. (2008) · Neuron · doi:10.1016/j.neuron.2008.02.003 · Cited by 635 · see citing works
Greter, M., Lelios, I., Pelczar, P., Hoeffel, G., Price, J., Leboeuf, M., Kündig, T. M., Frei, K., Ginhoux, F., Merad, M., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.11.001 · Cited by 630 · see citing works
TAM receptors regulate multiple features of microglial physiology
Fourgeaud, L., Través, P. G., Tufail, Y., Leal-Bailey, H., Lew, E. D., Burrola, P. G., Callaway, P., Zagórska, A., Rothlin, C. V., Nimmerjahn, A., et al. (2016) · Nature · doi:10.1038/nature17630 · Cited by 600 · see citing works
Lemke, G. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a009076 · Cited by 598 · see citing works
CD14 and Toll-Like Receptors 2 and 4 Are Required for Fibrillar Aβ-Stimulated Microglial Activation
Reed-Geaghan, E. G., Savage, J. C., Hise, A. G., & Landreth, G. E. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.3158-09.2009 · Cited by 591 · see citing works
Lakadamyali, M., Rust, M., & Zhuang, X. (2006) · Cell · doi:10.1016/j.cell.2005.12.038 · Cited by 589 · see citing works
Apolipoprotein E Is a Ligand for Triggering Receptor Expressed on Myeloid Cells 2 (TREM2)
Atagi, Y., Liu, C.-C., Painter, M. M., Chen, X.-F., Verbeeck, C., Zheng, H., Li, X., Rademakers, R., Kang, S. S., Xu, H., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.679043 · Cited by 587 · see citing works
Yamashiro, D. J., Tycko, B., Fluss, S. R., & Maxfield, F. R. (1984) · Cell · doi:10.1016/0092-8674(84)90414-8 · Cited by 577 · see citing works
Self-citationJanus-faced microglia: beneficial and detrimental consequences of microglial phagocytosis
Sierra, A., Abiega, O., Shahraz, A., & Neumann, H. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00006 · Cited by 574 · see citing works
Ferrer, I., Boada, M., Guerra, M. L. S., Rey, M. J., & Costa‐Jussà, F. R. (2004) · Brain Pathology · doi:10.1111/j.1750-3639.2004.tb00493.x · Cited by 567 · see citing works
Phagocytosis: Receptors, signal integration, and the cytoskeleton
Freeman, S. A., & Grinstein, S. (2014) · Immunological Reviews · doi:10.1111/imr.12212 · Cited by 548 · see citing works
Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis
Botelho, R. J., Teruel, M., Dierckman, R., Anderson, R., Wells, A., York, J. D., Meyer, T., & Grinstein, S. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.7.1353 · Cited by 539 · see citing works
Dynamics of the Microglial/Amyloid Interaction Indicate a Role in Plaque Maintenance
Bolmont, T., Haiss, F., Eicke, D., Radde, R., Mathis, C. A., Klunk, W. E., Kohsaka, S., Jucker, M., & Calhoun, M. E. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4814-07.2008 · Cited by 526 · see citing works
MacDonald, K. P. A., Palmer, J. S., Cronau, S. L., Seppanen, E. J., Olver, S. D., Raffelt, N. C., Kuns, R. D., Pettit, A. R., Clouston, A. D., Wainwright, B. J., et al. (2010) · Blood · doi:10.1182/blood-2010-02-266296 · Cited by 507 · see citing works
Dagher, N. N., Najafi, A. R., Kayala, K. M. N., Elmore, M. R. P., White, T. E., Medeiros, R., West, B. L., & Green, K. N. (2015) · Journal of Neuroinflammation · doi:10.1186/s12974-015-0366-9 · Cited by 505 · see citing works
A Cell Surface Receptor Complex for Fibrillar β-Amyloid Mediates Microglial Activation
Bamberger, M. E., Harris, M. E., McDonald, D. R., Husemann, J., & Landreth, G. E. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-07-02665.2003 · Cited by 501 · see citing works
Combs, C. K., Johnson, D. E., Karlo, J. C., Cannady, S. B., & Landreth, G. E. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-02-00558.2000 · Cited by 483 · see citing works
Molecular structure, function, and dynamics of clathrin-mediated membrane traffic.Preprint
Kirchhausen, T., Owen, D., & Harrison, S. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016725 · Cited by 479 · see citing works
Koenigsknecht-Talboo, J., & Landreth, G. E. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1808-05.2005 · Cited by 477 · see citing works
A role for TREM2 ligands in the phagocytosis of apoptotic neuronal cells by microglia
Hsieh, C. L., Koike, M., Spusta, S. C., Niemi, E. C., Yenari, M., Nakamura, M. C., & Seaman, W. E. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06042.x · Cited by 475 · see citing works
Wahrle, S. E., Jiang, H., Parsadanian, M., Legleiter, J., Han, X., Fryer, J. D., Kowalewski, T., & Holtzman, D. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407963200 · Cited by 474 · see citing works
Alzheimer’s Disease Genetics: From the Bench to the Clinic
Karch, C. M., Cruchaga, C., & Goate, A. M. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.041 · Cited by 473 · see citing works
Mueller-Steiner, S., Zhou, Y.-G., Arai, H., Roberson, E., Sun, B.-G., Chen, J., Wang, X., Yu, G.-Q., Esposito, L., Mucke, L., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.07.027 · Cited by 466 · see citing works
Terman, A., & Brunk, U. T. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2003.08.009 · Cited by 451 · see citing works
Origin of microglia: current concepts and past controversies
Ginhoux, F., & Prinz, M. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a020537 · Cited by 446 · 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
Norbury, C. C., Hewlett, L. J., Prescott, A. R., Shastri, N., & Watts, C. K. W. (1995) · Immunity · doi:10.1016/1074-7613(95)90067-5 · Cited by 410 · see citing works
Wilcke, M., Johannes, L., Galli, T., Mayau, V., Goud, B., & Salamero, J. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.6.1207 · Cited by 408 · see citing works
Formation and maintenance of Alzheimer's disease β-amyloid plaques in the absence of microglia
Grathwohl, S. A., Kälin, R. E., Bolmont, T., Prokop, S., Winkelmann, G., Kaeser, S. A., Odenthal, J., Radde, R., Eldh, T., Gandy, S., et al. (2009) · Nature Neuroscience · doi:10.1038/nn.2432 · Cited by 401 · see citing works
The Cl-/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes
Graves, A. R., Curran, P. K., Smith, C. L., & Mindell, J. A. (2008) · Nature · doi:10.1038/nature06907 · Cited by 399 · see citing works
The coated pit and macropinocytic pathways serve distinct endosome populations
Hewlett, L. J., Prescott, A., & Watts, C. K. W. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.124.5.689 · Cited by 380 · see citing works
Cataldo, A. M., Barnett, J. L., Berman, S. A., Li, J., Quarless, S., Bursztajn, S., Lippa, C., & Nixon, R. A. (1995) · Neuron · doi:10.1016/0896-6273(95)90324-0 · Cited by 379 · see citing works
Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease
Gouras, G. K., Tampellini, D., Takahashi, R. H., & Capetillo-Zarate, E. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0679-9 · Cited by 372 · see citing works
Self-citationPotolicchio, I., Carven, G. J., Xu, X., Stipp, C., Riese, R. J., Stern, L. J., & Santambrogio, L. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.4.2237 · Cited by 365 · see citing works
Ontogeny of Tissue-Resident Macrophages
Hoeffel, G., & Ginhoux, F. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00486 · Cited by 364 · see citing works
Aβ vaccination effects on plaque pathology in the absence of encephalitis in Alzheimer disease
Masliah, E., Hansen, L., Adame, A., Crews, L. A., Bard, F., Lee, C., Seubert, P. A., Games, D., Kirby, L., & Schenk, D. (2005) · Neurology · doi:10.1212/01.wnl.0000148590.39911.df · Cited by 355 · see citing works
Emerging Roles for CSF-1 Receptor and its Ligands in the Nervous System
Chiţu, V., Gökhan, Ş., Nandi, S., Mehler, M. F., & Stanley, E. R. (2016) · Trends in Neurosciences · doi:10.1016/j.tins.2016.03.005 · Cited by 354 · see citing works
Rag GTPases mediate amino acid–dependent recruitment of TFEB and MITF to lysosomes
Martina, J. A., & Puertollano, R. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201209135 · Cited by 350 · see citing works
Combs, C. K., Johnson, D. E., Cannady, S. B., Lehman, T. M., & Landreth, G. E. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-03-00928.1999 · Cited by 349 · see citing works
Microglia Function in Alzheimer’s Disease
Solito, E., & Sastre, M. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00014 · Cited by 347 · see citing works
Degradation of the Alzheimer's Amyloid β Peptide by Endothelin-converting Enzyme*
Eckman, E., Reed, D. K., & Eckman, C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007579200 · Cited by 345 · see citing works
ClC-7 requires Ostm1 as a β-subunit to support bone resorption and lysosomal function
Lange, P. F., Wartosch, L., Jentsch, T. J., & Fuhrmann, J. C. (2006) · Nature · doi:10.1038/nature04535 · Cited by 342 · see citing works
Nandi, S., Gökhan, Ş., Dai, X.-M., Wei, S., Enikolopov, G., Lin, H., Mehler, M. F., & Stanley, E. R. (2012) · Developmental Biology · doi:10.1016/j.ydbio.2012.03.026 · Cited by 341 · see citing works
Endolysosomal proteolysis and its regulation
Pillay, C. S., Elliott, E., & Dennison, C. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3630417 · Cited by 341 · see citing works
Macropinosome maturation and fusion with tubular lysosomes in macrophages.
Racoosin, E. L., & Swanson, J. A. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.121.5.1011 · Cited by 335 · see citing works
The biogenesis of lysosomes and lysosome-related organelles
Luzio, J. P., Hackmann, Y., Dieckmann, N. M. G., & Griffiths, G. M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016840 · Cited by 330 · see citing works
The Many Alternative Faces of Macrophage Activation
Hume, D. A. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00370 · Cited by 303 · see citing works
Lysosomes in iron metabolism, ageing and apoptosis
Kurz, T., Terman, A., Gustafsson, B., & Brunk, U. T. (2008) · Histochemistry and Cell Biology · doi:10.1007/s00418-008-0394-y · Cited by 302 · see citing works
Involvement of P2X 4 and P2Y 12 receptors in ATP‐induced microglial chemotaxis
Ohsawa, K., Irino, Y., Nakamura, Y., Akazawa, C., Inoue, K., & Kohsaka, S. (2007) · Glia · doi:10.1002/glia.20489 · Cited by 301 · see citing works
Wilcock, D. M., Rojiani, A. M., Rosenthal, A., Levkowitz, G., Subbarao, S., Alamed, J., Wilson, D. H., Wilson, N., Freeman, M. J., Gordon, M. N., et al. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1090-04.2004 · Cited by 298 · see citing works
Wunderlich, P., Glebov, K., Kemmerling, N., Tien, N. T., Neumann, H., & Walter, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.517540 · Cited by 296 · see citing works
TREM2 regulates microglial cell activation in response to demyelination in vivo
Cantoni, C., Bollman, B., Licastro, D., Xie, M., Mikesell, R., Schmidt, R., Yuede, C. M., Galimberti, D., Olivecrona, G., Klein, R. S., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1388-1 · Cited by 296 · see citing works
Immunotherapeutic Approaches for Alzheimer’s Disease
Wisniewski, T., & Goñi, F. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.064 · Cited by 284 · see citing works
A cation counterflux supports lysosomal acidification
Steinberg, B. E., Huynh, K. K., Brodovitch, A., Jabs, S., Stauber, T., Jentsch, T. J., & Grinstein, S. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200911083 · Cited by 280 · see citing works
Liu, Z., Condello, C., Schain, A., Harb, R., & Grutzendler, J. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4403-10.2010 · Cited by 276 · 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
Self-citationDifferential TAM receptor–ligand–phospholipid interactions delimit differential TAM bioactivities
Lew, E. D., Oh, J., Burrola, P., Lax, I., Zagórska, A., Través, P. G., Schlessinger, J., & Lemke, G. (2014) · eLife · doi:10.7554/elife.03385 · Cited by 271 · see citing works
Slow Degradation of Aggregates of the Alzheimer's Disease Amyloid β-Protein by Microglial Cells
Paresce, D. M., Chung, H., & Maxfield, F. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.46.29390 · Cited by 269 · see citing works
Self-citationLübke, T., Lobel, P., & Sleat, D. (2008) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamcr.2008.09.018 · Cited by 267 · see citing works
Aβ Species Removal After Aβ <sub>42</sub> Immunization
Nicoll, J. A. R., Barton, E., Boche, D., Neal, J. W., Ferrer, I., Thompson, P., Vlachouli, C., Wilkinson, D., Bayer, A., Games, D., et al. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000240466.10758.ce · Cited by 265 · see citing works
Alzheimer's Disease β-Amyloid Peptide Is Increased in Mice Deficient in Endothelin-converting Enzyme
Eckman, E. A., Watson, M., Marlow, L. A., Sambamurti, K., & Eckman, C. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200642200 · Cited by 263 · see citing works
Lysosomal Membrane Proteins and Their Central Role in Physiology
Schwake, M., Schröder, B., & Säftig, P. (2013) · Traffic · doi:10.1111/tra.12056 · Cited by 258 · see citing works
Ishimoto, Y., Ohashi, K., Mizuno, K., & Nakano, T. (2000) · Journal of Biochemistry (Tokyo) · doi:10.1093/oxfordjournals.jbchem.a022622 · Cited by 248 · see citing works
Endolysosomal proteolysis and its regulation
Pillay, C. S., Elliott, E., & Dennison, C. (2002) · Biochemical Journal · doi:10.1042/bj3630417 · Cited by 247 · see citing works
Martínez‐Vicente, M., Sovak, G., & Cuervo, A. M. (2005) · Experimental Gerontology · doi:10.1016/j.exger.2005.07.005 · Cited by 245 · see citing works
Molecular pharmacology of endothelin converting enzymes
Turner, A. J., & Murphy, L. J. (1996) · Biochemical Pharmacology · doi:10.1016/0006-2952(95)02036-5 · Cited by 237 · see citing works
The vacuolar-type H+-ATPase at a glance – more than a proton pump
Maxson, M. E., & Grinstein, S. (2014) · Journal of Cell Science · doi:10.1242/jcs.158550 · Cited by 234 · see citing works
Xiao, Q., Yan, P., Ma, X., Liu, H., Perez, R., Zhu, A., Gonzales, E. R., Tripoli, D. L., Czerniewski, L. R., Ballabio, A., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.0705-15.2015 · Cited by 230 · see citing works
Boissonneault, V., Filali, M., Lessard, M., Relton, J., Wong, G., & Rivest, S. (2008) · Brain · doi:10.1093/brain/awn331 · Cited by 221 · see citing works
PPAR-γ Agonists as Regulators of Microglial Activation and Brain Inflammation
Bernardo, A., & Minghetti, L. (2006) · Current Pharmaceutical Design · doi:10.2174/138161206780574579 · Cited by 220 · see citing works
Motyckova, G., Weilbaecher, K. N., Horstmann, M. A., Rieman, D. J., Fisher, D. E., & Fisher, D. E. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.091479298 · Cited by 220 · see citing works
Chloride in Vesicular Trafficking and Function
Stauber, T., & Jentsch, T. J. (2012) · Annual Review of Physiology · doi:10.1146/annurev-physiol-030212-183702 · Cited by 216 · see citing works
Cuervo, A. M., & Dice, J. F. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00075-9 · Cited by 215 · see citing works
Chung, H., Brazil, M. I., Soe, T. T., & Maxfield, F. R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.45.32301 · Cited by 212 · see citing works
Self-citationMallet, W. G., & Maxfield, F. R. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.2.345 · Cited by 208 · see citing works
Self-citationDunn, K., & Maxfield, F. R. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.117.2.301 · Cited by 195 · see citing works
Self-citationClC-7 requires Ostm1 as a beta-subunit to support bone resorption and lysosomal function
Fuhrmann, J. C., Lange, P. F., Wartosch, L., & Jentsch, T. J. (2007) · GBM Annual Spring meeting Mosbach 2007 · doi:10.1240/sav_gbm_2007_m_001701 · Cited by 184 · see citing works
A RANKL–PKCβ–TFEB signaling cascade is necessary for lysosomal biogenesis in osteoclastsPreprint
Ferron, M., Settembre, C., Shimazu, J., Lacombe, J., Kato, S., Rawlings, D. J., Ballabio, A., & Karsenty, G. (2013) · Genes & Development · doi:10.1101/gad.213827.113 · Cited by 182 · see citing works
Sunderland, T., Mirza, N., Putnam, K. T., Linker, G., Bhupali, D., Durham, R., Soares, H., Kimmel, L., Friedman, D., Bergeson, J., et al. (2004) · Biological Psychiatry · doi:10.1016/j.biopsych.2004.07.021 · Cited by 179 · see citing works
Lee, C. Y. D., Tse, W., Smith, J. D., & Landreth, G. E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.295451 · Cited by 178 · see citing works
Association between genetic traits for immune-mediated diseases and Alzheimer disease
Yokoyama, J. S., Wang, Y., Schork, A. J., Thompson, W. K., Karch, C. M., Cruchaga, C., McEvoy, L. K., Witoelar, A., Chen, C.-H., Holland, D., et al. (2016) · JAMA Neurology · doi:10.1001/jamaneurol.2016.0150 · Cited by 176 · see citing works
Putting cholesterol in its place: apoE and reverse cholesterol transport
Mahley, R. W. (2006) · Journal of Clinical Investigation · doi:10.1172/jci28632 · Cited by 173 · see citing works
Linkage of M-CSF Signaling to Mitf, TFE3, and the Osteoclast Defect in Mitfmi/mi Mice
Weilbaecher, K. N., Motyckova, G., Huber, W. E., Takemoto, C. M., Hemesath, T. J., Xu, Y., Hershey, C. L., Dowland, N., Wells, A. G., & Fisher, D. E. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00360-4 · Cited by 168 · see citing works
Medeiros, R., Kitazawa, M., Passos, G. F., Baglietto-Vargas, D., Cheng, D., Cribbs, D. H., & LaFerla, F. M. (2013) · The American Journal of Pathology · doi:10.1016/j.ajpath.2013.01.051 · Cited by 163 · 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
Prostaglandin signaling suppresses beneficial microglial function in Alzheimer’s disease models
Johansson, J. U., Woodling, N. S., Wang, Q., Panchal, M., Liang, X., Trueba-Saiz, A., Brown, H. D., Mhatre, S. D., Loui, T., & Andreasson, K. I. (2015) · Journal of Clinical Investigation · doi:10.1172/jci77487 · Cited by 161 · see citing works
Microglial Functions and Proteases
Nakanishi, H. (2003) · Molecular Neurobiology · doi:10.1385/mn:27:2:163 · Cited by 158 · see citing works
Martina, J. A., Diab, H. I., Li, H., & Puertollano, R. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1565-8 · Cited by 155 · see citing works
Tanaka, Y., Matsuwaki, T., Yamanouchi, K., & Nishihara, M. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.06.049 · Cited by 153 · see citing works
Koenigsknecht-Talboo, J., Meyer-Luehmann, M., Parsadanian, M., Garcia-Alloza, M., Finn, M. B., Hyman, B. T., Bacskai, B. J., & Holtzman, D. M. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4147-08.2008 · Cited by 149 · see citing works
Nakanishi, H., & Wu, Z. (2009) · Behavioural Brain Research · doi:10.1016/j.bbr.2009.02.001 · Cited by 149 · see citing works
ABCA7 Deficiency Accelerates Amyloid-β Generation and Alzheimer's Neuronal Pathology
Sakae, N., Liu, C., Shinohara, M., Frisch‐Daiello, J. L., Ma, L., Yamazaki, Y., Tachibana, M., Younkin, L. H., Kurti, A., Carrasquillo, M. M., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3757-15.2016 · Cited by 146 · see citing works
Dynamics and Function of Phospholipase D and Phosphatidic Acid During Phagocytosis
Corrotte, M., Chasserot‐Golaz, S., Huang, P., Du, G., Ktistakis, N. T., Frohman, M. A., Vitale, N., Bader, M. F., & Grant, N. J. (2006) · Traffic · doi:10.1111/j.1600-0854.2006.00389.x · Cited by 143 · see citing works
Neuropathology after active Aβ42 immunotherapy: implications for Alzheimer’s disease pathogenesis
Boche, D., Denham, N., Holmes, C., & Nicoll, J. A. R. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0719-5 · Cited by 135 · see citing works
IL-34 and CSF-1: similarities and differences
Nakamichi, Y., Udagawa, N., & Takahashi, N. (2013) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-013-0476-3 · Cited by 133 · see citing works
Extracellular amyloid formation and associated pathology in neural grafts
Meyer‐Luehmann, M., Stalder, M., Herzig, M. C., Kaeser, S. A., Kohler, E., Pfeifer, M., Boncristiano, S., Mathews, P. M., Mercken, M. H., Abramowski, D., et al. (2003) · Nature Neuroscience · doi:10.1038/nn1022 · Cited by 133 · see citing works
Choi, S., Aïd, S., Caracciolo, L., Minami, S., Niikura, T., Matsuoka, Y., Turner, R. S., Mattson, M. P., & Bosetti, F. (2012) · Journal of Neurochemistry · doi:10.1111/jnc.12059 · Cited by 131 · see citing works
Moskot, M., Montefusco, S., Jakóbkiewicz‐Banecka, J., Mozolewski, P., Węgrzyn, A., di Bernardo, D., Węgrzyn, G., Medina, D. L., Ballabio, A., & Gabig‐Cimińska, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.555300 · Cited by 130 · see citing works
Ghosh, A., Jana, M., Modi, K. K., Gonzalez, F. J., Sims, K. B., Berry‐Kravis, E., & Pahan, K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.610659 · Cited by 129 · see citing works
How longevity research can lead to therapies for Alzheimer's disease: The rapamycin story
Richardson, A. G., Galván, V., Lin, A., & Oddo, S. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.12.002 · Cited by 122 · see citing works
Chitu, V., Gokhan, S., Gulinello, M., Branch, C. A., Patil, M., Basu, R., Stoddart, C., Mehler, M. F., & Stanley, E. R. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.12.001 · Cited by 119 · see citing works
Endocytic accessory factors and regulation of clathrin-mediated endocytosis.Preprint
Merrifield, C. J., & Kaksonen, M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016733 · Cited by 119 · see citing works
Jiang, D., Rauda, I. E., Han, S., Chen, S., & Zhou, F. (2012) · Langmuir · doi:10.1021/la3021436 · Cited by 115 · see citing works
Banati, R. B., Rothe, G., Valet, G., & Kreutzberg, G. W. (1993) · Glia · doi:10.1002/glia.440070208 · Cited by 111 · see citing works
Lin, S. X. H., Mallet, W. G., Huang, A. Y., & Maxfield, F. R. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-07-0497 · Cited by 111 · see citing works
Self-citationKinetics of endosome acidification in mutant and wild-type Chinese hamster ovary cells.
Yamashiro, D. J., & Maxfield, F. R. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.105.6.2713 · Cited by 110 · see citing works
Self-citationDegradation of Alzheimer's amyloid fibrils by microglia requires delivery of ClC-7 to lysosomes
Majumdar, A., Capetillo‐Zarate, E., Cruz, D. L., Gouras, G. K., & Maxfield, F. R. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-09-0745 · Cited by 106 · see citing works
Self-citationABCA1 influences neuroinflammation and neuronal death
Karasinska, J. M., de Haan, W., Franciosi, S., Ruddle, P., Fan, J., Kruit, J. K., Stukas, S., Lütjohann, D., Gutmann, D. H., Wellington, C. L., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.01.018 · Cited by 104 · see citing works
Clathrin uncoating: Auxilin comes to life
Lemmon, S. K. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00010-0 · Cited by 104 · see citing works
Bonet-Costa, V., Herranz‐Pérez, V., Blanco-Gandía, M. C., Mas‐Bargues, C., Inglés, M., García-Tárraga, P., Rodríguez‐Arias, M., Miñarro, J., Borrás, C., García‐Verdugo, J. M., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-151020 · Cited by 103 · see citing works
Endothelin-Converting Enzyme-2 Is Increased in Alzheimer’s Disease and Up-Regulated by Aβ
Palmer, J. C., Baig, S., Kehoe, P. G., & Love, S. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.081054 · Cited by 100 · see citing works
Cathepsin D is involved in the clearance of Alzheimer's β‐amyloid protein
Hamazaki, H. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)01087-3 · Cited by 92 · see citing works
Acidic pH as a physiological regulator of human cathepsin L activity
Turk, B., Dolenc, I., Lenar≷cic̆, B., Križaj, I., Türk, V., Bieth, J. G., & Björk, I. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00145.x · Cited by 91 · see citing works
Insights into immunoglobulin E receptor signaling from structurally defined ligands
Holowka, D., Sil, D., Torigoe, C., & Baird, B. A. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00517.x · Cited by 90 · see citing works
Dunn, H. C., Ager, R. R., Baglietto‐Vargas, D., Cheng, D., Kitazawa, M., Cribbs, D. H., & Medeiros, R. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-141335 · Cited by 89 · see citing works
Mackay, E. A., Ehrhard, A., Moniatte, M., Guénet, C., Tardif, C., Tarnus, C., Sorokine, O., Heintzelmann, B., Nay, C., Rémy, J.-M., et al. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00414.x · Cited by 89 · see citing works
Involvement of Cathepsin E in Exogenous Antigen Processing in Primary Cultured Murine Microglia
Nishioku, T., Hashimoto, K., Yamashita, K., Liou, S., Kagamiishi, Y., Maegawa, H., Katsube, N. C., Peters, C., FIGURA, K. V., Säftig, P., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108382200 · Cited by 89 · see citing works
Pacheco‐Quinto, J., & Eckman, E. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.422964 · Cited by 87 · see citing works
Meadows, N. A., Sharma, S. M., Faulkner, G. J., Ostrowski, M. C., Hume, D. A., & Cassady, A. I. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608572200 · Cited by 86 · see citing works
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Neuroinflammation and microglial activation in Alzheimer disease: where do we go from here?
Leng, F., & Edison, P. (2021) · Nature Reviews Neurology · doi:10.1038/s41582-020-00435-y · Cited by 3,179 · 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
Inflammatory Processes in Alzheimer’s Disease—Pathomechanism, Diagnosis and Treatment: A Review
Twarowski, B., & Herbet, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076518 · Cited by 458 · see citing works
Autophagy and Microglia: Novel Partners in Neurodegeneration and Aging
Plaza-Zabala, A., Sierra-Torre, V., & Sierra, A. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18030598 · Cited by 323 · see citing works
TDP-43 depletion in microglia promotes amyloid clearance but also induces synapse loss
Paolicelli, R. C., Jawaid, A., Henstridge, C. M., Valeri, A., Merlini, M., Robinson, J. L., Lee, E. B., Rose, J., Appel, S., Lee, V. M.-Y., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.05.037 · Cited by 239 · see citing works
Outdoor Ambient Air Pollution and Neurodegenerative Diseases: the Neuroinflammation Hypothesis
Jayaraj, R. L., Rodriguez, E. A., Wang, Y., & Block, M. L. (2017) · Current Environmental Health Reports · doi:10.1007/s40572-017-0142-3 · Cited by 233 · see citing works
Ren, C., Li, D., Zhou, Q., & Hu, X. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2019.119752 · Cited by 228 · see citing works
Emerging Microglia Biology Defines Novel Therapeutic Approaches for Alzheimer’s Disease
Lewcock, J. W., Schlepckow, K., Di Paolo, G., Tahirovic, S., Monroe, K. M., & Haass, C. (2020) · Neuron · doi:10.1016/j.neuron.2020.09.029 · Cited by 221 · see citing works
Microglial Phagocytosis: A Disease-Associated Process Emerging from Alzheimer’s Disease Genetics
Podleśny-Drabiniok, A., Marcora, E., & Goate, A. M. (2020) · Trends in Neurosciences · doi:10.1016/j.tins.2020.10.002 · Cited by 211 · 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
Autophagy and ALS: mechanistic insights and therapeutic implications
Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189 · see citing works
“nections between phagocytosis and autophagy, microglial phagocytosis of Aβ deposits in Alzheimer disease models [430,431] requires the autophagy-related factors BECN1, ATG7 and LC3 [432,433].”
BackgroundKnupp, A., Mishra, S., Martinez, R. A., Braggin, J. E., Szabo, M. P., Kinoshita, C., Hailey, D. W., Small, S. A., Jayadev, S., & Young, J. E. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107719 · Cited by 177 · see citing works
Endosomal Traffic Jams Represent a Pathogenic Hub and Therapeutic Target in Alzheimer’s Disease
Small, S. A., Simoes, S., Mayeux, R. P., & Petsko, G. A. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.08.003 · Cited by 163 · see citing works
Ultrastructural evidence of microglial heterogeneity in Alzheimer’s disease amyloid pathology
El Hajj, H., Savage, J. C., Bisht, K., Parent, M., Vallières, L., Rivest, S., & Tremblay, M.-È. (2019) · Journal of Neuroinflammation · doi:10.1186/s12974-019-1473-9 · Cited by 119 · see citing works
Hoogmartens, J., Cacace, R., & Broeckhoven, C. V. (2021) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1002/dad2.12155 · Cited by 101 · see citing works
The P2X7 Receptor in Microglial Cells Modulates the Endolysosomal Axis, Autophagy, and Phagocytosis
Campagno, K. E., & Mitchell, C. H. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.645244 · Cited by 90 · see citing works
Friend, Foe or Both? Immune Activity in Alzheimer’s Disease
Frost, G. R., Jonas, L. A., & Li, Y. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00337 · Cited by 86 · see citing works
Kynurenine Pathway Metabolites as Biomarkers in Alzheimer’s Disease
Liang, Y., Xie, S., He, Y., Xu, M., Qiao, X., Zhu, Y. H., & Wu, W. (2022) · Disease Markers · doi:10.1155/2022/9484217 · Cited by 86 · see citing works
SFRP1 modulates astrocyte-to-microglia crosstalk in acute and chronic neuroinflammation
Rueda‐Carrasco, J., Martín‐Bermejo, M. J., Pereyra, G., Mateo, M. I., Borroto, A., Brosseron, F., Kummer, M. P., Schwartz, S., López‐Atalaya, J. P., Alarcón, B., et al. (2021) · EMBO Reports · doi:10.15252/embr.202051696 · Cited by 77 · see citing works
Andersson, C. R., Falsig, J., Stavenhagen, J. B., Christensen, S., Kartberg, F., Rosenqvist, N., Finsen, B. R., & Pedersen, J. T. (2019) · Scientific Reports · doi:10.1038/s41598-019-41105-4 · Cited by 78 · see citing works
MFG-E8 Selectively Inhibited Aβ-Induced Microglial M1 Polarization via NF-κB and PI3K-Akt Pathways
Shi, X., Cai, X., Di, W., Li, J., Xu, X., Zhang, A., Qi, W., Zhou, Z., & Fang, Y. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0255-y · Cited by 76 · see citing works
Wasén, C., Beauchamp, L. C., Vincentini, J., Li, S., LeServe, D. S., Gauthier, C. D., Lopes, J. R., Moreira, T. G., Ekwudo, M. N., Yin, Z., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47683-w · Cited by 75 · see citing works
Microglial Progranulin: Involvement in Alzheimer’s Disease and Neurodegenerative Diseases
Mendsaikhan, A., Tooyama, I., & Walker, D. G. (2019) · Cells · doi:10.3390/cells8030230 · Cited by 72 · see citing works
Song, J., Choi, S., & Kim, B. C. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00064 · Cited by 62 · see citing works
Role of Neuron and Glia in Alzheimer’s Disease and Associated Vascular Dysfunction
Bandyopadhyay, S. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.653334 · Cited by 62 · see citing works
Microglia: Friend and foe in tauopathy
Odfalk, K. F., Bieniek, K. F., & Hopp, S. C. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102306 · Cited by 60 · see citing works
Role of microglial amylin receptors in mediating beta amyloid (Aβ)-induced inflammation
Fu, W., Vukojevic, V., Patel, A., Soudy, R., MacTavish, D., Westaway, D. A., Kaur, K., Goncharuk, V. D., & Jhamandas, J. H. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-017-0972-9 · Cited by 52 · see citing works
A role of the frontotemporal lobar degeneration risk factor TMEM106B in myelination
Feng, T., Sheng, R. R., Solé‐Domènech, S., Ullah, M., Zhou, X., Mendoza, C. S., Enriquez, L. C. M., Katz, I. I., Paushter, D. H., Sullivan, P. M., et al. (2020) · Brain · doi:10.1093/brain/awaa154 · Cited by 53 · see citing works
Self-citationHammel, G., Zivkovic, S., Ayazi, M., & Ren, Y. (2022) · Cellular Immunology · doi:10.1016/j.cellimm.2022.104591 · Cited by 53 · see citing works
PRCD is essential for high-fidelity photoreceptor disc formation
Spencer, W. J., Ding, J., Lewis, T. R., Chen, Y., Phan, S., Pearring, J. N., Kim, K.-Y., Thor, A., Mathew, R., Kalnitsky, J., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1906421116 · Cited by 49 · see citing works
A lysosomal regulatory circuit essential for the development and function of microglia
Iyer, H., Shen, K., Meireles, A. M., & Talbot, W. S. (2022) · Science Advances · doi:10.1126/sciadv.abp8321 · Cited by 51 · see citing works
Aβ42 Protofibrils Interact with and Are Trafficked through Microglial-Derived Microvesicles
Gouwens, L. K., Ismail, M. S., Rogers, V. A., Zeller, N. T., Garrad, E. C., Amtashar, F. S., Makoni, N. J., Osborn, D. C., & Nichols, M. R. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00029 · Cited by 48 · see citing works
Cuddy, L. K., Prokopenko, D., Cunningham, E. P., Brimberry, R., Song, P., Kirchner, R., Chapman, B., Hofmann, O., Hide, W., Procissi, D., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aaz2541 · Cited by 45 · see citing works
Solé‐Domènech, S., Rojas, A. V., Maisuradze, G. G., Scheraga, H. A., Lobel, P., & Maxfield, F. R. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1719808115 · Cited by 47 · see citing works
Self-citationAloi, M. S., Prater, K. E., Sánchez, R. E. A., Beck, A., Pathan, J. L., Davidson, S., Wilson, A., Keene, C. D., de la Iglesia, H., Jayadev, S., et al. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02745-6 · Cited by 43 · see citing works
Microglia degrade Alzheimer’s amyloid-beta deposits extracellularly via digestive exophagy
Jacquet, R. G., Ibáñez, F. G., Picard, K., Funes, L., Khakpour, M., Gouras, G. K., Tremblay, M., Maxfield, F. R., & Solé‐Domènech, S. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.115052 · Cited by 37 · see citing works
Self-citationChar, R., & Pierre, P. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00779 · Cited by 38 · see citing works
Qian, W., Liu, D., Liu, J., Liu, M., Ji, Q., Zhang, B., Yang, Z., Cheng, Y., & Zhou, S. (2024) · Small · doi:10.1002/smll.202408581 · Cited by 36 · see citing works
Europium-Doped Cerium Oxide Nanoparticles for Microglial Amyloid Beta Clearance and Homeostasis
Machhi, J., Yeapuri, P., Marković, M., Patel, M., Yan, W., Lu, Y., Cohen, J. D., Hasan, M., Abdelmoaty, M. M., Zhou, Y., et al. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00847 · Cited by 34 · see citing works
Ernest James Phillips, T., & Maguire, E. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.652593 · Cited by 33 · see citing works
Jiang, X., Liu, Z., Yang, Y., Li, H., Qi, X., Ren, W. X., Deng, M., Lü, M., Wu, J., & Liang, S. (2019) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2019.117435 · Cited by 33 · see citing works
The Pathological Activation of Microglia Is Modulated by Sexually Dimorphic Pathways
O'Connor, J. L., & Nissen, J. C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054739 · Cited by 31 · see citing works
Microglia: roles and genetic risk in Parkinson’s disease
Trainor, A. R., MacDonald, D. S., & Penney, J. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1506358 · Cited by 33 · see citing works
Erythropoietin signaling in peripheral macrophages is required for systemic β‐amyloid clearance
Xu, L., Li, L., Pan, C., Song, J., Zhang, C., Wu, X., Hu, F., Liu, X., Zhang, Z., & Zhang, Z. (2022) · The EMBO Journal · doi:10.15252/embj.2022111038 · Cited by 29 · see citing works
Cheng, Y., Saville, L., Gollen, B., Isaac, C., Belay, A., Mehla, J., Patel, K., Thakor, N., Mohajerani, M. H., & Zovoilis, A. (2020) · eLife · doi:10.7554/elife.61265 · Cited by 28 · see citing works
Stevenson, M. E., Varghese, R. S., Hebron, M. L., Liu, X., Ratliff, N., Smith, A., Turner, R. S., & Moussa, C. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02802-0 · Cited by 28 · see citing works
Cahalane, C., Bonezzi, J., Shelestak, J., Clements, R. J., Boika, A., Yun, Y., & Shriver, L. P. (2020) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.9b00489 · Cited by 28 · see citing works
Identification of Immune Cells and Key Genes associated with Alzheimer's Disease
Liu, C., Zhang, X., Chai, H., Xu, S., Liu, Q., Luo, Y., & Li, S. (2021) · International Journal of Medical Sciences · doi:10.7150/ijms.66422 · Cited by 28 · see citing works
Assaying Microglia Functions In Vitro
Maguire, E., Connor‐Robson, N., Shaw, B., O’Donoghue, R., Stöberl, N., & Hall‐Roberts, H. (2022) · Cells · doi:10.3390/cells11213414 · Cited by 27 · see citing works
Microglial Endocannabinoid Signalling in AD
Scipioni, L., Ciaramellano, F., Carnicelli, V., Leuti, A., Lizzi, A. R., Dominicis, N. D., Oddi, S., & Maccarrone, M. (2022) · Cells · doi:10.3390/cells11071237 · Cited by 25 · see citing works
Ma, Y., Li, S., Qin, Y., He, X., Li, W., & Zhang, Y. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c00171 · Cited by 25 · see citing works
Xu, J., Liu, J., Li, Q., Li, G., Zhang, G., Mi, Y., Zhao, T., Mu, D., Wang, D., Zeng, K., et al. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.155011 · Cited by 26 · see citing works
Ge, X., Wang, Y., Yu, S., Cao, X., Chen, Y., Cheng, Q., & Ding, F. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.716177 · Cited by 22 · see citing works
Liu, A., Wang, T., Yang, L., & Zhou, Y. (2025) · Brain Sciences · doi:10.3390/brainsci15070675 · Cited by 22 · see citing works
Xu, Z., Nan, W., Zhang, X., Sun, Y., Yang, J., Lu, K., Liu, Y., Gao, Y., Yang, F., Mao, W., et al. (2018) · Journal of Molecular Neuroscience · doi:10.1007/s12031-018-1075-5 · Cited by 19 · see citing works
A multifaceted role of progranulin in regulating amyloid-beta dynamics and responses
Du, H., Wong, M. Y., Zhang, T., Santos, M. N., Hsu, C., Zhang, J., Yu, H., Luo, W., & Hu, F. (2021) · Life Science Alliance · doi:10.26508/lsa.202000874 · Cited by 19 · see citing works
Daily, K. P., Badr, A., Eltobgy, M. M., Estfanous, S. Z. K., Whitham, O. D., Tan, M. H., Carafice, C., Krause, K., McNamara, A. J., Hamilton, K., et al. (2024) · Alzheimer s Research & Therapy · doi:10.1186/s13195-024-01390-2 · Cited by 19 · see citing works
Cai, M., Zhang, Y., Chen, S. X., Wu, Z., & Zhu, L. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.968444 · Cited by 18 · see citing works
Functional aspects of the brain lymphatic drainage system in aging and neurodegenerative diseases
Chen, Y., He, X., Cai, J., & Li, Q. (2024) · Journal of Biomedical Research · doi:10.7555/jbr.37.20230264 · Cited by 18 · see citing works
Anwar, M. M., Özkan, E., Shomalizadeh, N., Sapancı, S., Özler, C., Kesibi, J., & Özdemir, Y. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.1041461 · Cited by 18 · see citing works
Periodic Variation of AAK1 in an Aβ1–42-Induced Mouse Model of Alzheimer’s Disease
Fu, X. L., Ke, M., Yu, W., Wang, X., Xiao, Q., Gu, M., & Lü, Y. (2018) · Journal of Molecular Neuroscience · doi:10.1007/s12031-018-1085-3 · Cited by 17 · see citing works
Ferrisi, R., Gado, F., Ricardi, C., Polini, B., Manera, C., & Chiellini, G. (2023) · Journal of Clinical Medicine · doi:10.3390/jcm12237201 · Cited by 16 · see citing works
Tsujioka, H., & Yamashita, T. (2019) · BMC Genomics · doi:10.1186/s12864-019-5974-9 · Cited by 16 · see citing works
Varinthra, P., Ganesan, K., Huang, S., Chompoopong, S., Eurtivong, C., Suresh, P., Wen, Z., & Liu, I. Y. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.615079 · Cited by 15 · see citing works
Marín-Castañeda, L. A., González-Garibay, G., Garcia-Quintana, I., Aispuro, G. P., & Rubio, C. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1494356 · Cited by 16 · see citing works
Mishra, S., Jayadev, S., & Young, J. E. (2024) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2022.0389 · Cited by 13 · see citing works
Temporal Quantitative Profiling of Newly Synthesized Proteins during Aβ Accumulation
Ma, Y., McClatchy, D. B., Martínez‐Bartolomé, S., Bamberger, C., & Yates, J. R. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00645 · Cited by 10 · see citing works
The Effect of Alzheimer’s Disease-Associated Genetic Variants on Longevity
Tesi, N., Hulsman, M., van der Lee, S. J., Jansen, I. E., Stringa, N., van Schoor, N. M., Scheltens, P., van der Flier, W. M., Huisman, M. A., Reinders, M. J. T., et al. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.748781 · Cited by 13 · see citing works
Xu, Y., Koch, S. C., Chamessian, A. G., He, Q., Sundukova, M., Heppenstall, P. A., Xu, Y., Fitzgerald, M., & Beggs, S. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.1354-23.2023 · Cited by 12 · see citing works
Bodart‐Santos, V., Ruan, Z., Melvin, B. C., Pandey, I., Ikezu, S., & Ikezu, T. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.115025 · Cited by 12 · see citing works
How Microglia Manages Non-cell Autonomous Vicious Cycling of Aβ Toxicity in the Pathogenesis of AD
Seol, Y., Ki, S., Ryu, H. L., Chung, S., Lee, J.-H., & Ryu, H. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.593724 · Cited by 12 · see citing works
Jiao, H., Ge, Y., Huang, L.-Y., Liu, Y., Wu, B., Lian, P., Hao, Y., Han, S., Li, Y., Wu, K., et al. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00887-0 · Cited by 11 · see citing works
Fritze, J., Muralidharan, C., Stamp, E., & Ahlenius, H. (2024) · Developmental Neurobiology · doi:10.1002/dneu.22939 · Cited by 12 · see citing works
Lachish, M., Fainstein, N., Ganz, T., Sofer, L., & Ben‐Hur, T. (2022) · Cells · doi:10.3390/cells11050876 · Cited by 12 · see citing works
Feng, L., Lo, H., Hong, Z., Zheng, J., Yan, Y., Ye, Z., Chen, X., & Pan, X. (2023) · Glia · doi:10.1002/glia.24422 · Cited by 12 · see citing works
Morais, G. P., Neto, I. V. D. S., Marafon, B. B., Ropelle, E. R., Cintra, D. E., Pauli, J. R., & da Silva, A. S. R. (2023) · Journal of Cellular Physiology · doi:10.1002/jcp.31005 · Cited by 11 · see citing works
Chongtham, A., Sharma, A., Nath, B., Murtha, K., Gorbachev, K., Ramakrishnan, A., Schmidt, E. F., Shen, L., & Pereira, A. C. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.114967 · Cited by 10 · see citing works
Leng, F., Initiative, O. B. O. A. D. N., Zhan, Z., Sun, Y., Liu, F., Edison, P., Sun, Y., & Wang, Z. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220102 · Cited by 11 · see citing works
Satoh, J., Kino, Y., Yanaizu, M., Ishida, T., & Saito, Y. (2018) · Intractable & Rare Diseases Research · doi:10.5582/irdr.2018.01119 · Cited by 10 · see citing works
Varinthra, P., Suresh, P., Chokkalingam, P., Ibiayo, A. G., & Liu, I. Y. (2022) · Tzu Chi Medical Journal · doi:10.4103/tcmj.tcmj_139_22 · Cited by 10 · see citing works
The Implication of Glial Metabotropic Glutamate Receptors in Alzheimer’s Disease
de Lima, I. B. Q., & Ribeiro, F. M. (2021) · Current Neuropharmacology · doi:10.2174/1570159x20666211223140303 · Cited by 9 · see citing works
The Cl− transporter ClC-7 is essential for phagocytic clearance by microglia
Iyer, H., & Talbot, W. S. (2024) · Journal of Cell Science · doi:10.1242/jcs.261616 · Cited by 7 · see citing works
Singh, A. S., Naqvi, A. R., & Chanu, M. T. (2026) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2026.01.050 · Cited by 7 · see citing works
FOXP1 is a Transcription Factor for the Alzheimer's Disease Risk Gene SORL1
Fu, X., Quan, S., Liang, W., Li, Y., Cai, H., Ren, Z., Xu, Y., Wang, Z., & Jia, L. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70011 · Cited by 5 · see citing works
Real-time pH imaging of macrophage lysosomes using the pH-sensitive probe ApHID
Solé‐Domènech, S., Singh, P. K., Funes, L., Ma, C.-I. J., Warren, J. D., & Maxfield, F. R. (2025) · Cell Reports Methods · doi:10.1016/j.crmeth.2025.101203 · Cited by 5 · see citing works
Self-citationWang, H., Guo, Y., Liang, Z., Liu, W., Guo, Z., Zhang, Y., Chen, Y., Jiang, B., & Zhang, L. (2026) · Aggregate · doi:10.1002/agt2.70289 · Cited by 5 · see citing works
Tejwani, L., Heffner, C. M., Balak, C. D., Skuja, L. L., Tatarakis, D., Rana, A., Yu, S. B., Fitzgerald, G. A., Ha, C., de Melo, G. L., et al. (2026) · Immunity · doi:10.1016/j.immuni.2026.07.009 · Cited by 7 · see citing works
Mazrad, Z. A. I., Leiske, M. N., Tabor, R. F., Nicolazzo, J. A., & Kempe, K. (2023) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.3c00140 · Cited by 5 · see citing works
Mécanismes, facteurs de risque et stratégies thérapeutiques dans la maladie d’Alzheimer
Maître, M., Klein, C., & Mensah‐Nyagan, A. G. (2017) · NPG. Neurologie, psychiatrie, gériatrie/NPG · doi:10.1016/j.npg.2016.12.006 · Cited by 5 · see citing works
Neurons Internalize Functionalized Micron-Sized Silicon Dioxide Microspheres
Wallace, V. J., Cimbro, R., Rubio, F. J., Fortuno, L. V., Necarsulmer, J., Koivula, P. P., Henderson, M. J., DeBiase, L. M., Warren, B. L., Harvey, B. K., et al. (2017) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-017-0479-z · Cited by 5 · see citing works
Tao, L., Hu, M., Zhang, X., Wang, X., Zhang, Y., Chen, X., Tang, J., & Wang, J. (2022) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2022.116090 · Cited by 4 · see citing works
Neuronal aging potentiates beta-amyloid generation via amyloid precursor protein endocytosisPreprint
Burrinha, T., Gomes, R. A., Terrasso, A. P., & Almeida, C. G. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/616540 · Cited by 4 · see citing works
Lysosomal enzyme tripeptidyl peptidase 1 plays a role in degradation of beta amyloid fibrilsPreprint
Cruz, D. L., El-Banna, M., Majumdar, A., Sleat, D. E., Muldowney, M., Lobel, P., & Maxfield, F. R. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/639682 · Cited by 4 · see citing works
Self-citationA comprehensive view of cell-type-specific temporal dynamics in human and mouse brainsPreprint
Lu, Z., Zhang, M., Lee, J., Sziraki, A., Anderson, S., Ge, S., Nelson, P. T., Zhou, W. Y., & Cao, J. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.01.509820 · Cited by 4 · see citing works
Daily, K. P., Badr, A., Eltobgy, M. M., Estfanous, S. Z. K., Whitham, O. D., Tan, M. H., Carafice, C., Krause, K., McNamara, A. J., Hamilton, K., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.30.555526 · Cited by 4 · see citing works
Lysosomes cell autonomously regulate myeloid cell states and immune responses
Tejwani, L., Balak, C., Skuja, L. L., Tatarakis, D., Rana, A., Fitzgerald, G. A., Ha, C., Lunkes de Melo, G., Sun, E. W., Heffner, C. M., et al. (2024) · doi:10.1101/2024.11.11.623074 · Cited by 4 · see citing works
Bolland, E., Burca, A. D., Wang, S. H., Khalil, A. K., & McLoughlin, G. (2025) · npj Aging · doi:10.1038/s41514-025-00305-1 · Cited by 4 · see citing works
Eto, S. F., Fernandes, D. C., Baldassi, A. C., Balbuena, T. S., Alecrim, J. V. D. C., de Carvalho, F. C. A., Lima, C., Lopes‐Ferreira, M., & Pizauro, J. M. (2021) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2021.08.019 · Cited by 3 · see citing works
La génétique de la maladie d’Alzheimer
Halla, S. B., Moutawakil, B. E., Kadmiri, N. E., & Nadifi, S. (2019) · NPG. Neurologie, psychiatrie, gériatrie/NPG · doi:10.1016/j.npg.2018.11.006 · Cited by 3 · see citing works
Iyer, H., Shen, K., Meireles, A. M., & Talbot, W. S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.27.357897 · Cited by 2 · see citing works
- Authors
- Solé-Domènech, S., Cruz, D. L., Capetillo-Zarate, E., & Maxfield, F. R.
- Affiliations
- Weill Cornell Medicine (US)
- Corresponding author
- Maxfield, Frederick R.
- Venue
- Ageing Research Reviews
- Publisher
- Elsevier BV
- Published
- 2016-12
- Volume
- 32
- Pages
- 89-103
- ISSN
- 1568-1637 (ISSN-L)
- PMC
- PMC5127718
- OpenAlex
- W2465699308
- Cited by
- 133
- References
- 218
- Citations by year
- 2026: 12 · 2025: 13 · 2024: 23 · 2023: 15 · 2022: 17 · 2021: 14 · 2020: 12 · 2019: 12 · 2018: 5 · 2017: 9 · 2016: 1
- FWCI
- 0.79
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Ageing Research Reviews (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Funders
- Swedish Research Council (637-2013-503)
- Topics
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- microglia, endocytic pathway, lysosomal biogenesis, Alzheimer's disease, amyloid beta degradation, aging, phagocytosis, antigen presentation, late endosomes, lysosomal storage disease, Alzheimer's disease therapeutics
- MeSH terms
- Aging, Alzheimer Disease, Animals, Humans, Lysosomes, Phagocytosis, Signal Transduction, Amyloid beta-Peptides, Microglia
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