The role of microglia in amyloid clearance from the AD brain
Open accessAbstract
Alzheimer's disease (AD), the most prominent cause of senile dementia, is clinically characterized by the extracellular deposition of beta-amyloid (Abeta) and the intracellular neurofibrillary tangles. It has been well accepted that AD pathogenesis arises from perturbation in the homeostasis of Abeta in the brain. Abeta is normally produced at high levels in the brain and cleared in an equivalent rate. Thus, even a moderate decrease in the clearance leads to the accumulation of Abeta and subsequent amyloid deposition. Microglia are the tissue macrophages in the central nervous system (CNS) and have been shown to play major roles in internalization and degradation of Abeta. Abeta exists in the brain both in soluble and in fibrillar forms. Microglia interact with these two forms of Abeta in different ways. They take up soluble forms of Abeta through macropinocytosis and LDL receptor-related proteins (LRPs) mediated pathway. Fibrillar forms of Abeta interact with the cell surface innate immune receptor complex, initiating intracellular signaling cascades that stimulate phagocytosis. Inflammatory responses influence the activation status of microglia and subsequently regulate their ability to take up and degrade Abeta. ApoE and its receptors have been shown to play critical roles in these processes. In this review, we will explore the mechanisms that microglia utilize to clear Abeta and the effectors that modulate the processes.
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Restricting microglial Aβ uptake leads to increased cerebral Aβ levels.
“Evidence for a important role of microglial phagocytosis comes from studies that show that restricting microglial A uptake leads to increased cerebral A levels (El Khoury et al., 2007;Lee and Landreth, 2010).”
From PPARγ/RXRα-Induced and CD36-Mediated Microglial Amyloid-β Phagocytosis Results in Cognitive Improvement in Amyloid Precursor Protein/Presenilin 1 Mice (2012) · cites this paper as Lee and Landreth, 2010
The Fibrillar Aβ clearance section reports that mice with inactive TLR4 had greater cortical and hippocampal Aβ burden, and that their microglia were less efficient at taking up Aβ. It describes reduced microglial clearance as the study authors’ proposed explanation, not an established causal finding, and notes differing results for TLR2-deficient mice. The claim states the causal relationship more definitively than this review does. (LLM, conf=0.84)
Experimental — accuracy not yet measuredMicroglial expression of receptors that promote clearance and phagocytosis of Aβ, such as CD36, TLR4, and TLR6, are mandatory for restricting amyloid plaque formation.
“Microglial expression of receptors that promote the clearance and phagocytosis of A, such as CD36, TLR4, and TLR6 (Lee and Landreth, 2010), are mandatory for restricting amyloid plaque formation.”
From PPARγ/RXRα-Induced and CD36-Mediated Microglial Amyloid-β Phagocytosis Results in Cognitive Improvement in Amyloid Precursor Protein/Presenilin 1 Mice (2012) · cites this paper as Lee and Landreth, 2010
The Fibrillar Aβ clearance section identifies CD36, TLR4 and TLR6 in the microglial receptor complex involved in Aβ uptake and phagocytosis. It does not establish that expression of all three is mandatory for restricting plaques: it calls the effects of TLR inactivation on Aβ deposition confusing and reports differing outcomes across mouse models. (LLM, conf=0.88)
Experimental — accuracy not yet measuredMicroglia interacts with Aβ through a cell-surface receptor complex comprising CD36, α6β1 integrin, and CD47.
“Thus, microglia interacts with A through a recently characterized cell-surface receptor complex comprising CD36, ␣61 integrin, and CD47 (Lee and Landreth, 2010).”
From PPARγ/RXRα-Induced and CD36-Mediated Microglial Amyloid-β Phagocytosis Results in Cognitive Improvement in Amyloid Precursor Protein/Presenilin 1 Mice (2012) · cites this paper as Lee and Landreth, 2010
The “Fibrillar Aβ clearance” section identifies CD36, α6β1 integrin, and CD47 as components of a microglial cell-surface receptor complex for fibrillar Aβ. The “Soluble Aβ clearance” section says soluble Aβ is taken up differently, so the claim is too broad when it says Aβ without specifying its fibrillar form. (LLM, conf=0.87)
Experimental — accuracy not yet measuredMicroglia facilitate Aβ clearance through phagocytosis and can also exacerbate neurodegeneration by driving persistent neuroinflammation.
“For example, they facilitate the clearance of Aβ through phagocytosis42, yet they can also exacerbate neurodegeneration by driving persistent neuroinflammation43.”
From Deletion of SPI1 in microglia exacerbates amyloid pathology by impairing microglial response in Alzheimer’s disease models (2026) · cites this paper as [42]
Microglia dynamically interact with disease processes to influence AD progression.
“Microglia, the innate immune cells of the brain, dynamically interact with these disease processes to influence AD progression.”
From PLCG2 modulates TREM2 expression and signaling in response to Alzheimer's disease pathology (2025) · cites this paper as [5]
Microglia are critical for Aβ phagocytosis.
“Because microglia are critical for A phagocytosis, the microglial presence at the A plaque can be interpreted as an attempt to clear this pathological deposit.”
From PPARγ/RXRα-Induced and CD36-Mediated Microglial Amyloid-β Phagocytosis Results in Cognitive Improvement in Amyloid Precursor Protein/Presenilin 1 Mice (2012) · cites this paper as Lee and Landreth, 2010
Persisting neuroinflammation and sustained exposure to proinflammatory stimuli compromises microglial clearance functions as AD progresses.
“However, persisting neuroinflammation and sustained exposure to proinflammatory stimuli compromises microglial clearance functions as AD progresses (Lee and Landreth, 2010).”
From PPARγ/RXRα-Induced and CD36-Mediated Microglial Amyloid-β Phagocytosis Results in Cognitive Improvement in Amyloid Precursor Protein/Presenilin 1 Mice (2012) · cites this paper as Lee and Landreth, 2010
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Cites
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
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
Alzheimer's disease: the amyloid cascade hypothesis
Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484 · see citing works
Resting microglial cells are highly dynamic surveillants of brain parenchyma in vivo
Nimmerjahn, A., Kirchhoff, F., & Helmchen, F. (2005) · Science · doi:10.1126/science.1110647 · Cited by 5,827 · see citing works
Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659 · see citing works
Microglia-mediated neurotoxicity: uncovering the molecular mechanisms
Block, M. L., Zecca, L., & Hong, J.-S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2038 · Cited by 4,110 · 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
A genome-wide association study identifies novel risk loci for type 2 diabetes
Sladek, R., Rocheleau, G., Rung, J., Dina, C., Shen, L., Serre, D., Boutin, P., Vincent, D., Belisle, A., Hadjadj, S., et al. (2007) · Nature · doi:10.1038/nature05616 · Cited by 2,993 · see citing works
Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., et al. (1995) · Nature · doi:10.1038/373523a0 · Cited by 2,516 · see citing works
Heterogeneity in the distribution and morphology of microglia in the normal adult mouse brain
Lawson, L. J., Perry, V. H., Dri, P., & Gordon, S. (1990) · Neuroscience · doi:10.1016/0306-4522(90)90229-w · Cited by 2,045 · 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
Microglial physiology: unique stimuli, specialized responses
Ransohoff, R. M., & Perry, V. H. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132528 · Cited by 1,858 · see citing works
Citron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A. Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., & Selkoe, D. J. (1992) · Nature · doi:10.1038/360672a0 · Cited by 1,757 · see citing works
APP Processing and Synaptic Function
Kamenetz, F., Tomita, T., Hsieh, H., Seabrook, G., Borchelt, D., Iwatsubo, T., Sisodia, S., & Malinow, R. (2003) · Neuron · doi:10.1016/s0896-6273(03)00124-7 · Cited by 1,644 · see citing works
Local self-renewal can sustain CNS microglia maintenance and function throughout adult life
Ajami, B., Bennett, J. L., Krieger, C., Tetzlaff, W., & Rossi, F. M. V. (2007) · Nature Neuroscience · doi:10.1038/nn2014 · Cited by 1,643 · see citing works
Purification and cloning of amyloid precursor protein β-secretase from human brain
Sinha, S., Anderson, J. P., Barbour, R., Basi, G. S., Caccavello, R., Davis, D., Doan, M., Dovey, H. F., Frigon, N., Hong, J., et al. (1999) · Nature · doi:10.1038/990114 · Cited by 1,612 · 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
Mullan, M., Crawford, F., Axelman, K., Houlden, H., Lilius, L., Winblad, B., & Lannfelt, L. (1992) · Nature Genetics · doi:10.1038/ng0892-345 · Cited by 1,513 · 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
Suzuki, N., Cheung, T. T., Cai, X.-D., Odaka, A., Otvos, L., Eckman, C., Golde, T. E., & Younkin, S. G. (1994) · Science · doi:10.1126/science.8191290 · Cited by 1,471 · see citing works
Shibata, M., Yamada, S., Kumar, S. R., Calero, M., Bading, J., Frangione, B., Holtzman, D. M., Miller, C. A., Strickland, D. K., Ghiso, J., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10498 · Cited by 1,413 · see citing works
Farris, W., Mansourian, S., Chang, Y., Lindsley, L., Eckman, E., Frosch, M., Eckman, C., Tanzi, R., Selkoe, D., & Guénette, S. (2003) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0230450100 · Cited by 1,361 · 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 · cited 4× · see citing works
“reported that the levels of IDE, NEP and MMP9 were dramatically reduced in older mice with the concomitant upregulation of proinflammatory cytokines (Hickman et al. 2008).”
BackgroundInfluentialSynaptic Activity Regulates Interstitial Fluid Amyloid-β Levels In Vivo
Cirrito, J. R., Yamada, K. A., Finn, M. B., Sloviter, R. S., Bales, K. R., May, P. C., Schoepp, D. D., Paul, S. M., Mennerick, S., & Holtzman, D. M. (2005) · Neuron · doi:10.1016/j.neuron.2005.10.028 · Cited by 1,265 · see citing works
Simard, A. R., Soulet, D., Gowing, G., Julien, J.-P., & Rivest, S. (2006) · Neuron · doi:10.1016/j.neuron.2006.01.022 · Cited by 1,265 · see citing works
Amyloid β-Protein Fibrillogenesis
Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., & Teplow, D. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22364 · Cited by 1,139 · see citing works
Microglia in the adult brain arise from Ly-6ChiCCR2+ monocytes only under defined host conditions
Mildner, A., Schmidt, H., Nitsche, M., Merkler, D., Hanisch, U.-K., Mack, M., Heikenwalder, M., Brück, W., Priller, J., & Prinz, M. (2007) · Nature Neuroscience · doi:10.1038/nn2015 · Cited by 1,089 · see citing works
Microglia and neuroinflammation: a pathological perspective
Streit (2004) · Journal of Neuroinflammation · doi:10.1186/1742-2094-1-14 · Cited by 1,039 · see citing works
Rapid appearance and local toxicity of amyloid-β plaques in a mouse model of Alzheimer’s disease
Meyer-Luehmann, M., Spires-Jones, T. L., Prada, C., Garcia-Alloza, M., de Calignon, A., Rozkalne, A., Koenigsknecht-Talboo, J., Holtzman, D. M., Bacskai, B. J., & Hyman, B. T. (2008) · Nature · doi:10.1038/nature06616 · Cited by 987 · see citing works
El Khoury, J., Toft, M., Hickman, S. E., Means, T. K., Terada, K., Geula, C., & Luster, A. D. (2007) · Nature Medicine · doi:10.1038/nm1555 · Cited by 915 · see citing works
Release of Excess Amyloid β Protein from a Mutant Amyloid β Protein Precursor
Cai, X.-D., Golde, T. E., & Younkin, S. G. (1993) · Science · doi:10.1126/science.8424174 · Cited by 913 · see citing works
Mahley, R. W., Weisgraber, K. H., & Huang, Y. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600549103 · Cited by 912 · see citing works
Adult mouse astrocytes degrade amyloid-β in vitro and in situ
Wyss-Coray, T., Loike, J. D., Brionne, T. C., Lu, E., Anankov, R., Yan, F., Silverstein, S. C., & Husemann, J. (2003) · Nature Medicine · doi:10.1038/nm838 · Cited by 909 · see citing works
Metabolic Regulation of Brain Aβ by Neprilysin
Iwata, N., Tsubuki, S., Takaki, Y., Shirotani, K., Lu, B., Gerard, N., Gerard, C., Hama, E., Lee, H., & Saido, T. (2001) · Science · doi:10.1126/science.1059946 · Cited by 894 · 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
Self-citationIbuprofen Suppresses Plaque Pathology and Inflammation in a Mouse Model for Alzheimer's Disease
Lim, G. P., Yang, F., Chu, T., Chen, P., Beech, W. K., Teter, B., Tran, T., Ubeda, O. J., Ashe, K. H., Frautschy, S. A., et al. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-15-05709.2000 · Cited by 876 · see citing works
Functional gamma‐secretase inhibitors reduce beta‐amyloid peptide levels in brain
Dovey, H. F., John, V., Anderson, J. P., Chen, L. Z., Andrieu, P. D. S. I., Fang, L. Y., Freedman, S. B., Folmer, B., Goldbach, E. G., Holsztynska, E. J., et al. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00012.x · Cited by 870 · see citing works
Iwata, N., Tsubuki, S., Takaki, Y., Watanabe, K., Sekiguchi, M., Hosoki, E., Kawashima-Morishima, M., Lee, H.-J., Hama, E., Sekine-Aizawa, Y., et al. (2000) · Nature Medicine · doi:10.1038/72237 · Cited by 867 · see citing works
LRP/Amyloid β-Peptide Interaction Mediates Differential Brain Efflux of Aβ Isoforms
Deane, R., Wu, Z., Sagare, A., Davis, J., Du Yan, S., Hamm, K., Xu, F., Parisi, M., LaRue, B., Hu, H. W., et al. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.017 · Cited by 828 · see citing works
Complement activation by beta-amyloid in Alzheimer disease.
Rogers, J., Cooper, N. R., Webster, S., Schultz, J., McGeer, P. L., Styren, S. D., Civin, W. H., Brachova, L., Bradt, B., & Ward, P. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.21.10016 · Cited by 817 · see citing works
Apolipoprotein E: a pathological chaperone protein in patients with cerebral and systemic amyloid
Wisniewski, T., & Frangione, B. (1992) · Neuroscience Letters · doi:10.1016/0304-3940(92)90444-c · Cited by 802 · see citing works
Hendriks, L., van Duijn, C. M., Cras, P. P., Cruts, M., Hul, W. V., van Harskamp, F., Warren, A., McInnis, M. G., Antonarakis, S. E., Martin, J., et al. (1992) · Nature Genetics · doi:10.1038/ng0692-218 · Cited by 735 · see citing works
Leissring, M. A., Farris, W., Chang, A. Y., Walsh, D. M., Wu, X., Sun, X., Frosch, M. P., & Selkoe, D. J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00787-6 · Cited by 708 · see citing works
APOLIPOPROTEIN E ALLELES AS RISK FACTORS IN ALZHEIMER'S DISEASE
Roses, M. D. (1996) · Annual Review of Medicine · doi:10.1146/annurev.med.47.1.387 · Cited by 707 · see citing works
Kirkitadze, M. D., Condron, M. M., & Teplow, D. B. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4970 · Cited by 684 · see citing works
Bell, R. D., Sagare, A. P., Friedman, A. E., Bedi, G. S., Holtzman, D. M., Deane, R., & Zlokovic, B. V. (2007) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600419 · Cited by 670 · 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
Priller, J., Flügel, A., Wehner, T., Boentert, M., Haas, C. A., Prinz, M., Fernández-Klett, F., Prass, K., Bechmann, I., de Boer, B. A., et al. (2001) · Nature Medicine · doi:10.1038/nm1201-1356 · Cited by 637 · see citing works
Human amyloid-β synthesis and clearance rates as measured in cerebrospinal fluid in vivo
Bateman, R. J., Munsell, L. Y., Morris, J. C., Swarm, R., Yarasheski, K. E., & Holtzman, D. M. (2006) · Nature Medicine · doi:10.1038/nm1438 · Cited by 599 · see citing works
Microglial response to amyloid plaques in APPsw transgenic mice.
Frautschy, S. A., Yang, F., Irrizarry, M., Hyman, B. T., Saido, T. C., Hsiao, K., & Cole, G. M. (1998) · Europe PMC (PubMed Central) · Cited by 592 · 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
Self-citationApolipoprotein E promotes astrocyte colocalization and degradation of deposited amyloid-β peptides
Koistinaho, M., Lin, S., Wu, X., Esterman, M., Koger, D., Hanson, J., Higgs, R., Liu, F., Malkani, S., Bales, K. R., et al. (2004) · Nature Medicine · doi:10.1038/nm1058 · Cited by 571 · see citing works
Heneka, M. T., Sastre, M., Dumitrescu-Ozimek, L., Hanke, A., Dewachter, I., Kuiperi, C., O'Banion, K., Klockgether, T., Van Leuven, F., & Landreth, G. E. (2005) · Brain · doi:10.1093/brain/awh452 · Cited by 565 · see citing works
Self-citationDeane, R., Bell, R. D., Sagare, A. P., & Zloković, B. V. (2009) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152709787601867 · Cited by 549 · see citing works
Qiu, W. Q., & Folstein, M. F. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.01.004 · Cited by 538 · 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
Guillemin, G. J., & Brew, B. J. (2003) · Journal of Leukocyte Biology · doi:10.1189/jlb.0303114 · Cited by 520 · 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
Self-citationRole of toll-like receptor signalling in A uptake and clearance
Tahara, K., Kim, H.-D., Jin, J.-J., Maxwell, J. A., Li, L., & Fukuchi, K.-I. (2006) · Brain · doi:10.1093/brain/awl249 · Cited by 493 · 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
Self-citationWahrle, 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
Chemokine Expression by Glial Cells Directs Leukocytes to Sites of Axonal Injury in the CNS
Babcock, A. A., Kuziel, W. A., Rivest, S., & Owens, T. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-21-07922.2003 · Cited by 472 · see citing works
Microglial Phagocytosis of Fibrillar β-Amyloid through a β1Integrin-Dependent Mechanism
Koenigsknecht-Talboo, J., & Landreth, G. E. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.2557-04.2004 · Cited by 444 · see citing works
Self-citationZlokovic, B. V., Martel, C. L., Matsubara, E., McComb, J. G., Zheng, G., McCluskey, R. T., Frangione, B., & Ghiso, J. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4229 · Cited by 430 · see citing works
Astrocytes accumulate Aβ42 and give rise to astrocytic amyloid plaques in Alzheimer disease brains
Nagele, R. G., D’Andrea, M. R., Lee, H., Venkataraman, V., & Wang, H.-Y. (2003) · Brain Research · doi:10.1016/s0006-8993(03)02361-8 · Cited by 416 · 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
Self-citationKurochkin, I. V., & Goto, S. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00387-4 · Cited by 401 · 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
Alzheimer's disease and Aβ toxicity: from top to bottom
Small, D. H., Mok, S. S., & Bornstein, J. C. (2001) · Nature reviews. Neuroscience · doi:10.1038/35086072 · Cited by 390 · see citing works
Sheng, J. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(03)00069-x · Cited by 388 · see citing works
Deficiency of ABCA1 Impairs Apolipoprotein E Metabolism in Brain
Hirsch-Reinshagen, V., Zhou, S., Burgess, B. L., Bernier, L., McIsaac, S. A., Chan, J. Y., Tansley, G. H., Cohn, J. S., Hayden, M. R., & Wellington, C. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407962200 · Cited by 385 · see citing works
Microglia and inflammatory mechanisms in the clearance of amyloid β peptide
Rogers, J., Strohmeyer, R., Kovelowski, C. J., & Li, R. (2002) · Glia · doi:10.1002/glia.10153 · Cited by 381 · see citing works
Microglia: activation and their significance in the central nervous system
Nakajima, K., & Kohsaka, S. (2001) · Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a002969 · Cited by 371 · see citing works
Overexpression of ABCA1 reduces amyloid deposition in the PDAPP mouse model of Alzheimer disease
Wahrle, S. E., Jiang, H., Parsadanian, M., Kim, J., Li, A., Knoten, A., Jain, S., Hirsch-Reinshagen, V., Wellington, C. L., Bales, K. R., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci33622 · Cited by 370 · cited 2× · see citing works
“On the other hand, overexpression of ABCA1 in the brain of PDAPP mouse model of AD reduced amyloid deposition (Wahrle et al. 2008).”
BackgroundRole of the Blood-Brain Barrier in the Pathogenesis of Alzheimers Disease
Deane, R., & Zloković, B. V. (2007) · Current Alzheimer Research · doi:10.2174/156720507780362245 · Cited by 365 · see citing works
Attenuation of neuroinflammation and Alzheimer's disease pathology by liver x receptors
Zelcer, N., Khanlou, N., Clare, R., Jiang, Q., Reed-Geaghan, E. G., Landreth, G. E., Vinters, H. V., & Tontonoz, P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701096104 · Cited by 358 · see citing works
Self-citationSimard, A. R., & Rivest, S. (2004) · The FASEB Journal · doi:10.1096/fj.04-1517fje · Cited by 354 · see citing works
Lack of ABCA1 Considerably Decreases Brain ApoE Level and Increases Amyloid Deposition in APP23 Mice
Koldamova, R., Staufenbiel, M., & Lefterov, I. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504513200 · Cited by 350 · see citing works
LPS receptor (CD14): a receptor for phagocytosis of Alzheimer's amyloid peptide
Liu, Y., Walter, S., Stagi, M., Cherny, D., Letièmbre, M., Schulz‐Schaeffer, W., Heine, H., Penke, B., Neumann, H., & Fassbender, K. C. (2005) · Brain · doi:10.1093/brain/awh531 · Cited by 344 · see citing works
Kennedy, D. W., & Abkowitz, J. L. (1997) · Blood · doi:10.1182/blood.v90.3.986 · Cited by 342 · see citing works
Jiang, H., Burdick, D., Glabe, C. G., Cotman, C. W., & Tenner, A. J. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.152.10.5050 · Cited by 330 · cited 2× · see citing works
“can activate the classical (antibody-dependent) pathway by binding Clq and the alternative (antibody-independent) pathway by binding C3b (Bradt et al. 1998; Chen et al. 1996; Jiang et al. 1994; Rogers et al. 1992; Webster et al. 1997).”
BackgroundDeletion of Abca1 Increases Aβ Deposition in the PDAPP Transgenic Mouse Model of Alzheimer Disease
Wahrle, S. E., Jiang, H., Parsadanian, M., Hartman, R. E., Bales, K. R., Paul, S. M., & Holtzman, D. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508780200 · Cited by 325 · see citing works
Maier, M., Peng, Y., Jiang, L., Seabrook, T. J., Carroll, M. C., & Lemere, C. A. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0829-08.2008 · Cited by 323 · see citing works
Glabinski, A. R., Balasingam, V., Tani, M., Kunkel, S. L., Strieter, R. M., Yong, V. W., & Ransohoff, R. M. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.156.11.4363 · Cited by 309 · see citing works
Malm, T. M., Koistinaho, M., Pärepalo, M., Vatanen, T., Ooka, A., Karlsson, S., & Koistinaho, J. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.09.009 · Cited by 301 · see citing works
Miller, B. C., Eckman, E. A., Sambamurti, K., Dobbs, N., Chow, K. M., Eckman, C. B., Hersh, L. B., & Thiele, D. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1031520100 · Cited by 294 · see citing works
PRESENILE DEMENTIA AND ALZHEIMER'S DISEASE IN MONGOLISM
Olson, M. I., & Shaw, C. (1969) · Brain · doi:10.1093/brain/92.1.147 · Cited by 290 · see citing works
Reply to: 'Clearance of amyloid β-peptide from brain: transport or metabolism?'
Iwata, N., Tsubuki, S., Hama, E., Takaki, Y., Shirotani, K., & Saido, T. C. (2000) · Nature Medicine · doi:10.1038/77399 · Cited by 285 · see citing works
Hematopoietic origin of microglial and perivascular cells in brain
Hess, D. C., Abe, T., Hill, W., Martin-Studdard, A., Carothers, J., Masuya, M., Fleming, P. A., Drake, C. J., & Ogawa, M. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2003.11.005 · Cited by 281 · see citing works
Frackowiak, J., Wisniewski, H. M., Wegiel, J., Merz, G. S., Iqbal, K., & Wang, K. C. (1992) · Acta Neuropathologica · doi:10.1007/bf00227813 · Cited by 276 · see citing works
Human<i>APOE</i>Isoform-Dependent Effects on Brain β-Amyloid Levels in PDAPP Transgenic Mice
Bales, K. R., Liu, F., Wu, S., Lin, S., Koger, D., DeLong, C., Hansen, J. C., Sullivan, P. M., & Paul, S. M. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.0887-09.2009 · Cited by 274 · see citing works
TOKUDA, T., CALERO, M., MATSUBARA, E., VIDAL, R., KUMAR, A., PERMANNE, B., ZLOKOVIC, B., SMITH, J. D., LADU, M. J., ROSTAGNO, A., et al. (2000) · Biochemical Journal · doi:10.1042/bj3480359 · Cited by 272 · 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
McAlpine, F. E., Lee, J., Harms, A. S., Ruhn, K. A., Blurton-Jones, M. M., Hong, J. J., Das, P., Golde, T. E., LaFerla, F. M., Oddo, S., et al. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.01.006 · Cited by 269 · 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
Formation and maintenance of Alzheimer’s disease beta-amyloid plaques in the absence of microglia
Grathwohl, S. A., Kälin, R., Bolmont, T., Prokop, S., Winkelmann, G., Kaeser, S. A., Odenthal, J., Radde, R., Eldh, T., Gandy, S. E., et al. (2010) · e-Neuroforum · doi:10.1515/nf-2010-0107 · Cited by 269 · see citing works
Characterizing the Appearance and Growth of Amyloid Plaques in APP/PS1 Mice
Yan, P., Bero, A. W., Cirrito, J. R., Xiao, Q., Hu, X., Wang, Y., Gonzales, E., Holtzman, D. M., & Lee, J.-M. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.2637-09.2009 · Cited by 264 · see citing works
Richard, K. L., Filali, M., Préfontaine, P., & Rivest, S. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.1146-08.2008 · Cited by 261 · see citing works
Narita, M., Holtzman, D. M., Schwartz, A. L., & Bu, G. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69051904.x · Cited by 259 · see citing works
Complement-dependent Proinflammatory Properties of the Alzheimer's Disease β-Peptide
Bradt, B. M., Kolb, W. P., & Cooper, N. R. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.3.431 · Cited by 255 · see citing works
Wısnıewskı, T., Ghiso, J. A., & Frangione, B. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91706-i · Cited by 247 · see citing works
Ultrastructural Studies of the Cells Forming Amyloid Fibers in Classical Plaques
Wisniewski, H. M., Węgiel, J., WANG, K. C., Kujawa, M., & Lach, B. (1989) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/s0317167100029887 · Cited by 244 · see citing works
A population study on blood-brain barrier function in 85-year-olds
Skoog, I. G., Wallin, A., Fredman, P., Hesse, C., Aevarsson, Ó., Karlsson, I., Gottfries, C. G., & Blennow, K. (1998) · Neurology · doi:10.1212/wnl.50.4.966 · Cited by 241 · see citing works
Morphologic association between microglia and senile plaque amyloid in Alzheimer's disease
Perlmutter, L. S., Barron, E., & Chui, H. C. (1990) · Neuroscience Letters · doi:10.1016/0304-3940(90)90748-x · Cited by 240 · see citing works
Reduced levels of amyloid β-peptide antibody in Alzheimer disease
Du, Y., Dodel, R. C., Hampel, H. J., Büerger, K., Lin, S., Eastwood, B. J., Bales, K. R., Gao, F., Moeller, H. –., Oertel, W. H., et al. (2001) · Neurology · doi:10.1212/wnl.57.5.801 · Cited by 234 · see citing works
Hirsch-Reinshagen, V., Maia, L. F., Burgess, B. L., Blain, J.-F., Naus, K. E., McIsaac, S. A., Parkinson, P. F., Chan, J. Y., Tansley, G. H., Hayden, M. R., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508781200 · Cited by 233 · see citing works
Wilcock, D. M., DiCarlo, G., Henderson, D., Jackson, J., Clarke, K., Ugen, K. E., Gordon, M. N., & Morgan, D. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-09-03745.2003 · Cited by 232 · see citing works
Liang, X., Wang, Q., Hand, T. A., Wu, L., BREYER, R. M., Montine, T. J., & Andreasson, K. I. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3591-05.2005 · Cited by 228 · see citing works
Intrahippocampal LPS injections reduce Aβ load in APP+PS1 transgenic mice
DiCarlo, G. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00292-5 · Cited by 223 · see citing works
The microglial phagocytic role with specific plaque types in the Alzheimer disease brain
D’Andrea, M. R., Cole, G. M., & Ard, M. D. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.12.026 · Cited by 215 · see citing works
Comery, T. A., Martone, R. L., Aschmies, S., Atchison, K. P., Diamantidis, G., Gong, X., Zhou, H., Kreft, A. F., Pangalos, M. N., Sonnenberg‐Reines, J., et al. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.2693-05.2005 · Cited by 214 · 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
Streit, W. J., & Xue, Q.-S. (2009) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-009-9163-5 · Cited by 205 · see citing works
Region‐specific reduction of Aβ‐degrading endopeptidase, neprilysin, in mouse hippocampus upon aging
Iwata, N., Takaki, Y., Fukami, S., Tsubuki, S., & Saido, T. C. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10390 · Cited by 203 · see citing works
Degradation of the Amyloid β-Protein by the Novel Mitochondrial Peptidasome, PreP
Falkevall, A., Alikhani, N., Bhushan, S., Pavlov, P. F., Busch, K., Johnson, K. A., Eneqvist, T., Tjernberg, L. O., Ankarcrona, M., & Glaser, E. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602532200 · Cited by 202 · see citing works
Eckman, E. A., Adams, S. K., Troendle, F. J., Stodola, B. A., Kahn, M. A., Fauq, A. H., Xiao, H. D., Bernstein, K. E., & Eckman, C. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605827200 · Cited by 196 · see citing works
Jordán, J., Galindo, M. F., Miller, R. J., Reardon, C. A., Getz, G. S., & LaDu, M. J. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-01-00195.1998 · Cited by 178 · see citing works
Amyloid β-degrading cryptidases: insulin degrading enzyme, presequence peptidase, and neprilysin
Malito, E., Hulse, R. E., & Tang, W.-J. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8112-4 · 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
The role of microglial cells and astrocytes in fibrillar plaque evolution in transgenic APPSW mice
Wegiel, J. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00181-0 · Cited by 159 · see citing works
Loss of Neprilysin Function Promotes Amyloid Plaque Formation and Causes Cerebral Amyloid Angiopathy
Farris, W., Schütz, S. G., Cirrito, J. R., Shankar, G. M., Sun, X., George, A., Leissring, M. A., Walsh, D. M., Qiu, W. Q., Holtzman, D. M., et al. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070105 · Cited by 155 · see citing works
(1998) · Europe PMC (PubMed Central) · Cited by 146 · see citing works
Autoantibodies to amyloid-? and Alzheimer's disease
Hyman, B. T., Smith, C. R., Buldyrev, I., Whelan, C. M., Brown, H., Tang, M., & Mayeux, R. P. (2001) · Annals of Neurology · doi:10.1002/ana.1061 · Cited by 144 · see citing works
Herber, D. L., Mercer, M., Roth, L. M., Symmonds, K., Maloney, J. L., Wilson, N., Freeman, M. J., Morgan, D., & Gordon, M. N. (2007) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-007-9069-z · Cited by 138 · see citing works
Complement Component C1q Modulates the Phagocytosis of Aβ by Microglia
Webster, S. D., Yang, A. J., Margol, L., Garzon-Rodriguez, W., Glabe, C. G., & Tenner, A. J. (2000) · Experimental Neurology · doi:10.1006/exnr.1999.7260 · Cited by 138 · see citing works
Grehan, S., Tse, E., & Taylor, J. M. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-03-00812.2001 · Cited by 138 · see citing works
Hardy, J. (1992) · Nature Genetics · doi:10.1038/ng0792-233 · Cited by 127 · see citing works
Does my mouse have Alzheimer's disease?
Dodart, J., Mathis, C., Bales, K. R., & Paul, S. M. (2002) · Genes Brain & Behavior · doi:10.1034/j.1601-183x.2002.10302.x · Cited by 125 · see citing works
Wegiel, J., Wang, K. C., Tarnawski, M., & Lach, B. (2000) · Acta Neuropathologica · doi:10.1007/s004010000199 · Cited by 124 · see citing works
Urmoneit, B., Prikulis, I., Wihl, G. E., D’Urso, D., Frank, R. W., Heeren, J., Beisiegel†, U., & Prior, R. (1997) · PubMed · Cited by 124 · see citing works
Qiao, X., Cummins, D. J., & Paul, S. M. (2001) · European Journal of Neuroscience · doi:10.1046/j.0953-816x.2001.01666.x · Cited by 119 · see citing works
Hemming, M. L., Patterson, M., Reske-Nielsen, C., Lin, L., Ole Isacson, A., & Selkoe, D. J. (2007) · PLoS Medicine · doi:10.1371/journal.pmed.0040262 · Cited by 119 · see citing works
Soto, C. A., & Castaño, E. M. (1996) · Biochemical Journal · doi:10.1042/bj3140701 · Cited by 116 · see citing works
Cerebrovascular Degeneration Is Related to Amyloid‐β Protein Deposition in Alzheimer's Disease a
Kalaria, R. N. (1997) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1997.tb48478.x · Cited by 109 · see citing works
Phagocytosis of ?/A4 amyloid fibrils of the neuritic neocortical plaques
Wisniewski, H. M., Barcikowska, M., & Kida, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00310142 · Cited by 109 · see citing works
Webster, S. D., Galvan, M. D., Ferran, E., Garzon-Rodriguez, W., Glabe, C. G., & Tenner, A. J. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.12.7496 · Cited by 104 · see citing works
Aggregation State‐Dependent Activation of the Classical Complement Pathway by the Amyloid β Peptide
Webster, S. D., Bradt, B. M., Rogers, J., & Cooper, N. R. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69010388.x · Cited by 103 · see citing works
Yamamoto, M., Kiyota, T., Walsh, S. M., Liu, J., Kipnis, J., & Ikezu, T. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.6.3877 · Cited by 100 · see citing works
Amyloid Angiopathy and Blood–Brain Barrier Changes in Alzheimer's Disease a, b
Wı́sniewski, H. M., VORBRODT, A. W., & WEGIEL, J. (1997) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1997.tb48468.x · Cited by 98 · see citing works
Lipid binding-induced conformational changes in the N-terminal domain of human apolipoprotein E
Fisher, C. A., & Ryan, R. O. (1999) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)33343-5 · Cited by 95 · see citing works
Production of Monocyte Chemotactic Protein‐1 By Rat Brain Macrophages
Calvo, C., Yoshirnura, T., Gelrnan, M., & Mallat, M. (1996) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1996.tb01316.x · Cited by 94 · see citing works
Moir, R. D., Tseitlin, K. A., Soscia, S. J., Hyman, B. T., Irizarry, M. C., & Tanzi, R. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414176200 · Cited by 88 · see citing works
Marzolo, M., Rommy von Bernhardi, M., Bu, G., & Inestrosa, N. C. (2000) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(20000501)60:3 · Cited by 87 · see citing works
Neprylisin decreases uniformly in Alzheimer's disease and in normal aging
Russo, R., Borghi, R., Markesbery, W. R., Tabaton, M., & Piccini, A. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.09.054 · Cited by 87 · see citing works
Chen, S., Frederickson, R. C. A., & Brunden, K. R. (1996) · Neurobiology of Aging · doi:10.1016/0197-4580(96)00103-0 · Cited by 69 · see citing works
Brazil, M. I., Chung, H., & Maxfield, F. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000937200 · Cited by 64 · see citing works
Zerbinatti, C., & Bu, G. (2005) · Reviews in the Neurosciences · doi:10.1515/revneuro.2005.16.2.123 · Cited by 62 · see citing works
Węgiel, J., Imaki, H., Wang, K.-C., Wegiel, J., & Rubenstein, R. (2004) · Brain Research · doi:10.1016/j.brainres.2004.06.058 · Cited by 61 · see citing works
Processing of Amyloid Precursor Protein and Amyloid Peptide Neurotoxicity
Pierrot, N., & Jean-Noël, O. (2008) · Current Alzheimer Research · doi:10.2174/156720508783954721 · Cited by 60 · see citing works
Origin and turnover of microglial cells in fibrillar plaques of APPsw transgenic mice
Węgiel, J., Imaki, H., Wang, K.-C., Wegiel, J., Wronska, A., Osuchowski, M., & Rubenstein, R. (2003) · Acta Neuropathologica · doi:10.1007/s00401-002-0660-3 · Cited by 59 · see citing works
Insulin Insults May Spur Alzheimer's Disease
Taubes, G. (2003) · Science · doi:10.1126/science.301.5629.40 · Cited by 52 · see citing works
Pluta, R. M., Barcikowska, M., Misicka, A., Lipkowski, A. W., Spisacka, S., & Januszewski, S. (1999) · Neuroreport · doi:10.1097/00001756-199911260-00028 · Cited by 47 · see citing works
Regulation of amyloid β-peptide levels by enzymatic degradation
Mukherjee, A., & Hersh, L. B. (2002) · Journal of Alzheimer s Disease · doi:10.3233/jad-2002-4501 · Cited by 41 · see citing works
LaDu, M. J., Stine, Narita, M., Getz, G. S., Reardon, C. A., & Bu, G. (2006) · Biochemistry · doi:10.1021/bi051765s · Cited by 36 · see citing works
[Senile dementia and Alzheimer's disease ].
Sanz, G. (1991) · PubMed · Cited by 30 · see citing works
Dergunov, A. D., Smirnova, E. A., Merched, A., Visvikis, S., Siest, G., Yakushkin, V. V., & Tsibulsky, V. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(99)00196-1 · Cited by 20 · see citing works
Volume 179, Number 3, September 30, 1991
(1991) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)81370-1 · Cited by 12 · see citing works
Flagged first, then by citations
4 of the 161 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
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
Self-citationNLRP3 is activated in Alzheimer’s disease and contributes to pathology in APP/PS1 mice
Heneka, M. T., Kummer, M. P., Stutz, A., Delekate, A., Schwartz, S., Vieira-Saecker, A., Griep, A., Axt, D., Remus, A., Tzeng, T.-C., et al. (2013) · Nature · doi:10.1038/nature11729 · Cited by 2,898 · see citing works
Immune attack: the role of inflammation in Alzheimer disease
Heppner, F. L., Ransohoff, R. M., & Becher, B. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3880 · Cited by 2,134 · see citing works
Neuroinflammation and M2 Microglia: The Good, the Bad, and the Inflamed
Cherry, J. D., Olschowka, J. A., & O’Banion, M. K. (2014) · Journal of Neuroinflammation · doi:10.1186/1742-2094-11-98 · Cited by 1,748 · see citing works
Clearance systems in the brain—implications for Alzheimer disease
Tarasoff-Conway, J. M., Carare, R. O., Osorio, R. S., Glodzik, L., Butler, T., Fieremans, E., Axel, L., Rusinek, H., Nicholson, C., Zlokovic, B. V., et al. (2015) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.119 · Cited by 1,678 · see citing works
Innate immune activation in neurodegenerative disease
Heneka, M. T., Kummer, M. P., & Latz, E. (2014) · Nature Reviews Immunology · doi:10.1038/nri3705 · Cited by 1,437 · 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
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
Innate immunity in Alzheimer's disease
Heneka, M. T., Golenbock, D. T., & Latz, E. (2015) · Nature Immunology · doi:10.1038/ni.3102 · Cited by 902 · see citing works
Microglia-mediated neuroinflammation in neurodegenerative diseases
Subhramanyam, C. S., Wang, C., Hu, Q., & Dheen, S. T. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.004 · Cited by 875 · see citing works
Yuan, P., Condello, C., Keene, C. D., Wang, Y., Bird, T. D., Paul, S. M., Luo, W., Colonna, M., Baddeley, D., & Grutzendler, J. (2016) · Neuron · doi:10.1016/j.neuron.2016.05.003 · Cited by 817 · see citing works
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
Therapeutics of Alzheimer's disease: Past, present and future
Anand, R., Gill, K. D., & Mahdi, A. A. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.07.004 · Cited by 748 · see citing works
Dash, U. C., Bhol, N. K., Swain, S. K., Samal, R. R., Nayak, P. K., Raina, V., Panda, S. K., Kerry, R. G., Duttaroy, A. K., & Jena, A. B. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.10.004 · Cited by 726 · see citing works
Phagocytosis of Microglia in the Central Nervous System Diseases
Fu, R., Shen, Q., Xu, P., Luo, J. J., & Tang, Y. (2014) · Molecular Neurobiology · doi:10.1007/s12035-013-8620-6 · Cited by 646 · see citing works
Protein transmission in neurodegenerative disease
Peng, C., Trojanowski, J. Q., & Lee, V. M.-Y. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-020-0333-7 · Cited by 625 · see citing works
Cannabidiol: State of the art and new challenges for therapeutic applications
Pisanti, S., Malfitano, A. M., Ciaglia, E., Lamberti, A., Ranieri, R., Cuomo, G., Abate, M., Faggiana, G., Proto, M., Fiore, D., et al. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.02.041 · Cited by 625 · see citing works
Physical exercise in the prevention and treatment of Alzheimer's disease
la Rosa, A. D., González, G. O., Arc‐Chagnaud, C., Millán-Domingo, F., Salvador‐Pascual, A., García-Lucerga, C., Blasco-Lafarga, C., García-Domínguez, E., Carretero, A., Correas, Á. G., et al. (2020) · Journal of sport and health science/Journal of Sport and Health Science · doi:10.1016/j.jshs.2020.01.004 · Cited by 617 · see citing works
Mechanisms of Aβ Clearance and Degradation by Glial Cells
Ries, M., & Sastre, M. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00160 · Cited by 527 · see citing works
“It is widely accepted that microglia phagocytose fibrillar Aβ, particularly more vigorously when bound by the C3b complement system (Lee and Landreth, 2010).”
BackgroundThe NLRP3 and NLRP1 inflammasomes are activated in Alzheimer’s disease
Saresella, M., La Rosa, F., Piancone, F., Zoppis, M., Marventano, I., Calabrese, E., Rainone, V., Nemni, R., Mancuso, R., & Clerici, M. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0088-1 · Cited by 489 · see citing works
Microglia and Astrocytes in Alzheimer's Disease: Implications for Therapy
Fakhoury, M. (2017) · Current Neuropharmacology · doi:10.2174/1570159x15666170720095240 · Cited by 482 · see citing works
Krabbe, G., Halle, A., Matyash, V., Rinnenthal, J. L., Eom, G. D., Bernhardt, U., Miller, K. R., Prokop, S., Kettenmann, H., & Heppner, F. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060921 · Cited by 478 · see citing works
Deciphering the mechanism underlying late-onset Alzheimer disease
Krstic, D., & Knuesel, I. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.236 · Cited by 457 · see citing works
The contribution of neuroinflammation to amyloid toxicity in Alzheimer's disease
Minter, M. R., Taylor, J. M., & Crack, P. J. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13411 · Cited by 451 · see citing works
An Efficient Platform for Astrocyte Differentiation from Human Induced Pluripotent Stem Cells
TCW, J., Wang, M., Pimenova, A. A., Bowles, K. R., Hartley, B. J., Lacin, E., Machlovi, S. I., Abdelaal, R., Karch, C. M., Phatnani, H., et al. (2017) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.06.018 · Cited by 435 · see citing works
Marsh, S. E., Abud, E. M., Lakatos, A., Karimzadeh, A., Yeung, S. T., Davtyan, H., Fote, G. M., Lau, L., Weinger, J. G., Lane, T. E., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1525466113 · Cited by 411 · see citing works
Neuroprotective strategies involving ROS in Alzheimer disease
Dumont, M., & Beal, M. F. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.11.026 · Cited by 402 · see citing works
Majumder, S., Richardson, A. G., Strong, R., & Oddo, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025416 · Cited by 401 · see citing works
RIPK1 mediates a disease-associated microglial response in Alzheimer’s disease
Ofengeim, D., Mazzitelli, S., Ito, Y., DeWitt, J. P., Mifflin, L., Zou, C., Das, S., Adiconis, X., Chen, H., Zhu, H., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1714175114 · Cited by 395 · see citing works
Zhong, L., Xu, Y., Zhuo, R., Wang, T., Wang, K., Huang, R., Wang, D., Gao, Y., Zhu, Y., Sheng, X., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09118-9 · Cited by 371 · see citing works
Webers, A., Heneka, M. T., & Gleeson, P. A. (2019) · Immunology and Cell Biology · doi:10.1111/imcb.12301 · Cited by 371 · see citing works
Salminen, A., Kaarniranta, K., Kauppinen, A., Ojala, J. O., Haapasalo, A., Soininen, H. S., & Hiltunen, M. O. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.06.002 · Cited by 366 · see citing works
Luo, R., Su, L.-Y., Li, G., Yang, J., Liu, Q., Yang, L.-X., Zhang, D.-F., Zhou, H., Xu, M., Fan, Y., et al. (2020) · Autophagy · doi:10.1080/15548627.2019.1596488 · Cited by 364 · see citing works
Bisht, K., Sharma, K. P., & Tremblay, M. (2018) · Neurobiology of Stress · doi:10.1016/j.ynstr.2018.05.003 · Cited by 351 · see citing works
Butovsky, O., Jedrychowski, M. P., Cialic, R., Krasemann, S., Murugaiyan, G., Fanek, Z., Greco, D. J., Wu, P. M., Doykan, C. E., Kiner, O., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24304 · Cited by 358 · see citing works
Inflammation, defective insulin signaling, and neuronal dysfunction in Alzheimer's disease
Ferreira, S. T., Clarke, J. R., Bomfim, T. R., & Felice, F. G. D. (2014) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.12.010 · Cited by 354 · see citing works
Microglia-Mediated Synapse Loss in Alzheimer's Disease
Rajendran, L., & Paolicelli, R. C. (2018) · The Journal of Neuroscience · doi:10.1523/jneurosci.1136-17.2017 · Cited by 355 · see citing works
Microglia Phenotypes in Aging and Neurodegenerative Diseases
Wendimu, M. Y., & Hooks, S. B. (2022) · Cells · doi:10.3390/cells11132091 · Cited by 336 · see citing works
Neuron–glia crosstalk in health and disease: fractalkine and CX 3 CR1 take centre stage
Sheridan, G. K., & Murphy, K. J. (2013) · Open Biology · doi:10.1098/rsob.130181 · Cited by 336 · see citing works
TREM2 Promotes Microglial Survival by Activating Wnt/β-Catenin Pathway
Zheng, H., Jia, L., Liu, C.-C., Rong, Z., Zhong, L., Yang, L., Chen, X.-F., Fryer, J. D., Wang, X., Zhang, Y.-W., et al. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.2459-16.2017 · Cited by 317 · see citing works
Features of Microglia and Neuroinflammation Relevant to Environmental Exposure and Neurotoxicity
Kraft, A. D., & Harry, G. J. (2011) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph8072980 · Cited by 330 · see citing works
Yamanaka, M., Ishikawa, T., Griep, A., Axt, D., Kummer, M. P., & Heneka, M. T. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.1569-12.2012 · Cited by 326 · see citing works
Immunologic Privilege in the Central Nervous System and the Blood–Brain Barrier
Muldoon, L. L., Alvarez, J. I., Begley, D. J., Boado, R. J., del Zoppo, G. J., Doolittle, N. D., Engelhardt, B., Hallenbeck, J. M., Lonser, R. R., Ohlfest, J. R., et al. (2012) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2012.153 · Cited by 327 · see citing works
Necroptosis in the Pathophysiology of Disease
Khoury, M. K., Gupta, K., Franco, S. R., & Liu, B. (2019) · American Journal Of Pathology · doi:10.1016/j.ajpath.2019.10.012 · Cited by 326 · see citing works
The identity and function of microglia in neurodegeneration
Song, W. M., & Colonna, M. (2018) · Nature Immunology · doi:10.1038/s41590-018-0212-1 · Cited by 308 · see citing works
Phagocytosis in the Brain: Homeostasis and Disease
Galloway, D. A., Phillips, A. E. M., Owen, D. R., & Moore, C. S. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00790 · Cited by 304 · see citing works
Lonnemann, N., Hosseini, S., Marchetti, C., Skouras, D. B., Stefanoni, D., D’Alessandro, A., Dinarello, C. A., & Korte, M. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2009680117 · Cited by 298 · see citing works
Anti-Inflammatory Effects of Resveratrol: Mechanistic Insights
Coutinho, D. D. S., Pacheco, M. T., Frozza, R. L., & Bernardi, A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19061812 · Cited by 298 · see citing works
Targeting Astrocytes Ameliorates Neurologic Changes in a Mouse Model of Alzheimer's Disease
Furman, J. L., Sama, D. M., Gant, J. C., Beckett, T. L., Murphy, M. P., Bachstetter, A. D., Van Eldik, L. J., & Norris, C. M. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.2323-12.2012 · Cited by 313 · see citing works
Arcuri, C., Mecca, C., Bianchi, R., Giambanco, I., & Donato, R. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00191 · Cited by 279 · see citing works
Microglia convert aggregated amyloid-β into neurotoxic forms through the shedding of microvesicles
Joshi, P., Turola, E., Ruiz, A., Bergami, A., Libera, D. D., Benussi, L., Giussani, P., Magnani, G., Comı, G., Legname, G., et al. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.180 · Cited by 274 · see citing works
Blood–brain-barriers in aging and in Alzheimer’s disease
Marques, F., Sousa, J. C., Sousa, N., & Palha, J. A. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-38 · Cited by 273 · see citing works
Aβ-degrading enzymes: potential for treatment of Alzheimer disease
Miners, J. S., Barua, N., Kehoe, P. G., Gill, S., & Love, S. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182345e46 · Cited by 265 · see citing works
How Do Immune Cells Support and Shape the Brain in Health, Disease, and Aging?
Schwartz, M., Kipnis, J., Rivest, S., & Prat, A. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3241-13.2013 · Cited by 256 · see citing works
Ceyzériat, K., Ben Haim, L., Denizot, A., Pommier, D., Matos, M., Guillemaud, O., Palomares, M.-A., Abjean, L., Petit, F., Gipchtein, P., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0606-1 · Cited by 256 · see citing works
Sex, glia, and development: Interactions in health and disease
Schwarz, J. M., & Bilbo, S. D. (2012) · Hormones and Behavior · doi:10.1016/j.yhbeh.2012.02.018 · Cited by 247 · see citing works
Neuroinflammation: A Common Pathway in CNS Diseases as Mediated at the Blood-Brain Barrier
Erickson, M. A., Dohi, K., & Banks, W. A. (2012) · NeuroImmunoModulation · doi:10.1159/000330247 · Cited by 246 · see citing works
Clayton, K., Delpech, J. C., Herron, S., Iwahara, N., Ericsson, M., Saito, T., Saido, T. C., Ikezu, S., & Ikezu, T. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00440-9 · Cited by 245 · see citing works
Booz, G. W. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.01.007 · Cited by 246 · see citing works
Spreading of Neurodegenerative Pathology via Neuron-to-Neuron Transmission of -Amyloid
Nath, S., Agholme, L., Kurudenkandy, F. R., Granseth, B., Marcusson, J., & Hallbeck, M. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0615-12.2012 · Cited by 244 · see citing works
Luo, W., Liu, W., Hu, X., Hanna, M., Caravaca, A., & Paul, S. M. (2015) · Scientific Reports · doi:10.1038/srep11161 · Cited by 241 · see citing works
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
Microglia and Alzheimer’s Disease
Merighi, S., Nigro, M., Travagli, A., & Gessi, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112990 · Cited by 236 · see citing works
The changing phenotype of microglia from homeostasis to disease
Luo, X., & Chen, S. (2012) · Translational Neurodegeneration · doi:10.1186/2047-9158-1-9 · Cited by 232 · see citing works
iPS-cell-derived microglia promote brain organoid maturation via cholesterol transfer
Park, D. S., Kozaki, T., Tiwari, S. K., Moreira, M., Khalilnezhad, A., Torta, F. T., Olivié, N., Thiam, C. H., Liani, O., Silvin, A., et al. (2023) · Nature · doi:10.1038/s41586-023-06713-1 · Cited by 237 · see citing works
Production and functions of IL-33 in the central nervous system
Yasuoka, S., Kawanokuchi, J., Parajuli, B., Jin, S., Doi, Y., Noda, M., Sonobe, Y., Takeuchi, H., Mizuno, T., & Suzumura, A. (2011) · Brain Research · doi:10.1016/j.brainres.2011.02.045 · Cited by 222 · see citing works
Zhong, L., Wang, Z., Wang, D., Wang, Z., Martens, Y. A., Wu, L., Xu, Y., Wang, K., Li, J., Huang, R., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0247-7 · Cited by 217 · see citing works
Alzheimer’s disease as an inflammatory disease
Bolós, M., Perea, J. R., & Avila, J. (2017) · BioMolecular Concepts · doi:10.1515/bmc-2016-0029 · Cited by 216 · see citing works
Qin, J., Ma, Z., Chen, X., & Shu, S. (2023) · Frontiers in Neurology · doi:10.3389/fneur.2023.1103416 · Cited by 229 · see citing works
Clearance of Amyloid Beta and Tau in Alzheimer’s Disease: from Mechanisms to Therapy
Xin, S.-H., Tan, L., Cao, X., Yu, J.-T., & Tan, L. (2018) · Neurotoxicity Research · doi:10.1007/s12640-018-9895-1 · Cited by 213 · see citing works
Kamphuis, W., Kooijman, L., Schetters, S., Orre, M., & Hol, E. M. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.07.007 · Cited by 209 · see citing works
Goyal, D., Ali, S. A., & Singh, R. K. (2020) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2020.110112 · Cited by 205 · see citing works
Challenges for Alzheimer's Disease Therapy: Insights from Novel Mechanisms Beyond Memory Defects
Frozza, R. L., Lourenco, M. V., & Felice, F. G. D. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00037 · Cited by 202 · see citing works
Maloney, J. A., Bainbridge, T. W., Gustafson, A. E., Zhang, S., Kyauk, R. V., Steiner, P., van der Brug, M., Liu, Y., Ernst, J. A., Watts, R. J., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.589069 · Cited by 199 · 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
Neuroinflammation and neurogenesis in Alzheimer's disease and potential therapeutic approaches
Sung, P.-S., Lin, P.-Y., Liu, C.-H., Su, H.-C., & Tsai, K.-J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030701 · Cited by 193 · see citing works
Basak, J. M., Verghese, P. B., Yoon, H., Kim, J., & Holtzman, D. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.288746 · Cited by 192 · see citing works
PSEN1ΔE9, APPswe, and APOE4 Confer Disparate Phenotypes in Human iPSC-Derived Microglia
Konttinen, H., Cabral-da-Silva, M. E. C., Ohtonen, S., Wojciechowski, S., Shakirzyanova, A., Caligola, S., Giugno, R., Ishchenko, Y., Hernández, D., Fazaludeen, M. F., et al. (2019) · Stem Cell Reports · doi:10.1016/j.stemcr.2019.08.004 · Cited by 191 · see citing works
Young microglia restore amyloid plaque clearance of aged microglia
Daria, A., Colombo, A., Llovera, G., Hampel, H., Willem, M., Liesz, A., Haass, C., & Tahirovic, S. (2017) · The EMBO Journal · doi:10.15252/embj.201694591 · Cited by 174 · see citing works
Mitochondrial Dysfunction in Alzheimers Disease: Opportunities forDrug Development
Bhatia, S., Rawal, R., Sharma, P., Singh, T., Singh, M., & Singh, V. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666210517114016 · Cited by 197 · see citing works
Migration of neutrophils targeting amyloid plaques in Alzheimer's disease mouse model
Baik, S. H., Cha, M.-Y., Hyun, Y.-M., Cho, H., Hamza, B., Kim, D. K., Han, S.-H., Choi, H., Kim, K. H., Moon, M., et al. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.01.003 · Cited by 181 · see citing works
Alzheimer's Disease Puzzle: Delving into Pathogenesis Hypotheses
(2024) · aging and disease · doi:10.14336/ad.2023.0608 · Cited by 183 · see citing works
Sphingolipids: Critical players in Alzheimer’s disease
van Echten‐Deckert, G., & Walter, J. (2012) · Progress in Lipid Research · doi:10.1016/j.plipres.2012.07.001 · Cited by 172 · see citing works
CD33 modulates TREM2: convergence of Alzheimer loci
Chan, G., White, C. C., Winn, P. A., Cimpean, M., Replogle, J. M., Glick, L. R., Cuerdon, N. E., Ryan, K. J., Johnson, K. A., Schneider, J. A., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4126 · Cited by 162 · see citing works
Clearance of Amyloid-β Peptides By Microglia and Macrophages: the Issue of What, When and Where
Lai, A. Y., & McLaurin, J. (2012) · Future Neurology · doi:10.2217/fnl.12.6 · Cited by 161 · see citing works
Bourgade, K., Le Page, A., Bocti, C., Witkowski, J. M., Dupuis, G., Frost, E. H., & Fülöp, T. (2016) · Journal of Alzheimer’s Disease · doi:10.3233/jad-150652 · Cited by 161 · see citing works
PLD3 affects axonal spheroids and network defects in Alzheimer’s disease
Yuan, P., Zhang, M., Tong, L., Morse, T. M., McDougal, R. A., Ding, H., Chan, D., Cai, Y., & Grutzendler, J. (2022) · Nature · doi:10.1038/s41586-022-05491-6 · Cited by 155 · see citing works
Neuroinflammation, gut microbiome, and Alzheimer's disease
Lin, L., Zheng, L. J., & Zhang, L. J. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0983-2 · Cited by 147 · see citing works
AlzPathway: a comprehensive map of signaling pathways of Alzheimer’s disease
Mizuno, S., Iijima, R., Ogishima, S., Kikuchi, M., Matsuoka, Y., Ghosh, S., Miyamoto, T., Miyashita, A., Kuwano, R., & Tanaka, H. (2012) · BMC Systems Biology · doi:10.1186/1752-0509-6-52 · Cited by 151 · see citing works
Intracellular Aβ-oligomers and early inflammation in a model of Alzheimer's disease
Ferretti, M. T., Bruno, M. A., Ducatenzeiler, A., Klein, W. L., & Cuello, A. C. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.01.007 · Cited by 146 · see citing works
Amyloid-β-Induced Astrocytic Phagocytosis is Mediated by CD36, CD47 and RAGE
Jones, R. S., Minogue, A. M., Connor, T. J., & Lynch, M. A. (2013) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-012-9427-3 · Cited by 147 · see citing works
Millan, M. J. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.03.004 · Cited by 146 · see citing works
Zhao, P., Xu, Y., Jiang, L., Fan, X., Li, L., Li, X., Arase, H., Zhao, Y., Cao, W., Zheng, H., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abq0095 · Cited by 141 · see citing works
Ma, T., Gong, K., Ao, Q., Yan, Y., Song, B., Huang, H.-Y., Zhang, X.-F., & Gong, Y.-D. (2013) · Cell Transplantation · doi:10.3727/096368913x672181 · Cited by 128 · see citing works
Guo, Z., Chen, Y., Mao, Y., Zheng, T., Jiang, Y., Yan, Y., Yin, X., & Zhang, B. (2017) · Scientific Reports · doi:10.1038/srep45971 · Cited by 143 · see citing works
Elia, C. A., Tamborini, M., Rasile, M., Desiato, G., Marchetti, S., Swuec, P., Mazzitelli, S., Clemente, F., Anselmo, A., Matteoli, M., et al. (2019) · Cells · doi:10.3390/cells8091059 · Cited by 142 · see citing works
New developments on the role of NMDA receptors in Alzheimer's disease
Malinow, R. (2012) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2011.09.001 · Cited by 132 · see citing works
Immunotherapy for neurodegenerative diseases: Focus on α-synucleinopathies
Valera, E., & Masliah, E. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.01.013 · Cited by 132 · see citing works
Microglia-Mediated Neuroprotection, TREM2, and Alzheimer’s Disease: Evidence From Optical Imaging
Condello, C., Yuan, P., & Grutzendler, J. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.10.007 · Cited by 131 · see citing works
Fairley, L. H., Lai, K. O., Wong, J. H., Chong, W. J., Vincent, A. S., D’Agostino, G. A., Wu, X., Naik, R. R., Jayaraman, A., Langley, S. R., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2209177120 · Cited by 127 · see citing works
- Authors
- Lee, C. Y. D., & Landreth, G. E.
- Affiliations
- Case Western Reserve University (US)
- Corresponding author
- Landreth, Gary E.
- ORCID
- Landreth, Gary E.
- Venue
- Journal of Neural Transmission
- Published
- 2010-06-15
- Volume
- 117
- Issue
- 8
- Pages
- 949-960
- ISSN
- 0300-9564 (ISSN-L)
- 1435-1463
- PMC
- PMC3653296
- OpenAlex
- W2038594716
- Cited by
- 701
- References
- 161
- Citations by year
- 2026: 26 · 2025: 49 · 2024: 74 · 2023: 54 · 2022: 66 · 2021: 50 · 2020: 51 · 2019: 43 · 2018: 56 · 2017: 31 · 2016: 29 · 2015: 43 · 2014: 35 · 2013: 36 · 2012: 31
- FWCI
- 3.02
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Journal of Neural Transmission (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (R01AG020202, R01AG030482, R01AG016740)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- microglia, amyloid-beta clearance, Alzheimer's disease, amyloid deposition, macropinocytosis, LDL receptor-related protein, phagocytosis, innate immune receptors, inflammation, microglial activation, apolipoprotein E, amyloid clearance
- MeSH terms
- Alzheimer Disease, Amyloid, Apolipoproteins E, Brain, Humans, Inflammation, Microglia
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