The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Scavenger receptor-mediated adhesion of microglia to β-amyloid fibrils
Abstract
A pathological hallmark of Alzheimer's disease is the senile plaque, containing beta-amyloid fibrils, microglia and astrocytes. Beta-amyloid fibrils exert a cytotoxic effect on neurons, and stimulate microglia to produce neurotoxins, such as reactive oxygen species. Mononuclear phagocytes, including microglia, express scavenger receptors that mediate endocytosis of oxidized low-density lipoproteins, and adhesion to glucose-modified extra-cellular matrix proteins. Here we report that class A scavenger receptors mediate adhesion of rodent microglia and human monocytes to beta-amyloid fibril-coated surfaces leading to secretion of reactive oxygen species and cell immobilization. Thus, class A scavenger receptors are potential therapeutic targets in Alzheimer's disease.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Aβ clearance involves, in part36, phagocytosis and endocytosis via microglial scavenger receptors (SRs)37,38 and extracellular degradation by Aβ-degrading enzymes6,36.”
From Microglia in neurodegeneration (2018) · cites this paper as [38]
In the citing paper
“SR-A1 is an Aβ-phagocytic receptor37,38 expressed on microglia surrounding Aβ plaques in humans and Aβ-mice.”
From Microglia in neurodegeneration (2018) · cites this paper as [38]
Citations
Cites
Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.
Lorenzo, A., & Yankner, B. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12243 · Cited by 1,324
Activation of microglial cells by β-amyloid protein and interferon-γ
Meda, L., Cassatella, M. A., Szendrei, G. I., Otvos, L., Baron, P., Villalba, M., Ferrari, D., & Rossi, F. (1995) · Nature · doi:10.1038/374647a0 · Cited by 1,314
Characterization of ameboid microglia isolated from developing mammalian brain
Giulian, D., & Baker, T. J. (1986) · Journal of Neuroscience · doi:10.1523/jneurosci.06-08-02163.1986 · Cited by 1,300
Krieger, M., & Krieger, J. (1994) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.63.1.601 · Cited by 1,169
Quinn, M. T., Parthasarathy, S., Fong, L. G., & Steinberg, D. I. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.9.2995 · Cited by 1,138
Advanced glycation end products contribute to amyloidosis in Alzheimer disease
Vitek, M. P., Bhattacharya, K., Glendening, J. M., Stopa, E., Vlassara, H., Bucala, R., Manogue, K., & Cerami, A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.11.4766 · Cited by 806
Advanced Maillard reaction end products are associated with Alzheimer disease pathology.
Smith, M. A., Taneda, S., Richey, P. L., Miyata, S., Yan, S. D., Stern, D., Sayre, L. M., Monnier, V. M., & Perry, G. L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.12.5710 · Cited by 715
Pike, C. J., Walencewicz‐Wasserman, A. J., Kosmoski, J., Cribbs, D. H., Glabe, C. G., & Cotman, C. W. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64010253.x · Cited by 699
Fraser, I. P., Hughes, D. A., & Gordon, S. (1993) · Nature · doi:10.1038/364343a0 · Cited by 341
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
Flagged first, then by citations
Research works printed but not linked: 5
- Krieger, M. & Herz, J. A. Rev. Biochem. 63, 601–637 (1994). · DOI
- Narindrasorasak, S. et al. Lab. Invest. 72, 272–282 (1995).
- Elghetany, M. T., Saleem, A. & Ban, K. Annls clin. lab. Sci. 19, 190–195 (1989).
- Christie, R. H., Freeman, M. & Hyman, B. T. Am. J. Path. 148, 399–403 (1996).
- Hartung, H.-P. et al. Lab. Invest. 55, 209–216 (1986).
Cited by
Sorted by citations
Items 201–300 of 723
Blood-brain barrier integrity in the pathogenesis of Alzheimer’s disease
Huang, Z., Wong, L., Su, Y., Huang, X., Wang, N., Chen, H., & Yi, C. (2020) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2020.100857 · Cited by 135
Neuronal and microglial cathepsins in aging and age-related diseases
Nakanishi, H. (2003) · Ageing Research Reviews · doi:10.1016/s1568-1637(03)00027-8 · Cited by 128
Microglia in Alzheimer’s Disease in the Context of Tau Pathology
Perea, J. R., Bolós, M., & Ávila, J. (2020) · Biomolecules · doi:10.3390/biom10101439 · Cited by 134
Scavenger receptors: diverse activities and promiscuous binding of polyanionic ligands
Platt, N., & Gordon, S. (1998) · Chemistry & Biology · doi:10.1016/s1074-5521(98)90156-9 · Cited by 126
Maezawa, I., Nguyen, H. M., Di Lucente, J., Jenkins, D. P., Singh, V., Hilt, S., Kim, K., Rangaraju, S., Levey, A. I., Wulff, H., et al. (2018) · Brain · doi:10.1093/brain/awx346 · Cited by 125
Mechanism mediating oligomeric Aβ clearance by naïve primary microglia
Yang, C.-N., Shiao, Y.-J., Shie, F.-S., Guo, B.-S., Chen, P.-H., Cho, C.-Y., Chen, Y.-J., Huang, F.-L., & Tsay, H.-J. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.01.005 · Cited by 117
Gough, P. J., Greaves, D. R., & Gordon, S. (1998) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)33292-2 · Cited by 123
Ionic effects of the Alzheimer's disease β-amyloid precursor protein and its metabolic fragments
Fraser, S. P., Suh, Y.-H., & Djamgoz, M. B. A. (1997) · Trends in Neurosciences · doi:10.1016/s0166-2236(96)10079-5 · Cited by 127
Takeuchi, H., & Suzumura, A. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00189 · Cited by 127
Inflammatory mechanisms in neurodegeneration
Nichols, M. R., St‐Pierre, M., Wendeln, A., Makoni, N. J., Gouwens, L. K., Garrad, E. C., Sohrabi, M., Neher, J. J., Tremblay, M., & Combs, C. K. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14674 · Cited by 129
Husemann, J., Loike, J. D., Kodama, T., & Silverstein, S. C. (2001) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(01)00239-9 · Cited by 122
Self-citationRole of ERAB/l-3-Hydroxyacyl-coenzyme A Dehydrogenase Type II Activity in Aβ-induced Cytotoxicity
Yan, S. D., Shi, Y., Zhu, A., Fu, J., Zhu, H., Zhu, Y., Gibson, L., Stern, E., Collison, K. S., Al-Mohanna, F. A., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.4.2145 · Cited by 121
Prominent Receptors of Liver Sinusoidal Endothelial Cells in Liver Homeostasis and Disease
Pandey, E., Nour, A. S., & Harris, E. N. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00873 · Cited by 123
Schilling, T., & Eder, C. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22675 · Cited by 117
Amyloid fibril formation by pulmonary surfactant protein C
Gustafsson, M., Thyberg, J., Näslund, J., Eliasson, E., & Johansson, J. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01692-0 · Cited by 117
Murphy, G. M., Yang, L., & Cordell, B. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.33.20967 · Cited by 118
Yu, X., Guo, C., Fisher, P. B., Subjeck, J. R., & Wang, X. (2015) · Advances in cancer research · doi:10.1016/bs.acr.2015.04.004 · Cited by 122
Only amyloidogenic intermediates of transthyretin induce apoptosis
Andersson, K., Olofsson, A., Nielsen, E. H., Svehag, S., & Lundgren, E. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00465-5 · Cited by 116
Guedes, J. R., Lao, T., Cardoso, A. L., & El Khoury, J. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00549 · Cited by 115
Self-citationHusemann, J., & Silverstein, S. C. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64030-8 · Cited by 119
Self-citationShie, F., BREYER, R. M., & Montine, T. J. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)62336-x · Cited by 116
Aggregation and disaggregation of senile plaques in Alzheimer disease
Cruz, L., Urbanc, B., Buldyrev, S. V., Christie, R. H., Gómez‐Isla, T., Havlin, S., McNamara, M. J., Stanley, E., & Hyman, B. T. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.14.7612 · Cited by 115
Microglial metabolic flexibility: emerging roles for lactate
Monsorno, K., Buckinx, A., & Paolicelli, R. C. (2022) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2021.12.001 · Cited by 115
Kirkham, P., Spooner, G. M., Ffoulkes-Jones, C., & Calvez, R. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00390-3 · Cited by 113
Immunopathogenesis of brain abscess.
Kielian, T. (2004) · Journal of Neuroinflammation · doi:10.1186/1742-2094-1-16 · Cited by 111
Giri, R. K., Selvaraj, S. K., & Kalra, V. K. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.10.5281 · Cited by 111
Klegeris, A., Walker, D. G., & McGeer, P. L. (1997) · Brain Research · doi:10.1016/s0006-8993(96)01229-2 · Cited by 110
Lipid raft microdomains mediate class A scavenger receptor-dependent infection of Brucella abortus
Kim, S., Watarai, M., Suzuki, H., Makino, S., Kodama, T., & Shirahata, T. (2004) · Microbial Pathogenesis · doi:10.1016/j.micpath.2004.04.002 · Cited by 109
Badie, B., Schartner, J. M., Klaver, J., & Vorpahl, J. (1999) · Neurosurgery · doi:10.1097/00006123-199905000-00075 · Cited by 109
RAGE is a key cellular target for A -induced perturbation in Alzheimer s disease
Yan, S. S. (2011) · Frontiers in Bioscience-Scholar · doi:10.2741/265 · Cited by 108
Jhamandas, J. H., Wie, M., Harris, K. H., MacTavish, D., & Kar, S. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04111.x · Cited by 108
The role of complement in Alzheimer’s disease pathology
Emmerling, M. R., Watson, M. D., Raby, C. A., & Spiegel, K. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00042-9 · Cited by 110
Piermartiri, T., Figueiredo, C. P., Rial, D., Duarte, F. S., Bezerra, S. C., Mancini, G., Bem, A. F. D., Prediger, R. D., & Tasca, C. I. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2010.08.030 · Cited by 106
Lotz, M., Ebert, S., Esselmann, H., Iliev, A. I., Prinz, M., Wiazewicz, N., Wiltfang, J., Gerber, J., & Nau, R. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03188.x · Cited by 106
Sasaki, N., Takeuchi, M., Chowei, H., Kikuchi, S., Hayashi, Y., Nakano, N., Ikeda, H., Yamagishi, S., Kitamoto, T., Saito, T., et al. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(02)00310-5 · Cited by 105
Iribarren, P., Zhou, Y., Hu, J., Le, Y., & Wang, J. M. (2005) · Immunologic Research · doi:10.1385/ir:31:3:165 · Cited by 108
Tomokiyo, R.-I., Jinnouchi, K., Honda, M., Wada, Y., Hanada, N., Hiraoka, T., Suzuki, H., Kodama, T., Takahashi, K., & Takeya, M. (2002) · Atherosclerosis · doi:10.1016/s0021-9150(01)00624-4 · Cited by 103
Todt, J. C., Hu, B., & Curtis, J. L. (2008) · Journal of Leukocyte Biology · doi:10.1189/jlb.0307135 · Cited by 109
Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures
LaDu, M. J., Shah, J. A., Reardon, C. A., Getz, G. S., Bu, G., Hu, J., Guo, L., & Van Eldik, L. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000602200 · Cited by 103
Roberts, K., Zeineddine, R., Corcoran, L., Li, W., Campbell, I. L., & Yerbury, J. J. (2012) · Glia · doi:10.1002/glia.22444 · Cited by 107
The Blood–Brain Barrier in Alzheimer's Disease
Sharma, H. S., Castellani, R. J., Smith, M. A., & Sharma, A. (2012) · International review of neurobiology · doi:10.1016/b978-0-12-386986-9.00003-x · Cited by 105
Ray, B., Chauhan, N. B., & Lahiri, D. K. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07145.x · Cited by 104
Hu, J., & Eldik, L. J. V. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01804-1 · Cited by 101
Santiago-Garcı́a, J., Kodama, T., & Pitas, R. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208358200 · Cited by 100
Combs, C. K., Bates, P., Karlo, J. C., & Landreth, G. E. (2001) · Neurochemistry International · doi:10.1016/s0197-0186(01)00052-3 · Cited by 101
Macrophage Apoptosis in Advanced Atherosclerosis
Tabas, I. A., Seimon, T. A., Timmins, J. M., Li, G., & Lim, W.-S. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.04957.x · Cited by 100
Advances and Challenges in the Prevention and Treatment of Alzheimer's Disease
Brinton, R. D., & Yamazaki, R. S. (1998) · Pharmaceutical Research · doi:10.1023/a:1011963929012 · Cited by 99
The amyloid‐β peptide and its role in Alzheimer's disease
Clippingdale, A. B., Wade, J. D., & Barrow, C. J. (2001) · Journal of Peptide Science · doi:10.1002/psc.324 · Cited by 103
The α5β1 Integrin Mediates Elimination of Amyloid-β Peptide and Protects Against Apoptosis
Matter, M. L., Zhang, Z., Nordstedt, C., & Ruoslahti, E. I. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.4.1019 · Cited by 97
Shin, R., Ogino, K., Kondo, A., Saido, T. C., Trojanowski, J. Q., Kitamoto, T., & Tateishi, J. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-21-08187.1997 · Cited by 96
A key role for the microglial NADPH oxidase in APP-dependent killing of neurons
Qin, B., Cartier, L., Dubois‐Dauphin, M., Li, B., Serrander, L., & Krause, K. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.09.036 · Cited by 99
Nolte, C., Kirchhoff, F., & Kettenmann, H. (1997) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1997.tb01526.x · Cited by 95
Liu, L., Wan, W., Xia, S., Kalionis, B., & Li, Y. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.05.004 · Cited by 96
Microglial Contribution to Oxidative Stress in Alzheimer's Disease
Colton, C. A., Chernyshev, O. N., Gilbert, D. L., & Vitek, M. P. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06195.x · Cited by 96
Amyloid-β Induces Hepatic Insulin Resistance by Activating JAK2/STAT3/SOCS-1 Signaling Pathway
Zhang, Y., Zhou, B., Zhang, F., Wu, J., Hu, Y., Liu, Y., & Zhai, Q. (2012) · Diabetes · doi:10.2337/db11-0499 · Cited by 92
Receptors for chemotactic formyl peptides as pharmacological targets
Le, Y., Yang, Y., Cui, Y., Yazawa, H., Gong, W., Qiu, C., & Wang, J. M. (2002) · International Immunopharmacology · doi:10.1016/s1567-5769(01)00150-3 · Cited by 96
Calcium signaling in microglial cells
Möller, T. (2002) · Glia · doi:10.1002/glia.10152 · Cited by 92
Gough, P. J., Gordon, S., & Greaves, D. R. (2001) · Immunology · doi:10.1046/j.1365-2567.2001.01256.x · Cited by 92
Tomiyama, T., Kaneko, H., Kataoka, K.-I., Asano, S., & Endo, N. (1997) · Biochemical Journal · doi:10.1042/bj3220859 · Cited by 91
Monsonego, A., Imitola, J., Zota, V., Oida, T., & Weiner, H. L. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.5.2216 · Cited by 91
Kiyota, T., Gendelman, H. E., Weir, R. A., Higgins, E. E., Zhang, G., & Jain, M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.08.009 · Cited by 92
Wilkinson, K., Boyd, J. D., Glicksman, M. A., Moore, K. J., & Khoury, J. B. E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.232116 · Cited by 90
Self-citationMicroglial signalling cascades in neurodegenerative disease
Pocock, J. M., & Liddle, A. C. (2001) · Progress in brain research · doi:10.1016/s0079-6123(01)32103-9 · Cited by 91
Mitochondrial dysfunction and neurological disorders: A narrative review and treatment overview
Alshial, E. E., Abdulghaney, M. I., Wadan, A. S., Abdellatif, M. A., Ramadan, N. E., Suleiman, A. M., Waheed, N., Abdellatif, M., & Mohammed, H. S. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.122257 · Cited by 91
Role of Nuclear Factor‐Kappa B (NF‐κB) in Inflammation, Periodontitis, and Atherogenesis
Nichols, T. C., Fischer, T. H., Deliargyris, E., & Baldwin, A. S. (2001) · Annals of Periodontology · doi:10.1902/annals.2001.6.1.20 · Cited by 89
Clusterin and Alzheimer’s Disease
Calero, M., Rostagno, A. A., Frangione, B., & Ghiso, J. A. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_14 · Cited by 89
Molecular basis of Alzheimer's disease
Drouet, B., Pinçon‐Raymond, M., Chambaz, J., & Pillot, T. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050035 · Cited by 96
Do, H., Pyo, S., & Sohn, E. (2009) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2009.03.013 · Cited by 88
Tichauer, J. E., & Rommy von Bernhardi, M. (2012) · Journal of Neuroscience Research · doi:10.1002/jnr.23082 · Cited by 91
Iribarren, P., Chen, K., Hu, J., Gong, W., Cho, E. H., Lockert, S., Uranchimeg, B., & Wang, J. M. (2005) · The FASEB Journal · doi:10.1096/fj.05-4578fje · Cited by 92
All-D-Enantiomers of β-Amyloid Exhibit Similar Biological Properties to All-L-β-Amyloids
Cribbs, D. H., Pike, C. J., Weinstein, S. L., Velázquez, P., & Cotman, C. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.11.7431 · Cited by 89
Strohmeyer, R., Ramirez, M., Cole, G. J., Mueller, K., & Rogers, J. (2002) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(02)00272-2 · Cited by 87
Szczepanik, A. M., Rampe, D., & Ringheim, G. E. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.t01-1-00240.x · Cited by 94
Ershov, A. V., & Bazan, N. G. (2000) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(20000501)60:3 · Cited by 74
Zhang, D., Hu, X., Li, Q., Chen, S., Zhou, H., Wilson, B. C., Miller, D. S., & Hong, J. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-3 · Cited by 87
Neurotoxicity by microglia: Mechanisms and potential therapeutic strategy
Takeuchi, H. (2010) · Clinical and Experimental Neuroimmunology · doi:10.1111/j.1759-1961.2009.00001.x · Cited by 88
Statins reduce the neurofibrillary tangle burden in a mouse model of tauopathy
Boimel, M., Grigoriadis, N., Lourbopoulos, A., Touloumi, O., Rosenmann, D., Abramsky, O., & Rosenmann, H. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31819ac3cb · Cited by 86
Linehan, S. A., Martínez‐Pomares, L., & Gordon, S. (2002) · Advances in experimental medicine and biology · doi:10.1007/0-306-46831-x_1 · Cited by 85
Yang, L., Wang, W., Chen, J., Wang, N., & Zheng, G. (2018) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.36493 · Cited by 84
Zhang, K., Li, T. X., Liu, L., Feng, Y., Dong, Y.-B., Li, B., Shang, D., Fang, W., Cao, Y., & Chen, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072744 · Cited by 89
Wang, H., Li, Y., Ryder, J. W., Hole, J. T., Ebert, P. J., Airey, D. C., Qian, H.-R., Logsdon, B., Fisher, A., Ahmed, Z., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0296-y · Cited by 83
Herring, A., Blome, M., Ambrée, O., Sachser, N., Paulus, W., & Keyvani, K. (2009) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00257.x · Cited by 87
Non-steroidal Anti-inflammatory Drugs Stimulate Secretion of Non-amyloidogenic Precursor Protein
Avramovich‐Tirosh, Y., Amit, T., & Youdim, M. B. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201308200 · Cited by 86
Maxeiner, H., Husemann, J., Thomas, C. A., Loike, J. D., Khoury, J. B. E., & Silverstein, S. C. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.12.2257 · Cited by 80
Self-citationShapira, R., Solomon, B., Efrati, S., Frenkel, D., & Ashery, U. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.10.007 · Cited by 80
The Many Roles of the Class A Macrophage Scavenger Receptor
Platt, N., Haworth, R., Darley, L., & Gordon, S. (2002) · International review of cytology · doi:10.1016/s0074-7696(01)12002-4 · Cited by 81
Microglia and Synapse: Interactions in Health and Neurodegeneration
Šišková, Z., & Tremblay, M.-È. (2013) · Neural Plasticity · doi:10.1155/2013/425845 · Cited by 80
Molecular subtypes of ALS are associated with differences in patient prognosis
Eshima, J., O’Connor, S. A., Marschall, E., Bowser, R. P., Plaisier, C. L., & Smith, B. S. (2023) · Nature Communications · doi:10.1038/s41467-022-35494-w · Cited by 81
Untangling the role of amyloid in atherosclerosis
Howlett, G. J., & Moore, K. J. (2006) · Current Opinion in Lipidology · doi:10.1097/01.mol.0000245260.63505.4f · Cited by 79
Selective targeting of microglia by quantum dots
Minami, S., Sun, B., Popat, K. C., Kauppinen, T. M., Pleiss, M., Zhou, Y., Ward, M. E., Floreancig, P. E., Mucke, L., Desai, T. A., et al. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-22 · Cited by 79
Biological Role of the N-Formyl Peptide Receptors
Panaro, M. A., Acquafredda, A., Sisto, M., Lisi, S., Maffione, A. B., & Mitolo, V. (2006) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923970600625975 · Cited by 79
Chrysamine-G, a lipophilic analogue of congo red, inhibits Aβ-induced toxicity in PC12 cells
Klunk, W. E., Debnath, M. L., Koros, A. M. C., & Pettegrew, J. W. (1998) · Life Sciences · doi:10.1016/s0024-3205(98)00454-8 · Cited by 80
Muscarinic m1 receptor agonists increase the secretion of the amyloid precursor protein ectodomain
Müller, D., Mendla, K. D., Farber, S. A., & Nitsch, R. M. (1997) · Life Sciences · doi:10.1016/s0024-3205(97)00038-6 · Cited by 79
Cui, Y., Le, Y., Yazawa, H., Gong, W., & Wang, J. M. (2002) · Journal of Leukocyte Biology · doi:10.1189/jlb.72.4.628 · Cited by 79
Microglia as a critical player in both developmental and late-life CNS pathologies
Derecki, N. C., Katzmarski, N., Kipnis, J., & Meyer-Luehmann, M. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1321-z · Cited by 78
Oxidation of Aβ and Plaque Biogenesis in Alzheimer's Disease and Down Syndrome
Head, E., Garzon-Rodriguez, W., Johnson, J. K., Lott, I. T., Cotman, C. W., & Glabe, C. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0431 · Cited by 75
Misfolded Truncated Protein τ Induces Innate Immune Response via MAPK Pathway
Kovac, A., Zilka, N., Kazmerova, Z., Cente, M., Zilkova, M., & Novak, M. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100216 · Cited by 75
Efficacy and mechanism of cGAMP to suppress Alzheimer’s disease by elevating TREM2
Xu, Q., Xu, W., Cheng, H., Yuan, H., & Tan, X. (2019) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2019.07.004 · Cited by 75
Mazur, A., Holthoff, E. R., Vadali, S., Kelly, T. J., & Post, S. R. (2016) · PLoS ONE · doi:10.1371/journal.pone.0150287 · Cited by 75
Co-injection of β-amyloid with ibotenic acid induces synergistic loss of rat hippocampal neurons
Morimoto, K., Yoshimi, K., Tonohiro, T., Yamada, N., Oda, T., & Kaneko, I. (1998) · Neuroscience · doi:10.1016/s0306-4522(97)00507-1 · Cited by 75
Metadata
- Authors
- Khoury, J. E., Hickman, S. E., Thomas, C. A., Cao, L., Silverstein, S. C., & Loike, J. D.
- Affiliations
- Columbia University (US)
- Venue
- Nature
- Published
- 1996-08
- Volume
- 382
- Issue
- 6593
- Pages
- 716-719
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2045560271
- Cited by
- 727
- References
- 21
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 12 · 2023: 10 · 2022: 18 · 2021: 19 · 2020: 20 · 2019: 15 · 2018: 12 · 2017: 10 · 2016: 18 · 2015: 21 · 2014: 20 · 2013: 22 · 2012: 31
- FWCI
- 29.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
- Keywords
- scavenger receptors, scavenger receptor A, microglia, amyloid-beta fibrils, Alzheimer's disease, amyloid plaques, reactive oxygen species, monocytes, cell immobilization, therapeutic target
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Animals, Cell Adhesion, Cell Line, Cell Movement, Collagen, Humans, Ligands, Membrane Proteins, Molecular Sequence Data, Monocytes, Peptides, Receptors, Immunologic, Amyloid beta-Peptides, Reactive Oxygen Species, Microglia, Receptors, Lipoprotein, Receptors, Scavenger, Scavenger Receptors, Class A, Scavenger Receptors, Class B, Mice, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review