Scavenger receptor-mediated adhesion of microglia to β-amyloid fibrils

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

STRUCTURES AND FUNCTIONS OF MULTILIGAND LIPOPROTEIN RECEPTORS: Macrophage Scavenger Receptors and LDL Receptor-Related Protein (LRP)

Krieger, M., & Krieger, J. (1994) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.63.1.601 · Cited by 1,169

Oxidatively modified low density lipoproteins: a potential role in recruitment and retention of monocyte/macrophages during atherogenesis.

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

Structure‐Activity Analyses of β‐Amyloid Peptides: Contributions of the β25–35 Region to Aggregation and Neurotoxicity

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

Divalent cation-independent macrophage adhesion inhibited by monoclonal antibody to murine scavenger receptor

Fraser, I. P., Hughes, D. A., & Gordon, S. (1993) · Nature · doi:10.1038/364343a0 · Cited by 341

beta-Amyloid activates complement by binding to a specific region of the collagen-like domain of the C1q A chain.

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

Characterization of the Signaling Pathway Downstream p75 Neurotrophin Receptor Involved in β-Amyloid Peptide-Dependent Cell Death

Costantini, C., Rossi, F., Formaggio, E., Bernardoni, R., Cecconi, D., & Bianca, V. D. (2005) · Journal of Molecular Neuroscience · doi:10.1385/jmn:25:2:141 · Cited by 74

Shifting equilibriums in Alzheimer’s disease: the complex roles of microglia in neuroinflammation, neuronal survival and neurogenesis

Gray, S. C., Kinghorn, K. J., & Woodling, N. S. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.272571 · Cited by 76

Perturbations in calcium‐mediated signal transduction in microglia from Alzheimer's disease patients

McLarnon, J. G., Choi, H. B., Lue, L., Walker, D. G., & Kim, S. U. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20487 · Cited by 73

Chemotactic-like receptors and Aβ peptide induced responses in Alzheimer's Disease

Lorton, D. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00092-0 · Cited by 73

Innate Immunity in Alzheimer’s Disease: A Complex Affair

Guillot‐Sestier, M., & Town, T. (2013) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527311312050008 · Cited by 72

Role of scavenger receptor MARCO in macrophage responses to CpG oligodeoxynucleotides

Józefowski, S., Sulahian, T. H., Arredouani, M. S., & Kobzik, L. (2006) · Journal of Leukocyte Biology · doi:10.1189/jlb.0705357 · Cited by 71

DHA-PC and DHA-PS improved Aβ1–40 induced cognitive deficiency uncoupled with an increase in brain DHA in rats

Wen, M., Ding, L., Zhang, L., Zhou, M., Xu, J., Wang, J., Wang, Y., & Xue, C. (2016) · Journal of Functional Foods · doi:10.1016/j.jff.2016.02.004 · Cited by 71

Microglial interaction with β‐amyloid: Implications for the pathogenesis of Alzheimer's disease

Bamberger, M. E., & Landreth, G. E. (2001) · Microscopy Research and Technique · doi:10.1002/jemt.1121 · Cited by 74

Modulation of Nitric Oxide Production in Human Macrophages by Apolipoprotein-E and Amyloid-Beta Peptide

Vitek, M. P., Snell, J. C., Dawson, H. N., & Colton, C. A. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7408 · Cited by 71

3H-Deprenyl and 3H-PIB autoradiography show different laminar distributions of astroglia and fibrillar β-amyloid in Alzheimer brain

Marutle, A., Gillberg, P.-G., Bergfors, A., Yu, W., Ni, R., Nennesmo, I., Voytenko, L., & Nordberg, A. (2013) · Journal of Neuroinflammation · doi:10.1186/1742-2094-10-90 · Cited by 70

Cellular Mechanisms for Amyloid β-Protein Activation of Rat Cholinergic Basal Forebrain Neurons

Jhamandas, J. H., Cho, C., Jassar, B. S., Harris, K. H., MacTavish, D., & Easaw, J. C. (2001) · Journal of Neurophysiology · doi:10.1152/jn.2001.86.3.1312 · Cited by 70

A nasal proteosome adjuvant activates microglia and prevents amyloid deposition

Frenkel, D., Puckett, L. L., Petrovic, S., Xia, W., Chen, G., Vega, J., Dembinsky‐Vaknin, A., Shen, J., Plante, M., Burt, D. S., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21340 · Cited by 70

Broad-Spectrum Effects of 4-Aminopyridine to Modulate Amyloid β1–42-Induced Cell Signaling and Functional Responses in Human Microglia

Franciosi, S., Ryu, J. K., Choi, H. B., Radov, L. A., Kim, S. U., & McLarnon, J. G. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2490-06.2006 · Cited by 69

Subacute NO generation induced by Alzheimer's beta-amyloid in the living brain: reversal by inhibition of the inducible NO synthase

Ishii, K., Muelhauser, F., Liebl, U., Picard, M. A., Kühl, S., Penke, B., Bayer, T. A., Wießler, M., Hennerici, M. G., Beyreuther, K. T., et al. (2000) · The FASEB Journal · doi:10.1096/fj.99-0786com · Cited by 68

Modulation of β-Amyloid Fibril Formation in Alzheimer’s Disease by Microglia and Infection

Brown, M. R., Radford, S. E., & Hewitt, E. W. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.609073 · Cited by 67

Amyloid β-interacting partners in Alzheimer's disease: From accomplices to possible therapeutic targets

Han, S.-H., Park, J.-C., & Mook-Jung, I. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.12.004 · Cited by 67

The Biphasic Role of Microglia in Alzheimer's Disease

Mizuno, T. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/737846 · Cited by 73

Alpha7 nicotinic acetylcholine receptor-specific agonist DMXBA (GTS-21) attenuates Aβ accumulation through suppression of neuronal γ-secretase activity and promotion of microglial amyloid-β phagocytosis and ameliorates cognitive impairment in a mouse model of Alzheimer's disease

Takata, K., Amamiya, T., Mizoguchi, H., Kawanishi, S., Kuroda, E., Kitamura, R., Ito, A., Saito, Y., Tawa, M., Nagasawa, T., et al. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.10.021 · Cited by 68

CD36 overexpression in human brain correlates with β-amyloid deposition but not with Alzheimer's disease

Ricciarelli, R., d'Abramo, C., Zingg, J.-M., Giliberto, L., Markesbery, W., Azzi, A., Marinari, U. M., Pronzato, M. A., & Tabaton, M. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.01.007 · Cited by 66

Class A scavenger receptor promotes cerebral ischemic injury by pivoting microglia/macrophage polarization

Xu, Y., Qian, L., Zong, G., Ma, K., Zhu, X., Zhang, H., Li, N., Yang, Q., Bai, H., Ben, J., et al. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.05.036 · Cited by 66

Exploring the Formation of Alzheimer's Disease Senile Plaques in Silico

Edelstein‐Keshet, L., & Spiros, Ä. (2002) · Journal of Theoretical Biology · doi:10.1006/jtbi.2002.2540 · Cited by 66

Amyloid-Beta Peptide Is Toxic to Neurons In Vivo via Indirect Mechanisms

Walsh, D. T., Montero, R., Bresciani, L. G., Jen, A., Leclercq, P. D., Saunders, D., EL-Amir, A. N., Gbadamoshi, L., Gentleman, S. M., & Jen, L. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0485 · Cited by 70

Protective effects of asiaticoside derivatives against beta-amyloid neurotoxicity

Mook‐Jung, I., Shin, J., Yun, S. H., Huh, K., Koh, J. Y., Park, H. K., Jew, S., & Jung, M. W. (1999) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19991101)58:3 · Cited by 140

Dynamics of Plaque Formation in Alzheimer's Disease

Urbanc, B., Cruz, L., Buldyrev, S. V., Havlin, S., Irizarry, M. C., Stanley, E., & Hyman, B. T. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77295-4 · Cited by 65

Elimination of the Class A Scavenger Receptor Does Not Affect Amyloid Plaque Formation or Neurodegeneration in Transgenic Mice Expressing Human Amyloid Protein Precursors

Huang, F., Buttini, M., Wyss-Coray, T., McConlogue, L., Kodama, T., Pitas, R. E., & Mucke, L. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65489-2 · Cited by 49

PrP and β‐Amyloid Fragments Activate Different Neurotoxic Mechanisms in Cultured Mouse Cells

Brown, D. R., Herms, J. W., Schmidt, B., & Kretzschmar, H. A. (1997) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1997.tb01470.x · Cited by 65

Germ-line alterations in MSR1 gene and prostate cancer risk.

Seppälä, E. H., Ikonen, T., Autio, V., Rökman, A., Mononen, N., Matikainen, M. P., Tammela, T. L. J., & Schleutker, J. (2003) · PubMed · Cited by 64

Effects of Incorporation of Immunoglobulin G and Complement Component C1q on Uptake and Degradation of Alzheimer's Disease Amyloid Fibrils by Microglia

Brazil, M. I., Chung, H., & Maxfield, F. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000937200 · Cited by 64

μ-Amyloid Peptide-induced Apoptosis Regulated by a Novel Protein Containing a G Protein Activation Module

Kajkowski, E. M., Lo, C. F., Ning, X., Walker, S., Sofia, H. J., Wang, W., Edris, W., Chanda, P., Wagner, E., Vile, S., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011161200 · Cited by 63

Amyloid and lipids in the pathology of Alzheimer disease

Roher, A. E., Kuo, Y., Kokjohn, K., Emmerling, M. R., & Gracon, S. I. (1999) · Amyloid · doi:10.3109/13506129909007315 · Cited by 63

Amyloid Beta Peptide-Induced Cerebral Neuronal Loss Is Mediated By Caspase-3 In Vivo

Takuma, H., Tomiyama, T., Kuida, K., & Mori, H. (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.3.255 · Cited by 66

Therapeutic Potential of Allicin and Aged Garlic Extract in Alzheimer’s Disease

Tedeschi, P., Nigro, M., Travagli, A., Catani, M., Cavazzini, A., Merighi, S., & Gessi, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23136950 · Cited by 61

Macrophage Pattern Recognition Receptors in Immunity, Homeostasis and Self Tolerance

Mukhopadhyay, S., Plüddemann, A., & Gordon, S. (2009) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-0901-5_1 · Cited by 61

Amyloid cored plaques in Tg2576 transgenic mice are characterized by giant plaques, slightly activated microglia, and the lack of paired helical filament-typed, dystrophic neurites

Sasaki, A., Shoji, M., Harigaya, Y., Kawarabayashi, T., Ikeda, M., Naito, M., Matsubara, E., Abe, K., & Nakazato, Y. (2002) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/s00428-002-0643-8 · Cited by 63

Amyloid β-peptide induces cholinergic dysfunction and cognitive deficits: a minireview

Tran, M. H., Yamada, K., & Nabeshima, T. (2002) · Peptides · doi:10.1016/s0196-9781(02)00062-1 · Cited by 61

Receptors for Advanced Glycosylation Endproducts in Human Brain: Role in Brain Homeostasis

Li, J., Dickson, D. W., Hof, P. R., & Vlassara, H. (1998) · Molecular Medicine · doi:10.1007/bf03401729 · Cited by 62

The Neurobiology and Pharmacotherapy of Alzheimer's Disease

Félician, O., & Sandson, T. A. (1999) · Journal of Neuropsychiatry · doi:10.1176/jnp.11.1.19 · Cited by 61

Long-term changes in the aggregation state and toxic effects of β-amyloid injected into the rat brain

Giovannelli, L., Scali, C., Faussone‐Pellegrini, M. S., Pepeu, G., & Casamenti, F. (1998) · Neuroscience · doi:10.1016/s0306-4522(98)00169-9 · Cited by 61

Role of the Macrophage Inflammatory Protein-1α/CC Chemokine Receptor 5 Signaling Pathway in the Neuroinflammatory Response and Cognitive Deficits Induced by β-Amyloid Peptide

Passos, G. F., Figueiredo, C. P., Prediger, R. D., Pandolfo, P., Duarte, F. S., Medeiros, R., & Calixto, J. Β. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.081113 · Cited by 65

Inhibition of amyloid formation: a strategy to delay the onset of Alzheimer's disease

Lansbury, P. T. (1997) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(97)80018-x · Cited by 60

Expression of lipoprotein receptors in atherosclerotic lesions

Hiltunen, T. P., & Ylä‐Herttuala, S. (1998) · Atherosclerosis · doi:10.1016/s0021-9150(97)00307-9 · Cited by 60

Genetic requirement of p47 phox for superoxide production by murine microglia

Lavigne, M. C., Malech, H. L., Holland, S. M., & Leto, T. L. (2000) · The FASEB Journal · doi:10.1096/fj.00-0608fje · Cited by 59

Dendrimers reduce toxicity of Aβ 1-28 peptide during aggregation and accelerate fibril formation

Klajnert‐Maculewicz, B., Wasiak, T., Йонов, М., Fernandez‐Villamarin, M., Sousa‐Herves, A., Correa, J., Riguera, R., & Fernández-Megía, E. (2012) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2012.03.005 · Cited by 59

Antagonist of the Amylin Receptor Blocks β-Amyloid Toxicity in Rat Cholinergic Basal Forebrain Neurons

Jhamandas, J. H., & MacTavish, D. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1051-04.2004 · Cited by 62

Nondisposable materials, chronic inflammation, and adjuvant action

Hamilton, J. A. (2003) · Journal of Leukocyte Biology · doi:10.1189/jlb.0103037 · Cited by 59

Stress proteins and glial functions: possible therapeutic targets for neurodegenerative disorders

Kitamura, Y., & Nomura, Y. (2002) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(02)00301-7 · Cited by 59

Scavenger receptor A mediates H2O2 production and suppression of IL-12 release in murine macrophages

Józefowski, S., & Kobzik, L. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0504270 · Cited by 58

Cellular cofactors potentiating induction of stress and cytotoxicity by amyloid β-peptide

Yan, S. D., Roher, A. E., Chaney, M., Zloković, B. V., Schmidt, A. M., & Stern, D. M. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00041-7 · Cited by 58

Proinflammatory cytokine interferon‐γ increases induction of indoleamine 2,3‐dioxygenase in monocytic cells primed with amyloid β peptide 1–42: implications for the pathogenesis of Alzheimer’s disease

Yamada, A., Akimoto, H., Kagawa, S., Guillemin, G. J., & Takikawa, O. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06175.x · Cited by 58

CLAC Binds to Amyloid β Peptides through the Positively Charged Amino Acid Cluster within the Collagenous Domain 1 and Inhibits Formation of Amyloid Fibrils

Osada, Y., Hashimoto, T., Nishimura, A., Matsuo, Y., Wakabayashi, T., & Iwatsubo, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m413340200 · Cited by 57

Amyloid ox–tox transducers

Mattson, M. P., & Rydel, R. E. (1996) · Nature · doi:10.1038/382674a0 · Cited by 57

The amino-terminus of the amyloid-β protein is critical for the cellular binding and consequent activation of the respiratory burst of human macrophages

Muiswinkel, F. L. V., Raupp, S. F. A., Vos, N., Smits, H. A., Verhoef, J., Eikelenboom, P., & Nottet, H. S. L. M. (1999) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(99)00019-3 · Cited by 57

Macrophage Scavenger Receptor A Mediates Adhesion to Apolipoproteins A-I and E

Neyen, C. D., Plüddemann, A., Roversi, P., Thomas, B., Cai, L., van der Westhuyzen, D. R., Sim, R. B., & Gordon, S. (2009) · Biochemistry · doi:10.1021/bi9013769 · Cited by 56

γ‐Secretase component presenilin is important for microglia β‐amyloid clearance

Farfara, D., Trudler, D., Segev‐Amzaleg, N., Galron, R., Stein, R., & Frenkel, D. (2010) · Annals of Neurology · doi:10.1002/ana.22191 · Cited by 57

Regulation of glutamate in cultures of human monocytic THP-1 and astrocytoma U-373 MG cells

Klegeris, A., Walker, D. G., & McGeer, P. L. (1997) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(97)00094-5 · Cited by 56

Emerging Brain‐Pathophysiology‐Mimetic Platforms for Studying Neurodegenerative Diseases: Brain Organoids and Brains‐on‐a‐Chip

Bang, S., Lee, S., Choi, N., & Kim, H. N. (2021) · Advanced Healthcare Materials · doi:10.1002/adhm.202002119 · Cited by 57

β-Amyloid-related peptides potentiate K+-evoked glutamate release from adult rat hippocampal slices

Kabogo, D., Rauw, G. A., Amritraj, A., Baker, G. B., & Kar, S. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.08.009 · Cited by 55

Neuroinflammation in Alzheimer's disease: protector or promoter?

Žilka, N., Ferencĭk, M., & Hulín, I. (2006) · Bratislavské lekárske listy/Bratislava medical journal · doi:10.1007/bf03656856 · Cited by 58

Effects of Transforming Growth Factor-β (Isoforms 1–3) on Amyloid-β Deposition, Inflammation, and Cell Targeting in Organotypic Hippocampal Slice Cultures

Harris‐White, M. E., Chu, T., Balverde, Z., Sigel, J. J., Flanders, K. C., & Frautschy, S. A. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-24-10366.1998 · Cited by 55

Neural stem/progenitor cells in Alzheimer's disease.

Tincer, G., Mashkaryan, V., Bhattarai, P., & Kızıl, Ç. (2016) · Europe PMC (PubMed Central) · Cited by 56

Microglial activation depends on beta‐amyloid conformation: role of the formylpeptide receptor 2

Heurtaux, T., Michelucci, A., Losciuto, S., Gallotti, C., Felten, P., Dorban, G., Grandbarbe, L., Morga, E., & Heuschling, P. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06783.x · Cited by 55

Myeloid differentiation factor 88-deficient bone marrow cells improve Alzheimer’s disease-related symptoms and pathology

Hao, W., Liu, Y., Liu, S., Walter, S., Grimm, M. O. W., Kiliaan, A. J., Penke, B., Hartmann, T., Rübe, C. E., Menger, M. D., et al. (2010) · Brain · doi:10.1093/brain/awq325 · Cited by 54

Ameliorating Amyloid-β Fibrils Triggered Inflammation via Curcumin-Loaded Polymeric Nanoconstructs

Ameruoso, A., Palomba, R., Palange, A. L., Cervadoro, A., Lee, A., Mascolo, D. D., & Decuzzi, P. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01411 · Cited by 54

Oxidized lipoproteins increase reactive oxygen species formation in microglia and astrocyte cell lines

Keller, J. N., Hanni, K. B., Gabbita, S. P., Friebe, V., Mattson, M. P., & Kindy, M. S. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01272-x · Cited by 53

Effect of β-amyloid block of the fast-inactivating K + channel on intracellular Ca 2+ and excitability in a modeled neuron

Good, T. A., & Murphy, R. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.26.15130 · Cited by 53

Minocycline does not affect amyloid β phagocytosis by human microglial cells

Familian, A., Eikelenboom, P., & Veerhuis, R. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.01.052 · Cited by 53

Comparison of Inflammatory and Acute-Phase Responses in the Brain and Peripheral Organs of the ME7 Model of Prion Disease

Cunningham, C. M., Wilcockson, D. C., Boche, D., & Perry, V. H. (2005) · Journal of Virology · doi:10.1128/jvi.79.8.5174-5184.2005 · Cited by 53

Class A scavenger receptors and the phagocytosis of apoptotic cells

Platt, N., da Silva, R. P., & Gordon, S. (1999) · Immunology Letters · doi:10.1016/s0165-2478(98)00118-7 · Cited by 53

The Role of the Mouse Macrophage Scavenger Receptor in Myelin Phagocytosis

Costa, C. C., van der Laan, L. J. W., Dijkstra, C. D., & Brück, W. (1997) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1997.tb01694.x · Cited by 53

Oxidized low density lipoprotein caused CNS neuron cell death

Sugawa, M., Ikeda, S., Kushima, Y., Takashima, Y., & Cynshi, O. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00468-x · Cited by 53

Involvement of phosphoinositide 3-kinase γ in the neuro-inflammatory response and cognitive impairments induced by β-amyloid 1–40 peptide in mice

Passos, G. F., Figueiredo, C. P., Prediger, R. D., Silva, K. A. B. S., Siqueira, J. M., Duarte, F. S., Leal, P. C., Medeiros, R., & Calixto, J. Β. (2009) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2009.12.003 · Cited by 55

Class A Scavenger Receptor-mediated Adhesion and Internalization Require Distinct Cytoplasmic Domains

Kosswig, N., Rice, S., Daugherty, A., & Post, S. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303465200 · Cited by 52

Blockade of α5β1 Integrins Reverses the Inhibitory Effect of Tenascin on Chemotaxis of Human Monocytes and Polymorphonuclear Leukocytes Through Three-Dimensional Gels of Extracellular Matrix Proteins

Loike, J. D., Cao, L., Budhu, S., Hoffman, S., & Silverstein, S. C. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.12.7534 · Cited by 52

Innate Immune Response Gene Expression Profiles of N9 Microglia Are Pathogen-Type Specific

McKimmie, C. S., Roy, D., Forster, T., & Fazakerley, J. K. (2006) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2006.03.012 · Cited by 51

Guanosine Prevents Anhedonic-Like Behavior and Impairment in Hippocampal Glutamate Transport Following Amyloid-β1–40 Administration in Mice

Lanznaster, D., Mack, J. M., Coelho, V., Ganzella, M., Almeida, R. F., Dal-Cim, T. A., Hansel, G., Zimmer, E. R., Souza, D. O., Prediger, R. D., et al. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0082-1 · Cited by 53

Molecular and cellular mediators of Alzheimer's disease inflammation

Strohmeyer, R., & Rogers, J. (2001) · Journal of Alzheimer s Disease · doi:10.3233/jad-2001-3118 · Cited by 52

Inflammation in Alzheimer’s disease: insights from immunotherapy

Schott, J. M., & Révész, T. (2013) · Brain · doi:10.1093/brain/awt231 · Cited by 51

β-Amyloid peptide toxicity in organotypic hippocampal slice culture involves Akt/PKB, GSK-3β, and PTEN

Nassif, M., Hoppe, J. B., Santin, K., Frozza, R. L., Zamin, L. L., Simão, F., Horn, A. P., & Salbego, C. G. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2006.08.008 · Cited by 52

Pro-inflammatory conditions promote neuronal damage mediated by Amyloid Precursor Protein and decrease its phagocytosis and degradation by microglial cells in culture

Rommy von Bernhardi, M., Ramírez, G., Toro, R., & Eugenín, J. L. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.12.006 · Cited by 51

Integrin Mac-1 and β-amyloid in microglial release of nitric oxide

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Honda, M., Akiyama, H., Yamada, Y., Kondo, H., Kawabe, Y., Takeya, M., Takahashi, K., Suzuki, H., Doi, T., Sakamoto, A., et al. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8120 · Cited by 48

Untitled work

(1999) · doi:10.1002/(sici)1097-4547(19990815)57:4

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Viel, J. J., McManus, D. Q., Smith, S. S., & Brewer, G. J. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.1097 · Cited by 46

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