Involvement of Wiskott-Aldrich Syndrome Protein Family Verprolin-Homologous Protein (WAVE) and Rac1 in the Phagocytosis of Amyloid-β(1 – 42) in Rat Microglia

Rho GTPases and the Actin Cytoskeleton

Hall, A. (1998) · Science · doi:10.1126/science.279.5350.509 · Cited by 6,138 · see citing works

Inflammation and Alzheimer’s disease

Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514 · see citing works

Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia

Nobes, C. D., & Hall, A. (1995) · Cell · doi:10.1016/0092-8674(95)90370-4 · Cited by 4,414 · see citing works

Microglia: a sensor for pathological events in the CNS

Kreutzberg, G. W. (1996) · Trends in Neurosciences · doi:10.1016/0166-2236(96)10049-7 · Cited by 4,396 · see citing works

Peripherally administered antibodies against amyloid β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease

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

Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes

Holcomb, L., Gordon, M. N., McGowan, E., Yu, X., Benkovic, S., Jantzen, P., Wright, K., Saad, I., Mueller, R., Morgan, D., et al. (1998) · Nature Medicine · doi:10.1038/nm0198-097 · Cited by 1,386 · see citing works

Nonsteroidal Antiinflammatory Drugs and the Risk of Alzheimer's Disease

in 't Veld, B. A., Ruitenberg, A., Hofman, A., Launer, L. J., van Duijn, C. M., Stijnen, T., Breteler, M. M. B., & Stricker, B. H. C. (2001) · New England Journal of Medicine · doi:10.1056/nejmoa010178 · Cited by 1,196 · see citing works

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

Khoury, J. E., Hickman, S. E., Thomas, C. A., Cao, L., Silverstein, S. C., & Loike, J. D. (1996) · Nature · doi:10.1038/382716a0 · Cited by 727 · see citing works

WAVE, a novel WASP‐family protein involved in actin reorganization induced by Rac

Miki, H., Suetsugu, S., & Takenawa, T. (1998) · The EMBO Journal · doi:10.1093/emboj/17.23.6932 · Cited by 709 · see citing works

N‐WASP, a novel actin‐depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2‐dependent manner downstream of tyrosine kinases.

Miki, H., Miura, K., & Takenawa, T. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00917.x · Cited by 672 · see citing works

Microglial Cells Internalize Aggregates of the Alzheimer's Disease Amyloid β-Protein Via a Scavenger Receptor

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

Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP

Miki, H., Sasaki, T., Takai, Y., & Takenawa, T. (1998) · Nature · doi:10.1038/34208 · Cited by 644 · see citing works

WASP and WAVE family proteins: key molecules for rapid rearrangement of cortical actin filaments and cell mov

Takenawa, T., & Miki, H. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.10.1801 · Cited by 604 · see citing works

TGF-β1 promotes microglial amyloid-β clearance and reduces plaque burden in transgenic mice

Wyss-Coray, T., Lin, C., Yan, F., Yu, G.-Q., Rohde, M., McConlogue, L., Masliah, E., & Mucke, L. (2001) · Nature Medicine · doi:10.1038/87945 · Cited by 587 · see citing works

Brain to Plasma Amyloid-β Efflux: a Measure of Brain Amyloid Burden in a Mouse Model of Alzheimer's Disease

DeMattos, R. B., Bales, K. R., Cummins, D. J., Paul, S. M., & Holtzman, D. M. (2002) · Science · doi:10.1126/science.1067568 · Cited by 563 · see citing works

IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling

Miki, H., Yamaguchi, H., Suetsugu, S., & Takenawa, T. (2000) · Nature · doi:10.1038/35047107 · Cited by 557 · see citing works

Untitled work

Selkoe (1999) · doi:10.1038/19866 · Cited by 468 · see citing works

Amyloid-β immunotherapy for Alzheimer's disease: the end of the beginning

Schenk, D. (2002) · Nature Reviews Neuroscience · doi:10.1038/nrn938 · Cited by 436 · see citing works

Involvement of Iba1 in membrane ruffling and phagocytosis of macrophages/microglia

Ohsawa, K., Imai, Y., Kanazawa, H., Sasaki, Y., & Kohsaka, S. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.17.3073 · Cited by 420 · see citing works

Rho, Rac and Cdc42 regulate actin organization and cell adhesion in macrophages

Allen, W. E., Jones, G. E., Pollard, J. W., & Ridley, A. J. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.6.707 · Cited by 409 · see citing works

Association of Microglia with Amyloid Plaques in Brains of APP23 Transgenic Mice

Stalder, M., Phinney, A., Probst, A., Sommer, B., Staufenbiel, M., & Jucker, M. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65423-5 · Cited by 345 · see citing works

Microglial Activation and β-Amyloid Deposit Reduction Caused by a Nitric Oxide-Releasing Nonsteroidal Anti-Inflammatory Drug in Amyloid Precursor Protein Plus Presenilin-1 Transgenic Mice

Jantzen, P. T., Connor, K. E., DiCarlo, G., Wenk, G. L., Wallace, J. L., Rojiani, A. M., Coppola, D., Morgan, D., & Gordon, M. N. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-06-02246.2002 · Cited by 337 · see citing works

Microglial activation and amyloid‐β clearance induced by exogenous heat‐shock proteins

Kakimura, J., Kitamura, Y., Takata, K., Umeki, M., Suzuki, S., Shibagaki, K., Taniguchi, T., Nomura, Y., Gebicke‐Haerter, P. J., Smith, M. A., et al. (2002) · The FASEB Journal · doi:10.1096/fj.01-0530fje · Cited by 331 · see citing works

Age-Related Amyloid β Deposition in Transgenic Mice Overexpressing Both Alzheimer Mutant Presenilin 1 and Amyloid β Precursor Protein Swedish Mutant Is Not Associated with Global Neuronal Loss

Takeuchi, A., Irizarry, M. C., Duff, K., Saido, T. C., Hsiao Ashe, K., Hasegawa, M., Mann, D. M. A., Hyman, B. T., & Iwatsubo, T. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64544-0 · Cited by 229 · see citing works

Signal transduction of phagocytosis

Greenberg, S. (1995) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)88957-6 · Cited by 183 · see citing works

The complex of microglial cells and amyloid star in three-dimensional reconstruction

Węgiel, J., & Wı́sniewski, H. M. (1990) · Acta Neuropathologica · doi:10.1007/bf00334499 · Cited by 160 · see citing works

Expression of the macrophage scavenger receptor, a multifunctional lipoprotein receptor, in microglia associated with senile plaques in Alzheimer's disease.

Christie, R. H., Freeman, M. W., & Hyman, B. T. (1996) · PubMed · Cited by 152 · see citing works

A Novel Neural Wiskott-Aldrich Syndrome Protein (N-Wasp) Binding Protein, Wish, Induces Arp2/3 Complex Activation Independent of Cdc42

Fukuoka, M., Suetsugu, S., Miki, H., Fukami, K., Endo, T., & Takenawa, T. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.3.471 · Cited by 149 · see citing works

Dosing in phase II trial of Alzheimer's vaccine suspended

Senior, K. (2002) · The Lancet Neurology · doi:10.1016/s1474-4422(02)00023-6 · Cited by 88 · see citing works

Interleukin-4-inhibited mRNA expression in mixed rat glial and in isolated microglial cultures

Kitamura, Y., Taniguchi, T., Kimura, H., Nomura, Y., & Gebicke‐Haerter, P. J. (2000) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(00)00239-3 · Cited by 68 · see citing works

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 · see citing works

Synergistic effect of colchicine and cytochalasin D on phagocytosis by peritoneal macrophages

Mimura, N., & ASANO, A. (1976) · Nature · doi:10.1038/261319a0 · Cited by 54 · see citing works

Identification of N-WASP homologs in human and rat brain

Fukuoka, M., Miki, H., & Takenawa, T. (1997) · Gene · doi:10.1016/s0378-1119(97)00184-4 · Cited by 51 · see citing works

BiP/GRP78-Induced Production of Cytokines and Uptake of Amyloid-β(1-42) Peptide in Microglia

Kakimura, J., Kitamura, Y., Taniguchi, T., Shimohama, S., & Gebicke‐Haerter, P. J. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4299 · Cited by 48 · see citing works

Apoptotic cell death in neurons and glial cells: implications for Alzheimer's disease

Yoshihisa, K., Takashi, T., & Shun, S. (1999) · Japanese Journal of Pharmacology · doi:10.1254/jjp.79.1 · Cited by 47 · see citing works

Hyperbilirubinemia protects against focal ischemia in rats

Kitamura, Y., Ishida, Y., Takata, K., Mizutani, H., Kakimura, J., Inden, M., Nakata, J., Taniguchi, T., Tsukahara, T., Akaike, A., et al. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10514 · Cited by 36 · 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

The coordination of signaling during Fc receptor-mediated phagocytosis

Swanson, J. A., & Hoppe, A. D. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0804439 · Cited by 326 · see citing works

Transcription Factors NRF2 and NF-κB Are Coordinated Effectors of the Rho Family, GTP-binding Protein RAC1 during Inflammation

Cuadrado, A., Martín‐Moldes, Z., Ye, J., & Lastres‐Becker, I. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.540633 · Cited by 318 · see citing works

Galantamine-induced Amyloid-β Clearance Mediated via Stimulation of Microglial Nicotinic Acetylcholine Receptors

Takata, K., Kitamura, Y., Saeki, M., Terada, M., Kagitani, S., Kitamura, R., Fujikawa, Y., Maelicke, A., Tomimoto, H., Taniguchi, T., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.142356 · Cited by 176 · see citing works

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

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

Intracerebroventricular injection of microglia protects against focal brain ischemia

Kitamura, Y., Takata, K., Inden, M., Tsuchiya, D., Yanagisawa, D., Nakata, J., & Taniguchi, T. (2004) · Journal of Pharmacological Sciences · doi:10.1254/jphs.94.203 · Cited by 104 · see citing works

Small GTPases of the Ras and Rho Families Switch on/off Signaling Pathways in Neurodegenerative Diseases

Arrazola Sastre, A., Luque Montoro, M., Gálvez-Martín, P., Lacerda, H. M., Lucia, A., Llavero, F., & Zugaza, J. L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176312 · Cited by 103 · see citing works

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 67 · see citing works

Microglial Amyloid- β 1-40 Phagocytosis Dysfunction Is Caused by High-Mobility Group Box Protein-1: Implications for the Pathological Progression of Alzheimer’s Disease

Takata, K., Takada, T., Ito, A., Asai, M., Tawa, M., Saito, Y., Ashihara, E., Tomimoto, H., Kitamura, Y., & Shimohama, S. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/685739 · Cited by 58 · see citing works

Recovery of Focal Brain Ischemia-Induced Behavioral Dysfunction by Intracerebroventricular Injection of Microglia

Kitamura, Y., Yanagisawa, D., Inden, M., Takata, K., Tsuchiya, D., Kawasaki, T., Taniguchi, T., & Shimohama, S. (2005) · Journal of Pharmacological Sciences · doi:10.1254/jphs.sc0040129 · Cited by 58 · see citing works

Dock GEFs and their therapeutic potential: Neuroprotection and axon regeneration

Namekata, K., Kimura, A., Kawamura, K., Harada, C., & Harada, T. (2014) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2014.06.005 · Cited by 57 · see citing works

Deletion of <i>Abi3</i> gene locus exacerbates neuropathological features of Alzheimer’s disease in a mouse model of Aβ amyloidosis

Karahan, H., Smith, D. C., Kim, B., Dabin, L. C., Al-Amin, M. M., Wijeratne, H. R. S., Pennington, T., Viana di Prisco, G., McCord, B., Lin, P. B.-C., et al. (2021) · Science Advances · doi:10.1126/sciadv.abe3954 · Cited by 53 · see citing works

Evaluation of oxidative stress in the brain of a transgenic mouse model of Alzheimer disease by in vivo electron paramagnetic resonance imaging

Matsumura, A., Emoto, M. C., Suzuki, S., Iwahara, N., Hisahara, S., Kawamata, J., Suzuki, H., Yamauchi, A., Sato‐Akaba, H., Fujii, H. G., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.04.013 · Cited by 52 · see citing works

Lovastatin modulation of microglial activation via suppression of functional CD40 expression

Townsend, K. P., Shytle, D., Bai, Y., San, N., Zeng, J., Freeman, M. J., Mori, T., Fernandez, F., Morgan, D., Sanberg, P. R., et al. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20234 · Cited by 52 · see citing works

Pharmacological Modulators of Small GTPases of Rho Family in Neurodegenerative Diseases

Guiler, W., Koehler, A., Boykin, C., & Lu, Q. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.661612 · Cited by 51 · see citing works

Proteomic Modeling for HIV-1 Infected Microglia-Astrocyte Crosstalk

Wang, T., Gong, N., Liu, J., Kadiu, I., Kraft-Terry, S. D., Mosley, R. L., Volsky, D. J., Ciborowski, P. S., & Gendelman, H. E. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002507 · Cited by 51 · see citing works

DOCK2 Is a Microglial Specific Regulator of Central Nervous System Innate Immunity Found in Normal and Alzheimer’s Disease Brain

Cimino, P. J., Sokal, I., Leverenz, J., Fukui, Y., & Montine, T. J. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.090443 · Cited by 49 · see citing works

Bone-Marrow-Derived Microglia-Like Cells Ameliorate Brain Amyloid Pathology and Cognitive Impairment in a Mouse Model of Alzheimer’s Disease

Kawanishi, S., Takata, K., Itezono, S., Nagayama, H., Konoya, S., Chisaki, Y., Toda, Y., Nakata, S., Yano, Y., Kitamura, Y., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170994 · Cited by 47 · see citing works

Possible Involvement of Both Endoplasmic Reticulum-and Mitochondria-Dependent Pathways in Thapsigargin-Induced Apoptosis in Human Neuroblastoma SH-SY5Y Cells

Kitamura, Y., Miyamura, A., Takata, K., Inden, M., Tsuchiya, D., Nakamura, K., & Taniguchi, T. (2003) · Journal of Pharmacological Sciences · doi:10.1254/jphs.92.228 · Cited by 41 · see citing works

CDK5 knockdown in astrocytes provide neuroprotection as a trophic source via Rac1

Posada‐Duque, R., Palacio-Castañeda, V., & Cardona‐Gómez, G. P. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.07.001 · Cited by 35 · see citing works

Molecular Approaches to the Treatment, Prophylaxis, and Diagnosis of Alzheimer’s Disease: Tangle Formation, Amyloid-β, and Microglia in Alzheimer’s Disease

Takata, K., & Kitamura, Y. (2012) · Journal of Pharmacological Sciences · doi:10.1254/jphs.11r10fm · Cited by 34 · see citing works

Rac-Mediated Macropinocytosis Is a Critical Route for Naked Plasmid DNA Transfer in Mice

Fumoto, S., Nishi, J., Ishii, H., Wang, X., Miyamoto, H., Yoshikawa, N., Nakashima, M., Nakamura, J., & Nishida, K. (2009) · Molecular Pharmaceutics · doi:10.1021/mp900042p · Cited by 33 · see citing works

Microglia‐targeted stem cell therapies for Alzheimer disease: A preclinical data review

Shen, Z., Li, X., Bao, X., & Wang, R. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.24066 · Cited by 32 · see citing works

Involvement of small GTPase RhoA in the regulation of superoxide production in BV2 cells in response to fibrillar Aβ peptides

Moon, M.-Y., Kim, H.-J., Li, Y., Kim, J.-G., Jeon, Y.-J., Won, H.-Y., Kim, J.-S., Kwon, H.-Y., Choi, I.-G., Ro, E., et al. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.05.023 · Cited by 27 · see citing works

Mouse Bone Marrow-derived Microglia-like Cells Secrete Transforming Growth Factor-β1 and Promote Microglial Aβ Phagocytosis and Reduction of Brain Aβ

Kuroda, E., Nishimura, K., Kawanishi, S., Sueyoshi, M., Ueno, F., Toji, Y., Abo, N., Konishi, T., Harada, K., Satake, S., et al. (2020) · Neuroscience · doi:10.1016/j.neuroscience.2020.05.004 · Cited by 24 · see citing works

The effect of Abi3 locus deletion on the progression of Alzheimer’s disease-related pathologies

Karahan, H., Smith, D. C., Kim, B., McCord, B., Mantor, J., John, S. K., Al-Amin, M. M., Dabin, L. C., & Kim, J. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1102530 · Cited by 20 · see citing works

Peripheral Blood-Derived Microglia-Like Cells Decrease Amyloid-β Burden and Ameliorate Cognitive Impairment in a Mouse Model of Alzheimer’s Disease

Kuroda, E., Takata, K., Nishimura, K., Oka, H., Sueyoshi, M., Aitani, M., Kouda, A., Satake, S., Shima, C., Toda, Y., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190974 · Cited by 19 · see citing works

Shuttling Protein Nucleolin Is a Microglia Receptor for Amyloid Beta Peptide 1-42

Ozawa, D., Nakamura, T., Koike, M., Hirano, K., Miki, Y., & Beppu, M. (2013) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b13-00432 · Cited by 17 · see citing works

LRRK2 and WAVE2 regulate microglial‐transition through distinct morphological phenotypes to induce neurotoxicity in a novel two‐hit in vitro model of neurodegeneration

Fenner, B. M., Fenner, M. E., Prowse, N., & Hayley, S. P. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30588 · Cited by 14 · see citing works

Roles of Rac1-Dependent Intrinsic Forgetting in Memory-Related Brain Disorders: Demon or Angel

Wang, W., Wang, Z., Cao, J., Dong, Y., & Chen, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241310736 · Cited by 11 · see citing works

Clearing Amyloid-Beta by Astrocytes: The Role of Rho GTPases Signaling Pathways as Potential Therapeutic Targets

Park, K. A., Jin, Z. H., Lü, H., & Du, J. (2024) · Brain Sciences · doi:10.3390/brainsci14121239 · Cited by 10 · see citing works

Role of Membrane Tension Sensitive Endocytosis and Rho GTPases in the Uptake of the Alzheimer’s Disease Peptide Aβ(1-42)

Wesén, E. V., Lundmark, R., & Esbjörner, E. K. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00053 · Cited by 9 · see citing works

Effects of chemical inhibition of N-WASP, a critical regulator of actin polymerization on aqueous humor outflow through the conventional pathway

Inoue, T., Pattabiraman, P. P., Epstein, D. L., & Rao, P. V. (2009) · Experimental Eye Research · doi:10.1016/j.exer.2009.11.015 · Cited by 6 · see citing works

Preparation and Characterization of Microglia-Like Cells Derived from Rat, Mouse, and Human Bone Marrow Cells for Therapeutic Strategy of Alzheimer?s Disease

Takada, K. T. T., & Tsuruno, H. T. T. (2011) · Journal of Addiction Research & Therapy · doi:10.4172/2155-6105.s5-001 · Cited by 5 · see citing works

Stimulation of α7 Nicotinic Acetylcholine Receptors by PNU282987 Demonstrates Efferocytosis-Like Activation and Neuroprotection in Human Models of Microglia and Cholinergic Neurons under the Pathophysiological Conditions of Alzheimer’s Disease

Sueyoshi, M., Harada, K., Okawa, M., Matsuhara, T., Ando, M., Araki, R., Minote, Y., Ishihara, K., Shimohama, S., & Takata, K. (2025) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b25-00308 · Cited by 4 · see citing works

Molecular Targeting and Translational Research for New Therapeutic Strategies on Alzheimer's Disease

Takata, K. (2013) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.13-00219 · Cited by 3 · see citing works

Stress proteins and regulation of microglial amyloid-β phagocytosis

Kitamura, Y., Takata, K., & Taniguchi, T. (2004) · Folia Pharmacologica Japonica · doi:10.1254/fpj.124.407 · Cited by 1 · see citing works

Moesin is Involved in Migration and Phagocytosis Activities of Primary Microglia

Okazaki, T., Kawaguchi, K., Hirao, T., & Asano, S. (2020) · BPB Reports · doi:10.1248/bpbreports.3.6_185

Dysregulated oligodendrocyte and myelin dynamics as an early pathological feature of neuropil degeneration in Alzheimer’s disease: an ultrastructural study

Erişir, A., Maher, E. E., Anderson, Z., Chawla, S., Hanley, L., Zhao, A., Birisik, K., Toklucu, E. S., & Keskinöz, E. N. (2026) · Acta Neuropathologica Communications · doi:10.1186/s40478-026-02320-z

Alzheimer's β‐Amyloid Peptide 1–42 Induces a Phagocytic Response in Murine Microglia

Kopec, K. K., & Carroll, R. T. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71052123.x · Cited by 102 · see citing works

Stress proteins and regulation of microglial amyloid-β phagocytosis

Kitamura, Y., Takata, K., & Taniguchi, T. (2004) · Folia Pharmacologica Japonica · doi:10.1254/fpj.124.407 · Cited by 1 · see citing works

Microglial phagocytosis induced by fibrillar β-amyloid is attenuated by oligomeric β-amyloid: implications for Alzheimer’s disease

Pan, X.-D., Zhu, Y.-G., Lin, N., Zhang, J., Ye, Q.-Y., Huang, H.-P., & Chen, X.-C. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-45 · Cited by 292 · see citing works

Microglial Amyloid- β 1-40 Phagocytosis Dysfunction Is Caused by High-Mobility Group Box Protein-1: Implications for the Pathological Progression of Alzheimer’s Disease

Takata, K., Takada, T., Ito, A., Asai, M., Tawa, M., Saito, Y., Ashihara, E., Tomimoto, H., Kitamura, Y., & Shimohama, S. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/685739 · Cited by 58 · 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