Systemic LPS-induced Aβ-solubilization and clearance in AβPP-transgenic mice is diminished by heparanase overexpression

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

The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes

Benilova, I., Karran, E., & De Strooper, B. (2012) · Nature Neuroscience · doi:10.1038/nn.3028 · Cited by 1,962 · see citing works

Bacterial endotoxin: molecular relationships of structure to activity and function

Rietschel, E., Kirikae, T., Schade, F. U., Mamat, U., Schmidt, G., Loppnow, H., Ulmer, A. J., Zähringer, U., Seydel, U., Padova, F. D., et al. (1994) · The FASEB Journal · doi:10.1096/fasebj.8.2.8119492 · Cited by 1,608 · see citing works

A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N–terminus of β–amyloid

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

Inflammation in Neurodegenerative Disease—A Double-Edged Sword

Wyss-Coray, T., & Mucke, L. (2002) · Neuron · doi:10.1016/s0896-6273(02)00794-8 · Cited by 1,235 · see citing works

Apolipoprotein E immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer's disease and kuru plaque amyloid in Creutzfeldt-Jakob disease

Namba, Y., Tomonaga, M., Kawasaki, H., Otomo, E., & Ikeda, K. (1991) · Brain Research · doi:10.1016/0006-8993(91)91092-f · Cited by 1,157 · see citing works

Infiltrating monocytes trigger EAE progression, but do not contribute to the resident microglia pool

Ajami, B., Bennett, J. L., Krieger, C., McNagny, K. M., & Rossi, F. M. V. (2011) · Nature Neuroscience · doi:10.1038/nn.2887 · Cited by 1,061 · see citing works

Relationship of microglia and astrocytes to amyloid deposits of Alzheimer disease

Itagaki, S., McGeer, P. L., Akiyama, H., Zhu, S., & Selkoe, D. (1989) · Journal of Neuroimmunology · doi:10.1016/0165-5728(89)90115-x · Cited by 940 · see citing works

Immunochemical identification of the serine protease inhibitor α1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease

Abraham, C. R., Selkoe, D. J., & Potter, H. (1988) · Cell · doi:10.1016/0092-8674(88)90462-x · Cited by 893 · see citing works

The pulmonary endothelial glycocalyx regulates neutrophil adhesion and lung injury during experimental sepsis

Schmidt, E. P., Yang, Y., Janssen, W. J., Gandjeva, A., Perez, M. J., Barthel, L., Zemans, R. L., Bowman, J. C., Koyanagi, D., Yunt, Z. X., et al. (2012) · Nature Medicine · doi:10.1038/nm.2843 · Cited by 842 · see citing works

Interleukin-6: Biology, signaling and strategies of blockade

Schaper, F., & Rose‐John, S. (2015) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2015.07.004 · Cited by 511 · see citing works

The role of heparan sulphate in inflammation

Parish, C. R. (2006) · Nature reviews. Immunology · doi:10.1038/nri1918 · Cited by 498 · see citing works

Role 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

Lipopolysaccharide-induced-neuroinflammation increases intracellular accumulation of amyloid precursor protein and amyloid β peptide in APPswe transgenic mice

Sheng, J. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(03)00069-x · Cited by 388 · see citing works

Bone-marrow-derived cells contribute to the recruitment of microglial cells in response to β-amyloid deposition in APP/PS1 double transgenic Alzheimer mice

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

P2Y ₁₂ receptor is expressed on human microglia under physiological conditions throughout development and is sensitive to neuroinflammatory diseases: P2Y ₁₂ Expression on Human Microglia

Mildner, A., Huang, H., Radke, J., Stenzel, W., & Priller, J. (2017) · Glia · doi:10.1002/glia.23097 · Cited by 301 · see citing works

Sensitive ELISA detection of amyloid‐β protofibrils in biological samples

Englund, H., Sehlin, D., Johansson, A., Nilsson, L. N. G., Gellerfors, P., Paulie, S., Lannfelt, L., & Pettersson, F. E. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04759.x · Cited by 292 · see citing works

Inhibition of soluble TNF signaling in a mouse model of Alzheimer's disease prevents pre-plaque amyloid-associated neuropathology

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

The Arctic Alzheimer mutation facilitates early intraneuronal Aβ aggregation and senile plaque formation in transgenic mice

Lord, A., Kalimo, H., Eckman, C., Zhang, X.-Q., Lannfelt, L., & Nilsson, L. N. G. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.12.007 · Cited by 260 · see citing works

Toll-like receptor 4 stimulation with the detoxified ligand monophosphoryl lipid A improves Alzheimer’s disease-related pathology

Michaud, J.-P., Hallé, M., Lampron, A., Thériault, P., Préfontaine, P., Filali, M., Tribout-Jover, P., Lanteigne, A.-M., Jodoin, R., Cluff, C. W., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1215165110 · Cited by 251 · see citing works

Transgenic expression of mammalian heparanase uncovers physiological functions of heparan sulfate in tissue morphogenesis, vascularization, and feeding behavior

Zcharia, E., Metzger, S., Chajek‐Shaul, T., Aingorn, H., Elkin, M., Friedmann, Y., Weinstein, T., Li, J.-P., Lindahl, U., & Vlodavsky, I. (2004) · The FASEB Journal · doi:10.1096/fj.03-0572com · Cited by 242 · see citing works

The Sulfate Moieties of Glycosaminoglycans Are Critical for the Enhancement of β‐Amyloid Protein Fibril Formation

Castillo, G. M., Lukito, W., Wight, T. N., & Snow, A. D. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.721681.x · Cited by 224 · see citing works

Gender Differences in Murine Airway Responsiveness and Lipopolysaccharide-Induced Inflammation

Card, J. W., Carey, M. A., Bradbury, J. A., DeGraff, L. M., Morgan, D. L., Moorman, M. P., Flake, G. P., & Zeldin, D. C. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.1.621 · Cited by 223 · 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

Sulfated glycosaminoglycans: a common constituent of all amyloids?

Snow, A. D., Willmer, J., & Kisilevsky, R. (1987) · PubMed · Cited by 215 · see citing works

Characterization of stable complexes involving apolipoprotein E and the amyloid β peptide in Alzheimer's disease brain

Näslund, J., Thyberg, J., Tjernberg, L. O., Wernstedt, C., Karlström, A. R., Bogdanović, N., Gandy, S., Lannfelt, L., Terenius, L. Y., & Nordstedt, C. (1995) · Neuron · doi:10.1016/0896-6273(95)90079-9 · Cited by 189 · see citing works

Heparanase powers a chronic inflammatory circuit that promotes colitis-associated tumorigenesis in mice

Lerner, I., Hermano, E., Zcharia, E., Rodkin, D., Bulvik, R., Doviner, V., Rubinstein, A. M., Ishai-Michaeli, R., Atzmon, R., Sherman, Y., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci43792 · Cited by 187 · see citing works

Neuronal heparan sulfates promote amyloid pathology by modulating brain amyloid-β clearance and aggregation in Alzheimer’s disease

Liu, C.-C., Zhao, N., Yamaguchi, Y., Cirrito, J. R., Kanekiyo, T., Holtzman, D. M., & Bu, G. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aad3650 · Cited by 180 · see citing works

Endogenous brain cytokine mRNA and inflammatory responses to lipopolysaccharide are elevated in the Tg2576 transgenic mouse model of Alzheimer’s disease

Sly, L. M., KRZESICKI, R. F., Brashler, J. R., Buhl, A.-L., McKinley, D. D., Carter, D. B., & Chin, J. E. (2001) · Brain Research Bulletin · doi:10.1016/s0361-9230(01)00730-4 · Cited by 174 · see citing works

Agrin Binds to β-Amyloid (Aβ), Accelerates Aβ Fibril Formation, and Is Localized to Aβ Deposits in Alzheimer's Disease Brain

Cotman, S. L., Halfter, W. M., & Cole, G. J. (2000) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1999.0816 · Cited by 170 · see citing works

Time-dependent reduction in Aβ levels after intracranial LPS administration in APP transgenic mice

Herber, D. L., Roth, L. M., Wilson, D. H., Wilson, N., Mason, J. E., Morgan, D., & Gordon, M. N. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2004.07.007 · Cited by 147 · see citing works

APP Transgenic Mice Tg2576 Accumulate Aβ Peptides That Are Distinct from the Chemically Modified and Insoluble Peptides Deposited in Alzheimer's Disease Senile Plaques

Kalback, W. M., Watson, M. D., Kokjohn, T. A., Kuo, Y., Weiss, N., Luehrs, D. C., Lopez, J. C., Brune, D. C., Sisodia, S. S., Staufenbiel, M., et al. (2001) · Biochemistry · doi:10.1021/bi015685+ · Cited by 146 · see citing works

Age and sex differences in immune response following LPS treatment in mice

Cai, K. C., van Mil, S., Murray, E., Mallet, J., Matar, C., & Ismail, N. (2016) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2016.08.002 · Cited by 142 · see citing works

Microglial Activation is Required for Aβ Clearance After Intracranial Injection of Lipopolysaccharide in APP Transgenic Mice

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

α-1-Antichymotrypsin Promotes β-Sheet Amyloid Plaque Deposition in a Transgenic Mouse Model of Alzheimer's Disease

Nilsson, L. N. G., Bales, K. R., DiCarlo, G., Gordon, M. N., Morgan, D., Paul, S. M., & Potter, H. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-05-01444.2001 · Cited by 137 · see citing works

Increased blood-brain barrier vulnerability to systemic inflammation in an Alzheimer disease mouse model

Takeda, S., Sato, N., Ikimura, K., Nishino, H., Rakugi, H., & Morishita, R. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.02.010 · Cited by 135 · see citing works

Versatile role of heparanase in inflammation

Goldberg, R., Meirovitz, A., Hirshoren, N., Bulvik, R., Gallimidi, A. B., Rubinstein, A. M., & Elkin, M. (2013) · Matrix Biology · doi:10.1016/j.matbio.2013.02.008 · Cited by 132 · see citing works

Differential Binding of Vascular Cell-Derived Proteoglycans (Perlecan, Biglycan, Decorin, and Versican) to the Beta-Amyloid Protein of Alzheimer′s Disease

Snow, A. D., Kinsella, M. G., Parks, E., Sekiguchi, R., Miller, J., Kimata, K., & Wight, T. N. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1345 · Cited by 123 · see citing works

Neuroinflammation‐induced acceleration of amyloid deposition in the APP^V717F transgenic mouse

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

A highly insoluble state of Aβ similar to that of Alzheimer's disease brain is found in Arctic APP transgenic mice

Philipson, O., Hammarström, P., Nilsson, K. P. R., Portelius, E., Olofsson, T., Ingelsson, M., Hyman, B. T., Blennow, K., Lannfelt, L., Kalimo, H., et al. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.11.022 · Cited by 106 · see citing works

Early Stage Drug Treatment That Normalizes Proinflammatory Cytokine Production Attenuates Synaptic Dysfunction in a Mouse Model That Exhibits Age-Dependent Progression of Alzheimer's Disease-Related Pathology

Bachstetter, A. D., Norris, C. M., Sompol, P. M., Wilcock, D. M., Goulding, D. S., Neltner, J. H., Clair, D. K. S., Watterson, D. M., & Eldik, L. J. V. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1496-12.2012 · Cited by 105 · see citing works

Inflammation and cerebral amyloidosis are disconnected in an animal model of Alzheimer's disease

Quinn, J. (2003) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(03)00037-7 · Cited by 102 · see citing works

Microglial response to LPS increases in wild-type mice during aging but diminishes in an Alzheimer's mouse model: Implication of TLR4 signaling in disease progression

Go, M., Kou, J., Lim, J.-E., Yang, J., & Fukuchi, K.-I. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.09.073 · Cited by 87 · see citing works

Heparanase in inflammation and inflammation‐associated cancer

Meirovitz, A., Goldberg, R. L., Gallimidi, A. B., Rubinstein, A. M., Hermano, E., & Elkin, M. (2013) · FEBS Journal · doi:10.1111/febs.12184 · Cited by 82 · see citing works

Heparan Sulfate Accumulation with Aβ Deposits in Alzheimer's Disease and Tg2576 Mice is Contributed by Glial Cells

O'Callaghan, P. W., Sandwall, E., Li, J.-P., Yu, H., Ravid, R., Guan, Z., Kuppevelt, T. H. V., Nilsson, L. N. G., Ingelsson, M., Hyman, B. T., et al. (2008) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00152.x · Cited by 81 · see citing works

Heparanase overexpression impairs inflammatory response and macrophage-mediated clearance of amyloid-β in murine brain

Zhang, X., Wang, B., O'Callaghan, P. W., Hjertström, E., Jia, J., Gong, F., Zcharia, E., Nilsson, L. N. G., Lannfelt, L., Vlodavsky, I., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0997-1 · Cited by 65 · see citing works

Implications of heparan sulfate and heparanase in neuroinflammation

Zhang, X. L., Wang, B., & Li, J. (2014) · Matrix Biology · doi:10.1016/j.matbio.2013.12.009 · Cited by 60 · see citing works

Resorufin analogs preferentially bind cerebrovascular amyloid: potential use as imaging ligands for cerebral amyloid angiopathy

Han, B. W., Zhou, M., Vellimana, A. K., Milner, E., Kim, D. H., Greenberg, J. K., Chu, W., Mach, R. H., & Zipfel, G. J. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-86 · Cited by 60 · see citing works

Microglial Heparan Sulfate Proteoglycans Facilitate the Cluster-of-Differentiation 14 (CD14)/Toll-like Receptor 4 (TLR4)-Dependent Inflammatory Response

O'Callaghan, P. W., Li, J., Lannfelt, L., Lindahl, U., & Zhang, X. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.634337 · Cited by 58 · see citing works

Overexpression of Heparanase Lowers the Amyloid Burden in Amyloid-β Precursor Protein Transgenic Mice

Jendresen, C., Hao, C., Zhang, X. L., Vlodavsky, I., Nilsson, L. N. G., & Li, J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.600569 · Cited by 57 · see citing works

Fine Tuning the Transcriptional Regulation of the CXCL1 Chemokine

Amiri, K. I., & Richmond, A. J. (2003) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(03)01009-2 · Cited by 51 · see citing works

Diverse Protein Profiles in CNS Myeloid Cells and CNS Tissue From Lipopolysaccharide- and Vehicle-Injected APPSWE/PS1ΔE9 Transgenic Mice Implicate Cathepsin Z in Alzheimer’s Disease

Thygesen, C., Ilkjær, L., Kempf, S. J., Hemdrup, A. L., von Linstow, C. U., Babcock, A. A., Darvesh, S., Larsen, M. R., & Finsen, B. R. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00397 · Cited by 43 · see citing works

Aggregation and cytotoxic properties towards cultured cerebrovascular cells of Dutch-mutated Aβ40 (DAβ1-40) are modulated by sulfate moieties of heparin

Timmer, N., Schirris, T. J. J., Bruinsma, I. B., Otte‐Höller, I., Kuppevelt, T. H. V., de Waal, R. M. W., & Verbeek, M. M. (2009) · Neuroscience Research · doi:10.1016/j.neures.2009.12.012 · Cited by 36 · see citing works

Heparanase of murine effector lymphocytes and neutrophils is not required for their diapedesis into sites of inflammation

Stoler‐Barak, L., Petrovich, E., Aychek, T., Gurevich, I., Tal, O., Hatzav, M., Ilan, N., Feigelson, S. W., Shakhar, G., Vlodavsky, I., et al. (2015) · The FASEB Journal · doi:10.1096/fj.14-265447 · Cited by 30 · see citing works

Heparanase Overexpression Reduces Hepcidin Expression, Affects Iron Homeostasis and Alters the Response to Inflammation

Asperti, M., Stuemler, T., Poli, M., Gryzik, M., Lifshitz, L., Meyron‐Holtz, E. G., Vlodavsky, I., & Arosio, P. (2016) · PLoS ONE · doi:10.1371/journal.pone.0164183 · Cited by 19 · see citing works

The expanding appreciation of heparanase in human disease

Schmidt, E. P. (2012) · Neuroscience Letters · doi:10.1016/j.neulet.2012.01.027 · Cited by 3 · see citing works

Myelin dysfunction drives amyloid-β deposition in models of Alzheimer’s disease

Depp, C., Sun, T., Sasmita, A. O., Spieth, L., Berghoff, S. A., Nazarenko, T., Overhoff, K., Steixner-Kumar, A. A., Subramanian, S., Arinrad, S., et al. (2023) · Nature · doi:10.1038/s41586-023-06120-6 · Cited by 476 · see citing works

The Impact of Systemic Inflammation on Alzheimer’s Disease Pathology

Xie, J., Van Hoecke, L., & Vandenbroucke, R. E. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2021.796867 · Cited by 324 · see citing works

Gram-negative bacteria and their lipopolysaccharides in Alzheimer’s disease: pathologic roles and therapeutic implications

Kim, H. S., Kim, S., Shin, S. J., Park, Y. H., Nam, Y., Lee, K. W., Lee, K. W., Kim, S., Yang, H. D., Yang, H. D., et al. (2021) · Translational Neurodegeneration · doi:10.1186/s40035-021-00273-y · Cited by 161 · see citing works

Dietary Fiber Modulates the Release of Gut Bacterial Products Preventing Cognitive Decline in an Alzheimer’s Mouse Model

Cuervo-Zanatta, D., Syeda, T., Sánchez-Valle, V., Irene-Fierro, M., Torres‐Aguilar, P. C., Torres-Ramos, M., Shibayama-Salas, M., Silva-Olivares, A., Noriega, L. G., Torres, N., et al. (2022) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-022-01268-7 · Cited by 71 · see citing works

Low-grade peripheral inflammation affects brain pathology in the AppNL-G-Fmouse model of Alzheimer’s disease

Xie, J., Gorlé, N., Vandendriessche, C., Imschoot, G. V., Wonterghem, E. V., Cauwenberghe, C. V., Parthoens, E., Hamme, E. V., Lippens, S., Hoecke, L. V., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01253-z · Cited by 69 · see citing works

Neuroinflammation in neurodegeneration via microbial infections

Tran, V. T. A., Lee, L. P., & Cho, H. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.907804 · Cited by 68 · see citing works

Low-dose lipopolysaccharide as an immune regulator for homeostasis maintenance in the central nervous system through transformation to neuroprotective microglia

Mizobuchi, H., & Soma, G. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.308067 · Cited by 51 · see citing works

Microglia and Astrocytes in Alzheimer’s Disease in the Context of the Aberrant Copper Homeostasis Hypothesis

Pal, A., Rani, I., Pawar, A. T., Picozza, M., Rongioletti, M. C. A., & Squitti, R. (2021) · Biomolecules · doi:10.3390/biom11111598 · Cited by 47 · see citing works

Racial and ethnic differences in plasma biomarker eligibility for a preclinical Alzheimer's disease trial

Molina‐Henry, D. P., Raman, R., Liu, A., Langford, O., Johnson, K. A., Shum, L. K., Glover, C. M., Dhadda, S., Irizarry, M. C., Jimenez‐Maggiora, G. A., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.13803 · Cited by 44 · see citing works

Amyloid Beta Pathology Exacerbates Weight Loss and Brain Cytokine Responses following Low-Dose Lipopolysaccharide in Aged Female Tg2576 Mice

Knopp, R. C., Baumann, K. K., Wilson, M. L., Banks, W. A., & Erickson, M. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042377 · Cited by 17 · see citing works

Acute experimental colitis in 5xFAD Alzheimer's disease mice leads to enhanced monocyte infiltration into the brain accompanied by reduced β‐amyloid deposition

Shanmugam, N. K. N., Zamudio, F., Kumar, D. K. V., Barrett, K. A., VanDoren, R., Chen, M., Barr, O. M., Watson, S., Lin, C., Eimer, W. A., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70292 · Cited by 8 · see citing works

Gut Microbiota Dysbiosis and Neuroinflammation in Alzheimer’s Disease: a Systematic Review of Mechanistic Insights

Katsigianni, S., & Koutsouraki, E. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05914-9 · Cited by 7 · see citing works

Tualang honey and its methanolic fraction ameliorate lipopolysaccharide-induced oxidative stress, amyloid deposition and neuronal loss of the rat hippocampus

Yaacob, W. M. H. W., Long, I., Zakaria, R., & Othman, Z. (2020) · Oriental Pharmacy and Experimental Medicine · doi:10.1007/s13596-020-00449-3 · Cited by 5 · see citing works

Prolonged systemic inflammation worsens impairments to astrocyte Ca 2+ and functional hyperemia in Alzheimer's disease

Liu, C., Sakha, K., Anton, J., Cárdenas‐Rivera, A., & Yaseen, M. A. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71607 · Cited by 2 · see citing works

Animal model for sporadic dementia of Alzheimer’s type (SDAT) using streptozotocin and lipopolysaccharide combinations in rats

Hartantyo, R. Y., Hidayat, M. R. M., Azzam, A. B., & Mulyati, M. (2020) · Journal of the Medical Sciences (Berkala Ilmu Kedokteran) · doi:10.19106/jmedsci005203202003 · Cited by 1 · see citing works

LPS-induced systemic inflammation reduced sensory stimulation-evoked astrocyte Ca2+ without altering the vascular response in the APP/PS1dE9 mouse model

Liu, C., Sakha, K. A., Anton, J., Cárdenas‐Rivera, A., & Yaseen, M. A. (2025) · Neural Imaging and Sensing · doi:10.1117/12.3043431

Additional file 4 of Low-grade peripheral inflammation affects brain pathology in the AppNL-G-Fmouse model of Alzheimer’s disease

Xie, J., Gorlé, N., Vandendriessche, C., Imschoot, G. V., Wonterghem, E. V., Cauwenberghe, C. V., Parthoens, E., Hamme, E. V., Lippens, S., Hoecke, L. V., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16767284

Exploring vagus nerve stimulation in postoperative delirium and dementia

Spicer, R. M., Olofsson, P. S., & Harrison, F. E. (2026) · Bioelectronic Medicine · doi:10.1186/s42234-026-00200-4

Microglia-mediated endotoxin tolerance: A protective role of LPS preconditioning in the central nervous system

Dong, L., Doorduin, J., & de Vries, E. F. J. (2026) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2026.106771

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

Heparanase overexpression impairs inflammatory response and macrophage-mediated clearance of amyloid-β in murine brain

Zhang, X., Wang, B., O'Callaghan, P. W., Hjertström, E., Jia, J., Gong, F., Zcharia, E., Nilsson, L. N. G., Lannfelt, L., Vlodavsky, I., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0997-1 · Cited by 65 · see citing works

Microglial Activation is Required for Aβ Clearance After Intracranial Injection of Lipopolysaccharide in APP Transgenic Mice

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

Time-dependent reduction in Aβ levels after intracranial LPS administration in APP transgenic mice

Herber, D. L., Roth, L. M., Wilson, D. H., Wilson, N., Mason, J. E., Morgan, D., & Gordon, M. N. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2004.07.007 · Cited by 147 · see citing works

ORIGINAL PAPER Heparanase overexpression impairs inflammatory response and macrophage-mediated clearance of amyloid-b in murine brain

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