The NALP3 inflammasome is involved in the innate immune response to amyloid-β
Open accessAbstract
The fibrillar peptide amyloid-beta (A beta) has a chief function in the pathogenesis of Alzheimer's disease. Interleukin 1 beta (IL-1 beta) is a key cytokine in the inflammatory response to A beta. Insoluble materials such as crystals activate the inflammasome formed by the cytoplasmic receptor NALP3, which results in the release of IL-1 beta. Here we identify the NALP3 inflammasome as a sensor of A beta in a process involving the phagocytosis of A beta and subsequent lysosomal damage and release of cathepsin B. Furthermore, the IL-1 beta pathway was essential for the microglial synthesis of proinflammatory and neurotoxic factors, and the inflammasome, caspase-1 and IL-1 beta were critical for the recruitment of microglia to exogenous A beta in the brain. Our findings suggest that activation of the NALP3 inflammasome is important for inflammation and tissue damage in Alzheimer's disease.
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Cathepsin B leaking from destabilized lysosomes may mediate NLRP3 inflammasome activation upon SHIP1 inhibition.
“Based on the previous literature42,43,46, we reasoned that cathepsin B leaking from the destabilized lysosomes may mediate the NLRP3 inflammasome activation upon SHIP1 inhibition11.”
From INPP5D/SHIP1 regulates endo-lysosomal function and cargo-selective phagocytosis in human microglia (2025) · cites this paper as [43]
In Results (“Lysosomal damage triggers release of cathepsin B”; page unavailable), the paper reports that amyloid-β damages microglial lysosomes, releases cathepsin B, and links cathepsin B to inflammasome activation. It does not examine SHIP1 inhibition, so it supports the proposed mechanism as a rationale, not its occurrence upon SHIP1 inhibition. (LLM, conf=0.88)
Experimental — accuracy not yet measuredFibrillar Aβ, following phagocytosis by microglia, activates the NLRP3 inflammasome and leads to increases in secretion of IL-1β and IL-18.
“Fibrillar Aβ (fAβ), following phagocytosis by microglia, activates the NLRP3 inflammasome and leads to increases in secretion of IL-1β and IL-18.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [78]
The Results sections “Fibrillar Aβ induces IL-1β from microglia” and “Aβ causes lysosomal damage and IL-1β release” report that fibrillar Aβ triggers IL-1β release from microglia and that phagocytosis is required; the paper also identifies NALP3 (NLRP3) inflammasome activation in this pathway. The copy does not report increased IL-18 secretion after Aβ exposure; its Discussion mentions IL-18 only when describing its receptor. The IL-1β experiments used LPS-primed mouse microglia. (LLM, conf=0.89)
Experimental — accuracy not yet measuredHalle et al. found that fibrillar Aβ can induce secretion of IL-1β which depends on the presence of NLRP3.
“Halle et al. found that fibrillar Aβ can induce the secretion of IL-1β which depends on the presence of NLRP3.352,353”
From Role of neuroinflammation in neurodegeneration development (2023) · cites this paper as [352]
Lysosomal cathepsins, such as cathepsin B, can induce NLRP3 inflammasome activation upon leaking into the cytosol following lysosomal membrane permeabilization (LMP).
“lysosomal cathepsins, such as cathepsin B, can induce NLRP3 inflammasome activation upon leaking into the cytosol following lysosomal membrane permeabilization (LMP)42,43”
From INPP5D/SHIP1 regulates endo-lysosomal function and cargo-selective phagocytosis in human microglia (2025) · cites this paper as [43]
Fibrillar Aβ phagocytosis results in lysosomal dysfunction and release of lysosomal contents into the cytoplasm, including cathepsin B, which is a mediator of inflammasome activation induced by Aβ.
“fAβ phagocytosis results in lysosomal dysfunction and release of lysosomal contents into the cytoplasm, including the lysosomal protease cathepsin B, which is a mediator of inflammasome activation induced by Aβ [78].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [78]
Aggregated tau seeds activate the NLRP3 inflammasome in primary mouse microglia by inducing lysosomal destabilization and release of cathepsin B, similar to fAβ.
“In line with these findings, another study showed that aggregated tau seeds activated the NLRP3 inflammasome in primary mouse microglia by inducing lysosomal destabilization and release of the lysosomal protease cathepsin B, similar to fAβ [78, 82].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [78]
Reduction of SHIP1 activity is poised to disinhibit signaling pathways involved in the phagocytosis of Aβ, which is a required step for Aβ-induced activation of the NLRP3 inflammasome.
“In parallel, reduction of SHIP1 activity is poised to disinhibit signaling pathways that are involved in the phagocytosis of Aβ, which is a required step for Aβ-induced activation of the NLRP3 inflammasome [78].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [78]
Aβ activates NF-κB signaling and the NLRP3-ASC inflammasome.
“Notably, Aβ also can activate NF-κB signaling and the NLRP3-ASC inflammasome [426, 427], suggesting that Aβ and tau share common mechanisms in microglia activation.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [426]
After microglial phagocytosis, Aβ activates the NLRP3 inflammasome, leading to caspase-1 activation and IL-1β maturation and release.
“Following phagocytosis by microglia, Aβ activates the NLRP3 inflammasome leading to caspase-1 activation and IL-1β maturation and release (Halle et al., 2008).”
From Alzheimer Disease: An Update on Pathobiology and Treatment Strategies (2019) · cites this paper as Halle et al., 2008
Fibrillar Aβ amyloids can induce secretion of IL-1β from microglia via the NLRP3 inflammasome.
“Fibrillar Aβ amyloids can induce the secretion of IL-1β from microglia, via the NLRP3 inflammasome (228, 249).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [228]
ASC-, caspase-1-, IL-1 receptor-, and MyD88-deficient mice had less recruitment of microglia and mononuclear phagocytes to Aβ in the brain compared to wild type after injection of Aβ into the striatum.
“Importantly, researchers also found that ASC-, caspase-1-, IL-1 receptor-, and MyD88-deficient mice had less recruitment of microglia and mononuclear phagocytes to Aβ in the brain as compared to the wild type control after the injection of Aβ into the striatum (228).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [228]
NLRP3 has been shown to respond to sterile stimuli, including asbestos, silica, MSU and CPPD crystals, cholesterol crystals and β-amyloid fibrils.
“NLRP3 has been shown to respond to sterile stimuli, including asbestos, silica, MSU and CPPD crystals55, cholesterol crystals and β-amyloid fibrils56.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [56]
There is only partial inhibition of neutrophil infiltration and IL-1β production associated with sterile inflammation in response to cholesterol crystals.
“Furthermore, there is only partial inhibition of the neutrophil infiltration and IL-1β production associated with sterile inflammation in response to cholesterol crystals44,56,59,67.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [56]
Cathepsin B-deficient macrophages have no impairment in IL-1β production in response to certain NLRP3 agonists, including LPS plus ATP, or MSU crystals, despite the impairment in their response to silica.
“However, cathepsin b-deficient macrophages have no impairment in IL-1β production in response to certain NLRP3 agonists, including LPS plus ATP, or MSU crystals, despite the impairment in their response to silica44,56,59,67.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [56]
Artificial lysosomal rupture alone can activate NLRP3, and pharmacological inhibition or genetic depletion of cathepsin B results in inhibition of caspase 1 activation, although this inhibition was only partial.
“evidence to support this are the observations that artificial lysosomal rupture alone can activate NLRP3 and that pharmacological inhibition or genetic depletion of cathepsin b results in inhibition of caspase 1 activation, although this inhibition was only partial44,56,59.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [56]
Direct treatment of ATP on primed microglia is sufficient for maturation and release of IL-1β in vitro via the P2X7 receptor expressed on microglia.
“In support of this, direct treatment of ATP on primed microglia is sufficient for maturation and release of IL-1β in vitro (Halle et al, 2008) and does so via the P2X 7 receptor (Colomar et al, 2003) expressed on microglia (Monif et al, 2009).”
From Repeated Social Defeat, Neuroinflammation, and Behavior: Monocytes Carry the Signal (2017) · cites this paper as Halle et al, 2008
Microglial NLRP3 is a major driver of amyloid beta and tau toxicity in AD.
“In particular, microglial NLRP3 has been shown to be a major driver of amyloid beta and tau toxicity in AD, suggesting its activation has important implications for disease progression (Halle et al, 2008; Venegas et al, 2017; Ising et al, 2019).”
From Mechanisms of DNA damage-mediated neurotoxicity in neurodegenerative disease (2022) · cites this paper as Halle et al, 2008
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Cites
Gout-associated uric acid crystals activate the NALP3 inflammasome
Martinon, F., Pétrilli, V., Mayor, A., Tardivel, A., & Tschopp, J. (2006) · Nature · doi:10.1038/nature04516 · Cited by 5,326 · see citing works
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160 · see citing works
Cryopyrin activates the inflammasome in response to toxins and ATP
Mariathasan, S., Weiss, D. S., Newton, K., McBride, J., O'Rourke, K., Roose-Girma, M., Lee, W. P., Weinrauch, Y., Monack, D. M., & Dixit, V. M. (2006) · Nature · doi:10.1038/nature04515 · Cited by 3,080 · see citing works
Innate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica
Dostert, C., Pétrilli, V., Van Bruggen, R., Steele, C., Mossman, B. T., & Tschopp, J. (2008) · Science · doi:10.1126/science.1156995 · Cited by 2,658 · see citing works
Germline Transmission and Tissue-Specific Expression of Transgenes Delivered by Lentiviral Vectors
Lois, C., Hong, E. J., Pease, S., Brown, E. J., & Baltimore, D. (2002) · Science · doi:10.1126/science.1067081 · Cited by 1,974 · see citing works
Brain interleukin 1 and S-100 immunoreactivity are elevated in Down syndrome and Alzheimer disease.
Griffin, W. S., Stanley, L. C., Ling, C., White, L., MacLeod, V, Perrot, L. J., White, C. L., & Araoz, C. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.19.7611 · Cited by 1,777 · see citing works
Agostini, L., Martinon, F., Burns, K., McDermott, M. F., Hawkins, P. N., & Tschopp, J. (2004) · Immunity · doi:10.1016/s1074-7613(04)00046-9 · Cited by 1,768 · see citing works
Altered Cytokine Export and Apoptosis in Mice Deficient in Interleukin-1β Converting Enzyme
Kuida, K., Lippke, J. A., Ku, G., Harding, M. W., Livingston, D. J., Su, M. S. S., & Flavell, R. A. (1995) · Science · doi:10.1126/science.7535475 · Cited by 1,606 · see citing works
A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity
Weggen, S., Eriksen, J. L., Das, P., Sagi, S. A., Wang, R., Pietrzik, C. U., Findlay, K. A., Smith, T. E., Murphy, M. P., Bulter, T., et al. (2001) · Nature · doi:10.1038/35102591 · Cited by 1,388 · see citing works
Simard, A. R., Soulet, D., Gowing, G., Julien, J.-P., & Rivest, S. (2006) · Neuron · doi:10.1016/j.neuron.2006.01.022 · Cited by 1,265 · see citing works
Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3
Kanneganti, T., Özören, N., Body–Malapel, M., Amer, A. O., Park, J., Franchi, L., Whitfield, J. R., Barchet, W., Colonna, M., Vandenabeele, P., et al. (2006) · Nature · doi:10.1038/nature04517 · Cited by 1,149 · see citing works
Franchi, L., Amer, A., Body-Malapel, M., Kanneganti, T.-D., Özören, N., Jagirdar, R., Inohara, N., Vandenabeele, P., Bertin, J., Coyle, A., et al. (2006) · Nature Immunology · doi:10.1038/ni1346 · Cited by 1,131 · see citing works
Immortalization of murine microglial cells by a v-raf / v-myc carrying retrovirus
Blasi, E., Barluzzi, R., Bocchini, V., Mazzolla, R., & Bistoni, F. (1990) · Journal of Neuroimmunology · doi:10.1016/0165-5728(90)90073-v · Cited by 1,053 · see citing works
Fernandes-Alnemri, T., Wu, J., Yu, J.-W., Datta, P., Miller, B., Jankowski, W., Rosenberg, S., Zhang, J., & Alnemri, E. S. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402194 · Cited by 1,026 · see citing works
Rapid appearance and local toxicity of amyloid-β plaques in a mouse model of Alzheimer’s disease
Meyer-Luehmann, M., Spires-Jones, T. L., Prada, C., Garcia-Alloza, M., de Calignon, A., Rozkalne, A., Koenigsknecht-Talboo, J., Holtzman, D. M., Bacskai, B. J., & Hyman, B. T. (2008) · Nature · doi:10.1038/nature06616 · Cited by 987 · see citing works
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
El Khoury, J., Toft, M., Hickman, S. E., Means, T. K., Terada, K., Geula, C., & Luster, A. D. (2007) · Nature Medicine · doi:10.1038/nm1555 · Cited by 915 · see citing works
Inflammasome adaptors and sensors: intracellular regulators of infection and inflammation
Mariathasan, S., & Monack, D. M. (2006) · Nature reviews. Immunology · doi:10.1038/nri1997 · Cited by 863 · see citing works
Blum-Degena, D., Müller, T., Kuhn, W., Gerlach, M., Przuntek, H., & Riederer, P. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)12192-7 · Cited by 801 · see citing works
Combs, C. K., Karlo, J. C., Kao, S.-C., & Landreth, G. E. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-04-01179.2001 · Cited by 721 · see citing works
Role of cathepsin B in intracellular trypsinogen activation and the onset of acute pancreatitis
Halangk, W., Lerch, M. M., Brandt-Nedelev, B., Roth, W., Ruthenbürger, M., Reinheckel, T., Domschke, W., Lippert, H., Peters, C., & Deussing, J. M. (2000) · Journal of Clinical Investigation · doi:10.1172/jci9411 · Cited by 564 · see citing works
Self-citationKummer, J. A., Broekhuizen, R., Everett, H., Agostini, L., Kuijk, L., Martinon, F., Bruggen, R. V., & Tschopp, J. (2007) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.6a7101.2006 · Cited by 531 · 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
CD36 Mediates the Innate Host Response to β-Amyloid
El Khoury, J. B., Moore, K. J., Means, T. K., Leung, J., Terada, K., Toft, M., Freeman, M. W., & Luster, A. D. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20021546 · Cited by 483 · see citing works
Self-citationMueller-Steiner, S., Zhou, Y.-G., Arai, H., Roberson, E., Sun, B.-G., Chen, J., Wang, X., Yu, G.-Q., Esposito, L., Mucke, L., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.07.027 · Cited by 466 · see citing works
Shaftel, S. S., Kyrkanides, S., Olschowka, J. A., Miller, J.-N. H., Johnson, R. E., & O’Banion, M. K. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31450 · Cited by 433 · see citing works
Cataldo, A. M., Barnett, J. L., Pieroni, C., & Nixon, R. A. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-16-06142.1997 · Cited by 393 · see citing works
Akama, K. T., & Eldik, L. J. V. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.7918 · Cited by 356 · see citing works
Weldon, D. T., Rogers, S. D., Ghilardi, J. R., Finke, M. P., Cleary, J. P., O’Hare, E., Esler, W. P., Maggio, J. E., & Mantyh, P. W. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-06-02161.1998 · Cited by 348 · see citing works
LPS receptor (CD14): a receptor for phagocytosis of Alzheimer's amyloid peptide
Liu, Y., Walter, S., Stagi, M., Cherny, D., Letièmbre, M., Schulz‐Schaeffer, W., Heine, H., Penke, B., Neumann, H., & Fassbender, K. C. (2005) · Brain · doi:10.1093/brain/awh531 · Cited by 344 · see citing works
Immunology and immunotherapy of Alzheimer's disease
Weiner, H. L., & Frenkel, D. (2006) · Nature Reviews Immunology · doi:10.1038/nri1843 · Cited by 335 · see citing works
Qi, Y., Wang, J. K. T., McMillian, M., & Chikaraishi, D. M. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-04-01217.1997 · Cited by 330 · see citing works
A CD36-initiated Signaling Cascade Mediates Inflammatory Effects of β-Amyloid
Moore, K. J., El Khoury, J., Medeiros, L. A., Terada, K., Geula, C., Luster, A. D., & Freeman, M. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208788200 · Cited by 327 · see citing works
Self-citationFrackowiak, J., Wisniewski, H. M., Wegiel, J., Merz, G. S., Iqbal, K., & Wang, K. C. (1992) · Acta Neuropathologica · doi:10.1007/bf00227813 · Cited by 276 · see citing works
Xie, Z., Wei, M., Morgan, T. E., Fabrizio, P., Han, D., Finch, C. E., & Longo, V. D. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-09-03484.2002 · Cited by 272 · see citing works
Richard, K. L., Filali, M., Préfontaine, P., & Rivest, S. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.1146-08.2008 · Cited by 261 · see citing works
HOOK, V. Y. H., Kindy, M. S., & Hook, G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708362200 · Cited by 207 · see citing works
CA074 methyl ester: A proinhibitor for intracellular cathepsin B
Buttle, D. J., Murata, M., Knight, C. G., & Barrett, A. J. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90290-d · Cited by 201 · see citing works
Lehnardt, S., Henneke, P., Lien, E., Kasper, D. L., Volpe, J. J., Bechmann, I., Nitsch, R., Weber, J. R., Golenbock, D. T., & Vartanian, T. K. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.1.583 · Cited by 171 · see citing works
Self-citationThe Interleukin‐1 Receptor Family
Boraschi, D., & Tagliabue, A. (2006) · Vitamins & Hormones · doi:10.1016/s0083-6729(06)74009-2 · Cited by 133 · see citing works
Severa, M., Coccia, E. M., & Fitzgerald, K. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604516200 · Cited by 127 · see citing works
Self-citationManifold Mechanisms of Toll-Like Receptor-Ligand Recognition
Ishii, K. J., Coban, C., & Akira, S. (2005) · Journal of Clinical Immunology · doi:10.1007/s10875-005-7829-1 · Cited by 102 · see citing works
Detection of Caspase Activation In Situ by Fluorochrome-Labeled Caspase Inhibitors
Amstad, P., Yu, G., Johnson, G. L., Lee, B. W., Dhawan, S., & Phelps, D. J. (2001) · BioTechniques · doi:10.2144/01313pf01 · Cited by 86 · see citing works
Roberson, S. M., & Walker, W. S. (1988) · Cellular Immunology · doi:10.1016/0008-8749(88)90236-5 · Cited by 81 · see citing works
A Signal for the Caspase-1 Inflammasome Free of TLR
Dinarello, C. A. (2007) · Immunity · doi:10.1016/j.immuni.2007.04.005 · Cited by 46 · see citing works
Li, M., Pisalyaput, K., Galvan, M. D., & Tenner, A. J. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02765.x · Cited by 39 · see citing works
Flagged first, then by citations
3 of the 50 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Neuroinflammation in Alzheimer's disease
Heneka, M. T., Carson, M. J., Khoury, J. E., Landreth, G. E., Brosseron, F., Feinstein, D. L., Jacobs, A. H., Wyss-Coray, T., Vitorica, J., Ransohoff, R. M., et al. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(15)70016-5 · Cited by 6,226 · see citing works
Self-citationSchroder, K., & Tschopp, J. (2010) · Cell · doi:10.1016/j.cell.2010.01.040 · Cited by 5,475 · see citing works
NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals
Duewell, P., Kono, H., Rayner, K. J., Sirois, C. M., Vladimer, G., Bauernfeind, F. G., Abela, G. S., Franchi, L., Nuñez, G., Schnurr, M., et al. (2010) · Nature · doi:10.1038/nature08938 · Cited by 4,026 · see citing works
Self-citationThe NLRP3 Inflammasome: an overview of mechanisms of activation and regulation
Kelley, N., Jeltema, D., Duan, Y., & He, Y. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133328 · Cited by 3,539 · see citing works
Mechanisms underlying inflammation in neurodegeneration
Glass, C. K., Saijo, K., Winner, B., Marchetto, M. C., & Gage, F. H. (2010) · Cell · doi:10.1016/j.cell.2010.02.016 · Cited by 3,580 · see citing works
Alzheimer Disease: An Update on Pathobiology and Treatment Strategies
Long, J. M., & Holtzman, D. M. (2019) · Cell · doi:10.1016/j.cell.2019.09.001 · Cited by 3,204 · see citing works
Inflammasomes: mechanism of action, role in disease, and therapeutics
Guo, H., Callaway, J. B., & Ting, J. P.-Y. (2015) · Nature Medicine · doi:10.1038/nm.3893 · Cited by 3,340 · see citing works
Ageing as a risk factor for neurodegenerative disease
Hou, Y., Dan, X., Babbar, M., Wei, Y., Hasselbalch, S. G., Croteau, D. L., & Bohr, V. A. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0244-7 · Cited by 3,310 · see citing works
Sterile inflammation: sensing and reacting to damage
Chen, G. Y., & Nuñez, G. (2010) · Nature Reviews Immunology · doi:10.1038/nri2873 · Cited by 3,051 · see citing works
Bauernfeind, F. G., Horvath, G. L., Stutz, A., Alnemri, E. S., MacDonald, K. L., Speert, D. P., Fernandes‐Alnemri, T., Wu, J., Monks, B. G., Fitzgerald, K. A., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901363 · Cited by 3,006 · see citing works
Self-citationNLRP3 is activated in Alzheimer’s disease and contributes to pathology in APP/PS1 mice
Heneka, M. T., Kummer, M. P., Stutz, A., Delekate, A., Schwartz, S., Vieira-Saecker, A., Griep, A., Axt, D., Remus, A., Tzeng, T.-C., et al. (2013) · Nature · doi:10.1038/nature11729 · Cited by 2,898 · see citing works
Self-citationMechanism and Regulation of NLRP3 Inflammasome Activation
He, Y., Hara, H., & Núñez, G. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.09.002 · Cited by 2,759 · see citing works
Thioredoxin-interacting protein links oxidative stress to inflammasome activation
Zhou, R., Tardivel, A., Thorens, B., Choi, I., & Tschopp, J. (2010) · Nature Immunology · doi:10.1038/ni.1831 · Cited by 2,708 · see citing works
The NLRP3 inflammasome instigates obesity-induced inflammation and insulin resistance
Vandanmagsar, B., Youm, Y.-H., Ravussin, A., Galgani, J. E., Stadler, K., Mynatt, R. L., Ravussin, E., Stephens, J. M., & Dixit, V. D. (2011) · Nature Medicine · doi:10.1038/nm.2279 · Cited by 2,655 · see citing works
Activation and regulation of the inflammasomes
Latz, E., Xiao, T. S., & Stutz, A. (2013) · Nature Reviews Immunology · doi:10.1038/nri3452 · Cited by 2,884 · see citing works
Self-citationCaspase Functions in Cell Death and DiseasePreprint
McIlwain, D. R., Berger, T., & Mak, T. W. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008656 · Cited by 2,607 · see citing works
Mechanisms and Functions of Inflammasomes
Lamkanfi, M., & Dixit, V. M. (2014) · Cell · doi:10.1016/j.cell.2014.04.007 · Cited by 2,521 · see citing works
The Inflammasomes: Guardians of the Body
Martinon, F., Mayor, A., & Tschopp, J. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132715 · Cited by 2,436 · see citing works
Immune attack: the role of inflammation in Alzheimer disease
Heppner, F. L., Ransohoff, R. M., & Becher, B. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3880 · Cited by 2,134 · see citing works
Targeting the NLRP3 inflammasome in inflammatory diseases
Mangan, M. S. J., Olhava, E. J., Roush, W. R., Seidel, H. M., Glick, G. D., & Latz, E. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.97 · Cited by 1,885 · see citing works
Self-citationFranchi, L., Eigenbrod, T., Muñoz-Planillo, R., & Nuñez, G. (2009) · Nature Immunology · doi:10.1038/ni.1703 · Cited by 1,834 · see citing works
NLRP3 inflammasome activation: the convergence of multiple signalling pathways on ROS production?
Tschopp, J., & Schroder, K. (2010) · Nature reviews. Immunology · doi:10.1038/nri2725 · Cited by 1,859 · see citing works
AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
Fernandes-Alnemri, T., Yu, J.-W., Datta, P., Wu, J., & Alnemri, E. S. (2009) · Nature · doi:10.1038/nature07710 · Cited by 1,831 · see citing works
DAMP-sensing receptors in sterile inflammation and inflammatory diseases
Gong, T., Liu, L., Jiang, W., & Zhou, R. (2020) · Nature Reviews Immunology · doi:10.1038/s41577-019-0215-7 · Cited by 1,672 · see citing works
The roles of TLRs, RLRs and NLRs in pathogen recognition
Kawai, T., & Akira, S. (2009) · International Immunology · doi:10.1093/intimm/dxp017 · Cited by 1,666 · see citing works
Role of neuroinflammation in neurodegeneration development
Zhang, W., Xiao, D., Mao, Q., & Xia, H. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01486-5 · Cited by 1,668 · see citing works
The Inflammasome NLRs in Immunity, Inflammation, and Associated Diseases
Davis, B. K., Wen, H., & Ting, J. P.-Y. (2011) · Annual Review of Immunology · doi:10.1146/annurev-immunol-031210-101405 · Cited by 1,618 · see citing works
NLRP3 inflammasome activation and cell death
Huang, Y., Xu, W., & Zhou, R. (2021) · Cellular & Molecular Immunology · doi:10.1038/s41423-021-00740-6 · Cited by 1,527 · see citing works
Stewart, C. R., Stuart, L. M., Wilkinson, K., van Gils, J. M., Deng, J., Halle, A., Rayner, K. J., Boyer, L., Zhong, R., Frazier, W. A., et al. (2010) · Nature Immunology · doi:10.1038/ni.1836 · Cited by 1,513 · see citing works
Self-citationUnderstanding the mechanism of IL-1β secretion
Lopez-Castejon, G., & Brough, D. (2011) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2011.10.001 · Cited by 1,519 · see citing works
NLRP3 inflammasome activation drives tau pathology
Ising, C., Venegas, C., Zhang, S., Scheiblich, H., Schmidt, S. V., Vieira-Saecker, A., Schwartz, S., Albasset, S., McManus, R. M., Tejera, D., et al. (2019) · Nature · doi:10.1038/s41586-019-1769-z · Cited by 1,487 · see citing works
Self-citationInnate immune activation in neurodegenerative disease
Heneka, M. T., Kummer, M. P., & Latz, E. (2014) · Nature Reviews Immunology · doi:10.1038/nri3705 · Cited by 1,437 · see citing works
Self-citationHMGB1 and RAGE in Inflammation and Cancer
Sims, G. P., Rowe, D. C., Rietdijk, S. T., Herbst, R., & Coyle, A. J. (2010) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132603 · Cited by 1,436 · see citing works
Molecular mechanisms regulating NLRP3 inflammasome activation
Jo, E.-K., Kim, J. K., Shin, D.-M., & Sasakawa, C. (2016) · Cellular & Molecular Immunology · doi:10.1038/cmi.2015.95 · Cited by 1,378 · see citing works
Cattaneo, A., Cattane, N., Galluzzi, S., Provasi, S., Lopizzo, N., Festari, C., Ferrari, C., Guerra, U. P., Paghera, B., Muscio, C., et al. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.08.019 · Cited by 1,382 · see citing works
Masters, S. L., Dunne, A., Subramanian, S. L., Hull, R. L., Tannahill, G. M., Sharp, F. A., Becker, C., Franchi, L., Yoshihara, E., Chen, Z., et al. (2010) · Nature Immunology · doi:10.1038/ni.1935 · Cited by 1,330 · see citing works
Recent advances in the mechanisms of NLRP3 inflammasome activation and its inhibitors
Yang, Y., Wang, H., Kouadir, M., Song, H., & Shi, F. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1413-8 · Cited by 1,285 · see citing works
The far-reaching scope of neuroinflammation after traumatic brain injury
Simon, D. W., McGeachy, M. J., Bayır, H., Clark, R. S. B., Loane, D. J., & Kochanek, P. M. (2017) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.13 · Cited by 1,190 · see citing works
Age-dependent dysregulation of innate immunity
Shaw, A. C., Goldstein, D. R., & Montgomery, R. R. (2013) · Nature Reviews Immunology · doi:10.1038/nri3547 · Cited by 1,061 · see citing works
NLRP3 inflammasome in cancer and metabolic diseases
Sharma, B. R., & Kanneganti, T. (2021) · Nature Immunology · doi:10.1038/s41590-021-00886-5 · Cited by 1,111 · see citing works
Microglial cell origin and phenotypes in health and disease
Saijo, K., & Glass, C. K. (2011) · Nature Reviews Immunology · doi:10.1038/nri3086 · Cited by 1,100 · see citing works
The calcium-sensing receptor regulates the NLRP3 inflammasome through Ca2+ and cAMP
Lee, G., Subramanian, N., Kim, A. I., Aksentijevich, I. A., Goldbach‐Mansky, R. T., Sacks, D. B., Germain, R. N., Kastner, D. L., & Chae, J. J. (2012) · Nature · doi:10.1038/nature11588 · Cited by 1,077 · see citing works
Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease
Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994 · see citing works
Horror Autoinflammaticus: The Molecular Pathophysiology of Autoinflammatory Disease
Masters, S. L., Simon, A., Aksentijevich, I. A., & Kastner, D. L. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.25.022106.141627 · Cited by 1,063 · see citing works
Inflammasome activation and regulation: toward a better understanding of complex mechanisms
Zheng, D., Liwinski, T., & Elinav, E. (2020) · Cell Discovery · doi:10.1038/s41421-020-0167-x · Cited by 1,042 · see citing works
Innate immunity in the central nervous system
Ransohoff, R. M., & Brown, M. A. (2012) · Journal of Clinical Investigation · doi:10.1172/jci58644 · Cited by 1,034 · see citing works
Dopamine controls systemic inflammation through inhibition of NLRP3 inflammasome
Yan, Y., Jiang, W., Liu, L., Wang, X., Ding, C., Tian, Z., & Zhou, R. (2015) · Cell · doi:10.1016/j.cell.2014.11.047 · Cited by 1,014 · see citing works
Autophagy‐based unconventional secretory pathway for extracellular delivery of IL‐1β
Dupont, N., Jiang, S., Pilli, M., Ornatowski, W., Bhattacharya, D., & Deretic, V. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.398 · Cited by 967 · see citing works
Innate immunity in Alzheimer's disease
Heneka, M. T., Golenbock, D. T., & Latz, E. (2015) · Nature Immunology · doi:10.1038/ni.3102 · Cited by 902 · see citing works
Self-citationSheedy, F. J., Grebe, A., Rayner, K. J., Kalantari, P., Ramkhelawon, B., Carpenter, S. B., Becker, C. E., Ediriweera, H. N., Mullick, A. E., Golenbock, D. T., et al. (2013) · Nature Immunology · doi:10.1038/ni.2639 · Cited by 935 · see citing works
Self-citationRedox Regulation of NLRP3 Inflammasomes: ROS as Trigger or Effector?
Abais, J. M., Xia, M., Zhang, Y., Boini, K. M., & Li, P. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5994 · Cited by 936 · see citing works
Regulation of inflammasome signaling
Rathinam, V. A. K., Vanaja, S. K., & Fitzgerald, K. A. (2012) · Nature Immunology · doi:10.1038/ni.2237 · Cited by 927 · see citing works
Self-citationSyk kinase signalling couples to the Nlrp3 inflammasome for anti-fungal host defence
Groß, O., Poeck, H., Bscheider, M., Dostert, C., Hannesschläger, N., Endres, S., Hartmann, G., Tardivel, A., Schweighoffer, E., Tybulewicz, V. L. J., et al. (2009) · Nature · doi:10.1038/nature07965 · Cited by 922 · see citing works
Inflammasome inhibition prevents α-synuclein pathology and dopaminergic neurodegeneration in mice
Gordon, R., Albornoz, E. A., Christie, D. C., Langley, M. R., Kumar, V., Mantovani, S., Robertson, A. A. B., Butler, M. S., Rowe, D. B., O’Neill, L. A., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aah4066 · Cited by 897 · see citing works
Kawaguchi, M., Takahashi, M., Hata, T., Kashima, Y., Usui, F., Morimoto, H., Izawa, A., Takahashi, Y., Masumoto, J., Koyama, J., et al. (2011) · Circulation · doi:10.1161/circulationaha.110.982777 · Cited by 884 · see citing works
Microglia-mediated neuroinflammation in neurodegenerative diseases
Subhramanyam, C. S., Wang, C., Hu, Q., & Dheen, S. T. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.004 · Cited by 875 · see citing works
The Sterile Inflammatory Response
Rock, K. L., Latz, E., Ontiveros, F., & Kono, H. (2010) · Annual Review of Immunology · doi:10.1146/annurev-immunol-030409-101311 · Cited by 865 · see citing works
Self-citationInflammasomes and Their Roles in Health and Disease
Lamkanfi, M., & Dixit, V. M. (2012) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155745 · Cited by 935 · see citing works
Inflammasome signalling in brain function and neurodegenerative disease
Heneka, M. T., McManus, R. M., & Latz, E. (2018) · Nature Reviews Neuroscience · doi:10.1038/s41583-018-0055-7 · Cited by 836 · see citing works
Self-citationA guiding map for inflammation
Netea, M. G., Balkwill, F., Chonchol, M., Cominelli, F., Donath, M. Y., Giamarellos-Bourboulis, E. J., Golenbock, D., Gresnigt, M. S., Heneka, M. T., Hoffman, H. M., et al. (2017) · Nature Immunology · doi:10.1038/ni.3790 · Cited by 831 · see citing works
Self-citationRegulation of innate immune responses in the brain
Rivest, S. (2009) · Nature Reviews Immunology · doi:10.1038/nri2565 · Cited by 843 · see citing works
Xian, H., Watari, K., Sanchez-Lopez, E., Offenberger, J., Onyuru, J., Sampath, H., Ying, W., Hoffman, H. M., Shadel, G. S., & Karin, M. (2022) · Immunity · doi:10.1016/j.immuni.2022.06.007 · Cited by 850 · see citing works
The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology
Rutsch, A., Kantsjö, J. B., & Ronchi, F. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.604179 · Cited by 821 · see citing works
Initiation and perpetuation of <scp>NLRP</scp> 3 inflammasome activation and assembly
Elliott, E. I., & Sutterwala, F. S. (2015) · Immunological Reviews · doi:10.1111/imr.12286 · Cited by 821 · see citing works
Glyburide inhibits the Cryopyrin/Nalp3 inflammasome
Lamkanfi, M., Mueller, J. L., Vitari, A. C., Misaghi, S., Fedorova, A., Deshayes, K., Lee, W. P., Hoffman, H. M., & Dixit, V. M. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200903124 · Cited by 820 · see citing works
Baroja-Mazo, A., Martín-Sánchez, F., Gomez, A. I., Martínez, C. M., Amores-Iniesta, J., Compan, V., Barberà-Cremades, M., Yagüe, J., Ruiz-Ortiz, E., Antón, J., et al. (2014) · Nature Immunology · doi:10.1038/ni.2919 · Cited by 790 · see citing works
The inflammasome: an integrated view
Gross, O., Thomas, C. J., Guarda, G., & Tschopp, J. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01046.x · Cited by 778 · see citing works
Lysosomal membrane permeabilization and cell death
Wang, F., Gómez‐Sintes, R., & Boya, P. (2018) · Traffic · doi:10.1111/tra.12613 · Cited by 781 · see citing works
Inflammasomes in neuroinflammatory and neurodegenerative diseases
Voet, S., Srinivasan, S., Lamkanfi, M., & van Loo, G. (2019) · EMBO Molecular Medicine · doi:10.15252/emmm.201810248 · Cited by 761 · see citing works
Microglia and neurodegeneration: The role of systemic inflammation
Cunningham, C. (2013) · Glia · doi:10.1002/glia.22350 · Cited by 769 · see citing works
Autophagy Controls IL-1β Secretion by Targeting Pro-IL-1β for Degradation
Harris, J., Hartman, M., Roche, C., Zeng, S. G., O'Shea, A., Sharp, F. A., Lambe, E. M., Creagh, E. M., Golenbock, D. T., Tschopp, J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.202911 · Cited by 794 · see citing works
Self-citationThe adaptor ASC has extracellular and 'prionoid' activities that propagate inflammation
Franklin, B. S., Bossaller, L., De Nardo, D., Ratter, J. M., Stutz, A., Engels, G., Brenker, C., Nordhoff, M., Mirandola, S. R., Al-Amoudi, A., et al. (2014) · Nature Immunology · doi:10.1038/ni.2913 · Cited by 773 · see citing works
Self-citationAbderrazak, A., Syrovets, T., Couchie, D., Hadri, K. E., Friguet, B., Simmet, T., & Rouis, M. (2015) · Redox Biology · doi:10.1016/j.redox.2015.01.008 · Cited by 737 · see citing works
The cell biology of inflammasomes: Mechanisms of inflammasome activation and regulation
Sharma, D., & Kanneganti, T. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201602089 · Cited by 733 · see citing works
The AIM2 inflammasome is critical for innate immunity to Francisella tularensis
Fernandes-Alnemri, T., Yu, J.-W., Juliana, C., Solorzano, L., Kang, S., Wu, J., Datta, P., McCormick, M., Huang, L., McDermott, E., et al. (2010) · Nature Immunology · doi:10.1038/ni.1859 · Cited by 732 · see citing works
The Adverse Effects of Air Pollution on the Nervous System
Genç, Ş., Zadeoğluları, Z., Fuss, S. H., & Genç, K. (2012) · Journal of Toxicology · doi:10.1155/2012/782462 · Cited by 728 · see citing works
Mechanisms of regulated unconventional protein secretion
Nickel, W., & Rabouille, C. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2617 · Cited by 703 · see citing works
Inflammasome activation and IL-1β and IL-18 processing during infection
van de Veerdonk, F. L., Netea, M. G., Dinarello, C. A., & Joosten, L. A. B. (2011) · Trends in Immunology · doi:10.1016/j.it.2011.01.003 · Cited by 693 · see citing works
Cao, X. (2015) · Nature reviews. Immunology · doi:10.1038/nri.2015.8 · Cited by 661 · see citing works
Pharmacological Inhibitors of the NLRP3 Inflammasome
Zahid, A., Li, B., Kombe, A. J. K., Jin, T., & Tao, J. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02538 · Cited by 671 · see citing works
The role of peripheral immune cells in the CNS in steady state and disease
Prinz, M., & Priller, J. (2017) · Nature Neuroscience · doi:10.1038/nn.4475 · Cited by 657 · see citing works
Walsh, J. G., Muruve, D. A., & Power, C. (2014) · Nature Reviews Neuroscience · doi:10.1038/nrn3638 · Cited by 637 · see citing works
The role of IL-1β and TNF-α in intervertebral disc degeneration
Wang, Y., Che, M., Xin, J., Zheng, Z. J., Li, J., & Zhang, S. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110660 · Cited by 626 · see citing works
The role of interleukin-1 in general pathology
Kaneko, N., Kurata, M., Yamamoto, T., Morikawa, S., & Masumoto, J. (2019) · Inflammation and Regeneration · doi:10.1186/s41232-019-0101-5 · Cited by 616 · see citing works
Anti-inflammatory Compounds Parthenolide and Bay 11-7082 Are Direct Inhibitors of the Inflammasome
Juliana, C. A., Fernandes‐Alnemri, T., Wu, J., Datta, P., Solórzano, L., Yu, J., Meng, R., Quong, A. A., Latz, E., Scott, C. P., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.082305 · Cited by 617 · see citing works
Self-citationInformation processing during phagocytosis
Underhill, D. M., & Goodridge, H. S. (2012) · Nature Reviews Immunology · doi:10.1038/nri3244 · Cited by 616 · see citing works
Interplay Between NLRP3 Inflammasome and Autophagy
Biasizzo, M., & Kopitar‐Jerala, N. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.591803 · Cited by 620 · see citing works
DICER1 loss and Alu RNA induce age-related macular degeneration via the NLRP3 inflammasome and MyD88
Tarallo, V., Hirano, Y., Gelfand, B. D., Dridi, S., Kerur, N., Kim, Y., Cho, W. G., Kaneko, H., Fowler, B. J., Bogdanovich, S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.036 · Cited by 592 · see citing works
Inflammasome activation and function in liver disease
Szabó, G., & Petrasek, J. (2015) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2015.94 · Cited by 600 · see citing works
Li, N., Zhou, H., Wu, H., Wu, Q., Duan, M., Deng, W., & Tang, Q. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101215 · Cited by 595 · see citing works
Interplay between innate immunity and Alzheimer disease: APOE and TREM2 in the spotlight
Shi, Y., & Holtzman, D. M. (2018) · Nature Reviews Immunology · doi:10.1038/s41577-018-0051-1 · Cited by 595 · see citing works
Pathogen recognition in the innate immune response
Kumar, H., Kawai, T., & Akira, S. (2009) · Biochemical Journal · doi:10.1042/bj20090272 · Cited by 586 · see citing works
Blevins, H. M., Xu, Y., Biby, S., & Zhang, S. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.879021 · Cited by 587 · see citing works
Triggering of inflammasome by aggregated α-synuclein, an inflammatory response in synucleinopathies
Codolo, G., Plotegher, N., Pozzobon, T., Brucale, M., Tessari, I., Bubacco, L., & de Bernard, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055375 · Cited by 585 · see citing works
The inflammasome: Pathways linking psychological stress, depression, and systemic illnesses
Iwata, M., Ota, K. T., & Duman, R. S. (2013) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2012.12.008 · Cited by 580 · see citing works
Franchi, L., Eigenbrod, T., & Núñez, G. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900173 · Cited by 574 · see citing works
Microglial cell dysregulation in brain aging and neurodegeneration
von Bernhardi, R., Eugenín-von Bernhardi, L., & Eugenín, J. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00124 · Cited by 556 · see citing works
Dempsey, C., Rubio Araiz, A., Bryson, K. J., Finucane, O., Larkin, C., Mills, E. L., Robertson, A. A. B., Cooper, M. A., O'Neill, L. A. J., & Lynch, M. A. (2017) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2016.12.014 · Cited by 571 · see citing works
Heid, M. E., Keyel, P. A., Kamga, C., Shiva, S., Watkins, S. C., & Salter, R. D. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301490 · Cited by 570 · see citing works
Hise, A. G., Tomalka, J. A., Ganesan, S., Patel, K., Hall, B. A., Brown, G. D., & Fitzgerald, K. A. (2009) · Cell Host & Microbe · doi:10.1016/j.chom.2009.05.002 · Cited by 568 · see citing works
Self-citation
- Authors
- Halle, A., Hornung, V., Petzold, G. C., Stewart, C. R., Monks, B. G., Reinheckel, T., Fitzgerald, K. A., Latz, E., Moore, K. J., & Golenbock, D. T.
- Affiliations
- University of Massachusetts Chan Medical School (US)
- Harvard University (US)
- University of Freiburg (DE)
- Corresponding author
- Golenbock, Douglas T
- ORCID
- Venue
- Nature Immunology
- Published
- 2008-07-11
- Volume
- 9
- Issue
- 8
- Pages
- 857-865
- ISSN
- 1529-2908 (ISSN-L)
- 1529-2916
- PMC
- PMC3101478
- OpenAlex
- W2119098586
- Cited by
- 2,441
- References
- 50
- Citations by year
- 2026: 92 · 2025: 124 · 2024: 143 · 2023: 165 · 2022: 191 · 2021: 188 · 2020: 169 · 2019: 151 · 2018: 136 · 2017: 139 · 2016: 138 · 2015: 146 · 2014: 149 · 2013: 153 · 2012: 98
- FWCI
- 35.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Immunology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship@UMassChan (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- National Institute on Aging (R01AG020255, AG20255)
- National Institute of General Medical Sciences (R37GM054060, R01GM054060, GM 54060)
- National Institute of Allergy and Infectious Diseases (AI065483, R01AI065483)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- NLRP3 inflammasome, amyloid-beta, Alzheimer's disease, innate immunity, IL-1β, caspase-1, microglia, phagocytosis, lysosomal damage, cathepsin B, neuroinflammation, neurotoxicity
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Alzheimer Disease, Carrier Proteins, Immunity, Innate, Inflammation, Amyloid beta-Peptides, Inflammation Mediators
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