Inflammasomes: mechanism of action, role in disease, and therapeutics
Open accessAbstract
The inflammasomes are innate immune system receptors and sensors that regulate the activation of caspase-1 and induce inflammation in response to infectious microbes and molecules derived from host proteins. They have been implicated in a host of inflammatory disorders. Recent developments have greatly enhanced our understanding of the molecular mechanisms by which different inflammasomes are activated. Additionally, increasing evidence in mouse models, supported by human data, strongly implicates an involvement of the inflammasome in the initiation or progression of diseases with a high impact on public health, such as metabolic disorders and neurodegenerative diseases. Finally, recent developments pointing toward promising therapeutics that target inflammasome activity in inflammatory diseases have been reported. This review will focus on these three areas of inflammasome research.
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Inflammasomes activate Caspase-1, interleukin (IL)-1β, and IL-18 to produce pyroptosis that releases damage-associated molecular patterns (DAMPs) to subsequently recruit more immune cells.
“Inflammasomes activate Caspase-1, interleukin (IL)-1β, and IL-18 to produce pyroptosis that releases damage-associated molecular patterns (DAMPs) to subsequently recruit more immune cells to mount a robust immune attack against pathogens102.”
From Key points for the development of antioxidant cocktails to prevent cellular stress and damage caused by reactive oxygen species (ROS) during manned space missions (2021) · cites this paper as [102]
The Introduction and “General principles of inflammasome activation” describe inflammasome activation of caspase-1, which processes IL-1β and IL-18 and induces pyroptosis. “Therapies that target inflammasomes” says pyroptosis releases DAMPs that induce more inflammation. The copy does not establish the claimed next step—that those DAMPs recruit more immune cells to attack pathogens. (LLM, conf=0.85)
Experimental — accuracy not yet measuredThe NLRP3 inflammasome mediates proteolytic cleavage of pro-caspase-1 leading to activation of caspase-1, which cleaves pro-interleukin 1β and 18 into their active cytokine forms.
“The NLR3P inflammasome mediates proteolytic cleave of pro-caspase-1 leading to activation of caspase-1, which cleaves pro-interleukin 1β and 18 into their active cytokine forms (47).”
From Chronic stress, neuroinflammation, and depression: an overview of pathophysiological mechanisms and emerging anti-inflammatories (2023) · cites this paper as [47]
Transcriptomic data showed an increased inflammatory response in hepatocytes under lipotoxic conditions, with upregulation of Toll-like receptors, chemokines, and STATs.
“Transcriptomic data support an increased inflammatory response triggered by the lipotoxic milieu in hepatocytes, where gene expression changes in inflammation and inflammasome (33) signaling pathways were increased”
From Development of an in vitro human liver system for interrogating nonalcoholic steatohepatitis (2016) · cites this paper as [33]
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Obesity is associated with macrophage accumulation in adipose tissue
Weisberg, S. P., McCann, D., Desai, M., Rosenbaum, M., Leibel, R. L., & Ferrante, A. W. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200319246 · Cited by 10,041 · see citing works
Pattern Recognition Receptors and Inflammation
Takeuchi, O., & Akira, S. (2010) · Cell · doi:10.1016/j.cell.2010.01.022 · Cited by 8,895 · see citing works
Adipose Expression of Tumor Necrosis Factor-α: Direct Role in Obesity-Linked Insulin Resistance
Hotamisligil, G. S., Shargill, N. S., & Spiegelman, B. M. (1993) · Science · doi:10.1126/science.7678183 · Cited by 7,518 · see citing works
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,435 · see citing works
Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066 · see citing works
Functional interactions between the gut microbiota and host metabolism
Tremaroli, V., & Bäckhed, F. (2012) · Nature · doi:10.1038/nature11552 · Cited by 4,387 · 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
Type 2 diabetes as an inflammatory disease
Donath, M. Y., & Shoelson, S. E. (2011) · Nature Reviews Immunology · doi:10.1038/nri2925 · Cited by 3,737 · see citing works
Kim, H. J., Park, S. Y., Choi, Y. J., Han, S. J., Lee, K. W., & Kim, D. J. (2013) · Hormone Research in Paediatrics · doi:10.1159/000348848 · Cited by 3,061 · 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
NLRP3 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
A small-molecule inhibitor of the NLRP3 inflammasome for the treatment of inflammatory diseases
Coll, R. C., Robertson, A. A. B., Chae, J. J., Higgins, S. C., Muñoz-Planillo, R., Inserra, M. C., Vetter, I., Dungan, L. S., Monks, B. G., Stutz, A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3806 · Cited by 2,849 · 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
AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
Hornung, V., Ablasser, A., Charrel-Dennis, M., Bauernfeind, F., Horvath, G., Caffrey, D. R., Latz, E., & Fitzgerald, K. A. (2009) · Nature · doi:10.1038/nature07725 · Cited by 2,627 · see citing works
Non-canonical inflammasome activation targets caspase-11
Kayagaki, N., Warming, S., Lamkanfi, M., Walle, L. V., Louie, S., Dong, J., Newton, K., Qu, Y., Liu, J., Heldens, S., et al. (2011) · Nature · doi:10.1038/nature10558 · Cited by 2,530 · 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 NALP3 inflammasome is involved in the innate immune response to amyloid-β
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. (2008) · Nature Immunology · doi:10.1038/ni.1636 · Cited by 2,441 · see citing works
Adipocyte dysfunctions linking obesity to insulin resistance and type 2 diabetes.
Guilherme, A., Virbasius, J. V., Puri, V., & Czech, M. P. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2391 · Cited by 2,292 · see citing works
Inflammatory caspases are innate immune receptors for intracellular LPS
Shi, J., Zhao, Y., Wang, Y., Gao, W., Ding, J., Li, P., Hu, L., & Shao, F. (2014) · Nature · doi:10.1038/nature13683 · Cited by 2,285 · see citing works
Inflammasomes in health and disease
Strowig, T., Henao-Mejia, J., Elinav, E., & Flavell, R. (2012) · Nature · doi:10.1038/nature10759 · Cited by 2,230 · see citing works
Atherosclerosis: current pathogenesis and therapeutic options
Weber, C., & Noels, H. (2011) · Nature Medicine · doi:10.1038/nm.2538 · Cited by 2,203 · see citing works
The ketone metabolite β-hydroxybutyrate blocks NLRP3 inflammasome-mediated inflammatory disease
Youm, Y.-H., Nguyen, K. Y., Grant, R. W., Goldberg, E. L., Bodogai, M., Kim, D., D'Agostino, D., Planavsky, N., Lupfer, C., Kanneganti, T. D., et al. (2015) · Nature Medicine · doi:10.1038/nm.3804 · Cited by 2,172 · 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
Fatty acid–induced NLRP3-ASC inflammasome activation interferes with insulin signaling
Wen, H., Gris, D., Lei, Y. L., Jha, S., Zhang, L., Huang, M. T.-H., Brickey, W. J., & Ting, J. P. ‐. (2011) · Nature Immunology · doi:10.1038/ni.2022 · Cited by 1,811 · see citing works
Self-citationInterleukin-1-receptor antagonist in type 2 diabetes mellitus
Larsen, C. M., Faulenbach, M., Vaag, A., Vølund, A., Ehses, J. A., Seifert, B., Mandrup-Poulsen, T., & Donath, M. Y. (2007) · New England Journal of Medicine · doi:10.1056/nejmoa065213 · Cited by 1,798 · see citing works
Noncanonical Inflammasome Activation by Intracellular LPS Independent of TLR4
Kayagaki, N., Wong, M. T., Stowe, I. B., Ramani, S. R., Gonzalez, L. C., Akashi‐Takamura, S., Miyake, K., Zhang, J., Lee, W. P., Muszyński, A., et al. (2013) · Science · doi:10.1126/science.1240248 · Cited by 1,544 · see citing works
Unified Polymerization Mechanism for the Assembly of ASC-Dependent Inflammasomes
Lu, A., Magupalli, V. G., Ruan, J., Yin, Q., Atianand, M. K., Vos, M. R., Schröder, G. F., Fitzgerald, K. A., Wu, H., & Egelman, E. H. (2014) · Cell · doi:10.1016/j.cell.2014.02.008 · Cited by 1,353 · 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
Cooper, G. J., Willis, A. C., Clark, A., Turner, R. C., Sim, R. B., & Reid, K. B. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.23.8628 · Cited by 1,299 · see citing works
The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus
Zhao, Y., Yang, J., Shi, J., Gong, Y., Lu, Q., Xu, H., Liu, L., & Shao, F. (2011) · Nature · doi:10.1038/nature10510 · Cited by 1,273 · see citing works
Cytoplasmic LPS Activates Caspase-11: Implications in TLR4-Independent Endotoxic Shock
Hagar, J. A., Powell, D. A., Aachoui, Y., Ernst, R. K., & Miao, E. A. (2013) · Science · doi:10.1126/science.1240988 · Cited by 1,265 · see citing works
Caspase-1 processes IFN-γ-inducing factor and regulates LPS-induced IFN- γ production
Ghayur, T., Banerjee, S., Hugunin, M., Butler, D., Herzog, L., Carter, A. B., Quintal, L. J., Sekut, L., Talanian, R. V., Paskind, M. P., et al. (1997) · Nature · doi:10.1038/386619a0 · Cited by 1,204 · see citing works
Compston, A., & Coles, A. (2008) · The Lancet · doi:10.1016/s0140-6736(08)61620-7 · Cited by 1,184 · see citing works
Activation of Interferon-γ Inducing Factor Mediated by Interleukin-1β Converting Enzyme
Gu, Y., Kuida, K., Tsutsui, H., Ku, G., Hsiao, K., Fleming, M. A., Hayashi, N., Higashino, K., Okamura, H., Nakanishi, K., et al. (1997) · Science · doi:10.1126/science.275.5297.206 · Cited by 1,159 · see citing works
Glucose-induced β cell production of IL-1β contributes to glucotoxicity in human pancreatic islets
Maedler, K., Sergeev, P., Ris, F., Oberholzer, J., Joller‐Jemelka, H. I., Spinas, G. A., Kaiser, N., Halban, P. A., & Donath, M. Y. (2017) · Journal of Clinical Investigation · doi:10.1172/jci92172 · Cited by 1,114 · 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
Autoimmune T cell responses in the central nervous system
Goverman, J. M. (2009) · Nature reviews. Immunology · doi:10.1038/nri2550 · Cited by 1,025 · 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
Glucose-induced β cell production of IL-1β contributes to glucotoxicity in human pancreatic islets
Maedler, K., Sergeev, P., Ris, F., Oberholzer, J., Joller‐Jemelka, H. I., Spinas, G. A., Kaiser, N., Halban, P. A., & Donath, M. Y. (2002) · Journal of Clinical Investigation · doi:10.1172/jci200215318 · Cited by 1,006 · see citing works
Interleukin-18 and IL-18 Binding Protein
Dinarello, C. A., Novick, D., Kim, S., & Kaplanski, G. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00289 · Cited by 938 · see citing works
Sheedy, 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
Inflammasomes 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
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
Critical role for calcium mobilization in activation of the NLRP3 inflammasome
Murakami, T., Öckinger, J., Yu, J., Byles, V., McColl, A., Hofer, A. M., & Horng, T. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117765109 · Cited by 926 · see citing works
Type I Interferon Inhibits Interleukin-1 Production and Inflammasome Activation
Guarda, G., Braun, M., Staehli, F., Tardivel, A., Mattmann, C., Förster, I., Farlik, M., Decker, T., Pasquier, R. D., Romero, P. J., et al. (2011) · Immunity · doi:10.1016/j.immuni.2011.02.006 · Cited by 924 · 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
Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity
Kofoed, E. M., & Vance, R. E. (2011) · Nature · doi:10.1038/nature10394 · Cited by 894 · 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
Parkinson’s disease: genetics and pathogenesis
Shulman, J. M., De Jager, P. L., & Feany, M. B. (2011) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-011110-130242 · Cited by 801 · see citing works
Yan, Y., Jiang, W., Spinetti, T., Tardivel, A., Castillo, R., Bourquin, C., Guarda, G., Tian, Z., Tschopp, J., & Zhou, R. (2013) · Immunity · doi:10.1016/j.immuni.2013.05.015 · Cited by 784 · see citing works
The 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
Non-transcriptional Priming and Deubiquitination Regulate NLRP3 Inflammasome Activation
Juliana, C. A., Fernandes‐Alnemri, T., Kang, S., Farias, A., Qin, F., & Alnemri, E. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407130 · Cited by 771 · see citing works
Lack of Interleukin-1β Decreases the Severity of Atherosclerosis in ApoE-Deficient Mice
Kirii, H., Niwa, T., Yamada, Y., Wada, H., Saito, K., Iwakura, Y., Asano, M., Moriwaki, H., & Seishima, M. (2003) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000064374.15232.c3 · Cited by 748 · see citing works
Canna, S., de Jesus, A. A., Gouni, S., Brooks, S. R., Marrero, B., Liu, Y., DiMattia, M. A., Zaal, K. J. M., Sanchez, G. A. M., Kim, H., et al. (2014) · Nature Genetics · doi:10.1038/ng.3089 · Cited by 739 · see citing works
Mechanism of NLRP3 inflammasome activation
Sutterwala, F. S., Haasken, S., & Cassel, S. L. (2014) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12458 · Cited by 736 · see citing works
Upregulated NLRP3 Inflammasome Activation in Patients With Type 2 Diabetes
Lee, H., Kim, J.-J., Kim, H. J., Shong, M., Ku, B. J., & Jo, E. (2012) · Diabetes · doi:10.2337/db12-0420 · Cited by 730 · see citing works
Inflammasome is a central player in the induction of obesity and insulin resistance
Stienstra, R., van Diepen, J. A., Tack, C. J., Zaki, M. H., van de Veerdonk, F. L., Perera, D., Neale, G. A., Hooiveld, G. J., Hijmans, A., Vroegrijk, I., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100255108 · Cited by 727 · see citing works
Deubiquitination of NLRP3 by BRCC3 Critically Regulates Inflammasome Activity
Py, B. F., Kim, M.-S., Vakifahmetoglu-Norberg, H., & Yuan, J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.11.009 · Cited by 718 · see citing works
Stienstra, R., Joosten, L. A. B., Koenen, T. B., van Tits, B. L. J. H., van Diepen, J. A., van den Berg, S. A. A., Rensen, P. C. N., Voshol, P. J., Fantuzzi, G., Hijmans, A., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.011 · Cited by 681 · 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
Gringhuis, S. I., Kaptein, T. M., Wevers, B. A., Theelen, B., van der Vlist, M., Boekhout, T., & Geijtenbeek, T. B. H. (2012) · Nature Immunology · doi:10.1038/ni.2222 · Cited by 612 · 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 PYRIN-CARD Protein ASC Is an Activating Adaptor for Caspase-1
Srinivasula, S. M., Poyet, J.-L., Razmara, M., Datta, P., Zhang, Z., & Alnemri, E. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200179200 · Cited by 573 · see citing works
Jin, T., Perry, A., Jiang, J., Smith, P. T., Curry, J. A., Unterholzner, L., Jiang, Z., Horvath, G. L., Rathinam, V. A. K., Johnstone, R. W., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.02.014 · Cited by 571 · see citing works
Cai, X., Chen, J., Xu, H., Liu, S., Jiang, Q., Halfmann, R., & Chen, Z. J. (2014) · Cell · doi:10.1016/j.cell.2014.01.063 · Cited by 567 · see citing works
Gurung, P., Anand, P., Malireddi, R. K. S., Walle, L. V., Opdenbosch, N. V., Dillon, C. P., Weinlich, R., Green, D. R., Lamkanfi, M., & Kanneganti, T. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302839 · Cited by 558 · see citing works
Mutation of NLRC4 causes a syndrome of enterocolitis and autoinflammation
Romberg, N. D., Moussawi, K. A., Nelson-Williams, C. J., Stiegler, A. L., Loring, E. C., Choi, M., Overton, J. D., Meffre, E., Khokha, M. K., Huttner, A. J., et al. (2014) · Nature Genetics · doi:10.1038/ng.3066 · Cited by 512 · see citing works
AIM2 and NLRP3 inflammasomes activate both apoptotic and pyroptotic death pathways via ASC
Sagulenko, V., Thygesen, S. J., Sester, D. P., Idris, A., Cridland, J. A., Vajjhala, P. R., Roberts, T. L., Schroder, K., Vince, J. E., Hill, J. M., et al. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.37 · Cited by 511 · see citing works
Adipose Tissue Macrophages Promote Myelopoiesis and Monocytosis in Obesity
Nagareddy, P. R., Kraakman, M. J., Masters, S. L., Stirzaker, R. A., Gorman, D. J., Grant, R. W., Dragoljevic, D., Hong, E. S., Abdel‐Latif, A., Smyth, S. S., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.029 · Cited by 510 · see citing works
Mechanisms of inflammasome activation: recent advances and novel insights
Vanaja, S. K., Rathinam, V. A. K., & Fitzgerald, K. A. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.12.009 · Cited by 499 · see citing works
Identification of Ipaf, a Human Caspase-1-activating Protein Related to Apaf-1
Poyet, J., Srinivasula, S. M., Tnani, M., Razmara, M., Fernandes‐Alnemri, T., & Alnemri, E. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100250200 · Cited by 456 · see citing works
25-Hydroxycholesterol suppresses interleukin-1–driven inflammation downstream of type I interferon
Reboldi, A., Dang, E. V., McDonald, J. G., Liang, G., Russell, D. W., & Cyster, J. G. (2014) · Science · doi:10.1126/science.1254790 · Cited by 444 · see citing works
Autoproteolytic Activation of Pro-Caspases by Oligomerization
Yang, X., Chang, H. Y., & Baltimore, D. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80032-5 · Cited by 435 · see citing works
Gris, D., Ye, Z., Iocca, H. A., Wen, H., Craven, R. R., Gris, P., Huang, M., Schneider, M., Miller, S. D., & Ting, J. P.-Y. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0904145 · Cited by 429 · see citing works
Self-citationDeficiency of interleukin-18 in mice leads to hyperphagia, obesity and insulin resistance
Netea, M. G., Joosten, L. A. B., Lewis, E., Jensen, D. R., Voshol, P. J., Kullberg, B. J., Tack, C. J., van Krieken, H., Kim, S.-H., Stalenhoef, A. F., et al. (2006) · Nature Medicine · doi:10.1038/nm1415 · Cited by 424 · see citing works
Mechanisms of NOD-like Receptor-Associated Inflammasome Activation
Wen, H., Miao, E. A., & Ting, J. P. ‐. (2013) · Immunity · doi:10.1016/j.immuni.2013.08.037 · Cited by 415 · see citing works
Self-citationYang, J., Zhao, Y., Shi, J., & Shao, F. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1306376110 · Cited by 415 · see citing works
Mallat, Z., Corbaz, A., Scoazec, A., Graber, P., Alouani, S., Esposito, B., Humbert, Y., Chvatchko, Y., & Tedgui, A. (2001) · Circulation Research · doi:10.1161/hh1901.098735 · Cited by 404 · see citing works
Malarial Hemozoin Is a Nalp3 Inflammasome Activating Danger Signal
Dostert, C., Guarda, G., Romero, J. F., Menu, P., Groß, O., Tardivel, A., Suvà, M.-L., Stehle, J., Köpf, M., Stamenkovic, I., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006510 · Cited by 397 · see citing works
Jourdan, T., Godlewski, G., Cinar, R., Bertola, A., Szanda, G., Liu, J., Tam, J., Han, T., Mukhopadhyay, B., Skarulis, M. C., et al. (2013) · Nature Medicine · doi:10.1038/nm.3265 · Cited by 388 · see citing works
Hara, H., Tsuchiya, K., Kawamura, I., Fang, R., Hernández-Cuellar, E., Shen, Y., Mizuguchi, J., Schweighoffer, E., Tybulewicz, V. L. J., & Mitsuyama, M. (2013) · Nature Immunology · doi:10.1038/ni.2749 · Cited by 382 · see citing works
Man, S. M., Karki, R., Malireddi, R. K. S., Neale, G., Vogel, P., Yamamoto, M., Lamkanfi, M., & Kanneganti, T.-D. (2015) · Nature Immunology · doi:10.1038/ni.3118 · Cited by 380 · see citing works
Reduced atherosclerosis in interleukin-18 deficient apolipoprotein E-knockout mice
Elhage, R. (2003) · Cardiovascular Research · doi:10.1016/s0008-6363(03)00343-2 · Cited by 374 · see citing works
Glucose-induced β cell production of IL-1β contributes to glucotoxicity in human pancreatic islets
Maedler, K., Sergeev, P., Ris, F., Oberholzer, J., Joller‐Jemelka, H. I., Spinas, G. A., Kaiser, N., Halban, P. A., & Donath, M. Y. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15318 · Cited by 363 · see citing works
Chalkiadaki, A., & Guarente, L. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.07.003 · Cited by 352 · see citing works
Spontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide.
Janson, J., Soeller, W. C., Roche, P. C., Nelson, R. T., Torchia, A. J., Kreutter, D. K., & Butler, P. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.14.7283 · Cited by 343 · see citing works
Kang, S.-J., Wang, S., Hara, H., Peterson, E. P., Namura, S., Amin‐Hanjani, S., Huang, Z., Srinivasan, A. N., Tomaselli, K. J., Thornberry, N. A., et al. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.3.613 · Cited by 326 · see citing works
IL-1 Blockade in Autoinflammatory Syndromes
de Jesus, A. A., & Goldbach‐Mansky, R. T. (2014) · Annual Review of Medicine · doi:10.1146/annurev-med-061512-150641 · Cited by 326 · see citing works
Howard, A. D., Kostura, M. J., Thornberry, N. A., DING, G. J.-F., Limjuco, G. A., Weidner, J. R., Salley, J. P., Hogquist, K. A., Chaplin, D., & Mumford, R. A. (1991) · The Journal of Immunology · doi:10.4049/jimmunol.147.9.2964 · Cited by 323 · see citing works
Phosphorylation of NLRC4 is critical for inflammasome activation
Qu, Y., Misaghi, S., Izrael-Tomasevic, A., Newton, K., Gilmour, L. L., Lamkanfi, M., Louie, S., Kayagaki, N., Liu, J., Kömüves, L. G., et al. (2012) · Nature · doi:10.1038/nature11429 · Cited by 320 · see citing works
Jha, S., Srivastava, S. Y., Brickey, W. J., Iocca, H., Toews, A., Morrison, J. P., Chen, V. S., Gris, D., Matsushima, G. K., & Ting, J. P.-Y. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4088-10.2010 · Cited by 310 · see citing works
Self-citationFreigang, S., Ampenberger, F., Weiss, A., Kanneganti, T., Iwakura, Y., Hersberger, M., & Köpf, M. (2013) · Nature Immunology · doi:10.1038/ni.2704 · Cited by 304 · see citing works
Inoue, M., Williams, K. L., Gunn, M. D., & Shinohara, M. L. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1201836109 · Cited by 288 · see citing works
Finucane, O. M., Lyons, C. L., Murphy, A. M., Reynolds, C. M., Klinger, R. W., Healy, N. P., Cooke, A. A., Coll, R. C., McAllan, L., Nilaweera, K. N., et al. (2015) · Diabetes · doi:10.2337/db14-1098 · Cited by 281 · see citing works
K+ Efflux Agonists Induce NLRP3 Inflammasome Activation Independently of Ca2+ Signaling
Katsnelson, M. J., Rucker, L. G., Russo, H. M., & Dubyak, G. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402658 · Cited by 278 · see citing works
He, Y., Varadarajan, S., Muñoz-Planillo, R., Burberry, A., Nakamura, Y., & Núñez, G. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.515080 · Cited by 272 · see citing works
The Inflammasome Puts Obesity in the Danger Zone
Stienstra, R., Tack, C. J., Kanneganti, T., Joosten, L. A. B., & Netea, M. G. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2011.10.011 · Cited by 272 · see citing works
Bryan, N. B., Dorfleutner, A., Rojanasakul, Y., & Stehlik, C. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0802367 · Cited by 260 · see citing works
Atherosclerosis in ApoE-deficient mice progresses independently of the NLRP3 inflammasome
Menu, P., Pellegrin, M., Aubert, J.-F., Bouzourène, K., Tardivel, A., Mazzolai, L., & Tschopp, J. (2011) · Cell Death and Disease · doi:10.1038/cddis.2011.18 · Cited by 249 · see citing works
The linear ubiquitin assembly complex (LUBAC) is essential for NLRP3 inflammasome activation
Rodgers, M. A., Bowman, J. W., Fujita, H., Orazio, N., Shi, M., Liang, Q., Amatya, R., Kelly, T. J., Iwai, K., Ting, J., et al. (2014) · Journal of Experimental Medicine · doi:10.1084/jem.20132486 · Cited by 247 · see citing works
Self-citationChavarría‐Smith, J., & Vance, R. E. (2015) · Immunological Reviews · doi:10.1111/imr.12283 · Cited by 247 · see citing works
Man, S. M., Tourlomousis, P., Hopkins, L., Monie, T. P., Fitzgerald, K. A., & Bryant, C. E. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301581 · Cited by 239 · see citing works
Allam, R., Lawlor, K. E., Yu, E. C.-W., Mildenhall, A., Moujalled, D. M., Lewis, R. S., Ke, F., Mason, K. D., White, M. J., Stacey, K. J., et al. (2014) · EMBO Reports · doi:10.15252/embr.201438463 · Cited by 238 · see citing works
Blockade of interleukin 1 in type 1 diabetes mellitus
Mandrup-Poulsen, T. R., Pickersgill, L., & Donath, M. Y. (2010) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2009.271 · Cited by 236 · see citing works
Ferrari, C. C., Pott Godoy, M. C., Tarelli, R., Chertoff, M., Depino, A. M., & Pitossi, F. J. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.06.013 · Cited by 235 · see citing works
Divergence of IL-1, IL-18, and cell death in NLRP3 inflammasomopathies
Brydges, S. D., Broderick, L., McGeough, M. D., Peña, C. A., Mueller, J. L., & Hoffman, H. M. (2013) · Journal of Clinical Investigation · doi:10.1172/jci71543 · Cited by 228 · see citing works
Bhaskar, V., Yin, J., Mirza, A. M., Phan, D., Vanegas, S., Issafras, H., Michelson, K. S., Hunter, J., & Kantak, S. S. (2011) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2011.02.026 · Cited by 226 · see citing works
Nucleoside reverse transcriptase inhibitors possess intrinsic anti-inflammatory activity
Fowler, B. J., Gelfand, B. D., Kim, Y., Kerur, N., Tarallo, V., Hirano, Y., Amarnath, S., Fowler, D. H., Radwan, M., Young, M. T., et al. (2014) · Science · doi:10.1126/science.1261754 · Cited by 225 · see citing works
Honda, H., Nagai, Y., Matsunaga, T., Okamoto, N., Watanabe, Y., Tsuneyama, K., Hayashi, H., Fujii, I., Ikutani, M., Hirai, Y., et al. (2014) · Journal of Leukocyte Biology · doi:10.1189/jlb.3a0114-005rr · Cited by 213 · see citing works
Vance, R. E. (2015) · Current Opinion in Immunology · doi:10.1016/j.coi.2015.01.010 · Cited by 210 · 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
Molecular Basis for Specific Recognition of Bacterial Ligands by NAIP/NLRC4 Inflammasomes
Tenthorey, J. L., Kofoed, E. M., Daugherty, M. D., Malik, H. S., & Vance, R. E. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.018 · Cited by 196 · see citing works
Free fatty acids as modulators of the NLRP3 inflammasome in obesity/type 2 diabetes
Legrand-Poels, S., Esser, N., L’homme, L., Scheen, A., Paquot, N., & Piette, J. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.08.013 · Cited by 194 · see citing works
Caspase-1 Regulates the Inflammatory Process Leading to Autoimmune Demyelination
Furlan, R., Martino, G., Galbiati, F., Poliani, P. L., Smiroldo, S., Bergami, A., Desina, G., Comı, G., Flavell, R. A., Su, M. S. S., et al. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.5.2403 · Cited by 194 · see citing works
Inoue, M., Williams, K. L., Oliver, T. N., Vandenabeele, P., Rajan, J. V., Miao, E. A., & Shinohara, M. L. (2012) · Science Signaling · doi:10.1126/scisignal.2002767 · Cited by 193 · see citing works
Cutting Edge: Mouse NAIP1 Detects the Type III Secretion System Needle Protein
Rayamajhi, M., Zak, D. E., Chavarría‐Smith, J., Vance, R. E., & Miao, E. A. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301549 · Cited by 185 · see citing works
Shi, F., Takeda, K., Akira, S., Sarvetnick, N., & Ljunggren, H. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.6.3099 · Cited by 178 · see citing works
Jin, T., Perry, A., Smith, P. T., Jiang, J., & Xiao, T. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.468033 · Cited by 174 · see citing works
Unsaturated fatty acids prevent activation of NLRP3 inflammasome in human monocytes/macrophages
L’homme, L., Esser, N., Riva, L., Scheen, A. J., Paquot, N., Piette, J. G., & Legrand-Poels, S. (2013) · Journal of Lipid Research · doi:10.1194/jlr.m037861 · Cited by 169 · see citing works
The Inflammasome in Atherosclerosis and Type 2 Diabetes
Masters, S. L., Latz, E., & O’Neill, L. A. J. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3001902 · Cited by 169 · see citing works
Shaw, P. J., Lukens, J. R., Burns, S., Chi, H., McGargill, M. A., & Kanneganti, T. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000217 · Cited by 160 · see citing works
Origins and Effects of Extracellular α-synuclein: Implications in Parkinson’s Disease
Lee, S. (2007) · Journal of Molecular Neuroscience · doi:10.1007/s12031-007-0012-9 · Cited by 159 · see citing works
Matsuki, T., Nakae, S., Sudo, K., Horai, R., & Iwakura, Y. (2006) · International Immunology · doi:10.1093/intimm/dxh379 · Cited by 142 · see citing works
Coll, R. C., & O'Neill, L. A. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0029539 · Cited by 137 · see citing works
Functions of caspase 8: The identified and the mysterious
Salvesen, G. S., & Walsh, C. M. (2014) · Seminars in Immunology · doi:10.1016/j.smim.2014.03.005 · Cited by 136 · see citing works
Misfolded α-synuclein and toll-like receptors: therapeutic targets for Parkinson's disease
Béraud, D., & Maguire‐Zeiss, K. A. (2011) · Parkinsonism & Related Disorders · doi:10.1016/s1353-8020(11)70008-6 · Cited by 135 · see citing works
Ganesan, S., Rathinam, V. A. K., Bossaller, L., Army, K., Kaiser, W. J., Mocarski, E. S., Dillon, C. P., Green, D. R., Mayadas, T. N., Levitz, S. M., et al. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1400276 · Cited by 131 · see citing works
Flagellin-induced NLRC4 phosphorylation primes the inflammasome for activation by NAIP5
Matusiak, M., Opdenbosch, N. V., Walle, L. V., Sirard, J., Kanneganti, T., & Lamkanfi, M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417945112 · Cited by 129 · see citing works
A Critical Role for Human Caspase-4 in Endotoxin Sensitivity
Kajiwara, Y., Schiff, T., Voloudakis, G., Sosa, M. A. G., Elder, G. A., Bozdagi, O., & Buxbaum, J. D. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1303424 · Cited by 119 · see citing works
Inflammasomes and Metabolic Disorders: Old Genes in Modern Diseases
Robbins, G. R., Wen, H., & Ting, J. P. ‐. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.029 · Cited by 114 · see citing works
Self-citationAn Update on PYRIN Domain-Containing Pattern Recognition Receptors: From Immunity to Pathology
Ratsimandresy, R. A., Dorfleutner, A., & Stehlik, C. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00440 · Cited by 109 · see citing works
de Nooijer, R., von der Thüsen, J. H., Verkleij, C. J. N., Kuiper, J., Jukema, J. W., van der Wall, E. E., van Berkel, T. J. C., & Biessen, E. A. L. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000147126.99529.0a · Cited by 97 · see citing works
Yin, Z., Deng, T., Peterson, L. E., Yu, R., Lin, J., Hamilton, D. J., Reardon, P. R., Sherman, V., Winnier, G. E., Zhan, M., et al. (2014) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2014.06.018 · Cited by 85 · see citing works
Dumas, A., Amiable, N., Vaccari, J. P. D. R., Chae, J. J., Keane, R. W., Lacroix, S., & Vallières, L. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004150 · Cited by 81 · see citing works
Huang, M. T.-H., Taxman, D. J., Holley-Guthrie, E., Moore, C. B., Willingham, S. B., Madden, V. J., Parsons, R. K., Featherstone, G. L., Arnold, R. R., O’Connor, B. P., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0800909 · Cited by 79 · see citing works
Self-citationRole of caspase-1 in regulation of triglyceride metabolism
Kotas, M. E., Jurczak, M. J., Annicelli, C., Gillum, M. P., Cline, G. W., Shulman, G. I., & Medzhitov, R. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301996110 · Cited by 76 · see citing works
Monie, T. P., & Bryant, C. E. (2015) · Immunological Reviews · doi:10.1111/imr.12284 · Cited by 73 · see citing works
Peelen, E., Damoiseaux, J., Muris, A., Knippenberg, S., Smolders, J., Hupperts, R., & Thewissen, M. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2014.10.008 · Cited by 66 · see citing works
Inhibition of IL-1β Improves Fatigue in Type 2 Diabetes
Cavelti‐Weder, C., Furrer, R., Keller, C., Babians-Brunner, A., Solinger, A. M., Gast, H., Fontana, A., Donath, M. Y., & Penner, I. (2011) · Diabetes Care · doi:10.2337/dc11-1196 · Cited by 64 · see citing works
The Cyclopentenone Prostaglandin 15d-PGJ2 Inhibits the NLRP1 and NLRP3 Inflammasomes
Maier, N. K., Leppla, S. H., & Moayeri, M. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1401611 · Cited by 62 · see citing works
Isakov, E., Weisman-Shomer, P., & Benhar, M. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.07.012 · Cited by 46 · see citing works
Hematopoietic IKBKE limits the chronicity of inflammasome priming and metaflammation
Patel, M. N., Bernard, W. G., Milev, N. B., Cawthorn, W. P., Figg, N. L., Hart, D., Prieur, X., Virtue, S., Hegyi, K., Bonnafous, S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414536112 · Cited by 42 · see citing works
Tan, H., Liu, X., Bi, X., Xing, S., Li, L., Gong, H., Zhong, M., Wang, Z., Zhang, Y., & Zhang, W. (2009) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2009.07.053 · Cited by 40 · see citing works
Obesity development in caspase-1-deficient mice
Wang, H., Capell, W. H., JiSun, Y. O. O. N., Faubel, S. G., & Eckel, R. H. (2013) · International Journal of Obesity · doi:10.1038/ijo.2013.59 · Cited by 32 · see citing works
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NF-κB signaling in inflammation
Liu, T., Zhang, L., Joo, D., & Sun, S.-C. (2017) · Signal Transduction and Targeted Therapy · doi:10.1038/sigtrans.2017.23 · Cited by 8,791 · see citing works
The NLRP3 inflammasome: molecular activation and regulation to therapeutics
Swanson, K. V., Deng, M., & Ting, J. P.-Y. (2019) · Nature Reviews Immunology · doi:10.1038/s41577-019-0165-0 · Cited by 4,884 · 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
Chemotherapy drugs induce pyroptosis through caspase-3 cleavage of a gasdermin
Wang, Y., Gao, W., Shi, X., Ding, J., Liu, W., He, H., Wang, K., & Shao, F. (2017) · Nature · doi:10.1038/nature22393 · Cited by 3,199 · see citing works
Inflammation in obesity, diabetes, and related disorders
Rohm, T. V., Meier, D. T., Olefsky, J. M., & Donath, M. Y. (2022) · Immunity · doi:10.1016/j.immuni.2021.12.013 · Cited by 2,066 · see citing works
Rogers, C., Fernandes-Alnemri, T., Mayes, L., Alnemri, D., Cingolani, G., & Alnemri, E. S. (2017) · Nature Communications · doi:10.1038/ncomms14128 · Cited by 1,510 · see citing works
“…treated DFNA5 þ / þ and DFNA5 (cid:2) / (cid:2) macrophages initiate the apoptotic programme with plasma membrane blebbing that progresses to plasma membrane swelling and ballooning (secondary necrosis) in DFNA5 þ / þ but not in DFNA5 (cid:2) / (cid:2) macrophages (Supplementary Videos 4 and 5).”
InfluentialRETRACTED ARTICLE: Parkin and PINK1 mitigate STING-induced inflammation
Sliter, D. A., Martinez, J., Hao, L., Chen, X., Sun, N., Fischer, T. D., Burman, J. L., Li, Y., Zhang, Z., Narendra, D. P., et al. (2018) · Nature · doi:10.1038/s41586-018-0448-9 · Cited by 1,287 · see citing works
RetractedNEK7 is an essential mediator of NLRP3 activation downstream of potassium efflux
He, Y., Zeng, M. Y., Yang, D., Motro, B., & Núñez, G. (2016) · Nature · doi:10.1038/nature16959 · Cited by 1,295 · see citing works
NLRP3 Inflammasome and the IL-1 Pathway in Atherosclerosis
Grebe, A., Hoss, F., & Latz, E. (2018) · Circulation Research · doi:10.1161/circresaha.118.311362 · Cited by 926 · see citing works
Akdis, M., Aab, A., Altunbulakli, C., Azkur, K., Costa, R. A., Crameri, R., Duan, S., Eiwegger, T., Eljaszewicz, A., Ferstl, R., et al. (2016) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2016.06.033 · Cited by 912 · see citing works
Lipotoxicity and the gut-liver axis in NASH pathogenesis
Marra, F., & Svegliati-Baroni, G. (2018) · Journal of Hepatology · doi:10.1016/j.jhep.2017.11.014 · Cited by 847 · see citing works
Bile Acids Control Inflammation and Metabolic Disorder through Inhibition of NLRP3 Inflammasome
Guo, C., Xie, S., Chi, Z., Zhang, J., Liu, Y., Zhang, L., Zheng, M., Zhang, X., Xia, D., Ke, Y., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.09.008 · Cited by 838 · 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
Integrating neuroimmune systems in the neurobiology of depression
Wohleb, E. S., Franklin, T., Iwata, M., & Duman, R. S. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.69 · Cited by 668 · see citing works
Hassamal, S. (2023) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2023.1130989 · Cited by 578 · see citing works
“Several PRRs, toll-like receptor-4 (TLR-4) and NLR family pyrin domain containing 3 (NLRP3), have been implicated in depression (47).”
BackgroundParkinson disease and the immune system - Associations, mechanisms and therapeutics
Tan, E.-K., Chao, Y.-X., West, A., Chan, L.-L., Poewe, W., & Jankovic, J. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-020-0344-4 · Cited by 457 · see citing works
Stancu, I.-C., Cremers, N., Vanrusselt, H., Couturier, J., Vanoosthuyse, A., Kessels, S., Lodder, C., Brône, B., Huaux, F., Octave, J.-N., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-018-01957-y · Cited by 447 · see citing works
He, M., Chiang, H.-H., Luo, H., Zheng, Z., Qiao, Q., Wang, L., Tan, M., Ohkubo, R., Mu, W.-C., Zhao, S., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.01.009 · Cited by 425 · see citing works
Han, X., Sun, S., Sun, Y., Song, Q., Zhu, J., Song, N., Chen, M., Sun, T., Xia, M., Ding, J., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1596481 · Cited by 408 · see citing works
NLR members NLRC4 and NLRP3 mediate sterile inflammasome activation in microglia and astrocytes
Freeman, L., Guo, H., David, C. N., Brickey, W. J., Jha, S., & Ting, J. P.-Y. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20150237 · Cited by 397 · see citing works
Self-citationTLR4 Cross-Talk With NLRP3 Inflammasome and Complement Signaling Pathways in Alzheimer's Disease
Yang, J., Wise, L., & Fukuchi, K.-I. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00724 · Cited by 387 · see citing works
The Immunomodulatory Functions of Butyrate
Siddiqui, M. T., & Cresci, G. A. (2021) · Journal of Inflammation Research · doi:10.2147/jir.s300989 · Cited by 381 · see citing works
Metal Drugs and the Anticancer Immune Response
Englinger, B., Pirker, C., Heffeter, P., Terenzi, A., Kowol, C. R., Keppler, B. K., & Berger, W. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00396 · Cited by 355 · see citing works
Autophagy and Microglia: Novel Partners in Neurodegeneration and Aging
Plaza-Zabala, A., Sierra-Torre, V., & Sierra, A. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18030598 · Cited by 323 · see citing works
Chen, Z., Zhong, H., Wei, J., Lin, S., Zong, Z., Gong, F., Huang, X., Sun, J., Li, P., Lin, H., et al. (2019) · Arthritis Research & Therapy · doi:10.1186/s13075-019-2085-6 · Cited by 275 · see citing works
Inflammatory osteolysis: A conspiracy against bone
Mbalaviele, G., Novack, D. V., Schett, G., & Teitelbaum, S. L. (2017) · Journal of Clinical Investigation · doi:10.1172/jci93356 · Cited by 251 · see citing works
Mehto, S., Jena, K. K., Nath, P., Chauhan, S., Kolapalli, S. P., Das, S. K., Sahoo, P. K., Jain, A., Taylor, G. A., & Chauhan, S. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.11.018 · Cited by 238 · see citing works
The microglial NLRP3 inflammasome is activated by amyotrophic lateral sclerosis proteins
Deora, V., Lee, J. D., Albornoz, E. A., McAlary, L., Jagaraj, C. J., Robertson, A. A. B., Atkin, J. D., Cooper, M. A., Schroder, K., Yerbury, J. J., et al. (2020) · Glia · doi:10.1002/glia.23728 · Cited by 245 · see citing works
Interactions Between the Gut Microbiota and the Host Innate Immune Response Against Pathogens
Cheng, H.-Y., Ning, M.-X., Chen, D.-K., & Ma, W.-T. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00607 · Cited by 244 · see citing works
Inflammasome Priming in Sterile Inflammatory Disease
Patel, M. N., Carroll, R. G., Galván-Peña, S., Mills, E. L., Olden, R., Triantafilou, M., Wolf, A. I., Bryant, C. E., Triantafilou, K., & Masters, S. L. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.12.007 · Cited by 241 · see citing works
Zirngibl, M., Assinck, P., Sizov, A., Caprariello, A. V., & Plemel, J. R. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00538-8 · Cited by 233 · see citing works
AIM2 inflammasome surveillance of DNA damage shapes neurodevelopment
Lammert, C. R., Frost, E. L., Bellinger, C. E., Bolte, A. C., McKee, C. A., Hurt, M. E., Paysour, M. J., Ennerfelt, H. E., & Lukens, J. R. (2020) · Nature · doi:10.1038/s41586-020-2174-3 · Cited by 223 · see citing works
Alzheimer’s disease as an inflammatory disease
Bolós, M., Perea, J. R., & Avila, J. (2017) · BioMolecular Concepts · doi:10.1515/bmc-2016-0029 · Cited by 216 · see citing works
Inflammasome and Autophagy Regulation: A Two-way Street
Sun, Q., Fan, J., Billiar, T. R., & Scott, M. J. (2017) · Molecular Medicine · doi:10.2119/molmed.2017.00077 · Cited by 203 · see citing works
Immune Surveillance of the CNS following Infection and Injury
Russo, M. V., & McGavern, D. B. (2015) · Trends in Immunology · doi:10.1016/j.it.2015.08.002 · Cited by 191 · see citing works
TREM2 dependent and independent functions of microglia in Alzheimer’s disease
Hou, J., Chen, Y., Grajales-Reyes, G., & Colonna, M. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00588-y · Cited by 191 · see citing works
Shi, Y., Su, W., Zhang, L., Shi, C., Zhou, J., Wang, P., Wang, H., Shi, X., Wei, S., Wang, Q., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.609060 · Cited by 177 · see citing works
The World Goes Bats: Living Longer and Tolerating Viruses
Gorbunova, V., Seluanov, A., & Kennedy, B. K. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.06.013 · Cited by 162 · see citing works
Cheng, Y., Pardo, M., Armini, R. D. S., Martinez, A., Mouhsine, H., Zagury, J.-F., Jope, R. S., & Beurel, E. (2016) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2015.12.012 · Cited by 174 · see citing works
The P2X7 Receptor-Interleukin-1 Liaison
Giuliani, A. L., Sarti, A. C., Falzoni, S., & Di Virgilio, F. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00123 · Cited by 166 · see citing works
Liu, Z., Ma, X., Ilyas, I., Zheng, X., Luo, S., Little, P. J., Kamato, D., Sahebkar, A., Wu, W., Weng, J., et al. (2021) · Theranostics · doi:10.7150/thno.54498 · Cited by 155 · see citing works
Development of an in vitro human liver system for interrogating nonalcoholic steatohepatitis
Feaver, R. E., Cole, B. K., Lawson, M. J., Hoang, S. A., Marukian, S., Blackman, B. R., Figler, R. A., Sanyal, A. J., Wamhoff, B. R., & Dash, A. (2016) · JCI Insight · doi:10.1172/jci.insight.90954 · Cited by 153 · see citing works
NF-κB: a double-edged sword controlling inflammation
Liu, D., Zhong, Z., & Karin, M. (2022) · Biomedicines · doi:10.3390/biomedicines10061250 · Cited by 157 · see citing works
Luo, H., Mu, W.-C., Karki, R., Chiang, H.-H., Mohrin, M., Shin, J. J., Ohkubo, R., Ito, K., Kanneganti, T.-D., & Chen, D. (2019) · Cell Reports · doi:10.1016/j.celrep.2018.12.101 · Cited by 161 · see citing works
The P2X7 Receptor Primes IL-1β and the NLRP3 Inflammasome in Astrocytes Exposed to Mechanical Strain
Albalawi, F., Lu, W., Beckel, J. M., Lim, J. C., McCaughey, S. A., & Mitchell, C. H. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00227 · Cited by 155 · see citing works
Immune System: An Emerging Player in Mediating Effects of Endocrine Disruptors on Metabolic Health
Bansal, A., Henao-Mejia, J., & Simmons, R. A. (2018) · Endocrinology · doi:10.1210/en.2017-00882 · Cited by 152 · see citing works
AIM2 inflammasome is activated by pharmacological disruption of nuclear envelope integrity
Di Micco, A., Frera, G., Lugrin, J., Jamilloux, Y., Hsu, E.-T., Tardivel, A., De Gassart, A., Zaffalon, L., Bujisic, B., Siegert, S., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1602419113 · Cited by 143 · see citing works
Activation of the <scp>NLRP</scp>3 inflammasome in microglia: the role of ceramide
Scheiblich, H., Schlütter, A., Golenbock, D. T., Latz, E., Martinez‐Martinez, P., & Heneka, M. T. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14225 · Cited by 147 · see citing works
Diet in Parkinson’s Disease: Critical Role for the Microbiome
Jackson, A., Forsyth, C. B., Shaikh, M., Voigt, R. M., Engen, P. A., Ramirez, V., & Keshavarzian, A. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.01245 · Cited by 145 · see citing works
The Microbiota-Inflammasome Hypothesis of Major Depression
Inserra, A., Rogers, G. B., Licinio, J., & Wong, M. (2018) · BioEssays · doi:10.1002/bies.201800027 · Cited by 134 · see citing works
Mitochondria as a centrally positioned hub in the innate immune response
Sandhir, R., Halder, A., & Sunkaria, A. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.10.020 · Cited by 135 · see citing works
Fatty acid activates NLRP3 inflammasomes in mouse Kupffer cells through mitochondrial DNA release
Pan, J., Ou, Z., Cai, C., Li, P., Gong, J., Ruan, X. Z., & He, K. (2018) · Cellular Immunology · doi:10.1016/j.cellimm.2018.08.006 · Cited by 132 · see citing works
Neuroinflammation as an etiological trigger for depression comorbid with inflammatory bowel disease
Craig, C. F., Filippone, R. T., Stavely, R., Bornstein, J. C., Apostolopoulos, V., & Nurgali, K. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02354-1 · Cited by 124 · see citing works
Scheiblich, H., Bousset, L., Schwartz, S., Griep, A., Latz, E., Melki, R., & Heneka, M. T. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2100035 · Cited by 122 · see citing works
Alzheimer’s Disease and Inflammaging
Kosyreva, A., Sentyabreva, A., Tsvetkov, I., & Makarova, O. (2022) · Brain Sciences · doi:10.3390/brainsci12091237 · Cited by 98 · see citing works
Chiang, C.-Y., Uzoma, I., Moore, R. T., Gilbert, M., Duplantier, A. J., & Panchal, R. G. (2018) · mBio · doi:10.1128/mbio.01932-17 · Cited by 95 · see citing works
Gómez, X., Sanon, S., Zambrano, K., Asquel, S., Bassantes, M., Morales, J. E., Otáñez, G., Pomaquero, C., Villarroel, S., Zurita, A., et al. (2021) · npj Microgravity · doi:10.1038/s41526-021-00162-8 · Cited by 92 · see citing works
Autophagy in Pulmonary Diseases
Nakahira, K., Pabon Porras, M. A., & Choi, A. M. K. (2016) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201512-2468so · Cited by 78 · see citing works
Lopategi, A., Flores-Costa, R., Rius, B., López-Vicario, C., Alcaraz-Quiles, J., Titos, E., & Clària, J. (2018) · Journal of Leukocyte Biology · doi:10.1002/jlb.3hi0517-206rr · Cited by 87 · see citing works
Pierantonelli, I., Rychlicki, C., Agostinelli, L., Giordano, D. M., Gaggini, M., Fraumene, C., Saponaro, C., Manghina, V., Sartini, L., Mingarelli, E., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-11744-6 · Cited by 82 · see citing works
Debye, B., Schmülling, L., Zhou, L., Rune, G., Beyer, C., & Johann, S. (2018) · Brain Pathology · doi:10.1111/bpa.12467 · Cited by 81 · see citing works
Structural basis for the oligomerization-facilitated NLRP3 activation
Yu, X., Matico, R. E., Miller, R., Chauhan, D., Van Schoubroeck, B., Grauwen, K., Suarez, J., Pietrak, B., Haloi, N., Yin, Y., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45396-8 · Cited by 78 · see citing works
Downregulation of the NLRP3 inflammasome by adiponectin rescues Duchenne muscular dystrophy
Boursereau, R., Abou-Samra, M., Lecompte, S., Noel, L., & Brichard, S. M. (2018) · BMC Biology · doi:10.1186/s12915-018-0501-z · Cited by 72 · see citing works
Macrophages in metabolic associated fatty liver disease
Alharthi, J., Latchoumanin, O., George, J., & Eslam, M. (2020) · World Journal of Gastroenterology · doi:10.3748/wjg.v26.i16.1861 · Cited by 65 · see citing works
Adipose tissue aging is regulated by an altered immune system
Zhang, Y.-X., Ou, M.-Y., Yang, Z.-H., Sun, Y., Li, Q.-F., & Zhou, S.-B. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1125395 · Cited by 62 · see citing works
Analysis of extracellular vesicles generated from monocytes under conditions of lytic cell death
Baxter, A. A., Phan, T. K., Hanssen, E., Liem, M., Hulett, M. D., Mathivanan, S., & Poon, I. K. H. (2019) · Scientific Reports · doi:10.1038/s41598-019-44021-9 · Cited by 60 · see citing works
Therapeutic Role of Inflammasome Inhibitors in Neurodegenerative Disorders
Lahooti, B., Chhibber, T., Bagchi, S., Varahachalam, S. P., & Jayant, R. D. (2021) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2020.11.004 · Cited by 50 · see citing works
Li, F., Ayaki, T., Maki, T., Sawamoto, N., & Takahashi, R. (2018) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nly090 · Cited by 44 · see citing works
Zhong, X., Xie, L., Yang, X., Liang, F., Yang, Y., Tong, J., Zhong, Y., Zhao, K., Tang, Y., & Yuan, C. (2020) · Molecular Medicine · doi:10.1186/s10020-020-00181-3 · Cited by 42 · see citing works
Tyagi, P., Tasleem, M., Prakash, S., & Chouhan, G. (2020) · Food Research International · doi:10.1016/j.foodres.2020.109489 · Cited by 42 · see citing works
High-fat diet exacerbates imiquimod-induced psoriasis-like dermatitis in mice
Higashi, Y., Yamakuchi, M., Fukushige, T., Ibusuki, A., Hashiguchi, T., & Kanekura, T. (2018) · Experimental Dermatology · doi:10.1111/exd.13484 · Cited by 39 · see citing works
Nutrient excess and autophagic deficiency: explaining metabolic diseases in obesity
van Niekerk, G., du Toit, A., Loos, B., & Engelbrecht, A.-M. (2018) · Metabolism · doi:10.1016/j.metabol.2017.12.007 · Cited by 34 · see citing works
Increased inflammasome activity in markedly ill psychiatric patients: an explorative study
Hylén, U., Eklund, D., Humble, M., Bartoszek, J., Särndahl, E., & Bejerot, S. (2020) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2019.577119 · Cited by 32 · see citing works
Ding, Y., & Xu, X. (2021) · Journal of Sports Sciences · doi:10.1080/02640414.2021.1932279 · Cited by 30 · see citing works
Xie, B., Lu, C., Chen, C., Zhou, J., & Deng, Z. (2020) · Mediators of Inflammation · doi:10.1155/2020/1231243 · Cited by 25 · see citing works
Pollock, N. M., Fernandes, J. P., Woodfield, J., Moussa, E., Hlavay, B., Branton, W. G., Wuest, M., Mohammadzadeh, N., Schmitt, L., Plemel, J. R., et al. (2024) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2023.10.022 · Cited by 21 · see citing works
NLRP3 inflammasome: common nexus between depression and cardiovascular diseases
Alcocer-Gómez, E., & Cordero, M. D. (2017) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2016.214 · Cited by 20 · see citing works
Kalkman, H. O. (2023) · Biomedicines · doi:10.3390/biomedicines11030806 · Cited by 18 · see citing works
Yao, H., Yan, J., Yin, L., & Chen, W. (2022) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923973.2022.2054425 · Cited by 17 · see citing works
Zhang, Z., Qiu, X., Zeng, X., Liu, X., Lu, J., Xu, C., Huang, J., Zhao, C., & Zhan, Y. (2025) · Scientific Reports · doi:10.1038/s41598-025-18650-2 · Cited by 6 · see citing works
- Authors
- Guo, H., Callaway, J. B., & Ting, J. P.-Y.
- Affiliations
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Ting, Jenny P-Y
- Venue
- Nature Medicine
- Published
- 2015-06-29
- Volume
- 21
- Issue
- 7
- Pages
- 677-687
- ISSN
- 1078-8956 (ISSN-L)
- 1546-170X
- PMC
- PMC4519035
- OpenAlex
- W1561041814
- Cited by
- 3,340
- References
- 146
- Citations by year
- 2026: 228 · 2025: 270 · 2024: 351 · 2023: 343 · 2022: 377 · 2021: 392 · 2020: 341 · 2019: 277 · 2018: 291 · 2017: 270 · 2016: 165 · 2015: 32 · 2013: 1
- FWCI
- 24.29
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
- UNC Libraries
- Funders
- National Multiple Sclerosis Society
- National Institutes of Health
- National Cancer Institute (R01CA156330, CA156330)
- National Institute of Allergy and Infectious Diseases (R37AI029564)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Keywords
- inflammasome, caspase-1 activation, innate immunity, inflammatory diseases, metabolic disorders, neurodegenerative diseases
- MeSH terms
- Animals, Disease, Disease Models, Animal, Humans, Inflammation, Models, Immunological, Inflammasomes, Molecular Targeted Therapy
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