Critical role for NALP3/CIAS1/Cryopyrin in innate and adaptive immunity through its regulation of caspase-1

The Inflammasome

Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066 · see citing works

IL-33, an Interleukin-1-like Cytokine that Signals via the IL-1 Receptor-Related Protein ST2 and Induces T Helper Type 2-Associated Cytokines

Schmitz, J., Owyang, A. M., Oldham, E. R., Song, Y., Murphy, E., McClanahan, T. K., Zurawski, G., Moshrefi, M., Qin, J., Li, X., et al. (2005) · Immunity · doi:10.1016/j.immuni.2005.09.015 · Cited by 3,701 · see citing works

Nod2 Is a General Sensor of Peptidoglycan through Muramyl Dipeptide (MDP) Detection

Girardin, S. E., Boneca, I. G., Viala, J., Chamaillard, M., Labigne-Roussel, A., Thomas, G. D., Philpott, D. J., & Sansonetti, P. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200651200 · Cited by 2,397 · see citing works

Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf

Mariathasan, S., Newton, K., Monack, D. M., Vucic, D., French, D. M., Lee, W. P., Roose-Girma, M., Erickson, S. L., & Dixit, V. M. (2004) · Nature · doi:10.1038/nature02664 · Cited by 1,822 · see citing works

NALP3 Forms an IL-1β-Processing Inflammasome with Increased Activity in Muckle-Wells Autoinflammatory Disorder

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

Host Recognition of Bacterial Muramyl Dipeptide Mediated through NOD2

Inohara, N., Ogura, Y., Fontalba, A., Gutierrez, O., Pons, F., Crespo, J., Fukase, K., Inamura, S., Kusumoto, S., Hashimoto, M., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200673200 · Cited by 1,694 · see citing works

Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle–Wells syndrome

Hoffman, H. M., Mueller, J. L., Broide, D. H., Wanderer, A. A., & Kolodner, R. D. (2001) · Nature Genetics · doi:10.1038/ng756 · Cited by 1,679 · 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

Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock

Li, P., Allen, H., Banerjee, S., Franklin, S., Herzog, L., Johnston, C. G., McDowell, J., Paskind, M. P., Rodman, L., Salfeld, J. G., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90490-5 · Cited by 1,408 · see citing works

NOD-LRR PROTEINS: Role in Host-Microbial Interactions and Inflammatory Disease

Inohara, N., Chamaillard, M., McDonald, C., & Núñez, G. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133347 · Cited by 993 · see citing works

Altered Cytokine Production in Mice Lacking P2X7Receptors

Solle, M., Labasi, J. M., Perregaux, D. G., Stam, E. J., Petrushova, N., Koller, B. H., Griffiths, R., & Gabel, C. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006781200 · Cited by 924 · see citing works

The Salmonella invasin SipB induces macrophage apoptosis by binding to caspase-1

Hersh, D., Monack, D. M., Smith, M. R., Ghori, N., Falkow, S., & Zychlinsky, A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2396 · Cited by 788 · see citing works

Interleukin-1 beta maturation and release in response to ATP and nigericin. Evidence that potassium depletion mediated by these agents is a necessary and common feature of their activity.

Perregaux, D. G., & Gabel, C. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36591-2 · Cited by 760 · see citing works

Chronic Infantile Neurological Cutaneous and Articular Syndrome Is Caused by Mutations in CIAS1, a Gene Highly Expressed in Polymorphonuclear Cells and Chondrocytes

Feldmann, J., Prieur, A., Quartier, P., Berquin, P. C., Dogniaux, S., Cortis, E., Hamel‐Teillac, D., Fischer, A., & Basile, G. D. S. (2002) · The American Journal of Human Genetics · doi:10.1086/341357 · Cited by 737 · see citing works

NLRs join TLRs as innate sensors of pathogens

Martinon, F., & Tschopp, J. (2005) · Trends in Immunology · doi:10.1016/j.it.2005.06.004 · Cited by 673 · see citing works

Interleukin-1–Receptor Antagonist in the Muckle–Wells Syndrome

Hawkins, P. N., Lachmann, H. J., & McDermott, M. F. (2003) · New England Journal of Medicine · doi:10.1056/nejm200306193482523 · Cited by 654 · see citing works

Identification of Bacterial Muramyl Dipeptide as Activator of the NALP3/Cryopyrin Inflammasome

Martinon, F., Agostini, L., Meylan, E., & Tschopp, J. (2004) · Current Biology · doi:10.1016/j.cub.2004.10.027 · Cited by 579 · 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

Prevention of cold-associated acute inflammation in familial cold autoinflammatory syndrome by interleukin-1 receptor antagonist

Hoffman, H. M., Rosengren, S., Boyle, D. L., Cho, J. Y., Nayar, J., Mueller, J. L., Anderson, J. P., Wanderer, A. A., & Firestein, G. S. (2004) · The Lancet · doi:10.1016/s0140-6736(04)17401-1 · Cited by 552 · see citing works

ASC, a Novel 22-kDa Protein, Aggregates during Apoptosis of Human Promyelocytic Leukemia HL-60 Cells

Masumoto, J., Taniguchi, S., Ayukawa, K., Sarvotham, H., Kishino, T., Niikawa, N., Hidaka, E., Katsuyama, T., Higuchi, T., & Sagara, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.48.33835 · Cited by 542 · see citing works

Interleukin‐1β, Interleukin‐18, and the Interleukin‐1β Converting Enzymea

Dinarello, C. A. (1998) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1998.tb08307.x · Cited by 497 · see citing works

An essential role for Langerhans cell-derived IL-1 beta in the initiation of primary immune responses in skin

Enk, A., Angeloni, V. L., Udey, M. C., & Katz, S. I. (1993) · The Journal of Immunology · doi:10.4049/jimmunol.150.9.3698 · Cited by 423 · see citing works

Salmonella spp. are cytotoxic for cultured macrophages

Chen, L.-M., Kaniga, K., & Galán, J. E. (1996) · Molecular Microbiology · doi:10.1046/j.1365-2958.1996.471410.x · Cited by 379 · see citing works

PYPAF7, a Novel PYRIN-containing Apaf1-like Protein That Regulates Activation of NF-κB and Caspase-1-dependent Cytokine Processing

Wang, L., Manji, G. A., Grenier, J. M., Al-Garawi, A. A., Merriam, S., Lora, J. M., Geddes, B. J., Briskin, M., DiStefano, P. S., & Bertin, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203915200 · Cited by 371 · see citing works

Selective Suppression of Interleukin-12 Induction after Macrophage Receptor Ligation

Sutterwala, F. S., Noel, G. J., Clynes, R., & Mosser, D. M. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.185.11.1977 · Cited by 351 · see citing works

CATERPILLER: A Novel Gene Family Important in Immunity, Cell Death, and Diseases

Ting, J. P.-Y., & Davis, B. K. (2004) · Annual Review of Immunology · doi:10.1146/annurev.immunol.23.021704.115616 · Cited by 349 · see citing works

The Salmonella typhimurium invasion genes invF and invG encode homologues of the AraC and PulD family of proteins

Kaniga, K., Bossio, J. C., & Galán, J. E. (1994) · Molecular Microbiology · doi:10.1111/j.1365-2958.1994.tb00450.x · Cited by 322 · see citing works

New Mutations of CIAS1 That Are Responsible for Muckle-Wells Syndrome and Familial Cold Urticaria: A Novel Mutation Underlies Both Syndromes

Dodé, C., Dû, N. L., Cuisset, L., Letourneur, F., Berthelot, J., Vaudour, G., Meyrier, A. Y., Watts, R. A., Scott, G. I. D., Nicholls, A., et al. (2002) · The American Journal of Human Genetics · doi:10.1086/340786 · Cited by 303 · see citing works

PYPAF1, a PYRIN-containing Apaf1-like Protein That Assembles with ASC and Regulates Activation of NF-κB

Manji, G. A., Wang, L., Geddes, B. J., Brown, M., Merriam, S., Al-Garawi, A. A., Mak, S., Lora, J. M., Briskin, M., Jurman, M. E., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112208200 · Cited by 275 · see citing works

The relationship of IL-4- and IFNγ-producing T cells studied by lineage ablation of IL-4-producing cells

Kamogawa, Y., Minasi, L. A. E., Carding, S. R., Bottomly, K., & Flavell, R. A. (1993) · Cell · doi:10.1016/0092-8674(93)90542-x · Cited by 257 · see citing works

TMS1, a novel proapoptotic caspase recruitment domain protein, is a target of methylation-induced gene silencing in human breast cancers.

Conway, K. E., McConnell, B. B., Bowring, C. E., Donald, C. D., Warren, S. T., & Vertino, P. M. (2000) · PubMed · Cited by 249 · see citing works

Apoptosis-Associated Speck-Like Protein Containing a Caspase Recruitment Domain Is a Regulator of Procaspase-1 Activation

Stehlik, C., Lee, S. H., Dorfleutner, A., Stassinopoulos, A., Sagara, J., & Reed, J. C. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.11.6154 · Cited by 238 · see citing works

Mice deficient in IL-1beta manifest impaired contact hypersensitivity to trinitrochlorobenzone.

Shornick, L. P., Togni, P. D., Mariathasan, S., Goellner, J. J., Strauss‐Schoenberger, J., Karr, R. W., Ferguson, T. A., & Chaplin, D. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.183.4.1427 · Cited by 237 · see citing works

Cryopyrin-induced Interleukin 1β Secretion in Monocytic Cells

Dowds, T. A., Masumoto, J., Li, Z., Inohara, N., & Núñez, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401178200 · Cited by 235 · see citing works

Cutting Edge: CIAS1/Cryopyrin/PYPAF1/NALP3/ CATERPILLER 1.1 Is an Inducible Inflammatory Mediator with NF-κB Suppressive Properties

O’Connor, W., Harton, J. A., Zhu, X., Linhoff, M. W., & Ting, J. P. ‐. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.12.6329 · Cited by 195 · see citing works

ASC is essential for LPS‐induced activation of procaspase‐1 independently of TLR‐associated signal adaptor molecules

Yamamoto, M., Yaginuma, K., Tsutsui, H., Sagara, J., Guan, X., Seki, E., Yasuda, K., Yamamoto, M., Akira, S., Nakanishi, K., et al. (2004) · Genes to Cells · doi:10.1111/j.1365-2443.2004.00789.x · Cited by 184 · see citing works

Salmonella pathogenicity island 2-dependent macrophage death is mediated in part by the host cysteine protease caspase-1

Monack, D. M., Detweiler, C. S., & Falkow, S. (2001) · Cellular Microbiology · doi:10.1046/j.1462-5822.2001.00162.x · Cited by 137 · see citing works

Salmonella-induced macrophage death: multiple mechanisms, different outcomes

Hueffer, K., & Galán, J. E. (2004) · Cellular Microbiology · doi:10.1111/j.1462-5822.2004.00451.x · Cited by 92 · see citing works

Increased Mature Interleukin-1β (IL-1β) Secretion from THP-1 Cells Induced by Nigericin Is a Result of Activation of p45 IL-1β-converting Enzyme Processing

Cheneval, D., Ramage, P., Kastelic, T., Szelestenyi, T., Niggli, H., Hemmig, R., Bachmann, M. F., & MacKenzie, A. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.28.17846 · Cited by 78 · see citing works

Structural, expression, and evolutionary analysis of mouse CIAS1

Anderson, J. P., Mueller, J. L., Rosengren, S., Boyle, D. L., Schaner, P. E., Cannon, S. B., Goodyear, C. S., & Hoffman, H. M. (2004) · Gene · doi:10.1016/j.gene.2004.05.002 · Cited by 55 · see citing works

The Inflammasomes

Schroder, K., & Tschopp, J. (2010) · Cell · doi:10.1016/j.cell.2010.01.040 · Cited by 5,475 · see citing works

Reactive Oxygen Species in Inflammation and Tissue Injury

Mittal, M., Siddiqui, M. R., Tran, K., Reddy, S. P., & Malik, A. B. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5149 · Cited by 4,897 · see citing works

Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome

Nakahira, K., Haspel, J. A., Rathinam, V. A. K., Lee, S.-J., Dolinay, T., Lam, H. C., Englert, J. A., Rabinovitch, M., Cernadas, M., Kim, H. P., et al. (2011) · Nature Immunology · doi:10.1038/ni.1980 · Cited by 3,049 · see citing works

Caspase 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

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

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

Inflammasome-mediated dysbiosis regulates progression of NAFLD and obesity

Henao-Mejia, J., Elinav, E., Jin, C., Hao, L., Mehal, W. Z., Strowig, T., Thaiss, C. A., Kau, A. L., Eisenbarth, S. C., Jurczak, M. J., et al. (2012) · Nature · doi:10.1038/nature10809 · Cited by 2,435 · see citing works

Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis

Shimada, K., Crother, T. R., Karlin, J., Dagvadorj, J., Chiba, N., Chen, S., Ramanujan, V. K., Wolf, A. J., Vergnes, L., Ojcius, D. M., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.009 · Cited by 2,282 · see citing works

Overview of the immune response

Chaplin, D. D. (2010) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2009.12.980 · Cited by 2,235 · see citing works

NLRP6 Inflammasome Regulates Colonic Microbial Ecology and Risk for Colitis

Elinav, E., Strowig, T., Kau, A. L., Henao-Mejia, J., Thaiss, C. A., Booth, C. J., Peaper, D. R., Bertin, J., Eisenbarth, S. C., Gordon, J. I., et al. (2011) · Cell · doi:10.1016/j.cell.2011.04.022 · Cited by 2,024 · see citing works

Activation of the NLRP3 inflammasome in dendritic cells induces IL-1β–dependent adaptive immunity against tumors

Ghiringhelli, F., Apetoh, L., Tesniere, A., Aymeric, L., Ma, Y., Ortiz, C., Vermaelen, K., Panaretakis, T., Mignot, G., Ullrich, E., et al. (2009) · Nature Medicine · doi:10.1038/nm.2028 · Cited by 1,898 · 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

The inflammasome: a caspase-1-activation platform that regulates immune responses and disease pathogenesis

Franchi, L., Eigenbrod, T., Muñoz-Planillo, R., & Nuñez, G. (2009) · Nature Immunology · doi:10.1038/ni.1703 · Cited by 1,834 · 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

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

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

Crucial role for the Nalp3 inflammasome in the immunostimulatory properties of aluminium adjuvants

Eisenbarth, S. C., Colegio, O. R., O’Connor, W., Sutterwala, F. S., & Flavell, R. A. (2008) · Nature · doi:10.1038/nature06939 · Cited by 1,542 · see citing works

Transkingdom Control of Microbiota Diurnal Oscillations Promotes Metabolic Homeostasis

Thaiss, C. A., Zeevi, D., Levy, M., Zilberman-Schapira, G., Suez, J., Tengeler, A. C., Abramson, L., Katz, M. N., Korem, T., Zmora, N., et al. (2014) · Cell · doi:10.1016/j.cell.2014.09.048 · Cited by 1,449 · see citing works

Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration

Pétrilli, V, Papin, S., Dostert, C., Mayor, A., Martinon, F., & Tschopp, J. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402195 · Cited by 1,445 · see citing works

Pannexin‐1 mediates large pore formation and interleukin‐1β release by the ATP‐gated P2X7 receptor

Pelegrı́n, P., & Surprenant, A. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601378 · Cited by 1,428 · see citing works

Activation of autophagy by inflammatory signals limits IL-1β production by targeting ubiquitinated inflammasomes for destruction

Shi, C.-S., Shenderov, K., Huang, N.-N., Kabat, J., Abu-Asab, M., Fitzgerald, K. A., Sher, A., & Kehrl, J. H. (2012) · Nature Immunology · doi:10.1038/ni.2215 · Cited by 1,367 · see citing works

Cooperation of Toll-like receptor signals in innate immune defence

Trinchieri, G., & Sher, A. (2007) · Nature reviews. Immunology · doi:10.1038/nri2038 · Cited by 1,357 · see citing works

NEK7 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

Reactive oxygen species and mitochondria: A nexus of cellular homeostasis

Dunn, J. D., Álvarez, L., Zhang, X., & Soldati, T. (2015) · Redox Biology · doi:10.1016/j.redox.2015.09.005 · Cited by 1,199 · see citing works

Intracellular pattern recognition receptors in the host response

Meylan, E., Tschopp, J., & Karin, M. (2006) · Nature · doi:10.1038/nature04946 · Cited by 1,196 · see citing works

Caspase‐1‐induced pyroptotic cell death

Miao, E. A., Rajan, J. V., & Aderem, A. A. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01044.x · Cited by 1,139 · see citing works

The NLRP3 Inflammasome Mediates In Vivo Innate Immunity to Influenza A Virus through Recognition of Viral RNA

Allen, I. C., Scull, M. A., Moore, C. B., Holl, E. K., McElvania-TeKippe, E., Taxman, D. J., Guthrie, E. H., Pickles, R. J., & Ting, J. P.-Y. (2009) · Immunity · doi:10.1016/j.immuni.2009.02.005 · Cited by 1,113 · see citing works

Chronic inflammation: importance of NOD2 and NALP3 in interleukin-1β generation

Ferrero‐Miliani, L., Nielsen, O. H., Andersen, P. S., & Girardin, S. E. (2006) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2006.03261.x · Cited by 1,102 · 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

Intracellular NOD-like Receptors in Host Defense and Disease

Kanneganti, T., Lamkanfi, M., & Núñez, G. (2007) · Immunity · doi:10.1016/j.immuni.2007.10.002 · Cited by 1,056 · see citing works

The pyroptosome: a supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation

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

The NLRP3 inflammasome protects against loss of epithelial integrity and mortality during experimental colitis

Zaki, M. H., Boyd, K. L., Vogel, P., Kastan, M. B., Lamkanfi, M., & Kanneganti, T.-D. (2010) · Immunity · doi:10.1016/j.immuni.2010.03.003 · Cited by 989 · see citing works

Microbiota-modulated metabolites shape the intestinal microenvironment by regulating NLRP6 inflammasome signaling

Levy, M., Thaiss, C. A., Zeevi, D., Dohnalová, L., Zilberman-Schapira, G., Mahdi, J. A., David, E., Savidor, A., Korem, T., Herzig, Y., et al. (2015) · Cell · doi:10.1016/j.cell.2015.10.048 · Cited by 960 · see citing works

NADPH oxidases: An overview from structure to innate immunity-associated pathologies

Panday, A., Sahoo, M. K., Osorio, D., & Batra, S. (2015) · Cellular & Molecular Immunology · doi:10.1038/cmi.2014.89 · Cited by 944 · see citing works

Mitochondrial Cardiolipin Is Required for Nlrp3 Inflammasome Activation

Iyer, S. S., He, Q., Janczy, J. R., Elliott, E. I., Zhong, Z., Olivier, A. K., Sadler, J. J., Knepper-Adrian, V., Han, R., Qiao, L., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.08.001 · Cited by 939 · 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

IL‐1, IL‐18, and IL‐33 families of cytokines

Arend, W. P., Palmer, G., & Gabay, C. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00624.x · Cited by 912 · see citing works

The Nalp3 inflammasome is essential for the development of silicosis

Cassel, S. L., Eisenbarth, S. C., Iyer, S. S., Sadler, J. J., Colegio, O. R., Tephly, L. A., Carter, A. B., Rothman, P. B., Flavell, R. A., & Sutterwala, F. S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803933105 · Cited by 907 · see citing works

Function of Nod‐like receptors in microbial recognition and host defense

Franchi, L., Warner, N. E., Viani, K. L., & Núñez, G. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00734.x · Cited by 900 · see citing works

Nod-like proteins in immunity, inflammation and disease

Fritz, J. H., Ferrero, R. L., Philpott, D. J., & Girardin, S. E. (2006) · Nature Immunology · doi:10.1038/ni1412 · Cited by 889 · see citing works

Understanding the Holobiont: How Microbial Metabolites Affect Human Health and Shape the Immune System

Postler, T. S., & Ghosh, S. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.05.008 · Cited by 876 · 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

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

Active Caspase-1 Is a Regulator of Unconventional Protein Secretion

Keller, M., Rüegg, A., Werner, S., & Beer, H. (2008) · Cell · doi:10.1016/j.cell.2007.12.040 · Cited by 851 · see citing works

The NLRP3 inflammasome functions as a negative regulator of tumorigenesis during colitis-associated cancer

Allen, I. C., TeKippe, E. M., Woodford, R.-M. T., Uronis, J. M., Holl, E. K., Rogers, A. B., Herfarth, H. H., Jobin, C., & Ting, J. P.-Y. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20100050 · Cited by 826 · see citing works

Inflammatory caspases and inflammasomes: master switches of inflammation

Martinon, F., & Tschopp, J. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402038 · 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

Differential requirement for the activation of the inflammasome for processing and release of IL-1β in monocytes and macrophages

Netea, M. G., Nold‐Petry, C. A., Nold, M. F., Joosten, L. A. B., Opitz, B., van der Meer, J. H. M., van de Veerdonk, F. L., Ferwerda, G., Heinhuis, B., Devesa, I., et al. (2008) · Blood · doi:10.1182/blood-2008-03-146720 · Cited by 787 · 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

NOD-Like Receptors: Role in Innate Immunity and Inflammatory Disease

Chen, G., Shaw, M. H., Kim, Y., & Núñez, G. (2008) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092239 · Cited by 770 · see citing works

The Intracellular Sensor NLRP3 Mediates Key Innate and Healing Responses to Influenza A Virus via the Regulation of Caspase-1

Thomas, P. G., Dash, P., Aldridge, J. R., Ellebedy, A. H., Reynolds, C., Funk, A. J., Martin, W. J., Lamkanfi, M., Webby, R. J., Boyd, K. L., et al. (2009) · Immunity · doi:10.1016/j.immuni.2009.02.006 · Cited by 749 · see citing works

ZBP1 and TAK1: Master Regulators of NLRP3 Inflammasome/Pyroptosis, Apoptosis, and Necroptosis (PAN-optosis)

Malireddi, R. K. S., Kesavardhana, S., & Kanneganti, T. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00406 · Cited by 750 · see citing works

NLRP3 inflammasome: From a danger signal sensor to a regulatory node of oxidative stress and inflammatory diseases

Abderrazak, 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

Pattern recognition receptors and control of adaptive immunity

Palm, N. W., & Medzhitov, R. M. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00731.x · Cited by 724 · 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

NLRP6 Inflammasome Orchestrates the Colonic Host-Microbial Interface by Regulating Goblet Cell Mucus Secretion

Wlodarska, M., Thaiss, C. A., Nowarski, R., Henao-Mejia, J., Zhang, J.-P., Brown, E. M., Frankel, G., Levy, M., Katz, M. N., Philbrick, W. M., et al. (2014) · Cell · doi:10.1016/j.cell.2014.01.026 · Cited by 708 · see citing works

IL-22BP is regulated by the inflammasome and modulates tumorigenesis in the intestine

Huber, S., Gagliani, N., Zenewicz, L. A., Huber, F. J., Bosurgi, L., Hu, B., Hedl, M., Zhang, W. K., O’Connor, W., Murphy, A. J., et al. (2012) · Nature · doi:10.1038/nature11535 · Cited by 713 · see citing works

Critical Role for Cryopyrin/Nalp3 in Activation of Caspase-1 in Response to Viral Infection and Double-stranded RNA

Kanneganti, T., Body–Malapel, M., Amer, A. O., Park, J., Whitfield, J. R., Franchi, L., Taraporewala, Z. F., Miller, D. J., Patton, J. T., Inohara, N., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607594200 · Cited by 706 · see citing works

The inflammasome: a danger sensing complex triggering innate immunity

Pétrilli, V., Dostert, C., Muruve, D. A., & Tschopp, J. (2007) · Current Opinion in Immunology · doi:10.1016/j.coi.2007.09.002 · Cited by 700 · see citing works

Necrotic cells trigger a sterile inflammatory response through the Nlrp3 inflammasome

Iyer, S. S., Pulskens, W. P., Sadler, J. J., Butter, L. M., Teske, G. J., Ulland, T. K., Eisenbarth, S. C., Florquin, S., Flavell, R. A., Leemans, J. C., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908698106 · Cited by 691 · see citing works

Inflammasome recognition of influenza virus is essential for adaptive immune responses

Ichinohe, T., Lee, H. K., Ogura, Y., Flavell, R. A., & Iwasaki, A. (2009) · The Journal of Experimental Medicine · doi:10.1084/jem.20081667 · Cited by 682 · see citing works

NLRP3 Inflammasome and Inflammatory Bowel Disease

Yu, Z., & Zhang, H. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00276 · Cited by 660 · see citing works

Interleukin-17–producing innate lymphoid cells and the NLRP3 inflammasome facilitate obesity-associated airway hyperreactivity

Kim, H. Y., Lee, H. J., Chang, Y., Pichavant, M., Shore, S. A., Fitzgerald, K. A., Iwakura, Y., Israel, E., Bolger, K., Faul, J. L., et al. (2013) · Nature Medicine · doi:10.1038/nm.3423 · Cited by 639 · see citing works

Influenza virus activates inflammasomes via its intracellular M2 ion channel

Ichinohe, T., Pang, I. K., & Iwasaki, A. (2010) · Nature Immunology · doi:10.1038/ni.1861 · Cited by 632 · see citing works

Autophagy Links Inflammasomes to Atherosclerotic Progression

Razani, B., Feng, C., Coleman, T., Emanuel, R., Wen, H., Hwang, S., Ting, J. P., Virgin, H. W., Kastan, M. B., & Semenkovich, C. F. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.02.011 · Cited by 601 · see citing works

Macrophage activation by endogenous danger signals

Zhang, X., & Mosser, D. (2007) · The Journal of Pathology · doi:10.1002/path.2284 · Cited by 607 · see citing works

Acetaminophen-induced hepatotoxicity in mice is dependent on Tlr9 and the Nalp3 inflammasome

Imaeda, A. B., Watanabe, A., Sohail, M. A., Mahmood, S., Mohamadnejad, M., Sutterwala, F. S., Flavell, R. A., & Mehal, W. Z. (2009) · Journal of Clinical Investigation · doi:10.1172/jci35958 · Cited by 604 · see citing works

Inflammasome-regulated Cytokines Are Critical Mediators of Acute Lung Injury

Dolinay, T., Kim, Y. S., Howrylak, J. A., Hunninghake, G. M., An, C. H., Fredenburgh, L. E., Massaro, A. F., Rogers, A. J., Gazourian, L., Nakahira, K., et al. (2012) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201201-0003oc · Cited by 562 · see citing works

Nonclassical IL-1β Secretion Stimulated by P2X7 Receptors Is Dependent on Inflammasome Activation and Correlated with Exosome Release in Murine Macrophages

Qu, Y., Franchi, L., Nunez, G., & Dubyak, G. R. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.3.1913 · Cited by 563 · see citing works

The Inflammasome Mediates UVB-Induced Activation and Secretion of Interleukin-1β by Keratinocytes

Feldmeyer, L., Keller, M., Niklaus, G., Hohl, D., Werner, S., & Beer, H.-D. (2007) · Current Biology · doi:10.1016/j.cub.2007.05.074 · Cited by 544 · see citing works

Differential Regulation of Caspase-1 Activation, Pyroptosis, and Autophagy via Ipaf and ASC in Shigella-Infected Macrophages

Suzuki, T., Franchi, L., Toma, C., Ashida, H., Ogawa, M., Yoshikawa, Y., Mimuro, H., Inohara, N., Sasakawa, C., & Núñez, G. (2007) · PLoS Pathogens · doi:10.1371/journal.ppat.0030111 · Cited by 532 · see citing works

Inflammasome Components NALP 1 and 3 Show Distinct but Separate Expression Profiles in Human Tissues Suggesting a Site-specific Role in the Inflammatory Response

Kummer, J. A., Broekhuizen, R., Everett, H., Agostini, L., Kuijk, L., Martinon, F., Bruggen, R. V., & Tschopp, J. (2007) · Journal of Histochemistry &amp; Cytochemistry · doi:10.1369/jhc.6a7101.2006 · Cited by 531 · see citing works

A Method for the Acute and Rapid Degradation of Endogenous Proteins

Clift, D., McEwan, W. A., Labzin, L. I., Konieczny, V., Mogessie, B., James, L. C., & Schuh, M. (2017) · Cell · doi:10.1016/j.cell.2017.10.033 · Cited by 531 · see citing works

NLRP3 inflammasome activity is negatively controlled by miR-223

Bauernfeind, F., Rieger, A., Schildberg, F. A., Knolle, P. A., Schmid-Burgk, J. L., & Hornung, V. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1201516 · Cited by 463 · see citing works

IFI16 DNA Sensor Is Required for Death of Lymphoid CD4 T Cells Abortively Infected with HIV

Monroe, K. M., Yang, Z., Johnson, J. R., Geng, X., Doitsh, G., Krogan, N. J., & Greene, W. C. (2014) · Science · doi:10.1126/science.1243640 · Cited by 511 · see citing works

Pannexin-1-Mediated Recognition of Bacterial Molecules Activates the Cryopyrin Inflammasome Independent of Toll-like Receptor Signaling

Kanneganti, T., Lamkanfi, M., Kim, Y., Chen, G., Park, J., Franchi, L., Vandenabeele, P., & Núñez, G. (2007) · Immunity · doi:10.1016/j.immuni.2007.03.008 · Cited by 526 · see citing works

Early immune events in the induction of allergic contact dermatitis

Kaplan, D. H., Igyártó, B. Z., & Gaspari, A. A. (2012) · Nature reviews. Immunology · doi:10.1038/nri3150 · Cited by 517 · see citing works

Patterns of Pathogenesis: Discrimination of Pathogenic and Nonpathogenic Microbes by the Innate Immune System

Vance, R. E., Isberg, R. R., & Portnoy, D. A. (2009) · Cell Host & Microbe · doi:10.1016/j.chom.2009.06.007 · Cited by 512 · see citing works

Immune recognition of Pseudomonas aeruginosa mediated by the IPAF/NLRC4 inflammasome

Sutterwala, F. S., Mijares, L. A., Li, L., Ogura, Y., Kazmierczak, B. I., & Flavell, R. A. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20071239 · Cited by 509 · see citing works

Caspase-1 Activation of Lipid Metabolic Pathways in Response to Bacterial Pore-Forming Toxins Promotes Cell Survival

Gurcel, L., Abrami, L., Girardin, S. E., Tschopp, J., & van der Goot, F. G. (2006) · Cell · doi:10.1016/j.cell.2006.07.033 · Cited by 508 · see citing works

Cryopyrin/NALP3 binds ATP/dATP, is an ATPase, and requires ATP binding to mediate inflammatory signaling

Duncan, J. A., Bergstralh, D. T., Wang, Y., Willingham, S. B., Ye, Z., Zimmermann, A. G., & Ting, J. P.-Y. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611496104 · Cited by 503 · see citing works

Liaisons dangereuses: P2X7 and the inflammasome

Di Virgilio, F. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.07.002 · Cited by 493 · see citing works

NLRP3 Phosphorylation Is an Essential Priming Event for Inflammasome Activation

Song, N., Liu, Z.-S., Xue, W., Bai, Z., Wang, Q., Dai, J., Liu, X., Huang, Y.-J., Cai, H., Zhan, X., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.08.017 · Cited by 494 · see citing works

IL-1β Processing in Host Defense: Beyond the Inflammasomes

Netea, M. G., Simon, A., van de Veerdonk, F. L., Kullberg, B. J., van der Meer, J. W. M., & Joosten, L. A. B. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000661 · Cited by 496 · see citing works

NLRP3 inflammasome activation is required for fibrosis development in NAFLD

Wree, A., McGeough, M. D., Peña, C. A., Schlattjan, M., Li, H., Inzaugarat, M. E., Messer, K., Canbay, A., Hoffman, H. M., & Feldstein, A. E. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1170-1 · Cited by 486 · see citing works

Cutting Edge: Caspase-1 Independent IL-1β Production Is Critical for Host Resistance to Mycobacterium tuberculosis and Does Not Require TLR Signaling In Vivo

Mayer-Barber, K. D., Barber, D. L., Shenderov, K., White, S., Wilson, M. S., Cheever, A. W., Kugler, D. G., Hieny, S. E., Caspar, P., Núñez, G., et al. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0904189 · Cited by 472 · see citing works

The Inflammasome: First Line of the Immune Response to Cell Stress

Ogura, Y., Sutterwala, F. S., & Flavell, R. A. (2006) · Cell · doi:10.1016/j.cell.2006.08.002 · Cited by 474 · see citing works

Biglycan, a Danger Signal That Activates the NLRP3 Inflammasome via Toll-like and P2X Receptors

Bábelová, A., Moreth, K., Tsalastra, W., Zeng-Brouwers, J., Eickelberg, O., Young, M. F., Brückner, P., Pfeilschifter, J. M., Schaefer, R. M., Gröne, H., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014266 · Cited by 474 · see citing works

Gain-of-Function Pyrin Mutations Induce NLRP3 Protein-Independent Interleukin-1β Activation and Severe Autoinflammation in Mice

Chae, J. J., Cho, Y.-H., Lee, G., Cheng, J., Liu, P. P., Feigenbaum, L., Katz, S. I., & Kastner, D. L. (2011) · Immunity · doi:10.1016/j.immuni.2011.02.020 · Cited by 473 · see citing works

NLRP3 inflammasome in neurological diseases, from functions to therapies

Song, L., Pei, L., Yao, S., Wu, Y., & Shang, Y. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00063 · Cited by 467 · see citing works

Inflammasome-Dependent Release of the Alarmin HMGB1 in Endotoxemia

Lamkanfi, M., Sarkar, A., Walle, L. V., Vitari, A. C., Amer, A. O., Wewers, M. D., Tracey, K. J., Kanneganti, T., & Dixit, V. M. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000803 · Cited by 468 · see citing works

ATP is released by monocytes stimulated with pathogen-sensing receptor ligands and induces IL-1β and IL-18 secretion in an autocrine way

Piccini, A., Carta, S., Tassi, S., Lasigliè, D., Fossati, G., & Rubartelli, A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709684105 · Cited by 460 · see citing works

A 360° view of the inflammasome: Mechanisms of activation, cell death, and diseases

Barnett, K. C., Li, S., Liang, K., & Ting, J. P.-Y. (2023) · Cell · doi:10.1016/j.cell.2023.04.025 · Cited by 458 · see citing works

Manipulation of Host Cell Death Pathways during Microbial Infections

Lamkanfi, M., & Dixit, V. M. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.06.007 · Cited by 450 · see citing works

The Nlrp3 inflammasome is critical for aluminium hydroxide‐mediated IL‐1β secretion but dispensable for adjuvant activity

Franchi, L., & Núñez, G. (2008) · European Journal of Immunology · doi:10.1002/eji.200838549 · Cited by 452 · see citing works

Uric acid as a danger signal in gout and its comorbidities

Rock, K. L., Kataoka, H., & Lai, J. (2012) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2012.143 · Cited by 453 · see citing works

Molecular Mechanism of NLRP3 Inflammasome Activation

Jin, C., & Flavell, R. A. (2010) · Journal of Clinical Immunology · doi:10.1007/s10875-010-9440-3 · Cited by 440 · see citing works

A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses

Mayor, A., Martinon, F., Smedt, T. D., Pétrilli, V., & Tschopp, J. (2007) · Nature Immunology · doi:10.1038/ni1459 · Cited by 438 · see citing works

Staphylococcus aureus α-Hemolysin Activates the NLRP3-Inflammasome in Human and Mouse Monocytic Cells

Craven, R. R., Gao, X., Allen, I. C., Gris, D., Wardenburg, J. B., McElvania, E., Ting, J. P. ‐., & Duncan, J. A. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007446 · Cited by 433 · see citing works

NALP3: a key player in caspase-1 activation

Sutterwala, F. S., Ogura, Y., Zamboni, D. S., Roy, C. R., & Flavell, R. A. (2006) · Journal of Endotoxin Research · doi:10.1177/09680519060120040701 · Cited by 84 · see citing works

NALP3 Forms an IL-1β-Processing Inflammasome with Increased Activity in Muckle-Wells Autoinflammatory Disorder

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

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

Inflammasome Components NALP 1 and 3 Show Distinct but Separate Expression Profiles in Human Tissues Suggesting a Site-specific Role in the Inflammatory Response

Kummer, J. A., Broekhuizen, R., Everett, H., Agostini, L., Kuijk, L., Martinon, F., Bruggen, R. V., & Tschopp, J. (2007) · Journal of Histochemistry &amp; Cytochemistry · doi:10.1369/jhc.6a7101.2006 · Cited by 531 · see citing works

In Vitro Reconstitution of the NALP1 Inflammasome Reveals Requirements for Caspase Activation.

Faustin, B., Lartigue, L., Bruey, J., Luciano, F., Hanein, D., Rouiller, I., & Reed, J. C. (2006) · Blood · doi:10.1182/blood.v108.11.3658.3658