{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,10]],"date-time":"2026-11-10T02:31:12Z","timestamp":1794277872687,"version":"4.9.0"},"reference-count":392,"publisher":"Springer Science and Business Media LLC","issue":"10","license":[{"start":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T00:00:00Z","timestamp":1788307200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T00:00:00Z","timestamp":1788307200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/100000002","name":"U.S. Department of Health & Human Services | National Institutes of Health","doi-asserted-by":"publisher","award":["R35GM151390"],"award-info":[{"award-number":["R35GM151390"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Cell Mol Immunol"],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The NLRP3 inflammasome is a central signaling pathway of innate immunity that orchestrates host defense and inflammatory responses through the activation of proinflammatory cytokines and the induction of pyroptotic cell death. Accumulating evidence indicates that NLRP3 functions within an extensive network of innate immune and cell death pathways. Reciprocal interactions between NLRP3 and other pattern-recognition receptor pathways, including Toll-like receptors, DNA-sensing cGAS\u2013STING signaling, and RNA-sensing RIG-I\/MDA5\u2013MAVS signaling, shape the magnitude and duration of inflammatory responses during pathogen infection. Moreover, substantial crosstalk exists between NLRP3 and other inflammasomes and programmed cell death pathways, reflecting the integrated nature of cellular stress and inflammatory signaling. In this review, we summarize recent advances in our understanding of the molecular mechanisms that mediate these interactions, focusing on shared signaling components, organelle dynamics, posttranslational modifications, and feedback regulatory circuits. We further discuss how these signaling networks contribute to infectious and inflammatory diseases and highlight key unanswered questions and emerging areas of investigation that may guide the development of therapies targeting inflammasome-associated pathologies.<\/jats:p>","DOI":"10.1038\/s41423-026-01463-2","type":"journal-article","created":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T07:47:51Z","timestamp":1788335271000},"page":"1194-1218","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["The NLRP3 inflammasome at the crossroads of innate immune signaling and cell death"],"prefix":"10.1038","volume":"23","author":[{"given":"Nanyang","family":"Xiao","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zexuan","family":"Lu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Destiny K.","family":"Cooper","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jueqi","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,9,2]]},"reference":[{"key":"1463_CR1","doi-asserted-by":"publisher","first-page":"407","DOI":"10.1038\/nri.2016.58","volume":"16","author":"P Broz","year":"2016","unstructured":"Broz P, Dixit VM. Inflammasomes: mechanism of assembly, regulation and signalling. Nat Rev Immunol. 2016;16:407\u201320.","journal-title":"Nat Rev Immunol"},{"key":"1463_CR2","doi-asserted-by":"publisher","first-page":"1313","DOI":"10.1038\/s41423-025-01354-y","volume":"22","author":"SR Dubey","year":"2025","unstructured":"Dubey SR, Turnbull C, Pandey A, Zhao A, Kurera M, Al-Zidan R, et al. Molecular mechanisms and regulation of inflammasome activation and signaling: sensing of pathogens and damage molecular patterns. Cell Mol Immunol. 2025;22:1313\u201344.","journal-title":"Cell Mol Immunol"},{"key":"1463_CR3","doi-asserted-by":"publisher","first-page":"1012","DOI":"10.1016\/j.tibs.2016.09.002","volume":"41","author":"Y He","year":"2016","unstructured":"He Y, Hara H, N\u00fa\u00f1ez G. Mechanism and regulation of NLRP3 inflammasome activation. Trends Biochem Sci. 2016;41:1012\u201321.","journal-title":"Trends Biochem Sci"},{"key":"1463_CR4","doi-asserted-by":"publisher","first-page":"683","DOI":"10.1038\/s42003-026-10207-x","volume":"9","author":"N Xiao","year":"2026","unstructured":"Xiao N, Lu Z, Chen J. Sensing the spectrum: diverse stimuli for the NLRP3 inflammasome. Commun Biol. 2026;9:683.","journal-title":"Commun Biol"},{"key":"1463_CR5","doi-asserted-by":"publisher","first-page":"325","DOI":"10.1038\/ni.2231","volume":"13","author":"L Franchi","year":"2012","unstructured":"Franchi L, Mu\u00f1oz-Planillo R, N\u00fa\u00f1ez G. Sensing and reacting to microbes through the inflammasomes. Nat Immunol. 2012;13:325\u201332.","journal-title":"Nat Immunol"},{"key":"1463_CR6","doi-asserted-by":"publisher","first-page":"1453","DOI":"10.1038\/s41590-025-02230-7","volume":"26","author":"A Weber","year":"2025","unstructured":"Weber A, McManus RM, Hornung V, Geyer M, Kuemmerle-Deschner JB, Latz E. The expanding role of the NLRP3 inflammasome from periodic fevers to therapeutic targets. Nat Immunol. 2025;26:1453\u201366.","journal-title":"Nat Immunol"},{"key":"1463_CR7","doi-asserted-by":"publisher","first-page":"137","DOI":"10.1146\/annurev-cellbio-101011-155745","volume":"28","author":"M Lamkanfi","year":"2012","unstructured":"Lamkanfi M, Dixit VM. Inflammasomes and their roles in health and disease. Annu Rev Cell Dev Biol. 2012;28:137\u201361.","journal-title":"Annu Rev Cell Dev Biol"},{"key":"1463_CR8","doi-asserted-by":"publisher","first-page":"379","DOI":"10.1002\/JLB.3MIR0919-191R","volume":"107","author":"S Tartey","year":"2020","unstructured":"Tartey S, Kanneganti T-D. Inflammasomes in the pathophysiology of autoinflammatory syndromes. J Leukoc Biol. 2020;107:379\u201391.","journal-title":"J Leukoc Biol"},{"key":"1463_CR9","doi-asserted-by":"publisher","first-page":"128","DOI":"10.3390\/jcm10010128","volume":"10","author":"T Welzel","year":"2021","unstructured":"Welzel T, Kuemmerle-Deschner JB. Diagnosis and management of the cryopyrin-associated periodic syndromes (CAPS): what do we know today? J Clin Med. 2021;10:128.","journal-title":"J Clin Med"},{"key":"1463_CR10","doi-asserted-by":"publisher","first-page":"277","DOI":"10.1007\/s10875-019-00638-z","volume":"39","author":"LM Booshehri","year":"2019","unstructured":"Booshehri LM, Hoffman HM. CAPS and NLRP3. J Clin Immunol. 2019;39:277\u201386.","journal-title":"J Clin Immunol"},{"key":"1463_CR11","doi-asserted-by":"publisher","first-page":"301","DOI":"10.1146\/annurev-immunol-081022-021207","volume":"41","author":"J Fu","year":"2023","unstructured":"Fu J, Wu H. Structural mechanisms of NLRP3 inflammasome assembly and activation. Annu Rev Immunol. 2023;41:301\u201316.","journal-title":"Annu Rev Immunol"},{"key":"1463_CR12","doi-asserted-by":"publisher","first-page":"3173","DOI":"10.4049\/jimmunol.0802367","volume":"182","author":"NB Bryan","year":"2009","unstructured":"Bryan NB, Dorfleutner A, Rojanasakul Y, Stehlik C. Activation of inflammasomes requires intracellular redistribution of the apoptotic speck-like protein containing a caspase recruitment domain. J Immunol. 2009;182:3173\u201382.","journal-title":"J Immunol"},{"key":"1463_CR13","doi-asserted-by":"publisher","first-page":"1207","DOI":"10.1016\/j.cell.2014.01.063","volume":"156","author":"X Cai","year":"2014","unstructured":"Cai X, Chen J, Xu H, Liu S, Jiang QX, Halfmann R, et al. Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation. Cell. 2014;156:1207\u201322.","journal-title":"Cell"},{"key":"1463_CR14","doi-asserted-by":"publisher","first-page":"1193","DOI":"10.1016\/j.cell.2014.02.008","volume":"156","author":"A Lu","year":"2014","unstructured":"Lu A, Magupalli VG, Ruan J, Yin Q, Atianand MK, Vos MR, et al. Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes. Cell. 2014;156:1193\u2013206.","journal-title":"Cell"},{"key":"1463_CR15","doi-asserted-by":"publisher","first-page":"567","DOI":"10.1146\/annurev-immunol-073119-095439","volume":"38","author":"S Kesavardhana","year":"2020","unstructured":"Kesavardhana S, Malireddi RKS, Kanneganti T-D. Caspases in cell death, inflammation, and pyroptosis. Annu Rev Immunol. 2020;38:567\u201395.","journal-title":"Annu Rev Immunol"},{"key":"1463_CR16","doi-asserted-by":"publisher","first-page":"660","DOI":"10.1038\/nature15514","volume":"526","author":"J Shi","year":"2015","unstructured":"Shi J, Zhao Y, Wang K, Shi X, Wang Y, Huang H, et al. Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death. Nature. 2015;526:660\u20135.","journal-title":"Nature"},{"key":"1463_CR17","doi-asserted-by":"publisher","first-page":"1285","DOI":"10.1038\/cr.2015.139","volume":"25","author":"WT He","year":"2015","unstructured":"He WT, Wan H, Hu L, Chen P, Wang X, Huang Z, et al. Gasdermin D is an executor of pyroptosis and required for interleukin-1\u03b2 secretion. Cell Res. 2015;25:1285\u201398.","journal-title":"Cell Res"},{"key":"1463_CR18","doi-asserted-by":"publisher","first-page":"666","DOI":"10.1038\/nature15541","volume":"526","author":"N Kayagaki","year":"2015","unstructured":"Kayagaki N, Stowe IB, Lee BL, O'Rourke K, Anderson K, Warming S, et al. Caspase-11 cleaves gasdermin D for noncanonical inflammasome signaling. Nature. 2015;526:666\u201371.","journal-title":"Nature"},{"key":"1463_CR19","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1038\/s41586-021-03218-7","volume":"591","author":"N Kayagaki","year":"2021","unstructured":"Kayagaki N, Kornfeld OS, Lee BL, Stowe IB, O'Rourke K, Li Q, et al. NINJ1 mediates plasma membrane rupture during lytic cell death. Nature. 2021;591:131\u20136.","journal-title":"Nature"},{"key":"1463_CR20","doi-asserted-by":"publisher","first-page":"1250","DOI":"10.1126\/science.1240988","volume":"341","author":"JA Hagar","year":"2013","unstructured":"Hagar JA, Powell DA, Aachoui Y, Ernst RK, Miao EA. Cytoplasmic LPS activates caspase-11: implications in TLR4-independent endotoxic shock. Science. 2013;341:1250\u20133.","journal-title":"Science"},{"key":"1463_CR21","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1038\/nature13683","volume":"514","author":"J Shi","year":"2014","unstructured":"Shi J, Zhao Y, Wang Y, Gao W, Ding J, Li P, et al. Inflammatory caspases are innate immune receptors for intracellular LPS. Nature. 2014;514:187\u201392.","journal-title":"Nature"},{"key":"1463_CR22","doi-asserted-by":"publisher","first-page":"1246","DOI":"10.1126\/science.1240248","volume":"341","author":"N Kayagaki","year":"2013","unstructured":"Kayagaki N, Wong MT, Stowe IB, Ramani SR, Gonzalez LC, Akashi-Takamura S, et al. Noncanonical inflammasome activation by intracellular LPS independent of TLR4. Science. 2013;341:1246\u20139.","journal-title":"Science"},{"key":"1463_CR23","doi-asserted-by":"publisher","first-page":"761","DOI":"10.1016\/j.immuni.2016.08.010","volume":"45","author":"CJ Gro\u00df","year":"2016","unstructured":"Gro\u00df CJ, Mishra R, Schneider KS, M\u00e9dard G, Wettmarshausen J, Dittlein DC, et al. K + Efflux-independent NLRP3 inflammasome activation by small molecules targeting mitochondria. Immunity. 2016;45:761\u201373.","journal-title":"Immunity"},{"key":"1463_CR24","doi-asserted-by":"publisher","first-page":"1142","DOI":"10.1016\/j.immuni.2013.05.016","volume":"38","author":"R Mu\u00f1oz-Planillo","year":"2013","unstructured":"Mu\u00f1oz-Planillo R, Kuffa P, Mart\u00ednez-Col\u00f3n G, Smith BL, Rajendiran TM, N\u00fa\u00f1ez G. K+ efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter. Immunity. 2013;38:1142\u201353.","journal-title":"Immunity"},{"key":"1463_CR25","doi-asserted-by":"publisher","first-page":"3937","DOI":"10.4049\/jimmunol.1402658","volume":"194","author":"MA Katsnelson","year":"2015","unstructured":"Katsnelson MA, Rucker LG, Russo HM, Dubyak GR. K+ efflux agonists induce NLRP3 inflammasome activation independently of Ca2+ signaling. J Immunol. 2015;194:3937\u201352.","journal-title":"J Immunol"},{"key":"1463_CR26","doi-asserted-by":"publisher","first-page":"1110","DOI":"10.1016\/j.cell.2017.09.039","volume":"171","author":"MM Gaidt","year":"2017","unstructured":"Gaidt MM, Ebert TS, Chauhan D, Ramshorn K, Pinci F, Zuber S, et al. The DNA inflammasome in human myeloid cells is initiated by a STING-cell death program upstream of NLRP3. Cell. 2017;171:1110\u20131124.e18.","journal-title":"Cell"},{"key":"1463_CR27","doi-asserted-by":"publisher","first-page":"EMBJ2019101638","DOI":"10.15252\/embj.2019101638","volume":"38","author":"KW Chen","year":"2019","unstructured":"Chen KW, Demarco B, Heilig R, Shkarina K, Boettcher A, Farady CJ, et al. Extrinsic and intrinsic apoptosis activate pannexin-1 to drive NLRP3 inflammasome assembly. EMBO J. 2019;38:EMBJ2019101638.","journal-title":"EMBO J"},{"key":"1463_CR28","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1038\/s41586-018-0761-3","volume":"564","author":"J Chen","year":"2018","unstructured":"Chen J, Chen ZJ. PtdIns4P on dispersed trans-Golgi network mediates NLRP3 inflammasome activation. Nature. 2018;564:71\u201376.","journal-title":"Nature"},{"key":"1463_CR29","doi-asserted-by":"publisher","first-page":"1673","DOI":"10.1038\/s41590-025-02277-6","volume":"26","author":"N Xiao","year":"2025","unstructured":"Xiao N, Kogishi A, Radochonski L, Lei Y, Chen J. Type A cholesterol-dependent cytolysins translocate to the trans-Golgi network for NLRP3 inflammasome activation. Nat Immunol. 2025;26:1673\u201385.","journal-title":"Nat Immunol"},{"key":"1463_CR30","doi-asserted-by":"publisher","first-page":"720655","DOI":"10.3389\/fimmu.2021.720655","volume":"12","author":"I Diaz-Del-Olmo","year":"2021","unstructured":"Diaz-Del-Olmo I, Worboys J, Martin-Sanchez F, Gritsenko A, Ambrose AR, Tannahill GM, et al. Internalization of the membrane attack complex triggers NLRP3 inflammasome activation and IL-1beta secretion in human macrophages. Front Immunol. 2021;12:720655.","journal-title":"Front Immunol"},{"key":"1463_CR31","doi-asserted-by":"publisher","first-page":"88","DOI":"10.3390\/v14010088","volume":"14","author":"KP Pandey","year":"2022","unstructured":"Pandey KP, Zhou Y. Influenza A virus infection activates NLRP3 inflammasome through trans-golgi network dispersion. Viruses. 2022;14:88.","journal-title":"Viruses"},{"key":"1463_CR32","doi-asserted-by":"publisher","first-page":"e50743","DOI":"10.15252\/embr.202050743","volume":"22","author":"SK Nanda","year":"2021","unstructured":"Nanda SK, Prescott AR, Figueras-Vadillo C, Cohen P. IKK\u03b2 is required for the formation of the NLRP3 inflammasome. EMBO Rep. 2021;22:e50743.","journal-title":"EMBO Rep"},{"key":"1463_CR33","doi-asserted-by":"publisher","first-page":"2271","DOI":"10.1016\/j.immuni.2022.10.021","volume":"55","author":"NA Schmacke","year":"2022","unstructured":"Schmacke NA, O'Duill F, Gaidt MM, Szymanska I, Kamper JM, Schmid-Burgk JL, et al. IKK\u03b2 primes inflammasome formation by recruiting NLRP3 to the trans-Golgi network. Immunity. 2022;55:2271\u20132284.e7.","journal-title":"Immunity"},{"key":"1463_CR34","doi-asserted-by":"publisher","first-page":"362","DOI":"10.1038\/s41564-018-0318-0","volume":"4","author":"A Mathur","year":"2019","unstructured":"Mathur A, Feng S, Hayward JA, Ngo C, Fox D, Atmosukarto II, et al. A multicomponent toxin from Bacillus cereus incites inflammation and shapes host outcome via the NLRP3 inflammasome. Nat Microbiol. 2019;4:362\u201374.","journal-title":"Nat Microbiol"},{"key":"1463_CR35","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-020-14534-3","volume":"11","author":"D Fox","year":"2020","unstructured":"Fox D, Mathur A, Xue Y, Liu Y, Tan WH, Feng S, et al. Bacillus cereus nonhaemolytic enterotoxin activates the NLRP3 inflammasome. Nat Commun. 2020;11:760.","journal-title":"Nat Commun"},{"key":"1463_CR36","doi-asserted-by":"publisher","first-page":"54600","DOI":"10.15252\/embr.202254600","volume":"24","author":"A Mathur","year":"2023","unstructured":"Mathur A, Kay C, Xue Y, Pandey A, Lee J, Jing W, et al. Clostridium perfringens virulence factors are nonredundant activators of the NLRP3 inflammasome. EMBO Rep. 2023;24:54600.","journal-title":"EMBO Rep"},{"key":"1463_CR37","doi-asserted-by":"publisher","first-page":"847","DOI":"10.1038\/ni.1631","volume":"9","author":"V Hornung","year":"2008","unstructured":"Hornung V, Bauernfeind F, Halle A, Samstad EO, Kono H, Rock KL, et al. Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat Immunol. 2008;9:847\u201356.","journal-title":"Nat Immunol"},{"key":"1463_CR38","doi-asserted-by":"publisher","first-page":"857","DOI":"10.1038\/ni.1636","volume":"9","author":"A Halle","year":"2008","unstructured":"Halle A, Hornung V, Petzold GC, Stewart CR, Monks BG, Reinheckel T, et al. The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat Immunol. 2008;9:857\u201365.","journal-title":"Nat Immunol"},{"key":"1463_CR39","first-page":"1685","volume":"195","author":"GM Orlowski","year":"2015","unstructured":"Orlowski GM, et al. Multiple cathepsins promote pro-IL-1\u03b2 synthesis and NLRP3-mediated IL-1\u03b2 activation. J Immunol Baltim Md. 2015;195:1685.","journal-title":"J Immunol Baltim Md"},{"key":"1463_CR40","doi-asserted-by":"publisher","first-page":"167","DOI":"10.3389\/fcell.2020.00167","volume":"8","author":"A Chevriaux","year":"2020","unstructured":"Chevriaux A, Pilot T, Derang\u00e8re V, Simonin H, Martine P, Chalmin F, et al. Cathepsin B is required for NLRP3 inflammasome activation in macrophages, through NLRP3 interaction. Front Cell Dev Biol. 2020;8:167.","journal-title":"Front Cell Dev Biol"},{"key":"1463_CR41","doi-asserted-by":"publisher","first-page":"956","DOI":"10.1038\/sj.cdd.4401264","volume":"10","author":"H Hentze","year":"2003","unstructured":"Hentze H, Lin XY, Choi MSK, Porter AG. Critical role for cathepsin B in mediating caspase-1-dependent interleukin-18 maturation and caspase-1-independent necrosis triggered by the microbial toxin nigericin. Cell Death Differ. 2003;10:956\u201368.","journal-title":"Cell Death Differ"},{"key":"1463_CR42","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1038\/nature09663","volume":"469","author":"R Zhou","year":"2011","unstructured":"Zhou R, Yazdi AS, Menu P, Tschopp J. A role for mitochondria in NLRP3 inflammasome activation. Nature. 2011;469:221\u20135.","journal-title":"Nature"},{"key":"1463_CR43","doi-asserted-by":"publisher","first-page":"401","DOI":"10.1016\/j.immuni.2012.01.009","volume":"36","author":"K Shimada","year":"2012","unstructured":"Shimada K, Crother TR, Karlin J, Dagvadorj J, Chiba N, Chen S, et al. Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis. Immunity. 2012;36:401\u201314.","journal-title":"Immunity"},{"key":"1463_CR44","doi-asserted-by":"publisher","first-page":"222","DOI":"10.1038\/ni.1980","volume":"12","author":"K Nakahira","year":"2011","unstructured":"Nakahira K, Haspel JA, Rathinam VA, Lee SJ, Dolinay T, Lam HC, et al. Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome. Nat Immunol. 2011;12:222\u201330.","journal-title":"Nat Immunol"},{"key":"1463_CR45","doi-asserted-by":"publisher","first-page":"311","DOI":"10.1016\/j.immuni.2013.08.001","volume":"39","author":"SS Iyer","year":"2013","unstructured":"Iyer SS, He Q, Janczy JR, Elliott EI, Zhong Z, Olivier AK, et al. Mitochondrial cardiolipin is required for Nlrp3 inflammasome activation. Immunity. 2013;39:311\u201323.","journal-title":"Immunity"},{"key":"1463_CR46","doi-asserted-by":"publisher","first-page":"613","DOI":"10.4049\/jimmunol.1100613","volume":"187","author":"F Bauernfeind","year":"2011","unstructured":"Bauernfeind F, Bartok E, Rieger A, Franchi L, N\u00fa\u00f1ez G, Hornung V. Cutting edge: reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome. J Immunol. 2011;187:613\u20137.","journal-title":"J Immunol"},{"key":"1463_CR47","doi-asserted-by":"publisher","first-page":"1433","DOI":"10.1016\/j.bbagen.2013.08.014","volume":"1840","author":"KE Lawlor","year":"2014","unstructured":"Lawlor KE, Vince JE. Ambiguities in NLRP3 inflammasome regulation: is there a role for mitochondria? Biochim Biophys Acta. 2014;1840:1433\u201340.","journal-title":"Biochim Biophys Acta"},{"key":"1463_CR48","doi-asserted-by":"publisher","first-page":"982","DOI":"10.15252\/embr.201438463","volume":"15","author":"R Allam","year":"2014","unstructured":"Allam R, Lawlor KE, Yu EC, Mildenhall AL, Moujalled DM, Lewis RS, et al. Mitochondrial apoptosis is dispensable for NLRP3 inflammasome activation but nonapoptotic caspase-8 is required for inflammasome priming. EMBO Rep. 2014;15:982\u201390.","journal-title":"EMBO Rep"},{"key":"1463_CR49","doi-asserted-by":"publisher","first-page":"198","DOI":"10.1038\/s41586-018-0372-z","volume":"560","author":"Z Zhong","year":"2018","unstructured":"Zhong Z, Liang S, Sanchez-Lopez E, He F, Shalapour S, Lin XJ, et al. New mitochondrial DNA synthesis enables NLRP3 inflammasome activation. Nature. 2018;560:198\u2013203.","journal-title":"Nature"},{"key":"1463_CR50","doi-asserted-by":"publisher","first-page":"90","DOI":"10.1016\/j.immuni.2024.10.012","volume":"58","author":"BS Saller","year":"2025","unstructured":"Saller BS, W\u00f6hrle S, Fischer L, Dufossez C, Ingerl IL, Kessler S, et al. Acute suppression of mitochondrial ATP production prevents apoptosis and provides an essential signal for NLRP3 inflammasome activation. Immunity. 2025;58:90\u2013107.e11.","journal-title":"Immunity"},{"key":"1463_CR51","doi-asserted-by":"publisher","first-page":"11282","DOI":"10.1073\/pnas.1117765109","volume":"109","author":"T Murakami","year":"2012","unstructured":"Murakami T, Ockinger J, Yu J, Byles V, McColl A, Hofer AM, et al. Critical role for calcium mobilization in activation of the NLRP3 inflammasome. Proc Natl Acad Sci USA. 2012;109:11282\u20137.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR52","doi-asserted-by":"publisher","first-page":"e1954","DOI":"10.1038\/cddis.2015.277","volume":"6","author":"JR Yaron","year":"2015","unstructured":"Yaron JR, Gangaraju S, Rao MY, Kong X, Zhang L, Su F, et al. K+ regulates Ca2+ to drive inflammasome signaling: dynamic visualization of ion flux in live cells. Cell Death Dis. 2015;6:e1954\u2013e1954.","journal-title":"Cell Death Dis"},{"key":"1463_CR53","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1038\/nature11588","volume":"492","author":"G-S Lee","year":"2012","unstructured":"Lee G-S, Subramanian N, Kim AI, Aksentijevich I, Goldbach-Mansky R, Sacks DB, et al. The calcium-sensing receptor regulates the NLRP3 inflammasome through Ca2+ and cAMP. Nature. 2012;492:123\u20137.","journal-title":"Nature"},{"key":"1463_CR54","doi-asserted-by":"publisher","first-page":"30","DOI":"10.1038\/s41590-022-01355-3","volume":"24","author":"Z Zhang","year":"2023","unstructured":"Zhang Z, Venditti R, Ran L, Liu Z, Vivot K, Sch\u00fcrmann A, et al. Distinct changes in endosomal composition promote NLRP3 inflammasome activation. Nat Immunol. 2023;24:30\u201341.","journal-title":"Nat Immunol"},{"key":"1463_CR55","doi-asserted-by":"publisher","first-page":"7134","DOI":"10.1126\/scisignal.abm7134","volume":"16","author":"B Lee","year":"2023","unstructured":"Lee B, Hoyle C, Wellens R, Green JP, Martin-Sanchez F, Williams DM, et al. Disruptions in endocytic traffic contribute to the activation of the NLRP3 inflammasome. Sci Signal. 2023;16:7134.","journal-title":"Sci Signal"},{"key":"1463_CR56","doi-asserted-by":"publisher","first-page":"451","DOI":"10.1016\/j.immuni.2015.08.008","volume":"43","author":"DN Bronner","year":"2015","unstructured":"Bronner DN, Abuaita BH, Chen X, Fitzgerald KA, Nu\u00f1ez G, He Y, et al. Endoplasmic reticulum stress activates the inflammasome via NLRP3- and Caspase-2-driven mitochondrial damage. Immunity. 2015;43:451\u201362.","journal-title":"Immunity"},{"key":"1463_CR57","doi-asserted-by":"publisher","first-page":"373","DOI":"10.1038\/ni.1863","volume":"11","author":"T Kawai","year":"2010","unstructured":"Kawai T, Akira S. The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nat Immunol. 2010;11:373\u201384.","journal-title":"Nat Immunol"},{"key":"1463_CR58","doi-asserted-by":"publisher","first-page":"1044","DOI":"10.1016\/j.cell.2020.02.041","volume":"180","author":"KA Fitzgerald","year":"2020","unstructured":"Fitzgerald KA, Kagan JC. Toll-like receptors and the control of immunity. Cell. 2020;180:1044\u201366.","journal-title":"Cell"},{"key":"1463_CR59","doi-asserted-by":"publisher","first-page":"394","DOI":"10.1038\/41131","volume":"388","author":"R Medzhitov","year":"1997","unstructured":"Medzhitov R, Preston-Hurlburt P, Janeway CA. A human homolog of the Drosophila Toll protein signals activation of adaptive immunity. Nature. 1997;388:394\u20137.","journal-title":"Nature"},{"key":"1463_CR60","doi-asserted-by":"publisher","first-page":"2085","DOI":"10.1126\/science.282.5396.2085","volume":"282","author":"A Poltorak","year":"1998","unstructured":"Poltorak A, He X, Smirnova I, Liu MY, Van Huffel C, Du X, et al. Defective LPS signaling in C3H\/HeJ and C57BL\/10ScCr mice: mutations in Tlr4 gene. Science. 1998;282:2085\u20138.","journal-title":"Science"},{"key":"1463_CR61","doi-asserted-by":"publisher","first-page":"3749","DOI":"10.4049\/jimmunol.162.7.3749","volume":"162","author":"K Hoshino","year":"1999","unstructured":"Hoshino K, Takeuchi O, Kawai T, Sanjo H, Ogawa T, Takeda Y, et al. Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: evidence for TLR4 as the Lps gene product. J Immunol. 1999;162:3749\u201352.","journal-title":"J Immunol"},{"key":"1463_CR62","doi-asserted-by":"publisher","first-page":"615","DOI":"10.1084\/jem.189.4.615","volume":"189","author":"ST Qureshi","year":"1999","unstructured":"Qureshi ST, Larivi\u00e8re L, Leveque G, Clermont S, Moore KJ, Gros P, et al. Endotoxin-tolerant mice have mutations in Toll-like receptor 4 (Tlr4). J Exp Med. 1999;189:615\u201325.","journal-title":"J Exp Med"},{"key":"1463_CR63","doi-asserted-by":"publisher","first-page":"1191","DOI":"10.1038\/nature07830","volume":"458","author":"BS Park","year":"2009","unstructured":"Park BS, Song DH, Kim HM, Choi BS, Lee H, Lee JO. The structural basis of lipopolysaccharide recognition by the TLR4\u2013MD-2 complex. Nature. 2009;458:1191\u20135.","journal-title":"Nature"},{"key":"1463_CR64","doi-asserted-by":"publisher","first-page":"4186","DOI":"10.1073\/pnas.0306906101","volume":"101","author":"TL Gioannini","year":"2004","unstructured":"Gioannini TL, Teghanemt A, Zhang D, Coussens NP, Dockstader W, Ramaswamy S, et al. Isolation of an endotoxin-MD-2 complex that produces Toll-like receptor 4-dependent cell activation at picomolar concentrations. Proc Natl Acad Sci USA. 2004;101:4186\u201391.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR65","doi-asserted-by":"publisher","first-page":"79","DOI":"10.1084\/jem.194.1.79","volume":"194","author":"AB Schromm","year":"2001","unstructured":"Schromm AB, Lien E, Henneke P, Chow JC, Yoshimura A, Heine H, et al. Molecular genetic analysis of an endotoxin nonresponder mutant cell line: a point mutation in a conserved region of Md-2 abolishes endotoxin-induced signaling. J Exp Med. 2001;194:79\u201388.","journal-title":"J Exp Med"},{"key":"1463_CR66","doi-asserted-by":"publisher","first-page":"1777","DOI":"10.1084\/jem.189.11.1777","volume":"189","author":"R Shimazu","year":"1999","unstructured":"Shimazu R, Akashi S, Ogata H, Nagai Y, Fukudome K, Miyake K, et al. MD-2, a molecule that confers lipopolysaccharide responsiveness on toll-like receptor 4. J Exp Med. 1999;189:1777\u201382.","journal-title":"J Exp Med"},{"key":"1463_CR67","doi-asserted-by":"publisher","first-page":"443","DOI":"10.1016\/S1074-7613(00)80119-3","volume":"11","author":"O Takeuchi","year":"1999","unstructured":"Takeuchi O, Hoshino K, Kawai T, Sanjo H, Takada H, Ogawa T, et al. Differential roles of TLR2 and TLR4 in recognition of gram-negative and gram-positive bacterial cell wall components. Immunity. 1999;11:443\u201351.","journal-title":"Immunity"},{"key":"1463_CR68","doi-asserted-by":"publisher","first-page":"933","DOI":"10.1093\/intimm\/13.7.933","volume":"13","author":"O Takeuchi","year":"2001","unstructured":"Takeuchi O, Kawai T, M\u00fchlradt PF, Morr M, Radolf JD, Zychlinsky A, et al. Discrimination of bacterial lipoproteins by Toll-like receptor 6. Int Immunol. 2001;13:933\u201340.","journal-title":"Int Immunol"},{"key":"1463_CR69","doi-asserted-by":"publisher","first-page":"10","DOI":"10.4049\/jimmunol.169.1.10","volume":"169","author":"O Takeuchi","year":"2002","unstructured":"Takeuchi O, Sato S, Horiuchi T, Hoshino K, Takeda K, Dong Z, et al. Cutting edge: role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins. J Immunol. 2002;169:10\u201314.","journal-title":"J Immunol"},{"key":"1463_CR70","doi-asserted-by":"publisher","first-page":"1071","DOI":"10.1016\/j.cell.2007.09.008","volume":"130","author":"MS Jin","year":"2007","unstructured":"Jin MS, Kim SE, Heo JY, Lee ME, Kim HM, Paik SG, et al. Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide. Cell. 2007;130:1071\u201382.","journal-title":"Cell"},{"key":"1463_CR71","doi-asserted-by":"publisher","first-page":"873","DOI":"10.1016\/j.immuni.2009.09.018","volume":"31","author":"JY Kang","year":"2009","unstructured":"Kang JY, Nan X, Jin MS, Youn SJ, Ryu YH, Mah S, et al. Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer. Immunity. 2009;31:873\u201384.","journal-title":"Immunity"},{"key":"1463_CR72","doi-asserted-by":"publisher","first-page":"1099","DOI":"10.1038\/35074106","volume":"410","author":"F Hayashi","year":"2001","unstructured":"Hayashi F, Smith KD, Ozinsky A, Hawn TR, Yi EC, Goodlett DR, et al. The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5. Nature. 2001;410:1099\u2013103.","journal-title":"Nature"},{"key":"1463_CR73","doi-asserted-by":"publisher","first-page":"1882","DOI":"10.4049\/jimmunol.167.4.1882","volume":"167","author":"AT Gewirtz","year":"2001","unstructured":"Gewirtz AT, Navas TA, Lyons S, Godowski PJ, Madara JL. Cutting edge: bacterial flagellin activates basolaterally expressed TLR5 to induce epithelial proinflammatory gene expression. J Immunol. 2001;167:1882\u20135.","journal-title":"J Immunol"},{"key":"1463_CR74","doi-asserted-by":"publisher","first-page":"234","DOI":"10.1038\/nature06726","volume":"452","author":"Y-M Kim","year":"2008","unstructured":"Kim Y-M, Brinkmann MM, Paquet M-E, Ploegh HL. UNC93B1 delivers nucleotide-sensing toll-like receptors to endolysosomes. Nature. 2008;452:234\u20138.","journal-title":"Nature"},{"key":"1463_CR75","doi-asserted-by":"publisher","first-page":"00291","DOI":"10.7554\/eLife.00291","volume":"2","author":"BL Lee","year":"2013","unstructured":"Lee BL, Moon JE, Shu JH, Yuan L, Newman ZR, Schekman R, et al. UNC93B1 mediates differential trafficking of endosomal TLRs. eLife. 2013;2:00291.","journal-title":"eLife"},{"key":"1463_CR76","doi-asserted-by":"publisher","first-page":"732","DOI":"10.1038\/35099560","volume":"413","author":"L Alexopoulou","year":"2001","unstructured":"Alexopoulou L, Holt AC, Medzhitov R, Flavell RA. Recognition of double-stranded RNA and activation of NF-\u03baB by Toll-like receptor 3. Nature. 2001;413:732\u20138.","journal-title":"Nature"},{"key":"1463_CR77","doi-asserted-by":"publisher","first-page":"1529","DOI":"10.1126\/science.1093616","volume":"303","author":"SS Diebold","year":"2004","unstructured":"Diebold SS, Kaisho T, Hemmi H, Akira S, Reis e Sousa C. Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA. Science. 2004;303:1529\u201331.","journal-title":"Science"},{"key":"1463_CR78","doi-asserted-by":"publisher","first-page":"1526","DOI":"10.1126\/science.1093620","volume":"303","author":"F Heil","year":"2004","unstructured":"Heil F, Hemmi H, Hochrein H, Ampenberger F, Kirschning C, Akira S, et al. Species-specific recognition of single-stranded RNA via toll-like receptor 7 and 8. Science. 2004;303:1526\u20139.","journal-title":"Science"},{"key":"1463_CR79","doi-asserted-by":"publisher","first-page":"196","DOI":"10.1038\/ni758","volume":"3","author":"H Hemmi","year":"2002","unstructured":"Hemmi H, Kaisho T, Takeuchi O, Sato S, Sanjo H, Hoshino K, et al. Small anti-viral compounds activate immune cells via the TLR7 MyD88\u2013dependent signaling pathway. Nat Immunol. 2002;3:196\u2013200.","journal-title":"Nat Immunol"},{"key":"1463_CR80","doi-asserted-by":"publisher","first-page":"740","DOI":"10.1038\/35047123","volume":"408","author":"H Hemmi","year":"2000","unstructured":"Hemmi H, Takeuchi O, Kawai T, Kaisho T, Sato S, Sanjo H, et al. A Toll-like receptor recognizes bacterial DNA. Nature. 2000;408:740\u20135.","journal-title":"Nature"},{"key":"1463_CR81","doi-asserted-by":"publisher","first-page":"2717","DOI":"10.4049\/jimmunol.1200898","volume":"189","author":"A Hidmark","year":"2012","unstructured":"Hidmark A, von Saint Paul A, Dalpke AH. Cutting edge: TLR13 is a receptor for bacterial RNA. J Immunol. 2012;189:2717\u201321.","journal-title":"J Immunol"},{"key":"1463_CR82","doi-asserted-by":"publisher","first-page":"1111","DOI":"10.1126\/science.1220363","volume":"337","author":"M Oldenburg","year":"2012","unstructured":"Oldenburg M, Kr\u00fcger A, Ferstl R, Kaufmann A, Nees G, Sigmund A, et al. TLR13 recognizes bacterial 23S rRNA devoid of erythromycin resistance\u2013forming modification. Science. 2012;337:1111\u20135.","journal-title":"Science"},{"key":"1463_CR83","doi-asserted-by":"publisher","first-page":"772","DOI":"10.1038\/ni1479","volume":"8","author":"E Latz","year":"2007","unstructured":"Latz E, Verma A, Visintin A, Gong M, Sirois CM, Klein DC, et al. Ligand-induced conformational changes allosterically activate Toll-like receptor 9. Nat Immunol. 2007;8:772\u20139.","journal-title":"Nat Immunol"},{"key":"1463_CR84","doi-asserted-by":"publisher","first-page":"1043","DOI":"10.1084\/jem.20031023","volume":"198","author":"KA Fitzgerald","year":"2003","unstructured":"Fitzgerald KA, Rowe DC, Barnes BJ, Caffrey DR, Visintin A, Latz E, et al. LPS-TLR4 signaling to IRF-3\/7 and NF-\u03baB involves the Toll adapters TRAM and TRIF. J Exp Med. 2003;198:1043\u201355.","journal-title":"J Exp Med"},{"key":"1463_CR85","doi-asserted-by":"publisher","first-page":"1144","DOI":"10.1038\/ni986","volume":"4","author":"M Yamamoto","year":"2003","unstructured":"Yamamoto M, Sato S, Hemmi H, Uematsu S, Hoshino K, Kaisho T, et al. TRAM is specifically involved in the Toll-like receptor 4\u2013mediated MyD88-independent signaling pathway. Nat Immunol. 2003;4:1144\u201350.","journal-title":"Nat Immunol"},{"key":"1463_CR86","doi-asserted-by":"publisher","first-page":"640","DOI":"10.1126\/science.1087262","volume":"301","author":"M Yamamoto","year":"2003","unstructured":"Yamamoto M, Sato S, Hemmi H, Hoshino K, Kaisho T, Sanjo H, et al. Role of adaptor TRIF in the MyD88-independent toll-like receptor signaling pathway. Science. 2003;301:640\u20133.","journal-title":"Science"},{"key":"1463_CR87","doi-asserted-by":"publisher","first-page":"835","DOI":"10.1038\/ni0901-835","volume":"2","author":"T Horng","year":"2001","unstructured":"Horng T, Barton GM, Medzhitov R. TIRAP: an adapter molecule in the Toll signaling pathway. Nat Immunol. 2001;2:835\u201341.","journal-title":"Nat Immunol"},{"key":"1463_CR88","doi-asserted-by":"publisher","first-page":"78","DOI":"10.1038\/35092578","volume":"413","author":"KA Fitzgerald","year":"2001","unstructured":"Fitzgerald KA, Palsson-McDermott EM, Bowie AG, Jefferies CA, Mansell AS, Brady G, et al. Mal (MyD88-adapter-like) is required for Toll-like receptor-4 signal transduction. Nature. 2001;413:78\u201383.","journal-title":"Nature"},{"key":"1463_CR89","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1016\/S1097-2765(00)80136-7","volume":"2","author":"R Medzhitov","year":"1998","unstructured":"Medzhitov R, Preston-Hurlburt P, Kopp E, Stadlen A, Chen C, Ghosh S, et al. MyD88 is an adaptor protein in the hToll\/IL-1 receptor family signaling pathways. Mol Cell. 1998;2:253\u20138.","journal-title":"Mol Cell"},{"key":"1463_CR90","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1016\/S1074-7613(00)80596-8","volume":"9","author":"O Adachi","year":"1998","unstructured":"Adachi O, Kawai T, Takeda K, Matsumoto M, Tsutsui H, Sakagami M, et al. Targeted disruption of the MyD88 gene results in loss of IL-1- and IL-18-mediated function. Immunity. 1998;9:143\u201350.","journal-title":"Immunity"},{"key":"1463_CR91","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1016\/S1074-7613(00)80086-2","volume":"11","author":"T Kawai","year":"1999","unstructured":"Kawai T, Adachi O, Ogawa T, Takeda K, Akira S. Unresponsiveness of MyD88-deficient mice to endotoxin. Immunity. 1999;11:115\u201322.","journal-title":"Immunity"},{"key":"1463_CR92","doi-asserted-by":"publisher","first-page":"1128","DOI":"10.1126\/science.271.5252.1128","volume":"271","author":"Z Cao","year":"1996","unstructured":"Cao Z, Henzel WJ, Gao X. IRAK: a kinase associated with the interleukin-1 receptor. Science. 1996;271:1128\u201331.","journal-title":"Science"},{"key":"1463_CR93","doi-asserted-by":"publisher","first-page":"5567","DOI":"10.1073\/pnas.082100399","volume":"99","author":"S Li","year":"2002","unstructured":"Li S, Strelow A, Fontana EJ, Wesche H. IRAK-4: a novel member of the IRAK family with the properties of an IRAK-kinase. Proc Natl Acad Sci USA. 2002;99:5567\u201372.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR94","doi-asserted-by":"publisher","first-page":"1015","DOI":"10.1101\/gad.13.8.1015","volume":"13","author":"MA Lomaga","year":"1999","unstructured":"Lomaga MA, Yeh WC, Sarosi I, Duncan GS, Furlonger C, Ho A, et al. TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signaling. Genes Dev. 1999;13:1015\u201324.","journal-title":"Genes Dev"},{"key":"1463_CR95","doi-asserted-by":"publisher","first-page":"15247","DOI":"10.1073\/pnas.1314715110","volume":"110","author":"CH Emmerich","year":"2013","unstructured":"Emmerich CH, Ordureau A, Strickson S, Arthur JS, Pedrioli PG, Komander D, et al. Activation of the canonical IKK complex by K63\/M1-linked hybrid ubiquitin chains. Proc Natl Acad Sci USA. 2013;110:15247\u201352.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR96","doi-asserted-by":"publisher","first-page":"346","DOI":"10.1038\/35085597","volume":"412","author":"C Wang","year":"2001","unstructured":"Wang C, Deng L, Hong M, Akkaraju GR, Inoue J, Chen ZJ. TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature. 2001;412:346\u201351.","journal-title":"Nature"},{"key":"1463_CR97","doi-asserted-by":"publisher","first-page":"252","DOI":"10.1038\/18465","volume":"398","author":"J Ninomiya-Tsuji","year":"1999","unstructured":"Ninomiya-Tsuji J, Kishimoto K, Hiyama A, Inoue J, Cao Z, Matsumoto K. The kinase TAK1 can activate the NIK-I\u03baB as well as the MAP kinase cascade in the IL-1 signaling pathway. Nature. 1999;398:252\u20136.","journal-title":"Nature"},{"key":"1463_CR98","doi-asserted-by":"publisher","first-page":"787","DOI":"10.4049\/jimmunol.0901363","volume":"183","author":"FG Bauernfeind","year":"2009","unstructured":"Bauernfeind FG, Horvath G, Stutz A, Alnemri ES, MacDonald K, Speert D, et al. Cutting edge: NF-\u03baB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP3 expression. J Immunol. 2009;183:787\u201391.","journal-title":"J Immunol"},{"key":"1463_CR99","doi-asserted-by":"publisher","first-page":"1022","DOI":"10.1016\/j.febslet.2012.02.045","volume":"586","author":"Y Qiao","year":"2012","unstructured":"Qiao Y, Wang P, Qi J, Zhang L, Gao C. TLR-induced NF-\u03baB activation regulates NLRP3 expression in murine macrophages. FEBS Lett. 2012;586:1022\u20136.","journal-title":"FEBS Lett"},{"key":"1463_CR100","doi-asserted-by":"publisher","first-page":"36617","DOI":"10.1074\/jbc.M112.407130","volume":"287","author":"C Juliana","year":"2012","unstructured":"Juliana C, Fernandes-Alnemri T, Kang S, Farias A, Qin F, Alnemri ES. Nontranscriptional priming and deubiquitination regulate NLRP3 inflammasome activation. J Biol Chem. 2012;287:36617\u201322.","journal-title":"J Biol Chem"},{"key":"1463_CR101","doi-asserted-by":"publisher","first-page":"792","DOI":"10.4049\/jimmunol.0900173","volume":"183","author":"L Franchi","year":"2009","unstructured":"Franchi L, Eigenbrod T, N\u00fa\u00f1ez G. Cutting edge: TNF-\u03b1 mediates sensitization to ATP and silica via the NLRP3 inflammasome in the absence of microbial stimulation. J Immunol. 2009;183:792\u20136.","journal-title":"J Immunol"},{"key":"1463_CR102","doi-asserted-by":"publisher","first-page":"3995","DOI":"10.4049\/jimmunol.1301681","volume":"191","author":"T Fernandes-Alnemri","year":"2013","unstructured":"Fernandes-Alnemri T, Kang S, Anderson C, Sagara J, Fitzgerald KA, Alnemri ES. Cutting edge: TLR signaling licenses IRAK1 for rapid activation of the NLRP3 inflammasome. J Immunol. 2013;191:3995\u20139.","journal-title":"J Immunol"},{"key":"1463_CR103","doi-asserted-by":"publisher","first-page":"1325","DOI":"10.1016\/j.imbio.2012.07.020","volume":"217","author":"K Schroder","year":"2012","unstructured":"Schroder K, Sagulenko V, Zamoshnikova A, Richards AA, Cridland JA, Irvine KM, et al. Acute lipopolysaccharide priming boosts inflammasome activation independently of inflammasome sensor induction. Immunobiology. 2012;217:1325\u20139.","journal-title":"Immunobiology"},{"key":"1463_CR104","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1016\/j.molcel.2017.08.017","volume":"68","author":"N Song","year":"2017","unstructured":"Song N, Liu ZS, Xue W, Bai ZF, Wang QY, Dai J, et al. NLRP3 phosphorylation is an essential priming event for inflammasome activation. Mol Cell. 2017;68:185\u2013197.e6.","journal-title":"Mol Cell"},{"key":"1463_CR105","doi-asserted-by":"publisher","first-page":"2324","DOI":"10.1182\/blood-2008-03-146720","volume":"113","author":"MG Netea","year":"2009","unstructured":"Netea MG, Nold-Petry CA, Nold MF, Joosten LA, Opitz B, van der Meer JH, et al. Differential requirement for the activation of the inflammasome for processing and release of IL-1beta in monocytes and macrophages. Blood. 2009;113:2324\u201335.","journal-title":"Blood"},{"key":"1463_CR106","doi-asserted-by":"publisher","first-page":"8067","DOI":"10.1073\/pnas.0709684105","volume":"105","author":"A Piccini","year":"2008","unstructured":"Piccini A, Carta S, Tassi S, Lasigli\u00e9 D, Fossati G, Rubartelli A. ATP is released by monocytes stimulated with pathogen-sensing receptor ligands and induces IL-1\u03b2 and IL-18 secretion in an autocrine way. Proc Natl Acad Sci USA. 2008;105:8067\u201372.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR107","doi-asserted-by":"publisher","first-page":"501","DOI":"10.1038\/s41580-020-0244-x","volume":"21","author":"K-P Hopfner","year":"2020","unstructured":"Hopfner K-P, Hornung V. Molecular mechanisms and cellular functions of cGAS\u2013STING signaling. Nat Rev Mol Cell Biol. 2020;21:501\u201321.","journal-title":"Nat Rev Mol Cell Biol"},{"key":"1463_CR108","doi-asserted-by":"publisher","first-page":"786","DOI":"10.1126\/science.1232458","volume":"339","author":"L Sun","year":"2013","unstructured":"Sun L, Wu J, Du F, Chen X, Chen ZJ. Cyclic GMP-AMP synthase is a cytosolic dna sensor that activates the type I interferon pathway. Science. 2013;339:786\u201391.","journal-title":"Science"},{"key":"1463_CR109","doi-asserted-by":"publisher","first-page":"1019","DOI":"10.1016\/j.immuni.2013.10.019","volume":"39","author":"X Li","year":"2013","unstructured":"Li X, Shu C, Yi G, Chaton CT, Shelton CL, Diao J, et al. Cyclic GMP-AMP synthase is activated by double-stranded DNA-induced oligomerization. Immunity. 2013;39:1019\u201331.","journal-title":"Immunity"},{"key":"1463_CR110","doi-asserted-by":"publisher","first-page":"421","DOI":"10.1016\/j.celrep.2014.01.003","volume":"6","author":"X Zhang","year":"2014","unstructured":"Zhang X, Wu J, Du F, Xu H, Sun L, Chen Z, et al. The cytosolic DNA sensor cGAS forms an oligomeric complex with DNA and undergoes switch-like conformational changes in the activation loop. Cell Rep. 2014;6:421\u201330.","journal-title":"Cell Rep"},{"key":"1463_CR111","doi-asserted-by":"publisher","first-page":"826","DOI":"10.1126\/science.1229963","volume":"339","author":"J Wu","year":"2013","unstructured":"Wu J, Sun L, Chen X, Du F, Shi H, Chen C, et al. Cyclic GMP-AMP Is an Endogenous Second Messenger in Innate Immune Signaling by Cytosolic DNA. Science. 2013;339:826\u201330.","journal-title":"Science"},{"key":"1463_CR112","doi-asserted-by":"publisher","first-page":"226","DOI":"10.1016\/j.molcel.2013.05.022","volume":"51","author":"X Zhang","year":"2013","unstructured":"Zhang X, Shi H, Wu J, Zhang X, Sun L, Chen C, et al. Cyclic GMP-AMP containing mixed phosphodiester linkages is an endogenous high-affinity ligand for STING. Mol Cell. 2013;51:226\u201335.","journal-title":"Mol Cell"},{"key":"1463_CR113","doi-asserted-by":"publisher","first-page":"380","DOI":"10.1038\/nature12306","volume":"498","author":"A Ablasser","year":"2013","unstructured":"Ablasser A, Goldeck M, Cavlar T, Deimling T, Witte G, R\u00f6hl I, et al. cGAS produces a 2\u2032-5\u2032-linked cyclic dinucleotide second messenger that activates STING. Nature. 2013;498:380\u20134.","journal-title":"Nature"},{"key":"1463_CR114","doi-asserted-by":"publisher","first-page":"1094","DOI":"10.1016\/j.cell.2013.04.046","volume":"153","author":"P Gao","year":"2013","unstructured":"Gao P, Ascano M, Wu Y, Barchet W, Gaffney BL, Zillinger T, et al. Cyclic [G(2\u2032,5\u2032)pA(3\u2032,5\u2032)p] is the metazoan second messenger produced by DNA-activated cyclic GMP-AMP synthase. Cell. 2013;153:1094\u2013107.","journal-title":"Cell"},{"key":"1463_CR115","doi-asserted-by":"publisher","first-page":"1355","DOI":"10.1016\/j.celrep.2013.05.009","volume":"3","author":"EJ Diner","year":"2013","unstructured":"Diner EJ, Burdette DL, Wilson SC, Monroe KM, Kellenberger CA, Hyodo M, et al. The innate immune DNA sensor cGAS produces a noncanonical cyclic dinucleotide that activates human sting. Cell Rep. 2013;3:1355\u201361.","journal-title":"Cell Rep"},{"key":"1463_CR116","doi-asserted-by":"publisher","first-page":"674","DOI":"10.1038\/nature07317","volume":"455","author":"H Ishikawa","year":"2008","unstructured":"Ishikawa H, Barber GN. STING is an endoplasmic reticulum adaptor that facilitates innate immune signaling. Nature. 2008;455:674\u20138.","journal-title":"Nature"},{"key":"1463_CR117","doi-asserted-by":"publisher","first-page":"538","DOI":"10.1016\/j.immuni.2008.09.003","volume":"29","author":"B Zhong","year":"2008","unstructured":"Zhong B, Yang Y, Li S, Wang YY, Li Y, Diao F, et al. The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation. Immunity. 2008;29:538\u201350.","journal-title":"Immunity"},{"key":"1463_CR118","doi-asserted-by":"publisher","first-page":"8653","DOI":"10.1073\/pnas.0900850106","volume":"106","author":"W Sun","year":"2009","unstructured":"Sun W, Li Y, Chen L, Chen H, You F, Zhou X, et al. ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization. Proc Natl Acad Sci USA. 2009;106:8653\u20138.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR119","doi-asserted-by":"publisher","first-page":"389","DOI":"10.1038\/s41586-019-0998-5","volume":"567","author":"G Shang","year":"2019","unstructured":"Shang G, Zhang C, Chen ZJ, Bai X-C, Zhang X. Cryo-EM structures of STING reveal its mechanism of activation by cyclic GMP-AMP. Nature. 2019;567:389\u201393.","journal-title":"Nature"},{"key":"1463_CR120","doi-asserted-by":"publisher","first-page":"788","DOI":"10.1038\/nature08476","volume":"461","author":"H Ishikawa","year":"2009","unstructured":"Ishikawa H, Ma Z, Barber GN. STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity. Nature. 2009;461:788\u201392.","journal-title":"Nature"},{"key":"1463_CR121","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1016\/j.chom.2015.07.001","volume":"18","author":"N Dobbs","year":"2015","unstructured":"Dobbs N, Burnaevskiy N, Chen D, Gonugunta VK, Alto NM, Yan N. STING activation by translocation from the ER is associated with infection and autoinflammatory disease. Cell Host Microbe. 2015;18:157\u201368.","journal-title":"Cell Host Microbe"},{"key":"1463_CR122","doi-asserted-by":"publisher","first-page":"262","DOI":"10.1038\/s41586-019-1006-9","volume":"567","author":"X Gui","year":"2019","unstructured":"Gui X, Yang H, Li T, Tan X, Shi P, Li M, et al. Autophagy induction via STING trafficking is a primordial function of the cGAS pathway. Nature. 2019;567:262\u20136.","journal-title":"Nature"},{"key":"1463_CR123","doi-asserted-by":"publisher","first-page":"5328","DOI":"10.1128\/JVI.00037-14","volume":"88","author":"T Abe","year":"2014","unstructured":"Abe T, Barber GN. Cytosolic-DNA-mediated, STING-dependent proinflammatory gene induction necessitates canonical NF-\u03baB activation through TBK1. J Virol. 2014;88:5328\u201341.","journal-title":"J Virol"},{"key":"1463_CR124","doi-asserted-by":"publisher","first-page":"491","DOI":"10.1038\/ni921","volume":"4","author":"KA Fitzgerald","year":"2003","unstructured":"Fitzgerald KA, McWhirter SM, Faia KL, Rowe DC, Latz E, Golenbock DT, et al. IKK\u03b5 and TBK1 are essential components of the IRF3 signaling pathway. Nat Immunol. 2003;4:491\u20136.","journal-title":"Nat Immunol"},{"key":"1463_CR125","doi-asserted-by":"publisher","first-page":"ra20","DOI":"10.1126\/scisignal.2002521","volume":"5","author":"Y Tanaka","year":"2012","unstructured":"Tanaka Y, Chen ZJ. STING specifies IRF3 phosphorylation by TBK1 in the cytosolic DNA signaling pathway. Sci Signal. 2012;5:ra20\u2013ra20.","journal-title":"Sci Signal"},{"key":"1463_CR126","doi-asserted-by":"publisher","first-page":"3611","DOI":"10.1084\/jem.20171749","volume":"214","author":"KV Swanson","year":"2017","unstructured":"Swanson KV, Junkins RD, Kurkjian CJ, Holley-Guthrie E, Pendse AA, El Morabiti R, et al. A noncanonical function of cGAMP in inflammasome priming and activation. J Exp Med. 2017;214:3611\u201326.","journal-title":"J Exp Med"},{"key":"1463_CR127","doi-asserted-by":"publisher","first-page":"e1008335","DOI":"10.1371\/journal.ppat.1008335","volume":"16","author":"W Wang","year":"2020","unstructured":"Wang W, Hu D, Wu C, Feng Y, Li A, Liu W, et al. STING promotes NLRP3 localization in ER and facilitates NLRP3 deubiquitination to activate the inflammasome upon HSV-1 infection. PLOS Pathog. 2020;16:e1008335.","journal-title":"PLOS Pathog"},{"key":"1463_CR128","doi-asserted-by":"publisher","first-page":"393","DOI":"10.1016\/j.immuni.2017.02.011","volume":"46","author":"Y Wang","year":"2017","unstructured":"Wang Y, Ning X, Gao P, Wu S, Sha M, Lv M, et al. Inflammasome activation triggers caspase-1-mediated cleavage of cGAS to regulate responses to DNA virus infection. Immunity. 2017;46:393\u2013404.","journal-title":"Immunity"},{"key":"1463_CR129","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1016\/j.immuni.2011.02.006","volume":"34","author":"G Guarda","year":"2011","unstructured":"Guarda G, Braun M, Staehli F, Tardivel A, Mattmann C, F\u00f6rster I, et al. Type I interferon inhibits interleukin-1 production and inflammasome activation. Immunity. 2011;34:213\u201323.","journal-title":"Immunity"},{"key":"1463_CR130","doi-asserted-by":"publisher","first-page":"EMBJ201899347","DOI":"10.15252\/embj.201899347","volume":"37","author":"Y Zheng","year":"2018","unstructured":"Zheng Y, Liu Q, Wu Y, Ma L, Zhang Z, Liu T, et al. Zika virus elicits inflammation to evade antiviral response by cleaving cGAS via NS1-caspase-1 axis. EMBO J. 2018;37:EMBJ201899347.","journal-title":"EMBO J"},{"key":"1463_CR131","doi-asserted-by":"publisher","first-page":"413","DOI":"10.1016\/j.immuni.2018.07.006","volume":"49","author":"I Banerjee","year":"2018","unstructured":"Banerjee I, Behl B, Mendonca M, Shrivastava G, Russo AJ, Menoret A, et al. Gasdermin D restrains type I interferon response to cytosolic DNA by disrupting ionic homeostasis. Immunity. 2018;49:413\u201326.e5.","journal-title":"Immunity"},{"key":"1463_CR132","doi-asserted-by":"publisher","first-page":"238","DOI":"10.1007\/s00262-025-04088-y","volume":"74","author":"C Mowat","year":"2025","unstructured":"Mowat C, Schiller D, Baker K. NLRP3 activation promotes cGAS\/STING signaling and antitumor immunity by colorectal cancer cells. Cancer Immunol Immunother. 2025;74:238.","journal-title":"Cancer Immunol Immunother"},{"key":"1463_CR133","doi-asserted-by":"publisher","first-page":"447","DOI":"10.1146\/annurev-micro-102215-095605","volume":"72","author":"X Tan","year":"2018","unstructured":"Tan X, Sun L, Chen J, Chen ZJ. Detection of microbial infections through innate immune sensing of nucleic acids. Annu Rev Microbiol. 2018;72:447\u201378.","journal-title":"Annu Rev Microbiol"},{"key":"1463_CR134","doi-asserted-by":"publisher","first-page":"1512","DOI":"10.1073\/pnas.0912986107","volume":"107","author":"T Satoh","year":"2010","unstructured":"Satoh T, Kato H, Kumagai Y, Yoneyama M, Sato S, Matsushita K, et al. LGP2 is a positive regulator of RIG-I\u2013 and MDA5-mediated antiviral responses. Proc Natl Acad Sci USA. 2010;107:1512\u20137.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR135","doi-asserted-by":"publisher","first-page":"2851","DOI":"10.4049\/jimmunol.175.5.2851","volume":"175","author":"M Yoneyama","year":"2005","unstructured":"Yoneyama M, Kikuchi M, Matsumoto K, Imaizumi T, Miyagishi M, Taira K, et al. Shared and unique functions of the DExD\/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity. J Immunol. 2005;175:2851\u20138.","journal-title":"J Immunol"},{"key":"1463_CR136","doi-asserted-by":"publisher","first-page":"730","DOI":"10.1038\/ni1087","volume":"5","author":"M Yoneyama","year":"2004","unstructured":"Yoneyama M, Kikuchi M, Natsukawa T, Shinobu N, Imaizumi T, Miyagishi M, et al. The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. Nat Immunol. 2004;5:730\u20137.","journal-title":"Nat Immunol"},{"key":"1463_CR137","doi-asserted-by":"publisher","first-page":"637","DOI":"10.1073\/pnas.022637199","volume":"99","author":"DC Kang","year":"2002","unstructured":"Kang DC, Gopalkrishnan RV, Wu Q, Jankowsky E, Pyle AM, Fisher PB. mda-5: An interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties. Proc Natl Acad Sci USA. 2002;99:637\u201342.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR138","doi-asserted-by":"publisher","first-page":"582","DOI":"10.1073\/pnas.0606699104","volume":"104","author":"T Saito","year":"2007","unstructured":"Saito T, Hirai R, Loo YM, Owen D, Johnson CL, Sinha SC, et al. Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2. Proc Natl Acad Sci USA. 2007;104:582\u20137.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR139","doi-asserted-by":"publisher","first-page":"6444","DOI":"10.4049\/jimmunol.178.10.6444","volume":"178","author":"T Venkataraman","year":"2007","unstructured":"Venkataraman T, Valdes M, Elsby R, Kakuta S, Caceres G, Saijo S, et al. Loss of DExD\/H Box RNA helicase LGP2 manifests disparate antiviral responses. J Immunol. 2007;178:6444\u201355.","journal-title":"J Immunol"},{"key":"1463_CR140","doi-asserted-by":"publisher","first-page":"25","DOI":"10.1016\/j.immuni.2009.05.008","volume":"31","author":"M Schlee","year":"2009","unstructured":"Schlee M, Roth A, Hornung V, Hagmann CA, Wimmenauer V, Barchet W, et al. Recognition of 5\u2032 triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus. Immunity. 2009;31:25\u201334.","journal-title":"Immunity"},{"key":"1463_CR141","doi-asserted-by":"publisher","first-page":"997","DOI":"10.1126\/science.1132998","volume":"314","author":"A Pichlmair","year":"2006","unstructured":"Pichlmair A, Schulz O, Tan CP, N\u00e4slund TI, Liljestr\u00f6m P, Weber F, et al. RIG-I-mediated antiviral responses to single-stranded RNA bearing 5\u2019-phosphates. Science. 2006;314:997\u20131001.","journal-title":"Science"},{"key":"1463_CR142","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1038\/nature04734","volume":"441","author":"H Kato","year":"2006","unstructured":"Kato H, Takeuchi O, Sato S, Yoneyama M, Yamamoto M, Matsui K, et al. Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses. Nature. 2006;441:101\u20135.","journal-title":"Nature"},{"key":"1463_CR143","doi-asserted-by":"publisher","first-page":"1601","DOI":"10.1084\/jem.20080091","volume":"205","author":"H Kato","year":"2008","unstructured":"Kato H, Takeuchi O, Mikamo-Satoh E, Hirai R, Kawai T, Matsushita K, et al. Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid\u2013inducible gene-I and melanoma differentiation\u2013associated gene 5. J Exp Med. 2008;205:1601\u201310.","journal-title":"J Exp Med"},{"key":"1463_CR144","doi-asserted-by":"publisher","first-page":"423","DOI":"10.1016\/j.cell.2011.09.039","volume":"147","author":"E Kowalinski","year":"2011","unstructured":"Kowalinski E, Lunardi T, McCarthy AA, Louber J, Brunel J, Grigorov B, et al. Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. Cell. 2011;147:423\u201335.","journal-title":"Cell"},{"key":"1463_CR145","doi-asserted-by":"publisher","first-page":"669","DOI":"10.1016\/j.cell.2005.08.012","volume":"122","author":"RB Seth","year":"2005","unstructured":"Seth RB, Sun L, Ea C-K, Chen ZJ. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-\u03baB and IRF3. Cell. 2005;122:669\u201382.","journal-title":"Cell"},{"key":"1463_CR146","doi-asserted-by":"publisher","first-page":"1167","DOI":"10.1038\/nature04193","volume":"437","author":"E Meylan","year":"2005","unstructured":"Meylan E, Curran J, Hofmann K, Moradpour D, Binder M, Bartenschlager R, et al. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature. 2005;437:1167\u201372.","journal-title":"Nature"},{"key":"1463_CR147","doi-asserted-by":"publisher","first-page":"981","DOI":"10.1038\/ni1243","volume":"6","author":"T Kawai","year":"2005","unstructured":"Kawai T, Takahashi K, Sato S, Coban C, Kumar H, Kato H, et al. IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction. Nat Immunol. 2005;6:981\u20138.","journal-title":"Nat Immunol"},{"key":"1463_CR148","doi-asserted-by":"publisher","first-page":"727","DOI":"10.1016\/j.molcel.2005.08.014","volume":"19","author":"L-G Xu","year":"2005","unstructured":"Xu L-G, Wang YY, Han KJ, Li LY, Zhai Z, Shu HB. VISA is an adapter protein required for virus-triggered IFN-\u03b2 signaling. Mol Cell. 2005;19:727\u201340.","journal-title":"Mol Cell"},{"key":"1463_CR149","doi-asserted-by":"publisher","first-page":"668","DOI":"10.1016\/j.cell.2010.04.018","volume":"141","author":"E Dixit","year":"2010","unstructured":"Dixit E, Boulant S, Zhang Y, Lee AS, Odendall C, Shum B, et al. Peroxisomes are signaling platforms for antiviral innate immunity. Cell. 2010;141:668\u201381.","journal-title":"Cell"},{"key":"1463_CR150","doi-asserted-by":"publisher","first-page":"448","DOI":"10.1016\/j.cell.2011.06.041","volume":"146","author":"F Hou","year":"2011","unstructured":"Hou F, Sun L, Zheng H, Skaug B, Jiang QX, Chen ZJ. MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell. 2011;146:448\u201361.","journal-title":"Cell"},{"key":"1463_CR151","doi-asserted-by":"publisher","first-page":"01489","DOI":"10.7554\/eLife.01489","volume":"3","author":"H Xu","year":"2014","unstructured":"Xu H, He X, Zheng H, Huang LJ, Hou F, Yu Z, et al. Structural basis for the prion-like MAVS filaments in antiviral innate immunity. eLife. 2014;3:01489.","journal-title":"eLife"},{"key":"1463_CR152","doi-asserted-by":"publisher","first-page":"00785","DOI":"10.7554\/eLife.00785","volume":"2","author":"S Liu","year":"2013","unstructured":"Liu S, Chen J, Cai X, Wu J, Chen X, Wu YT, et al. MAVS recruits multiple ubiquitin E3 ligases to activate antiviral signaling cascades. eLife. 2013;2:00785.","journal-title":"eLife"},{"key":"1463_CR153","doi-asserted-by":"publisher","first-page":"3257","DOI":"10.1038\/sj.emboj.7601220","volume":"25","author":"SK Saha","year":"2006","unstructured":"Saha SK, Pietras EM, He JQ, Kang JR, Liu SY, Oganesyan G, et al. Regulation of antiviral responses by a direct and specific interaction between TRAF3 and Cardif. EMBO J. 2006;25:3257\u201363.","journal-title":"EMBO J"},{"key":"1463_CR154","doi-asserted-by":"publisher","first-page":"315","DOI":"10.1016\/j.molcel.2009.09.037","volume":"36","author":"W Zeng","year":"2009","unstructured":"Zeng W, Xu M, Liu S, Sun L, Chen ZJ. Key role of Ubc5 and lysine-63 polyubiquitination in viral activation of IRF3. Mol Cell. 2009;36:315\u201325.","journal-title":"Mol Cell"},{"key":"1463_CR155","doi-asserted-by":"publisher","first-page":"e9172","DOI":"10.1371\/journal.pone.0009172","volume":"5","author":"ED Tang","year":"2010","unstructured":"Tang ED, Wang C-Y. TRAF5 is a downstream target of MAVS in antiviral innate immune signaling. PLOS ONE. 2010;5:e9172.","journal-title":"PLOS ONE"},{"key":"1463_CR156","doi-asserted-by":"publisher","first-page":"1148","DOI":"10.1126\/science.1081315","volume":"300","author":"S Sharma","year":"2003","unstructured":"Sharma S, tenOever BR, Grandvaux N, Zhou GP, Lin R, Hiscott J. Triggering the interferon antiviral response through an IKK-related pathway. Science. 2003;300:1148\u201351.","journal-title":"Science"},{"key":"1463_CR157","doi-asserted-by":"publisher","first-page":"491","DOI":"10.1038\/ni921","volume":"4","author":"KA Fitzgerald","year":"2003","unstructured":"Fitzgerald KA, McWhirter SM, Faia KL, Rowe DC, Latz E, Golenbock DT, et al. IKKepsilon and TBK1 are essential components of the IRF3 signaling pathway. Nat Immunol. 2003;4:491\u20136.","journal-title":"Nat Immunol"},{"key":"1463_CR158","doi-asserted-by":"publisher","first-page":"537","DOI":"10.1038\/s41577-020-0288-3","volume":"20","author":"J Rehwinkel","year":"2020","unstructured":"Rehwinkel J, Gack MU. RIG-I-like receptors: their regulation and roles in RNA sensing. Nat Rev Immunol. 2020;20:537\u201351.","journal-title":"Nat Rev Immunol"},{"key":"1463_CR159","doi-asserted-by":"publisher","first-page":"348","DOI":"10.1016\/j.cell.2013.02.054","volume":"153","author":"N Subramanian","year":"2013","unstructured":"Subramanian N, Natarajan K, Clatworthy MR, Wang Z, Germain RN. The adaptor MAVS promotes NLRP3 mitochondrial localization and inflammasome activation. Cell. 2013;153:348\u201361.","journal-title":"Cell"},{"key":"1463_CR160","doi-asserted-by":"publisher","first-page":"4214","DOI":"10.4049\/jimmunol.1400582","volume":"193","author":"L Franchi","year":"2014","unstructured":"Franchi L, Eigenbrod T, Mu\u00f1oz-Planillo R, Ozkurede U, Kim YG, Arindam C, et al. Cytosolic double-stranded RNA activates the NLRP3 inflammasome via MAVS-induced membrane permeabilization and K+ efflux. J Immunol. 2014;193:4214\u201322.","journal-title":"J Immunol"},{"key":"1463_CR161","doi-asserted-by":"publisher","first-page":"4358","DOI":"10.4049\/jimmunol.1301170","volume":"191","author":"S Park","year":"2013","unstructured":"Park S, Juliana C, Hong S, Datta P, Hwang I, Fernandes-Alnemri T, et al. The mitochondrial antiviral protein MAVS associates with NLRP3 and regulates its inflammasome activity. J Immunol. 2013;191:4358\u201366.","journal-title":"J Immunol"},{"key":"1463_CR162","doi-asserted-by":"publisher","first-page":"84","DOI":"10.1016\/j.coi.2015.01.010","volume":"0","author":"RE Vance","year":"2015","unstructured":"Vance RE. The NAIP\/NLRC4 inflammasomes. Curr Opin Immunol. 2015;0:84\u201389.","journal-title":"Curr Opin Immunol"},{"key":"1463_CR163","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1111\/imr.12906","volume":"297","author":"C Kay","year":"2020","unstructured":"Kay C, Wang R, Kirkby M, Man SM. Molecular mechanisms activating the NAIP-NLRC4 inflammasome: Implications in infectious disease, autoinflammation, and cancer. Immunol Rev. 2020;297:67\u201382.","journal-title":"Immunol Rev"},{"key":"1463_CR164","doi-asserted-by":"publisher","first-page":"100863","DOI":"10.1016\/j.mam.2020.100863","volume":"76","author":"R Bauer","year":"2020","unstructured":"Bauer R, Rauch I. The NAIP\/NLRC4 inflammasome in infection and pathology. Mol Asp Med. 2020;76:100863.","journal-title":"Mol Asp Med"},{"key":"1463_CR165","doi-asserted-by":"publisher","first-page":"82","DOI":"10.1038\/s41594-023-01143-z","volume":"31","author":"RE Matico","year":"2024","unstructured":"Matico RE, Yu X, Miller R, Somani S, Ricketts MD, Kumar N, et al. Structural basis of the human NAIP\/NLRC4 inflammasome assembly and pathogen sensing. Nat Struct Mol Biol. 2024;31:82\u201391.","journal-title":"Nat Struct Mol Biol"},{"key":"1463_CR166","doi-asserted-by":"publisher","first-page":"596","DOI":"10.1038\/nature10510","volume":"477","author":"Y Zhao","year":"2011","unstructured":"Zhao Y, Yang J, Shi J, Gong YN, Lu Q, Xu H, et al. The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus. Nature. 2011;477:596\u2013600.","journal-title":"Nature"},{"key":"1463_CR167","doi-asserted-by":"publisher","first-page":"e18","DOI":"10.1371\/journal.ppat.0020018","volume":"2","author":"T Ren","year":"2006","unstructured":"Ren T, Zamboni DS, Roy CR, Dietrich WF, Vance RE. Flagellin-deficient Legionella mutants evade caspase-1- and Naip5-mediated macrophage immunity. PLoS Pathog. 2006;2:e18.","journal-title":"PLoS Pathog"},{"key":"1463_CR168","doi-asserted-by":"publisher","first-page":"657","DOI":"10.1084\/jem.20151809","volume":"213","author":"I Rauch","year":"2016","unstructured":"Rauch I, Tenthorey JL, Nichols RD, Al Moussawi K, Kang JJ, Kang C, et al. NAIP proteins are required for cytosolic detection of specific bacterial ligands in vivo. J Exp Med. 2016;213:657\u201365.","journal-title":"J Exp Med"},{"key":"1463_CR169","doi-asserted-by":"publisher","first-page":"592","DOI":"10.1038\/nature10394","volume":"477","author":"EM Kofoed","year":"2011","unstructured":"Kofoed EM, Vance RE. Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity. Nature. 2011;477:592\u20135.","journal-title":"Nature"},{"key":"1463_CR170","doi-asserted-by":"publisher","first-page":"647","DOI":"10.1084\/jem.20160006","volume":"213","author":"Y Zhao","year":"2016","unstructured":"Zhao Y, Shi J, Shi X, Wang Y, Wang F, Shao F. Genetic functions of the NAIP family of inflammasome receptors for bacterial ligands in mice. J Exp Med. 2016;213:647\u201356.","journal-title":"J Exp Med"},{"key":"1463_CR171","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1016\/j.molcel.2014.02.018","volume":"54","author":"JL Tenthorey","year":"2014","unstructured":"Tenthorey JL, Kofoed EM, Daugherty MD, Malik HS, Vance RE. Molecular basis for specific recognition of bacterial ligands by NAIP\/NLRC4 inflammasomes. Mol Cell. 2014;54:17\u201329.","journal-title":"Mol Cell"},{"key":"1463_CR172","doi-asserted-by":"publisher","first-page":"3986","DOI":"10.4049\/jimmunol.1301549","volume":"191","author":"M Rayamajhi","year":"2013","unstructured":"Rayamajhi M, Zak DE, Chavarria-Smith J, Vance RE, Miao EA. Cutting edge: mouse NAIP1 detects the type III secretion system needle protein. J Immunol. 2013;191:3986\u20139.","journal-title":"J Immunol"},{"key":"1463_CR173","doi-asserted-by":"publisher","first-page":"14408","DOI":"10.1073\/pnas.1306376110","volume":"110","author":"J Yang","year":"2013","unstructured":"Yang J, Zhao Y, Shi J, Shao F. Human NAIP and mouse NAIP1 recognize bacterial type III secretion needle protein for inflammasome activation. Proc Natl Acad Sci USA. 2013;110:14408\u201313.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR174","doi-asserted-by":"publisher","first-page":"815","DOI":"10.4049\/jimmunol.1403100","volume":"195","author":"J Kortmann","year":"2015","unstructured":"Kortmann J, Brubaker SW, Monack DM. Cutting edge: inflammasome activation in primary human macrophages is dependent on flagellin. J Immunol. 2015;195:815\u20139.","journal-title":"J Immunol"},{"key":"1463_CR175","doi-asserted-by":"publisher","first-page":"13242","DOI":"10.1073\/pnas.1710433114","volume":"114","author":"VM Reyes Ruiz","year":"2017","unstructured":"Reyes Ruiz VM, Ramirez J, Naseer N, Palacio NM, Siddarthan IJ, Yan BM, et al. Broad detection of bacterial type III secretion system and flagellin proteins by the human NAIP\/NLRC4 inflammasome. Proc Natl Acad Sci USA. 2017;114:13242\u20137.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR176","doi-asserted-by":"publisher","first-page":"172","DOI":"10.1126\/science.1236381","volume":"341","author":"Z Hu","year":"2013","unstructured":"Hu Z, Yan C, Liu P, Huang Z, Ma R, Zhang C, et al. Crystal structure of NLRC4 reveals its autoinhibition mechanism. Science. 2013;341:172\u20135.","journal-title":"Science"},{"key":"1463_CR177","doi-asserted-by":"publisher","first-page":"399","DOI":"10.1126\/science.aac5489","volume":"350","author":"Z Hu","year":"2015","unstructured":"Hu Z, Zhou Q, Zhang C, Fan S, Cheng W, Zhao Y, et al. Structural and biochemical basis for induced self-propagation of NLRC4. Science. 2015;350:399\u2013404.","journal-title":"Science"},{"key":"1463_CR178","doi-asserted-by":"publisher","first-page":"404","DOI":"10.1126\/science.aac5789","volume":"350","author":"L Zhang","year":"2015","unstructured":"Zhang L, Chen S, Ruan J, Wu J, Tong AB, Yin Q, et al. Cryo-EM structure of the activated NAIP2-NLRC4 inflammasome reveals nucleated polymerization. Science. 2015;350:404\u20139.","journal-title":"Science"},{"key":"1463_CR179","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1038\/cr.2017.148","volume":"28","author":"X Yang","year":"2018","unstructured":"Yang X, Yang F, Wang W, Lin G, Hu Z, Han Z, et al. Structural basis for specific flagellin recognition by the NLR protein NAIP5. Cell Res. 2018;28:35\u201347.","journal-title":"Cell Res"},{"key":"1463_CR180","doi-asserted-by":"publisher","first-page":"888","DOI":"10.1126\/science.aao1140","volume":"358","author":"JL Tenthorey","year":"2017","unstructured":"Tenthorey JL, Haloupek N, L\u00f3pez-Blanco JR, Grob P, Adamson E, Hartenian E, et al. The structural basis of flagellin detection by NAIP5: a strategy to limit pathogen immune evasion. Science. 2017;358:888\u201393.","journal-title":"Science"},{"key":"1463_CR181","doi-asserted-by":"publisher","first-page":"eadi8539","DOI":"10.1126\/sciadv.adi8539","volume":"9","author":"B Paidimuddala","year":"2023","unstructured":"Paidimuddala B, Cao J, Zhang L. Structural basis for flagellin-induced NAIP5 activation. Sci Adv. 2023;9:eadi8539.","journal-title":"Sci Adv"},{"key":"1463_CR182","doi-asserted-by":"publisher","first-page":"7403","DOI":"10.1073\/pnas.1402911111","volume":"111","author":"SM Man","year":"2014","unstructured":"Man SM, Hopkins LJ, Nugent E, Cox S, Gl\u00fcck IM, Tourlomousis P, et al. Inflammasome activation causes dual recruitment of NLRC4 and NLRP3 to the same macromolecular complex. Proc Natl Acad Sci USA. 2014;111:7403\u20138.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR183","doi-asserted-by":"publisher","first-page":"613","DOI":"10.1042\/BJ20121198","volume":"449","author":"M Proell","year":"2013","unstructured":"Proell M, Gerlic M, Mace PD, Reed JC, Riedl SJ. The CARD plays a critical role in ASC foci formation and inflammasome signaling. Biochem J. 2013;449:613\u201321.","journal-title":"Biochem J"},{"key":"1463_CR184","doi-asserted-by":"publisher","first-page":"539","DOI":"10.1038\/nature11429","volume":"490","author":"Y Qu","year":"2012","unstructured":"Qu Y, Misaghi S, Izrael-Tomasevic A, Newton K, Gilmour LL, Lamkanfi M, et al. Phosphorylation of NLRC4 is critical for inflammasome activation. Nature. 2012;490:539\u201342.","journal-title":"Nature"},{"key":"1463_CR185","doi-asserted-by":"publisher","first-page":"877","DOI":"10.1084\/jem.20132234","volume":"213","author":"Y Qu","year":"2016","unstructured":"Qu Y, Misaghi S, Newton K, Maltzman A, Izrael-Tomasevic A, Arnott D, et al. NLRP3 recruitment by NLRC4 during Salmonella infection. J Exp Med. 2016;213:877\u201385.","journal-title":"J Exp Med"},{"key":"1463_CR186","doi-asserted-by":"publisher","DOI":"10.1084\/jem.20191736","volume":"217","author":"JL Tenthorey","year":"2020","unstructured":"Tenthorey JL, Chavez RA, Thompson TW, Deets KA, Vance RE, Rauch I. NLRC4 inflammasome activation is NLRP3- and phosphorylation-independent during infection and does not protect from melanoma. J Exp Med. 2020;217:e20191736.","journal-title":"J Exp Med"},{"key":"1463_CR187","doi-asserted-by":"publisher","first-page":"1745","DOI":"10.1084\/jem.20100257","volume":"207","author":"P Broz","year":"2010","unstructured":"Broz P, Newton K, Lamkanfi M, Mariathasan S, Dixit VM, Monack DM. Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella. J Exp Med. 2010;207:1745\u201355.","journal-title":"J Exp Med"},{"key":"1463_CR188","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1038\/nature02664","volume":"430","author":"S Mariathasan","year":"2004","unstructured":"Mariathasan S, Newton K, Monack DM, Vucic D, French DM, Lee WP, et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature. 2004;430:213\u20138.","journal-title":"Nature"},{"key":"1463_CR189","doi-asserted-by":"publisher","first-page":"576","DOI":"10.1038\/ni1346","volume":"7","author":"L Franchi","year":"2006","unstructured":"Franchi L, Amer A, Body-Malapel M, Kanneganti TD, Oz\u00f6ren N, Jagirdar R, et al. Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1\u03b2 in salmonella-infected macrophages. Nat Immunol. 2006;7:576\u201382.","journal-title":"Nat Immunol"},{"key":"1463_CR190","doi-asserted-by":"publisher","first-page":"569","DOI":"10.1038\/ni1344","volume":"7","author":"EA Miao","year":"2006","unstructured":"Miao EA, Alpuche-Aranda CM, Dors M, Clark AE, Bader MW, Miller SI, et al. Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1\u03b2 via Ipaf. Nat Immunol. 2006;7:569\u201375.","journal-title":"Nat Immunol"},{"key":"1463_CR191","doi-asserted-by":"publisher","first-page":"417","DOI":"10.1016\/S1097-2765(02)00599-3","volume":"10","author":"F Martinon","year":"2002","unstructured":"Martinon F, Burns K, Tschopp J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-\u03b2. Mol Cell. 2002;10:417\u201326.","journal-title":"Mol Cell"},{"key":"1463_CR192","doi-asserted-by":"publisher","DOI":"10.1084\/jem.20211405","volume":"219","author":"S Bauernfried","year":"2022","unstructured":"Bauernfried S, Hornung V. Human NLRP1: from the shadows to center stage. J Exp Med. 2022;219:e20211405.","journal-title":"J Exp Med"},{"key":"1463_CR193","doi-asserted-by":"publisher","first-page":"3853","DOI":"10.1016\/j.molcel.2025.09.018","volume":"85","author":"JKY Yap","year":"2025","unstructured":"Yap JKY, Duszyc K, Schroder K. NLRP1 under pressure: an overview of the NLRP1 inflammasome as a sensor of cellular stress. Mol Cell. 2025;85:3853\u201361.","journal-title":"Mol Cell"},{"key":"1463_CR194","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1111\/imr.12884","volume":"297","author":"CY Taabazuing","year":"2020","unstructured":"Taabazuing CY, Griswold AR, Bachovchin DA. The NLRP1 and CARD8 inflammasomes. Immunol Rev. 2020;297:13\u201325.","journal-title":"Immunol Rev"},{"key":"1463_CR195","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2164-14-188","volume":"14","author":"I Sastalla","year":"2013","unstructured":"Sastalla I, Crown D, Masters SL, McKenzie A, Leppla SH, Moayeri M. Transcriptional analysis of the three Nlrp1 paralogs in mice. BMC Genom. 2013;14:188.","journal-title":"BMC Genom"},{"key":"1463_CR196","doi-asserted-by":"publisher","first-page":"25030","DOI":"10.1074\/jbc.M112.378323","volume":"287","author":"JN Finger","year":"2012","unstructured":"Finger JN, Lich JD, Dare LC, Cook MN, Brown KK, Duraiswami C, et al. Autolytic proteolysis within the function to find domain (FIIND) is required for NLRP1 inflammasome activity. J Biol Chem. 2012;287:25030\u20137.","journal-title":"J Biol Chem"},{"key":"1463_CR197","doi-asserted-by":"publisher","first-page":"82","DOI":"10.1126\/science.aau1208","volume":"364","author":"AJ Chui","year":"2019","unstructured":"Chui AJ, Okondo MC, Rao SD, Gai K, Griswold AR, Johnson DC, et al. N-terminal degradation activates the NLRP1B inflammasome. Science. 2019;364:82\u201385.","journal-title":"Science"},{"key":"1463_CR198","doi-asserted-by":"publisher","DOI":"10.1126\/science.aau1330","volume":"364","author":"A Sandstrom","year":"2019","unstructured":"Sandstrom A, Mitchell PS, Goers L, Mu EW, Lesser CF, Vance RE. Functional degradation: a mechanism of NLRP1 inflammasome activation by diverse pathogen enzymes. Science. 2019;364:eaau1330.","journal-title":"Science"},{"key":"1463_CR199","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.60609","volume":"10","author":"BV Tsu","year":"2021","unstructured":"Tsu BV, Beierschmitt C, Ryan AP, Agarwal R, Mitchell PS, Daugherty MD. Diverse viral proteases activate the NLRP1 inflammasome. eLife. 2021;10:e60609.","journal-title":"eLife"},{"key":"1463_CR200","doi-asserted-by":"publisher","DOI":"10.1126\/science.aay2002","volume":"370","author":"KS Robinson","year":"2020","unstructured":"Robinson KS, Teo D, Tan KS, Toh GA, Ong HH, Lim CK, et al. Enteroviral 3C protease activates the human NLRP1 inflammasome in airway epithelia. Science. 2020;370:eaay2002.","journal-title":"Science"},{"key":"1463_CR201","doi-asserted-by":"publisher","first-page":"2309579121","DOI":"10.1073\/pnas.2309579121","volume":"121","author":"P Rozario","year":"2024","unstructured":"Rozario P, Pinilla M, Gorse L, Vind AC, Robinson KS, Toh GA, et al. Mechanistic basis for potassium efflux\u2013driven activation of the human NLRP1 inflammasome. Proc Natl Acad Sci USA. 2024;121:2309579121.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR202","doi-asserted-by":"publisher","first-page":"916","DOI":"10.1038\/s41590-022-01199-x","volume":"23","author":"X Yang","year":"2022","unstructured":"Yang X, Zhou J, Liu C, Qu Y, Wang W, Xiao M, et al. KSHV-encoded ORF45 activates human NLRP1 inflammasome. Nat Immunol. 2022;23:916\u201326.","journal-title":"Nat Immunol"},{"key":"1463_CR203","doi-asserted-by":"publisher","DOI":"10.1126\/science.abd0811","volume":"371","author":"S Bauernfried","year":"2021","unstructured":"Bauernfried S, Scherr MJ, Pichlmair A, Duderstadt KE, Hornung V. Human NLRP1 is a sensor for double-stranded RNA. Science. 2021;371:eabd0811.","journal-title":"Science"},{"key":"1463_CR204","doi-asserted-by":"publisher","first-page":"e1003452","DOI":"10.1371\/journal.ppat.1003452","volume":"9","author":"J Chavarr\u00eda-Smith","year":"2013","unstructured":"Chavarr\u00eda-Smith J, Vance RE. Direct proteolytic cleavage of NLRP1B is necessary and sufficient for inflammasome activation by anthrax lethal factor. PLOS Pathog. 2013;9:e1003452.","journal-title":"PLOS Pathog"},{"key":"1463_CR205","doi-asserted-by":"publisher","first-page":"240","DOI":"10.1038\/ng1724","volume":"38","author":"ED Boyden","year":"2006","unstructured":"Boyden ED, Dietrich WF. Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nat Genet. 2006;38:240\u20134.","journal-title":"Nat Genet"},{"key":"1463_CR206","doi-asserted-by":"publisher","first-page":"262","DOI":"10.1016\/j.chembiol.2017.12.013","volume":"25","author":"MC Okondo","year":"2018","unstructured":"Okondo MC, Rao SD, Taabazuing CY, Chui AJ, Poplawski SE, Johnson DC, et al. Inhibition of Dpp8\/9 activates the Nlrp1b inflammasome. Cell Chem Biol. 2018;25:262\u2013267.e5.","journal-title":"Cell Chem Biol"},{"key":"1463_CR207","doi-asserted-by":"publisher","first-page":"18864","DOI":"10.1074\/jbc.RA118.004350","volume":"293","author":"FL Zhong","year":"2018","unstructured":"Zhong FL, Robinson K, Teo D, Tan KY, Lim C, Harapas CR, et al. Human DPP9 represses NLRP1 inflammasome and protects against autoinflammatory diseases via both peptidase activity and FIIND domain binding. J Biol Chem. 2018;293:18864\u201378.","journal-title":"J Biol Chem"},{"key":"1463_CR208","doi-asserted-by":"publisher","first-page":"778","DOI":"10.1038\/s41586-021-03350-4","volume":"592","author":"LR Hollingsworth","year":"2021","unstructured":"Hollingsworth LR, Sharif H, Griswold AR, Fontana P, Mintseris J, Dagbay KB, et al. DPP9 sequesters the C-terminus of NLRP1 to repress inflammasome activation. Nature. 2021;592:778\u201383.","journal-title":"Nature"},{"key":"1463_CR209","doi-asserted-by":"publisher","first-page":"773","DOI":"10.1038\/s41586-021-03320-w","volume":"592","author":"M Huang","year":"2021","unstructured":"Huang M, Zhang X, Toh GA, Gong Q, Wang J, Han Z, et al. Structural and biochemical mechanisms of NLRP1 inhibition by DPP9. Nature. 2021;592:773\u20137.","journal-title":"Nature"},{"key":"1463_CR210","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1016\/j.cell.2016.09.001","volume":"167","author":"FL Zhong","year":"2016","unstructured":"Zhong FL, Mama\u00ef O, Sborgi L, Boussofara L, Hopkins R, Robinson K, et al. Germline NLRP1 mutations cause skin inflammatory and cancer susceptibility syndromes via inflammasome activation. Cell. 2016;167:187\u2013202.e17.","journal-title":"Cell"},{"key":"1463_CR211","doi-asserted-by":"publisher","first-page":"3820","DOI":"10.1038\/onc.2017.26","volume":"36","author":"Z Zhai","year":"2017","unstructured":"Zhai Z, Liu W, Kaur M, Luo Y, Domenico J, Samson JM, et al. NLRP1 promotes tumor growth by enhancing inflammasome activation and suppressing apoptosis in metastatic melanoma. Oncogene. 2017;36:3820\u201330.","journal-title":"Oncogene"},{"key":"1463_CR212","doi-asserted-by":"publisher","first-page":"2644","DOI":"10.1016\/j.jid.2018.07.016","volume":"138","author":"G Fenini","year":"2018","unstructured":"Fenini G, Grossi S, Contassot E, Biedermann T, Reichmann E, French LE, et al. Genome editing of human primary keratinocytes by CRISPR\/Cas9 reveals an essential role of the NLRP1 inflammasome in UVB sensing. J Invest Dermatol. 2018;138:2644\u201352.","journal-title":"J Invest Dermatol"},{"key":"1463_CR213","doi-asserted-by":"publisher","first-page":"1380","DOI":"10.1016\/j.jid.2017.10.037","volume":"138","author":"G Fenini","year":"2018","unstructured":"Fenini G, Grossi S, Gehrke S, Beer HD, Satoh TK, Contassot E, et al. The p38 mitogen-activated protein kinase critically regulates human keratinocyte inflammasome activation. J Invest Dermatol. 2018;138:1380\u201390.","journal-title":"J Invest Dermatol"},{"key":"1463_CR214","doi-asserted-by":"publisher","first-page":"30","DOI":"10.1038\/s44318-025-00637-4","volume":"45","author":"A Boegli","year":"2026","unstructured":"Boegli A, Bernard EM, Lacante L, Majeux G, Hartenian E, Mack V, et al. The NLRP6 inflammasome is activated by sterile or pathogen-induced endolysosomal damage. EMBO J. 2026;45:30\u201363.","journal-title":"EMBO J"},{"key":"1463_CR215","doi-asserted-by":"crossref","unstructured":"Bracey, NA, Platnich JM, Lau A, Chung H, Hyndman ME, MacDonald JA, et al. Tissue-selective alternate promoters guide NLRP6 expression. Life Sci Alliance. 2021;4:e202000897.","DOI":"10.26508\/lsa.202000897"},{"key":"1463_CR216","doi-asserted-by":"publisher","first-page":"281","DOI":"10.1111\/imm.13293","volume":"162","author":"D Zheng","year":"2021","unstructured":"Zheng D, Kern L, Elinav E. The NLRP6 inflammasome. Immunology. 2021;162:281\u20139.","journal-title":"Immunology"},{"key":"1463_CR217","doi-asserted-by":"publisher","first-page":"100859","DOI":"10.1016\/j.mam.2020.100859","volume":"76","author":"R Li","year":"2020","unstructured":"Li R, Zhu S. NLRP6 inflammasome. Mol Asp Med. 2020;76:100859.","journal-title":"Mol Asp Med"},{"key":"1463_CR218","doi-asserted-by":"publisher","first-page":"745","DOI":"10.1016\/j.cell.2011.04.022","volume":"145","author":"E Elinav","year":"2011","unstructured":"Elinav E, Strowig T, Kau AL, Henao-Mejia J, Thaiss CA, Booth CJ, et al. NLRP6 inflammasome regulates colonic microbial ecology and risk for colitis. Cell. 2011;145:745\u201357.","journal-title":"Cell"},{"key":"1463_CR219","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1038\/nature10809","volume":"482","author":"J Henao-Mejia","year":"2012","unstructured":"Henao-Mejia J, Elinav E, Jin C, Hao L, Mehal WZ, Strowig T, et al. Inflammasome-mediated dysbiosis regulates progression of NAFLD and obesity. Nature. 2012;482:179\u201385.","journal-title":"Nature"},{"key":"1463_CR220","doi-asserted-by":"publisher","first-page":"1045","DOI":"10.1016\/j.cell.2014.01.026","volume":"156","author":"M Wlodarska","year":"2014","unstructured":"Wlodarska M, Thaiss CA, Nowarski R, Henao-Mejia J, Zhang JP, Brown EM, et al. NLRP6 inflammasome orchestrates the colonic host\u2013microbe interface by regulating goblet cell mucus secretion. Cell. 2014;156:1045\u201359.","journal-title":"Cell"},{"key":"1463_CR221","doi-asserted-by":"publisher","first-page":"1428","DOI":"10.1016\/j.cell.2015.10.048","volume":"163","author":"M Levy","year":"2015","unstructured":"Levy M, Thaiss CA, Zeevi D, Dohnalov\u00e1 L, Zilberman-Schapira G, Mahdi JA, et al. Microbiota-modulated metabolites shape the intestinal microenvironment by regulating NLRP6 inflammasome signaling. Cell. 2015;163:1428\u201343.","journal-title":"Cell"},{"key":"1463_CR222","doi-asserted-by":"publisher","first-page":"603","DOI":"10.1016\/j.immuni.2018.04.002","volume":"48","author":"E Elinav","year":"2018","unstructured":"Elinav E, Henao-Mejia J, Strowig T, Flavell R. NLRP6 and dysbiosis: avoiding the luring attraction of over-simplification. Immunity. 2018;48:603\u20134.","journal-title":"Immunity"},{"key":"1463_CR223","doi-asserted-by":"publisher","first-page":"339","DOI":"10.1016\/j.immuni.2017.07.011","volume":"47","author":"M Mamantopoulos","year":"2017","unstructured":"Mamantopoulos M, Ronchi F, Van Hauwermeiren F, Vieira-Silva S, Yilmaz B, Martens L, et al. Nlrp6- and ASC-dependent inflammasomes do not shape the commensal gut microbiota composition. Immunity. 2017;47:339\u201348.e4.","journal-title":"Immunity"},{"key":"1463_CR224","doi-asserted-by":"publisher","first-page":"3653","DOI":"10.1016\/j.celrep.2017.12.026","volume":"21","author":"P Lemire","year":"2017","unstructured":"Lemire P, Robertson SJ, Maughan H, Tattoli I, Streutker CJ, Platnich JM, et al. The NLR protein NLRP6 does not impact gut microbiota composition. Cell Rep. 2017;21:3653\u201361.","journal-title":"Cell Rep"},{"key":"1463_CR225","doi-asserted-by":"publisher","first-page":"5759","DOI":"10.1016\/j.cell.2021.09.032","volume":"184","author":"C Shen","year":"2021","unstructured":"Shen C, Li R, Negro R, Cheng J, Vora SM, Fu TM, et al. Phase separation drives RNA virus-induced activation of the NLRP6 inflammasome. Cell. 2021;184:5759\u20135774.e20.","journal-title":"Cell"},{"key":"1463_CR226","doi-asserted-by":"publisher","first-page":"109205","DOI":"10.1016\/j.celrep.2021.109205","volume":"35","author":"J Xing","year":"2021","unstructured":"Xing J, Zhou X, Fang M, Zhang E, Minze LJ, Zhang Z. DHX15 is required to control RNA virus-induced intestinal inflammation. Cell Rep. 2021;35:109205.","journal-title":"Cell Rep"},{"key":"1463_CR227","doi-asserted-by":"publisher","first-page":"826","DOI":"10.1126\/science.aab3145","volume":"350","author":"P Wang","year":"2015","unstructured":"Wang P, Zhu S, Yang L, Cui S, Pan W, Jackson R, et al. Nlrp6 regulates intestinal antiviral innate immunity. Science. 2015;350:826\u201330.","journal-title":"Science"},{"key":"1463_CR228","doi-asserted-by":"publisher","first-page":"1651","DOI":"10.1016\/j.cell.2018.09.047","volume":"175","author":"H Hara","year":"2018","unstructured":"Hara H, Seregin SS, Yang D, Fukase K, Chamaillard M, Alnemri ES, et al. The NLRP6 inflammasome recognizes lipoteichoic acid and regulates gram-positive pathogen infection. Cell. 2018;175:1651\u20131664.e14.","journal-title":"Cell"},{"key":"1463_CR229","doi-asserted-by":"publisher","first-page":"2885","DOI":"10.1016\/j.jid.2021.02.745","volume":"141","author":"S-H Yoon","year":"2021","unstructured":"Yoon S-H, Hwang I, Lee E, Cho HJ, Ryu JH, Kim TG, et al. Antimicrobial peptide LL-37 drives rosacea-like skin inflammation in an NLRP3-dependent manner. J Invest Dermatol. 2021;141:2885\u20132894.e5.","journal-title":"J Invest Dermatol"},{"key":"1463_CR230","doi-asserted-by":"publisher","first-page":"485","DOI":"10.1016\/j.bbrc.2020.05.171","volume":"528","author":"X Ji","year":"2020","unstructured":"Ji X, Li L, Lu P, Li X, Tian D, Liu M. NLRP6 exerts a protective role via NF-kB with involvement of CCL20 in a mouse model of alcoholic hepatitis. Biochem Biophys Res Commun. 2020;528:485\u201392.","journal-title":"Biochem Biophys Res Commun"},{"key":"1463_CR231","doi-asserted-by":"publisher","first-page":"389","DOI":"10.1038\/nature11250","volume":"488","author":"PK Anand","year":"2012","unstructured":"Anand PK, Malireddi RK, Lukens JR, Vogel P, Bertin J, Lamkanfi M, et al. NLRP6 negatively regulates innate immunity and host defense against bacterial pathogens. Nature. 2012;488:389\u201393.","journal-title":"Nature"},{"key":"1463_CR232","doi-asserted-by":"publisher","first-page":"999","DOI":"10.1111\/iej.13091","volume":"52","author":"WL Lu","year":"2019","unstructured":"Lu WL, Zhang L, Song DZ, Yi XW, Xu WZ, Ye L, et al. NLRP6 suppresses the inflammatory response of human periodontal ligament cells by inhibiting NF-\u03baB and ERK signaling pathways. Int Endod J. 2019;52:999\u20131009.","journal-title":"Int Endod J"},{"key":"1463_CR233","doi-asserted-by":"publisher","first-page":"105740","DOI":"10.1016\/j.intimp.2019.105740","volume":"74","author":"M Li","year":"2019","unstructured":"Li M, Chen Y, Shi J, Ju W, Qi K, Fu C, et al. NLRP6 deficiency aggravates liver injury after allogeneic hematopoietic stem cell transplantation. Int Immunopharmacol. 2019;74:105740.","journal-title":"Int Immunopharmacol"},{"key":"1463_CR234","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1016\/j.exer.2018.07.001","volume":"176","author":"H Chen","year":"2018","unstructured":"Chen H, Li Y, Gu J, Yin L, Bian F, Su L, et al. TLR4-MyD88 pathway promotes the imbalanced activation of NLRP3\/NLRP6 via caspase-8 stimulation after alkali burn injury. Exp Eye Res. 2018;176:59\u201368.","journal-title":"Exp Eye Res"},{"key":"1463_CR235","doi-asserted-by":"publisher","first-page":"1376","DOI":"10.1101\/gr.1053803","volume":"13","author":"JC Reed","year":"2003","unstructured":"Reed JC, Doctor K, Rojas A, Zapata JM, Stehlik C, Fiorentino L, et al. Comparative analysis of apoptosis and inflammation genes of mice and humans. Genome Res. 2003;13:1376\u201388.","journal-title":"Genome Res"},{"key":"1463_CR236","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-017-02073-3","volume":"8","author":"C Wu","year":"2017","unstructured":"Wu C, Su Z, Lin M, Ou J, Zhao W, Cui J, et al. NLRP11 attenuates Toll-like receptor signaling by targeting TRAF6 for degradation via the ubiquitin ligase RNF19A. Nat Commun. 2017;8:1977.","journal-title":"Nat Commun"},{"key":"1463_CR237","doi-asserted-by":"publisher","first-page":"2160","DOI":"10.15252\/embr.201744480","volume":"18","author":"Y Qin","year":"2017","unstructured":"Qin Y, Su Z, Wu Y, Wu C, Jin S, Xie W, et al. NLRP11 disrupts MAVS signalosome to inhibit type I interferon signaling and virus-induced apoptosis. EMBO Rep. 2017;18:2160\u201371.","journal-title":"EMBO Rep"},{"key":"1463_CR238","doi-asserted-by":"publisher","first-page":"2701","DOI":"10.1074\/jbc.RA117.000152","volume":"293","author":"K Ellwanger","year":"2018","unstructured":"Ellwanger K, Becker E, Kienes I, Sowa A, Postma Y, Cardona Gloria Y, et al. The NLR family pyrin domain-containing 11 protein contributes to the regulation of inflammatory signaling. J Biol Chem. 2018;293:2701\u201310.","journal-title":"J Biol Chem"},{"key":"1463_CR239","doi-asserted-by":"publisher","first-page":"892","DOI":"10.1038\/s41590-022-01220-3","volume":"23","author":"A Gangopadhyay","year":"2022","unstructured":"Gangopadhyay A, Devi S, Tenguria S, Carriere J, Nguyen H, J\u00e4ger E, et al. NLRP3 licenses NLRP11 for inflammasome activation in human macrophages. Nat Immunol. 2022;23:892\u2013903.","journal-title":"Nat Immunol"},{"key":"1463_CR240","doi-asserted-by":"publisher","first-page":"653883","DOI":"10.3389\/fimmu.2021.653883","volume":"12","author":"I Kienes","year":"2021","unstructured":"Kienes I, Bauer S, Gottschild C, Mirza N, Pfannstiel J, Schr\u00f6der M, et al. DDX3X links NLRP11 to the regulation of type I interferon responses and NLRP3 inflammasome activation. Front Immunol. 2021;12:653883.","journal-title":"Front Immunol"},{"key":"1463_CR241","doi-asserted-by":"publisher","first-page":"e0081825","DOI":"10.1128\/mbio.00818-25","volume":"16","author":"M Szczerba","year":"2025","unstructured":"Szczerba M, Ganesh A, Gil-Marqu\u00e9s ML, Briken V, Goldberg MB. NLRP11 is required for canonical NLRP3 and noncanonical inflammasome activation during human macrophage infection with mycobacteria. mBio. 2025;16:e0081825.","journal-title":"mBio"},{"key":"1463_CR242","doi-asserted-by":"publisher","first-page":"4767","DOI":"10.1126\/sciimmunol.abo4767","volume":"8","author":"M Rojas-Lopez","year":"2023","unstructured":"Rojas-Lopez M, Gil-Marqu\u00e9s ML, Kharbanda V, Zajac AS, Miller KA, Wood TE, et al. NLRP11 is a pattern recognition receptor for bacterial lipopolysaccharide in the cytosol of human macrophages. Sci Immunol. 2023;8:4767.","journal-title":"Sci Immunol"},{"key":"1463_CR243","doi-asserted-by":"publisher","first-page":"1418290","DOI":"10.3389\/fimmu.2024.1418290","volume":"15","author":"B Wei","year":"2024","unstructured":"Wei B, Billman ZP, Nozaki K, Goodridge HS, Miao EA. NLRP3, NLRP6, and NLRP12 are inflammasomes with distinct expression patterns. Front Immunol. 2024;15:1418290.","journal-title":"Front Immunol"},{"key":"1463_CR244","doi-asserted-by":"publisher","first-page":"29874","DOI":"10.1074\/jbc.M203915200","volume":"277","author":"L Wang","year":"2002","unstructured":"Wang L, Manji GA, Grenier JM, Al-Garawi A, Merriam S, Lora JM, et al. PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates activation of NF-\u03baB and Caspase-1-dependent cytokine processing. J Biol Chem. 2002;277:29874\u201380.","journal-title":"J Biol Chem"},{"key":"1463_CR245","doi-asserted-by":"publisher","first-page":"5354","DOI":"10.4049\/jimmunol.170.11.5354","volume":"170","author":"KL Williams","year":"2003","unstructured":"Williams KL, Taxman DJ, Linhoff MW, Reed W, Ting JP-Y. Cutting edge: Monarch-1: a pyrin\/nucleotide-binding domain\/leucine-rich repeat protein that controls classical and nonclassical MHC class I genes. J Immunol. 2003;170:5354\u20138.","journal-title":"J Immunol"},{"key":"1463_CR246","doi-asserted-by":"publisher","first-page":"742","DOI":"10.1016\/j.immuni.2012.03.012","volume":"36","author":"IC Allen","year":"2012","unstructured":"Allen IC, Wilson JE, Schneider M, Lich JD, Roberts RA, Arthur JC, et al. NLRP12 suppresses colon inflammation and tumorigenesis through the negative regulation of noncanonical NF-\u03baB signaling. Immunity. 2012;36:742\u201354.","journal-title":"Immunity"},{"key":"1463_CR247","doi-asserted-by":"publisher","first-page":"39914","DOI":"10.1074\/jbc.M502820200","volume":"280","author":"KL Williams","year":"2005","unstructured":"Williams KL, Lich JD, Duncan JA, Reed W, Rallabhandi P, Moore C, et al. The CATERPILLER Protein Monarch-1 is an antagonist of toll-like receptor-, tumor necrosis factor \u03b1-, and Mycobacterium tuberculosis-induced pro-inflammatory signals. J Biol Chem. 2005;280:39914\u201324.","journal-title":"J Biol Chem"},{"key":"1463_CR248","doi-asserted-by":"crossref","unstructured":"Arthur JC, Lich JD, Aziz RK, Kotb M, Ting J P-Y. Heat shock protein 90 associates with monarch-1 and regulates its ability to promote degradation of NF-kappaB-inducing kinase. J. Immunol. 2007;179:6291\u20136.","DOI":"10.4049\/jimmunol.179.9.6291"},{"key":"1463_CR249","doi-asserted-by":"publisher","first-page":"1256","DOI":"10.4049\/jimmunol.178.3.1256","volume":"178","author":"JD Lich","year":"2007","unstructured":"Lich JD, Williams KL, Moore CB, Arthur JC, Davis BK, Taxman DJ, et al. Cutting edge: Monarch-1 suppresses non-canonical NF-\u03baB activation and p52-dependent chemokine expression in monocytes. J Immunol. 2007;178:1256\u201360.","journal-title":"J Immunol"},{"key":"1463_CR250","doi-asserted-by":"publisher","first-page":"649","DOI":"10.1016\/j.ccr.2011.10.022","volume":"20","author":"MH Zaki","year":"2011","unstructured":"Zaki MH, Vogel P, Malireddi RK, Body-Malapel M, Anand PK, Bertin J, et al. The NOD-like receptor NLRP12 attenuates colon inflammation and tumorigenesis. Cancer Cell. 2011;20:649\u201360.","journal-title":"Cancer Cell"},{"key":"1463_CR251","doi-asserted-by":"publisher","first-page":"385","DOI":"10.1073\/pnas.1317643111","volume":"111","author":"MDH Zaki","year":"2014","unstructured":"Zaki MDH, Man SM, Vogel P, Lamkanfi M, Kanneganti T-D. Salmonella exploits NLRP12-dependent innate immune signaling to suppress host defenses during infection. Proc Natl Acad Sci USA. 2014;111:385\u201390.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR252","doi-asserted-by":"publisher","first-page":"1614","DOI":"10.1073\/pnas.0708616105","volume":"105","author":"I J\u00e9ru","year":"2008","unstructured":"J\u00e9ru I, Duquesnoy P, Fernandes-Alnemri T, Cochet E, Yu JW, Lackmy-Port-Lis M, et al. Mutations in NALP12 cause hereditary periodic fever syndromes. Proc Natl Acad Sci USA. 2008;105:1614\u20139.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR253","doi-asserted-by":"publisher","first-page":"96","DOI":"10.1016\/j.immuni.2012.07.006","volume":"37","author":"GI Vladimer","year":"2012","unstructured":"Vladimer GI, Weng D, Paquette SW, Vanaja SK, Rathinam VA, Aune MH, et al. The NLRP12 inflammasome recognizes Yersinia pestis. Immunity. 2012;37:96\u2013107.","journal-title":"Immunity"},{"key":"1463_CR254","doi-asserted-by":"publisher","first-page":"e60842","DOI":"10.1371\/journal.pone.0060842","volume":"8","author":"IC Allen","year":"2013","unstructured":"Allen IC, McElvania-TeKippe E, Wilson JE, Lich JD, Arthur JC, Sullivan JT, et al. Characterization of NLRP12 during the in vivo host immune response to Klebsiella pneumoniae and Mycobacterium tuberculosis. PLOS One. 2013;8:e60842.","journal-title":"PLOS One"},{"key":"1463_CR255","doi-asserted-by":"crossref","unstructured":"Li, X, Dong Z, Liu Y, Song W, Pu J, Jiang G, et al. A novel role for the regulatory nod-like receptor NLRP12 in anti-dengue virus response. Front Immunol. 2021;12:744880 .","DOI":"10.3389\/fimmu.2021.744880"},{"key":"1463_CR256","doi-asserted-by":"publisher","first-page":"1003885","DOI":"10.1371\/journal.ppat.1003885","volume":"10","author":"MA Ataide","year":"2014","unstructured":"Ataide MA, Andrade WA, Zamboni DS, Wang D, Souza Mdo C, Franklin BS, et al. Malaria-induced NLRP12\/NLRP3-dependent caspase-1 activation mediates inflammation and hypersensitivity to bacterial superinfection. PLoS Pathog. 2014;10:1003885.","journal-title":"PLoS Pathog"},{"key":"1463_CR257","doi-asserted-by":"publisher","first-page":"2783","DOI":"10.1016\/j.cell.2023.05.005","volume":"186","author":"B Sundaram","year":"2023","unstructured":"Sundaram B, Pandian N, Mall R, Wang Y, Sarkar R, Kim HJ, et al. NLRP12-PANoptosome activates PANoptosis and pathology in response to heme and PAMPs. Cell. 2023;186:2783\u20132801.e20.","journal-title":"Cell"},{"key":"1463_CR258","doi-asserted-by":"publisher","first-page":"4061","DOI":"10.1016\/j.cell.2024.05.034","volume":"187","author":"B Sundaram","year":"2024","unstructured":"Sundaram B, Pandian N, Kim HJ, Abdelaal HM, Mall R, Indari O, et al. NLRC5 senses NAD+ depletion, forming a PANoptosome and driving PANoptosis and inflammation. Cell. 2024;187:4061\u20134077.e17.","journal-title":"Cell"},{"key":"1463_CR259","doi-asserted-by":"publisher","first-page":"8145","DOI":"10.1126\/scisignal.abg8145","volume":"17","author":"JR Coombs","year":"2024","unstructured":"Coombs JR, Zamoshnikova A, Holley CL, Maddugoda MP, Teo D, Chauvin C, et al. NLRP12 interacts with NLRP3 to block the activation of the human NLRP3 inflammasome. Sci Signal. 2024;17:8145.","journal-title":"Sci Signal"},{"key":"1463_CR260","doi-asserted-by":"publisher","first-page":"1057","DOI":"10.1126\/science.1169841","volume":"323","author":"TL Roberts","year":"2009","unstructured":"Roberts TL, Idris A, Dunn JA, Kelly GM, Burnton CM, Hodgson S, et al. HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA. Science. 2009;323:1057\u201360.","journal-title":"Science"},{"key":"1463_CR261","doi-asserted-by":"publisher","first-page":"509","DOI":"10.1038\/nature07710","volume":"458","author":"T Fernandes-Alnemri","year":"2009","unstructured":"Fernandes-Alnemri T, Yu J-W, Datta P, Wu J, Alnemri ES. AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA. Nature. 2009;458:509\u201313.","journal-title":"Nature"},{"key":"1463_CR262","doi-asserted-by":"publisher","first-page":"514","DOI":"10.1038\/nature07725","volume":"458","author":"V Hornung","year":"2009","unstructured":"Hornung V, Ablasser A, Charrel-Dennis M, Bauernfeind F, Horvath G, Caffrey DR, et al. AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC. Nature. 2009;458:514\u20138.","journal-title":"Nature"},{"key":"1463_CR263","doi-asserted-by":"publisher","first-page":"266","DOI":"10.1038\/ni.1702","volume":"10","author":"T B\u00fcrckst\u00fcmmer","year":"2009","unstructured":"B\u00fcrckst\u00fcmmer T, Baumann C, Bl\u00fcml S, Dixit E, D\u00fcrnberger G, Jahn H, et al. An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome. Nat Immunol. 2009;10:266\u201372.","journal-title":"Nat Immunol"},{"key":"1463_CR264","doi-asserted-by":"publisher","first-page":"561","DOI":"10.1016\/j.immuni.2012.02.014","volume":"36","author":"T Jin","year":"2012","unstructured":"Jin T, Perry A, Jiang J, Smith P, Curry JA, Unterholzner L, et al. Structures of the HIN domain:DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor. Immunity. 2012;36:561\u201371.","journal-title":"Immunity"},{"key":"1463_CR265","doi-asserted-by":"publisher","first-page":"13225","DOI":"10.1074\/jbc.M113.468033","volume":"288","author":"T Jin","year":"2013","unstructured":"Jin T, Perry A, Smith P, Jiang J, Xiao TS. Structure of the absent in melanoma 2 (AIM2) pyrin domain provides insights into the mechanisms of AIM2 autoinhibition and inflammasome assembly. J Biol Chem. 2013;288:13225\u201335.","journal-title":"J Biol Chem"},{"key":"1463_CR266","doi-asserted-by":"publisher","first-page":"1420","DOI":"10.1016\/j.jmb.2013.12.029","volume":"426","author":"A Lu","year":"2014","unstructured":"Lu A, Kabaleeswaran V, Fu T, Magupalli VG, Wu H. Crystal structure of the F27G AIM2 PYD mutant and similarities of its self-association to DED\/DED interactions. J Mol Biol. 2014;426:1420\u20137.","journal-title":"J Mol Biol"},{"key":"1463_CR267","doi-asserted-by":"publisher","first-page":"15013","DOI":"10.1038\/celldisc.2015.13","volume":"1","author":"A Lu","year":"2015","unstructured":"Lu A, Li Y, Yin Q, Ruan J, Yu X, Egelman E, et al. Plasticity in PYD assembly revealed by cryo-EM structure of the PYD filament of AIM2. Cell Discov. 2015;1:15013.","journal-title":"Cell Discov"},{"key":"1463_CR268","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms8827","volume":"6","author":"SR Morrone","year":"2015","unstructured":"Morrone SR, Matyszewski M, Yu X, Delannoy M, Egelman EH, Sohn J. Assembly driven activation of the AIM2 foreign-dsDNA sensor provides a polymerization template for downstream ASC. Nat Commun. 2015;6:7827.","journal-title":"Nat Commun"},{"key":"1463_CR269","doi-asserted-by":"publisher","first-page":"385","DOI":"10.1038\/ni.1859","volume":"11","author":"T Fernandes-Alnemri","year":"2010","unstructured":"Fernandes-Alnemri T, Yu JW, Juliana C, Solorzano L, Kang S, Wu J, et al. The AIM2 inflammasome is critical for innate immunity to Francisella tularensis. Nat Immunol. 2010;11:385\u201393.","journal-title":"Nat Immunol"},{"key":"1463_CR270","doi-asserted-by":"publisher","first-page":"395","DOI":"10.1038\/ni.1864","volume":"11","author":"VA Rathinam","year":"2010","unstructured":"Rathinam VA, Jiang Z, Waggoner SN, Sharma S, Cole LE, Waggoner L, et al. The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses. Nat Immunol. 2010;11:395\u2013402.","journal-title":"Nat Immunol"},{"key":"1463_CR271","doi-asserted-by":"publisher","first-page":"467","DOI":"10.1038\/ni.3118","volume":"16","author":"SM Man","year":"2015","unstructured":"Man SM, Karki R, Malireddi RK, Neale G, Vogel P, Yamamoto M, et al. The transcription factor IRF1 and guanylate-binding proteins target activation of the AIM2 inflammasome by Francisella infection. Nat Immunol. 2015;16:467\u201375.","journal-title":"Nat Immunol"},{"key":"1463_CR272","doi-asserted-by":"publisher","first-page":"196","DOI":"10.1016\/j.celrep.2013.12.014","volume":"6","author":"P Kalantari","year":"2014","unstructured":"Kalantari P, DeOliveira RB, Chan J, Corbett Y, Rathinam V, Stutz A, et al. Dual engagement of the NLRP3 and AIM2 inflammasomes by plasmodium-derived hemozoin and DNA during malaria. Cell Rep. 2014;6:196\u2013210.","journal-title":"Cell Rep"},{"key":"1463_CR273","doi-asserted-by":"publisher","first-page":"9771","DOI":"10.1073\/pnas.1003738107","volume":"107","author":"JW Jones","year":"2010","unstructured":"Jones JW, Kayagaki N, Broz P, Henry T, Newton K, O'Rourke K, et al. Absent in melanoma 2 is required for innate immune recognition of Francisella tularensis. Proc Natl Acad Sci USA. 2010;107:9771\u20136.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR274","doi-asserted-by":"publisher","first-page":"412","DOI":"10.1016\/j.chom.2010.04.004","volume":"7","author":"J-D Sauer","year":"2010","unstructured":"Sauer J-D, Witte CE, Zemansky J, Hanson B, Lauer P, Portnoy DA. Listeria monocytogenes triggers AIM2-mediated pyroptosis upon infrequent bacteriolysis in the macrophage cytosol. Cell Host Microbe. 2010;7:412\u20139.","journal-title":"Cell Host Microbe"},{"key":"1463_CR275","doi-asserted-by":"publisher","first-page":"818","DOI":"10.4049\/jimmunol.1000724","volume":"185","author":"SE Warren","year":"2010","unstructured":"Warren SE, Armstrong A, Hamilton MK, Mao DP, Leaf IA, Miao EA, et al. Cutting edge: cytosolic bacterial DNA activates the inflammasome via Aim2. J Immunol. 2010;185:818\u201321.","journal-title":"J Immunol"},{"key":"1463_CR276","doi-asserted-by":"publisher","first-page":"925","DOI":"10.1007\/s10875-013-9881-6","volume":"33","author":"W Zhang","year":"2013","unstructured":"Zhang W, Cai Y, Xu W, Yin Z, Gao X, Xiong S. AIM2 facilitates the apoptotic DNA-induced systemic lupus erythematosus by arbitrating macrophage functional maturation. J Clin Immunol. 2013;33:925\u201337.","journal-title":"J Clin Immunol"},{"key":"1463_CR277","doi-asserted-by":"publisher","first-page":"102381","DOI":"10.1016\/j.jaut.2019.102381","volume":"108","author":"AG Vakrakou","year":"2020","unstructured":"Vakrakou AG, Svolaki IP, Evangelou K, Gorgoulis VG, Manoussakis MN. Cell-autonomous epithelial activation of AIM2 (absent in melanoma-2) inflammasome by cytoplasmic DNA accumulations in primary Sj\u00f6gren\u2019s syndrome. J Autoimmun. 2020;108:102381.","journal-title":"J Autoimmun"},{"key":"1463_CR278","doi-asserted-by":"publisher","first-page":"45","DOI":"10.1016\/j.cell.2015.06.001","volume":"162","author":"SM Man","year":"2015","unstructured":"Man SM, Zhu Q, Zhu L, Liu Z, Karki R, Malik A, et al. Critical role for the DNA sensor AIM2 in stem cell proliferation and cancer. Cell. 2015;162:45\u201358.","journal-title":"Cell"},{"key":"1463_CR279","doi-asserted-by":"publisher","first-page":"906","DOI":"10.1038\/nm.3908","volume":"21","author":"JE Wilson","year":"2015","unstructured":"Wilson JE, Petrucelli AS, Chen L, Koblansky AA, Truax AD, Oyama Y, et al. Inflammasome-independent role of AIM2 in suppressing colon tumorigenesis via DNA-PK and Akt. Nat Med. 2015;21:906\u201313.","journal-title":"Nat Med"},{"key":"1463_CR280","doi-asserted-by":"publisher","first-page":"1838","DOI":"10.1002\/ijc.24905","volume":"126","author":"G Patsos","year":"2010","unstructured":"Patsos G, Germann A, Gebert J, Dihlmann S. Restoration of absent in melanoma 2 (AIM2) induces G2\/M cell cycle arrest and promotes invasion of colorectal cancer cells. Int J Cancer. 2010;126:1838\u201349.","journal-title":"Int J Cancer"},{"key":"1463_CR281","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1158\/1535-7163.MCT-05-0310","volume":"5","author":"I-F Chen","year":"2006","unstructured":"Chen I-F, Ou-Yang F, Hung JY, Liu JC, Wang H, Wang SC, et al. AIM2 suppresses human breast cancer cell proliferation in vitro and mammary tumor growth in a mouse model. Mol Cancer Ther. 2006;5:1\u20137.","journal-title":"Mol Cancer Ther"},{"key":"1463_CR282","doi-asserted-by":"publisher","first-page":"2997","DOI":"10.1002\/ijc.31827","volume":"143","author":"C Mart\u00ednez-Cardona","year":"2018","unstructured":"Mart\u00ednez-Cardona C, Lozano-Ruiz B, Bachiller V, Peir\u00f3 G, Algaba-Chueca F, G\u00f3mez-Hurtado I, et al. AIM2 deficiency reduces the development of hepatocellular carcinoma in mice. Int J Cancer. 2018;143:2997\u20133007.","journal-title":"Int J Cancer"},{"key":"1463_CR283","doi-asserted-by":"publisher","first-page":"2707","DOI":"10.1038\/s41388-020-1176-9","volume":"39","author":"M Qi","year":"2020","unstructured":"Qi M, Dai D, Liu J, Li Z, Liang P, Wang Y, et al. AIM2 promotes the development of non-small cell lung cancer by modulating mitochondrial dynamics. Oncogene. 2020;39:2707\u201323.","journal-title":"Oncogene"},{"key":"1463_CR284","doi-asserted-by":"publisher","first-page":"306","DOI":"10.1111\/cas.15584","volume":"114","author":"J-Q Zheng","year":"2023","unstructured":"Zheng J-Q, Lin CH, Lee HH, Chang WM, Li LJ, Su CY, et al. AIM2 upregulation promotes metastatic progression and PD-L1 expression in lung adenocarcinoma. Cancer Sci. 2023;114:306\u201320.","journal-title":"Cancer Sci"},{"key":"1463_CR285","doi-asserted-by":"publisher","first-page":"357","DOI":"10.1016\/j.chom.2015.01.006","volume":"17","author":"R Karki","year":"2015","unstructured":"Karki R, Man SM, Malireddi R, Gurung P, Vogel P, Lamkanfi M, et al. Concerted activation of the AIM2 and the NLRP3 inflammasome orchestrates host protection against Aspergillus infection. Cell Host Microbe. 2015;17:357\u201368.","journal-title":"Cell Host Microbe"},{"key":"1463_CR286","doi-asserted-by":"publisher","first-page":"1919","DOI":"10.1073\/pnas.0608745104","volume":"104","author":"P Parroche","year":"2007","unstructured":"Parroche P, Lauw FN, Goutagny N, Latz E, Monks BG, Visintin A, et al. Malaria hemozoin is immunologically inert but radically enhances innate responses by presenting malaria DNA to Toll-like receptor 9. Proc Natl Acad Sci USA. 2007;104:1919\u201324.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR287","doi-asserted-by":"publisher","first-page":"476","DOI":"10.1038\/ni.3119","volume":"16","author":"E Meunier","year":"2015","unstructured":"Meunier E, Wallet P, Dreier RF, Costanzo S, Anton L, R\u00fchl S, et al. Guanylate-binding proteins promote activation of the AIM2 inflammasome during infection with Francisella novicida. Nat Immunol. 2015;16:476\u201384.","journal-title":"Nat Immunol"},{"key":"1463_CR288","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-022-32127-0","volume":"13","author":"S Feng","year":"2022","unstructured":"Feng S, Enosi Tuipulotu D, Pandey A, Jing W, Shen C, Ngo C, et al. Pathogen-selective killing by guanylate-binding proteins as a molecular mechanism leading to inflammasome signaling. Nat Commun. 2022;13:4395.","journal-title":"Nat Commun"},{"key":"1463_CR289","doi-asserted-by":"publisher","first-page":"382","DOI":"10.1016\/j.cell.2016.09.012","volume":"167","author":"SM Man","year":"2016","unstructured":"Man SM, Karki R, Sasai M, Place DE, Kesavardhana S, Temirov J, et al. IRGB10 liberates bacterial ligands for sensing by the AIM2 and Caspase-11-NLRP3 inflammasomes. Cell. 2016;167:382\u2013396.e17.","journal-title":"Cell"},{"key":"1463_CR290","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-017-02682-y","volume":"9","author":"B Lagrange","year":"2018","unstructured":"Lagrange B, Benaoudia S, Wallet P, Magnotti F, Provost A, Michal F, et al. Human caspase-4 detects tetra-acylated LPS and cytosolic Francisella and functions differently from murine caspase-11. Nat Commun. 2018;9:242.","journal-title":"Nat Commun"},{"key":"1463_CR291","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1016\/j.cell.2023.11.044","volume":"187","author":"K Newton","year":"2024","unstructured":"Newton K, Strasser A, Kayagaki N, Dixit VM. Cell death. Cell. 2024;187:235\u201356.","journal-title":"Cell"},{"key":"1463_CR292","doi-asserted-by":"publisher","first-page":"379","DOI":"10.1038\/s41580-023-00689-6","volume":"25","author":"J Yuan","year":"2024","unstructured":"Yuan J, Ofengeim D. A guide to cell death pathways. Nat Rev Mol Cell Biol. 2024;25:379\u201395.","journal-title":"Nat Rev Mol Cell Biol"},{"key":"1463_CR293","doi-asserted-by":"publisher","unstructured":"Vince JE, Silke J. The PANoptosis hypothesis examined. Nat Rev Mol Cell Biol. 2026;1\u20132. https:\/\/doi.org\/10.1038\/s41580-026-00970-4.","DOI":"10.1038\/s41580-026-00970-4"},{"key":"1463_CR294","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1038\/s41418-017-0012-4","volume":"25","author":"L Galluzzi","year":"2018","unstructured":"Galluzzi L, Vitale I, Aaronson SA, Abrams JM, Adam D, Agostinis P, et al. Molecular mechanisms of cell death: recommendations of the Nomenclature Committee on Cell Death 2018. Cell Death Differ. 2018;25:486\u2013541.","journal-title":"Cell Death Differ"},{"key":"1463_CR295","doi-asserted-by":"publisher","first-page":"647","DOI":"10.1038\/nrc883","volume":"2","author":"S Cory","year":"2002","unstructured":"Cory S, Adams JM. The Bcl2 family: regulators of the cellular life-or-death switch. Nat Rev Cancer. 2002;2:647\u201356.","journal-title":"Nat Rev Cancer"},{"key":"1463_CR296","doi-asserted-by":"publisher","first-page":"1389","DOI":"10.1016\/S1097-2765(00)00136-2","volume":"6","author":"T Lindsten","year":"2000","unstructured":"Lindsten T, Ross AJ, King A, Zong WX, Rathmell JC, Shiels HA, et al. The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues. Mol Cell. 2000;6:1389\u201399.","journal-title":"Mol Cell"},{"key":"1463_CR297","doi-asserted-by":"publisher","first-page":"65","DOI":"10.1038\/cdd.2017.186","volume":"25","author":"J Kale","year":"2018","unstructured":"Kale J, Osterlund EJ, Andrews DW. BCL-2 family proteins: changing partners in the dance toward death. Cell Death Differ. 2018;25:65\u201380.","journal-title":"Cell Death Differ"},{"key":"1463_CR298","doi-asserted-by":"publisher","first-page":"a041046","DOI":"10.1101\/cshperspect.a041046","volume":"14","author":"DR Green","year":"2022","unstructured":"Green DR. The mitochondrial pathway of apoptosis part II: the BCL-2 protein family. Cold Spring Harb Perspect Biol. 2022;14:a041046.","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"1463_CR299","doi-asserted-by":"publisher","first-page":"405","DOI":"10.1016\/S0092-8674(00)80501-2","volume":"90","author":"H Zou","year":"1997","unstructured":"Zou H, Henzel WJ, Liu X, Lutschg A, Wang X. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell. 1997;90:405\u201313.","journal-title":"Cell"},{"key":"1463_CR300","doi-asserted-by":"publisher","first-page":"11549","DOI":"10.1074\/jbc.274.17.11549","volume":"274","author":"H Zou","year":"1999","unstructured":"Zou H, Li Y, Liu X, Wang X. An APAF-1\u00b7cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9*. J Biol Chem. 1999;274:11549\u201356.","journal-title":"J Biol Chem"},{"key":"1463_CR301","doi-asserted-by":"publisher","first-page":"1380","DOI":"10.1038\/cdd.2017.44","volume":"24","author":"O Julien","year":"2017","unstructured":"Julien O, Wells JA. Caspases and their substrates. Cell Death Differ. 2017;24:1380\u20139.","journal-title":"Cell Death Differ"},{"key":"1463_CR302","doi-asserted-by":"publisher","first-page":"847","DOI":"10.1126\/science.1115035","volume":"311","author":"SA Lakhani","year":"2006","unstructured":"Lakhani SA, Masud A, Kuida K, Porter GA JR, Booth CJ, Mehal WZ, et al. Caspases 3 and 7: key mediators of mitochondrial events of apoptosis. Science. 2006;311:847\u201351.","journal-title":"Science"},{"key":"1463_CR303","doi-asserted-by":"publisher","first-page":"355","DOI":"10.1016\/S0092-8674(00)81874-7","volume":"88","author":"S Nagata","year":"1997","unstructured":"Nagata S. Apoptosis by death factor. Cell. 1997;88:355\u201365.","journal-title":"Cell"},{"key":"1463_CR304","doi-asserted-by":"publisher","first-page":"789","DOI":"10.1038\/35037728","volume":"407","author":"PH Krammer","year":"2000","unstructured":"Krammer PH. CD95\u2019s deadly mission in the immune system. Nature. 2000;407:789\u201395.","journal-title":"Nature"},{"key":"1463_CR305","doi-asserted-by":"publisher","first-page":"418","DOI":"10.1016\/j.cub.2007.01.027","volume":"17","author":"MA O\u2019Donnell","year":"2007","unstructured":"O\u2019Donnell MA, Legarda-Addison D, Skountzos P, Yeh WC, Ting AT. Ubiquitination of RIP1 regulates an NF-kappaB-independent cell-death switch in TNF signaling. Curr Biol CB. 2007;17:418\u201324.","journal-title":"Curr Biol CB"},{"key":"1463_CR306","doi-asserted-by":"publisher","first-page":"13636","DOI":"10.1074\/jbc.M600620200","volume":"281","author":"H Li","year":"2006","unstructured":"Li H, Kobayashi M, Blonska M, You Y, Lin X. Ubiquitination of RIP is required for tumor necrosis factor \u03b1-induced NF-\u03baB activation. J Biol Chem. 2006;281:13636\u201343.","journal-title":"J Biol Chem"},{"key":"1463_CR307","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1038\/nature09816","volume":"471","author":"B Gerlach","year":"2011","unstructured":"Gerlach B, Cordier SM, Schmukle AC, Emmerich CH, Rieser E, Haas TL, et al. Linear ubiquitination prevents inflammation and regulates immune signaling. Nature. 2011;471:591\u20136.","journal-title":"Nature"},{"key":"1463_CR308","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1016\/S0092-8674(03)00521-X","volume":"114","author":"O Micheau","year":"2003","unstructured":"Micheau O, Tschopp J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell. 2003;114:181\u201390.","journal-title":"Cell"},{"key":"1463_CR309","doi-asserted-by":"publisher","first-page":"387","DOI":"10.1016\/S1074-7613(00)80252-6","volume":"4","author":"H Hsu","year":"1996","unstructured":"Hsu H, Huang J, Shu HB, Baichwal V, Goeddel DV. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity. 1996;4:387\u201396.","journal-title":"Immunity"},{"key":"1463_CR310","doi-asserted-by":"publisher","first-page":"689","DOI":"10.1016\/j.molcel.2008.05.014","volume":"30","author":"MJ Bertrand","year":"2008","unstructured":"Bertrand MJ, Milutinovic S, Dickson KM, Ho WC, Boudreault A, Durkin J, et al. cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. Mol Cell. 2008;30:689\u2013700.","journal-title":"Mol Cell"},{"key":"1463_CR311","doi-asserted-by":"publisher","first-page":"11778","DOI":"10.1073\/pnas.0711122105","volume":"105","author":"DJ Mahoney","year":"2008","unstructured":"Mahoney DJ, Cheung HH, Mrad RL, Plenchette S, Simard C, Enwere E, et al. Both cIAP1 and cIAP2 regulate TNF\u03b1-mediated NF-\u03baB activation. Proc Natl Acad Sci USA. 2008;105:11778\u201383.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR312","doi-asserted-by":"publisher","first-page":"24295","DOI":"10.1074\/jbc.C800128200","volume":"283","author":"E Varfolomeev","year":"2008","unstructured":"Varfolomeev E, Goncharov T, Fedorova AV, Dynek JN, Zobel K, Deshayes K, et al. c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor \u03b1 (TNF\u03b1)-induced NF-\u03baB activation. J Biol Chem. 2008;283:24295\u20139.","journal-title":"J Biol Chem"},{"key":"1463_CR313","doi-asserted-by":"publisher","first-page":"831","DOI":"10.1016\/j.molcel.2009.10.013","volume":"36","author":"TL Haas","year":"2009","unstructured":"Haas TL, Emmerich CH, Gerlach B, Schmukle AC, Cordier SM, Rieser E, et al. Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction. Mol Cell. 2009;36:831\u201344.","journal-title":"Mol Cell"},{"key":"1463_CR314","doi-asserted-by":"publisher","first-page":"362","DOI":"10.1038\/nri3834","volume":"15","author":"D Brenner","year":"2015","unstructured":"Brenner D, Blaser H, Mak TW. Regulation of tumor necrosis factor signaling: live or let die. Nat Rev Immunol. 2015;15:362\u201374.","journal-title":"Nat Rev Immunol"},{"key":"1463_CR315","doi-asserted-by":"publisher","first-page":"693","DOI":"10.1016\/j.cell.2008.03.036","volume":"133","author":"L Wang","year":"2008","unstructured":"Wang L, Du F, Wang X. TNF-\u03b1 induces two distinct caspase-8 activation pathways. Cell. 2008;133:693\u2013703.","journal-title":"Cell"},{"key":"1463_CR316","doi-asserted-by":"publisher","first-page":"20054","DOI":"10.1073\/pnas.1116302108","volume":"108","author":"S He","year":"2011","unstructured":"He S, Liang Y, Shao F, Wang X. Toll-like receptors activate programmed necrosis in macrophages through a receptor-interacting kinase-3\u2013mediated pathway. Proc Natl Acad Sci USA. 2011;108:20054\u20139.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR317","doi-asserted-by":"publisher","first-page":"674","DOI":"10.1016\/j.chom.2016.09.014","volume":"20","author":"RJ Thapa","year":"2016","unstructured":"Thapa RJ, Ingram JP, Ragan KB, Nogusa S, Boyd DF, Benitez AA, et al. DAI senses influenza A virus genomic RNA and activates RIPK3-dependent cell death. Cell Host Microbe. 2016;20:674\u201381.","journal-title":"Cell Host Microbe"},{"key":"1463_CR318","doi-asserted-by":"publisher","first-page":"1112","DOI":"10.1016\/j.cell.2009.05.037","volume":"137","author":"YS Cho","year":"2009","unstructured":"Cho YS, Challa S, Moquin D, Genga R, Ray TD, Guildford M, et al. Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell. 2009;137:1112\u201323.","journal-title":"Cell"},{"key":"1463_CR319","doi-asserted-by":"publisher","first-page":"1100","DOI":"10.1016\/j.cell.2009.05.021","volume":"137","author":"S He","year":"2009","unstructured":"He S, Wang L, Miao L, Wang T, Du F, Zhao L, et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-\u03b1. Cell. 2009;137:1100\u201311.","journal-title":"Cell"},{"key":"1463_CR320","doi-asserted-by":"publisher","first-page":"332","DOI":"10.1126\/science.1172308","volume":"325","author":"D-W Zhang","year":"2009","unstructured":"Zhang D-W, Shao J, Lin J, Zhang N, Lu BJ, Lin SC, et al. RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis. Science. 2009;325:332\u20136.","journal-title":"Science"},{"key":"1463_CR321","doi-asserted-by":"publisher","first-page":"339","DOI":"10.1016\/j.cell.2012.06.019","volume":"150","author":"J Li","year":"2012","unstructured":"Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, et al. The RIP1\/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. Cell. 2012;150:339\u201350.","journal-title":"Cell"},{"key":"1463_CR322","doi-asserted-by":"publisher","first-page":"5322","DOI":"10.1073\/pnas.1200012109","volume":"109","author":"J Zhao","year":"2012","unstructured":"Zhao J, Jitkaew S, Cai Z, Choksi S, Li Q, Luo J, et al. Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis. Proc Natl Acad Sci USA. 2012;109:5322\u20137.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR323","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1016\/j.cell.2011.11.031","volume":"148","author":"L Sun","year":"2012","unstructured":"Sun L, Wang H, Wang Z, He S, Chen S, Liao D, et al. Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase. Cell. 2012;148:213\u201327.","journal-title":"Cell"},{"key":"1463_CR324","doi-asserted-by":"publisher","first-page":"10838","DOI":"10.1074\/jbc.275.15.10838","volume":"275","author":"WH Hu","year":"2000","unstructured":"Hu WH, Johnson H, Shu HB. Activation of NF-kappaB by FADD, Casper, and caspase-8. J Biol Chem. 2000;275:10838\u201344.","journal-title":"J Biol Chem"},{"key":"1463_CR325","doi-asserted-by":"publisher","first-page":"2627","DOI":"10.1128\/MCB.24.7.2627-2636.2004","volume":"24","author":"T Kataoka","year":"2004","unstructured":"Kataoka T, Tschopp J. N-terminal fragment of c-FLIP(L) processed by caspase 8 specifically interacts with TRAF2 and induces activation of the NF-\u03baB signaling pathway. Mol Cell Biol. 2004;24:2627\u201336.","journal-title":"Mol Cell Biol"},{"key":"1463_CR326","doi-asserted-by":"publisher","first-page":"7416","DOI":"10.1074\/jbc.M606721200","volume":"282","author":"B Lemmers","year":"2007","unstructured":"Lemmers B, Salmena L, Bid\u00e8re N, Su H, Matysiak-Zablocki E, Murakami K, et al. Essential role for caspase-8 in Toll-like receptors and NFkappaB signaling. J Biol Chem. 2007;282:7416\u201323.","journal-title":"J Biol Chem"},{"key":"1463_CR327","doi-asserted-by":"publisher","first-page":"267","DOI":"10.1016\/S1074-7613(00)80609-3","volume":"9","author":"EE Varfolomeev","year":"1998","unstructured":"Varfolomeev EE, Schuchmann M, Luria V, Chiannilkulchai N, Beckmann JS, Mett IL, et al. Targeted disruption of the mouse Caspase 8 gene ablates cell death induction by the TNF receptors, Fas\/Apo1, and DR3 and is lethal prenatally. Immunity. 1998;9:267\u201376.","journal-title":"Immunity"},{"key":"1463_CR328","doi-asserted-by":"publisher","first-page":"296","DOI":"10.1038\/32681","volume":"392","author":"J Zhang","year":"1998","unstructured":"Zhang J, Cado D, Chen A, Kabra NH, Winoto A. Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD\/Mort1. Nature. 1998;392:296\u2013300.","journal-title":"Nature"},{"key":"1463_CR329","doi-asserted-by":"publisher","first-page":"363","DOI":"10.1038\/nature09852","volume":"471","author":"A Oberst","year":"2011","unstructured":"Oberst A, Dillon CP, Weinlich R, McCormick LL, Fitzgerald P, Pop C, et al. Catalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosis. Nature. 2011;471:363\u20137.","journal-title":"Nature"},{"key":"1463_CR330","doi-asserted-by":"publisher","first-page":"368","DOI":"10.1038\/nature09857","volume":"471","author":"WJ Kaiser","year":"2011","unstructured":"Kaiser WJ, Upton JW, Long AB, Livingston-Rosanoff D, Daley-Bauer LP, Hakem R, et al. RIP3 mediates the embryonic lethality of caspase-8-deficient mice. Nature. 2011;471:368\u201372.","journal-title":"Nature"},{"key":"1463_CR331","first-page":"1835","volume":"192","author":"P Gurung","year":"2014","unstructured":"Gurung P, Anand PK, Malireddi RK, Vande Walle L, Van Opdenbosch N, Dillon CP, et al. FADD and caspase-8 mediate priming and activation of the canonical and noncanonical Nlrp3 inflammasomes. J Immunol Baltim Md. 2014;192:1835\u201346.","journal-title":"J Immunol Baltim Md"},{"key":"1463_CR332","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms8515","volume":"6","author":"S Kang","year":"2015","unstructured":"Kang S, Fernandes-Alnemri T, Rogers C, Mayes L, Wang Y, Dillon C, et al. Caspase-8 scaffolding function and MLKL regulate NLRP3 inflammasome activation downstream of TLR3. Nat Commun. 2015;6:7515.","journal-title":"Nat Commun"},{"key":"1463_CR333","doi-asserted-by":"publisher","first-page":"637","DOI":"10.1042\/bst0310637","volume":"31","author":"S Akira","year":"2003","unstructured":"Akira S, Yamamoto M, Takeda K. Role of adapters in Toll-like receptor signaling. Biochem Soc Trans. 2003;31:637\u201342.","journal-title":"Biochem Soc Trans"},{"key":"1463_CR334","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms7282","volume":"6","author":"KE Lawlor","year":"2015","unstructured":"Lawlor KE, Khan N, Mildenhall A, Gerlic M, Croker BA, D'Cruz AA, et al. RIPK3 promotes cell death and NLRP3 inflammasome activation in the absence of MLKL. Nat Commun. 2015;6:6282.","journal-title":"Nat Commun"},{"key":"1463_CR335","doi-asserted-by":"publisher","first-page":"215","DOI":"10.1016\/j.immuni.2012.01.012","volume":"36","author":"JE Vince","year":"2012","unstructured":"Vince JE, Wong WW, Gentle I, Lawlor KE, Allam R, O'Reilly L, et al. Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation. Immunity. 2012;36:215\u201327.","journal-title":"Immunity"},{"key":"1463_CR336","doi-asserted-by":"publisher","first-page":"389","DOI":"10.1016\/j.ccr.2006.08.027","volume":"10","author":"MF van Delft","year":"2006","unstructured":"van Delft MF, Wei AH, Mason KD, Vandenberg CJ, Chen L, Czabotar PE, et al. The BH3 mimetic ABT-737 targets selective Bcl-2 proteins and efficiently induces apoptosis via Bak\/Bax if Mcl-1 is neutralized. Cancer Cell. 2006;10:389\u201399.","journal-title":"Cancer Cell"},{"key":"1463_CR337","doi-asserted-by":"publisher","first-page":"677","DOI":"10.1038\/nature03579","volume":"435","author":"T Oltersdorf","year":"2005","unstructured":"Oltersdorf T, Elmore SW, Shoemaker AR, Armstrong RC, Augeri DJ, Belli BA, et al. An inhibitor of Bcl-2 family proteins induces regression of solid tumors. Nature. 2005;435:677\u201381.","journal-title":"Nature"},{"key":"1463_CR338","doi-asserted-by":"publisher","first-page":"477","DOI":"10.1038\/nature19830","volume":"538","author":"A Kotschy","year":"2016","unstructured":"Kotschy A, Szlavik Z, Murray J, Davidson J, Maragno AL, Le Toumelin-Braizat G, et al. The MCL1 inhibitor S63845 is tolerable and effective in diverse cancer models. Nature. 2016;538:477\u201382.","journal-title":"Nature"},{"key":"1463_CR339","doi-asserted-by":"publisher","first-page":"109","DOI":"10.1038\/nrd3627","volume":"11","author":"S Fulda","year":"2012","unstructured":"Fulda S, Vucic D. Targeting IAP proteins for therapeutic intervention in cancer. Nat Rev Drug Discov. 2012;11:109\u201324.","journal-title":"Nat Rev Drug Discov"},{"key":"1463_CR340","doi-asserted-by":"publisher","first-page":"EMBR202356865","DOI":"10.15252\/embr.202356865","volume":"24","author":"M Speir","year":"2023","unstructured":"Speir M, Tye H, Gottschalk TA, Simpson DS, Djajawi TM, Deo P, et al. A1 is induced by pathogen ligands to limit myeloid cell death and NLRP3 inflammasome activation. EMBO Rep. 2023;24:EMBR202356865.","journal-title":"EMBO Rep"},{"key":"1463_CR341","doi-asserted-by":"publisher","first-page":"11303","DOI":"10.1074\/jbc.M111.323378","volume":"287","author":"JK Sandilos","year":"2012","unstructured":"Sandilos JK, Chiu YH, Chekeni FB, Armstrong AJ, Walk SF, Ravichandran KS, et al. Pannexin 1, an ATP release channel, is activated by caspase cleavage of its pore-associated C-terminal autoinhibitory region. J Biol Chem. 2012;287:11303\u201311.","journal-title":"J Biol Chem"},{"key":"1463_CR342","doi-asserted-by":"publisher","first-page":"863","DOI":"10.1038\/nature09413","volume":"467","author":"FB Chekeni","year":"2010","unstructured":"Chekeni FB, Elliott MR, Sandilos JK, Walk SF, Kinchen JM, Lazarowski ER, et al. Pannexin 1 channels mediate \u2018find-me\u2019 signal release and membrane permeability during apoptosis. Nature. 2010;467:863\u20137.","journal-title":"Nature"},{"key":"1463_CR343","doi-asserted-by":"publisher","first-page":"E961","DOI":"10.1073\/pnas.1613305114","volume":"114","author":"SA Conos","year":"2017","unstructured":"Conos SA, Chen KW, De Nardo D, Hara H, Whitehead L, N\u00fa\u00f1ez G, et al. Active MLKL triggers the NLRP3 inflammasome in a cell-intrinsic manner. Proc Natl Acad Sci USA. 2017;114:E961\u2013E969.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR344","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1016\/j.immuni.2017.11.013","volume":"48","author":"CL Evavold","year":"2018","unstructured":"Evavold CL, Ruan J, Tan Y, Xia S, Wu H, Kagan JC. The pore-forming protein gasdermin D regulates interleukin-1 secretion from living macrophages. Immunity. 2018;48:35\u201344.e6.","journal-title":"Immunity"},{"key":"1463_CR345","doi-asserted-by":"publisher","first-page":"327","DOI":"10.1101\/gad.312561.118","volume":"32","author":"B Shan","year":"2018","unstructured":"Shan B, Pan H, Najafov A, Yuan J. Necroptosis in development and diseases. Genes Dev. 2018;32:327\u201340.","journal-title":"Genes Dev"},{"key":"1463_CR346","doi-asserted-by":"publisher","first-page":"1431","DOI":"10.3390\/biom10101431","volume":"10","author":"A Negroni","year":"2020","unstructured":"Negroni A, Colantoni E, Cucchiara S, Stronati L. Necroptosis in intestinal inflammation and cancer: new concepts and therapeutic perspectives. Biomolecules. 2020;10:1431.","journal-title":"Biomolecules"},{"key":"1463_CR347","doi-asserted-by":"crossref","unstructured":"Choi ME, Price DR, Ryter SW, Choi AMK. Necroptosis: a crucial pathogenic mediator of human disease. JCI Insight. 2019;4:e128834.","DOI":"10.1172\/jci.insight.128834"},{"key":"1463_CR348","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1146\/annurev-pathol-052016-100247","volume":"12","author":"L Galluzzi","year":"2017","unstructured":"Galluzzi L, Kepp O, Chan FK-M, Kroemer G. Necroptosis: mechanisms and relevance to disease. Annu Rev Pathol. 2017;12:103\u201330.","journal-title":"Annu Rev Pathol"},{"key":"1463_CR349","doi-asserted-by":"publisher","first-page":"20388","DOI":"10.1073\/pnas.0908698106","volume":"106","author":"SS Iyer","year":"2009","unstructured":"Iyer SS, Pulskens WP, Sadler JJ, Butter LM, Teske GJ, Ulland TK, et al. Necrotic cells trigger a sterile inflammatory response through the Nlrp3 inflammasome. Proc Natl Acad Sci USA. 2009;106:20388\u201393.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR350","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1016\/j.immuni.2012.09.015","volume":"38","author":"T-B Kang","year":"2013","unstructured":"Kang T-B, Yang S-H, Toth B, Kovalenko A, Wallach D. Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome. Immunity. 2013;38:27\u201340.","journal-title":"Immunity"},{"key":"1463_CR351","doi-asserted-by":"publisher","first-page":"817","DOI":"10.1016\/S0092-8674(00)81266-0","volume":"85","author":"M Muzio","year":"1996","unstructured":"Muzio M, Chinnaiyan AM, Kischkel FC, O'Rourke K, Shevchenko A, Ni J, et al. FLICE, a novel FADD-homologous ICE\/CED-3-like protease, is recruited to the CD95 (Fas\/APO-1) death\u2013inducing signaling complex. Cell. 1996;85:817\u201327.","journal-title":"Cell"},{"key":"1463_CR352","doi-asserted-by":"publisher","first-page":"803","DOI":"10.1016\/S0092-8674(00)81265-9","volume":"85","author":"MP Boldin","year":"1996","unstructured":"Boldin MP, Goncharov TM, Goltseve YV, Wallach D. Involvement of MACH, a novel MORT1\/FADD-interacting protease, in Fas\/APO-1- and TNF receptor\u2013induced cell death. Cell. 1996;85:803\u201315.","journal-title":"Cell"},{"key":"1463_CR353","doi-asserted-by":"publisher","first-page":"363","DOI":"10.1038\/nature09852","volume":"471","author":"A Oberst","year":"2011","unstructured":"Oberst A, Dillon CP, Weinlich R, McCormick LL, Fitzgerald P, Pop C, et al. Catalytic activity of the caspase-8\u2013FLIPL complex inhibits RIPK3-dependent necrosis. Nature. 2011;471:363\u20137.","journal-title":"Nature"},{"key":"1463_CR354","doi-asserted-by":"publisher","first-page":"513","DOI":"10.1016\/j.immuni.2016.07.016","volume":"45","author":"S Alvarez-Diaz","year":"2016","unstructured":"Alvarez-Diaz S, Dillon CP, Lalaoui N, Tanzer MC, Rodriguez DA, Lin A, et al. The pseudokinase MLKL and the kinase RIPK3 have distinct roles in autoimmune disease caused by loss of death-receptor-induced apoptosis. Immunity. 2016;45:513\u201326.","journal-title":"Immunity"},{"key":"1463_CR355","doi-asserted-by":"publisher","first-page":"683","DOI":"10.1038\/s41586-019-1770-6","volume":"575","author":"M Fritsch","year":"2019","unstructured":"Fritsch M, G\u00fcnther SD, Schwarzer R, Albert MC, Schorn F, Werthenbach JP, et al. Caspase-8 is the molecular switch for apoptosis, necroptosis and pyroptosis. Nature. 2019;575:683\u20137.","journal-title":"Nature"},{"key":"1463_CR356","doi-asserted-by":"publisher","first-page":"833","DOI":"10.1016\/j.immuni.2016.01.012","volume":"44","author":"MM Gaidt","year":"2016","unstructured":"Gaidt MM, Ebert TS, Chauhan D, Schmidt T, Schmid-Burgk JL, Rapino F, et al. Human monocytes engage an alternative inflammasome pathway. Immunity. 2016;44:833\u201346.","journal-title":"Immunity"},{"key":"1463_CR357","doi-asserted-by":"publisher","first-page":"313","DOI":"10.1038\/nchembio.83","volume":"4","author":"A Degterev","year":"2008","unstructured":"Degterev A, Hitomi J, Germscheid M, Ch'en IL, Korkina O, Teng X, et al. Identification of RIP1 kinase as a specific cellular target of necrostatins. Nat Chem Biol. 2008;4:313\u201321.","journal-title":"Nat Chem Biol"},{"key":"1463_CR358","doi-asserted-by":"publisher","first-page":"112","DOI":"10.1038\/nchembio711","volume":"1","author":"A Degterev","year":"2005","unstructured":"Degterev A, Huang Z, Boyce M, Li Y, Jagtap P, Mizushima N, et al. Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury. Nat Chem Biol. 2005;1:112\u20139.","journal-title":"Nat Chem Biol"},{"key":"1463_CR359","doi-asserted-by":"publisher","first-page":"2339","DOI":"10.1016\/j.celrep.2018.10.103","volume":"25","author":"JE Vince","year":"2018","unstructured":"Vince JE, De Nardo D, Gao W, Vince AJ, Hall C, McArthur K, et al. The mitochondrial apoptotic effectors BAX\/BAK activate Caspase-3 and -7 to trigger NLRP3 inflammasome and Caspase-8 driven IL-1\u03b2 activation. Cell Rep. 2018;25:2339\u20132353.e4.","journal-title":"Cell Rep"},{"key":"1463_CR360","doi-asserted-by":"publisher","first-page":"668","DOI":"10.1016\/j.celrep.2017.06.073","volume":"20","author":"KE Lawlor","year":"2017","unstructured":"Lawlor KE, Feltham R, Yabal M, Conos SA, Chen KW, Ziehe S, et al. XIAP loss triggers RIPK3- and Caspase-8-driven IL-1\u03b2 activation and cell death as a consequence of TLR-MyD88-induced cIAP1-TRAF2 degradation. Cell Rep. 2017;20:668\u201382.","journal-title":"Cell Rep"},{"key":"1463_CR361","doi-asserted-by":"publisher","first-page":"EMBJ2021110468","DOI":"10.15252\/embj.2021110468","volume":"42","author":"SA Hughes","year":"2023","unstructured":"Hughes SA, Lin M, Weir A, Huang B, Xiong L, Chua NK, et al. Caspase-8-driven apoptotic and pyroptotic crosstalk causes cell death and IL-1\u03b2 release in X-linked inhibitor of apoptosis (XIAP) deficiency. EMBO J. 2023;42:EMBJ2021110468.","journal-title":"EMBO J"},{"key":"1463_CR362","doi-asserted-by":"publisher","first-page":"924","DOI":"10.1016\/j.tcb.2021.06.010","volume":"31","author":"A Pandey","year":"2021","unstructured":"Pandey A, Shen C, Feng S, Man SM. Cell biology of inflammasome activation. Trends Cell Biol. 2021;31:924\u201339.","journal-title":"Trends Cell Biol"},{"key":"1463_CR363","doi-asserted-by":"publisher","unstructured":"Mangan MS, Gorki F, Krause K, Heinz A, Ebert T, Jahn D, et al. Clostridium difficile Toxin B activates the NLRP3 inflammasome in human macrophages, demonstrating a novel regulatory mechanism for the Pyrin inflammasome. Preprint at https:\/\/doi.org\/10.1101\/2021.07.07.451422 (2021).","DOI":"10.1101\/2021.07.07.451422"},{"key":"1463_CR364","doi-asserted-by":"publisher","first-page":"1331","DOI":"10.1038\/cdd.2016.14","volume":"23","author":"H Chung","year":"2016","unstructured":"Chung H, Vilaysane A, Lau A, Stahl M, Morampudi V, Bondzi-Simpson A, et al. NLRP3 regulates a noncanonical platform for caspase-8 activation during epithelial apoptosis. Cell Death Differ. 2016;23:1331\u201346.","journal-title":"Cell Death Differ"},{"key":"1463_CR365","doi-asserted-by":"publisher","first-page":"1149","DOI":"10.1038\/cdd.2013.37","volume":"20","author":"V Sagulenko","year":"2013","unstructured":"Sagulenko V, Thygesen SJ, Sester DP, Idris A, Cridland JA, Vajjhala PR, et al. AIM2 and the NLRP3 inflammasome activate both apoptotic and pyroptotic death pathways via ASC. Cell Death Differ. 2013;20:1149\u201360.","journal-title":"Cell Death Differ"},{"key":"1463_CR366","doi-asserted-by":"publisher","first-page":"1709","DOI":"10.1038\/cdd.2012.51","volume":"19","author":"R Pierini","year":"2012","unstructured":"Pierini R, Juruj C, Perret M, Jones CL, Mangeot P, Weiss DS, et al. AIM2\/ASC triggers caspase-8-dependent apoptosis in Francisella-infected caspase-1-deficient macrophages. Cell Death Differ. 2012;19:1709\u201321.","journal-title":"Cell Death Differ"},{"key":"1463_CR367","doi-asserted-by":"publisher","first-page":"5239","DOI":"10.4049\/jimmunol.1301581","volume":"191","author":"SM Man","year":"2013","unstructured":"Man SM, Tourlomousis P, Hopkins L, Monie TP, Fitzgerald KA, Bryant CE. Salmonella infection induces recruitment of Caspase-8 to the inflammasome to modulate IL-1\u03b2 production. J Immunol. 2013;191:5239\u201346.","journal-title":"J Immunol"},{"key":"1463_CR368","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1016\/j.ajpath.2014.08.025","volume":"185","author":"P Gurung","year":"2015","unstructured":"Gurung P, Kanneganti T-D. Novel roles for Caspase-8 in IL-1\u03b2 and inflammasome regulation. Am J Pathol. 2015;185:17\u201325.","journal-title":"Am J Pathol"},{"key":"1463_CR369","doi-asserted-by":"publisher","first-page":"0043","DOI":"10.1126\/sciimmunol.adq0043","volume":"10","author":"HI Muendlein","year":"2025","unstructured":"Muendlein HI, Connolly WM, Leiriao J, Nolan MA, Judge J, Smirnova I, et al. TNF switches homeostatic efferocytosis to lytic caspase-8\u2013dependent pyroptosis and IL-1\u03b2 maturation. Sci Immunol. 2025;10:0043.","journal-title":"Sci Immunol"},{"key":"1463_CR370","doi-asserted-by":"publisher","first-page":"406","DOI":"10.3389\/fcimb.2019.00406","volume":"9","author":"RKS Malireddi","year":"2019","unstructured":"Malireddi RKS, Kesavardhana S, Kanneganti T-D. ZBP1 and TAK1: master regulators of NLRP3 inflammasome\/pyroptosis, apoptosis, and necroptosis (PAN-optosis). Front Cell Infect Microbiol. 2019;9:406.","journal-title":"Front Cell Infect Microbiol"},{"key":"1463_CR371","doi-asserted-by":"publisher","first-page":"2141","DOI":"10.3390\/v15112141","volume":"15","author":"R Malireddi","year":"2023","unstructured":"Malireddi R, Sharma BR, Bynigeri RR, Wang Y, Lu J, Kanneganti TD. ZBP1 drives IAV-induced NLRP3 inflammasome activation and lytic cell death, PANoptosis, independent of the necroptosis executioner MLKL. Viruses. 2023;15:2141.","journal-title":"Viruses"},{"key":"1463_CR372","doi-asserted-by":"publisher","first-page":"aag2045","DOI":"10.1126\/sciimmunol.aag2045","volume":"1","author":"T Kuriakose","year":"2016","unstructured":"Kuriakose T, Man SM, Malireddi RK, Karki R, Kesavardhana S, Place DE, et al. ZBP1\/DAI is an innate sensor of influenza virus triggering the NLRP3 inflammasome and programmed cell death pathways. Sci Immunol. 2016;1:aag2045.","journal-title":"Sci Immunol"},{"key":"1463_CR373","doi-asserted-by":"publisher","first-page":"1236","DOI":"10.1093\/jimmun\/vkaf042","volume":"214","author":"BR Sharma","year":"2025","unstructured":"Sharma BR, Choudhury SM, Abdelaal HM, Wang Y, Kanneganti T-D. Innate immune sensor NLRP3 drives PANoptosome formation and PANoptosis. J Immunol. 2025;214:1236\u201346.","journal-title":"J Immunol"},{"key":"1463_CR374","doi-asserted-by":"publisher","first-page":"634","DOI":"10.1038\/s41580-026-00994-w","volume":"27","author":"RE Tweedell","year":"2026","unstructured":"Tweedell RE, Kanneganti T-D. Single-cell evidence for PANoptosome complexes. Nat Rev Mol Cell Biol. 2026;27:634\u20135.","journal-title":"Nat Rev Mol Cell Biol"},{"key":"1463_CR375","doi-asserted-by":"publisher","first-page":"636","DOI":"10.1038\/s41580-026-00995-9","volume":"27","author":"JE Vince","year":"2026","unstructured":"Vince JE, Silke J. Reply to \u2018Single-cell evidence for PANoptosome complexes\u2019. Nat Rev Mol Cell Biol. 2026;27:636\u20137.","journal-title":"Nat Rev Mol Cell Biol"},{"key":"1463_CR376","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-019-09753-2","volume":"10","author":"K Tsuchiya","year":"2019","unstructured":"Tsuchiya K, Nakajima S, Hosojima S, Thi Nguyen D, Hattori T, Manh Le T, et al. Caspase-1 initiates apoptosis in the absence of gasdermin D. Nat Commun. 2019;10:2091.","journal-title":"Nat Commun"},{"key":"1463_CR377","doi-asserted-by":"publisher","first-page":"653","DOI":"10.1016\/0092-8674(93)90486-A","volume":"75","author":"M Miura","year":"1993","unstructured":"Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J. Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3. Cell. 1993;75:653\u201360.","journal-title":"Cell"},{"key":"1463_CR378","doi-asserted-by":"publisher","first-page":"16012","DOI":"10.1073\/pnas.2534856100","volume":"100","author":"W-H Zhang","year":"2003","unstructured":"Zhang W-H, Wang X, Narayanan M, Zhang Y, Huo C, Reed JC, et al. Fundamental role of the Rip2\/caspase-1 pathway in hypoxia and ischemia-induced neuronal cell death. Proc Natl Acad Sci USA. 2003;100:16012\u20137.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR379","doi-asserted-by":"publisher","first-page":"1103","DOI":"10.1161\/01.RES.0000166925.45995.ed","volume":"96","author":"FM Syed","year":"2005","unstructured":"Syed FM, Hahn HS, Odley A, Guo Y, Vallejo JG, Lynch RA, et al. Proapoptotic effects of caspase-1\/interleukin-converting enzyme dominate in myocardial ischemia. Circ Res. 2005;96:1103\u20139.","journal-title":"Circ Res"},{"key":"1463_CR380","doi-asserted-by":"publisher","first-page":"507","DOI":"10.1016\/j.chembiol.2017.03.009","volume":"24","author":"CY Taabazuing","year":"2017","unstructured":"Taabazuing CY, Okondo MC, Bachovchin DA. Pyroptosis and apoptosis pathways engage in bidirectional crosstalk in monocytes and macrophages. Cell Chem Biol. 2017;24:507\u2013514.e4.","journal-title":"Cell Chem Biol"},{"key":"1463_CR381","doi-asserted-by":"publisher","first-page":"238","DOI":"10.1016\/j.jmb.2017.10.028","volume":"430","author":"V Sagulenko","year":"2018","unstructured":"Sagulenko V, Vitak N, Vajjhala PR, Vince JE, Stacey KJ. Caspase-1 is an apical caspase leading to caspase-3 cleavage in the AIM2 inflammasome response, independent of caspase-8. J Mol Biol. 2018;430:238\u201347.","journal-title":"J Mol Biol"},{"key":"1463_CR382","doi-asserted-by":"publisher","first-page":"180","DOI":"10.1097\/00004647-199802000-00009","volume":"18","author":"GP Schielke","year":"1998","unstructured":"Schielke GP, Yang GY, Shivers BD, Betz AL. Reduced ischemic brain injury in interleukin-1 beta converting enzyme-deficient mice. J Cereb Blood Flow Metab J Int Soc Cereb Blood Flow Metab. 1998;18:180\u20135.","journal-title":"J Cereb Blood Flow Metab J Int Soc Cereb Blood Flow Metab"},{"key":"1463_CR383","doi-asserted-by":"publisher","first-page":"335","DOI":"10.1126\/science.288.5464.335","volume":"288","author":"M Li","year":"2000","unstructured":"Li M, Ona VO, Gu\u00e9gan C, Chen M, Jackson-Lewis V, Andrews LJ, et al. Functional role of caspase-1 and caspase-3 in an ALS transgenic mouse model. Science. 2000;288:335\u20139.","journal-title":"Science"},{"key":"1463_CR384","doi-asserted-by":"publisher","first-page":"13901","DOI":"10.1073\/pnas.240305897","volume":"97","author":"P Pasinelli","year":"2000","unstructured":"Pasinelli P, Houseweart MK, Brown RH, Cleveland DW. Caspase-1 and -3 are sequentially activated in motor neuron death in Cu,Zn superoxide dismutase-mediated familial amyotrophic lateral sclerosis. Proc Natl Acad Sci USA. 2000;97:13901\u20136.","journal-title":"Proc Natl Acad Sci USA"},{"key":"1463_CR385","doi-asserted-by":"publisher","first-page":"553","DOI":"10.1006\/mcne.2002.1136","volume":"20","author":"C Gu\u00e9gan","year":"2002","unstructured":"Gu\u00e9gan C, Vila M, Teismann P, Chen C, Ont\u00e9niente B, Li M, et al. Instrumental activation of bid by caspase-1 in a transgenic mouse model of ALS. Mol Cell Neurosci. 2002;20:553\u201362.","journal-title":"Mol Cell Neurosci"},{"key":"1463_CR386","doi-asserted-by":"publisher","first-page":"3846","DOI":"10.1016\/j.celrep.2017.12.018","volume":"21","author":"KS Schneider","year":"2017","unstructured":"Schneider KS, Gro\u00df CJ, Dreier RF, Saller BS, Mishra R, Gorka O, et al. The inflammasome drives GSDMD-independent secondary pyroptosis and IL-1 release in the absence of caspase-1 protease activity. Cell Rep. 2017;21:3846\u201359.","journal-title":"Cell Rep"},{"key":"1463_CR387","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms14128","volume":"8","author":"C Rogers","year":"2017","unstructured":"Rogers C, Fernandes-Alnemri T, Mayes L, Alnemri D, Cingolani G, Alnemri ES. Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic\/pyroptotic cell death. Nat Commun. 2017;8:14128.","journal-title":"Nat Commun"},{"key":"1463_CR388","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1038\/nature22393","volume":"547","author":"Y Wang","year":"2017","unstructured":"Wang Y, Gao W, Shi X, Ding J, Liu W, He H, et al. Chemotherapy drugs induce pyroptosis through caspase-3 cleavage of a gasdermin. Nature. 2017;547:99\u2013103.","journal-title":"Nature"},{"key":"1463_CR389","doi-asserted-by":"publisher","first-page":"1631152","DOI":"10.3389\/fimmu.2025.1631152","volume":"16","author":"YQ Gan","year":"2025","unstructured":"Gan YQ, Cai YW, Liang XW, Wang LZ, Shi FL, Sun N, et al. Impaired NLRP3 inflammasome signaling diverts pyroptotic to apoptotic caspase activation in macrophages. Front Immunol. 2025;16:1631152.","journal-title":"Front Immunol"},{"key":"1463_CR390","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1016\/S0006-291X(03)00309-7","volume":"303","author":"J Masumoto","year":"2003","unstructured":"Masumoto J, Dowds TA, Schaner P, Chen FF, Ogura Y, Li M, et al. ASC is an activating adaptor for NF-kappa B and caspase-8-dependent apoptosis. Biochem Biophys Res Commun. 2003;303:69\u201373.","journal-title":"Biochem Biophys Res Commun"},{"key":"1463_CR391","doi-asserted-by":"publisher","first-page":"20167","DOI":"10.1074\/jbc.M115.652321","volume":"290","author":"C Antonopoulos","year":"2015","unstructured":"Antonopoulos C, Russo HM, El Sanadi C, Martin BN, Li X, Kaiser WJ, et al. Caspase-8 as an effector and regulator of NLRP3 inflammasome signaling. J Biol Chem. 2015;290:20167\u201384.","journal-title":"J Biol Chem"},{"key":"1463_CR392","doi-asserted-by":"publisher","first-page":"550","DOI":"10.1038\/s41590-021-00886-5","volume":"22","author":"BR Sharma","year":"2021","unstructured":"Sharma BR, Kanneganti T-D. NLRP3 inflammasome in cancer and metabolic diseases. Nat Immunol. 2021;22:550\u20139.","journal-title":"Nat Immunol"}],"container-title":["Cellular &amp; Molecular Immunology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41423-026-01463-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41423-026-01463-2","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41423-026-01463-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T22:02:18Z","timestamp":1790719338000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41423-026-01463-2"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,2]]},"references-count":392,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2026,10]]}},"alternative-id":["1463"],"URL":"https:\/\/doi.org\/10.1038\/s41423-026-01463-2","relation":{},"ISSN":["2042-0226"],"issn-type":[{"value":"2042-0226","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,2]]},"assertion":[{"value":"28 June 2026","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"9 August 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"2 September 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","label":"Competing interests","group":{"name":"EthicsHeading","label":"Ethics"}}]}}