Revealing the dance of NLRP3: spatiotemporal patterns in inflammasome activation-Immunometabolism-CSCIED科技核心评价数据库-手机版

Revealing the dance of NLRP3: spatiotemporal patterns in inflammasome activation

Revealing the dance of NLRP3: spatiotemporal patterns in inflammasome activation

ES评分 0 浏览量：1072 下载量：0

DOI	10.1097/IN9.0000000000000053
刊名	Immunometabolism IJ
年，卷(期)	2025, 7(1)
作者	Spector, Lauren; Subramanian, Naeha,
作者单位	[Spector, Lauren; Subramanian, Naeha] Inst Syst Biol, Seattle, WA 98109 USA; [Spector, Lauren; Subramanian, Naeha] Univ Washington, Dept Immunol, Seattle, WA 98195 USA
摘要	The nucleotide-binding domain, leucine-rich repeat, and pyrin domain containing-protein 3 (NLRP3) inflammasome is a multiprotein complex that plays a critical role in the innate immune response to both infections and sterile stressors. Dysregulated NLRP3 activation has been implicated in a variety of autoimmune and inflammatory diseases, including cryopyrin-associated periodic fever syndromes, diabetes, atherosclerosis, Alzheimer's disease, inflammatory bowel disease, and cancer. Consequently, fine-tuning NLRP3 activity holds significant therapeutic potential. Studies have implicated several organelles, including mitochondria, lysosomes, the endoplasmic reticulum (ER), the Golgi apparatus, endosomes, and the centrosome, in NLRP3 localization and inflammasome assembly. However, reports of conflict and many factors regulating interactions between NLRP3 and subcellular organelles remain unknown. This review synthesizes the current understanding of NLRP3 spatiotemporal dynamics, focusing on recent literature that elucidates the roles of subcellular localization and organelle stress in NLRP3 signaling and its crosstalk with other innate immune pathways converging at these organelles.
Abstract	The nucleotide-binding domain, leucine-rich repeat, and pyrin domain containing-protein 3 (NLRP3) inflammasome is a multiprotein complex that plays a critical role in the innate immune response to both infections and sterile stressors. Dysregulated NLRP3 activation has been implicated in a variety of autoimmune and inflammatory diseases, including cryopyrin-associated periodic fever syndromes, diabetes, atherosclerosis, Alzheimer's disease, inflammatory bowel disease, and cancer. Consequently, fine-tuning NLRP3 activity holds significant therapeutic potential. Studies have implicated several organelles, including mitochondria, lysosomes, the endoplasmic reticulum (ER), the Golgi apparatus, endosomes, and the centrosome, in NLRP3 localization and inflammasome assembly. However, reports of conflict and many factors regulating interactions between NLRP3 and subcellular organelles remain unknown. This review synthesizes the current understanding of NLRP3 spatiotemporal dynamics, focusing on recent literature that elucidates the roles of subcellular localization and organelle stress in NLRP3 signaling and its crosstalk with other innate immune pathways converging at these organelles.
关键词	inflammasome; NLRP3; subcellular; organelle; innate immunity
KeyWord	inflammasome; NLRP3; subcellular; organelle; innate immunity
基金项目
页码	1-9

参考文献
相关文献

[1]. Li D, Wu M. Pattern recognition receptors in health and diseases. Signal Transduct Target Ther. 2021;6(1):291.

[2]. Swanson KV, Deng M, Ting JP. The NLRP3 inflammasome: molecular activation and regulation to therapeutics. Nat Rev Immunol. 2019;19(8):477-89.

[3]. Xu J, Nunez G. The NLRP3 inflammasome: activation and regulation. Trends Biochem Sci. 2023;48(4):331-44.

[4]. Kelley N, Jeltema D, Duan Y, et al. The NLRP3 inflammasome: an overview of mechanisms of activation and regulation. Int J Mol Sci . 2019;20(13):3328.

[5]. Booshehri LM, Hoffman HM. CAPS and NLRP3. J Clin Immunol. 2019;39(3):277-86.

[6]. Cho S, Ying F, Sweeney G. Sterile inflammation and the NLRP3 inflammasome in cardiometabolic disease. Biomed J. 2023;46(5):100624.

[7]. Zheng Y, Xu L, Dong N, et al. NLRP3 inflammasome: the rising star in cardiovascular diseases. Front Cardiovasc Med. 2022;9:927061.

[8]. Sharma BR, Kanneganti TD. NLRP3 inflammasome in cancer and metabolic diseases. Nat Immunol. 2021;22(5):550-9.

[9]. Garcia-Puente LM, Fraile-Martinez O, Garcia-Montero C, et al. Placentas from women with late-onset preeclampsia exhibit increased expression of the NLRP3 inflammasome machinery. Biomolecules. 2023;13(11):1644.

[10]. Fraile-Martinez O, Garcia-Montero C, Pekarek L, et al. Decreased survival in patients with pancreatic cancer may be associated with an increase in histopathological expression of inflammasome marker NLRP3. Histol Histopathol. 2024;39(1):35-40.

[11]. Lin TY, Tsai MC, Tu W, et al. Role of the NLRP3 inflammasome: insights into cancer hallmarks. Front Immunol. 2020;11:610492.

[12]. Seok JK, Kang HC, Cho YY, et al. Regulation of the NLRP3 inflammasome by post-translational modifications and small molecules. Front Immunol. 2020;11:618231.

[13]. Seoane PI, Lee B, Hoyle C, et al. The NLRP3-inflammasome as a sensor of organelle dysfunction. J Cell Biol. 2020;219(12):e202006194.

[14]. Zhang Z, Meszaros G, He WT, et al. Protein kinase D at the Golgi controls NLRP3 inflammasome activation. J Exp Med. 2017;214(9):2671-93.

[15]. Iyer SS, He Q, Janczy JR, et al. Mitochondrial cardiolipin is required for Nlrp3 inflammasome activation. Immunity. 2013;39(2):311-23.

[16]. Subramanian N, Natarajan K, Clatworthy MR, et al. The adaptor MAVS promotes NLRP3 mitochondrial localization and inflammasome activation. Cell. 2013;153(2):348-61.

[17]. Yang CS, Kim JJ, Kim TS, et al. Small heterodimer partner interacts with NLRP3 and negatively regulates activation of the NLRP3 inflammasome. Nat Commun. 2015;6:6115.

[18]. Zhou R, Yazdi AS, Menu P, et al. A role for mitochondria in NLRP3 inflammasome activation. Nature. 2011;469(7329):221-5.

[19]. Sagulenko V, Thygesen SJ, Sester DP, et al. AIM2 and NLRP3 inflammasomes activate both apoptotic and pyroptotic death pathways via ASC. Cell Death Differ. 2013;20(9):1149-60.

[20]. Boini KM, Hussain T, Li PL, et al. Trimethylamine-,-oxide instigates NLRP3 inflammasome activation and endothelial dysfunction. Cell Physiol Biochem. 2017;44(1):152-62.

[21]. Elliott EI, Miller AN, Banoth B, et al. Cutting edge: mitochondrial assembly of the NLRP3 inflammasome complex is initiated at priming. J Immunol. 2018;200(9):3047-52.

[22]. Lee B, Hoyle C, Wellens R, et al. Disruptions in endocytic traffic contribute to the activation of the NLRP3 inflammasome. Sci Signal. 2023;16(773):eabm7134.

[23]. Tsujimoto K, Jo T, Nagira D, et al. The lysosomal ragulator complex activates NLRP3 inflammasome in vivo via HDAC6. EMBO J. 2023;42(1):e111389.

[24]. Chen J, Chen ZJ. PtdIns4P on dispersed trans-Golgi network mediates NLRP3 inflammasome activation. Nature. 2018;564(7734):71-6.

[25]. Bittner ZA, Liu X, Mateo Tortola M, et al. BTK operates a phospho-tyrosine switch to regulate NLRP3 inflammasome activity. J Exp Med. 2021;218(11):e20201656.

[26]. Nanda SK, Prescott AR, Figueras-Vadillo C, et al. IKKbeta is required for the formation of the NLRP3 inflammasome. EMBO Rep. 2021;22(10):e50743.

[27]. Zhang Z, Venditti R, Ran L, et al. Distinct changes in endosomal composition promote NLRP3 inflammasome activation. Nat Immunol. 2023;24(1):30-41.

[28]. Magupalli VG, Negro R, Tian Y, et al. HDAC6 mediates an aggresome-like mechanism for NLRP3 and pyrin inflammasome activation. Science. 2020;369(6510):eaas8995.

[29]. Li X, Thome S, Ma X, et al. MARK4 regulates NLRP3 positioning and inflammasome activation through a microtubule-dependent mechanism. Nat Commun. 2017;8:15986.

[30]. Guo C, Chi Z, Jiang D, et al. Cholesterol homeostatic regulator SCAP-SREBP2 integrates NLRP3 inflammasome activation and cholesterol biosynthetic signaling in macrophages. Immunity. 2018;49(5):842-56.e7.

[31]. Wang W, Hu D, Wu C, et al. STING promotes NLRP3 localization in ER and facilitates NLRP3 deubiquitination to activate the inflammasome upon HSV-1 infection. PLoS Pathog. 2020;16(3):e1008335.

[32]. Andreeva L, David L, Rawson S, et al. NLRP3 cages revealed by full-length mouse NLRP3 structure control pathway activation. Cell. 2021;184(26):6299-312.e22.

[33]. Arumugam S, Qin Y, Liang Z, et al. GSK3beta mediates the spatiotemporal dynamics of NLRP3 inflammasome activation. Cell Death Differ. 2022;29(10):2060-9.

[34]. Baik SH, Ramanujan VK, Becker C, et al. Hexokinase dissociation from mitochondria promotes oligomerization of VDAC that facilitates NLRP3 inflammasome assembly and activation. Sci Immunol. 2023;8(84):eade7652.

[35]. Sharma J, Khan S, Singh NC, et al. ORMDL3 regulates NLRP3 inflammasome activation by maintaining ER-mitochondria contacts in human macrophages and dictates ulcerative colitis patient outcome. J Biol Chem. 2024;300(4):107120.

[36]. Luo L, Wang F, Xu X, et al. STAT3 promotes NLRP3 inflammasome activation by mediating NLRP3 mitochondrial translocation. Exp Mol Med. 2024;56(9):1980-90.

[37]. Akbal A, Dernst A, Lovotti M, et al. How location and cellular signaling combine to activate the NLRP3 inflammasome. Cell Mol Immunol. 2022;19(11):1201-14.

[38]. Hamilton C, Anand PK. Right place, right time: localisation and assembly of the NLRP3 inflammasome. F1000Res. 2019;8:676.

[39]. Que X, Zheng S, Song Q, et al. Fantastic voyage: the journey of NLRP3 inflammasome activation. Genes Dis. 2024;11(2):819-29.

[40]. Bauernfeind F, Bartok E, Rieger A, et al. Cutting edge: reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome. J Immunol. 2011;187(2):613-7.

[41]. Xian H, Watari K, Sanchez-Lopez E, et al. Oxidized DNA fragments exit mitochondria via mPTP- and VDAC-dependent channels to activate NLRP3 inflammasome and interferon signaling. Immunity. 2022;55(8):1370-85.e8.

[42]. Shimada K, Crother TR, Karlin J, et al. Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis. Immunity. 2012;36(3):401-14.

[43]. Cabral A, Cabral JE, Wang A, et al. Differential binding of NLRP3 to non-oxidized and Ox-mtDNA mediates NLRP3 Inflammasome Activation. Commun Biol. 2023;6(1):578.

[44]. Zhong Z, Liang S, Sanchez-Lopez E, et al. New mitochondrial DNA synthesis enables NLRP3 inflammasome activation. Nature. 2018;560(7717):198-203.

[45]. Billingham LK, Stoolman JS, Vasan K, et al. Mitochondrial electron transport chain is necessary for NLRP3 inflammasome activation. Nat Immunol. 2022;23(5):692-704.

[46]. Zhong Z, Umemura A, Sanchez-Lopez E, et al. NF-kappaB restricts inflammasome activation via elimination of damaged mitochondria. Cell. 2016;164(5):896-910.

[47]. Kim MJ, Bae SH, Ryu JC, et al. SESN2/sestrin2 suppresses sepsis by inducing mitophagy and inhibiting NLRP3 activation in macrophages. Autophagy. 2016;12(8):1272-91.

[48]. Wu KKL, Long K, Lin H, et al. The APPL1-Rab5 axis restricts NLRP3 inflammasome activation through early endosomal-dependent mitophagy in macrophages. Nat Commun. 2021;12(1):6637.

[49]. Nakahira K, Haspel JA, Rathinam VA, et al. Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome. Nat Immunol. 2011;12(3):222-30.

[50]. Shi CS, Shenderov K, Huang NN, et al. Activation of autophagy by inflammatory signals limits IL-1beta production by targeting ubiquitinated inflammasomes for destruction. Nat Immunol. 2012;13(3):255-63.

[51]. Cui H, Banerjee S, Xie N, et al. MafB regulates NLRP3 inflammasome activation by sustaining p62 expression in macrophages. Commun Biol. 2023;6(1):1047.

[52]. Barrow ER, Valionyte E, Baxter CR, et al. Discovery of SQSTM1/p62-dependent P-bodies that regulate the NLRP3 inflammasome. Cell Rep. 2024;43(3):113935.

[53]. Park S, Juliana C, Hong S, et al. The mitochondrial antiviral protein MAVS associates with NLRP3 and regulates its inflammasome activity. J Immunol. 2013;191(8):4358-66.

[54]. Franchi L, Eigenbrod T, Munoz-Planillo R, et al. Cytosolic double-stranded RNA activates the NLRP3 inflammasome via MAVS-induced membrane permeabilization and K+ efflux. J Immunol. 2014;193(8):4214-22.

[55]. Ermler ME, Traylor Z, Patel K, et al. Rift Valley fever virus infection induces activation of the NLRP3 inflammasome. Virology. 2014;449:174-80.

[56]. Ichinohe T, Yamazaki T, Koshiba T, et al. Mitochondrial protein mitofusin 2 is required for NLRP3 inflammasome activation after RNA virus infection. Proc Natl Acad Sci U S A. 2013;110(44):17963-8.

[57]. Shi CS, Kehrl JH. Cytochrome c negatively regulates NLRP3 inflammasomes. PLoS One. 2016;11(12):e0167636.

[58]. Park YJ, Dodantenna N, Kim Y, et al. MARCH5-dependent NLRP3 ubiquitination is required for mitochondrial NLRP3-NEK7 complex formation and NLRP3 inflammasome activation. EMBO J. 2023;42(19):e113481.

[59]. Jiang Q, Tang G, Zhong XM, et al. Role of Stat3 in NLRP3/caspase-1-mediated hippocampal neuronal pyroptosis in epileptic mice. Synapse. 2021;75(12):e22221.

[60]. Liu Y, Yang H, Zhu F, et al. Inhibition of STAT3 phosphorylation by colchicine regulates NLRP3 activation to alleviate sepsis-induced acute lung injury. Inflammopharmacology. 2023;31(4):2007-21.

[61]. Zhu L, Wang Z, Sun X, et al. STAT3/Mitophagy axis coordinates macrophage NLRP3 inflammasome activation and inflammatory bone loss. J Bone Miner Res. 2023;38(2):335-53.

[62]. Bronner DN, Abuaita BH, Chen X, et al. Endoplasmic reticulum stress activates the inflammasome via NLRP3- and caspase-2-driven mitochondrial damage. Immunity. 2015;43(3):451-62.

[63]. Kim S, Joe Y, Jeong SO, et al. Endoplasmic reticulum stress is sufficient for the induction of IL-1beta production via activation of the NF-kappaB and inflammasome pathways. Innate Immun. 2014;20(8):799-815.

[64]. Lebeaupin C, Proics E, de Bieville CH, et al. ER stress induces NLRP3 inflammasome activation and hepatocyte death. Cell Death Dis. 2015;6(9):e1879.

[65]. Menu P, Mayor A, Zhou R, et al. ER stress activates the NLRP3 inflammasome via an UPR-independent pathway. Cell Death Dis. 2012;3(1):e261.

[66]. Lerner AG, Upton JP, Praveen PV, et al. IRE1alpha induces thioredoxin-interacting protein to activate the NLRP3 inflammasome and promote programmed cell death under irremediable ER stress. Cell Metab. 2012;16(2):250-64.

[67]. Pereira AC, De Pascale J, Resende R, et al. ER-mitochondria communication is involved in NLRP3 inflammasome activation under stress conditions in the innate immune system. Cell Mol Life Sci. 2022;79(4):213.

[68]. Ni H, Ou Z, Wang Y, et al. XBP1 modulates endoplasmic reticulum and mitochondria crosstalk via regulating NLRP3 in renal ischemia/reperfusion injury. Cell Death Discov. 2023;9(1):69.

[69]. de la Roche M, Hamilton C, Mortensen R, et al. Trafficking of cholesterol to the ER is required for NLRP3 inflammasome activation. J Cell Biol. 2018;217(10):3560-76.

[70]. Lee GS, Subramanian N, Kim AI, et al. The calcium-sensing receptor regulates the NLRP3 inflammasome through Ca2+ and cAMP. Nature. 2012;492(7427):123-7.

[71]. Csordas G, Weaver D, Hajnoczky G. Endoplasmic reticulum-mitochondrial contactology: structure and signaling functions. Trends Cell Biol. 2018;28(7):523-40.

[72]. Talty A, Deegan S, Ljujic M, et al. Inhibition of IRE1alpha RNase activity reduces NLRP3 inflammasome assembly and processing of pro-IL1beta. Cell Death Dis. 2019;10(9):622.

[73]. Halle A, Hornung V, Petzold GC, et al. The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat Immunol. 2008;9(8):857-65.

[74]. Hornung V, Bauernfeind F, Halle A, et al. Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat Immunol. 2008;9(8):847-56.

[75]. Chen Y, Li X, Boini KM, et al. Endothelial Nlrp3 inflammasome activation associated with lysosomal destabilization during coronary arteritis. Biochim Biophys Acta. 2015;1853(2):396-408.

[76]. Duewell P, Kono H, Rayner KJ, et al. NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals. Nature. 2010;464(7293):1357-61.

[77]. Barlan AU, Danthi P, Wiethoff CM. Lysosomal localization and mechanism of membrane penetration influence nonenveloped virus activation of the NLRP3 inflammasome. Virology. 2011;412(2):306-14.

[78]. Orlowski GM, Colbert JD, Sharma S, et al. Multiple cathepsins promote pro-IL-1beta synthesis and NLRP3-mediated IL-1beta activation. J Immunol. 2015;195(4):1685-97.

[79]. Chevriaux A, Pilot T, Derangere V, et al. Cathepsin B is required for NLRP3 inflammasome activation in macrophages, through NLRP3 interaction. Front Cell Dev Biol. 2020;8:167.

[80]. Amaral EP, Riteau N, Moayeri M, et al. Lysosomal cathepsin release is required for NLRP3-inflammasome activation by mycobacterium tuberculosis in infected macrophages. Front Immunol. 2018;9:1427.

[81]. Campden RI, Zhang Y. The role of lysosomal cysteine cathepsins in NLRP3 inflammasome activation. Arch Biochem Biophys. 2019;670:32-42.

[82]. Gaidt MM, Ebert TS, Chauhan D, et al. The DNA inflammasome in human myeloid cells is initiated by a STING-cell death program upstream of NLRP3. Cell. 2017;171(5):1110-24.e18.

[83]. Hou Y, He H, Ma M, et al. Apilimod activates the NLRP3 inflammasome through lysosome-mediated mitochondrial damage. Front Immunol. 2023;14:1128700.

[84]. Dong H, Zhao B, Chen J, et al. Mitochondrial calcium uniporter promotes phagocytosis-dependent activation of the NLRP3 inflammasome. Proc Natl Acad Sci U S A. 2022;119(26):e2123247119.

[85]. Hong S, Hwang I, Gim E, et al. Brefeldin A-sensitive ER-Golgi vesicle trafficking contributes to NLRP3-dependent caspase-1 activation. FASEB J. 2019;33(3):4547-58.

[86]. Yu T, Hou D, Zhao J, et al. NLRP3 Cys126 palmitoylation by ZDHHC7 promotes inflammasome activation. Cell Rep. 2024;43(4):114070.

[87]. Wang L, Cai J, Zhao X, et al. Palmitoylation prevents sustained inflammation by limiting NLRP3 inflammasome activation through chaperone-mediated autophagy. Mol Cell. 2023;83(2):281-97.e10.

[88]. Williams DM, Peden AA. ,-acylation of NLRP3 provides a nigericin sensitive gating mechanism that controls access to the Golgi. Elife. 2024;13:RP94302.

[89]. Zheng S, Que X, Wang S, et al. ZDHHC5-mediated NLRP3 palmitoylation promotes NLRP3-NEK7 interaction and inflammasome activation. Mol Cell. 2023;83(24):4570-85.e7.

[90]. Buser DP, Spang A. Protein sorting from endosomes to the TGN. Front Cell Dev Biol. 2023;11:1140605.

[91]. Misawa T, Takahama M, Kozaki T, et al. Microtubule-driven spatial arrangement of mitochondria promotes activation of the NLRP3 inflammasome. Nat Immunol. 2013;14(5):454-60.

[92]. He Y, Zeng MY, Yang D, et al. NEK7 is an essential mediator of NLRP3 activation downstream of potassium efflux. Nature. 2016;530(7590):354-7.

[93]. Shi H, Wang Y, Li X, et al. NLRP3 activation and mitosis are mutually exclusive events coordinated by NEK7, a new inflammasome component. Nat Immunol. 2016;17(3):250-8.

[94]. Yang XD, Li W, Zhang S, et al. PLK4 deubiquitination by Spata2-CYLD suppresses NEK7-mediated NLRP3 inflammasome activation at the centrosome. EMBO J. 2020;39(2):e102201.

[95]. Baroja-Mazo A, Martin-Sanchez F, Gomez AI, et al. The NLRP3 inflammasome is released as a particulate danger signal that amplifies the inflammatory response. Nat Immunol. 2014;15(8):738-48.

[96]. Gluck IM, Mathias GP, Strauss S, et al. Nanoscale organization of the endogenous ASC speck. iScience. 2023;26(12):108382.

[97]. Wang L, Shi S, Unterreiner A, et al. HDAC6/aggresome processing pathway importance for inflammasome formation is context-dependent. J Biol Chem. 2024;300(2):105638.

[98]. Hochheiser IV, Pilsl M, Hagelueken G, et al. Structure of the NLRP3 decamer bound to the cytokine release inhibitor CRID3. Nature. 2022;604(7904):184-9.

[99]. Ito M, Shichita T, Okada M, et al. Bruton’s tyrosine kinase is essential for NLRP3 inflammasome activation and contributes to ischaemic brain injury. Nat Commun. 2015;6:7360.

[100]. Liu X, Pichulik T, Wolz OO, et al. Human NACHT, LRR, and PYD domain-containing protein 3 (NLRP3) inflammasome activity is regulated by and potentially targetable through Bruton tyrosine kinase. J Allergy Clin Immunol. 2017;140(4):1054-67.e10.

[101]. Theodoropoulou K, Spel L, Zaffalon L, et al. NLRP3 leucine-rich repeats control induced and spontaneous inflammasome activation in cryopyrin-associated periodic syndrome. J Allergy Clin Immunol. 2023;151(1):222-32.e9.

[102]. Hoss F, Mueller JL, Rojas Ringeling F, et al. Alternative splicing regulates stochastic NLRP3 activity. Nat Commun. 2019;10(1):3238.

[103]. Zhang X, Wang Z, Zheng Y, et al. Inhibitors of the NLRP3 inflammasome pathway as promising therapeutic candidates for inflammatory diseases (Review). Int J Mol Med. 2023;51(4):35.

[104]. Tengesdal IW, Banks M, Dinarello CA, et al. Screening NLRP3 drug candidates in clinical development: lessons from existing and emerging technologies. Front Immunol. 2024;15:1422249.

[105]. Xu J, Pickard JM, Nunez G. FDA-approved disulfiram inhibits the NLRP3 inflammasome by regulating NLRP3 palmitoylation. Cell Rep. 2024;43(8):114609.

[106]. Deng W, Yang Z, Yue H, et al. Disulfiram suppresses NLRP3 inflammasome activation to treat peritoneal and gouty inflammation. Free Radic Biol Med. 2020;152:8-17.

[107]. Wei S, Xiao Z, Huang J, et al. Disulfiram inhibits oxidative stress and NLRP3 inflammasome activation to prevent LPS-induced cardiac injury. Int Immunopharmacol. 2022;105:108545.

[108]. Kang JH, Lee SB, Seok J, et al. Novel Activity of ODZ10117, a STAT3 Inhibitor, for Regulation of NLRP3 Inflammasome Activation. Int J Mol Sci . 2023;24(7):6079.,

引用本文

Spector, Lauren; Subramanian, Naeha. Revealing the dance of NLRP3: spatiotemporal patterns in inflammasome activation [J]. Immunometabolism. 2025; 7; (1). 1 - 9.

文献评论

相关学者

相关机构