메뉴 건너뛰기




Volumn 11, Issue , 2018, Pages 359-374

Spotlight on the NLRP3 inflammasome pathway

Author keywords

Inflammasome; Inflammation; NLRP3; Post translational modifications

Indexed keywords

APOPTOSIS REGULATORY PROTEIN; CRYOPYRIN; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME;

EID: 85057986542     PISSN: None     EISSN: 11787031     Source Type: Journal    
DOI: 10.2147/JIR.S141220     Document Type: Review
Times cited : (218)

References (121)
  • 1
    • 47949099098 scopus 로고    scopus 로고
    • Origin and physiological roles of inflammation
    • Medzhitov R. Origin and physiological roles of inflammation. Nature. 2008;454(7203):428–435.
    • (2008) Nature , vol.454 , Issue.7203 , pp. 428-435
    • Medzhitov, R.1
  • 2
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtues of a nonclonal system of recognition
    • Medzhitov R, Janeway CA. Innate immunity: the virtues of a nonclonal system of recognition. Cell. 1997;91(3):295–298.
    • (1997) Cell , vol.91 , Issue.3 , pp. 295-298
    • Medzhitov, R.1    Janeway, C.A.2
  • 3
    • 0028201732 scopus 로고
    • Tolerance, danger, and the extended family
    • Matzinger P. Tolerance, danger, and the extended family. Annu Rev Immunol. 1994;12:991–1045.
    • (1994) Annu Rev Immunol , vol.12 , pp. 991-1045
    • Matzinger, P.1
  • 4
    • 84944748927 scopus 로고    scopus 로고
    • Structural and biochemical basis for induced self-propagation of NLRC4
    • Hu Z, Zhou Q, Zhang C, et al. Structural and biochemical basis for induced self-propagation of NLRC4. Science. 2015;350(6259):399–404.
    • (2015) Science , vol.350 , Issue.6259 , pp. 399-404
    • Hu, Z.1    Zhou, Q.2    Zhang, C.3
  • 5
    • 63649145255 scopus 로고    scopus 로고
    • AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
    • 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(7237):509–513.
    • (2009) Nature , vol.458 , Issue.7237 , pp. 509-513
    • Fernandes-Alnemri, T.1    Yu, J.-W.2    Datta, P.3    Wu, J.4    Alnemri, E.S.5
  • 6
    • 84866512376 scopus 로고    scopus 로고
    • Cell volume regulation modulates NLRP3 inflammasome activation
    • Compan V, Baroja-Mazo A, López-Castejón G, et al. Cell volume regulation modulates NLRP3 inflammasome activation. Immunity. 2012;37(3):487–500.
    • (2012) Immunity , vol.37 , Issue.3 , pp. 487-500
    • Compan, V.1    Baroja-Mazo, A.2    López-Castejón, G.3
  • 7
    • 84896332642 scopus 로고    scopus 로고
    • Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes
    • Lu A, Magupalli VG, Ruan J, et al. Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes. Cell. 2014;156(6):1193–1206.
    • (2014) Cell , vol.156 , Issue.6 , pp. 1193-1206
    • Lu, A.1    Magupalli, V.G.2    Ruan, J.3
  • 8
    • 0033607768 scopus 로고    scopus 로고
    • ASC, a novel 22-kDa protein, aggregates during apoptosis of human promyelocytic leukemia HL-60 cells
    • Masumoto J, Taniguchi S, Ayukawa K, et al. ASC, a novel 22-kDa protein, aggregates during apoptosis of human promyelocytic leukemia HL-60 cells. J Biol Chem. 1999;274(48):33835–33838.
    • (1999) J Biol Chem , vol.274 , Issue.48 , pp. 33835-33838
    • Masumoto, J.1    Taniguchi, S.2    Ayukawa, K.3
  • 9
    • 84976315206 scopus 로고    scopus 로고
    • ASC filament formation serves as a signal amplification mechanism for inflammasomes
    • Dick MS, Sborgi L, Rühl S, Hiller S, Broz P. ASC filament formation serves as a signal amplification mechanism for inflammasomes. Nat Commun. 2016;7:11929.
    • (2016) Nat Commun , vol.7
    • Dick, M.S.1    Sborgi, L.2    Rühl, S.3    Hiller, S.4    Broz, P.5
  • 10
    • 84906571225 scopus 로고    scopus 로고
    • Inflammatory caspases are innate immune receptors for intracellular LPS
    • Shi J, Zhao Y, Wang Y, et al. Inflammatory caspases are innate immune receptors for intracellular LPS. Nature. 2014;514(7521):187–192.
    • (2014) Nature , vol.514 , Issue.7521 , pp. 187-192
    • Shi, J.1    Zhao, Y.2    Wang, Y.3
  • 11
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • Schroder K, Tschopp J. The inflammasomes. Cell. 2010;140(6):821–832.
    • (2010) Cell , vol.140 , Issue.6 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 12
    • 84942856523 scopus 로고    scopus 로고
    • Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling
    • Kayagaki N, Stowe IB, Lee BL, et al. Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling. Nature. 2015;526(7575):666–671.
    • (2015) Nature , vol.526 , Issue.7575 , pp. 666-671
    • Kayagaki, N.1    Stowe, I.B.2    Lee, B.L.3
  • 13
    • 84978128481 scopus 로고    scopus 로고
    • GsdmD p30 elicited by caspase-11 during pyroptosis forms pores in membranes
    • Aglietti RA, Estevez A, Gupta A, et al. GsdmD p30 elicited by caspase-11 during pyroptosis forms pores in membranes. Proc Natl Acad Sci U S A. 2016;113(28):7858–7863.
    • (2016) Proc Natl Acad Sci U S A , vol.113 , Issue.28 , pp. 7858-7863
    • Aglietti, R.A.1    Estevez, A.2    Gupta, A.3
  • 14
  • 15
    • 84904646033 scopus 로고    scopus 로고
    • The NLRP3 inflammasome is released as a particulate danger signal that amplifies the inflammatory response
    • Baroja-Mazo A, Martín-Sánchez 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):738–748.
    • (2014) Nat Immunol , vol.15 , Issue.8 , pp. 738-748
    • Baroja-Mazo, A.1    Martín-Sánchez, F.2    Gomez, A.I.3
  • 16
    • 84904692363 scopus 로고    scopus 로고
    • The adaptor ASC has extracellular and “prionoid” activities that propagate inflammation
    • Franklin BS, Bossaller L, De Nardo D, et al. The adaptor ASC has extracellular and “prionoid” activities that propagate inflammation. Nat Immunol. 2014;15(8):727–737.
    • (2014) Nat Immunol , vol.15 , Issue.8 , pp. 727-737
    • Franklin, B.S.1    Bossaller, L.2    de Nardo, D.3
  • 17
    • 84943200249 scopus 로고    scopus 로고
    • Caspase-11 activates a canonical NLRP3 inflammasome by promoting K+ efflux
    • Rühl S, Broz P. Caspase-11 activates a canonical NLRP3 inflammasome by promoting K+ efflux. Eur J Immunol. 2015;45(10):2927–2936.
    • (2015) Eur J Immunol , vol.45 , Issue.10 , pp. 2927-2936
    • Rühl, S.1    Broz, P.2
  • 18
    • 0034774916 scopus 로고    scopus 로고
    • Familial cold autoinflammatory syndrome
    • Hoffman DHM. Familial cold autoinflammatory syndrome. J Allergy Clin Immunol. 2001;108(4):615–620.
    • (2001) J Allergy Clin Immunol , vol.108 , Issue.4 , pp. 615-620
    • Hoffman, D.H.M.1
  • 19
    • 37349036932 scopus 로고    scopus 로고
    • Cryopyrin-associated periodic syndromes and autoinflammation
    • Shinkai K, Mccalmont TH, Leslie KS. Cryopyrin-associated periodic syndromes and autoinflammation. Clin Exp Dermatol. 2008;33(1):1–9.
    • (2008) Clin Exp Dermatol , vol.33 , Issue.1 , pp. 1-9
    • Shinkai, K.1    McCalmont, T.H.2    Leslie, K.S.3
  • 20
    • 32944468985 scopus 로고    scopus 로고
    • Gout-associ-ated uric acid crystals activate the NALP3 inflammasome
    • Martinon F, Pétrilli V, Mayor A, Tardivel A, Tschopp J. Gout-associ-ated uric acid crystals activate the NALP3 inflammasome. Nature. 2006;440(7081):237–241.
    • (2006) Nature , vol.440 , Issue.7081 , pp. 237-241
    • Martinon, F.1    Pétrilli, V.2    Mayor, A.3    Tardivel, A.4    Tschopp, J.5
  • 21
    • 79751512463 scopus 로고    scopus 로고
    • The NALP3/NLRP3 inflammasome instigates obesity-induced autoinflammation and insulin resistance
    • Vandanmagsar B, Youm Y-H, Ravussin A, et al. The NALP3/NLRP3 inflammasome instigates obesity-induced autoinflammation and insulin resistance. Nat Med. 2011;17(2):179–188.
    • (2011) Nat Med , vol.17 , Issue.2 , pp. 179-188
    • Vandanmagsar, B.1    Youm, Y.-H.2    Ravussin, A.3
  • 22
    • 84885167222 scopus 로고    scopus 로고
    • Canonical Nlrp3 inflammasome links systemic low grade inflammation to functional decline in aging
    • Youm Y-H, Grant RW, McCabe LR, et al. Canonical Nlrp3 inflammasome links systemic low grade inflammation to functional decline in aging. Cell Metab. 2013;18(4):519–532.
    • (2013) Cell Metab , vol.18 , Issue.4 , pp. 519-532
    • Youm, Y.-H.1    Grant, R.W.2    McCabe, L.R.3
  • 23
    • 84903269246 scopus 로고    scopus 로고
    • Innate immune activation in neurodegenerative disease
    • Heneka MT, Kummer MP, Latz E. Innate immune activation in neurodegenerative disease. Nat Rev Immunol. 2014;14(7):463–477.
    • (2014) Nat Rev Immunol , vol.14 , Issue.7 , pp. 463-477
    • Heneka, M.T.1    Kummer, M.P.2    Latz, E.3
  • 24
    • 84858677223 scopus 로고    scopus 로고
    • Sensing and reacting to microbes via the inflammasomes
    • Franchi L, Muñoz-Planillo R, Núñez G. Sensing and reacting to microbes via the inflammasomes. Nat Immunol. 2012;13(4):325–332.
    • (2012) Nat Immunol , vol.13 , Issue.4 , pp. 325-332
    • Franchi, L.1    Muñoz-Planillo, R.2    Núñez, G.3
  • 25
    • 84959917649 scopus 로고    scopus 로고
    • Molecular mechanisms regulating NLRP3 inflammasome activation
    • Jo E-K, Kim JK, Shin D-M, Sasakawa C. Molecular mechanisms regulating NLRP3 inflammasome activation. Cell Mol Immunol. 2016;13(2):148–159.
    • (2016) Cell Mol Immunol , vol.13 , Issue.2 , pp. 148-159
    • Jo, E.-K.1    Kim, J.K.2    Shin, D.-M.3    Sasakawa, C.4
  • 26
    • 84892149853 scopus 로고    scopus 로고
    • An update on PYRIN domain-containing pattern recognition receptors: From immunity to pathology
    • Ratsimandresy RA, Dorfleutner A, Stehlik C. An update on PYRIN domain-containing pattern recognition receptors: from immunity to pathology. Front Immunol. 2013;4:440.
    • (2013) Front Immunol , vol.4 , pp. 440
    • Ratsimandresy, R.A.1    Dorfleutner, A.2    Stehlik, C.3
  • 27
    • 84964388536 scopus 로고    scopus 로고
    • Monocytes take their own path to IL-1β
    • Elliott EI, Sutterwala FS. Monocytes take their own path to IL-1β. Immunity. 2016;44(4):713–715.
    • (2016) Immunity , vol.44 , Issue.4 , pp. 713-715
    • Elliott, E.I.1    Sutterwala, F.S.2
  • 28
    • 77955703092 scopus 로고    scopus 로고
    • RAGE: A multi-ligand receptor unveiling novel insights in health and disease
    • Alexiou P, Chatzopoulou M, Pegklidou K, Demopoulos VJ. RAGE: a multi-ligand receptor unveiling novel insights in health and disease. Curr Med Chem. 2010;17(21):2232–2252.
    • (2010) Curr Med Chem , vol.17 , Issue.21 , pp. 2232-2252
    • Alexiou, P.1    Chatzopoulou, M.2    Pegklidou, K.3    Demopoulos, V.J.4
  • 29
    • 80555126061 scopus 로고    scopus 로고
    • Hemorrhagic shock activation of NLRP3 inflammasome in lung endothelial cells
    • Xiang M, Shi X, Li Y, et al. Hemorrhagic shock activation of NLRP3 inflammasome in lung endothelial cells. J Immunol. 2011;187(9):4809–4817.
    • (2011) J Immunol , vol.187 , Issue.9 , pp. 4809-4817
    • Xiang, M.1    Shi, X.2    Li, Y.3
  • 30
    • 33846330896 scopus 로고    scopus 로고
    • Nod-like proteins in immunity, inflammation and disease
    • Fritz JH, Ferrero RL, Philpott DJ, Girardin SE. Nod-like proteins in immunity, inflammation and disease. Nat Immunol. 2006;7(12):1250–1257.
    • (2006) Nat Immunol , vol.7 , Issue.12 , pp. 1250-1257
    • Fritz, J.H.1    Ferrero, R.L.2    Philpott, D.J.3    Girardin, S.E.4
  • 31
    • 33746028777 scopus 로고    scopus 로고
    • Intracellular pattern recognition receptors in the host response
    • Meylan E, Tschopp J, Karin M. Intracellular pattern recognition receptors in the host response. Nature. 2006;442(7098):39–44.
    • (2006) Nature , vol.442 , Issue.7098 , pp. 39-44
    • Meylan, E.1    Tschopp, J.2    Karin, M.3
  • 32
    • 34447107898 scopus 로고    scopus 로고
    • Critical role of toll-like receptors and nucleotide oligomerisa-tion domain in the regulation of health and disease
    • Mitchell JA, Paul-Clark MJ, Clarke GW, McMaster SK, Cartwright N. Critical role of toll-like receptors and nucleotide oligomerisa-tion domain in the regulation of health and disease. J Endocrinol. 2007;193(3):323–330.
    • (2007) J Endocrinol , vol.193 , Issue.3 , pp. 323-330
    • Mitchell, J.A.1    Paul-Clark, M.J.2    Clarke, G.W.3    McMaster, S.K.4    Cartwright, N.5
  • 33
    • 70249110860 scopus 로고    scopus 로고
    • Cutting edge: TNF-alpha mediates sensitization to ATP and silica via the NLRP3 inflammasome in the absence of microbial stimulation
    • Franchi L, Eigenbrod T, Núñez G. Cutting edge: TNF-alpha mediates sensitization to ATP and silica via the NLRP3 inflammasome in the absence of microbial stimulation. J Immunol. 2009;183(2):792–796.
    • (2009) J Immunol , vol.183 , Issue.2 , pp. 792-796
    • Franchi, L.1    Eigenbrod, T.2    Núñez, G.3
  • 35
    • 70249138036 scopus 로고    scopus 로고
    • Cutting edge: NF-kappaB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP3 expression
    • Bauernfeind FG, Horvath G, Stutz A, et al. Cutting edge: NF-kappaB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP3 expression. J Immunol. 2009;183(2):787–791.
    • (2009) J Immunol , vol.183 , Issue.2 , pp. 787-791
    • Bauernfeind, F.G.1    Horvath, G.2    Stutz, A.3
  • 36
    • 84989962589 scopus 로고    scopus 로고
    • Aging-associated TNF production primes inflammasome activation and NLRP3-related metabolic disturbances
    • Bauernfeind F, Niepmann S, Knolle PA, Hornung V. Aging-associated TNF production primes inflammasome activation and NLRP3-related metabolic disturbances. J Immunol Baltim Md 1950. 2016;197(7):2900–2908.
    • (2016) J Immunol Baltim Md , vol.197 , Issue.7 , pp. 2900-2908
    • Bauernfeind, F.1    Niepmann, S.2    Knolle, P.A.3    Hornung, V.4
  • 37
    • 84894271641 scopus 로고    scopus 로고
    • FADD and caspase-8 mediate priming and activation of the canonical and noncanonical Nlrp3 inflammasomes
    • Gurung P, Anand PK, Malireddi RKS, et al. FADD and caspase-8 mediate priming and activation of the canonical and noncanonical Nlrp3 inflammasomes. J Immunol. 2014;192(4):1835–1846.
    • (2014) J Immunol , vol.192 , Issue.4 , pp. 1835-1846
    • Gurung, P.1    Anand, P.K.2    Malireddi, R.K.S.3
  • 38
    • 84990051077 scopus 로고    scopus 로고
    • MLKL and FADD are critical for suppressing progressive lymphoproliferative disease and activating the NLRP3 inflammasome
    • Zhang X, Fan C, Zhang H, et al. MLKL and FADD are critical for suppressing progressive lymphoproliferative disease and activating the NLRP3 inflammasome. Cell Rep. 2016;16(12):3247–3259.
    • (2016) Cell Rep , vol.16 , Issue.12 , pp. 3247-3259
    • Zhang, X.1    Fan, C.2    Zhang, H.3
  • 39
    • 79960542894 scopus 로고    scopus 로고
    • Cutting edge: Reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome
    • Bauernfeind F, Bartok E, Rieger A, Franchi L, Núñez G, Hornung V. Cutting edge: reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome. J Immunol Baltim Md 1950. 2011;187(2):613–617.
    • (2011) J Immunol Baltim Md 1950 , vol.187 , Issue.2 , pp. 613-617
    • Bauernfeind, F.1    Bartok, E.2    Rieger, A.3    Franchi, L.4    Núñez, G.5    Hornung, V.6
  • 40
    • 77951240589 scopus 로고    scopus 로고
    • Anti-inflammatory compounds parthenolide and Bay 11-7082 are direct inhibitors of the inflammasome
    • Juliana C, Fernandes-Alnemri T, Wu J, et al. Anti-inflammatory compounds parthenolide and Bay 11-7082 are direct inhibitors of the inflammasome. J Biol Chem. 2010;285(13):9792–9802.
    • (2010) J Biol Chem , vol.285 , Issue.13 , pp. 9792-9802
    • Juliana, C.1    Fernandes-Alnemri, T.2    Wu, J.3
  • 41
    • 84869088114 scopus 로고    scopus 로고
    • Acute lipopolysaccharide priming boosts inflammasome activation independently of inflammasome sensor induction
    • Schroder K, Sagulenko V, Zamoshnikova A, et al. Acute lipopolysaccharide priming boosts inflammasome activation independently of inflammasome sensor induction. Immunobiology. 2012;217(12):1325–1329.
    • (2012) Immunobiology , vol.217 , Issue.12 , pp. 1325-1329
    • Schroder, K.1    Sagulenko, V.2    Zamoshnikova, A.3
  • 42
    • 84867770402 scopus 로고    scopus 로고
    • Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation
    • Juliana C, Fernandes-Alnemri T, Kang S, Farias A, Qin F, Alnemri ES. Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation. J Biol Chem. 2012;287(43):36617–36622.
    • (2012) J Biol Chem , vol.287 , Issue.43 , pp. 36617-36622
    • Juliana, C.1    Fernandes-Alnemri, T.2    Kang, S.3    Farias, A.4    Qin, F.5    Alnemri, E.S.6
  • 43
    • 84885459019 scopus 로고    scopus 로고
    • Cutting edge: TLR signaling licenses IRAK1 for rapid activation of the NLRP3 inflammasome
    • 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(8): 3995–3999.
    • (2013) J Immunol , vol.191 , Issue.8 , pp. 3995-3999
    • Fernandes-Alnemri, T.1    Kang, S.2    Anderson, C.3    Sagara, J.4    Fitzgerald, K.A.5    Alnemri, E.S.6
  • 44
    • 84892610480 scopus 로고    scopus 로고
    • IRAK-1 bypasses priming and directly links TLRs to rapid NLRP3 inflammasome activation
    • Lin K-M, Hu W, Troutman TD, et al. IRAK-1 bypasses priming and directly links TLRs to rapid NLRP3 inflammasome activation. Proc Natl Acad Sci U S A. 2014;111(2):775–780.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , Issue.2 , pp. 775-780
    • Lin, K.-M.1    Hu, W.2    Troutman, T.D.3
  • 45
    • 84932601454 scopus 로고    scopus 로고
    • Caspase-8 scaffolding function and MLKL regulate NLRP3 inflammasome activation downstream of TLR3
    • Kang S, Fernandes-Alnemri T, Rogers C, et al. Caspase-8 scaffolding function and MLKL regulate NLRP3 inflammasome activation downstream of TLR3. Nat Commun. 2015;6:7515.
    • (2015) Nat Commun , vol.6 , pp. 7515
    • Kang, S.1    Fernandes-Alnemri, T.2    Rogers, C.3
  • 46
    • 84872764927 scopus 로고    scopus 로고
    • Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome
    • 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(1):27–40.
    • (2013) Immunity , vol.38 , Issue.1 , pp. 27-40
    • Kang, T.-B.1    Yang, S.-H.2    Toth, B.3    Kovalenko, A.4    Wallach, D.5
  • 47
    • 84869785875 scopus 로고    scopus 로고
    • Cutting edge: Nitric oxide inhibits the NLRP3 inflammasome
    • Hernandez-Cuellar E, Tsuchiya K, Hara H, et al. Cutting edge: nitric oxide inhibits the NLRP3 inflammasome. J Immunol. 2012;189(11):5113–5117.
    • (2012) J Immunol , vol.189 , Issue.11 , pp. 5113-5117
    • Hernandez-Cuellar, E.1    Tsuchiya, K.2    Hara, H.3
  • 48
    • 78650636576 scopus 로고    scopus 로고
    • Tripartite-motif protein 30 negatively regulates NLRP3 inflammasome activation by modulating reactive oxygen species production
    • Hu Y, Mao K, Zeng Y, et al. Tripartite-motif protein 30 negatively regulates NLRP3 inflammasome activation by modulating reactive oxygen species production. J Immunol Baltim Md 1950. 2010;185(12): 7699–7705.
    • (2010) J Immunol Baltim Md 1950 , vol.185 , Issue.12 , pp. 7699-7705
    • Hu, Y.1    Mao, K.2    Zeng, Y.3
  • 49
    • 79951740151 scopus 로고    scopus 로고
    • Type I interferon inhibits interleukin-1 production and inflammasome activation
    • Guarda G, Braun M, Staehli F, et al. Type I interferon inhibits interleukin-1 production and inflammasome activation. Immunity. 2011;34(2):213–223.
    • (2011) Immunity , vol.34 , Issue.2 , pp. 213-223
    • Guarda, G.1    Braun, M.2    Staehli, F.3
  • 50
    • 84921305910 scopus 로고    scopus 로고
    • A20 restricts ubiquitination of pro-interleukin-1β protein complexes and suppresses NLRP3 inflammasome activity
    • Duong BH, Onizawa M, Oses-Prieto JA, et al. A20 restricts ubiquitination of pro-interleukin-1β protein complexes and suppresses NLRP3 inflammasome activity. Immunity. 2015;42(1):55–67.
    • (2015) Immunity , vol.42 , Issue.1 , pp. 55-67
    • Duong, B.H.1    Onizawa, M.2    Oses-Prieto, J.A.3
  • 51
    • 84959420149 scopus 로고    scopus 로고
    • NF-κB restricts inflammasome activation via elimination of damaged mitochondria
    • Zhong Z, Umemura A, Sanchez-Lopez E, et al. NF-κB restricts inflammasome activation via elimination of damaged mitochondria. Cell. 2016;164(5):896–910.
    • (2016) Cell , vol.164 , Issue.5 , pp. 896-910
    • Zhong, Z.1    Umemura, A.2    Sanchez-Lopez, E.3
  • 52
    • 85037103030 scopus 로고    scopus 로고
    • TNF regulates transcription of NLRP3 inflammasome components and inflammatory molecules in cryopyrinopathies
    • McGeough MD, Wree A, Inzaugarat ME, et al. TNF regulates transcription of NLRP3 inflammasome components and inflammatory molecules in cryopyrinopathies. J Clin Invest. 2017;127(12):4488–4497.
    • (2017) J Clin Invest , vol.127 , Issue.12 , pp. 4488-4497
    • McGeough, M.D.1    Wree, A.2    Inzaugarat, M.E.3
  • 53
    • 0037154851 scopus 로고    scopus 로고
    • Relationship between beta-AP peptide aggregation and microglial activation
    • Casal C, Serratosa J, Tusell JM. Relationship between beta-AP peptide aggregation and microglial activation. Brain Res. 2002;928(1–2): 76–84.
    • (2002) Brain Res , vol.928 , Issue.1-2 , pp. 76-84
    • Casal, C.1    Serratosa, J.2    Tusell, J.M.3
  • 54
    • 0035283318 scopus 로고    scopus 로고
    • Pro-inflammatory programmed cell death
    • Cookson BT, Brennan MA. Pro-inflammatory programmed cell death. Trends Microbiol. 2001;9(3):113–114.
    • (2001) Trends Microbiol , vol.9 , Issue.3 , pp. 113-114
    • Cookson, B.T.1    Brennan, M.A.2
  • 55
    • 84880667818 scopus 로고    scopus 로고
    • Cutting edge: The NLRP3 inflammasome links complement-mediated inflammation and IL-1β release
    • Laudisi F, Spreafico R, Evrard M, et al. Cutting edge: the NLRP3 inflammasome links complement-mediated inflammation and IL-1β release. J Immunol. 2013;191(3):1006–1010.
    • (2013) J Immunol , vol.191 , Issue.3 , pp. 1006-1010
    • Laudisi, F.1    Spreafico, R.2    Evrard, M.3
  • 56
    • 84880651157 scopus 로고    scopus 로고
    • The complement membrane attack complex triggers intracellular Ca2+ fluxes leading to NLRP3 inflammasome activation
    • Triantafilou K, Hughes TR, Triantafilou M, Morgan BP. The complement membrane attack complex triggers intracellular Ca2+ fluxes leading to NLRP3 inflammasome activation. J Cell Sci. 2013;126(13):2903–2913.
    • (2013) J Cell Sci , vol.126 , Issue.13 , pp. 2903-2913
    • Triantafilou, K.1    Hughes, T.R.2    Triantafilou, M.3    Morgan, B.P.4
  • 57
    • 0035808396 scopus 로고    scopus 로고
    • Altered cytokine production in mice lacking P2X(7) receptors
    • Solle M, Labasi J, Perregaux DG, et al. Altered cytokine production in mice lacking P2X(7) receptors. J Biol Chem. 2001;276(1):125–132.
    • (2001) J Biol Chem , vol.276 , Issue.1 , pp. 125-132
    • Solle, M.1    Labasi, J.2    Perregaux, D.G.3
  • 58
    • 47849097202 scopus 로고    scopus 로고
    • Silica crystals and aluminum salts mediate NALP-3 inflammasome activation via phagosomal destabilization
    • Hornung V, Bauernfeind F, Halle A, et al. Silica crystals and aluminum salts mediate NALP-3 inflammasome activation via phagosomal destabilization. Nat Immunol. 2008;9(8):847–856.
    • (2008) Nat Immunol , vol.9 , Issue.8 , pp. 847-856
    • Hornung, V.1    Bauernfeind, F.2    Halle, A.3
  • 59
    • 77951800951 scopus 로고    scopus 로고
    • NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals
    • Duewell P, Kono H, Rayner KJ, et al. NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals. Nature. 2010;464(7293):1357–1361.
    • (2010) Nature , vol.464 , Issue.7293 , pp. 1357-1361
    • Duewell, P.1    Kono, H.2    Rayner, K.J.3
  • 60
    • 47849085872 scopus 로고    scopus 로고
    • The NALP3 inflammasome is involved in the innate immune response to amyloid-beta
    • 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):857–865.
    • (2008) Nat Immunol , vol.9 , Issue.8 , pp. 857-865
    • Halle, A.1    Hornung, V.2    Petzold, G.C.3
  • 61
    • 84875908991 scopus 로고    scopus 로고
    • TRPM2 links oxidative stress to NLRP3 inflammasome activation
    • Zhong Z, Zhai Y, Liang S, et al. TRPM2 links oxidative stress to NLRP3 inflammasome activation. Nat Commun. 2013;4:1611.
    • (2013) Nat Commun , vol.4 , pp. 1611
    • Zhong, Z.1    Zhai, Y.2    Liang, S.3
  • 62
    • 84863978096 scopus 로고    scopus 로고
    • Critical role for calcium mobilization in activation of the NLRP3 inflammasome
    • Murakami T, Ockinger J, Yu J, et al. Critical role for calcium mobilization in activation of the NLRP3 inflammasome. Proc Natl Acad Sci U S A. 2012;109(28):11282–11287.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.28 , pp. 11282-11287
    • Murakami, T.1    Ockinger, J.2    Yu, J.3
  • 63
    • 85039992429 scopus 로고    scopus 로고
    • Microglia-derived ASC specks cross-seed amyloid-β in Alzheimer’s disease
    • Venegas C, Kumar S, Franklin BS, et al. Microglia-derived ASC specks cross-seed amyloid-β in Alzheimer’s disease. Nature. 2017;552(7685):355–361.
    • (2017) Nature , vol.552 , Issue.7685 , pp. 355-361
    • Venegas, C.1    Kumar, S.2    Franklin, B.S.3
  • 64
    • 78651393239 scopus 로고    scopus 로고
    • A role for mitochondria in NLRP3 inflammasome activation
    • Zhou R, Yazdi AS, Menu P, Tschopp J. A role for mitochondria in NLRP3 inflammasome activation. Nature. 2011;469(7329):221–225.
    • (2011) Nature , vol.469 , Issue.7329 , pp. 221-225
    • Zhou, R.1    Yazdi, A.S.2    Menu, P.3    Tschopp, J.4
  • 65
    • 84870508924 scopus 로고    scopus 로고
    • The calcium-sensing receptor regulates the NLRP3 inflammasome through Ca2+ and cAMP
    • Lee G-S, Subramanian N, Kim AI, et al. The calcium-sensing receptor regulates the NLRP3 inflammasome through Ca2+ and cAMP. Nature. 2012;492(7427):123–127.
    • (2012) Nature , vol.492 , Issue.7427 , pp. 123-127
    • Lee, G.-S.1    Subramanian, N.2    Kim, A.I.3
  • 66
    • 84871797522 scopus 로고    scopus 로고
    • Extracellular Ca2+ is a danger signal activating the NLRP3 inflammasome through G protein-coupled calcium sensing receptors
    • Rossol M, Pierer M, Raulien N, et al. Extracellular Ca2+ is a danger signal activating the NLRP3 inflammasome through G protein-coupled calcium sensing receptors. Nat Commun. 2012;3:1329.
    • (2012) Nat Commun , vol.3 , pp. 1329
    • Rossol, M.1    Pierer, M.2    Raulien, N.3
  • 68
    • 84927724336 scopus 로고    scopus 로고
    • Initiation and perpetuation of NLRP3 inflammasome activation and assembly
    • Elliott EI, Sutterwala FS. Initiation and perpetuation of NLRP3 inflammasome activation and assembly. Immunol Rev. 2015;265(1):35–52.
    • (2015) Immunol Rev , vol.265 , Issue.1 , pp. 35-52
    • Elliott, E.I.1    Sutterwala, F.S.2
  • 69
    • 84879596906 scopus 로고    scopus 로고
    • K+ efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter
    • Muñoz-Planillo R, Kuffa P, Martínez-Colón G, Smith BL, Rajendiran TM, Núñez G. K+ efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter. Immunity. 2013;38(6):1142–1153.
    • (2013) Immunity , vol.38 , Issue.6 , pp. 1142-1153
    • Muñoz-Planillo, R.1    Kuffa, P.2    Martínez-Colón, G.3    Smith, B.L.4    Rajendiran, T.M.5    Núñez, G.6
  • 70
    • 84862777872 scopus 로고    scopus 로고
    • Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis
    • Shimada K, Crother TR, Karlin J, et al. Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis. Immunity. 2012;36(3):401–414.
    • (2012) Immunity , vol.36 , Issue.3 , pp. 401-414
    • Shimada, K.1    Crother, T.R.2    Karlin, J.3
  • 71
    • 84882614243 scopus 로고    scopus 로고
    • Mitochondrial cardiolipin is required for Nlrp3 inflammasome activation
    • Iyer SS, He Q, Janczy JR, et al. Mitochondrial cardiolipin is required for Nlrp3 inflammasome activation. Immunity. 2013;39(2):311–323.
    • (2013) Immunity , vol.39 , Issue.2 , pp. 311-323
    • Iyer, S.S.1    He, Q.2    Janczy, J.R.3
  • 72
    • 79951642032 scopus 로고    scopus 로고
    • Autophagy proteins regulate innate immune response by inhibiting NALP3 inflam-masome-mediated mitochondrial DNA release
    • Nakahira K, Haspel JA, Rathinam VA, et al. Autophagy proteins regulate innate immune response by inhibiting NALP3 inflam-masome-mediated mitochondrial DNA release. Nat Immunol. 2011;12(3):222–230.
    • (2011) Nat Immunol , vol.12 , Issue.3 , pp. 222-230
    • Nakahira, K.1    Haspel, J.A.2    Rathinam, V.A.3
  • 73
    • 84962219519 scopus 로고    scopus 로고
    • Human monocytes engage an alternative inflammasome pathway
    • Gaidt MM, Ebert TS, Chauhan D, et al. Human monocytes engage an alternative inflammasome pathway. Immunity. 2016;44(4):833–846.
    • (2016) Immunity , vol.44 , Issue.4 , pp. 833-846
    • Gaidt, M.M.1    Ebert, T.S.2    Chauhan, D.3
  • 74
    • 66049134994 scopus 로고    scopus 로고
    • Mast cells mediate neutrophil recruitment and vascular leakage through the NLRP3 inflammasome in histamine-independent urticaria
    • Nakamura Y, Kambe N, Saito M, et al. Mast cells mediate neutrophil recruitment and vascular leakage through the NLRP3 inflammasome in histamine-independent urticaria. J Exp Med. 2009;206(5):1037–1046.
    • (2009) J Exp Med , vol.206 , Issue.5 , pp. 1037-1046
    • Nakamura, Y.1    Kambe, N.2    Saito, M.3
  • 75
    • 84859492693 scopus 로고    scopus 로고
    • The NLRP3/ASC/Cas-pase-1 axis regulates IL-1β processing in neutrophils
    • Mankan AK, Dau T, Jenne D, Hornung V. The NLRP3/ASC/Cas-pase-1 axis regulates IL-1β processing in neutrophils. Eur J Immunol. 2012;42(3):710–715.
    • (2012) Eur J Immunol , vol.42 , Issue.3 , pp. 710-715
    • Mankan, A.K.1    Dau, T.2    Jenne, D.3    Hornung, V.4
  • 76
    • 64049084303 scopus 로고    scopus 로고
    • Differential requirement for the activation of the inflammasome for processing and release of IL-1β in monocytes and macrophages
    • Netea MG, Nold-Petry CA, Nold MF, et al. Differential requirement for the activation of the inflammasome for processing and release of IL-1β in monocytes and macrophages. Blood. 2009;113(10):2324–2335.
    • (2009) Blood , vol.113 , Issue.10 , pp. 2324-2335
    • Netea, M.G.1    Nold-Petry, C.A.2    Nold, M.F.3
  • 77
    • 45849102043 scopus 로고    scopus 로고
    • ATP is released by monocytes stimulated with pathogen-sensing receptor ligands and induces IL-1β and IL-18 secretion in an autocrine way
    • Piccini A, Carta S, Tassi S, Lasiglié D, Fossati G, Rubartelli A. ATP is released by monocytes stimulated with pathogen-sensing receptor ligands and induces IL-1β and IL-18 secretion in an autocrine way. Proc Natl Acad Sci U S A. 2008;105(23):8067–8072.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.23 , pp. 8067-8072
    • Piccini, A.1    Carta, S.2    Tassi, S.3    Lasiglié, D.4    Fossati, G.5    Rubartelli, A.6
  • 78
    • 85039069819 scopus 로고    scopus 로고
    • Familial Mediterranean fever mutations are hypermorphic mutations that specifically decrease the activation threshold of the Pyrin inflammasome
    • Jamilloux Y, Lefeuvre L, Magnotti F, et al. Familial Mediterranean fever mutations are hypermorphic mutations that specifically decrease the activation threshold of the Pyrin inflammasome. Rheumatology. 2018;57(1):100–111.
    • (2018) Rheumatology , vol.57 , Issue.1 , pp. 100-111
    • Jamilloux, Y.1    Lefeuvre, L.2    Magnotti, F.3
  • 79
    • 84876567161 scopus 로고    scopus 로고
    • Microtubule-driven spatial arrangement of mitochondria promotes activation of the NLRP3 inflammasome
    • 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):454–460.
    • (2013) Nat Immunol , vol.14 , Issue.5 , pp. 454-460
    • Misawa, T.1    Takahama, M.2    Kozaki, T.3
  • 80
    • 84876237736 scopus 로고    scopus 로고
    • The adaptor MAVS promotes NLRP3 mitochondrial localization and inflammasome activation
    • Subramanian N, Natarajan K, Clatworthy MR, Wang Z, Germain RN. The adaptor MAVS promotes NLRP3 mitochondrial localization and inflammasome activation. Cell. 2013;153(2):348–361.
    • (2013) Cell , vol.153 , Issue.2 , pp. 348-361
    • Subramanian, N.1    Natarajan, K.2    Clatworthy, M.R.3    Wang, Z.4    Germain, R.N.5
  • 81
    • 84923102584 scopus 로고    scopus 로고
    • Small heterodimer partner interacts with NLRP3 and negatively regulates activation of the NLRP3 inflammasome
    • Yang C-S, Kim J-J, Kim TS, et al. Small heterodimer partner interacts with NLRP3 and negatively regulates activation of the NLRP3 inflammasome. Nat Commun. 2015;6:6115.
    • (2015) Nat Commun , vol.6 , pp. 6115
    • Yang, C.-S.1    Kim, J.-J.2    Kim, T.S.3
  • 82
    • 85046257852 scopus 로고    scopus 로고
    • Cutting edge: Mitochondrial assembly of the NLRP3 inflammasome complex is initiated at priming
    • Elliott EI, Miller AN, Banoth B, et al. Cutting edge: mitochondrial assembly of the NLRP3 inflammasome complex is initiated at priming. J Immunol Baltim Md 1950. 2018;200(9):3047–3052.
    • (2018) J Immunol Baltim Md 1950 , vol.200 , Issue.9 , pp. 3047-3052
    • Elliott, E.I.1    Miller, A.N.2    Banoth, B.3
  • 83
    • 85021673709 scopus 로고    scopus 로고
    • MARK4 regulates NLRP3 positioning and inflammasome activation through a microtubule-dependent mechanism
    • 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.
    • (2017) Nat Commun , vol.8
    • Li, X.1    Thome, S.2    Ma, X.3
  • 84
    • 84893850623 scopus 로고    scopus 로고
    • Participation of c-FLIP in NLRP3 and AIM2 inflammasome activation
    • Wu Y-H, Kuo W-C, Wu Y-J, et al. Participation of c-FLIP in NLRP3 and AIM2 inflammasome activation. Cell Death Differ. 2014;21(3):451–461.
    • (2014) Cell Death Differ , vol.21 , Issue.3 , pp. 451-461
    • Wu, Y.-H.1    Kuo, W.-C.2    Wu, Y.-J.3
  • 86
    • 84885437002 scopus 로고    scopus 로고
    • The mitochondrial antiviral protein MAVS associates with NLRP3 and regulates its inflammasome activity
    • 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):4358–4366.
    • (2013) J Immunol , vol.191 , Issue.8 , pp. 4358-4366
    • Park, S.1    Juliana, C.2    Hong, S.3
  • 87
    • 84929119017 scopus 로고    scopus 로고
    • MAVS promotes inflammasome activation by targeting ASC for K63-linked ubiquitination via the E3 ligase TRAF3
    • Guan K, Wei C, Zheng Z, et al. MAVS promotes inflammasome activation by targeting ASC for K63-linked ubiquitination via the E3 ligase TRAF3. J Immunol Baltim Md 1950. 2015;194(10):4880–4890.
    • (2015) J Immunol Baltim Md 1950 , vol.194 , Issue.10 , pp. 4880-4890
    • Guan, K.1    Wei, C.2    Zheng, Z.3
  • 88
    • 84887086945 scopus 로고    scopus 로고
    • Mitochondrial protein mitofusin 2 is required for NLRP3 inflammasome activation after RNA virus infection
    • Ichinohe T, Yamazaki T, Koshiba T, Yanagi Y. Mitochondrial protein mitofusin 2 is required for NLRP3 inflammasome activation after RNA virus infection. Proc Natl Acad Sci U S A. 2013;110(44):17963–17968.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , Issue.44 , pp. 17963-17968
    • Ichinohe, T.1    Yamazaki, T.2    Koshiba, T.3    Yanagi, Y.4
  • 89
    • 64849097220 scopus 로고    scopus 로고
    • Activation of inflammasomes requires intracellular redistribution of the apoptotic speck-like protein containing a caspase recruitment domain
    • 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(5):3173–3182.
    • (2009) J Immunol , vol.182 , Issue.5 , pp. 3173-3182
    • Bryan, N.B.1    Dorfleutner, A.2    Rojanasakul, Y.3    Stehlik, C.4
  • 90
    • 85028806631 scopus 로고    scopus 로고
    • Protein kinase D at the Golgi controls NLRP3 inflammasome activation
    • Zhang Z, Meszaros G, He W-T, et al. Protein kinase D at the Golgi controls NLRP3 inflammasome activation. J Exp Med. 2017;214(9):2671–2693.
    • (2017) J Exp Med , vol.214 , Issue.9 , pp. 2671-2693
    • Zhang, Z.1    Meszaros, G.2    He, W.-T.3
  • 91
    • 34548031870 scopus 로고    scopus 로고
    • The pyroptosome: A supra-molecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation
    • Fernandes-Alnemri T, Wu J, Yu J-W, et al. The pyroptosome: a supra-molecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation. Cell Death Differ. 2007;14(9):1590–1604.
    • (2007) Cell Death Differ , vol.14 , Issue.9 , pp. 1590-1604
    • Fernandes-Alnemri, T.1    Wu, J.2    Yu, J.-W.3
  • 92
    • 84958971929 scopus 로고    scopus 로고
    • Nek7 is an essential mediator of NLRP3 activation downstream of potassium efflux
    • He Y, Zeng MY, Yang D, Motro B, Núñez G. Nek7 is an essential mediator of NLRP3 activation downstream of potassium efflux. Nature. 2016;530(7590):354–357.
    • (2016) Nature , vol.530 , Issue.7590 , pp. 354-357
    • He, Y.1    Zeng, M.Y.2    Yang, D.3    Motro, B.4    Núñez, G.5
  • 93
    • 84952931119 scopus 로고    scopus 로고
    • A genome-wide CRISPR (Clustered regularly interspaced short palindromic repeats) screen identifies NEK7 as an essential component of NLRP3 inflammasome activation
    • Schmid-Burgk JL, Chauhan D, Schmidt T, et al. A genome-wide CRISPR (clustered regularly interspaced short palindromic repeats) screen identifies NEK7 as an essential component of NLRP3 inflammasome activation. J Biol Chem. 2016;291(1):103–109.
    • (2016) J Biol Chem , vol.291 , Issue.1 , pp. 103-109
    • Schmid-Burgk, J.L.1    Chauhan, D.2    Schmidt, T.3
  • 94
    • 84949595485 scopus 로고    scopus 로고
    • NLRP3 activation and mitosis are mutually exclusive events coordinated by NEK7, a new inflammasome component
    • 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):250–258.
    • (2016) Nat Immunol , vol.17 , Issue.3 , pp. 250-258
    • Shi, H.1    Wang, Y.2    Li, X.3
  • 96
    • 84857195479 scopus 로고    scopus 로고
    • Activation of autophagy by inflammatory signals limits IL-1β production by targeting ubiquitinated inflammasomes for destruction
    • Shi C-S, Shenderov K, Huang N-N, et al. Activation of autophagy by inflammatory signals limits IL-1β production by targeting ubiquitinated inflammasomes for destruction. Nat Immunol. 2012;13(3):255–263.
    • (2012) Nat Immunol , vol.13 , Issue.3 , pp. 255-263
    • Shi, C.-S.1    Shenderov, K.2    Huang, N.-N.3
  • 97
    • 85028540373 scopus 로고    scopus 로고
    • PTPN22 regulates NLRP3-mediated IL1B secretion in an autophagy dependent manner
    • Epub 2017 Aug 8
    • Spalinger MR, Lang S, Gottier C, et al. PTPN22 regulates NLRP3-mediated IL1B secretion in an autophagy dependent manner. Autophagy. Epub 2017 Aug 8.
    • Autophagy
    • Spalinger, M.R.1    Lang, S.2    Gottier, C.3
  • 98
    • 85029686499 scopus 로고    scopus 로고
    • NLRP3 phosphorylation is an essential priming event for inflammasome activation
    • Song N, Liu Z-S, Xue W, et al. NLRP3 phosphorylation is an essential priming event for inflammasome activation. Mol Cell. 2017;68(1):185–187.
    • (2017) Mol Cell , vol.68 , Issue.1 , pp. 185-187
    • Song, N.1    Liu, Z.-S.2    Xue, W.3
  • 99
    • 27744440753 scopus 로고    scopus 로고
    • Somatic mosaicism of CIAS1 in a patient with chronic infantile neurologic, cutaneous, articular syndrome
    • Saito M, Fujisawa A, Nishikomori R, et al. Somatic mosaicism of CIAS1 in a patient with chronic infantile neurologic, cutaneous, articular syndrome. Arthritis Rheum. 2005;52(11):3579–3585.
    • (2005) Arthritis Rheum , vol.52 , Issue.11 , pp. 3579-3585
    • Saito, M.1    Fujisawa, A.2    Nishikomori, R.3
  • 100
    • 85045906104 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase Pel-lino2 mediates priming of the NLRP3 inflammasome
    • Humphries F, Bergin R, Jackson R, et al. The E3 ubiquitin ligase Pel-lino2 mediates priming of the NLRP3 inflammasome. Nat Commun. 2018;9(1):1560.
    • (2018) Nat Commun , vol.9 , Issue.1 , pp. 1560
    • Humphries, F.1    Bergin, R.2    Jackson, R.3
  • 101
    • 34247265509 scopus 로고    scopus 로고
    • A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses
    • Mayor A, Martinon F, De Smedt T, Pétrilli V, Tschopp J. A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses. Nat Immunol. 2007;8(5): 497–503.
    • (2007) Nat Immunol , vol.8 , Issue.5 , pp. 497-503
    • Mayor, A.1    Martinon, F.2    de Smedt, T.3    Pétrilli, V.4    Tschopp, J.5
  • 102
    • 84937468257 scopus 로고    scopus 로고
    • Lipopolysaccharide primes the NALP3 inflammasome by inhibiting its ubiquitination and degradation mediated by the SCFFBXL2 E3 ligase
    • Han S, Lear TB, Jerome JA, et al. Lipopolysaccharide primes the NALP3 inflammasome by inhibiting its ubiquitination and degradation mediated by the SCFFBXL2 E3 ligase. J Biol Chem. 2015;290(29):18124–18133.
    • (2015) J Biol Chem , vol.290 , Issue.29 , pp. 18124-18133
    • Han, S.1    Lear, T.B.2    Jerome, J.A.3
  • 103
    • 85008235257 scopus 로고    scopus 로고
    • Cigarette smoke destabilizes NLRP3 protein by promoting its ubiquitination
    • Han S, Jerome JA, Gregory AD, Mallampalli RK. Cigarette smoke destabilizes NLRP3 protein by promoting its ubiquitination. Respir Res. 2017;18(1):2.
    • (2017) Respir Res , vol.18 , Issue.1 , pp. 2
    • Han, S.1    Jerome, J.A.2    Gregory, A.D.3    Mallampalli, R.K.4
  • 104
    • 85021799413 scopus 로고    scopus 로고
    • A mechanistic insight into curcumin modulation of the IL-1β secretion and NLRP3 S-glutathi-onylation induced by needle-like cationic cellulose nanocrystals in myeloid cells
    • Guglielmo A, Sabra A, Elbery M, et al. A mechanistic insight into curcumin modulation of the IL-1β secretion and NLRP3 S-glutathi-onylation induced by needle-like cationic cellulose nanocrystals in myeloid cells. Chem Biol Interact. 2017;274:1–12.
    • (2017) Chem Biol Interact , vol.274 , pp. 1-12
    • Guglielmo, A.1    Sabra, A.2    Elbery, M.3
  • 105
    • 84872782298 scopus 로고    scopus 로고
    • Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity
    • Py BF, Kim M-S, Vakifahmetoglu-Norberg H, Yuan J. Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity. Mol Cell. 2013;49(2):331–338.
    • (2013) Mol Cell , vol.49 , Issue.2 , pp. 331-338
    • Py, B.F.1    Kim, M.-S.2    Vakifahmetoglu-Norberg, H.3    Yuan, J.4
  • 106
    • 85033364110 scopus 로고    scopus 로고
    • ARIH2 ubiquitinates NLRP3 and negatively regulates NLRP3 inflammasome activation in macrophages
    • Kawashima A, Karasawa T, Tago K, et al. ARIH2 ubiquitinates NLRP3 and negatively regulates NLRP3 inflammasome activation in macrophages. J Immunol Baltim Md 1950. 2017;199(10):3614–3622.
    • (2017) J Immunol Baltim Md 1950 , vol.199 , Issue.10 , pp. 3614-3622
    • Kawashima, A.1    Karasawa, T.2    Tago, K.3
  • 107
    • 84920990887 scopus 로고    scopus 로고
    • Dopamine controls systemic inflammation through inhibition of NLRP3 inflammasome
    • Yan Y, Jiang W, Liu L, et al. Dopamine controls systemic inflammation through inhibition of NLRP3 inflammasome. Cell. 2015;160(1–2):62–73.
    • (2015) Cell , vol.160 , Issue.1-2 , pp. 62-73
    • Yan, Y.1    Jiang, W.2    Liu, L.3
  • 108
    • 84994817318 scopus 로고    scopus 로고
    • Bile acids control inflammation and metabolic disorder through inhibition of NLRP3 inflammasome
    • Guo C, Xie S, Chi Z, et al. Bile acids control inflammation and metabolic disorder through inhibition of NLRP3 inflammasome. Immunity. 2016;45(4):802–816.
    • (2016) Immunity , vol.45 , Issue.4 , pp. 802-816
    • Guo, C.1    Xie, S.2    Chi, Z.3
  • 109
    • 84983525884 scopus 로고    scopus 로고
    • NLRP3 inflammasome inhibition is disrupted in a group of auto-inflammatory disease CAPS mutations
    • Mortimer L, Moreau F, MacDonald JA, Chadee K. NLRP3 inflammasome inhibition is disrupted in a group of auto-inflammatory disease CAPS mutations. Nat Immunol. 2016;17(10):1176–1186.
    • (2016) Nat Immunol , vol.17 , Issue.10 , pp. 1176-1186
    • Mortimer, L.1    Moreau, F.2    Macdonald, J.A.3    Chadee, K.4
  • 110
    • 85021854728 scopus 로고    scopus 로고
    • NLRP3 inflammasome assembly is regulated by phosphorylation of the pyrin domain
    • Stutz A, Kolbe C-C, Stahl R, et al. NLRP3 inflammasome assembly is regulated by phosphorylation of the pyrin domain. J Exp Med. 2017;214(6):1725–1736.
    • (2017) J Exp Med , vol.214 , Issue.6 , pp. 1725-1736
    • Stutz, A.1    Kolbe, C.-C.2    Stahl, R.3
  • 111
    • 84859515412 scopus 로고    scopus 로고
    • Sphingosine regulates the NLRP3-inflammasome and IL-1β release from macrophages
    • Luheshi NM, Giles JA, Lopez-Castejon G, Brough D. Sphingosine regulates the NLRP3-inflammasome and IL-1β release from macrophages. Eur J Immunol. 2012;42(3):716–725.
    • (2012) Eur J Immunol , vol.42 , Issue.3 , pp. 716-725
    • Luheshi, N.M.1    Giles, J.A.2    Lopez-Castejon, G.3    Brough, D.4
  • 112
    • 84988458393 scopus 로고    scopus 로고
    • NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22
    • Spalinger MR, Kasper S, Gottier C, et al. NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22. J Clin Invest. 2016;126(5):1783–1800.
    • (2016) J Clin Invest , vol.126 , Issue.5 , pp. 1783-1800
    • Spalinger, M.R.1    Kasper, S.2    Gottier, C.3
  • 113
    • 85006056503 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3
    • Song H, Liu B, Huai W, et al. The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3. Nat Commun. 2016;7:13727.
    • (2016) Nat Commun , vol.7
    • Song, H.1    Liu, B.2    Huai, W.3
  • 114
    • 84873710963 scopus 로고    scopus 로고
    • Nitric oxide suppresses NLRP3 inflammasome activation and protects against LPS-induced septic shock
    • Mao K, Chen S, Chen M, et al. Nitric oxide suppresses NLRP3 inflammasome activation and protects against LPS-induced septic shock. Cell Res. 2013;23(2):201–212.
    • (2013) Cell Res , vol.23 , Issue.2 , pp. 201-212
    • Mao, K.1    Chen, S.2    Chen, M.3
  • 115
    • 84871188736 scopus 로고    scopus 로고
    • Nitric oxide controls the immunopathology of tuberculosis by inhibiting NLRP3 inflamma-some-dependent processing of IL-1β
    • Mishra BB, Rathinam VAK, Martens GW, et al. Nitric oxide controls the immunopathology of tuberculosis by inhibiting NLRP3 inflamma-some-dependent processing of IL-1β. Nat Immunol. 2013;14(1):52–60.
    • (2013) Nat Immunol , vol.14 , Issue.1 , pp. 52-60
    • Mishra, B.B.1    Rathinam, V.A.K.2    Martens, G.W.3
  • 116
    • 84903761551 scopus 로고    scopus 로고
    • The linear ubiquitin assembly complex (LUBAC) is essential for NLRP3 inflammasome activation
    • Rodgers MA, Bowman JW, Fujita H, et al. The linear ubiquitin assembly complex (LUBAC) is essential for NLRP3 inflammasome activation. J Exp Med. 2014;211(7):1333–1347.
    • (2014) J Exp Med , vol.211 , Issue.7 , pp. 1333-1347
    • Rodgers, M.A.1    Bowman, J.W.2    Fujita, H.3
  • 117
    • 85011022713 scopus 로고    scopus 로고
    • The deubiquitinating enzyme, ubiquitin-specific peptidase 50, regulates inflammasome activation by targeting the ASC adaptor protein
    • Lee JY, Seo D, You J, et al. The deubiquitinating enzyme, ubiquitin-specific peptidase 50, regulates inflammasome activation by targeting the ASC adaptor protein. FEBS Lett. 2017;591(3):479–490.
    • (2017) FEBS Lett , vol.591 , Issue.3 , pp. 479-490
    • Lee, J.Y.1    Seo, D.2    You, J.3
  • 118
    • 0038682430 scopus 로고    scopus 로고
    • The PAAD/PYRIN-only protein POP1/ASC2 is a modulator of ASC-mediated nuclear-factor-kappa B and pro-caspase-1 regulation
    • Stehlik C, Krajewska M, Welsh K, Krajewski S, Godzik A, Reed JC. The PAAD/PYRIN-only protein POP1/ASC2 is a modulator of ASC-mediated nuclear-factor-kappa B and pro-caspase-1 regulation. Biochem J. 2003;373(Pt 1):101–113.
    • (2003) Biochem J , vol.373 , pp. 101-113
    • Stehlik, C.1    Krajewska, M.2    Welsh, K.3    Krajewski, S.4    Godzik, A.5    Reed, J.C.6
  • 119
    • 84887897805 scopus 로고    scopus 로고
    • Phosphorylation of ASC acts as a molecular switch controlling the formation of speck-like aggregates and inflammasome activity
    • Hara H, Tsuchiya K, Kawamura I, et al. Phosphorylation of ASC acts as a molecular switch controlling the formation of speck-like aggregates and inflammasome activity. Nat Immunol. 2013;14(12):1247–1255.
    • (2013) Nat Immunol , vol.14 , Issue.12 , pp. 1247-1255
    • Hara, H.1    Tsuchiya, K.2    Kawamura, I.3
  • 120
    • 84255178199 scopus 로고    scopus 로고
    • Cellular inhibitors of apoptosis proteins cIAP1 and cIAP2 are required for efficient caspase-1 activation by the inflammasome
    • Labbé K, McIntire CR, Doiron K, Leblanc PM, Saleh M. Cellular inhibitors of apoptosis proteins cIAP1 and cIAP2 are required for efficient caspase-1 activation by the inflammasome. Immunity. 2011;35(6):897–907.
    • (2011) Immunity , vol.35 , Issue.6 , pp. 897-907
    • Labbé, K.1    McIntire, C.R.2    Doiron, K.3    Leblanc, P.M.4    Saleh, M.5
  • 121
    • 47849120473 scopus 로고    scopus 로고
    • Superoxide dismutase 1 regulates caspase-1 and endotoxic shock
    • Meissner F, Molawi K, Zychlinsky A. Superoxide dismutase 1 regulates caspase-1 and endotoxic shock. Nat Immunol. 2008;9(8):866–872.
    • (2008) Nat Immunol , vol.9 , Issue.8 , pp. 866-872
    • Meissner, F.1    Molawi, K.2    Zychlinsky, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.