메뉴 건너뛰기




Volumn 64, Issue 5-6, 2016, Pages 1101-1117

Inflammasomes and its importance in viral infections

Author keywords

Inflammasome; NLRP3; NOD like receptor (NLR); Pyroptosis; Viral infection

Indexed keywords

ADAPTOR PROTEIN; AIM2 PROTEIN; APOPTOSIS ASSOCIATED SPECK LIKE PROTEIN CONTAINING CASPASE RECRUITMENT DOMAIN PROTEIN; CRYOPYRIN; INFLAMMASOME; INTERLEUKIN 18; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; NLRC5 PROTEIN; NLRX1 PROTEIN; NUCLEAR PROTEIN; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; PROCASPASE 1; REGULATOR PROTEIN; RETINOIC ACID INDUCIBLE PROTEIN I; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 84989896434     PISSN: 0257277X     EISSN: 15590755     Source Type: Journal    
DOI: 10.1007/s12026-016-8873-z     Document Type: Review
Times cited : (113)

References (148)
  • 1
    • 0031050034 scopus 로고    scopus 로고
    • Innate immunity: impact on the adaptive immune response
    • COI: 1:CAS:528:DyaK2sXhsl2hurs%3D, PID: 9039775
    • Medzhitov R, Janeway CA Jr. Innate immunity: impact on the adaptive immune response. Curr Opin Immunol. 1997;9(1):4–9.
    • (1997) Curr Opin Immunol , vol.9 , Issue.1 , pp. 4-9
    • Medzhitov, R.1    Janeway, C.A.2
  • 2
    • 0037066502 scopus 로고    scopus 로고
    • Decoding the patterns of self and nonself by the innate immune system
    • COI: 1:CAS:528:DC%2BD38XjtVWiurg%3D
    • Medzhitov R, Janeway CA Jr. Decoding the patterns of self and nonself by the innate immune system. Science (80-). 2002;296(5566):298–300. doi:10.1126/science.1068883.
    • (2002) Science (80-) , vol.296 , Issue.5566 , pp. 298-300
    • Medzhitov, R.1    Janeway, C.A.2
  • 3
    • 77249132637 scopus 로고    scopus 로고
    • Recognition of viruses by cytoplasmic sensors
    • COI: 1:CAS:528:DC%2BC3cXis1Shs70%3D, PID: 20061127
    • Wilkins C, Gale M. Recognition of viruses by cytoplasmic sensors. Curr Opin Immunol. 2010;22(1):41–7. doi:10.1016/j.coi.2009.12.003.
    • (2010) Curr Opin Immunol , vol.22 , Issue.1 , pp. 41-47
    • Wilkins, C.1    Gale, M.2
  • 4
    • 84876833883 scopus 로고    scopus 로고
    • Type I IFN triggers RIG-I/TLR3/NLRP3-dependent inflammasome activation in influenza A virus infected cells
    • COI: 1:CAS:528:DC%2BC3sXntlCrtbc%3D, PID: 23592984
    • Pothlichet J, Meunier I, Davis BK, et al. Type I IFN triggers RIG-I/TLR3/NLRP3-dependent inflammasome activation in influenza A virus infected cells. PLoS Pathog. 2013;9(4):e1003256. doi:10.1371/journal.ppat.1003256.
    • (2013) PLoS Pathog , vol.9 , Issue.4
    • Pothlichet, J.1    Meunier, I.2    Davis, B.K.3
  • 5
    • 84877315779 scopus 로고    scopus 로고
    • Rabies virus is recognized by the NLRP3 inflammasome and activates interleukin-1β release in murine dendritic cells
    • COI: 1:CAS:528:DC%2BC3sXnsV2ltrk%3D, PID: 23487464
    • Lawrence TM, Hudacek AW, de Zoete MR, Flavell RA, Schnell MJ. Rabies virus is recognized by the NLRP3 inflammasome and activates interleukin-1β release in murine dendritic cells. J Virol. 2013;87(10):5848–57. doi:10.1128/JVI.00203-13.
    • (2013) J Virol , vol.87 , Issue.10 , pp. 5848-5857
    • Lawrence, T.M.1    Hudacek, A.W.2    de Zoete, M.R.3    Flavell, R.A.4    Schnell, M.J.5
  • 6
    • 84876237736 scopus 로고    scopus 로고
    • The adaptor MAVS promotes NLRP3 mitochondrial localization and inflammasome activation
    • COI: 1:CAS:528:DC%2BC3sXlvVCmsbk%3D, PID: 23582325
    • Subramanian N, Natarajan K, Clatworthy MR, Wang Z, Germain RN. The adaptor MAVS promotes NLRP3 mitochondrial localization and inflammasome activation. Cell. 2013;153(2):348–61. doi:10.1016/j.cell.2013.02.054.
    • (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
  • 7
    • 84885437002 scopus 로고    scopus 로고
    • The mitochondrial antiviral protein MAVS associates with NLRP3 and regulates its inflammasome activity
    • COI: 1:CAS:528:DC%2BC3sXhsFOju73E, PID: 24048902
    • 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. doi:10.4049/jimmunol.1301170.
    • (2013) J Immunol , vol.191 , Issue.8 , pp. 4358-4366
    • Park, S.1    Juliana, C.2    Hong, S.3
  • 8
    • 84896381627 scopus 로고    scopus 로고
    • Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation
    • COI: 1:CAS:528:DC%2BC2cXksVWht74%3D, PID: 24630723
    • Cai X, Chen J, Xu H, et al. Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation. Cell. 2014;156(6):1207–22. doi:10.1016/j.cell.2014.01.063.
    • (2014) Cell , vol.156 , Issue.6 , pp. 1207-1222
    • Cai, X.1    Chen, J.2    Xu, H.3
  • 9
    • 84907494143 scopus 로고    scopus 로고
    • Cytosolic double-stranded RNA activates the NLRP3 inflammasome via MAVS-induced membrane permeabilization and K+ efflux
    • COI: 1:CAS:528:DC%2BC2cXhs1OitLbP, PID: 25225670
    • Franchi L, Eigenbrod T, Muñoz-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. doi:10.4049/jimmunol.1400582.
    • (2014) J Immunol , vol.193 , Issue.8 , pp. 4214-4222
    • Franchi, L.1    Eigenbrod, T.2    Muñoz-Planillo, R.3
  • 10
    • 84922615231 scopus 로고    scopus 로고
    • Impaired gamma delta T cell-derived IL-17A and inflammasome activation during early respiratory syncytial virus infection in infants
    • PID: 25267484
    • Huang H, Saravia J, You D, Shaw AJ, Cormier SA. Impaired gamma delta T cell-derived IL-17A and inflammasome activation during early respiratory syncytial virus infection in infants. Immunol Cell Biol. 2014;. doi:10.1038/icb.2014.79.
    • (2014) Immunol Cell Biol
    • Huang, H.1    Saravia, J.2    You, D.3    Shaw, A.J.4    Cormier, S.A.5
  • 11
    • 84924651472 scopus 로고    scopus 로고
    • Inflammasome control of viral infection
    • COI: 1:CAS:528:DC%2BC2MXjvFCju70%3D, PID: 25771504
    • Lupfer C, Malik A, Kanneganti T-D. Inflammasome control of viral infection. Curr Opin Virol. 2015;12:38–46. doi:10.1016/j.coviro.2015.02.007.
    • (2015) Curr Opin Virol , vol.12 , pp. 38-46
    • Lupfer, C.1    Malik, A.2    Kanneganti, T.-D.3
  • 12
    • 84890235827 scopus 로고    scopus 로고
    • The interleukin-1 family: back to the future
    • COI: 1:CAS:528:DC%2BC3sXhvFOhtLfE, PID: 24332029
    • Garlanda C, Dinarello CA, Mantovani A. The interleukin-1 family: back to the future. Immunity. 2013;39(6):1003–18. doi:10.1016/j.immuni.2013.11.010.
    • (2013) Immunity , vol.39 , Issue.6 , pp. 1003-1018
    • Garlanda, C.1    Dinarello, C.A.2    Mantovani, A.3
  • 13
    • 81155134753 scopus 로고    scopus 로고
    • Understanding the mechanism of IL-1beta secretion
    • COI: 1:CAS:528:DC%2BC3MXhsV2rsrnI, PID: 22019906
    • Lopez-Castejon G, Brough D. Understanding the mechanism of IL-1beta secretion. Cytokine Growth Factor Rev. 2011;22(4):189–95. doi:10.1016/j.cytogfr.2011.10.001.
    • (2011) Cytokine Growth Factor Rev , vol.22 , Issue.4 , pp. 189-195
    • Lopez-Castejon, G.1    Brough, D.2
  • 14
    • 44649132593 scopus 로고    scopus 로고
    • Sensing intracellular pathogens-NOD-like receptors
    • COI: 1:CAS:528:DC%2BD1cXmvVylsro%3D, PID: 18487086
    • Rietdijk ST, Burwell T, Bertin J, Coyle AJ. Sensing intracellular pathogens-NOD-like receptors. Curr Opin Pharmacol. 2008;8(3):261–6. doi:10.1016/j.coph.2008.04.003.
    • (2008) Curr Opin Pharmacol , vol.8 , Issue.3 , pp. 261-266
    • Rietdijk, S.T.1    Burwell, T.2    Bertin, J.3    Coyle, A.J.4
  • 15
    • 77953464026 scopus 로고    scopus 로고
    • Nlrp3: an immune sensor of cellular stress and infection
    • COI: 1:CAS:528:DC%2BC3cXlsFKms70%3D, PID: 20079456
    • Lamkanfi M, Kanneganti TD. Nlrp3: an immune sensor of cellular stress and infection. Int J Biochem Cell Biol. 2010;42(6):792–5. doi:10.1016/j.biocel.2010.01.008.
    • (2010) Int J Biochem Cell Biol , vol.42 , Issue.6 , pp. 792-795
    • Lamkanfi, M.1    Kanneganti, T.D.2
  • 16
    • 63649133278 scopus 로고    scopus 로고
    • AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
    • COI: 1:CAS:528:DC%2BD1MXht1ehu7w%3D, PID: 19158675
    • Hornung V, Ablasser A, Charrel-Dennis M, et al. AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC. Nature. 2009;458(7237):514–8. doi:10.1038/nature07725.
    • (2009) Nature , vol.458 , Issue.7237 , pp. 514-518
    • Hornung, V.1    Ablasser, A.2    Charrel-Dennis, M.3
  • 17
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • COI: 1:CAS:528:DC%2BD38XmslyrurY%3D, PID: 12191486
    • Martinon F, Burns K, Tschopp J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell. 2002;10(2):417–26.
    • (2002) Mol Cell , vol.10 , Issue.2 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 18
    • 84901310586 scopus 로고    scopus 로고
    • Mechanisms and functions of inflammasomes
    • COI: 1:CAS:528:DC%2BC2cXoslynsLg%3D, PID: 24855941
    • Lamkanfi M, Dixit VM. Mechanisms and functions of inflammasomes. Cell. 2014;157(5):1013–22. doi:10.1016/j.cell.2014.04.007.
    • (2014) Cell , vol.157 , Issue.5 , pp. 1013-1022
    • Lamkanfi, M.1    Dixit, V.M.2
  • 19
    • 84864755627 scopus 로고    scopus 로고
    • The mammalian PYHIN gene family: phylogeny, evolution and expression
    • COI: 1:CAS:528:DC%2BC38Xhs12ntrbN, PID: 22871040
    • Cridland JA, Curley EZ, Wykes MN, et al. The mammalian PYHIN gene family: phylogeny, evolution and expression. BMC Evol Biol. 2012;12(1):140. doi:10.1186/1471-2148-12-140.
    • (2012) BMC Evol Biol , vol.12 , Issue.1 , pp. 140
    • Cridland, J.A.1    Curley, E.Z.2    Wykes, M.N.3
  • 20
    • 84866307663 scopus 로고    scopus 로고
    • Inflammasomes and viruses: cellular defence versus viral offence
    • COI: 1:CAS:528:DC%2BC38Xhs1Siu7jK, PID: 22739062
    • Gram AM, Frenkel J, Ressing ME. Inflammasomes and viruses: cellular defence versus viral offence. J Gen Virol. 2012;93(Pt 10):2063–75. doi:10.1099/vir.0.042978-0.
    • (2012) J Gen Virol , vol.93 , pp. 2063-2075
    • Gram, A.M.1    Frenkel, J.2    Ressing, M.E.3
  • 21
    • 33746028777 scopus 로고    scopus 로고
    • Intracellular pattern recognition receptors in the host response
    • COI: 1:CAS:528:DC%2BD28XmsFWnurk%3D, PID: 16823444
    • Meylan E, Tschopp J, Karin M. Intracellular pattern recognition receptors in the host response. Nature. 2006;442(7098):39–44. doi:10.1038/nature04946.
    • (2006) Nature , vol.442 , Issue.7098 , pp. 39-44
    • Meylan, E.1    Tschopp, J.2    Karin, M.3
  • 22
    • 33846330896 scopus 로고    scopus 로고
    • Nod-like proteins in immunity, inflammation and disease
    • COI: 1:CAS:528:DC%2BD28Xht1Srur7K, PID: 17110941
    • Fritz JH, Ferrero RL, Philpott DJ, Girardin SE. Nod-like proteins in immunity, inflammation and disease. Nat Immunol. 2006;7(12):1250–7. doi:10.1038/ni1412.
    • (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
  • 23
    • 33645958613 scopus 로고    scopus 로고
    • TIR, CARD and PYRIN: three domains for an antimicrobial triad
    • COI: 1:CAS:528:DC%2BD28XjsFWitro%3D, PID: 16528382
    • Werts C, Girardin SE, Philpott DJ. TIR, CARD and PYRIN: three domains for an antimicrobial triad. Cell Death Differ. 2006;13(5):798–815. doi:10.1038/sj.cdd.4401890.
    • (2006) Cell Death Differ , vol.13 , Issue.5 , pp. 798-815
    • Werts, C.1    Girardin, S.E.2    Philpott, D.J.3
  • 24
    • 0038624558 scopus 로고    scopus 로고
    • NODs: intracellular proteins involved in inflammation and apoptosis
    • COI: 1:CAS:528:DC%2BD3sXjvF2mt7k%3D, PID: 12766759
    • Inohara N, Nunez G. NODs: intracellular proteins involved in inflammation and apoptosis. Nat Rev Immunol. 2003;3(5):371–82. doi:10.1038/nri1086.
    • (2003) Nat Rev Immunol , vol.3 , Issue.5 , pp. 371-382
    • Inohara, N.1    Nunez, G.2
  • 25
    • 3142654767 scopus 로고    scopus 로고
    • Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf
    • COI: 1:CAS:528:DC%2BD2cXlsVGjsrk%3D, PID: 15190255
    • Mariathasan S, Newton K, Monack DM, et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature. 2004;430(6996):213–8. doi:10.1038/nature02664.
    • (2004) Nature , vol.430 , Issue.6996 , pp. 213-218
    • Mariathasan, S.1    Newton, K.2    Monack, D.M.3
  • 26
    • 37849013277 scopus 로고    scopus 로고
    • Sunburned skin activates inflammasomes
    • COI: 1:CAS:528:DC%2BD1cXlvVyhuw%3D%3D, PID: 18083030
    • Faustin B, Reed JC. Sunburned skin activates inflammasomes. Trends Cell Biol. 2008;18(1):4–8. doi:10.1016/j.tcb.2007.10.004.
    • (2008) Trends Cell Biol , vol.18 , Issue.1 , pp. 4-8
    • Faustin, B.1    Reed, J.C.2
  • 27
    • 34548688429 scopus 로고    scopus 로고
    • The Nodosome: Nod1 and Nod2 control bacterial infections and inflammation
    • COI: 1:CAS:528:DC%2BD2sXhtVChurrN, PID: 17690884
    • Tattoli I, Travassos LH, Carneiro LA, Magalhaes JG, Girardin SE. The Nodosome: Nod1 and Nod2 control bacterial infections and inflammation. Semin Immunopathol. 2007;29(3):289–301. doi:10.1007/s00281-007-0083-2.
    • (2007) Semin Immunopathol , vol.29 , Issue.3 , pp. 289-301
    • Tattoli, I.1    Travassos, L.H.2    Carneiro, L.A.3    Magalhaes, J.G.4    Girardin, S.E.5
  • 28
    • 18844362879 scopus 로고    scopus 로고
    • Nucleotide binding to CARD12 and its role in CARD12-mediated caspase-1 activation
    • COI: 1:CAS:528:DC%2BD2MXjvFemurw%3D, PID: 15882992
    • Lu C, Wang A, Wang L, Dorsch M, Ocain TD, Xu Y. Nucleotide binding to CARD12 and its role in CARD12-mediated caspase-1 activation. Biochem Biophys Res Commun. 2005;331(4):1114–9. doi:10.1016/j.bbrc.2005.04.027.
    • (2005) Biochem Biophys Res Commun , vol.331 , Issue.4 , pp. 1114-1119
    • Lu, C.1    Wang, A.2    Wang, L.3    Dorsch, M.4    Ocain, T.D.5    Xu, Y.6
  • 29
    • 84881627553 scopus 로고    scopus 로고
    • The expanding role of NLRs in antiviral immunity
    • PID: 23947344
    • Lupfer C, Kanneganti T-D. The expanding role of NLRs in antiviral immunity. Immunol Rev. 2013;255(1):13–24. doi:10.1111/imr.12089.
    • (2013) Immunol Rev , vol.255 , Issue.1 , pp. 13-24
    • Lupfer, C.1    Kanneganti, T.-D.2
  • 30
    • 80052164574 scopus 로고    scopus 로고
    • The inflammasome: an integrated view
    • COI: 1:CAS:528:DC%2BC3MXht1ejtLbO, PID: 21884173
    • Gross O, Thomas CJ, Guarda G, Tschopp J. The inflammasome: an integrated view. Immunol Rev. 2011;243(1):136–51.
    • (2011) Immunol Rev , vol.243 , Issue.1 , pp. 136-151
    • Gross, O.1    Thomas, C.J.2    Guarda, G.3    Tschopp, J.4
  • 31
    • 33845497181 scopus 로고    scopus 로고
    • Inflammatory caspases and inflammasomes: master switches of inflammation
    • COI: 1:CAS:528:DC%2BD28XhtlSqur%2FJ, PID: 16977329
    • Martinon F, Tschopp J. Inflammatory caspases and inflammasomes: master switches of inflammation. Cell Death Differ. 2007;14(1):10–22. doi:10.1038/sj.cdd.4402038.
    • (2007) Cell Death Differ , vol.14 , Issue.1 , pp. 10-22
    • Martinon, F.1    Tschopp, J.2
  • 32
    • 70249138036 scopus 로고    scopus 로고
    • Cutting edge: NF-kappaB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP3 expression
    • COI: 1:CAS:528:DC%2BD1MXotFWgt78%3D, PID: 19570822
    • 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):787–91. doi:10.4049/jimmunol.0901363.
    • (2009) J Immunol , vol.183 , Issue.2 , pp. 787-791
    • Bauernfeind, F.G.1    Horvath, G.2    Stutz, A.3
  • 33
    • 66749174867 scopus 로고    scopus 로고
    • The inflammasomes: guardians of the body
    • COI: 1:CAS:528:DC%2BD1MXlsFSlsbc%3D, PID: 19302040
    • Martinon F, Mayor A, Tschopp J. The inflammasomes: guardians of the body. Annu Rev Immunol. 2009;27(1):229–65. doi:10.1146/annurev.immunol.021908.132715.
    • (2009) Annu Rev Immunol , vol.27 , Issue.1 , pp. 229-265
    • Martinon, F.1    Mayor, A.2    Tschopp, J.3
  • 34
    • 47849097202 scopus 로고    scopus 로고
    • Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
    • COI: 1:CAS:528:DC%2BD1cXoslCmurs%3D, PID: 18604214
    • 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. doi:10.1038/ni.1631.
    • (2008) Nat Immunol , vol.9 , Issue.8 , pp. 847-856
    • Hornung, V.1    Bauernfeind, F.2    Halle, A.3
  • 35
    • 34047261260 scopus 로고    scopus 로고
    • ATP activates a reactive oxygen species-dependent oxidative stress response and secretion of proinflammatory cytokines in macrophages
    • COI: 1:CAS:528:DC%2BD2sXptFCmsg%3D%3D, PID: 17132626
    • Cruz CM, Rinna A, Forman HJ, Ventura AL, Persechini PM, Ojcius DM. ATP activates a reactive oxygen species-dependent oxidative stress response and secretion of proinflammatory cytokines in macrophages. J Biol Chem. 2007;282(5):2871–9. doi:10.1074/jbc.M608083200.
    • (2007) J Biol Chem , vol.282 , Issue.5 , pp. 2871-2879
    • Cruz, C.M.1    Rinna, A.2    Forman, H.J.3    Ventura, A.L.4    Persechini, P.M.5    Ojcius, D.M.6
  • 36
    • 34247118826 scopus 로고    scopus 로고
    • Pannexin-1-mediated recognition of bacterial molecules activates the cryopyrin inflammasome independent of Toll-like receptor signaling
    • COI: 1:CAS:528:DC%2BD2sXltVKjsrY%3D, PID: 17433728
    • Kanneganti TD, Lamkanfi M, Kim YG, et al. Pannexin-1-mediated recognition of bacterial molecules activates the cryopyrin inflammasome independent of Toll-like receptor signaling. Immunity. 2007;26(4):433–43. doi:10.1016/j.immuni.2007.03.008.
    • (2007) Immunity , vol.26 , Issue.4 , pp. 433-443
    • Kanneganti, T.D.1    Lamkanfi, M.2    Kim, Y.G.3
  • 37
    • 84863978096 scopus 로고    scopus 로고
    • Critical role for calcium mobilization in activation of the NLRP3 inflammasome
    • COI: 1:CAS:528:DC%2BC38Xht1ahtL3E, PID: 22733741
    • Murakami T, Ockinger J, Yu J, et al. Critical role for calcium mobilization in activation of the NLRP3 inflammasome. Proc Natl Acad Sci USA. 2012;109(28):11282–7. doi:10.1073/pnas.1117765109.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.28 , pp. 11282-11287
    • Murakami, T.1    Ockinger, J.2    Yu, J.3
  • 38
    • 84870508924 scopus 로고    scopus 로고
    • The calcium-sensing receptor regulates the NLRP3 inflammasome through Ca2+ and cAMP
    • COI: 1:CAS:528:DC%2BC38Xhs1Ckt7bP, PID: 23143333
    • 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):123–7. doi:10.1038/nature11588.
    • (2012) Nature , vol.492 , Issue.7427 , pp. 123-127
    • Lee, G.-S.1    Subramanian, N.2    Kim, A.I.3
  • 39
    • 34250835251 scopus 로고    scopus 로고
    • The inflammasome mediates UVB-induced activation and secretion of interleukin-1beta by keratinocytes
    • COI: 1:CAS:528:DC%2BD2sXntFars70%3D, PID: 17600714
    • Feldmeyer L, Keller M, Niklaus G, Hohl D, Werner S, Beer HD. The inflammasome mediates UVB-induced activation and secretion of interleukin-1beta by keratinocytes. Curr Biol. 2007;17(13):1140–5. doi:10.1016/j.cub.2007.05.074.
    • (2007) Curr Biol , vol.17 , Issue.13 , pp. 1140-1145
    • Feldmeyer, L.1    Keller, M.2    Niklaus, G.3    Hohl, D.4    Werner, S.5    Beer, H.D.6
  • 40
    • 84880651157 scopus 로고    scopus 로고
    • The complement membrane attack complex triggers intracellular Ca2+ fluxes leading to NLRP3 inflammasome activation
    • COI: 1:CAS:528:DC%2BC3sXht1OmsbzJ, PID: 23613465
    • 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(Pt 13):2903–13. doi:10.1242/jcs.124388.
    • (2013) J Cell Sci , vol.126 , pp. 2903-2913
    • Triantafilou, K.1    Hughes, T.R.2    Triantafilou, M.3    Morgan, B.P.4
  • 41
    • 84871797522 scopus 로고    scopus 로고
    • Extracellular Ca2+ is a danger signal activating the NLRP3 inflammasome through G protein-coupled calcium sensing receptors
    • PID: 23271661
    • 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
  • 42
    • 84879596906 scopus 로고    scopus 로고
    • K(+) efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter
    • COI: 1:CAS:528:DC%2BC3sXhtVaitb3M, PID: 23809161
    • Munoz-Planillo R, Kuffa P, Martinez-Colon G, Smith BL, Rajendiran TM, Nunez G. K(+) efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter. Immunity. 2013;38(6):1142–53. doi:10.1016/j.immuni.2013.05.016.
    • (2013) Immunity , vol.38 , Issue.6 , pp. 1142-1153
    • Munoz-Planillo, R.1    Kuffa, P.2    Martinez-Colon, G.3    Smith, B.L.4    Rajendiran, T.M.5    Nunez, G.6
  • 43
    • 84936980740 scopus 로고    scopus 로고
    • NLRP3 inflammasome activation by viroporins of animal viruses
    • COI: 1:CAS:528:DC%2BC2MXhslOqt7zK, PID: 26114475
    • Guo HC, Jin Y, Zhi XY, Yan D, Sun SQ. NLRP3 inflammasome activation by viroporins of animal viruses. Viruses. 2015;7(7):3380–91. doi:10.3390/v7072777.
    • (2015) Viruses , vol.7 , Issue.7 , pp. 3380-3391
    • Guo, H.C.1    Jin, Y.2    Zhi, X.Y.3    Yan, D.4    Sun, S.Q.5
  • 44
    • 84920547918 scopus 로고    scopus 로고
    • Response of host inflammasomes to viral infection
    • COI: 1:CAS:528:DC%2BC2cXhslelsr3E, PID: 25456015
    • Chen IY, Ichinohe T. Response of host inflammasomes to viral infection. Trends Microbiol. 2015;23(1):55–63. doi:10.1016/j.tim.2014.09.007.
    • (2015) Trends Microbiol , vol.23 , Issue.1 , pp. 55-63
    • Chen, I.Y.1    Ichinohe, T.2
  • 45
    • 33846014297 scopus 로고    scopus 로고
    • Critical role for cryopyrin/Nalp3 in activation of caspase-1 in response to viral infection and double-stranded RNA
    • COI: 1:CAS:528:DC%2BD28Xht1eltrvO, PID: 17008311
    • Kanneganti TD, Body-Malapel M, Amer A, et al. Critical role for cryopyrin/Nalp3 in activation of caspase-1 in response to viral infection and double-stranded RNA. J Biol Chem. 2006;281(48):36560–8. doi:10.1074/jbc.M607594200.
    • (2006) J Biol Chem , vol.281 , Issue.48 , pp. 36560-36568
    • Kanneganti, T.D.1    Body-Malapel, M.2    Amer, A.3
  • 46
    • 79955370281 scopus 로고    scopus 로고
    • The NLRP3 inflammasome detects encephalomyocarditis virus and vesicular stomatitis virus infection
    • COI: 1:CAS:528:DC%2BC3MXhtVSmsLjP, PID: 21289120
    • Rajan JV, Rodriguez D, Miao EA, Aderem A. The NLRP3 inflammasome detects encephalomyocarditis virus and vesicular stomatitis virus infection. J Virol. 2011;85(9):4167–72. doi:10.1128/JVI.01687-10.
    • (2011) J Virol , vol.85 , Issue.9 , pp. 4167-4172
    • Rajan, J.V.1    Rodriguez, D.2    Miao, E.A.3    Aderem, A.4
  • 47
    • 84866156921 scopus 로고    scopus 로고
    • Encephalomyocarditis virus viroporin 2B activates NLRP3 inflammasome
    • COI: 1:CAS:528:DC%2BC38Xht1SrsLzO, PID: 22916014
    • Ito M, Yanagi Y, Ichinohe T. Encephalomyocarditis virus viroporin 2B activates NLRP3 inflammasome. PLoS Pathog. 2012;8(8):e1002857. doi:10.1371/journal.ppat.1002857.
    • (2012) PLoS Pathog , vol.8 , Issue.8
    • Ito, M.1    Yanagi, Y.2    Ichinohe, T.3
  • 48
    • 84855830938 scopus 로고    scopus 로고
    • Measles virus V protein inhibits NLRP3 inflammasome-mediated interleukin-1 secretion
    • COI: 1:CAS:528:DC%2BC3MXhs1Shs7jK, PID: 21994456
    • Komune N, Ichinohe T, Ito M, Yanagi Y. Measles virus V protein inhibits NLRP3 inflammasome-mediated interleukin-1 secretion. J Virol. 2011;85(24):13019–26. doi:10.1128/JVI.05942-11.
    • (2011) J Virol , vol.85 , Issue.24 , pp. 13019-13026
    • Komune, N.1    Ichinohe, T.2    Ito, M.3    Yanagi, Y.4
  • 49
    • 84884300082 scopus 로고    scopus 로고
    • Rhinovirus-induced calcium flux triggers NLRP3 and NLRC5 activation in bronchial cells
    • COI: 1:CAS:528:DC%2BC3sXhvVyhu7bO, PID: 23815151
    • Triantafilou K, Kar S, Van Kuppeveld FJM, Triantafilou M. Rhinovirus-induced calcium flux triggers NLRP3 and NLRC5 activation in bronchial cells. Am J Respir Cell Mol Biol. 2013;49:923–34. doi:10.1165/rcmb.2013-0032OC.
    • (2013) Am J Respir Cell Mol Biol , vol.49 , pp. 923-934
    • Triantafilou, K.1    Kar, S.2    Van Kuppeveld, F.J.M.3    Triantafilou, M.4
  • 50
    • 84886248519 scopus 로고    scopus 로고
    • Hepatitis C virus induces interleukin-1 (IL-1)/IL-18 in circulatory and resident liver macrophages
    • COI: 1:CAS:528:DC%2BC3sXhslSqsL7M, PID: 24006444
    • Shrivastava S, Mukherjee A, Ray R, Ray RB. Hepatitis C virus induces interleukin-1 (IL-1)/IL-18 in circulatory and resident liver macrophages. J Virol. 2013;87(22):12284–90. doi:10.1128/JVI.01962-13.
    • (2013) J Virol , vol.87 , Issue.22 , pp. 12284-12290
    • Shrivastava, S.1    Mukherjee, A.2    Ray, R.3    Ray, R.B.4
  • 51
    • 84876871333 scopus 로고    scopus 로고
    • IL-1β production through the NLRP3 inflammasome by hepatic macrophages links hepatitis C virus infection with liver inflammation and disease
    • COI: 1:CAS:528:DC%2BC3sXntlCqsr4%3D, PID: 23633957
    • Negash AA, Ramos HJ, Crochet N, et al. IL-1β production through the NLRP3 inflammasome by hepatic macrophages links hepatitis C virus infection with liver inflammation and disease. PLoS Pathog. 2013;9(4):e1003330. doi:10.1371/journal.ppat.1003330.
    • (2013) PLoS Pathog , vol.9 , Issue.4
    • Negash, A.A.1    Ramos, H.J.2    Crochet, N.3
  • 52
    • 84896456128 scopus 로고    scopus 로고
    • HCV genomic RNA activates the NLRP3 inflammasome in human myeloid cells
    • PID: 24400125
    • Chen W, Xu Y, Li H, et al. HCV genomic RNA activates the NLRP3 inflammasome in human myeloid cells. PLoS ONE. 2014;9(1):e84953. doi:10.1371/journal.pone.0084953.
    • (2014) PLoS ONE , vol.9 , Issue.1
    • Chen, W.1    Xu, Y.2    Li, H.3
  • 53
    • 64049113060 scopus 로고    scopus 로고
    • Fighting the flu with inflammasome signaling
    • COI: 1:CAS:528:DC%2BD1MXls1Sru70%3D, PID: 19371712
    • Owen DM, Gale M. Fighting the flu with inflammasome signaling. Immunity. 2009;30(4):476–8. doi:10.1016/j.immuni.2009.03.011.
    • (2009) Immunity , vol.30 , Issue.4 , pp. 476-478
    • Owen, D.M.1    Gale, M.2
  • 54
    • 78650754831 scopus 로고    scopus 로고
    • Inflammasomes as mediators of immunity against influenza virus
    • COI: 1:CAS:528:DC%2BC3MXkt1Cmtg%3D%3D, PID: 21147034
    • Pang IK, Iwasaki A. Inflammasomes as mediators of immunity against influenza virus. Trends Immunol. 2011;32(1):34–41. doi:10.1016/j.it.2010.11.004.
    • (2011) Trends Immunol , vol.32 , Issue.1 , pp. 34-41
    • Pang, I.K.1    Iwasaki, A.2
  • 55
    • 64049111768 scopus 로고    scopus 로고
    • The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA
    • COI: 1:CAS:528:DC%2BD1MXls1Sqsr8%3D, PID: 19362020
    • Allen IC, Scull MA, Moore CB, et al. The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA. Immunity. 2009;30(4):556–65. doi:10.1016/j.immuni.2009.02.005.
    • (2009) Immunity , vol.30 , Issue.4 , pp. 556-565
    • Allen, I.C.1    Scull, M.A.2    Moore, C.B.3
  • 56
    • 64049096334 scopus 로고    scopus 로고
    • The intracellular sensor NLRP3 mediates key innate and healing responses to influenza A virus via the regulation of caspase-1
    • COI: 1:CAS:528:DC%2BD1MXls1Sqsrw%3D, PID: 19362023
    • Thomas PG, Dash P, Aldridge JR Jr, et al. The intracellular sensor NLRP3 mediates key innate and healing responses to influenza A virus via the regulation of caspase-1. Immunity. 2009;30(4):566–75. doi:10.1016/j.immuni.2009.02.006.
    • (2009) Immunity , vol.30 , Issue.4 , pp. 566-575
    • Thomas, P.G.1    Dash, P.2    Aldridge, J.R.3
  • 57
    • 77951295418 scopus 로고    scopus 로고
    • Influenza virus activates inflammasomes via its intracellular M2 ion channel
    • COI: 1:CAS:528:DC%2BC3cXksFaks7Y%3D, PID: 20383149
    • Ichinohe T, Pang IK, Iwasaki A. Influenza virus activates inflammasomes via its intracellular M2 ion channel. Nat Immunol. 2010;11(5):404–10. doi:10.1038/ni.1861.
    • (2010) Nat Immunol , vol.11 , Issue.5 , pp. 404-410
    • Ichinohe, T.1    Pang, I.K.2    Iwasaki, A.3
  • 58
    • 84856249966 scopus 로고    scopus 로고
    • TLR2/MyD88/NF-kappaB pathway, reactive oxygen species, potassium efflux activates NLRP3/ASC inflammasome during respiratory syncytial virus infection
    • COI: 1:CAS:528:DC%2BC38Xit1Cis7Y%3D, PID: 22295065
    • Segovia J, Sabbah A, Mgbemena V, et al. TLR2/MyD88/NF-kappaB pathway, reactive oxygen species, potassium efflux activates NLRP3/ASC inflammasome during respiratory syncytial virus infection. PLoS ONE. 2012;7(1):e29695. doi:10.1371/journal.pone.0029695.
    • (2012) PLoS ONE , vol.7 , Issue.1
    • Segovia, J.1    Sabbah, A.2    Mgbemena, V.3
  • 59
    • 84878506112 scopus 로고    scopus 로고
    • Activation of the NLRP3 inflammasome by IAV virulence protein PB1-F2 contributes to severe pathophysiology and disease
    • McAuley JL, Tate MD, MacKenzie-Kludas CJ, et al. Activation of the NLRP3 inflammasome by IAV virulence protein PB1-F2 contributes to severe pathophysiology and disease. PLoS Pathog. 2013;. doi:10.1371/journal.ppat.1003392.
    • (2013) PLoS Pathog
    • McAuley, J.L.1    Tate, M.D.2    MacKenzie-Kludas, C.J.3
  • 60
    • 84871392549 scopus 로고    scopus 로고
    • Human respiratory syncytial virus viroporin SH: a viral recognition pathway used by the host to signal inflammasome activation
    • PID: 23229815
    • Triantafilou K, Kar S, Vakakis E, Kotecha S, Triantafilou M. Human respiratory syncytial virus viroporin SH: a viral recognition pathway used by the host to signal inflammasome activation. Thorax. 2013;68(1):66–75. doi:10.1136/thoraxjnl-2012-202182.
    • (2013) Thorax , vol.68 , Issue.1 , pp. 66-75
    • Triantafilou, K.1    Kar, S.2    Vakakis, E.3    Kotecha, S.4    Triantafilou, M.5
  • 61
    • 82455212051 scopus 로고    scopus 로고
    • HIV-1 induces NALP3-inflammasome expression and interleukin-1β secretion in dendritic cells from healthy individuals but not from HIV-positive patients
    • COI: 1:CAS:528:DC%2BC3MXhsFGqtrjE, PID: 21971358
    • Pontillo A, Silva LT, Oshiro TM, Finazzo C, Crovella S, Duarte AJS. HIV-1 induces NALP3-inflammasome expression and interleukin-1β secretion in dendritic cells from healthy individuals but not from HIV-positive patients. AIDS. 2012;26(1):11–8. doi:10.1097/QAD.0b013e32834d697f.
    • (2012) AIDS , vol.26 , Issue.1 , pp. 11-18
    • Pontillo, A.1    Silva, L.T.2    Oshiro, T.M.3    Finazzo, C.4    Crovella, S.5    Duarte, A.J.S.6
  • 62
    • 84870793191 scopus 로고    scopus 로고
    • IL-1β signaling promotes CNS-intrinsic immune control of West Nile virus infection
    • COI: 1:CAS:528:DC%2BC38XhvVKjt7zK, PID: 23209411
    • Ramos HJ, Lanteri MC, Blahnik G, et al. IL-1β signaling promotes CNS-intrinsic immune control of West Nile virus infection. PLoS Pathog. 2012;8(11):e1003039. doi:10.1371/journal.ppat.1003039.
    • (2012) PLoS Pathog , vol.8 , Issue.11
    • Ramos, H.J.1    Lanteri, M.C.2    Blahnik, G.3
  • 63
    • 84875532782 scopus 로고    scopus 로고
    • Inflammasome adaptor protein Apoptosis-associated speck-like protein containing CARD (ASC) is critical for the immune response and survival in west Nile virus encephalitis
    • COI: 1:CAS:528:DC%2BC3sXktlymsL8%3D, PID: 23302887
    • Kumar M, Roe K, Orillo B, et al. Inflammasome adaptor protein Apoptosis-associated speck-like protein containing CARD (ASC) is critical for the immune response and survival in west Nile virus encephalitis. J Virol. 2013;87(7):3655–67. doi:10.1128/JVI.02667-12.
    • (2013) J Virol , vol.87 , Issue.7 , pp. 3655-3667
    • Kumar, M.1    Roe, K.2    Orillo, B.3
  • 64
    • 84857684496 scopus 로고    scopus 로고
    • NLRP3 inflammasome: key mediator of neuroinflammation in murine Japanese encephalitis
    • COI: 1:CAS:528:DC%2BC38Xjs12ltrw%3D, PID: 22393394
    • Kaushik DK, Gupta M, Kumawat KL, Basu A. NLRP3 inflammasome: key mediator of neuroinflammation in murine Japanese encephalitis. PLoS ONE. 2012;7(2):e32270. doi:10.1371/journal.pone.0032270.
    • (2012) PLoS ONE , vol.7 , Issue.2
    • Kaushik, D.K.1    Gupta, M.2    Kumawat, K.L.3    Basu, A.4
  • 65
    • 84888222496 scopus 로고    scopus 로고
    • Platelets mediate increased endothelium permeability in dengue through NLRP3-inflammasome activation
    • COI: 1:CAS:528:DC%2BC3sXhvVehsr7O, PID: 24009231
    • Hottz ED, Lopes JF, Freitas C, et al. Platelets mediate increased endothelium permeability in dengue through NLRP3-inflammasome activation. Blood. 2013;122(20):3405–14. doi:10.1182/blood-2013-05-504449.
    • (2013) Blood , vol.122 , Issue.20 , pp. 3405-3414
    • Hottz, E.D.1    Lopes, J.F.2    Freitas, C.3
  • 66
    • 84872057098 scopus 로고    scopus 로고
    • CLEC5A is critical for dengue virus-induced inflammasome activation in human macrophages
    • COI: 1:CAS:528:DC%2BC3sXps1eqtA%3D%3D, PID: 23152543
    • Wu M-F, Chen S-T, Yang A-H, et al. CLEC5A is critical for dengue virus-induced inflammasome activation in human macrophages. Blood. 2013;121(1):95–106. doi:10.1182/blood-2012-05-430090.
    • (2013) Blood , vol.121 , Issue.1 , pp. 95-106
    • Wu, M.-F.1    Chen, S.-T.2    Yang, A.-H.3
  • 67
    • 84896983616 scopus 로고    scopus 로고
    • Rift valley fever virus infection induces activation of the NLRP3 inflammasome
    • COI: 1:CAS:528:DC%2BC2cXns1ansQ%3D%3D, PID: 24418550
    • Ermler ME, Traylor Z, Patel K, et al. Rift valley fever virus infection induces activation of the NLRP3 inflammasome. Virology. 2014;449:174–80. doi:10.1016/j.virol.2013.11.015.
    • (2014) Virology , vol.449 , pp. 174-180
    • Ermler, M.E.1    Traylor, Z.2    Patel, K.3
  • 68
    • 84899480971 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of white blood cells from chikungunya fever patients of different severities
    • PID: 24721947
    • Wikan N, Khongwichit S, Phuklia W, et al. Comprehensive proteomic analysis of white blood cells from chikungunya fever patients of different severities. J Transl Med. 2014;12(1):96. doi:10.1186/1479-5876-12-96.
    • (2014) J Transl Med , vol.12 , Issue.1 , pp. 96
    • Wikan, N.1    Khongwichit, S.2    Phuklia, W.3
  • 69
    • 40449097257 scopus 로고    scopus 로고
    • The inflammasome recognizes cytosolic microbial and host DNA and triggers an innate immune response
    • COI: 1:CAS:528:DC%2BD1cXivFynur8%3D, PID: 18288107
    • Muruve DA, Pétrilli V, Zaiss AK, et al. The inflammasome recognizes cytosolic microbial and host DNA and triggers an innate immune response. Nature. 2008;452(7183):103–7. doi:10.1038/nature06664.
    • (2008) Nature , vol.452 , Issue.7183 , pp. 103-107
    • Muruve, D.A.1    Pétrilli, V.2    Zaiss, A.K.3
  • 70
    • 67650915065 scopus 로고    scopus 로고
    • Innate immune sensing of modified vaccinia virus Ankara (MVA) is mediated by TLR2-TLR6, MDA-5 and the NALP3 inflammasome
    • PID: 19543380
    • Delaloye J, Roger T, Steiner-Tardivel Q-G, et al. Innate immune sensing of modified vaccinia virus Ankara (MVA) is mediated by TLR2-TLR6, MDA-5 and the NALP3 inflammasome. PLoS Pathog. 2009;5(6):e1000480. doi:10.1371/journal.ppat.1000480.
    • (2009) PLoS Pathog , vol.5 , Issue.6
    • Delaloye, J.1    Roger, T.2    Steiner-Tardivel, Q.-G.3
  • 71
    • 68249158537 scopus 로고    scopus 로고
    • Virus binding to a plasma membrane receptor triggers interleukin-1α-mediated proinflammatory macrophage response in vivo
    • PID: 19576795
    • Di Paolo NC, Miao EA, Iwakura Y, et al. Virus binding to a plasma membrane receptor triggers interleukin-1α-mediated proinflammatory macrophage response in vivo. Immunity. 2009;31(1):110–21. doi:10.1016/j.immuni.2009.04.015.
    • (2009) Immunity , vol.31 , Issue.1 , pp. 110-121
    • Di Paolo, N.C.1    Miao, E.A.2    Iwakura, Y.3
  • 72
    • 79952621850 scopus 로고    scopus 로고
    • Lysosomal localization and mechanism of membrane penetration influence nonenveloped virus activation of the NLRP3 inflammasome
    • COI: 1:CAS:528:DC%2BC3MXjsFyht7o%3D, PID: 21315400
    • 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. doi:10.1016/j.virol.2011.01.019.
    • (2011) Virology , vol.412 , Issue.2 , pp. 306-314
    • Barlan, A.U.1    Danthi, P.2    Wiethoff, C.M.3
  • 73
    • 78650038649 scopus 로고    scopus 로고
    • Adenovirus membrane penetration activates the NLRP3 inflammasome
    • COI: 1:CAS:528:DC%2BC3MXitlCjtL4%3D, PID: 20980503
    • Barlan AU, Griffin TM, McGuire KA, Wiethoff CM. Adenovirus membrane penetration activates the NLRP3 inflammasome. J Virol. 2011;85(1):146–55. doi:10.1128/JVI.01265-10.
    • (2011) J Virol , vol.85 , Issue.1 , pp. 146-155
    • Barlan, A.U.1    Griffin, T.M.2    McGuire, K.A.3    Wiethoff, C.M.4
  • 74
    • 79955961661 scopus 로고    scopus 로고
    • Varicella-zoster virus infection triggers formation of an interleukin-1β (IL-1β)-processing inflammasome complex
    • COI: 1:CAS:528:DC%2BC3MXmtVGjur0%3D, PID: 21385879
    • Nour AM, Reichelt M, Ku C-C, Ho M-Y, Heineman TC, Arvin AM. Varicella-zoster virus infection triggers formation of an interleukin-1β (IL-1β)-processing inflammasome complex. J Biol Chem. 2011;286(20):17921–33. doi:10.1074/jbc.M110.210575.
    • (2011) J Biol Chem , vol.286 , Issue.20 , pp. 17921-17933
    • Nour, A.M.1    Reichelt, M.2    Ku, C.-C.3    Ho, M.-Y.4    Heineman, T.C.5    Arvin, A.M.6
  • 75
    • 60749104535 scopus 로고    scopus 로고
    • HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA
    • COI: 1:CAS:528:DC%2BD1MXitVyntr8%3D, PID: 19131592
    • Roberts TL, Idris A, Dunn JA, et al. HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA. Science. 2009;323(5917):1057–60. doi:10.1126/science.1169841.
    • (2009) Science , vol.323 , Issue.5917 , pp. 1057-1060
    • Roberts, T.L.1    Idris, A.2    Dunn, J.A.3
  • 76
    • 60749136484 scopus 로고    scopus 로고
    • An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome
    • PID: 19158679
    • Burckstummer T, Baumann C, Bluml S, et al. An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome. Nat Immunol. 2009;10(3):266–72. doi:10.1038/ni.1702.
    • (2009) Nat Immunol , vol.10 , Issue.3 , pp. 266-272
    • Burckstummer, T.1    Baumann, C.2    Bluml, S.3
  • 77
    • 77951269392 scopus 로고    scopus 로고
    • The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses
    • COI: 1:CAS:528:DC%2BC3cXjvFartrs%3D, PID: 20351692
    • Rathinam VA, Jiang Z, Waggoner SN, et al. The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses. Nat Immunol. 2010;11(5):395–402. doi:10.1038/ni.1864.
    • (2010) Nat Immunol , vol.11 , Issue.5 , pp. 395-402
    • Rathinam, V.A.1    Jiang, Z.2    Waggoner, S.N.3
  • 78
    • 84927159089 scopus 로고    scopus 로고
    • Inflammasome signaling pathways exert antiviral effect against Chikungunya virus in human dermal fibroblasts
    • COI: 1:CAS:528:DC%2BC2MXmt1Skt7o%3D, PID: 25847693
    • Ekchariyawat P, Hamel R, Bernard E, et al. Inflammasome signaling pathways exert antiviral effect against Chikungunya virus in human dermal fibroblasts. Infect Genet Evol. 2015;32:401–8. doi:10.1016/j.meegid.2015.03.025.
    • (2015) Infect Genet Evol , vol.32 , pp. 401-408
    • Ekchariyawat, P.1    Hamel, R.2    Bernard, E.3
  • 79
    • 84938919218 scopus 로고    scopus 로고
    • Biology of Zika virus infection in human skin cells
    • PID: 26085147
    • Hamel R, Dejarnac O, Wichit S, et al. Biology of Zika virus infection in human skin cells. J Virol. 2015;. doi:10.1128/JVI.00354-15.
    • (2015) J Virol
    • Hamel, R.1    Dejarnac, O.2    Wichit, S.3
  • 80
    • 27144440523 scopus 로고    scopus 로고
    • IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction
    • COI: 1:CAS:528:DC%2BD2MXhtVajs7fJ, PID: 16127453
    • Kawai T, Takahashi K, Sato S, et al. IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction. Nat Immunol. 2005;6(10):981–8. doi:10.1038/ni1243.
    • (2005) Nat Immunol , vol.6 , Issue.10 , pp. 981-988
    • Kawai, T.1    Takahashi, K.2    Sato, S.3
  • 81
    • 75749140581 scopus 로고    scopus 로고
    • RIG-I detects viral genomic RNA during negative-strand RNA virus infection
    • COI: 1:CAS:528:DC%2BC3cXlt1Klsbg%3D, PID: 20144762
    • Rehwinkel J, Tan CP, Goubau D, et al. RIG-I detects viral genomic RNA during negative-strand RNA virus infection. Cell. 2010;140(3):397–408. doi:10.1016/j.cell.2010.01.020.
    • (2010) Cell , vol.140 , Issue.3 , pp. 397-408
    • Rehwinkel, J.1    Tan, C.P.2    Goubau, D.3
  • 82
    • 3242813113 scopus 로고    scopus 로고
    • The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses
    • COI: 1:CAS:528:DC%2BD2cXlt1Wmu78%3D, PID: 15208624
    • Yoneyama M, Kikuchi M, Natsukawa T, et al. The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. Nat Immunol. 2004;5(7):730–7. doi:10.1038/ni1087.
    • (2004) Nat Immunol , vol.5 , Issue.7 , pp. 730-737
    • Yoneyama, M.1    Kikuchi, M.2    Natsukawa, T.3
  • 83
    • 84869845792 scopus 로고    scopus 로고
    • A structure-based model of RIG-I activation
    • COI: 1:CAS:528:DC%2BC38XhsleqtrvO, PID: 23118418
    • Kolakofsky D, Kowalinski E, Cusack S. A structure-based model of RIG-I activation. RNA. 2012;18(12):2118–27. doi:10.1261/rna.035949.112.
    • (2012) RNA , vol.18 , Issue.12 , pp. 2118-2127
    • Kolakofsky, D.1    Kowalinski, E.2    Cusack, S.3
  • 84
    • 33750976374 scopus 로고    scopus 로고
    • 5′-Triphosphate RNA is the ligand for RIG-I
    • Hornung V, Ellegast J, Kim S, et al. 5′-Triphosphate RNA is the ligand for RIG-I. Science (80-). 2006;314(5801):994–7. doi:10.1126/science.1132505.
    • (2006) Science (80-) , vol.314 , Issue.5801 , pp. 994-997
    • Hornung, V.1    Ellegast, J.2    Kim, S.3
  • 85
    • 33646342149 scopus 로고    scopus 로고
    • Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses
    • COI: 1:CAS:528:DC%2BD28XktVGltLk%3D, PID: 16625202
    • Kato H, Takeuchi O, Sato S, et al. Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses. Nature. 2006;441(7089):101–5. doi:10.1038/nature04734.
    • (2006) Nature , vol.441 , Issue.7089 , pp. 101-105
    • Kato, H.1    Takeuchi, O.2    Sato, S.3
  • 86
    • 33846554134 scopus 로고    scopus 로고
    • Retinoic acid-inducible gene I mediates early antiviral response and Toll-like receptor 3 expression in respiratory syncytial virus-infected airway epithelial cells
    • COI: 1:CAS:528:DC%2BD2sXhtFCnsr0%3D, PID: 17108032
    • Liu P, Jamaluddin M, Li K, Garofalo RP, Casola A, Brasier AR. Retinoic acid-inducible gene I mediates early antiviral response and Toll-like receptor 3 expression in respiratory syncytial virus-infected airway epithelial cells. J Virol. 2007;81(3):1401–11. doi:10.1128/JVI.01740-06.
    • (2007) J Virol , vol.81 , Issue.3 , pp. 1401-1411
    • Liu, P.1    Jamaluddin, M.2    Li, K.3    Garofalo, R.P.4    Casola, A.5    Brasier, A.R.6
  • 87
    • 33644752821 scopus 로고    scopus 로고
    • West Nile virus evades activation of interferon regulatory factor 3 through RIG-I-dependent and -independent pathways without antagonizing host defense signaling
    • COI: 1:CAS:528:DC%2BD28Xis1Cqtrs%3D, PID: 16501100
    • Fredericksen BL, Gale M. West Nile virus evades activation of interferon regulatory factor 3 through RIG-I-dependent and -independent pathways without antagonizing host defense signaling. J Virol. 2006;80(6):2913–23. doi:10.1128/JVI.80.6.2913-2923.2006.
    • (2006) J Virol , vol.80 , Issue.6 , pp. 2913-2923
    • Fredericksen, B.L.1    Gale, M.2
  • 88
    • 26444539685 scopus 로고    scopus 로고
    • Activation of innate defense against a paramyxovirus is mediated by RIG-I and TLR7 and TLR8 in a cell-type-specific manner
    • COI: 1:CAS:528:DC%2BD2MXhtFWisbrJ, PID: 16188996
    • Melchjorsen J, Jensen SB, Malmgaard L, et al. Activation of innate defense against a paramyxovirus is mediated by RIG-I and TLR7 and TLR8 in a cell-type-specific manner. J Virol. 2005;79(20):12944–51. doi:10.1128/JVI.79.20.12944-12951.2005.
    • (2005) J Virol , vol.79 , Issue.20 , pp. 12944-12951
    • Melchjorsen, J.1    Jensen, S.B.2    Malmgaard, L.3
  • 89
    • 67449101291 scopus 로고    scopus 로고
    • RIG-I-mediated activation of p38 MAPK is essential for viral induction of interferon and activation of dendritic cells. Dependence on TRAF2 and TAK1
    • COI: 1:CAS:528:DC%2BD1MXktlGrsLY%3D, PID: 19224920
    • Mikkelsen SS, Jensen SB, Chiliveru S, et al. RIG-I-mediated activation of p38 MAPK is essential for viral induction of interferon and activation of dendritic cells. Dependence on TRAF2 and TAK1. J Biol Chem. 2009;284(16):10774–82. doi:10.1074/jbc.M807272200.
    • (2009) J Biol Chem , vol.284 , Issue.16 , pp. 10774-10782
    • Mikkelsen, S.S.1    Jensen, S.B.2    Chiliveru, S.3
  • 90
    • 33750984771 scopus 로고    scopus 로고
    • RIG-I-mediated antiviral responses to single-stranded RNA bearing 5′-phosphates
    • COI: 1:CAS:528:DC%2BD28XhtFyqtLbM
    • Pichlmair A, Schulz O, Tan CP, et al. RIG-I-mediated antiviral responses to single-stranded RNA bearing 5′-phosphates. Science (80-). 2006;314(5801):997–1001. doi:10.1126/science.1132998.
    • (2006) Science (80-) , vol.314 , Issue.5801 , pp. 997-1001
    • Pichlmair, A.1    Schulz, O.2    Tan, C.P.3
  • 91
    • 26844503987 scopus 로고    scopus 로고
    • The RNA helicase Lgp2 inhibits TLR-independent sensing of viral replication by retinoic acid-inducible gene-I
    • COI: 1:CAS:528:DC%2BD2MXhtVylsbbE, PID: 16210631
    • Rothenfusser S, Goutagny N, DiPerna G, et al. The RNA helicase Lgp2 inhibits TLR-independent sensing of viral replication by retinoic acid-inducible gene-I. J Immunol. 2005;175(8):5260–8. doi:10.4049/jimmunol.175.8.5260.
    • (2005) J Immunol , vol.175 , Issue.8 , pp. 5260-5268
    • Rothenfusser, S.1    Goutagny, N.2    DiPerna, G.3
  • 92
    • 37849045856 scopus 로고    scopus 로고
    • Establishment and maintenance of the innate antiviral response to West Nile Virus involves both RIG-I and MDA5 signaling through IPS-1
    • COI: 1:CAS:528:DC%2BD1cXmtFCnsQ%3D%3D, PID: 17977974
    • Fredericksen BL, Keller BC, Fornek J, Katze MG, Gale M. Establishment and maintenance of the innate antiviral response to West Nile Virus involves both RIG-I and MDA5 signaling through IPS-1. J Virol. 2008;82(2):609–16. doi:10.1128/JVI.01305-07.
    • (2008) J Virol , vol.82 , Issue.2 , pp. 609-616
    • Fredericksen, B.L.1    Keller, B.C.2    Fornek, J.3    Katze, M.G.4    Gale, M.5
  • 93
    • 31344477977 scopus 로고    scopus 로고
    • Flavivirus induces interferon-beta gene expression through a pathway involving RIG-I-dependent IRF-3 and PI3 K-dependent NF-κB activation
    • COI: 1:CAS:528:DC%2BD28Xos1ChtQ%3D%3D, PID: 16182584
    • Chang TH, Liao CL, Lin YL. Flavivirus induces interferon-beta gene expression through a pathway involving RIG-I-dependent IRF-3 and PI3 K-dependent NF-κB activation. Microbes Infect. 2006;8:157–71. doi:10.1016/j.micinf.2005.06.014.
    • (2006) Microbes Infect , vol.8 , pp. 157-171
    • Chang, T.H.1    Liao, C.L.2    Lin, Y.L.3
  • 94
    • 47949092573 scopus 로고    scopus 로고
    • Innate immunity induced by composition-dependent RIG-I recognition of hepatitis C virus RNA
    • COI: 1:CAS:528:DC%2BD1cXovV2mtLk%3D, PID: 18548002
    • Saito T, Owen DM, Jiang F, Marcotrigiano J, Gale M. Innate immunity induced by composition-dependent RIG-I recognition of hepatitis C virus RNA. Nature. 2008;454(July):523–7. doi:10.1038/nature07106.
    • (2008) Nature , vol.454 , Issue.July , pp. 523-527
    • Saito, T.1    Owen, D.M.2    Jiang, F.3    Marcotrigiano, J.4    Gale, M.5
  • 95
    • 74049126045 scopus 로고    scopus 로고
    • Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1 beta production
    • COI: 1:CAS:528:DC%2BD1MXhsVWlsLfK, PID: 19915568
    • Poeck H, Bscheider M, Gross O, et al. Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1 beta production. Nat Immunol. 2010;11(1):63–9. doi:10.1038/ni.1824.
    • (2010) Nat Immunol , vol.11 , Issue.1 , pp. 63-69
    • Poeck, H.1    Bscheider, M.2    Gross, O.3
  • 96
    • 77956409550 scopus 로고    scopus 로고
    • NLRC5 limits the activation of inflammatory pathways
    • COI: 1:CAS:528:DC%2BC3cXptV2jtLg%3D, PID: 20610642
    • Benko S, Magalhaes JG, Philpott DJ, Girardin SE. NLRC5 limits the activation of inflammatory pathways. J Immunol. 2010;185(3):1681–91. doi:10.4049/jimmunol.0903900.
    • (2010) J Immunol , vol.185 , Issue.3 , pp. 1681-1691
    • Benko, S.1    Magalhaes, J.G.2    Philpott, D.J.3    Girardin, S.E.4
  • 97
    • 77951902675 scopus 로고    scopus 로고
    • NLRC5 Negatively regulates the NF-κB and type I interferon signaling pathways
    • COI: 1:CAS:528:DC%2BC3cXlvFygt7w%3D, PID: 20434986
    • Cui J, Zhu L, Xia X, et al. NLRC5 Negatively regulates the NF-κB and type I interferon signaling pathways. Cell. 2010;141(3):483–96. doi:10.1016/j.cell.2010.03.040.
    • (2010) Cell , vol.141 , Issue.3 , pp. 483-496
    • Cui, J.1    Zhu, L.2    Xia, X.3
  • 98
    • 77949897797 scopus 로고    scopus 로고
    • The nucleotide-binding oligomerization domain-like receptor NLRC5 is involved in IFN-dependent antiviral immune responses
    • COI: 1:CAS:528:DC%2BC3cXhsVGlu7s%3D, PID: 20061403
    • Kuenzel S, Till A, Winkler M, et al. The nucleotide-binding oligomerization domain-like receptor NLRC5 is involved in IFN-dependent antiviral immune responses. J Immunol. 2010;184(4):1990–2000. doi:10.4049/jimmunol.0900557.
    • (2010) J Immunol , vol.184 , Issue.4 , pp. 1990-2000
    • Kuenzel, S.1    Till, A.2    Winkler, M.3
  • 99
    • 77956372057 scopus 로고    scopus 로고
    • NLR family member NLRC5 is a transcriptional regulator of MHC class I genes
    • COI: 1:CAS:528:DC%2BC3cXhtVWmtrfO, PID: 20639463
    • Meissner TB, Li A, Biswas A, et al. NLR family member NLRC5 is a transcriptional regulator of MHC class I genes. Proc Natl Acad Sci USA. 2010;107(31):13794–9. doi:10.1073/pnas.1008684107.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.31 , pp. 13794-13799
    • Meissner, T.B.1    Li, A.2    Biswas, A.3
  • 100
    • 77956220440 scopus 로고    scopus 로고
    • A role for the human NLR family member NLRC5 in antiviral responses
    • COI: 1:CAS:528:DC%2BC3cXhtVahtbjN, PID: 20538593
    • Neerincx A, Lautz K, Menning M, et al. A role for the human NLR family member NLRC5 in antiviral responses. J Biol Chem. 2010;285(34):26223–32. doi:10.1074/jbc.M110.109736.
    • (2010) J Biol Chem , vol.285 , Issue.34 , pp. 26223-26232
    • Neerincx, A.1    Lautz, K.2    Menning, M.3
  • 101
    • 79251550744 scopus 로고    scopus 로고
    • Cutting edge: NLRC5-dependent activation of the inflammasome
    • COI: 1:CAS:528:DC%2BC3MXnsVKrsA%3D%3D, PID: 21191067
    • Davis BK, Roberts RA, Huang MT, et al. Cutting edge: NLRC5-dependent activation of the inflammasome. J Immunol. 2011;186(3):1333–7. doi:10.4049/jimmunol.1003111.
    • (2011) J Immunol , vol.186 , Issue.3 , pp. 1333-1337
    • Davis, B.K.1    Roberts, R.A.2    Huang, M.T.3
  • 102
    • 38749097018 scopus 로고    scopus 로고
    • NLRX1 is a regulator of mitochondrial antiviral immunity
    • COI: 1:CAS:528:DC%2BD1cXhs1Sitrc%3D, PID: 18200010
    • Moore CB, Bergstralh DT, Duncan JA, et al. NLRX1 is a regulator of mitochondrial antiviral immunity. Nature. 2008;451(7178):573–7.
    • (2008) Nature , vol.451 , Issue.7178 , pp. 573-577
    • Moore, C.B.1    Bergstralh, D.T.2    Duncan, J.A.3
  • 103
    • 40249111682 scopus 로고    scopus 로고
    • NLRX1 is a mitochondrial NOD-like receptor that amplifies NF-κB and JNK pathways by inducing reactive oxygen species production
    • COI: 1:CAS:528:DC%2BD1cXislSntb8%3D, PID: 18219313
    • Tattoli I, Carneiro LA, Jéhanno M, et al. NLRX1 is a mitochondrial NOD-like receptor that amplifies NF-κB and JNK pathways by inducing reactive oxygen species production. EMBO Rep. 2008;9:293–300. doi:10.1038/sj.embor.7401161.
    • (2008) EMBO Rep , vol.9 , pp. 293-300
    • Tattoli, I.1    Carneiro, L.A.2    Jéhanno, M.3
  • 104
    • 70350365362 scopus 로고    scopus 로고
    • An N-terminal addressing sequence targets NLRX1 to the mitochondrial matrix
    • COI: 1:CAS:528:DC%2BD1MXht1WksbzJ, PID: 19692591
    • Arnoult D, Soares F, Tattoli I, Castanier C, Philpott DJ, Girardin SE. An N-terminal addressing sequence targets NLRX1 to the mitochondrial matrix. J Cell Sci. 2009;122(Pt 17):3161–8.
    • (2009) J Cell Sci , vol.122 , pp. 3161-3168
    • Arnoult, D.1    Soares, F.2    Tattoli, I.3    Castanier, C.4    Philpott, D.J.5    Girardin, S.E.6
  • 105
    • 84863005844 scopus 로고    scopus 로고
    • The mitochondrial proteins NLRX1 and TUFM form a complex that regulates type I interferon and autophagy
    • COI: 1:CAS:528:DC%2BC38XpsVWiur4%3D, PID: 22749352
    • Lei Y, Wen H, Yu Y, et al. The mitochondrial proteins NLRX1 and TUFM form a complex that regulates type I interferon and autophagy. Immunity. 2012;36(6):933–46.
    • (2012) Immunity , vol.36 , Issue.6 , pp. 933-946
    • Lei, Y.1    Wen, H.2    Yu, Y.3
  • 106
    • 84877344662 scopus 로고    scopus 로고
    • The NLR protein, NLRX1, and its partner, TUFM, reduce type I interferon, and enhance autophagy
    • COI: 1:CAS:528:DC%2BC3sXltl2hu78%3D, PID: 23321557
    • Lei Y, Wen H, Ting JPY. The NLR protein, NLRX1, and its partner, TUFM, reduce type I interferon, and enhance autophagy. Autophagy. 2013;9(3):432–3.
    • (2013) Autophagy , vol.9 , Issue.3 , pp. 432-433
    • Lei, Y.1    Wen, H.2    Ting, J.P.Y.3
  • 107
    • 84901002026 scopus 로고    scopus 로고
    • NLRX1 prevents mitochondrial induced apoptosis and enhances macrophage antiviral immunity by interacting with influenza virus PB1-F2 protein
    • PID: 24799673
    • Jaworska J, Coulombe F, Downey J, et al. NLRX1 prevents mitochondrial induced apoptosis and enhances macrophage antiviral immunity by interacting with influenza virus PB1-F2 protein. Proc Natl Acad Sci USA. 2014;. doi:10.1073/pnas.0507681102.
    • (2014) Proc Natl Acad Sci USA
    • Jaworska, J.1    Coulombe, F.2    Downey, J.3
  • 108
    • 84895498988 scopus 로고    scopus 로고
    • Nod-like receptor X-1 is required for rhinovirus-induced barrier dysfunction in airway epithelial cells
    • Unger BL, Ganesan S, Comstock AT, Faris AN, Hershenson MB, Sajjan US. Nod-like receptor X-1 is required for rhinovirus-induced barrier dysfunction in airway epithelial cells. J Virol. 2014;88(7):3705–3718. http://www.ncbi.nlm.nih.gov/pubmed/24429360.
    • (2014) J Virol , vol.88 , Issue.7 , pp. 3705-3718
    • Unger, B.L.1    Ganesan, S.2    Comstock, A.T.3    Faris, A.N.4    Hershenson, M.B.5    Sajjan, U.S.6
  • 109
    • 84963595977 scopus 로고    scopus 로고
    • NLRX1 sequesters STING to negatively regulate the interferon response, thereby facilitating the replication of HIV-1 and DNA viruses
    • COI: 1:CAS:528:DC%2BC28XksFOjt7o%3D, PID: 27078069
    • Guo H, König R, Deng M, et al. NLRX1 sequesters STING to negatively regulate the interferon response, thereby facilitating the replication of HIV-1 and DNA viruses. Cell Host Microbe. 2016;19(4):515–28.
    • (2016) Cell Host Microbe , vol.19 , Issue.4 , pp. 515-528
    • Guo, H.1    König, R.2    Deng, M.3
  • 110
    • 84927745897 scopus 로고    scopus 로고
    • Pyroptotic cell death defends against intracellular pathogens
    • COI: 1:CAS:528:DC%2BC2MXms1SqtLk%3D, PID: 25879289
    • Jorgensen I, Miao EA. Pyroptotic cell death defends against intracellular pathogens. Immunol Rev. 2015;265(1):130–42. doi:10.1111/imr.12287.
    • (2015) Immunol Rev , vol.265 , Issue.1 , pp. 130-142
    • Jorgensen, I.1    Miao, E.A.2
  • 111
    • 33749576792 scopus 로고    scopus 로고
    • Caspase-1-dependent pore formation during pyroptosis leads to osmotic lysis of infected host macrophages
    • COI: 1:CAS:528:DC%2BD28XhtFOkurfM, PID: 16824040
    • Fink SL, Cookson BT. Caspase-1-dependent pore formation during pyroptosis leads to osmotic lysis of infected host macrophages. Cell Microbiol. 2006;8(11):1812–25.
    • (2006) Cell Microbiol , vol.8 , Issue.11 , pp. 1812-1825
    • Fink, S.L.1    Cookson, B.T.2
  • 112
    • 84864883030 scopus 로고    scopus 로고
    • Caspase-1: is IL-1 just the tip of the ICEberg?
    • COI: 1:STN:280:DC%2BC38jnsFaqtg%3D%3D, PID: 22764097
    • Denes A, Lopez-Castejon G, Brough D. Caspase-1: is IL-1 just the tip of the ICEberg? Cell Death Dis. 2012;3(7):e338. doi:10.1038/cddis.2012.86.
    • (2012) Cell Death Dis , vol.3 , Issue.7
    • Denes, A.1    Lopez-Castejon, G.2    Brough, D.3
  • 113
    • 80052179138 scopus 로고    scopus 로고
    • Caspase-1-induced pyroptotic cell death
    • COI: 1:CAS:528:DC%2BC3MXht1ejtLfJ, PID: 21884178
    • Miao EA, Rajan JV, Aderem A. Caspase-1-induced pyroptotic cell death. Immunol Rev. 2011;243(1):206–14. doi:10.1111/j.1600-065X.2011.01044.x.
    • (2011) Immunol Rev , vol.243 , Issue.1 , pp. 206-214
    • Miao, E.A.1    Rajan, J.V.2    Aderem, A.3
  • 114
    • 84888240043 scopus 로고    scopus 로고
    • C3a modulates IL-1β secretion in human monocytes by regulating ATP efflux and subsequent NLRP3 inflammasome activation
    • COI: 1:CAS:528:DC%2BC3sXhvVehsr7F, PID: 23878142
    • Asgari E, Le Friec G, Yamamoto H, et al. C3a modulates IL-1β secretion in human monocytes by regulating ATP efflux and subsequent NLRP3 inflammasome activation. Blood. 2013;122(20):3473–81. doi:10.1182/blood-2013-05-502229.
    • (2013) Blood , vol.122 , Issue.20 , pp. 3473-3481
    • Asgari, E.1    Le Friec, G.2    Yamamoto, H.3
  • 115
    • 84947419652 scopus 로고    scopus 로고
    • Pyroptosis: caspase-11 unlocks the gates of death
    • PID: 26588774
    • de Gassart A, Martinon F. Pyroptosis: caspase-11 unlocks the gates of death. Immunity. 2015;43(5):835–7.
    • (2015) Immunity , vol.43 , Issue.5 , pp. 835-837
    • de Gassart, A.1    Martinon, F.2
  • 116
    • 84947441282 scopus 로고    scopus 로고
    • Caspase-11 requires the pannexin-1 channel and the purinergic P2X7 pore to mediate pyroptosis and endotoxic shock
    • Yang D, He Y, Muñoz-Planillo R, Liu Q, Núñez G. Caspase-11 requires the pannexin-1 channel and the purinergic P2X7 pore to mediate pyroptosis and endotoxic shock. Immunity. 2015;. doi:10.1016/j.immuni.2015.10.009.
    • (2015) Immunity
    • Yang, D.1    He, Y.2    Muñoz-Planillo, R.3    Liu, Q.4    Núñez, G.5
  • 117
    • 77957942834 scopus 로고    scopus 로고
    • Pannexin 1 channels mediate “find-me” signal release and membrane permeability during apoptosis
    • Chekeni FB, Elliott MR, Sandilos JK, et al. Pannexin 1 channels mediate “find-me” signal release and membrane permeability during apoptosis. Nature. 2010;467(7317):863–867. http://www.nature.com.iclibezp1.cc.ic.ac.uk/nature/journal/v467/n7317/full/nature09413.html.
    • (2010) Nature , vol.467 , Issue.7317 , pp. 863-867
    • Chekeni, F.B.1    Elliott, M.R.2    Sandilos, J.K.3
  • 118
    • 84896332642 scopus 로고    scopus 로고
    • Unified polymerization mechanism for the assembly of asc-dependent inflammasomes
    • COI: 1:CAS:528:DC%2BC2cXksVajsLY%3D, PID: 24630722
    • Lu A, Magupalli VG, Ruan J, et al. Unified polymerization mechanism for the assembly of asc-dependent inflammasomes. Cell. 2014;156(6):1193–206. doi:10.1016/j.cell.2014.02.008.
    • (2014) Cell , vol.156 , Issue.6 , pp. 1193-1206
    • Lu, A.1    Magupalli, V.G.2    Ruan, J.3
  • 119
    • 84921730204 scopus 로고    scopus 로고
    • Structural mechanisms of inflammasome assembly
    • COI: 1:CAS:528:DC%2BC2MXhslant7Y%3D, PID: 25354325
    • Lu A, Wu H. Structural mechanisms of inflammasome assembly. FEBS J. 2015;282(3):435–44. doi:10.1111/febs.13133.
    • (2015) FEBS J , vol.282 , Issue.3 , pp. 435-444
    • Lu, A.1    Wu, H.2
  • 120
    • 84885964931 scopus 로고    scopus 로고
    • Pyrin- and CARD-only proteins as regulators of NLR functions
    • PID: 24062743
    • Le HT, Harton JA. Pyrin- and CARD-only proteins as regulators of NLR functions. Front Immunol. 2013;4:275. doi:10.3389/fimmu.2013.00275.
    • (2013) Front Immunol , vol.4 , pp. 275
    • Le, H.T.1    Harton, J.A.2
  • 121
    • 0037121940 scopus 로고    scopus 로고
    • The PAAD/PYRIN-family protein ASC is a dual regulator of a conserved step in nuclear factor B activation pathways
    • COI: 1:CAS:528:DC%2BD38XpslWlu7w%3D, PID: 12486103
    • Stehlik C, Fiorentino L, Dorfleutner A, et al. The PAAD/PYRIN-family protein ASC is a dual regulator of a conserved step in nuclear factor B activation pathways. J Exp Med. 2002;196(12):1605–15. doi:10.1084/jem.20021552.
    • (2002) J Exp Med , vol.196 , Issue.12 , pp. 1605-1615
    • Stehlik, C.1    Fiorentino, L.2    Dorfleutner, A.3
  • 122
    • 33947219338 scopus 로고    scopus 로고
    • Pyrin-only protein 2 modulates NF-κB and disrupts ASC: CLR interactions
    • COI: 1:CAS:528:DC%2BD2sXisVGjt74%3D, PID: 17339483
    • Bedoya F, Sandler LL, Harton JA. Pyrin-only protein 2 modulates NF-κB and disrupts ASC: CLR interactions. J Immunol. 2007;178(6):3837–45. doi:10.4049/jimmunol.178.6.3837.
    • (2007) J Immunol , vol.178 , Issue.6 , pp. 3837-3845
    • Bedoya, F.1    Sandler, L.L.2    Harton, J.A.3
  • 123
    • 81755171449 scopus 로고    scopus 로고
    • Uncoupling of pyrin-only protein 2 (POP2)-mediated dual regulation of NF-κB and the inflammasome
    • COI: 1:CAS:528:DC%2BC3MXhsVOqu7rI, PID: 21976665
    • Atianand MK, Harton JA. Uncoupling of pyrin-only protein 2 (POP2)-mediated dual regulation of NF-κB and the inflammasome. J Biol Chem. 2011;286(47):40536–47. doi:10.1074/jbc.M111.274290.
    • (2011) J Biol Chem , vol.286 , Issue.47 , pp. 40536-40547
    • Atianand, M.K.1    Harton, J.A.2
  • 124
    • 84951097504 scopus 로고    scopus 로고
    • NLRP12 is a neutrophil-specific, negative regulator of in vitro cell migration but does not modulate LPS- or infection-induced NF-κB or ERK signalling
    • COI: 1:CAS:528:DC%2BC2MXhslanu7zN
    • Zamoshnikova A, Groß CJ, Schuster S, et al. NLRP12 is a neutrophil-specific, negative regulator of in vitro cell migration but does not modulate LPS- or infection-induced NF-κB or ERK signalling. Immunobiology. 2016;221(2):341–6. doi:10.1016/j.imbio.2015.10.001.
    • (2016) Acta Trop , vol.221 , Issue.2 , pp. 341-346
    • Zamoshnikova, A.1    Groß, C.J.2    Schuster, S.3
  • 125
    • 84896638307 scopus 로고    scopus 로고
    • The PYRIN domain-only protein POP3 inhibits ALR inflammasomes and regulates responses to infection with DNA viruses
    • Khare S, Ratsimandresy RA, de Almeida L, et al. The PYRIN domain-only protein POP3 inhibits ALR inflammasomes and regulates responses to infection with DNA viruses. Nat Immunol. 2014;15(4):343–353. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=4123781&tool=pmcentrez&rendertype=abstract.
    • (2014) Nat Immunol , vol.15 , Issue.4 , pp. 343-353
    • Khare, S.1    Ratsimandresy, R.A.2    de Almeida, L.3
  • 126
    • 84878237993 scopus 로고    scopus 로고
    • Latz E, Xiao TS, Stutz A. Activation and regulation of the inflammasomes
    • Latz E, Xiao TS, Stutz A. Activation and regulation of the inflammasomes. doi:10.1038/nri3452.
  • 127
    • 84897836190 scopus 로고    scopus 로고
    • Mechanisms underlying the inhibition of interferon signaling by viruses
    • PID: 24504013
    • Devasthanam AS. Mechanisms underlying the inhibition of interferon signaling by viruses. Virulence. 2014;5(2):270–7. doi:10.4161/viru.27902.
    • (2014) Virulence , vol.5 , Issue.2 , pp. 270-277
    • Devasthanam, A.S.1
  • 128
    • 84929461078 scopus 로고    scopus 로고
    • Different serotypes of dengue viruses differently regulate the expression of the host cell antigen processing machinery
    • COI: 1:CAS:528:DC%2BC2MXosFCitro%3D, PID: 25981524
    • Gan CS, Yusof R, Othman S. Different serotypes of dengue viruses differently regulate the expression of the host cell antigen processing machinery. Acta Trop. 2015;149:8–14. doi:10.1016/j.actatropica.2015.05.005.
    • (2015) Acta Trop , vol.149 , pp. 8-14
    • Gan, C.S.1    Yusof, R.2    Othman, S.3
  • 129
    • 84919397221 scopus 로고    scopus 로고
    • Hepatitis C virus infection decreases the expression of Toll-like receptors 3 and 7 via upregulation of miR-758
    • Yang Q, Fu S, Wang J. Hepatitis C virus infection decreases the expression of Toll-like receptors 3 and 7 via upregulation of miR-758. Arch Virol. 2014. doi:10.1007/s00705-014-2167-3.
    • (2014) Arch Virol
    • Yang, Q.1    Fu, S.2    Wang, J.3
  • 130
    • 79952687026 scopus 로고    scopus 로고
    • Human papillomavirus deregulates the response of a cellular network comprising of chemotactic and proinflammatory genes
    • COI: 1:CAS:528:DC%2BC3MXjvVCltrk%3D, PID: 21423754
    • Karim R, Meyers C, Backendorf C, et al. Human papillomavirus deregulates the response of a cellular network comprising of chemotactic and proinflammatory genes. PLoS ONE. 2011;6(3):e17848. doi:10.1371/journal.pone.0017848.
    • (2011) PLoS ONE , vol.6 , Issue.3
    • Karim, R.1    Meyers, C.2    Backendorf, C.3
  • 131
    • 84883368914 scopus 로고    scopus 로고
    • Post-translational control of IL-1b via the human papillomavirus type 16 E6 oncoprotein: a novel mechanism of innate immune escape mediated by the E3-ubiquitin ligase E6-AP and p53
    • COI: 1:CAS:528:DC%2BC3sXhsVChs7vN, PID: 23935506
    • Niebler M, Qian X, Höfler D, et al. Post-translational control of IL-1b via the human papillomavirus type 16 E6 oncoprotein: a novel mechanism of innate immune escape mediated by the E3-ubiquitin ligase E6-AP and p53. PLoS Pathog. 2013;9(8):e1003536. doi:10.1371/journal.ppat.1003536.
    • (2013) PLoS Pathog , vol.9 , Issue.8
    • Niebler, M.1    Qian, X.2    Höfler, D.3
  • 132
    • 84908389427 scopus 로고    scopus 로고
    • Adenovirus E1A targets the DREF nuclear factor to regulate virus gene expression, DNA replication, and growth
    • PID: 25210186
    • Radko S, Koleva M, James KMD, Jung R, Mymryk JS, Pelka P. Adenovirus E1A targets the DREF nuclear factor to regulate virus gene expression, DNA replication, and growth. J Virol. 2014;88(22):13469–81. doi:10.1128/JVI.02538-14.
    • (2014) J Virol , vol.88 , Issue.22 , pp. 13469-13481
    • Radko, S.1    Koleva, M.2    James, K.M.D.3    Jung, R.4    Mymryk, J.S.5    Pelka, P.6
  • 133
    • 84937003478 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport of nucleocapsid proteins of enveloped RNA viruses
    • Wulan WN, Heydet D, Walker EJ, Gahan ME, Ghildyal R. Nucleocytoplasmic transport of nucleocapsid proteins of enveloped RNA viruses. Front Microbiol. 2015;6:1–10. doi:10.3389/fmicb.2015.00553.
    • (2015) Front Microbiol , vol.6 , pp. 1-10
    • Wulan, W.N.1    Heydet, D.2    Walker, E.J.3    Gahan, M.E.4    Ghildyal, R.5
  • 134
    • 33847615627 scopus 로고    scopus 로고
    • Host shutoff during productive Epstein–Barr virus infection is mediated by BGLF5 and may contribute to immune evasion
    • COI: 1:CAS:528:DC%2BD2sXjtVWlt7g%3D, PID: 17360652
    • Rowe M, Glaunsinger B, van Leeuwen D, et al. Host shutoff during productive Epstein–Barr virus infection is mediated by BGLF5 and may contribute to immune evasion. Proc Natl Acad Sci USA. 2007;104(9):3366–71. doi:10.1073/pnas.0611128104.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.9 , pp. 3366-3371
    • Rowe, M.1    Glaunsinger, B.2    van Leeuwen, D.3
  • 135
    • 84925240058 scopus 로고    scopus 로고
    • Viral noncoding RNAs: more surprises
    • COI: 1:CAS:528:DC%2BC2MXmtlSjurc%3D, PID: 25792595
    • Tycowski KT, Guo YE, Lee N, et al. Viral noncoding RNAs: more surprises. Genes Dev. 2015;29(6):567–84. doi:10.1101/gad.259077.115.
    • (2015) Genes Dev , vol.29 , Issue.6 , pp. 567-584
    • Tycowski, K.T.1    Guo, Y.E.2    Lee, N.3
  • 136
    • 84867320879 scopus 로고    scopus 로고
    • Cutting edge: miR-223 and EBV miR-BART15 regulate the NLRP3 inflammasome and IL-1 production
    • COI: 1:CAS:528:DC%2BC38XhsVKrtL%2FO, PID: 22984081
    • Haneklaus M, Gerlic M, Kurowska-Stolarska M, et al. Cutting edge: miR-223 and EBV miR-BART15 regulate the NLRP3 inflammasome and IL-1 production. J Immunol. 2012;189(8):3795–9. doi:10.4049/jimmunol.1200312.
    • (2012) J Immunol , vol.189 , Issue.8 , pp. 3795-3799
    • Haneklaus, M.1    Gerlic, M.2    Kurowska-Stolarska, M.3
  • 137
    • 84862856415 scopus 로고    scopus 로고
    • The role of inflammasome modulation in virulence
    • PID: 22546900
    • Lupfer CR, Kanneganti T-D. The role of inflammasome modulation in virulence. Virulence. 2012;3(3):262–70. doi:10.4161/viru.20266.
    • (2012) Virulence , vol.3 , Issue.3 , pp. 262-270
    • Lupfer, C.R.1    Kanneganti, T.-D.2
  • 138
    • 84931008001 scopus 로고    scopus 로고
    • Variola virus F1L is a Bcl-2-like protein that unlike its vaccinia virus counterpart inhibits apoptosis independent of Bim
    • COI: 1:CAS:528:DC%2BC2MXjvFOhurc%3D, PID: 25766319
    • Marshall B, Puthalakath H, Caria S, et al. Variola virus F1L is a Bcl-2-like protein that unlike its vaccinia virus counterpart inhibits apoptosis independent of Bim. Cell Death Dis. 2015;6(3):e1680. doi:10.1038/cddis.2015.52.
    • (2015) Cell Death Dis , vol.6 , Issue.3
    • Marshall, B.1    Puthalakath, H.2    Caria, S.3
  • 139
    • 84877339331 scopus 로고    scopus 로고
    • Vaccinia virus F1L protein promotes virulence by inhibiting inflammasome activation
    • COI: 1:CAS:528:DC%2BC3sXptFWqsb8%3D, PID: 23603272
    • Gerlic M, Faustin B, Postigo A, et al. Vaccinia virus F1L protein promotes virulence by inhibiting inflammasome activation. Proc Natl Acad Sci USA. 2013;110(19):7808–13. doi:10.1073/pnas.1215995110.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.19 , pp. 7808-7813
    • Gerlic, M.1    Faustin, B.2    Postigo, A.3
  • 140
    • 78751680633 scopus 로고    scopus 로고
    • Discovery of a viral NLR homolog that inhibits the inflammasome
    • COI: 1:CAS:528:DC%2BC3MXmsVequw%3D%3D
    • Gregory SM, Davis BK, West JA, et al. Discovery of a viral NLR homolog that inhibits the inflammasome. Science (80-). 2011;331(6015):330–4. doi:10.1126/science.1199478.
    • (2011) Science (80-) , vol.331 , Issue.6015 , pp. 330-334
    • Gregory, S.M.1    Davis, B.K.2    West, J.A.3
  • 141
    • 28844466449 scopus 로고    scopus 로고
    • A poxvirus-encoded pyrin domain protein interacts with ASC-1 to inhibit host inflammatory and apoptotic responses to infection
    • COI: 1:CAS:528:DC%2BD28XjvFCrtQ%3D%3D, PID: 16356857
    • Johnston JB, Barrett JW, Nazarian SH, et al. A poxvirus-encoded pyrin domain protein interacts with ASC-1 to inhibit host inflammatory and apoptotic responses to infection. Immunity. 2005;23(6):587–98. doi:10.1016/j.immuni.2005.10.003.
    • (2005) Immunity , vol.23 , Issue.6 , pp. 587-598
    • Johnston, J.B.1    Barrett, J.W.2    Nazarian, S.H.3
  • 142
    • 84921522079 scopus 로고    scopus 로고
    • Hepatitis A virus 3C protease cleaves NEMO to impair induction of beta interferon
    • PID: 24920812
    • Wang D, Fang L, Wei D, et al. Hepatitis A virus 3C protease cleaves NEMO to impair induction of beta interferon. J Virol. 2014;88(17):10252–8. doi:10.1128/JVI.00869-14.
    • (2014) J Virol , vol.88 , Issue.17 , pp. 10252-10258
    • Wang, D.1    Fang, L.2    Wei, D.3
  • 143
    • 84937521591 scopus 로고    scopus 로고
    • Reciprocal regulation between enterovirus 71 and the NLRP3 inflammasome
    • Wang H, Lei X, Xiao X, et al. Reciprocal regulation between enterovirus 71 and the NLRP3 inflammasome. Cell Rep. 2015;12(1):1–7. doi:10.1016/j.celrep.2015.05.047.
    • (2015) Cell Rep , vol.12 , Issue.1 , pp. 1-7
    • Wang, H.1    Lei, X.2    Xiao, X.3
  • 144
    • 0026728952 scopus 로고
    • Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme
    • COI: 1:CAS:528:DyaK38Xks1yiu7Y%3D, PID: 1339309
    • Ray CA, Black RA, Kronheim SR, et al. Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme. Cell. 1992;69(4):597–604. doi:10.1016/0092-8674(92)90223-Y.
    • (1992) Cell , vol.69 , Issue.4 , pp. 597-604
    • Ray, C.A.1    Black, R.A.2    Kronheim, S.R.3
  • 145
    • 0029839388 scopus 로고    scopus 로고
    • Petit F, Bertagnoli S, Gelfi J, Fassy F, Boucraut-Baralon C, Milon A. Characterization of a myxoma virus-encoded serpin-like protein with activity against interleukin-1 beta-converting enzyme. J Virol. 1996;70(9):5860–5866.
    • Petit F, Bertagnoli S, Gelfi J, Fassy F, Boucraut-Baralon C, Milon A. Characterization of a myxoma virus-encoded serpin-like protein with activity against interleukin-1 beta-converting enzyme. J Virol. 1996;70(9):5860–5866. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8709205\nhttp://jvi.asm.org/content/70/9/5860.full.pdf.
  • 146
    • 0031052956 scopus 로고    scopus 로고
    • Vaccinia virus serpin B13R (SPI-2) inhibits interleukin-1beta-converting enzyme and protects virus-infected cells from TNF- and Fas-mediated apoptosis, but does not prevent IL-1beta-induced fever
    • COI: 1:CAS:528:DyaK2sXhsVaisr4%3D, PID: 9049422
    • Kettle S, Alcamí A, Khanna A, Ehret R, Jassoy C, Smith GL. Vaccinia virus serpin B13R (SPI-2) inhibits interleukin-1beta-converting enzyme and protects virus-infected cells from TNF- and Fas-mediated apoptosis, but does not prevent IL-1beta-induced fever. J Gen Virol. 1997;78(Pt 3):677–85.
    • (1997) J Gen Virol , vol.78 , pp. 677-685
    • Kettle, S.1    Alcamí, A.2    Khanna, A.3    Ehret, R.4    Jassoy, C.5    Smith, G.L.6
  • 147
    • 11444262203 scopus 로고    scopus 로고
    • Influenza A mutant viruses with altered NS1 protein function provoke caspase-1 activation in primary human macrophages, resulting in fast apoptosis and release of high levels of interleukins 1 and 18
    • COI: 1:CAS:528:DC%2BD2MXlt1Kmtg%3D%3D, PID: 15604446
    • Stasakova J. Influenza A mutant viruses with altered NS1 protein function provoke caspase-1 activation in primary human macrophages, resulting in fast apoptosis and release of high levels of interleukins 1 and 18. J Gen Virol. 2005;86(1):185–95. doi:10.1099/vir.0.80422-0.
    • (2005) J Gen Virol , vol.86 , Issue.1 , pp. 185-195
    • Stasakova, J.1
  • 148
    • 84929346755 scopus 로고    scopus 로고
    • Influenza A virus NS1 protein inhibits the NLRP3 inflammasome
    • PID: 25978411
    • Cheong W-C, Kang H-R, Yoon H, Kang S-J, Ting JP-Y, Song MJ. Influenza A virus NS1 protein inhibits the NLRP3 inflammasome. PLoS ONE. 2015;10(5):e0126456. doi:10.1371/journal.pone.0126456.
    • (2015) PLoS ONE , vol.10 , Issue.5
    • Cheong, W.-C.1    Kang, H.-R.2    Yoon, H.3    Kang, S.-J.4    Ting, J.P.-Y.5    Song, M.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.