메뉴 건너뛰기




Volumn 13, Issue 4, 2012, Pages 333-342

Regulation of inflammasome signaling

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 11; CRYOPYRIN; CYSTEINE PROTEINASE; GAMMA INTERFERON; INFLAMMASOME; INTERFERON; INTERLEUKIN 18; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; LEUCINE RICH REPEAT KINASE 2; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR C4; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR P1; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR P12; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR P6; UNCLASSIFIED DRUG;

EID: 84858688293     PISSN: 15292908     EISSN: 15292916     Source Type: Journal    
DOI: 10.1038/ni.2237     Document Type: Review
Times cited : (782)

References (114)
  • 1
    • 80455176839 scopus 로고    scopus 로고
    • Non-canonical inflammasome activation targets caspase-11
    • Kayagaki, N. et al. Non-canonical inflammasome activation targets caspase-11. Nature 479, 117-121 (2011).
    • (2011) Nature , vol.479 , pp. 117-121
    • Kayagaki, N.1
  • 2
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-β
    • Martinon, F., Burns, K. & Tschopp, J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-β. Mol. Cell 10, 417-426 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 3
    • 77957228318 scopus 로고    scopus 로고
    • Central roles of NLRs and inflammasomes in viral infection
    • Kanneganti, T. Central roles of NLRs and inflammasomes in viral infection. Nat. Rev. Immunol. 10, 688-698 (2010).
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 688-698
    • Kanneganti, T.1
  • 4
    • 75649106430 scopus 로고    scopus 로고
    • Intracellular DNA recognition
    • Hornung, V. & Latz, E. Intracellular DNA recognition. Nat. Rev. Immunol. 10, 123-130 (2010).
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 123-130
    • Hornung, V.1    Latz, E.2
  • 5
    • 79956061094 scopus 로고    scopus 로고
    • IFI16 Acts as a nuclear pathogen sensor to induce the inflammasome in response to Kaposi sarcoma-associated herpesvirus infection
    • Kerur, N. et al. IFI16 Acts as a nuclear pathogen sensor to induce the inflammasome in response to Kaposi sarcoma-associated herpesvirus infection. Cell Host Microbe 9, 363-375 (2011).
    • (2011) Cell Host Microbe , vol.9 , pp. 363-375
    • Kerur, N.1
  • 6
    • 77958140656 scopus 로고    scopus 로고
    • IFI16 is an innate immune sensor for intracellular DNA
    • Unterholzner, L. et al. IFI16 is an innate immune sensor for intracellular DNA. Nat. Immunol. 11, 997-1004 (2010).
    • (2010) Nat. Immunol. , vol.11 , pp. 997-1004
    • Unterholzner, L.1
  • 7
    • 70450250064 scopus 로고    scopus 로고
    • Structure and interdomain dynamics of apoptosis-associated speck-like protein containing a CARD (ASC)
    • de Alba, E. Structure and interdomain dynamics of apoptosis-associated speck-like protein containing a CARD (ASC). J. Biol. Chem. 284, 32932-32941 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 32932-32941
    • De Alba, E.1
  • 8
    • 64849097220 scopus 로고    scopus 로고
    • Activation of inflammasomes requires intracellular redistribution of the apoptotic speck-like protein containing a caspase recruitment domain
    • Bryan, N.B., 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. 182, 3173-3182 (2009).
    • (2009) J. Immunol. , vol.182 , pp. 3173-3182
    • Bryan, N.B.1    Dorfleutner, A.2    Rojanasakul, Y.3    Stehlik, C.4
  • 9
    • 80052968438 scopus 로고    scopus 로고
    • The inflammasome adaptor ASC regulates the function of adaptive immune cells by controlling Dock2-mediated Rac activation and actin polymerization
    • Ippagunta, S.K. et al. The inflammasome adaptor ASC regulates the function of adaptive immune cells by controlling Dock2-mediated Rac activation and actin polymerization. Nat. Immunol. 12, 1010-1016 (2011).
    • (2011) Nat. Immunol. , vol.12 , pp. 1010-1016
    • Ippagunta, S.K.1
  • 10
    • 79952159132 scopus 로고    scopus 로고
    • Emerging inflammasome effector mechanisms
    • Lamkanfi, M. Emerging inflammasome effector mechanisms. Nat. Rev. Immunol. 11, 213-220 (2011).
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 213-220
    • Lamkanfi, M.1
  • 11
    • 78650210802 scopus 로고    scopus 로고
    • Differential requirement for caspase-1 autoproteolysis in pathogen-induced cell death and cytokine processing
    • Broz, P., von Moltke, J., Jones, J.W., Vance, R.E. & Monack, D.M. Differential requirement for caspase-1 autoproteolysis in pathogen-induced cell death and cytokine processing. Cell Host Microbe 8, 471-483 (2010).
    • (2010) Cell Host Microbe , vol.8 , pp. 471-483
    • Broz, P.1    Von Moltke, J.2    Jones, J.W.3    Vance, R.E.4    Monack, D.M.5
  • 12
    • 39749084641 scopus 로고    scopus 로고
    • Active caspase-1 is a regulator of unconventional protein secretion
    • Keller, M., Ruegg, A., Werner, S. & Beer, H.D. Active caspase-1 is a regulator of unconventional protein secretion. Cell 132, 818-831 (2008).
    • (2008) Cell , vol.132 , pp. 818-831
    • Keller, M.1    Ruegg, A.2    Werner, S.3    Beer, H.D.4
  • 13
    • 70349334298 scopus 로고    scopus 로고
    • A critical role for hemolysins and bacterial lipoproteins in Staphylococcus aureus-induced activation of the NLRP3 inflammasome
    • Munoz-Planillo, R., Franchi, L., Miller, L.S. & Nunez, G. A critical role for hemolysins and bacterial lipoproteins in Staphylococcus aureus-induced activation of the NLRP3 inflammasome. J. Immunol. 183, 3942-3948 (2009).
    • (2009) J. Immunol. , vol.183 , pp. 3942-3948
    • Munoz-Planillo, R.1    Franchi, L.2    Miller, L.S.3    Nunez, G.4
  • 14
    • 76249108958 scopus 로고    scopus 로고
    • Listeria monocytogenes-infected human peripheral blood mononuclear cells produce IL-1β, depending on listeriolysin O and NLRP3
    • Meixenberger, K. et al. Listeria monocytogenes-infected human peripheral blood mononuclear cells produce IL-1β, depending on listeriolysin O and NLRP3. J. Immunol. 184, 922-930 (2010).
    • (2010) J. Immunol. , vol.184 , pp. 922-930
    • Meixenberger, K.1
  • 15
    • 77953305895 scopus 로고    scopus 로고
    • Listeria monocytogenes is sensed by the NLRP3 and AIM2 inflammasome
    • Kim, S. et al. Listeria monocytogenes is sensed by the NLRP3 and AIM2 inflammasome. Eur. J. Immunol. 40, 1545-1551 (2010).
    • (2010) Eur. J. Immunol. , vol.40 , pp. 1545-1551
    • Kim, S.1
  • 16
    • 68149100523 scopus 로고    scopus 로고
    • NLRP3 (NALP3, Cryopyrin) facilitates in vivo caspase-1 activation, necrosis, and HMGB1 release via inflammasome-dependent and -independent pathways
    • Willingham, S.B. et al. NLRP3 (NALP3, Cryopyrin) facilitates in vivo caspase-1 activation, necrosis, and HMGB1 release via inflammasome-dependent and -independent pathways. J. Immunol. 183, 2008-2015 (2009).
    • (2009) J. Immunol. , vol.183 , pp. 2008-2015
    • Willingham, S.B.1
  • 17
    • 70449448992 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae activates the proteinase cathepsin B to mediate the signaling activities of the NLRP3 and ASC-containing inflammasome
    • Duncan, J.A. et al. Neisseria gonorrhoeae activates the proteinase cathepsin B to mediate the signaling activities of the NLRP3 and ASC-containing inflammasome. J. Immunol. 182, 6460-6469 (2009).
    • (2009) J. Immunol. , vol.182 , pp. 6460-6469
    • Duncan, J.A.1
  • 18
    • 65549154784 scopus 로고    scopus 로고
    • An essential role for the NLRP3 inflammasome in host defense against the human fungal pathogen Candida albicans
    • Hise, A.G. et al. An essential role for the NLRP3 inflammasome in host defense against the human fungal pathogen Candida albicans. Cell Host Microbe 5, 487-497 (2009).
    • (2009) Cell Host Microbe , vol.5 , pp. 487-497
    • Hise, A.G.1
  • 19
    • 64049111768 scopus 로고    scopus 로고
    • The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA
    • Allen, I.C. et al. The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA. Immunity 30, 556-565 (2009).
    • (2009) Immunity , vol.30 , pp. 556-565
    • Allen, I.C.1
  • 20
    • 32944470765 scopus 로고    scopus 로고
    • Cryopyrin activates the inflammasome in response to toxins and ATP
    • Mariathasan, S. et al. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 440, 228-232 (2006).
    • (2006) Nature , vol.440 , pp. 228-232
    • Mariathasan, S.1
  • 21
    • 67649831360 scopus 로고    scopus 로고
    • NLRP3/cryopyrin is necessary for interleukin-1β (IL-1β) release in response to hyaluronan, an endogenous trigger of inflammation in response to injury
    • Yamasaki, K. et al. NLRP3/cryopyrin is necessary for interleukin-1β (IL-1β) release in response to hyaluronan, an endogenous trigger of inflammation in response to injury. J. Biol. Chem. 284, 12762-12771 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 12762-12771
    • Yamasaki, K.1
  • 22
    • 47849085872 scopus 로고    scopus 로고
    • The NALP3 inflammasome is involved in the innate immune response to amyloid-β
    • Halle, A. et al. The NALP3 inflammasome is involved in the innate immune response to amyloid-β. Nat. Immunol. 9, 857-865 (2008).
    • (2008) Nat. Immunol. , vol.9 , pp. 857-865
    • Halle, A.1
  • 23
    • 65649140025 scopus 로고    scopus 로고
    • Uric acid is a danger signal activating NALP3 inflammasome in lung injury inflammation and fibrosis
    • Gasse, P. et al. Uric acid is a danger signal activating NALP3 inflammasome in lung injury inflammation and fibrosis. Am. J. Respir. Crit. Care Med. 179, 903-913 (2009).
    • (2009) Am. J. Respir. Crit. Care Med. , vol.179 , pp. 903-913
    • Gasse, P.1
  • 24
    • 77957554717 scopus 로고    scopus 로고
    • Molecular mechanism of NLRP3 inflammasome activation
    • Jin, C. & Flavell, R.A. Molecular mechanism of NLRP3 inflammasome activation. J. Clin. Immunol. 30, 628-631 (2010).
    • (2010) J. Clin. Immunol. , vol.30 , pp. 628-631
    • Jin, C.1    Flavell, R.A.2
  • 25
    • 47849097202 scopus 로고    scopus 로고
    • Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
    • Hornung, V. et al. Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat. Immunol. 9, 847-856 (2008).
    • (2008) Nat. Immunol. , vol.9 , pp. 847-856
    • Hornung, V.1
  • 26
    • 77951295418 scopus 로고    scopus 로고
    • Influenza virus activates inflammasomes via its intracellular M2 ion channel
    • Ichinohe, T., Pang, I.K. & Iwasaki, A. Influenza virus activates inflammasomes via its intracellular M2 ion channel. Nat. Immunol. 11, 404-410 (2010).
    • (2010) Nat. Immunol. , vol.11 , pp. 404-410
    • Ichinohe, T.1    Pang, I.K.2    Iwasaki, A.3
  • 27
    • 77649241461 scopus 로고    scopus 로고
    • Innate immune detection of the type III secretion apparatus through the NLRC4 inflammasome
    • Miao, E.A. et al. Innate immune detection of the type III secretion apparatus through the NLRC4 inflammasome. Proc. Natl. Acad. Sci. USA 107, 3076-3080 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 3076-3080
    • Miao, E.A.1
  • 28
    • 3142654767 scopus 로고    scopus 로고
    • Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf
    • Mariathasan, S. et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 430, 213-218 (2004).
    • (2004) Nature , vol.430 , pp. 213-218
    • Mariathasan, S.1
  • 29
    • 33744493091 scopus 로고    scopus 로고
    • Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1β via Ipaf
    • Miao, E.A. et al. Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1β via Ipaf. Nat. Immunol. 7, 569-575 (2006).
    • (2006) Nat. Immunol. , vol.7 , pp. 569-575
    • Miao, E.A.1
  • 30
    • 80053349020 scopus 로고    scopus 로고
    • The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus
    • Zhao, Y. et al. The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus. Nature 477, 596-600 (2011).
    • (2011) Nature , vol.477 , pp. 596-600
    • Zhao, Y.1
  • 31
    • 80053379974 scopus 로고    scopus 로고
    • Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity
    • Kofoed, E.M. & Vance, R.E. Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity. Nature 477, 592-595 (2011).
    • (2011) Nature , vol.477 , pp. 592-595
    • Kofoed, E.M.1    Vance, R.E.2
  • 32
    • 77954056386 scopus 로고    scopus 로고
    • Susceptibility to anthrax lethal toxin-induced rat death is controlled by a single chromosome 10 locus that includes rNLRP1
    • Newman, Z.L. et al. Susceptibility to anthrax lethal toxin-induced rat death is controlled by a single chromosome 10 locus that includes rNLRP1. PLoS Pathog. 6, e1000906 (2010).
    • (2010) PLoS Pathog. , vol.6
    • Newman, Z.L.1
  • 33
    • 33847376042 scopus 로고    scopus 로고
    • Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation
    • Faustin, B. et al. Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation. Mol. Cell 25, 713-724 (2007).
    • (2007) Mol. Cell , vol.25 , pp. 713-724
    • Faustin, B.1
  • 34
    • 80052137604 scopus 로고    scopus 로고
    • Molecular mechanisms of inflammasome activation during microbial infections
    • Broz, P. & Monack, D.M. Molecular mechanisms of inflammasome activation during microbial infections. Immunol. Rev. 243, 174-190 (2011).
    • (2011) Immunol. Rev. , vol.243 , pp. 174-190
    • Broz, P.1    Monack, D.M.2
  • 35
    • 0037312509 scopus 로고    scopus 로고
    • NALPs: A novel protein family involved in inflammation
    • Tschopp, J., Martinon, F. & Burns, K. NALPs: a novel protein family involved in inflammation. Nat. Rev. Cell Biol. 4, 95-104 (2003).
    • (2003) Nat. Rev. Cell Biol. , vol.4 , pp. 95-104
    • Tschopp, J.1    Martinon, F.2    Burns, K.3
  • 36
    • 80555129622 scopus 로고    scopus 로고
    • CARD8 and NLRP1 Undergo Autoproteolytic Processing through a ZU5-Like Domain
    • D'Osualdo, A. et al. CARD8 and NLRP1 Undergo Autoproteolytic Processing through a ZU5-Like Domain. PLoS ONE 6, e27396 (2011).
    • (2011) PLoS ONE , vol.6
    • D'Osualdo, A.1
  • 37
    • 45549093755 scopus 로고    scopus 로고
    • A NOD2-NALP1 complex mediates caspase-1-dependent IL-1β secretion in response to Bacillus anthracis infection and muramyl dipeptide
    • Hsu, L.C. et al. A NOD2-NALP1 complex mediates caspase-1-dependent IL-1β secretion in response to Bacillus anthracis infection and muramyl dipeptide. Proc. Natl. Acad. Sci. USA 105, 7803-7808 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7803-7808
    • Hsu, L.C.1
  • 38
    • 79960450059 scopus 로고    scopus 로고
    • Anthrax toxin induces macrophage death by p38 MAPK inhibition but leads to inflammasome activation via ATP leakage
    • Ali, S.R. et al. Anthrax toxin induces macrophage death by p38 MAPK inhibition but leads to inflammasome activation via ATP leakage. Immunity 35, 34-44 (2011).
    • (2011) Immunity , vol.35 , pp. 34-44
    • Ali, S.R.1
  • 39
    • 70349413073 scopus 로고    scopus 로고
    • CA-074Me protection against anthrax lethal toxin
    • Newman, Z.L., Leppla, S.H. & Moayeri, M. CA-074Me protection against anthrax lethal toxin. Infect. Immun. 77, 4327-4336 (2009).
    • (2009) Infect. Immun. , vol.77 , pp. 4327-4336
    • Newman, Z.L.1    Leppla, S.H.2    Moayeri, M.3
  • 40
    • 0010464874 scopus 로고    scopus 로고
    • PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates activation of NF-κB and caspase-1-dependent cytokine processing
    • Wang, L. et al. PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates activation of NF-κB and caspase-1-dependent cytokine processing. J. Biol. Chem. 277, 29874-29880 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 29874-29880
    • Wang, L.1
  • 41
    • 18644368579 scopus 로고    scopus 로고
    • Functional screening of five PYPAF family members identifies PYPAF5 as a novel regulator of NF-κB and caspase-1
    • Grenier, J.M. et al. Functional screening of five PYPAF family members identifies PYPAF5 as a novel regulator of NF-κB and caspase-1. FEBS Lett. 530, 73-78 (2002).
    • (2002) FEBS Lett. , vol.530 , pp. 73-78
    • Grenier, J.M.1
  • 42
    • 33846473862 scopus 로고    scopus 로고
    • Monarch-1 suppresses non-canonical NF-κB activation and p52-dependent chemokine expression in monocytes
    • Lich, J.D. et al. Monarch-1 suppresses non-canonical NF-κB activation and p52-dependent chemokine expression in monocytes. J. Immunol. 178, 1256-1260 (2007).
    • (2007) J. Immunol. , vol.178 , pp. 1256-1260
    • Lich, J.D.1
  • 43
    • 28844494900 scopus 로고    scopus 로고
    • The CATERPILLER protein monarch-1 is an antagonist of toll-like receptor-, tumor necrosis factor α-, and Mycobacterium tuberculosis-induced pro-inflammatory signals
    • Williams, K.L. et al. The CATERPILLER protein monarch-1 is an antagonist of toll-like receptor-, tumor necrosis factor α-, and Mycobacterium tuberculosis-induced pro-inflammatory signals. J. Biol. Chem. 280, 39914-39924 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 39914-39924
    • Williams, K.L.1
  • 44
    • 79957576718 scopus 로고    scopus 로고
    • NLRP6 inflammasome regulates colonic microbial ecology and risk for colitis
    • Elinav, E. et al. NLRP6 inflammasome regulates colonic microbial ecology and risk for colitis. Cell 145, 745-757 (2011).
    • (2011) Cell , vol.145 , pp. 745-757
    • Elinav, E.1
  • 45
    • 78049489590 scopus 로고    scopus 로고
    • Cutting edge: NLRP12 controls dendritic and myeloid cell migration to affect contact hypersensitivity
    • Arthur, J.C. et al. Cutting edge: NLRP12 controls dendritic and myeloid cell migration to affect contact hypersensitivity. J. Immunol. 185, 4515-4519 (2010).
    • (2010) J. Immunol. , vol.185 , pp. 4515-4519
    • Arthur, J.C.1
  • 46
    • 34247367268 scopus 로고    scopus 로고
    • Monarch-1/PYPAF7 and other CATERPILLER (CLR, NOD, NLR) proteins with negative regulatory functions
    • Lich, J.D. & Ting, J.P. Monarch-1/PYPAF7 and other CATERPILLER (CLR, NOD, NLR) proteins with negative regulatory functions. Microbes Infect. 9, 672-676 (2007).
    • (2007) Microbes Infect. , vol.9 , pp. 672-676
    • Lich, J.D.1    Ting, J.P.2
  • 47
    • 33846473862 scopus 로고    scopus 로고
    • Monarch-1 suppresses non-canonical NF-κB activation and p52-dependent chemokine expression in monocytes
    • Lich, J.D. et al. Monarch-1 suppresses non-canonical NF-κB activation and p52-dependent chemokine expression in monocytes. J. Immunol. 178, 1256-1260 (2007).
    • (2007) J. Immunol. , vol.178 , pp. 1256-1260
    • Lich, J.D.1
  • 48
    • 40349113175 scopus 로고    scopus 로고
    • Mutations in NALP12 cause hereditary periodic fever syndromes
    • Jéru, I. et al. Mutations in NALP12 cause hereditary periodic fever syndromes. Proc. Natl. Acad. Sci. USA 105, 1614-1619 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 1614-1619
    • Jéru, I.1
  • 49
    • 79959840140 scopus 로고    scopus 로고
    • Role of interleukin-1β in NLRP12-associated autoinflammatory disorders and resistance to anti-interleukin-1 therapy
    • Jéru, I. et al. Role of interleukin-1β in NLRP12-associated autoinflammatory disorders and resistance to anti-interleukin-1 therapy. Arthritis Rheum. 63, 2142-2148 (2011).
    • (2011) Arthritis Rheum. , vol.63 , pp. 2142-2148
    • Jéru, I.1
  • 50
    • 66049094734 scopus 로고    scopus 로고
    • In vivo regulation of interleukin 1β in patients with cryopyrin-associated periodic syndromes
    • Lachmann, H.J. et al. In vivo regulation of interleukin 1β in patients with cryopyrin-associated periodic syndromes. J Exp. Med. 206, 1029-1036 (2009).
    • (2009) J Exp. Med. , vol.206 , pp. 1029-1036
    • Lachmann, H.J.1
  • 51
    • 0037792866 scopus 로고    scopus 로고
    • Interleukin-1-receptor antagonist in the Muckle-Wells syndrome
    • Hawkins, P.N., Lachmann, H.J. & McDermott, M.F. Interleukin-1- receptor antagonist in the Muckle-Wells syndrome. N. Engl. J. Med. 348, 2583-2584 (2003).
    • (2003) N. Engl. J. Med. , vol.348 , pp. 2583-2584
    • Hawkins, P.N.1    Lachmann, H.J.2    McDermott, M.F.3
  • 52
    • 81255189478 scopus 로고    scopus 로고
    • The NOD-like receptor NLRP12 attenuates colon inflammation and tumorigenesis
    • Zaki, M.H. et al. The NOD-like receptor NLRP12 attenuates colon inflammation and tumorigenesis. Cancer Cell 20, 649-660 (2011).
    • (2011) Cancer Cell , vol.20 , pp. 649-660
    • Zaki, M.H.1
  • 53
    • 80052152283 scopus 로고    scopus 로고
    • The PYHIN protein family as mediators of host defenses
    • Schattgen, S.A. & Fitzgerald, K.A. The PYHIN protein family as mediators of host defenses. Immunol. Rev. 243, 109-118 (2011).
    • (2011) Immunol. Rev. , vol.243 , pp. 109-118
    • Schattgen, S.A.1    Fitzgerald, K.A.2
  • 54
    • 60749136484 scopus 로고    scopus 로고
    • An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome
    • Burckstummer, T. et al. An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome. Nat. Immunol. 10, 266-272 (2009).
    • (2009) Nat. Immunol. , vol.10 , pp. 266-272
    • Burckstummer, T.1
  • 55
    • 63649133278 scopus 로고    scopus 로고
    • AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
    • Hornung, V. et al. AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC. Nature 458, 514-518 (2009).
    • (2009) Nature , vol.458 , pp. 514-518
    • Hornung, V.1
  • 56
    • 60749104535 scopus 로고    scopus 로고
    • HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA
    • Roberts, T.L. et al. HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA. Science 323, 1057-1060 (2009).
    • (2009) Science , vol.323 , pp. 1057-1060
    • Roberts, T.L.1
  • 57
    • 49549100511 scopus 로고    scopus 로고
    • Trex1 prevents cell-intrinsic initiation of autoimmunity
    • Stetson, D.B., Ko, J.S., Heidmann, T. & Medzhitov, R. Trex1 prevents cell-intrinsic initiation of autoimmunity. Cell 134, 587-598 (2008).
    • (2008) Cell , vol.134 , pp. 587-598
    • Stetson, D.B.1    Ko, J.S.2    Heidmann, T.3    Medzhitov, R.4
  • 58
    • 12344290452 scopus 로고    scopus 로고
    • Lethal anemia caused by interferon-β produced in mouse embryos carrying undigested DNA
    • Yoshida, H., Okabe, Y., Kawane, K., Fukuyama, H. & Nagata, S. Lethal anemia caused by interferon-β produced in mouse embryos carrying undigested DNA. Nat. Immunol. 6, 49-56 (2004).
    • (2004) Nat. Immunol. , vol.6 , pp. 49-56
    • Yoshida, H.1    Okabe, Y.2    Kawane, K.3    Fukuyama, H.4    Nagata, S.5
  • 59
    • 27944453599 scopus 로고    scopus 로고
    • Toll-like receptor-independent gene induction program activated by mammalian DNA escaped from apoptotic DNA degradation
    • Okabe, Y., Kawane, K., Akira, S., Taniguchi, T. & Nagata, S. Toll-like receptor-independent gene induction program activated by mammalian DNA escaped from apoptotic DNA degradation. J. Exp. Med. 202, 1333-1339 (2005).
    • (2005) J. Exp. Med. , vol.202 , pp. 1333-1339
    • Okabe, Y.1    Kawane, K.2    Akira, S.3    Taniguchi, T.4    Nagata, S.5
  • 60
    • 33750465224 scopus 로고    scopus 로고
    • Chronic polyarthritis caused by mammalian DNA that escapes from degradation in macrophages
    • Kawane, K. et al. Chronic polyarthritis caused by mammalian DNA that escapes from degradation in macrophages. Nature 443, 998-1002 (2006).
    • (2006) Nature , vol.443 , pp. 998-1002
    • Kawane, K.1
  • 61
    • 77951263260 scopus 로고    scopus 로고
    • The AIM2 inflammasome is critical for innate immunity to Francisella tularensis
    • Fernandes-Alnemri, T. et al. The AIM2 inflammasome is critical for innate immunity to Francisella tularensis. Nat. Immunol. 11, 385-393 (2010).
    • (2010) Nat. Immunol. , vol.11 , pp. 385-393
    • Fernandes-Alnemri, T.1
  • 62
    • 77953116282 scopus 로고    scopus 로고
    • Absent in melanoma 2 is required for innate immune recognition of Francisella tularensis
    • Jones, J.W. et al. Absent in melanoma 2 is required for innate immune recognition of Francisella tularensis. Proc. Natl. Acad. Sci. USA 107, 9771-9776 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 9771-9776
    • Jones, J.W.1
  • 63
    • 77951269392 scopus 로고    scopus 로고
    • The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses
    • Rathinam, V.A. et al. The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses. Nat. Immunol. 11, 395-402 (2010).
    • (2010) Nat. Immunol. , vol.11 , pp. 395-402
    • Rathinam, V.A.1
  • 64
    • 33344476398 scopus 로고    scopus 로고
    • CATERPILLERs, pyrin and hereditary immunological disorders
    • Kastner, D.L. & Hoffman, H.M. CATERPILLERs, pyrin and hereditary immunological disorders. Nat. Rev. Immunol. 6, 183-195 (2006).
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 183-195
    • Kastner, D.L.1    Hoffman, H.M.2
  • 65
    • 28844466449 scopus 로고    scopus 로고
    • A poxvirus-encoded pyrin domain protein interacts with ASC-1 to inhibit host inflammatory and apoptotic responses to infection
    • Johnston, J.B. et al. A poxvirus-encoded pyrin domain protein interacts with ASC-1 to inhibit host inflammatory and apoptotic responses to infection. Immunity 23, 587-598 (2005).
    • (2005) Immunity , vol.23 , pp. 587-598
    • Johnston, J.B.1
  • 66
    • 33847730763 scopus 로고    scopus 로고
    • Cellular pyrin domain-only protein 2 is a candidate regulator of inflammasome activation
    • Dorfleutner, A. et al. Cellular pyrin domain-only protein 2 is a candidate regulator of inflammasome activation. Infect. Immun. 75, 1484-1492 (2007).
    • (2007) Infect. Immun. , vol.75 , pp. 1484-1492
    • Dorfleutner, A.1
  • 67
    • 73449119324 scopus 로고    scopus 로고
    • Co-regulation of NF-κB and inflammasome-mediated inflammatory responses by myxoma virus pyrin domain-containing protein M013
    • Rahman, M.M., Mohamed, M.R., Kim, M., Smallwood, S. & McFadden, G. Co-regulation of NF-κB and inflammasome-mediated inflammatory responses by myxoma virus pyrin domain-containing protein M013. PLoS Pathog. 5, e1000635 (2009).
    • (2009) PLoS Pathog. , vol.5
    • Rahman, M.M.1    Mohamed, M.R.2    Kim, M.3    Smallwood, S.4    McFadden, G.5
  • 68
    • 0034194055 scopus 로고    scopus 로고
    • The serpin proteinase inhibitor 9 is an endogenous inhibitor of interleukin 1β-converting enzyme (caspase-1) activity in human vascular smooth muscle cells
    • Young, J.L. et al. The serpin proteinase inhibitor 9 is an endogenous inhibitor of interleukin 1β-converting enzyme (caspase-1) activity in human vascular smooth muscle cells. J. Exp. Med. 191, 1535-1544 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 1535-1544
    • Young, J.L.1
  • 69
    • 0026728952 scopus 로고
    • Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1β converting enzyme
    • Ray, C.A. et al. Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1β converting enzyme. Cell 69, 597-604 (1992).
    • (1992) Cell , vol.69 , pp. 597-604
    • Ray, C.A.1
  • 70
    • 0031052956 scopus 로고    scopus 로고
    • Vaccinia virus serpin B13R (SPI-2) inhibits interleukin-1β- converting enzyme and protects virus-infected cells from TNF- and Fas-mediated apoptosis, but does not prevent IL-1β-induced fever
    • Kettle, S. et al. Vaccinia virus serpin B13R (SPI-2) inhibits interleukin-1β-converting enzyme and protects virus-infected cells from TNF- and Fas-mediated apoptosis, but does not prevent IL-1β-induced fever. J. Gen. Virol. 78, 677-685 (1997).
    • (1997) J. Gen. Virol. , vol.78 , pp. 677-685
    • Kettle, S.1
  • 71
    • 0029839388 scopus 로고    scopus 로고
    • Characterization of a myxoma virus-encoded serpin-like protein with activity against interleukin-1β-converting enzyme
    • Petit, F. et al. Characterization of a myxoma virus-encoded serpin-like protein with activity against interleukin-1β-converting enzyme. J. Virol. 70, 5860-5866 (1996).
    • (1996) J. Virol. , vol.70 , pp. 5860-5866
    • Petit, F.1
  • 72
    • 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 1β and 18
    • Stasakova, J. et al. 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 1β and 18. J. Gen. Virol. 86, 185-195 (2005).
    • (2005) J. Gen. Virol. , vol.86 , pp. 185-195
    • Stasakova, J.1
  • 73
    • 0028817947 scopus 로고
    • Inhibition of ICE family proteases by baculovirus antiapoptotic protein p35
    • Bump, N.J. et al. Inhibition of ICE family proteases by baculovirus antiapoptotic protein p35. Science 269, 1885-1888 (1995).
    • (1995) Science , vol.269 , pp. 1885-1888
    • Bump, N.J.1
  • 74
    • 78751680633 scopus 로고    scopus 로고
    • Discovery of a viral NLR homolog that inhibits the inflammasome
    • Gregory, S.M. et al. Discovery of a viral NLR homolog that inhibits the inflammasome. Science 331, 330-334 (2011).
    • (2011) Science , vol.331 , pp. 330-334
    • Gregory, S.M.1
  • 75
    • 77953562208 scopus 로고    scopus 로고
    • A Yersinia effector protein promotes virulence by preventing inflammasome recognition of the type III secretion system
    • Brodsky, I.E. et al. A Yersinia effector protein promotes virulence by preventing inflammasome recognition of the type III secretion system. Cell Host Microbe 7, 376-387 (2010).
    • (2010) Cell Host Microbe , vol.7 , pp. 376-387
    • Brodsky, I.E.1
  • 76
    • 37549041954 scopus 로고    scopus 로고
    • Immune recognition of Pseudomonas aeruginosa mediated by the IPAF/NLRC4 inflammasome
    • Sutterwala, F.S. et al. Immune recognition of Pseudomonas aeruginosa mediated by the IPAF/NLRC4 inflammasome. J. Exp. Med. 204, 3235-3245 (2007).
    • (2007) J. Exp. Med. , vol.204 , pp. 3235-3245
    • Sutterwala, F.S.1
  • 77
    • 54049100347 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa Type III secretion system plays a dual role in the regulation of caspase-1 mediated IL-1β maturation
    • Galle, M. et al. The Pseudomonas aeruginosa Type III secretion system plays a dual role in the regulation of caspase-1 mediated IL-1β maturation. J. Cell Mol. Med. 12, 1767-1776 (2008).
    • (2008) J. Cell Mol. Med. , vol.12 , pp. 1767-1776
    • Galle, M.1
  • 78
    • 2942537824 scopus 로고    scopus 로고
    • Targeting Rac1 by the Yersinia effector protein YopE inhibits caspase-1-mediated maturation and release of interleukin-1β
    • Schotte, P. et al. Targeting Rac1 by the Yersinia effector protein YopE inhibits caspase-1-mediated maturation and release of interleukin-1β. J. Biol. Chem. 279, 25134-25142 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 25134-25142
    • Schotte, P.1
  • 79
    • 41849104578 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis prevents inflammasome activation
    • Master, S.S. et al. Mycobacterium tuberculosis prevents inflammasome activation. Cell Host Microbe 3, 224-232 (2008).
    • (2008) Cell Host Microbe , vol.3 , pp. 224-232
    • Master, S.S.1
  • 80
    • 78149489515 scopus 로고    scopus 로고
    • Deletion of ripA alleviates suppression of the inflammasome and MAPK by Francisella tularensis
    • Huang, M.T. et al. Deletion of ripA alleviates suppression of the inflammasome and MAPK by Francisella tularensis. J. Immunol. 185, 5476-5485 (2010).
    • (2010) J. Immunol. , vol.185 , pp. 5476-5485
    • Huang, M.T.1
  • 81
    • 78049394393 scopus 로고    scopus 로고
    • Cutting edge: Mutation of tularensis mviN leads to increased macrophage absent in melanoma 2 inflammasome activation and a loss of virulence
    • Ulland, T.K. et al. Cutting edge: mutation of tularensis mviN leads to increased macrophage absent in melanoma 2 inflammasome activation and a loss of virulence. J. Immunol. 185, 2670-2674 (2010).
    • (2010) J. Immunol. , vol.185 , pp. 2670-2674
    • Ulland, T.K.1
  • 82
    • 79952798601 scopus 로고    scopus 로고
    • Apoptosis-associated speck-like protein (ASC) controls Legionella pneumophila infection in human monocytes
    • Abdelaziz, D.H. et al. Apoptosis-associated speck-like protein (ASC) controls Legionella pneumophila infection in human monocytes. J. Biol. Chem. 286, 3203-3208 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 3203-3208
    • Abdelaziz, D.H.1
  • 83
    • 77952584658 scopus 로고    scopus 로고
    • Streptococcus pneumoniae evades human dendritic cell surveillance by pneumolysin expression
    • Littmann, M. et al. Streptococcus pneumoniae evades human dendritic cell surveillance by pneumolysin expression. EMBO Mol Med 1, 211-222 (2009).
    • (2009) EMBO Mol Med , vol.1 , pp. 211-222
    • Littmann, M.1
  • 84
    • 79251515144 scopus 로고    scopus 로고
    • Pneumolysin activates the NLRP3 inflammasome and promotes proinflammatory cytokines independently of TLR4
    • McNeela, E.A. et al. Pneumolysin activates the NLRP3 inflammasome and promotes proinflammatory cytokines independently of TLR4. PLoS Pathog. 6, e1001191 (2010).
    • (2010) PLoS Pathog. , vol.6
    • McNeela, E.A.1
  • 85
    • 79960408020 scopus 로고    scopus 로고
    • The NLRP3 inflammasome is differentially activated by pneumolysin variants and contributes to host defense in pneumococcal pneumonia
    • Witzenrath, M. et al. The NLRP3 inflammasome is differentially activated by pneumolysin variants and contributes to host defense in pneumococcal pneumonia. J. Immunol. 187, 434-440 (2011).
    • (2011) J. Immunol. , vol.187 , pp. 434-440
    • Witzenrath, M.1
  • 86
    • 80555133274 scopus 로고    scopus 로고
    • Critical Roles of ASC inflammasomes in caspase-1 activation and host innate resistance to Streptococcus pneumoniae infection
    • Fang, R. et al. Critical Roles of ASC inflammasomes in caspase-1 activation and host innate resistance to Streptococcus pneumoniae infection. J. Immunol. 187, 4890-4899 (2011).
    • (2011) J. Immunol. , vol.187 , pp. 4890-4899
    • Fang, R.1
  • 87
    • 81555204380 scopus 로고    scopus 로고
    • Structural basis of RNA recognition and activation by innate immune receptor RIG-I
    • Jiang, F. et al. Structural basis of RNA recognition and activation by innate immune receptor RIG-I. Nature 479, 423-427 (2011).
    • (2011) Nature , vol.479 , pp. 423-427
    • Jiang, F.1
  • 88
    • 34249044447 scopus 로고    scopus 로고
    • Type I interferon signaling is required for activation of the inflammasome during Francisella infection
    • Henry, T., Brotcke, A., Weiss, D.S., Thompson, L.J. & Monack, D.M. Type I interferon signaling is required for activation of the inflammasome during Francisella infection. J. Exp. Med. 204, 987 (2007).
    • (2007) J. Exp. Med. , vol.204 , pp. 987
    • Henry, T.1    Brotcke, A.2    Weiss, D.S.3    Thompson, L.J.4    Monack, D.M.5
  • 89
    • 79951740151 scopus 로고    scopus 로고
    • Type I interferon inhibits interleukin-1 production and inflammasome activation
    • Guarda, G. et al. Type I interferon inhibits interleukin-1 production and inflammasome activation. Immunity 34, 213-223 (2011).
    • (2011) Immunity , vol.34 , pp. 213-223
    • Guarda, G.1
  • 90
    • 84255162073 scopus 로고    scopus 로고
    • Innate and adaptive interferons suppress IL-1α and IL-1β production by distinct pulmonary myeloid subsets during Mycobacterium tuberculosis infection
    • Mayer-Barber, K.D. et al. Innate and adaptive interferons suppress IL-1α and IL-1β production by distinct pulmonary myeloid subsets during Mycobacterium tuberculosis infection. Immunity 35, 1023-1034 (2011).
    • (2011) Immunity , vol.35 , pp. 1023-1034
    • Mayer-Barber, K.D.1
  • 91
    • 77955055799 scopus 로고    scopus 로고
    • Regulation of interleukin-1β by interferon-γ is species specific, limited by suppressor of cytokine signalling 1 and influences interleukin-17 production
    • Masters, S.L. et al. Regulation of interleukin-1β by interferon-γ is species specific, limited by suppressor of cytokine signalling 1 and influences interleukin-17 production. EMBO Rep. 11, 640-646 (2010).
    • (2010) EMBO Rep. , vol.11 , pp. 640-646
    • Masters, S.L.1
  • 92
    • 67650421494 scopus 로고    scopus 로고
    • T cells dampen innate immune responses through inhibition of NLRP1 and NLRP3 inflammasomes
    • Guarda, G. et al. T cells dampen innate immune responses through inhibition of NLRP1 and NLRP3 inflammasomes. Nature 460, 269-273 (2009).
    • (2009) Nature , vol.460 , pp. 269-273
    • Guarda, G.1
  • 93
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • Levine, B., Mizushima, N. & Virgin, H.W. Autophagy in immunity and inflammation. Nature 469, 323-335 (2011).
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 94
    • 56249090667 scopus 로고    scopus 로고
    • Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1β production
    • Saitoh, T. et al. Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1β production. Nature 456, 264-268 (2008).
    • (2008) Nature , vol.456 , pp. 264-268
    • Saitoh, T.1
  • 95
    • 78651393239 scopus 로고    scopus 로고
    • A role for mitochondria in NLRP3 inflammasome activation
    • Zhou, R., Yazdi, A.S., Menu, P. & Tschopp, J. A role for mitochondria in NLRP3 inflammasome activation. Nature 469, 221-225 (2010).
    • (2010) Nature , vol.469 , pp. 221-225
    • Zhou, R.1    Yazdi, A.S.2    Menu, P.3    Tschopp, J.4
  • 96
    • 79951642032 scopus 로고    scopus 로고
    • Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome
    • Nakahira, K. et al. Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome. Nat. Immunol. 12, 222-230 (2010).
    • (2010) Nat. Immunol. , vol.12 , pp. 222-230
    • Nakahira, K.1
  • 97
    • 79953176280 scopus 로고    scopus 로고
    • Autophagy controls IL-1β secretion by targeting pro-IL-1β for degradation
    • Harris, J. et al. Autophagy controls IL-1β secretion by targeting pro-IL-1β for degradation. J. Biol. Chem. 286, 9587 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 9587
    • Harris, J.1
  • 98
    • 79954459822 scopus 로고    scopus 로고
    • Inflammasome-independent modulation of cytokine response by autophagy in human cells
    • Crisan, T.O. et al. Inflammasome-independent modulation of cytokine response by autophagy in human cells. PLoS ONE 6, e18666 (2011).
    • (2011) PLoS ONE , vol.6
    • Crisan, T.O.1
  • 99
    • 82455210868 scopus 로고    scopus 로고
    • Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1β
    • Dupont, N. et al. Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1β. EMBO J. 30, 4701-4711 (2011).
    • (2011) EMBO J. , vol.30 , pp. 4701-4711
    • Dupont, N.1
  • 100
    • 0030745449 scopus 로고    scopus 로고
    • Ancient missense mutations in a new member of the RoRet gene family are likely to cause familial Mediterranean fever
    • The International FMF Consortium
    • The International FMF Consortium. Ancient missense mutations in a new member of the RoRet gene family are likely to cause familial Mediterranean fever. Cell 90, 797-807 (1997).
    • (1997) Cell , vol.90 , pp. 797-807
  • 101
    • 16944365196 scopus 로고    scopus 로고
    • A candidate gene for familial Mediterranean fever
    • A candidate gene for familial Mediterranean fever. Nat. Genet. 17, 25-31 (1997).
    • (1997) Nat. Genet. , vol.17 , pp. 25-31
  • 102
    • 79956299492 scopus 로고    scopus 로고
    • Gain-of-function Pyrin mutations induce NLRP3 protein-independent interleukin-1β activation and severe autoinflammation in mice
    • Chae, J.J. et al. Gain-of-function Pyrin mutations induce NLRP3 protein-independent interleukin-1β activation and severe autoinflammation in mice. Immunity 34, 755-768 (2011).
    • (2011) Immunity , vol.34 , pp. 755-768
    • Chae, J.J.1
  • 103
    • 33749587661 scopus 로고    scopus 로고
    • The estrogen-responsive B box protein: A novel enhancer of interleukin-1β secretion
    • Munding, C. et al. The estrogen-responsive B box protein: a novel enhancer of interleukin-1β secretion. Cell Death Differ. 13, 1938-1949 (2006).
    • (2006) Cell Death Differ. , vol.13 , pp. 1938-1949
    • Munding, C.1
  • 104
    • 78650636576 scopus 로고    scopus 로고
    • Tripartite-motif protein 30 negatively regulates NLRP3 inflammasome activation by modulating reactive oxygen species production
    • Hu, Y. et al. Tripartite-motif protein 30 negatively regulates NLRP3 inflammasome activation by modulating reactive oxygen species production. J. Immunol. 185, 7699 (2010).
    • (2010) J. Immunol. , vol.185 , pp. 7699
    • Hu, Y.1
  • 105
    • 0038682430 scopus 로고    scopus 로고
    • The PAAD/PYRIN-only protein POP1/ASC2 is a modulator of ASC-mediated nuclear-factor-κB and pro-caspase-1 regulation
    • Stehlik, C. et al. The PAAD/PYRIN-only protein POP1/ASC2 is a modulator of ASC-mediated nuclear-factor-κB and pro-caspase-1 regulation. Biochem. J. 373, 101 (2003).
    • (2003) Biochem. J. , vol.373 , pp. 101
    • Stehlik, C.1
  • 106
    • 33947219338 scopus 로고    scopus 로고
    • Pyrin-only protein 2 modulates NF-κB and disrupts ASC:CLR interactions
    • Bedoya, F., Sandler, L.L. & Harton, J.A. Pyrin-only protein 2 modulates NF-κB and disrupts ASC:CLR interactions. J. Immunol. 178, 3837 (2007).
    • (2007) J. Immunol. , vol.178 , pp. 3837
    • Bedoya, F.1    Sandler, L.L.2    Harton, J.A.3
  • 107
    • 33646175602 scopus 로고    scopus 로고
    • Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice
    • Saleh, M. et al. Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice. Nature 440, 1064-1068 (2006).
    • (2006) Nature , vol.440 , pp. 1064-1068
    • Saleh, M.1
  • 108
    • 46649083006 scopus 로고    scopus 로고
    • Different evolutionary strategies for the origin of caspase-1 inhibitors
    • da Cunha, J.P.C., Galante, P.A.F. & de Souza, S.J. Different evolutionary strategies for the origin of caspase-1 inhibitors. J. Mol. Evol. 66, 591-597 (2008).
    • (2008) J. Mol. Evol. , vol.66 , pp. 591-597
    • Da Cunha, J.P.C.1    Galante, P.A.F.2    De Souza, S.J.3
  • 109
    • 0034194055 scopus 로고    scopus 로고
    • The Serpin proteinase inhibitor 9 is an endogenous inhibitor of interleukin 1β-converting enzyme (caspase-1) activity in human vascular smooth muscle cells
    • Young, J.L. et al. The Serpin proteinase inhibitor 9 is an endogenous inhibitor of interleukin 1β-converting enzyme (caspase-1) activity in human vascular smooth muscle cells. J. Exp. Med. 191, 1535 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 1535
    • Young, J.L.1
  • 110
    • 33947717153 scopus 로고    scopus 로고
    • Bcl-2 and Bcl-XL regulate proinflammatory caspase-1 activation by interaction with NALP1
    • Bruey, J.M. et al. Bcl-2 and Bcl-XL regulate proinflammatory caspase-1 activation by interaction with NALP1. Cell 129, 45-56 (2007).
    • (2007) Cell , vol.129 , pp. 45-56
    • Bruey, J.M.1
  • 111
    • 84858694905 scopus 로고    scopus 로고
    • Differential splicing of the apoptosis-associated speck like protein containing a caspase recruitment domain (ASC) regulates inflammasomes
    • Andrea, D., Sara, K., Chawon, Y., Yon, R. & Christian, S. Differential splicing of the apoptosis-associated speck like protein containing a caspase recruitment domain (ASC) regulates inflammasomes. J. Inflamm. 7, 7-23 (2010).
    • (2010) J. Inflamm. , vol.7 , pp. 7-23
    • Andrea, D.1    Sara, K.2    Chawon, Y.3    Yon, R.4    Christian, S.5
  • 112
    • 80055045773 scopus 로고    scopus 로고
    • IFI16 protein mediates the anti-inflammatory actions of the type-I interferons through suppression of activation of caspase-1 by inflammasomes
    • Veeranki, S., Duan, X., Panchanathan, R., Liu, H. & Choubey, D. IFI16 protein mediates the anti-inflammatory actions of the type-I interferons through suppression of activation of caspase-1 by inflammasomes. PLoS ONE 6, e27040 (2011).
    • (2011) PLoS ONE , vol.6
    • Veeranki, S.1    Duan, X.2    Panchanathan, R.3    Liu, H.4    Choubey, D.5
  • 113
    • 77953583256 scopus 로고    scopus 로고
    • Interferon-inducible p200-family proteins as novel sensors of cytoplasmic DNA: Role in inflammation and autoimmunity
    • Choubey, D. et al. Interferon-inducible p200-family proteins as novel sensors of cytoplasmic DNA: role in inflammation and autoimmunity. J. Interferon Cytokine Res. 30, 371-380 (2010).
    • (2010) J. Interferon Cytokine Res. , vol.30 , pp. 371-380
    • Choubey, D.1
  • 114
    • 79955897768 scopus 로고    scopus 로고
    • Cytosolic DNA triggers inflammasome activation in keratinocytes in psoriatic lesions
    • Dombrowski, Y. et al. Cytosolic DNA triggers inflammasome activation in keratinocytes in psoriatic lesions. Sci. Transl. Med. 3, 82ra38-82ra38 (2011).
    • (2011) Sci. Transl. Med. , vol.3
    • Dombrowski, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.