메뉴 건너뛰기




Volumn 265, Issue 1, 2015, Pages 103-111

The nucleic acid-sensing inflammasomes

Author keywords

Extracellular function; Filament formation; Inflammasome; Nucleic acid recognition

Indexed keywords

ABSENT IN MYELOMA 2 PROTEIN; CRYOPYRIN; DNA; GAMMA INTERFERON INDUCIBLE PROTEIN 16; INFLAMMASOME; NUCLEIC ACID; UNCLASSIFIED DRUG; AIM2 PROTEIN, HUMAN; CARRIER PROTEIN; DNA BINDING PROTEIN; IFI16 PROTEIN, HUMAN; MULTIPROTEIN COMPLEX; NLRP3 PROTEIN, HUMAN; NUCLEAR PROTEIN; PATTERN RECOGNITION RECEPTOR; PHOSPHOPROTEIN;

EID: 84927699710     PISSN: 01052896     EISSN: 1600065X     Source Type: Journal    
DOI: 10.1111/imr.12281     Document Type: Review
Times cited : (64)

References (91)
  • 1
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • Martinon F, Burns K, Tschopp J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell 2002;10:417-426.
    • (2002) Mol Cell , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 2
    • 84878237993 scopus 로고    scopus 로고
    • Activation and regulation of the inflammasomes
    • Latz E, Xiao TS, Stutz A. Activation and regulation of the inflammasomes. Nat Rev Immunol 2013;13:397-411.
    • (2013) Nat Rev Immunol , vol.13 , pp. 397-411
    • Latz, E.1    Xiao, T.S.2    Stutz, A.3
  • 3
    • 34247842740 scopus 로고    scopus 로고
    • The death domain superfamily in intracellular signaling of apoptosis and inflammation
    • Park HH, Lo Y-C, Lin S-C, Wang L, Yang JK, Wu H. The death domain superfamily in intracellular signaling of apoptosis and inflammation. Annu Rev Immunol 2007;25:561-586.
    • (2007) Annu Rev Immunol , vol.25 , pp. 561-586
    • Park, H.H.1    Lo, Y.-C.2    Lin, S.-C.3    Wang, L.4    Yang, J.K.5    Wu, H.6
  • 4
    • 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 2009;458:514-518.
    • (2009) Nature , vol.458 , pp. 514-518
    • Hornung, V.1
  • 5
    • 63649145255 scopus 로고    scopus 로고
    • AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
    • Fernandes-Alnemri T, Yu J-W, Datta P, Wu J, Alnemri ES. AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA. Nature 2009;458:509-513.
    • (2009) Nature , vol.458 , pp. 509-513
    • Fernandes-Alnemri, T.1    Yu, J.-W.2    Datta, P.3    Wu, J.4    Alnemri, E.S.5
  • 6
    • 60749136484 scopus 로고    scopus 로고
    • An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome
    • Bürckstümmer T, et al. An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome. Nat Immunol 2009;10:266-272.
    • (2009) Nat Immunol , vol.10 , pp. 266-272
    • Bürckstümmer, T.1
  • 7
    • 60749104535 scopus 로고    scopus 로고
    • HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA
    • Roberts TL, et al. HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA. Science 2009;323:1057-1060.
    • (2009) Science , vol.323 , pp. 1057-1060
    • Roberts, T.L.1
  • 8
    • 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 2011;9:363-375.
    • (2011) Cell Host Microbe , vol.9 , pp. 363-375
    • Kerur, N.1
  • 9
    • 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 2010;11:997-1004.
    • (2010) Nat Immunol , vol.11 , pp. 997-1004
    • Unterholzner, L.1
  • 10
    • 1642285783 scopus 로고    scopus 로고
    • NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder
    • Agostini L, Martinon F, Burns K, McDermott MF, Hawkins PN, Tschopp J. NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder. Immunity 2004;20:319-325.
    • (2004) Immunity , vol.20 , pp. 319-325
    • Agostini, L.1    Martinon, F.2    Burns, K.3    McDermott, M.F.4    Hawkins, P.N.5    Tschopp, J.6
  • 11
    • 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 2004;430:213-218.
    • (2004) Nature , vol.430 , pp. 213-218
    • Mariathasan, S.1
  • 12
    • 33744464740 scopus 로고    scopus 로고
    • Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1β in salmonella-infected macrophages
    • Franchi L, et al. Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1β in salmonella-infected macrophages. Nat Immunol 2006;7:576-582.
    • (2006) Nat Immunol , vol.7 , pp. 576-582
    • Franchi, L.1
  • 13
    • 33744493091 scopus 로고    scopus 로고
    • Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1β via Ipaf
    • Miao EA, et al. Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1β via Ipaf. Nat Immunol 2006;7:569-575.
    • (2006) Nat Immunol , vol.7 , pp. 569-575
    • Miao, E.A.1
  • 14
    • 33846024748 scopus 로고    scopus 로고
    • Regulation of Legionella phagosome maturation and infection through flagellin and host Ipaf
    • Amer A, et al. Regulation of Legionella phagosome maturation and infection through flagellin and host Ipaf. J Biol Chem 2006;281:35217-35223.
    • (2006) J Biol Chem , vol.281 , pp. 35217-35223
    • Amer, A.1
  • 15
    • 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 2011;145:745-757.
    • (2011) Cell , vol.145 , pp. 745-757
    • Elinav, E.1
  • 16
    • 84896691062 scopus 로고    scopus 로고
    • NLRP6 inflammasome orchestrates the colonic host-microbial interface by regulating goblet cell mucus secretion
    • Wlodarska M, et al. NLRP6 inflammasome orchestrates the colonic host-microbial interface by regulating goblet cell mucus secretion. Cell 2014;156:1045-1059.
    • (2014) Cell , vol.156 , pp. 1045-1059
    • Wlodarska, M.1
  • 17
    • 84858796861 scopus 로고    scopus 로고
    • An NLRP7-containing inflammasome mediates recognition of microbial lipopeptides in human macrophages
    • Khare S, et al. An NLRP7-containing inflammasome mediates recognition of microbial lipopeptides in human macrophages. Immunity 2012;36:464-476.
    • (2012) Immunity , vol.36 , pp. 464-476
    • Khare, S.1
  • 18
    • 84864317101 scopus 로고    scopus 로고
    • The NLRP12 inflammasome recognizes Yersinia pestis
    • Vladimer GI, et al. The NLRP12 inflammasome recognizes Yersinia pestis. Immunity 2012;37:96-107.
    • (2012) Immunity , vol.37 , pp. 96-107
    • Vladimer, G.I.1
  • 19
    • 84906571225 scopus 로고    scopus 로고
    • Inflammatory caspases are innate immune receptors for intracellular LPS
    • Shi J, et al. Inflammatory caspases are innate immune receptors for intracellular LPS. Nature 2014;514:187-192.
    • (2014) Nature , vol.514 , pp. 187-192
    • Shi, J.1
  • 20
    • 84883790050 scopus 로고    scopus 로고
    • Cytoplasmic LPS activates caspase-11: implications in TLR4-independent endotoxic shock
    • Hagar JA, Powell DA, Aachoui Y, Ernst RK, Miao EA. Cytoplasmic LPS activates caspase-11: implications in TLR4-independent endotoxic shock. Science 2013;341:1250-1253.
    • (2013) Science , vol.341 , pp. 1250-1253
    • Hagar, J.A.1    Powell, D.A.2    Aachoui, Y.3    Ernst, R.K.4    Miao, E.A.5
  • 21
    • 84883775365 scopus 로고    scopus 로고
    • Noncanonical inflammasome activation by intracellular LPS independent of TLR4
    • Kayagaki N, et al. Noncanonical inflammasome activation by intracellular LPS independent of TLR4. Science 2013;341:1246-1249.
    • (2013) Science , vol.341 , pp. 1246-1249
    • Kayagaki, N.1
  • 22
    • 84860225554 scopus 로고    scopus 로고
    • GBP5 promotes NLRP3 inflammasome assembly and immunity in mammals
    • Shenoy AR, et al. GBP5 promotes NLRP3 inflammasome assembly and immunity in mammals. Science 2012;336:481-485.
    • (2012) Science , vol.336 , pp. 481-485
    • Shenoy, A.R.1
  • 23
    • 84900564237 scopus 로고    scopus 로고
    • Caspase-11 activation requires lysis of pathogen-containing vacuoles by IFN-induced GTPases
    • Meunier E, et al. Caspase-11 activation requires lysis of pathogen-containing vacuoles by IFN-induced GTPases. Nature 2014;509:366-370.
    • (2014) Nature , vol.509 , pp. 366-370
    • Meunier, E.1
  • 24
    • 84899098318 scopus 로고    scopus 로고
    • Guanylate binding proteins promote caspase-11-dependent pyroptosis in response to cytoplasmic LPS
    • Pilla DM, et al. Guanylate binding proteins promote caspase-11-dependent pyroptosis in response to cytoplasmic LPS. Proc Natl Acad Sci USA 2014;111:6046-6051.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 6046-6051
    • Pilla, D.M.1
  • 25
    • 84859986329 scopus 로고    scopus 로고
    • Structures of the HIN domain:DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor
    • Jin T, et al. Structures of the HIN domain:DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor. Immunity 2012;36:561-571.
    • (2012) Immunity , vol.36 , pp. 561-571
    • Jin, T.1
  • 26
    • 84880818953 scopus 로고    scopus 로고
    • Molecular mechanism for p202-mediated specific inhibition of AIM2 inflammasome activation
    • Yin Q, et al. Molecular mechanism for p202-mediated specific inhibition of AIM2 inflammasome activation. Cell Rep 2013;4:327-339.
    • (2013) Cell Rep , vol.4 , pp. 327-339
    • Yin, Q.1
  • 27
    • 84878745041 scopus 로고    scopus 로고
    • Structural basis for termination of AIM2-mediated signaling by p202
    • Ru H, et al. Structural basis for termination of AIM2-mediated signaling by p202. Cell Res 2013;23:855-858.
    • (2013) Cell Res , vol.23 , pp. 855-858
    • Ru, H.1
  • 28
    • 84905376754 scopus 로고    scopus 로고
    • Structural mechanism of DNA recognition by the p202 HINa domain: insights into the inhibition of Aim2-mediated inflammatory signalling
    • Li H, Wang J, Wang J, Cao LS, Wang ZX, Wu JW. Structural mechanism of DNA recognition by the p202 HINa domain: insights into the inhibition of Aim2-mediated inflammatory signalling. Acta Crystallogr F Struct Biol Commun 2014;70:21-29.
    • (2014) Acta Crystallogr F Struct Biol Commun , vol.70 , pp. 21-29
    • Li, H.1    Wang, J.2    Wang, J.3    Cao, L.S.4    Wang, Z.X.5    Wu, J.W.6
  • 29
    • 32944462834 scopus 로고    scopus 로고
    • Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3
    • Kanneganti T-D, et al. Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3. Nat Cell Biol 2006;440:233-236.
    • (2006) Nat Cell Biol , vol.440 , pp. 233-236
    • Kanneganti, T.-D.1
  • 30
    • 64049111768 scopus 로고    scopus 로고
    • The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA
    • Allen IC, et al. The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA. Immunity 2009;30:556-565.
    • (2009) Immunity , vol.30 , pp. 556-565
    • Allen, I.C.1
  • 31
    • 84862777872 scopus 로고    scopus 로고
    • Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis
    • Shimada K, et al. Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis. Immunity 2012;36:401-414.
    • (2012) Immunity , vol.36 , pp. 401-414
    • Shimada, K.1
  • 32
    • 84901650255 scopus 로고    scopus 로고
    • Bacterial RNA:DNA hybrids are activators of the NLRP3 inflammasome
    • Kailasan Vanaja S, et al. Bacterial RNA:DNA hybrids are activators of the NLRP3 inflammasome. Proc Natl Acad Sci USA 2014;111:7765-7770.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 7765-7770
    • Kailasan Vanaja, S.1
  • 33
    • 84909595118 scopus 로고    scopus 로고
    • Human NLRP3 inflammasome senses multiple types of bacterial RNAs
    • 16509-16054
    • Sha W, et al. Human NLRP3 inflammasome senses multiple types of bacterial RNAs. Proc Natl Acad Sci USA 2014;111:16509-16054.
    • (2014) Proc Natl Acad Sci USA , vol.111
    • Sha, W.1
  • 34
    • 84901020681 scopus 로고    scopus 로고
    • RNA and β-hemolysin of group B Streptococcus induce interleukin-1β (IL-1β) by activating NLRP3 inflammasomes in mouse macrophages
    • Gupta R, et al. RNA and β-hemolysin of group B Streptococcus induce interleukin-1β (IL-1β) by activating NLRP3 inflammasomes in mouse macrophages. J Biol Chem 2014;289:13701-13705.
    • (2014) J Biol Chem , vol.289 , pp. 13701-13705
    • Gupta, R.1
  • 35
    • 84907494143 scopus 로고    scopus 로고
    • Cytosolic double-stranded RNA activates the NLRP3 inflammasome via MAVS-induced membrane permeabilization and K+ efflux
    • Franchi L, et al. Cytosolic double-stranded RNA activates the NLRP3 inflammasome via MAVS-induced membrane permeabilization and K+ efflux. J Immunol 2014;193:4114-4222.
    • (2014) J Immunol , vol.193 , pp. 4114-4222
    • Franchi, L.1
  • 36
    • 84880745984 scopus 로고    scopus 로고
    • The DHX33 RNA helicase senses cytosolic RNA and activates the NLRP3 inflammasome
    • Mitoma H, et al. The DHX33 RNA helicase senses cytosolic RNA and activates the NLRP3 inflammasome. Immunity 2013;39:123-135.
    • (2013) Immunity , vol.39 , pp. 123-135
    • Mitoma, H.1
  • 37
    • 84907210913 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase tripartite motif 33 is essential for cytosolic RNA-induced NLRP3 inflammasome activation
    • Weng L, et al. The E3 ubiquitin ligase tripartite motif 33 is essential for cytosolic RNA-induced NLRP3 inflammasome activation. J Immunol 2014;193:3676-3682.
    • (2014) J Immunol , vol.193 , pp. 3676-3682
    • Weng, L.1
  • 38
    • 84865394537 scopus 로고    scopus 로고
    • Interferon-inducible Ifi200-family genes as modifiers of lupus susceptibility
    • Choubey D. Interferon-inducible Ifi200-family genes as modifiers of lupus susceptibility. Immunol Lett 2012;147:10-17.
    • (2012) Immunol Lett , vol.147 , pp. 10-17
    • Choubey, D.1
  • 39
    • 23944473367 scopus 로고    scopus 로고
    • Identification of specific autoantigens in Sjögren's syndrome by SEREX
    • Uchida K, et al. Identification of specific autoantigens in Sjögren's syndrome by SEREX. Immunology 2005;116:53-63.
    • (2005) Immunology , vol.116 , pp. 53-63
    • Uchida, K.1
  • 40
    • 35748950430 scopus 로고    scopus 로고
    • Role of the interferon-inducible gene IFI16 in the etiopathogenesis of systemic autoimmune disorders
    • Mondini M, et al. Role of the interferon-inducible gene IFI16 in the etiopathogenesis of systemic autoimmune disorders. Ann N Y Acad Sci USA 2007;1110:47-56.
    • (2007) Ann N Y Acad Sci USA , vol.1110 , pp. 47-56
    • Mondini, M.1
  • 41
    • 79955897768 scopus 로고    scopus 로고
    • Cytosolic DNA triggers inflammasome activation in keratinocytes in psoriatic lesions
    • 82ra38
    • Dombrowski Y, et al. Cytosolic DNA triggers inflammasome activation in keratinocytes in psoriatic lesions. Sci Transl Med 2011;3:82ra38.
    • (2011) Sci Transl Med , vol.3
    • Dombrowski, Y.1
  • 42
    • 34948862264 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide
    • Lande R, et al. Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide. Nature 2007;449:564-569.
    • (2007) Nature , vol.449 , pp. 564-569
    • Lande, R.1
  • 43
    • 84856100861 scopus 로고    scopus 로고
    • Cathelicidin antimicrobial peptide LL-37 in psoriasis enables keratinocyte reactivity against TLR9 ligands
    • Morizane S, et al. Cathelicidin antimicrobial peptide LL-37 in psoriasis enables keratinocyte reactivity against TLR9 ligands. J Invest Dermatol 2011;132:135-143.
    • (2011) J Invest Dermatol , vol.132 , pp. 135-143
    • Morizane, S.1
  • 44
    • 0030775488 scopus 로고    scopus 로고
    • Cloning a novel member of the human interferon-inducible gene family associated with control of tumorigenicity in a model of human melanoma
    • DeYoung KL, et al. Cloning a novel member of the human interferon-inducible gene family associated with control of tumorigenicity in a model of human melanoma. Oncogene 1997;15:453-457.
    • (1997) Oncogene , vol.15 , pp. 453-457
    • DeYoung, K.L.1
  • 46
    • 77951269392 scopus 로고    scopus 로고
    • The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses
    • Rathinam VAK, et al. The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses. Nat Immunol 2010;11:395-402.
    • (2010) Nat Immunol , vol.11 , pp. 395-402
    • Rathinam, V.A.K.1
  • 47
    • 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 2010;11:385-393.
    • (2010) Nat Immunol , vol.11 , pp. 385-393
    • Fernandes-Alnemri, T.1
  • 48
    • 77953116282 scopus 로고    scopus 로고
    • Absent in melanoma 2 is required for innate immune recognition of Francisella tularensis
    • Jones JW, et al. Absent in melanoma 2 is required for innate immune recognition of Francisella tularensis. Proc Natl Acad Sci USA 2010;107:9771-9776.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 9771-9776
    • Jones, J.W.1
  • 49
    • 77955294800 scopus 로고    scopus 로고
    • Listeria monocytogenes triggers AIM2-mediated pyroptosis upon infrequent bacteriolysis in the macrophage cytosol
    • Sauer J-D, Witte CE, Zemansky J, Hanson B, Lauer P, Portnoy DA. Listeria monocytogenes triggers AIM2-mediated pyroptosis upon infrequent bacteriolysis in the macrophage cytosol. Cell Host Microbe 2010;7:412-419.
    • (2010) Cell Host Microbe , vol.7 , pp. 412-419
    • Sauer, J.-D.1    Witte, C.E.2    Zemansky, J.3    Hanson, B.4    Lauer, P.5    Portnoy, D.A.6
  • 50
    • 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 2010;40:1545-1551.
    • (2010) Eur J Immunol , vol.40 , pp. 1545-1551
    • Kim, S.1
  • 51
    • 77955501642 scopus 로고    scopus 로고
    • Cutting edge: cytosolic bacterial DNA activates the inflammasome via Aim2
    • Warren SE, et al. Cutting edge: cytosolic bacterial DNA activates the inflammasome via Aim2. J Immunol 2010;185:818-821.
    • (2010) J Immunol , vol.185 , pp. 818-821
    • Warren, S.E.1
  • 52
    • 84885472706 scopus 로고    scopus 로고
    • HPV16 activates the AIM2 inflammasome in keratinocytes
    • Reinholz M, et al. HPV16 activates the AIM2 inflammasome in keratinocytes. Arch Dermatol Res 2013;305:723-732.
    • (2013) Arch Dermatol Res , vol.305 , pp. 723-732
    • Reinholz, M.1
  • 53
  • 54
    • 0028172106 scopus 로고
    • Interferon-γ-inducible protein p16. a new target of antinuclear antibodies in patients with systemic lupus erythematosus
    • Seelig HP, Ehrfeld H, Renz M. Interferon-γ-inducible protein p16. a new target of antinuclear antibodies in patients with systemic lupus erythematosus. Arthritis Rheum 1994;37:1672-1683.
    • (1994) Arthritis Rheum , vol.37 , pp. 1672-1683
    • Seelig, H.P.1    Ehrfeld, H.2    Renz, M.3
  • 55
    • 84888002403 scopus 로고    scopus 로고
    • PNAS plus: from the cover: IFI16 senses DNA forms of the lentiviral replication cycle and controls HIV-1 replication
    • Jakobsen MR, et al. PNAS plus: from the cover: IFI16 senses DNA forms of the lentiviral replication cycle and controls HIV-1 replication. Proc Natl Acad Sci USA 2013;110:E4571-E4580.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. E4571-E4580
    • Jakobsen, M.R.1
  • 56
    • 84892739389 scopus 로고    scopus 로고
    • Cell death by pyroptosis drives CD4 T-cell depletion in HIV-1 infection
    • Doitsh G, et al. Cell death by pyroptosis drives CD4 T-cell depletion in HIV-1 infection. Nature 2013;505:509-514.
    • (2013) Nature , vol.505 , pp. 509-514
    • Doitsh, G.1
  • 57
    • 84892946076 scopus 로고    scopus 로고
    • IFI16 DNA sensor is required for death of lymphoid CD4 T cells abortively infected with HIV
    • Monroe KM, et al. IFI16 DNA sensor is required for death of lymphoid CD4 T cells abortively infected with HIV. Science 2013;343:428-432.
    • (2013) Science , vol.343 , pp. 428-432
    • Monroe, K.M.1
  • 58
    • 84896744932 scopus 로고    scopus 로고
    • T cells detect intracellular DNA but fail to induce type I IFN responses: implications for restriction of HIV replication
    • Berg RK, et al. T cells detect intracellular DNA but fail to induce type I IFN responses: implications for restriction of HIV replication. PLoS ONE 2014;9:e84513.
    • (2014) PLoS ONE , vol.9 , pp. e84513
    • Berg, R.K.1
  • 59
    • 79952468076 scopus 로고    scopus 로고
    • Interferon-inducible protein 16: insight into the interaction with tumor suppressor p53
    • Liao JCC, et al. Interferon-inducible protein 16: insight into the interaction with tumor suppressor p53. Structure 2011;19:418-429.
    • (2011) Structure , vol.19 , pp. 418-429
    • Liao, J.C.C.1
  • 60
    • 0042567245 scopus 로고    scopus 로고
    • Role of IFI 16, a member of the interferon-inducible p200-protein family, in prostate epithelial cellular senescence
    • Xin H, Curry J, Johnstone RW, Nickoloff BJ, Choubey D. Role of IFI 16, a member of the interferon-inducible p200-protein family, in prostate epithelial cellular senescence. Oncogene 2003;22:4831-4840.
    • (2003) Oncogene , vol.22 , pp. 4831-4840
    • Xin, H.1    Curry, J.2    Johnstone, R.W.3    Nickoloff, B.J.4    Choubey, D.5
  • 61
    • 0026644771 scopus 로고
    • A novel gene constitutively expressed in human lymphoid cells is inducible with interferon-gamma in myeloid cells
    • Trapani JA, et al. A novel gene constitutively expressed in human lymphoid cells is inducible with interferon-gamma in myeloid cells. Immunogenetics 1992;36:369-376.
    • (1992) Immunogenetics , vol.36 , pp. 369-376
    • Trapani, J.A.1
  • 62
    • 2442494082 scopus 로고    scopus 로고
    • Requirement of IFI16 for the maximal activation of p53 induced by ionizing radiation
    • Fujiuchi N, et al. Requirement of IFI16 for the maximal activation of p53 induced by ionizing radiation. J Biol Chem 2004;279:20339-20344.
    • (2004) J Biol Chem , vol.279 , pp. 20339-20344
    • Fujiuchi, N.1
  • 65
    • 77951881456 scopus 로고    scopus 로고
    • Crystal structure of the Caenorhabditis elegans apoptosome reveals an octameric assembly of CED-4
    • Qi S, et al. Crystal structure of the Caenorhabditis elegans apoptosome reveals an octameric assembly of CED-4. Cell 2010;141:446-457.
    • (2010) Cell , vol.141 , pp. 446-457
    • Qi, S.1
  • 67
    • 78651241652 scopus 로고    scopus 로고
    • Structure of the drosophila apoptosome at 6.9 å resolution
    • Yuan S, et al. Structure of the drosophila apoptosome at 6.9 å resolution. Structure 2011;19:128-140.
    • (2011) Structure , vol.19 , pp. 128-140
    • Yuan, S.1
  • 68
    • 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 2007;25:713-724.
    • (2007) Mol Cell , vol.25 , pp. 713-724
    • Faustin, B.1
  • 69
    • 84869044838 scopus 로고    scopus 로고
    • Formation and structure of a NAIP5-NLRC4 inflammasome induced by direct interactions with conserved N- and C-terminal regions of flagellin
    • Halff EF, Diebolder CA, Versteeg M, Schouten A, Brondijk THC, Huizinga EG. Formation and structure of a NAIP5-NLRC4 inflammasome induced by direct interactions with conserved N- and C-terminal regions of flagellin. J Biol Chem 2012;287:38460-38472.
    • (2012) J Biol Chem , vol.287 , pp. 38460-38472
    • Halff, E.F.1    Diebolder, C.A.2    Versteeg, M.3    Schouten, A.4    Brondijk, T.H.C.5    Huizinga, E.G.6
  • 70
    • 34548031870 scopus 로고    scopus 로고
    • The pyroptosome: a supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation
    • Fernandes-Alnemri T, et al. The pyroptosome: a supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation. Cell Death Differ 2007;14:1590-1604.
    • (2007) Cell Death Differ , vol.14 , pp. 1590-1604
    • Fernandes-Alnemri, T.1
  • 71
    • 0033607768 scopus 로고    scopus 로고
    • ASC, a novel 22-kDa protein, aggregates during apoptosis of human promyelocytic leukemia HL-60 cells
    • Masumoto J, et al. ASC, a novel 22-kDa protein, aggregates during apoptosis of human promyelocytic leukemia HL-60 cells. J Biol Chem 1999;274:33835-33838.
    • (1999) J Biol Chem , vol.274 , pp. 33835-33838
    • Masumoto, J.1
  • 72
    • 84906544294 scopus 로고    scopus 로고
    • Identification of multifaceted binding modes for pyrin and ASC pyrin domains gives insights into pyrin inflammasome assembly
    • Vajjhala PR, et al. Identification of multifaceted binding modes for pyrin and ASC pyrin domains gives insights into pyrin inflammasome assembly. J Biol Chem 2014;289:23504-23519.
    • (2014) J Biol Chem , vol.289 , pp. 23504-23519
    • Vajjhala, P.R.1
  • 73
    • 84896332642 scopus 로고    scopus 로고
    • Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes
    • Lu A, et al. Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes. Cell 2014;156:1193-1206.
    • (2014) Cell , vol.156 , pp. 1193-1206
    • Lu, A.1
  • 74
    • 84896381627 scopus 로고    scopus 로고
    • Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation
    • Cai X, et al. Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation. Cell 2014;156:1207-1222.
    • (2014) Cell , vol.156 , pp. 1207-1222
    • Cai, X.1
  • 75
    • 77953714711 scopus 로고    scopus 로고
    • Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling
    • Lin S-C, Lo Y-C, Wu H. Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling. Nature 2010;465:885-890.
    • (2010) Nature , vol.465 , pp. 885-890
    • Lin, S.-C.1    Lo, Y.-C.2    Wu, H.3
  • 76
    • 33846702221 scopus 로고    scopus 로고
    • Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex
    • Park HH, et al. Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex. Cell 2007;128:533-546.
    • (2007) Cell , vol.128 , pp. 533-546
    • Park, H.H.1
  • 77
    • 84904646033 scopus 로고    scopus 로고
    • The NLRP3 inflammasome is released as a particulate danger signal that amplifies the inflammatory response
    • Baroja-Mazo A, et al. The NLRP3 inflammasome is released as a particulate danger signal that amplifies the inflammatory response. Nat Immunol 2014;15:738-748.
    • (2014) Nat Immunol , vol.15 , pp. 738-748
    • Baroja-Mazo, A.1
  • 79
    • 84904692363 scopus 로고    scopus 로고
    • The adaptor ASC has extracellular and "prionoid" activities that propagate inflammation
    • Franklin BS, et al. The adaptor ASC has extracellular and "prionoid" activities that propagate inflammation. Nat Immunol 2014;15:727-737.
    • (2014) Nat Immunol , vol.15 , pp. 727-737
    • Franklin, B.S.1
  • 80
  • 81
    • 84913556254 scopus 로고    scopus 로고
    • Neutralization of ASC improves sperm motility in men with spinal cord injury
    • Ibrahim E, et al. Neutralization of ASC improves sperm motility in men with spinal cord injury. Hum Reprod 2014;29:2368-2373.
    • (2014) Hum Reprod , vol.29 , pp. 2368-2373
    • Ibrahim, E.1
  • 82
    • 84877692253 scopus 로고    scopus 로고
    • Structure of the absent in melanoma 2 (AIM2) pyrin domain provides insights into the mechanisms of AIM2 autoinhibition and inflammasome assembly
    • Jin T, Perry A, Smith P, Jiang J, Xiao TS. Structure of the absent in melanoma 2 (AIM2) pyrin domain provides insights into the mechanisms of AIM2 autoinhibition and inflammasome assembly. J Biol Chem 2013;288:13225-13235.
    • (2013) J Biol Chem , vol.288 , pp. 13225-13235
    • Jin, T.1    Perry, A.2    Smith, P.3    Jiang, J.4    Xiao, T.S.5
  • 83
    • 84880280093 scopus 로고    scopus 로고
    • Crystal structure of NLRC4 reveals its autoinhibition mechanism
    • Hu Z, et al. Crystal structure of NLRC4 reveals its autoinhibition mechanism. Science 2013;341:172-175.
    • (2013) Science , vol.341 , pp. 172-175
    • Hu, Z.1
  • 84
    • 80054703126 scopus 로고    scopus 로고
    • Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA
    • Kowalinski E, et al. Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. Cell 2011;147:423-435.
    • (2011) Cell , vol.147 , pp. 423-435
    • Kowalinski, E.1
  • 85
    • 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 2011;6:e27040.
    • (2011) PLoS ONE , vol.6 , pp. e27040
    • Veeranki, S.1    Duan, X.2    Panchanathan, R.3    Liu, H.4    Choubey, D.5
  • 86
    • 84896638307 scopus 로고    scopus 로고
    • The PYRIN domain-only protein POP3 inhibits ALR inflammasomes and regulates responses to infection with DNA viruses
    • Khare S, et al. The PYRIN domain-only protein POP3 inhibits ALR inflammasomes and regulates responses to infection with DNA viruses. Nat Immunol 2014;15:343-353.
    • (2014) Nat Immunol , vol.15 , pp. 343-353
    • Khare, S.1
  • 87
    • 0038682430 scopus 로고    scopus 로고
    • The PAAD/PYRIN-only protein POP1/ASC2 is a modulator of ASC-mediated nuclear-factor-kappa B and pro-caspase-1 regulation
    • Stehlik C, Krajewska M, Welsh K, Krajewski S, Godzik A, Reed JC. The PAAD/PYRIN-only protein POP1/ASC2 is a modulator of ASC-mediated nuclear-factor-kappa B and pro-caspase-1 regulation. Biochem J 2003;373:101-113.
    • (2003) Biochem J , vol.373 , pp. 101-113
    • Stehlik, C.1    Krajewska, M.2    Welsh, K.3    Krajewski, S.4    Godzik, A.5    Reed, J.C.6
  • 88
    • 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 JB, et al. A poxvirus-encoded pyrin domain protein interacts with ASC-1 to inhibit host inflammatory and apoptotic responses to infection. Immunity 2005;23:587-598.
    • (2005) Immunity , vol.23 , pp. 587-598
    • Johnston, J.B.1
  • 89
    • 35548929476 scopus 로고    scopus 로고
    • A Shope Fibroma virus PYRIN-only protein modulates the host immune response
    • Dorfleutner A, et al. A Shope Fibroma virus PYRIN-only protein modulates the host immune response. Virus Genes 2007;35:685-694.
    • (2007) Virus Genes , vol.35 , pp. 685-694
    • Dorfleutner, A.1
  • 90
    • 84883759334 scopus 로고    scopus 로고
    • RIG-I forms signaling-competent filaments in an ATP-dependent. Ubiquitin-independent manner
    • Peisley A, Bin W, Yao H, Walz T, Hur S. RIG-I forms signaling-competent filaments in an ATP-dependent. Ubiquitin-independent manner. Mol Cell 2013;51:1-11.
    • (2013) Mol Cell , vol.51 , pp. 1-11
    • Peisley, A.1    Bin, W.2    Yao, H.3    Walz, T.4    Hur, S.5
  • 91
    • 84857195479 scopus 로고    scopus 로고
    • Activation of autophagy by inflammatory signals limits IL-1β production by targeting ubiquitinated inflammasomes for destruction
    • Shi C-S, et al. Activation of autophagy by inflammatory signals limits IL-1β production by targeting ubiquitinated inflammasomes for destruction. Nat Immunol 2012;13:255-263.
    • (2012) Nat Immunol , vol.13 , pp. 255-263
    • Shi, C.-S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.