메뉴 건너뛰기




Volumn 14, Issue 1, 2007, Pages 10-22

Inflammatory caspases and inflammasomes: Master switches of inflammation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; CASPASE; CASPASE 11; CASPASE 12; CASPASE 5; CASPASE 9; CYTOKINE; ICE PROTEASE ACTIVATING FACTO; INFLAMMASOM; INTERLEUKIN 1BETA CONVERTING ENZYME; MULTIPROTEIN COMPLEX; NAL; NEURONAL APOPTOSIS INHIBITOR PROTEI; NOD LIKE RECEPTOR; PROTEINASE;

EID: 33845497181     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/sj.cdd.4402038     Document Type: Review
Times cited : (705)

References (137)
  • 1
    • 0024551325 scopus 로고
    • A pre-aspartate-specific protease from human leukocytes that cleaves pro-interleukin-1 beta
    • Black RA, Kronheim SR, Merriam JE, March CJ, Hopp TP. A pre-aspartate-specific protease from human leukocytes that cleaves pro-interleukin-1 beta. J Biol Chem 1989; 264: 5323-5326.
    • (1989) J Biol Chem , vol.264 , pp. 5323-5326
    • Black, R.A.1    Kronheim, S.R.2    Merriam, J.E.3    March, C.J.4    Hopp, T.P.5
  • 4
    • 0026507126 scopus 로고
    • A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes
    • Thornberry NA, Bull HG, Calaycay JR, Chapman KT, Howard AD, Kostura MJ et al. A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes. Nature 1992; 356: 768-774.
    • (1992) Nature , vol.356 , pp. 768-774
    • Thornberry, N.A.1    Bull, H.G.2    Calaycay, J.R.3    Chapman, K.T.4    Howard, A.D.5    Kostura, M.J.6
  • 5
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme
    • Yuan J, Shaham S, Ledoux S, Ellis HM, Horvitz HR. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme. Cell 1993; 75: 641-652.
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5
  • 7
    • 2542457495 scopus 로고    scopus 로고
    • Inflammatory caspases: Linking an intracellular innate immune system to autoinflammatory diseases
    • Martinon F, Tschopp J. Inflammatory caspases: Linking an intracellular innate immune system to autoinflammatory diseases. Cell 2004; 117: 561-574.
    • (2004) Cell , vol.117 , pp. 561-574
    • Martinon, F.1    Tschopp, J.2
  • 8
    • 24344500211 scopus 로고    scopus 로고
    • Initial sequence of the chimpanzee genome and comparison with the human genome
    • Initial sequence of the chimpanzee genome and comparison with the human genome. Nature 2005; 437: 69-87.
    • (2005) Nature , vol.437 , pp. 69-87
  • 9
  • 10
    • 33645462359 scopus 로고    scopus 로고
    • Spread of an inactive form of caspase-12 in humans is due to recent positive selection
    • Xue Y, Daly A, Yngvadottir B, Liu M, Coop G, Kim Y et al. Spread of an inactive form of caspase-12 in humans is due to recent positive selection. Am J Hum Genet 2006; 78: 659-670.
    • (2006) Am J Hum Genet , vol.78 , pp. 659-670
    • Xue, Y.1    Daly, A.2    Yngvadottir, B.3    Liu, M.4    Coop, G.5    Kim, Y.6
  • 11
    • 27744446058 scopus 로고    scopus 로고
    • IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-related protein ST2 and induces T helper type 2-associated cytokines
    • Schmitz J, Owyang A, Oldham E, Song Y, Murphy E, McClanahan TK et al. IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-related protein ST2 and induces T helper type 2-associated cytokines, Immunity 2005; 23: 479-490.
    • (2005) Immunity , vol.23 , pp. 479-490
    • Schmitz, J.1    Owyang, A.2    Oldham, E.3    Song, Y.4    Murphy, E.5    McClanahan, T.K.6
  • 12
    • 0028984948 scopus 로고
    • Mice deficient in IL-1 beta-converting enzyme are defective in production of mature IL-1 beta and resistant to endotoxic shock
    • Li P, Allen H, Banerjee S, Franklin S, Herzog L, Johnston C et al. Mice deficient in IL-1 beta-converting enzyme are defective in production of mature IL-1 beta and resistant to endotoxic shock. Cell 1995; 80: 401-411.
    • (1995) Cell , vol.80 , pp. 401-411
    • Li, P.1    Allen, H.2    Banerjee, S.3    Franklin, S.4    Herzog, L.5    Johnston, C.6
  • 13
    • 0028920863 scopus 로고
    • Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme
    • Kuida K, Lippke JA, Ku G, Harding MW, Livingston DJ, Su MS et al. Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme. Science 1995; 267: 2000-2003.
    • (1995) Science , vol.267 , pp. 2000-2003
    • Kuida, K.1    Lippke, J.A.2    Ku, G.3    Harding, M.W.4    Livingston, D.J.5    Su, M.S.6
  • 14
    • 15644369352 scopus 로고    scopus 로고
    • Activation of interferon-gamma inducing factor mediated by interleukin-1 beta converting enzyme
    • Gu Y, Kuida K, Tsutsui H, Ku G, Hsiao K, Fleming MA et al. Activation of interferon-gamma inducing factor mediated by interleukin-1 beta converting enzyme. Science 1997; 275: 206-209.
    • (1997) Science , vol.275 , pp. 206-209
    • Gu, Y.1    Kuida, K.2    Tsutsui, H.3    Ku, G.4    Hsiao, K.5    Fleming, M.A.6
  • 15
    • 0031004174 scopus 로고    scopus 로고
    • Caspase-1 processes IFN-gamma-inducing factor and regulates LPS-induced IFN-gamma production
    • Ghayur T, Banerjee S, Hugunin M, Butler D, Herzog L, Carter A et al. Caspase-1 processes IFN-gamma-inducing factor and regulates LPS-induced IFN-gamma production. Nature 1997; 386: 619-623.
    • (1997) Nature , vol.386 , pp. 619-623
    • Ghayur, T.1    Banerjee, S.2    Hugunin, M.3    Butler, D.4    Herzog, L.5    Carter, A.6
  • 16
    • 0038687082 scopus 로고    scopus 로고
    • Interleukin-18 and host defense against infection
    • Dinarello CA, Fantuzzi G. Interleukin-18 and host defense against infection. J Infect Dis 2003; 187: S370-384.
    • (2003) J Infect Dis , vol.187
    • Dinarello, C.A.1    Fantuzzi, G.2
  • 17
    • 8344261590 scopus 로고    scopus 로고
    • Infection, fever, and exogenous and endogenous pyrogens: Some concepts have changed
    • Dinarello CA. Infection, fever, and exogenous and endogenous pyrogens: some concepts have changed. J Endotoxin Res 2004; 10: 201-222.
    • (2004) J Endotoxin Res , vol.10 , pp. 201-222
    • Dinarello, C.A.1
  • 18
    • 0020586432 scopus 로고
    • The adjuvanticity of interleukin 1 in vivo
    • Staruch MJ, Wood DD. The adjuvanticity of interleukin 1 in vivo. J Immunol 1983; 130: 2191-2194.
    • (1983) J Immunol , vol.130 , pp. 2191-2194
    • Staruch, M.J.1    Wood, D.D.2
  • 19
    • 0022472749 scopus 로고
    • Tumor necrosis factor (cachectin) is an endogenous pyrogen and induces production of interleukin 1
    • Dinarello CA, Cannon JG, Wolff SM, Bernheim HA, Beutler B, Cerami A et al. Tumor necrosis factor (cachectin) is an endogenous pyrogen and induces production of interleukin 1. J Exp Med 1986; 163: 1433-1450.
    • (1986) J Exp Med , vol.163 , pp. 1433-1450
    • Dinarello, C.A.1    Cannon, J.G.2    Wolff, S.M.3    Bernheim, H.A.4    Beutler, B.5    Cerami, A.6
  • 20
    • 0037791779 scopus 로고    scopus 로고
    • Humoral links between sleep and the immune system: Research issues
    • Krueger JM, Majde JA. Humoral links between sleep and the immune system: research issues. Ann N Y Acad Sci 2003; 992: 9-20.
    • (2003) Ann N Y Acad Sci , vol.992 , pp. 9-20
    • Krueger, J.M.1    Majde, J.A.2
  • 21
    • 0035932121 scopus 로고    scopus 로고
    • Interleukin-1beta-mediated induction of Cox-2 in the CNS contributes to inflammatory pain hypersensitivity
    • Samad TA, Moore KA, Sapirstein A, Billet S, Allchome A, Poole S et al. Interleukin-1beta-mediated induction of Cox-2 in the CNS contributes to inflammatory pain hypersensitivity. Nature 2001; 410: 471-475.
    • (2001) Nature , vol.410 , pp. 471-475
    • Samad, T.A.1    Moore, K.A.2    Sapirstein, A.3    Billet, S.4    Allchome, A.5    Poole, S.6
  • 22
    • 33645891172 scopus 로고    scopus 로고
    • Cytokines in atherosclerosis: Pathogenic and regulatory pathways
    • Tedgui A, Mallat Z. Cytokines in atherosclerosis: Pathogenic and regulatory pathways. Physiol Rev 2006; 86: 515-581.
    • (2006) Physiol Rev , vol.86 , pp. 515-581
    • Tedgui, A.1    Mallat, Z.2
  • 23
    • 0037180771 scopus 로고    scopus 로고
    • Inflammation in atherosclerosis
    • Libby P. Inflammation in atherosclerosis. Nature 2002; 420: 868-874.
    • (2002) Nature , vol.420 , pp. 868-874
    • Libby, P.1
  • 25
    • 27644549559 scopus 로고    scopus 로고
    • Infiltration of COX-2-expressing macrophages is a prerequisite for IL-1 beta-induced neovascularization and tumor growth
    • Nakao S, Kuwano T, Tsutsumi-Miyahara C, Ueda S, Kimura YN, Hamano S et al. Infiltration of COX-2-expressing macrophages is a prerequisite for IL-1 beta-induced neovascularization and tumor growth. J Clin Invest 2005; 115: 2979-2991.
    • (2005) J Clin Invest , vol.115 , pp. 2979-2991
    • Nakao, S.1    Kuwano, T.2    Tsutsumi-Miyahara, C.3    Ueda, S.4    Kimura, Y.N.5    Hamano, S.6
  • 26
    • 31544479592 scopus 로고    scopus 로고
    • Chondroprotective drugs in degenerative joint diseases
    • Verbruggen G. Chondroprotective drugs in degenerative joint diseases. Rheumatology (Oxford) 2006; 45: 129-138.
    • (2006) Rheumatology (Oxford) , vol.45 , pp. 129-138
    • Verbruggen, G.1
  • 27
    • 0031850873 scopus 로고    scopus 로고
    • Aspects of the involvement of interleukin-1 and nitric oxide in the pathogenesis of insulin-dependent diabetes mellitus
    • Sjoholm A. Aspects of the involvement of interleukin-1 and nitric oxide in the pathogenesis of insulin-dependent diabetes mellitus. Cell Death Differ 1998; 5: 461-468.
    • (1998) Cell Death Differ , vol.5 , pp. 461-468
    • Sjoholm, A.1
  • 28
    • 0036738398 scopus 로고    scopus 로고
    • Glucose-induced beta cell production of IL-1beta contributes to glucotoxicity in human pancreatic islets
    • Maedler K, Sergeev P, Ris F, Oberholzer J, Joller-Jemelka HI, Spinas GA et al. Glucose-induced beta cell production of IL-1beta contributes to glucotoxicity in human pancreatic islets. J Clin Invest 2002; 110: 851-860.
    • (2002) J Clin Invest , vol.110 , pp. 851-860
    • Maedler, K.1    Sergeev, P.2    Ris, F.3    Oberholzer, J.4    Joller-Jemelka, H.I.5    Spinas, G.A.6
  • 29
  • 30
    • 0023951485 scopus 로고
    • The kinetics of interleukin 1 secretion from activated monocytes. Differences between interleukin 1 alpha and interleukin 1 beta
    • Hazuda DJ, Lee JC, Young PR. The kinetics of interleukin 1 secretion from activated monocytes. Differences between interleukin 1 alpha and interleukin 1 beta. J Biol Chem 1988; 263: 8473-8479.
    • (1988) J Biol Chem , vol.263 , pp. 8473-8479
    • Hazuda, D.J.1    Lee, J.C.2    Young, P.R.3
  • 31
    • 0023947763 scopus 로고
    • Generation of biologically active interleukin-1 beta by proteolytic cleavage of the inactive precursor
    • Black RA, Kronheim SR, Cantrell M, Deeley MC, March CJ, Prickett KS et al. Generation of biologically active interleukin-1 beta by proteolytic cleavage of the inactive precursor. J Biol Chem 1988; 263: 9437-9442.
    • (1988) J Biol Chem , vol.263 , pp. 9437-9442
    • Black, R.A.1    Kronheim, S.R.2    Cantrell, M.3    Deeley, M.C.4    March, C.J.5    Prickett, K.S.6
  • 32
    • 0027327223 scopus 로고
    • Purification and characterization of active human interleukin-1 beta-converting enzyme from THP.1 monocytic cells
    • Miller DK, Ayala JM, Egger LA, Raju SM, Yamin TT, Ding GJ et al. Purification and characterization of active human interleukin-1 beta-converting enzyme from THP.1 monocytic cells. J Biol Chem 1993; 268: 18062-18069.
    • (1993) J Biol Chem , vol.268 , pp. 18062-18069
    • Miller, D.K.1    Ayala, J.M.2    Egger, L.A.3    Raju, S.M.4    Yamin, T.T.5    Ding, G.J.6
  • 33
    • 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
  • 34
    • 0032548919 scopus 로고    scopus 로고
    • Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE
    • Wang S, Miura M, Jung YK, Zhu H, Li E, Yuan J. Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE. Cell 1998; 92: 501-509.
    • (1998) Cell , vol.92 , pp. 501-509
    • Wang, S.1    Miura, M.2    Jung, Y.K.3    Zhu, H.4    Li, E.5    Yuan, J.6
  • 35
    • 0034704161 scopus 로고    scopus 로고
    • Expression analysis of the human caspase-1 subfamily reveals specific regulation of the CASP5 gene by lipopolysaccharide and interferon-gamma
    • Lin XY, Choi MS, Porter AG. Expression analysis of the human caspase-1 subfamily reveals specific regulation of the CASP5 gene by lipopolysaccharide and interferon-gamma. J Biol Chem 2000; 275: 39920-39926.
    • (2000) J Biol Chem , vol.275 , pp. 39920-39926
    • Lin, X.Y.1    Choi, M.S.2    Porter, A.G.3
  • 37
    • 2442432416 scopus 로고    scopus 로고
    • Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death
    • Hitomi J, Katayama T, Eguchi Y, Kudo T, Taniguchi M, Koyama Y et al. Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death. J Cell Biol 2004; 165: 347-356.
    • (2004) J Cell Biol , vol.165 , pp. 347-356
    • Hitomi, J.1    Katayama, T.2    Eguchi, Y.3    Kudo, T.4    Taniguchi, M.5    Koyama, Y.6
  • 38
    • 23844481790 scopus 로고    scopus 로고
    • Caspase-12 and caspase-4 are not required for caspase-dependent endoplasmic reticulum stress-induced apoptosis
    • Obeng EA, Boise LH. Caspase-12 and caspase-4 are not required for caspase-dependent endoplasmic reticulum stress-induced apoptosis. J Biol Chem 2005; 280: 29578-29587.
    • (2005) J Biol Chem , vol.280 , pp. 29578-29587
    • Obeng, E.A.1    Boise, L.H.2
  • 39
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T, Zhu H, Morishima N, Li E, Xu J, Yankner BA et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 2000; 403: 98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6
  • 40
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • Hetz C, Russelakis-Carneiro M, Maundrell K, Castilla J, Soto C. Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J 2003; 22: 5435-5445.
    • (2003) EMBO J , vol.22 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 42
    • 33645124763 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces apoptosis by an apoptosome-dependent but caspase 12-independent mechanism
    • Di Sano F, Ferraro E, Tufi R, Achsel T, Piacentini M, Cecconi F. Endoplasmic reticulum stress induces apoptosis by an apoptosome-dependent but caspase 12-independent mechanism. J Biol Chem 2006; 281: 2693-2700.
    • (2006) J Biol Chem , vol.281 , pp. 2693-2700
    • Di Sano, F.1    Ferraro, E.2    Tufi, R.3    Achsel, T.4    Piacentini, M.5    Cecconi, F.6
  • 45
    • 0034930561 scopus 로고    scopus 로고
    • Evolutionary lines of cysteine peptidases
    • Barrett AJ, Rawlings ND. Evolutionary lines of cysteine peptidases. Biol Chem 2001; 382: 727-733.
    • (2001) Biol Chem , vol.382 , pp. 727-733
    • Barrett, A.J.1    Rawlings, N.D.2
  • 47
    • 28444491105 scopus 로고    scopus 로고
    • Mechanisms of apoptosis through structural biology
    • Yan N, Shi Y. Mechanisms of apoptosis through structural biology. Annu Rev Cell Dev Biol 2005; 21: 35-56.
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 35-56
    • Yan, N.1    Shi, Y.2
  • 48
    • 2442453730 scopus 로고    scopus 로고
    • The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress
    • Tinel A, Tschopp J. The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress. Science 2004; 304: 843-846.
    • (2004) Science , vol.304 , pp. 843-846
    • Tinel, A.1    Tschopp, J.2
  • 49
    • 3943071150 scopus 로고    scopus 로고
    • Cytochrome C-mediated apoptosis
    • Jiang X, Wang X. Cytochrome C-mediated apoptosis. Annu Rev Biochem 2004; 73: 87-106.
    • (2004) Annu Rev Biochem , vol.73 , pp. 87-106
    • Jiang, X.1    Wang, X.2
  • 50
    • 0037276437 scopus 로고    scopus 로고
    • The CD95(APO-1/Fas) DISC and beyond
    • Peter ME, Krammer PH. The CD95(APO-1/Fas) DISC and beyond. Cell Death Differ 2003; 10: 26-35.
    • (2003) Cell Death Differ , vol.10 , pp. 26-35
    • Peter, M.E.1    Krammer, P.H.2
  • 51
    • 33646024628 scopus 로고    scopus 로고
    • The apoptosome activates caspase-9 by dimerization
    • Pop C, Timmer J, Sperandio S, Salvesen GS. The apoptosome activates caspase-9 by dimerization. Mol Cell 2006; 22: 269-275.
    • (2006) Mol Cell , vol.22 , pp. 269-275
    • Pop, C.1    Timmer, J.2    Sperandio, S.3    Salvesen, G.S.4
  • 53
    • 33645958613 scopus 로고    scopus 로고
    • TIR, CARD and PYRIN: Three domains for an antimicrobial triad
    • Werts C, Girardin SE, Philpott DJ. TIR, CARD and PYRIN: Three domains for an antimicrobial triad. Cell Death Differ 2006; 13: 798-815.
    • (2006) Cell Death Differ , vol.13 , pp. 798-815
    • Werts, C.1    Girardin, S.E.2    Philpott, D.J.3
  • 54
    • 22444433175 scopus 로고    scopus 로고
    • NLRs join TLRs as innate sensors of pathogens
    • Martinon F, Tschopp J. NLRs join TLRs as innate sensors of pathogens. Trends Immunol 2005; 26: 447-454.
    • (2005) Trends Immunol , vol.26 , pp. 447-454
    • Martinon, F.1    Tschopp, J.2
  • 55
    • 17644366913 scopus 로고    scopus 로고
    • NOD-LRR proteins: Role in host-microbial interactions and inflammatory disease
    • Inohara N, Chamaillard M, McDonald C, Nunez G. NOD-LRR proteins: Role in host-microbial interactions and inflammatory disease. Annu Rev Biochem 2005: 74: 355-383.
    • (2005) Annu Rev Biochem , vol.74 , pp. 355-383
    • Inohara, N.1    Chamaillard, M.2    McDonald, C.3    Nunez, G.4
  • 57
    • 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 Mol Cell Biol 2003; 4: 95-104.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 95-104
    • Tschopp, J.1    Martinon, F.2    Burns, K.3
  • 58
    • 0028896092 scopus 로고
    • The gene for neuronal apoptosis inhibitory protein is partially deleted in individuals with spinal muscular atrophy
    • Roy N, Mahadevan MS, McLean M, Shutler G, Yaraghi Z, Farahani R et al. The gene for neuronal apoptosis inhibitory protein is partially deleted in individuals with spinal muscular atrophy. Cell 1995; 80: 167-178.
    • (1995) Cell , vol.80 , pp. 167-178
    • Roy, N.1    Mahadevan, M.S.2    McLean, M.3    Shutler, G.4    Yaraghi, Z.5    Farahani, R.6
  • 59
    • 0033215040 scopus 로고    scopus 로고
    • Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases
    • Deveraux QL, Leo E, Stennicke HR, Welsh K, Salvesen GS, Reed JC. Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases. EMBO J 1999; 18: 5242-5251.
    • (1999) EMBO J , vol.18 , pp. 5242-5251
    • Deveraux, Q.L.1    Leo, E.2    Stennicke, H.R.3    Welsh, K.4    Salvesen, G.S.5    Reed, J.C.6
  • 61
    • 33645770203 scopus 로고    scopus 로고
    • The Birc1e cytosolic pattern-recognition receptor contributes to the detection and control of Legionella pneumophila infection
    • Zamboni DS, Kobayashi KS, Kohlsdorf T, Ogura Y, Long EM, Vance RE et al. The Birc1e cytosolic pattern-recognition receptor contributes to the detection and control of Legionella pneumophila infection. Nat Immunol 2006; 7: 318-325.
    • (2006) Nat Immunol , vol.7 , pp. 318-325
    • Zamboni, D.S.1    Kobayashi, K.S.2    Kohlsdorf, T.3    Ogura, Y.4    Long, E.M.5    Vance, R.E.6
  • 62
    • 7944231451 scopus 로고    scopus 로고
    • ASC is essential for LPS-induced activation of procaspase-1 independently of TLR-associated signal adaptor molecules
    • Yamamoto M, Yaginuma K, Tsutsui H, Sagara J, Guan X, Seki E et al. ASC is essential for LPS-induced activation of procaspase-1 independently of TLR-associated signal adaptor molecules. Genes Cells 2004; 9: 1055-1067.
    • (2004) Genes Cells , vol.9 , pp. 1055-1067
    • Yamamoto, M.1    Yaginuma, K.2    Tsutsui, H.3    Sagara, J.4    Guan, X.5    Seki, E.6
  • 64
    • 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
  • 65
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe B, Kajava AV. The leucine-rich repeat as a protein recognition motif. Curr Opin Struct Biol 2001; 11: 725-732.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 66
    • 0036745064 scopus 로고    scopus 로고
    • Association of mutations in the NALP3/CIAS1/PYPAF1 gene with a broad phenotype including recurrent fever, cold sensitivity, sensorineural deafness, and AA amyloidosis
    • Aganna E, Martinon F, Hawkins PN, Ross JB, Swan DC, Booth DR et al. Association of mutations in the NALP3/CIAS1/PYPAF1 gene with a broad phenotype including recurrent fever, cold sensitivity, sensorineural deafness, and AA amyloidosis. Arthritis Rheum 2002; 46: 2445-2452.
    • (2002) Arthritis Rheum , vol.46 , pp. 2445-2452
    • Aganna, E.1    Martinon, F.2    Hawkins, P.N.3    Ross, J.B.4    Swan, D.C.5    Booth, D.R.6
  • 67
    • 0346350694 scopus 로고    scopus 로고
    • Cutting edge: CIAS1/cryopyrin/PYPAF1/NALP3/CATERPILLER 1.1 is an inducible inflammatory mediator with NF-kappa B suppressive properties
    • O'Connor Jr W, Harton JA, Zhu X, Linhoff MW, Ting JP. Cutting edge: CIAS1/cryopyrin/PYPAF1/NALP3/CATERPILLER 1.1 is an inducible inflammatory mediator with NF-kappa B suppressive properties. J Immunol 2003; 171: 6329-6333.
    • (2003) J Immunol , vol.171 , pp. 6329-6333
    • O'Connor Jr., W.1    Harton, J.A.2    Zhu, X.3    Linhoff, M.W.4    Ting, J.P.5
  • 68
    • 0036275479 scopus 로고    scopus 로고
    • Evolution of ribonuclease inhibitor by exon duplication
    • Haigis MC, Haag ES, Raines RT. Evolution of ribonuclease inhibitor by exon duplication. Mol Biol Evol 2002; 19: 959-963.
    • (2002) Mol Biol Evol , vol.19 , pp. 959-963
    • Haigis, M.C.1    Haag, E.S.2    Raines, R.T.3
  • 70
    • 32944479048 scopus 로고    scopus 로고
    • Host-microbe interactions: Shaping the evolution of the plant immune response
    • Chisholm ST, Coaker G, Day B, Staskawicz BJ. Host-microbe interactions: shaping the evolution of the plant immune response. Cell 2006; 124: 803-814.
    • (2006) Cell , vol.124 , pp. 803-814
    • Chisholm, S.T.1    Coaker, G.2    Day, B.3    Staskawicz, B.J.4
  • 71
    • 0037290889 scopus 로고    scopus 로고
    • Resistance gene signaling in plants - Complex similarities to animal innate immunity
    • Holt III BF, Hubert DA, Dangl JL. Resistance gene signaling in plants - complex similarities to animal innate immunity. Curr Opin Immunol 2003; 15: 20-25.
    • (2003) Curr Opin Immunol , vol.15 , pp. 20-25
    • Holt III, B.F.1    Hubert, D.A.2    Dangl, J.L.3
  • 74
    • 0034192082 scopus 로고    scopus 로고
    • Kinetics and mechanism of ATP-dependent IL-1 beta release from microglial cells
    • Sanz JM, Di Virgilio F. Kinetics and mechanism of ATP-dependent IL-1 beta release from microglial cells. J Immunol 2000; 164: 4893-4898.
    • (2000) J Immunol , vol.164 , pp. 4893-4898
    • Sanz, J.M.1    Di Virgilio, F.2
  • 75
    • 0034667943 scopus 로고    scopus 로고
    • ATP acts as an agonist to promote stimulus-induced secretion of IL-1 beta and IL-18 in human blood
    • Perregaux DG, McNiff P, Laliberte R, Conklyn M, Gabel CA. ATP acts as an agonist to promote stimulus-induced secretion of IL-1 beta and IL-18 in human blood. J Immunol 2000; 165: 4615-4623.
    • (2000) J Immunol , vol.165 , pp. 4615-4623
    • Perregaux, D.G.1    McNiff, P.2    Laliberte, R.3    Conklyn, M.4    Gabel, C.A.5
  • 76
    • 0032532942 scopus 로고    scopus 로고
    • Blockade of human P2X7 receptor function with a monoclonal antibody
    • Buell G, Chessell IP, Michel AD, Collo G, Salazzo M, Herren S et al. Blockade of human P2X7 receptor function with a monoclonal antibody. Blood 1998; 92: 3521-3528.
    • (1998) Blood , vol.92 , pp. 3521-3528
    • Buell, G.1    Chessell, I.P.2    Michel, A.D.3    Collo, G.4    Salazzo, M.5    Herren, S.6
  • 77
    • 0037096207 scopus 로고    scopus 로고
    • Absence of the P2X7 receptor alters leukocyte function and attenuates an inflammatory response
    • Labasi JM, Petrushova N, Donovan C, McCurdy S, Lira P, Payette MM et al. Absence of the P2X7 receptor alters leukocyte function and attenuates an inflammatory response. J Immunol 2002; 168: 6436-6445.
    • (2002) J Immunol , vol.168 , pp. 6436-6445
    • Labasi, J.M.1    Petrushova, N.2    Donovan, C.3    McCurdy, S.4    Lira, P.5    Payette, M.M.6
  • 79
    • 1942422683 scopus 로고    scopus 로고
    • Mechanisms of caspase-1 activation by P2X7 receptor-mediated K+ release
    • Kahlenberg JM, Dubyak GR. Mechanisms of caspase-1 activation by P2X7 receptor-mediated K+ release. Am J Physiol Cell Physiol 2004; 286: C1100-1108.
    • (2004) Am J Physiol Cell Physiol , vol.286
    • Kahlenberg, J.M.1    Dubyak, G.R.2
  • 80
    • 3142654767 scopus 로고    scopus 로고
    • Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf
    • Mariathasan S, Newton K, Monack DM, Vucic D, French DM, Lee WP 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    Newton, K.2    Monack, D.M.3    Vucic, D.4    French, D.M.5    Lee, W.P.6
  • 82
    • 32944468985 scopus 로고    scopus 로고
    • Gout-associated uric acid crystals activate the NALP3 inflammasome
    • Martinon F, Petrilli V, Mayor A, Tardivel A, Tschopp J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 20D6; 440: 237-241.
    • (2006) Nature , vol.440 , pp. 237-241
    • Martinon, F.1    Petrilli, V.2    Mayor, A.3    Tardivel, A.4    Tschopp, J.5
  • 83
    • 33644985564 scopus 로고    scopus 로고
    • Critical role for NALP3/CIAS1/Cryopyrin in innate and adaptive immunity through its regulation of caspase-1
    • Sutterwala FS, Ogura Y, Szczepanik M, Lara-Tejero M, Lichtenberger GS, Grant EP et al. Critical role for NALP3/CIAS1/Cryopyrin in innate and adaptive immunity through its regulation of caspase-1. Immunity 2006; 24: 317-327.
    • (2006) Immunity , vol.24 , pp. 317-327
    • Sutterwala, F.S.1    Ogura, Y.2    Szczepanik, M.3    Lara-Tejero, M.4    Lichtenberger, G.S.5    Grant, E.P.6
  • 84
    • 32944462834 scopus 로고    scopus 로고
    • Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3
    • Kanneganti TD, Ozoren N, Body-Malapel M, Amer A, Park JH, Franchi L et al. Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3. Nature 2006; 440: 233-236.
    • (2006) Nature , vol.440 , pp. 233-236
    • Kanneganti, T.D.1    Ozoren, N.2    Body-Malapel, M.3    Amer, A.4    Park, J.H.5    Franchi, L.6
  • 85
    • 33646017449 scopus 로고    scopus 로고
    • Distinct roles of TLR2 and the adaptor ASC in IL-1beta/IL-18 secretion in response to Listeria monocytogenes
    • Ozoren N, Masumoto J, Franchi L, Kanneganti TD, Body-Malapel M, Erturk I et al. Distinct roles of TLR2 and the adaptor ASC in IL-1beta/IL-18 secretion in response to Listeria monocytogenes. J Immunol 2006; 176: 4337-4342.
    • (2006) J Immunol , vol.176 , pp. 4337-4342
    • Ozoren, N.1    Masumoto, J.2    Franchi, L.3    Kanneganti, T.D.4    Body-Malapel, M.5    Erturk, I.6
  • 86
    • 18344385660 scopus 로고    scopus 로고
    • New mutations of CIAS1 that are responsible for Muckle-Wells syndrome and familial cold urticaria: A novel mutation underlies both syndromes
    • Dode C, Le Du N, Cuisset L, Letourneur F, Berthelot JM, Vaudour G et al. New mutations of CIAS1 that are responsible for Muckle-Wells syndrome and familial cold urticaria: A novel mutation underlies both syndromes. Am J Hum Genet 2002; 70: 1498-1506.
    • (2002) Am J Hum Genet , vol.70 , pp. 1498-1506
    • Dode, C.1    Le Du, N.2    Cuisset, L.3    Letourneur, F.4    Berthelot, J.M.5    Vaudour, G.6
  • 87
    • 0035179970 scopus 로고    scopus 로고
    • Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome
    • Hoffman HM, Mueller JL, Broide DH, Wanderer AA, Kolodner RD. Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome. Nat Genet 2001; 29: 301-305.
    • (2001) Nat Genet , vol.29 , pp. 301-305
    • Hoffman, H.M.1    Mueller, J.L.2    Broide, D.H.3    Wanderer, A.A.4    Kolodner, R.D.5
  • 88
    • 0037792866 scopus 로고    scopus 로고
    • Interleukin-1-receptor antagonist in the Muckle-Wells syndrome
    • Hawkins PN, Lachmann HJ, McDermott MF. Interleukin-1-receptor antagonist in the Muckle-Wells syndrome. N Engl J Med 2003; 346: 2583-2584.
    • (2003) N Engl J Med , vol.346 , pp. 2583-2584
    • Hawkins, P.N.1    Lachmann, H.J.2    McDermott, M.F.3
  • 89
    • 8444225132 scopus 로고    scopus 로고
    • Prevention of cold-associated acute inflammation in familial cold autoinflammatory syndrome by interleukin-1 receptor antagonist
    • Hoffman HM, Rosengren S, Boyle DL, Cho JY, Nayar J, Mueller JL et al. Prevention of cold-associated acute inflammation in familial cold autoinflammatory syndrome by interleukin-1 receptor antagonist. Lancet 2004; 364: 1779-1785.
    • (2004) Lancet , vol.364 , pp. 1779-1785
    • Hoffman, H.M.1    Rosengren, S.2    Boyle, D.L.3    Cho, J.Y.4    Nayar, J.5    Mueller, J.L.6
  • 90
    • 32344438251 scopus 로고    scopus 로고
    • Plasma interleukin (IL)-18 (interferon-gamma-inducing factor) and other inflammatory cytokines in patients with gouty arthritis and monosodium urate monohydrate crystal-induced secretion of IL-18
    • Inokuchi T, Moriwaki Y, Tsutsui H, Yamamoto A, Takahashi S, Tsutsumi Z et al. Plasma interleukin (IL)-18 (interferon-gamma-inducing factor) and other inflammatory cytokines in patients with gouty arthritis and monosodium urate monohydrate crystal-induced secretion of IL-18. Cytokine 2006; 33: 21-27.
    • (2006) Cytokine , vol.33 , pp. 21-27
    • Inokuchi, T.1    Moriwaki, Y.2    Tsutsui, H.3    Yamamoto, A.4    Takahashi, S.5    Tsutsumi, Z.6
  • 91
    • 0035869399 scopus 로고    scopus 로고
    • Functional caspase-1 is required for Langerhans cell migration and optimal contact sensitization in mice
    • Antonopoulos C, Cumberbatch M, Dearman RJ, Daniel RJ, Kimber I, Groves RW. Functional caspase-1 is required for Langerhans cell migration and optimal contact sensitization in mice. J Immunol 2001; 166: 3672-3677.
    • (2001) J Immunol , vol.166 , pp. 3672-3677
    • Antonopoulos, C.1    Cumberbatch, M.2    Dearman, R.J.3    Daniel, R.J.4    Kimber, I.5    Groves, R.W.6
  • 93
    • 25644454243 scopus 로고    scopus 로고
    • Release of IL-1beta via IL-1beta-converting enzyme in a skin dendritic cell line exposed to 2,4-dinitrofluorobenzene
    • Matos TJ, Jaleco SP, Goncalo M, Duarte CB, Lopes MC. Release of IL-1beta via IL-1beta-converting enzyme in a skin dendritic cell line exposed to 2,4-dinitrofluorobenzene. Mediators Inflamm 2005; 2005: 131-138.
    • (2005) Mediators Inflamm , vol.2005 , pp. 131-138
    • Matos, T.J.1    Jaleco, S.P.2    Goncalo, M.3    Duarte, C.B.4    Lopes, M.C.5
  • 94
    • 0345735833 scopus 로고    scopus 로고
    • Salmonella rapidly kill dendritic cells via a caspase-1-dependent mechanism
    • van der Velden AW, Velasquez M, Stambach MN. Salmonella rapidly kill dendritic cells via a caspase-1-dependent mechanism. J Immunol 2003; 171: 6742-6749.
    • (2003) J Immunol , vol.171 , pp. 6742-6749
    • van der Velden, A.W.1    Velasquez, M.2    Stambach, M.N.3
  • 96
    • 26844452231 scopus 로고    scopus 로고
    • Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis
    • Mariathasan S, Weiss DS, Dixit VM, Monack DM. Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis. J Exp Med 2005; 202: 1043-1049.
    • (2005) J Exp Med , vol.202 , pp. 1043-1049
    • Mariathasan, S.1    Weiss, D.S.2    Dixit, V.M.3    Monack, D.M.4
  • 97
    • 30444455439 scopus 로고    scopus 로고
    • Internalization and phagosome escape required for Francisella to induce human monocyte IL-1 beta processing and release
    • Gavrilin MA, Bouakl IJ, Knatz NL, Duncan MD, Hall MW, Gunn JS et al. Internalization and phagosome escape required for Francisella to induce human monocyte IL-1 beta processing and release. Proc Natl Acad Sci USA 2006; 103: 141-146.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 141-146
    • Gavrilin, M.A.1    Bouakl, I.J.2    Knatz, N.L.3    Duncan, M.D.4    Hall, M.W.5    Gunn, J.S.6
  • 98
    • 2442701424 scopus 로고    scopus 로고
    • Anthrax lethal toxin rapidly activates caspase-1/ACE and induces extracellular release of interleukin (IL)-1beta and IL-18
    • Cordoba-Rodriguez R, Fang H, Lankford CS, Frucht DM. Anthrax lethal toxin rapidly activates caspase-1/ACE and induces extracellular release of interleukin (IL)-1beta and IL-18. J Biol Chem 2004; 279: 20563-20566.
    • (2004) J Biol Chem , vol.279 , pp. 20563-20566
    • Cordoba-Rodriguez, R.1    Fang, H.2    Lankford, C.S.3    Frucht, D.M.4
  • 99
    • 31744441475 scopus 로고    scopus 로고
    • Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin
    • Boyden ED, Dietrich WF. Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nat Genet 2006; 38: 240-244.
    • (2006) Nat Genet , vol.38 , pp. 240-244
    • Boyden, E.D.1    Dietrich, W.F.2
  • 100
    • 33744464740 scopus 로고    scopus 로고
    • Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1beta in salmonella-infected macrophages
    • Franchi L, Amer A, Body-Malapel M, Kanneganti TD, Ozoren N, Jagirdar R et al. Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1beta in salmonella-infected macrophages. Nat Immunol 2006; 7: 576-582.
    • (2006) Nat Immunol , vol.7 , pp. 576-582
    • Franchi, L.1    Amer, A.2    Body-Malapel, M.3    Kanneganti, T.D.4    Ozoren, N.5    Jagirdar, R.6
  • 102
    • 33645843633 scopus 로고    scopus 로고
    • Cytosolic recognition of flagellin by mouse macrophages restricts Legionella pneumophila infection
    • Molofsky AB, Byrne BG, Whitfield NN, Madigan CA, Fuse ET, Tateda K et al. Cytosolic recognition of flagellin by mouse macrophages restricts Legionella pneumophila infection. J Exp Med 2006; 203: 1093-1104.
    • (2006) J Exp Med , vol.203 , pp. 1093-1104
    • Molofsky, A.B.1    Byrne, B.G.2    Whitfield, N.N.3    Madigan, C.A.4    Fuse, E.T.5    Tateda, K.6
  • 103
    • 33645791082 scopus 로고    scopus 로고
    • Flagellin-deficient Legionella mutants evade caspase-1- and Naip5-mediated macrophage immunity
    • Ran T, Zamboni DS, Roy CH, Dietrich WF, Vance RE. Flagellin-deficient Legionella mutants evade caspase-1- and Naip5-mediated macrophage immunity. PLoS Pathol 2006; 2: E18.
    • (2006) PLoS Pathol , vol.2
    • Ran, T.1    Zamboni, D.S.2    Roy, C.H.3    Dietrich, W.F.4    Vance, R.E.5
  • 104
    • 21244460672 scopus 로고    scopus 로고
    • Naip5/Birc1e and susceptibility to Legionella pneumophila
    • Fortier A, Diez E, Gros P. Naip5/Birc1e and susceptibility to Legionella pneumophila. Trends Microbiol 2005; 13: 328-335.
    • (2005) Trends Microbiol , vol.13 , pp. 328-335
    • Fortier, A.1    Diez, E.2    Gros, P.3
  • 105
    • 0033757582 scopus 로고    scopus 로고
    • Mater, a maternal effect gene required for early embryonic development in mice
    • Tong ZB, Gold L, Pfeifer KE, Dorward H, Lee E, Bondy CA et al. Mater, a maternal effect gene required for early embryonic development in mice. Nat Genet 2000; 26: 267-268.
    • (2000) Nat Genet , vol.26 , pp. 267-268
    • Tong, Z.B.1    Gold, L.2    Pfeifer, K.E.3    Dorward, H.4    Lee, E.5    Bondy, C.A.6
  • 106
    • 0036101735 scopus 로고    scopus 로고
    • A human homologue of mouse Mater, a maternal effect gene essential for early embryonic development
    • Tong ZB, Bondy CA, Zhou J, Nelson LM. A human homologue of mouse Mater, a maternal effect gene essential for early embryonic development. Hum Reprod 2002; 17: 903-911.
    • (2002) Hum Reprod , vol.17 , pp. 903-911
    • Tong, Z.B.1    Bondy, C.A.2    Zhou, J.3    Nelson, L.M.4
  • 107
    • 5144227778 scopus 로고    scopus 로고
    • In silico identification and structural features of six new genes similar to MATER specifically expressed in the oocyte
    • Dade S, Callebaut I, Paillisson A, Bontoux M, Dalbies-Tran R, Monget P. In silico identification and structural features of six new genes similar to MATER specifically expressed in the oocyte. Biochem Biophys Res Commun 2004; 324: 547-553.
    • (2004) Biochem Biophys Res Commun , vol.324 , pp. 547-553
    • Dade, S.1    Callebaut, I.2    Paillisson, A.3    Bontoux, M.4    Dalbies-Tran, R.5    Monget, P.6
  • 109
    • 33144485255 scopus 로고    scopus 로고
    • Bovine NALP5, NALP8, and NALP9 genes: Assignment to a QTL region and the expression in adult tissues, oocytes, and preimplantation embryos
    • Ponsuksili S, Brunner RM, Goldammer T, Kuhn C, Walz C, Chomdej S et al. Bovine NALP5, NALP8, and NALP9 genes: Assignment to a QTL region and the expression in adult tissues, oocytes, and preimplantation embryos. Biol Reprod 2006; 74: 577-584.
    • (2006) Biol Reprod , vol.74 , pp. 577-584
    • Ponsuksili, S.1    Brunner, R.M.2    Goldammer, T.3    Kuhn, C.4    Walz, C.5    Chomdej, S.6
  • 111
    • 15544379483 scopus 로고    scopus 로고
    • The mouse germ-cell-specific leucine-rich repeat protein NALP14: A member of the NACHT nucleoside triphosphatase family
    • Horikawa M, Kirkman NJ, Mayo KE, Mulders SM, Zhou J, Bondy CA et al. The mouse germ-cell-specific leucine-rich repeat protein NALP14: A member of the NACHT nucleoside triphosphatase family. Biol Reprod 2005; 72: 879-889.
    • (2005) Biol Reprod , vol.72 , pp. 879-889
    • Horikawa, M.1    Kirkman, N.J.2    Mayo, K.E.3    Mulders, S.M.4    Zhou, J.5    Bondy, C.A.6
  • 112
    • 0036681550 scopus 로고    scopus 로고
    • Interacting quantitative trait loci control loss of peripheral tolerance and susceptibility to autoimmune ovarian dysgenesis after day 3 thymectomy in mice
    • Roper RJ, Ma RZ, Biggins JE, Butterfield RJ, Michael SD, Tung KS et al. Interacting quantitative trait loci control loss of peripheral tolerance and susceptibility to autoimmune ovarian dysgenesis after day 3 thymectomy in mice. J Immunol 2002; 169: 1640-1646.
    • (2002) J Immunol , vol.169 , pp. 1640-1646
    • Roper, R.J.1    Ma, R.Z.2    Biggins, J.E.3    Butterfield, R.J.4    Michael, S.D.5    Tung, K.S.6
  • 113
    • 33644615366 scopus 로고    scopus 로고
    • Mutations in NALP7 cause recurrent hydatidiform moles and reproductive wastage in humans
    • Murdoch S, Djuric U, Mazhar B, Seoud M, Khan R, Kuick R et al. Mutations in NALP7 cause recurrent hydatidiform moles and reproductive wastage in humans. Nat Genet 2006; 38: 300-302.
    • (2006) Nat Genet , vol.38 , pp. 300-302
    • Murdoch, S.1    Djuric, U.2    Mazhar, B.3    Seoud, M.4    Khan, R.5    Kuick, R.6
  • 115
    • 27344460591 scopus 로고    scopus 로고
    • In vivo effect of interleukin-1beta and interleukin-1RA on oocyte cytoplasmic maturation, ovulation, and early embryonic development in the mare
    • Caillaud M, Duchamp G, Gerard N. In vivo effect of interleukin-1beta and interleukin-1RA on oocyte cytoplasmic maturation, ovulation, and early embryonic development in the mare. Reprod Biol Endocrinol 2005; 22: 3:26.
    • (2005) Reprod Biol Endocrinol , vol.22 , Issue.3 , pp. 26
    • Caillaud, M.1    Duchamp, G.2    Gerard, N.3
  • 116
    • 0028180757 scopus 로고
    • Effect of interleukin-1 beta on ovulation in the in vitro perfused rabbit ovary
    • Takehara Y, Dharmarajan AM, Kaufman G, Wallach EE. Effect of interleukin-1 beta on ovulation in the in vitro perfused rabbit ovary. Endocrinology 1994; 134: 1788-1793.
    • (1994) Endocrinology , vol.134 , pp. 1788-1793
    • Takehara, Y.1    Dharmarajan, A.M.2    Kaufman, G.3    Wallach, E.E.4
  • 117
    • 33646560323 scopus 로고    scopus 로고
    • Promoter mutations of an essential gene for pollen development result in disease resistance in rice
    • Chu Z, Yuan M, Yao J, Ge X, Yuan B, Xu C et al. Promoter mutations of an essential gene for pollen development result in disease resistance in rice. Genes Dev 2006; 20: 1250-1255.
    • (2006) Genes Dev , vol.20 , pp. 1250-1255
    • Chu, Z.1    Yuan, M.2    Yao, J.3    Ge, X.4    Yuan, B.5    Xu, C.6
  • 118
    • 0036085807 scopus 로고    scopus 로고
    • An evolutionarily conserved mediator of plant disease resistance gone function is required for normal Arabidopsis development
    • Holt 3rd BF, Boyes DC, Ellerstrom M, Siefers N, Wiig A, Kauffman S et al. An evolutionarily conserved mediator of plant disease resistance gone function is required for normal Arabidopsis development. Dev Cell 2002; 2: 807-817.
    • (2002) Dev Cell , vol.2 , pp. 807-817
    • Holt III, B.F.1    Boyes, D.C.2    Ellerstrom, M.3    Siefers, N.4    Wiig, A.5    Kauffman, S.6
  • 120
    • 0035860780 scopus 로고    scopus 로고
    • Cop, a caspase recruitment domain-containing protein and inhibitor of caspase-1 activation processing
    • Lee SH, Stehlik C, Reed JC. Cop, a caspase recruitment domain-containing protein and inhibitor of caspase-1 activation processing. J Biol Chem 2001; 276: 34495-34500.
    • (2001) J Biol Chem , vol.276 , pp. 34495-34500
    • Lee, S.H.1    Stehlik, C.2    Reed, J.C.3
  • 121
    • 0034743434 scopus 로고    scopus 로고
    • Regulation of IL-1beta generation by Pseudo-ICE and ICEBERG, two dominant negative caspase recruitment domain proteins
    • Druilhe A, Srinivasula SM, Razmara M, Ahmad M, Alnemri ES. Regulation of IL-1beta generation by Pseudo-ICE and ICEBERG, two dominant negative caspase recruitment domain proteins. Cell Death Differ 2001; 8: 649-657.
    • (2001) Cell Death Differ , vol.8 , pp. 649-657
    • Druilhe, A.1    Srinivasula, S.M.2    Razmara, M.3    Ahmad, M.4    Alnemri, E.S.5
  • 122
    • 10644270650 scopus 로고    scopus 로고
    • INCA, a novel human caspase recruitment domain protein that inhibits interleukin-1beta generation
    • Lamkanfi M, Denecker G, Kalai M, D'Hondt K, Meeus A, Declercq W et al. INCA, a novel human caspase recruitment domain protein that inhibits interleukin-1beta generation. J Biol Chem 2004; 279: 51729-51738.
    • (2004) J Biol Chem , vol.279 , pp. 51729-51738
    • Lamkanfi, M.1    Denecker, G.2    Kalai, M.3    D'Hondt, K.4    Meeus, A.5    Declercq, W.6
  • 123
    • 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 (Part 1): 101-113.
    • (2003) Biochem J , vol.373 , Issue.PART 1 , pp. 101-113
    • Stehlik, C.1    Krajewska, M.2    Welsh, K.3    Krajewski, S.4    Godzik, A.5    Reed, J.C.6
  • 124
    • 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, Barrett JW, Nazarian SH, Goodwin M, Ricuttio D, Wang G 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    Barrett, J.W.2    Nazarian, S.H.3    Goodwin, M.4    Ricuttio, D.5    Wang, G.6
  • 125
    • 28844437999 scopus 로고    scopus 로고
    • Poxviruses aren't stuPYD
    • Benedict CA, Ware CF. Poxviruses aren't stuPYD. Immunity 2005; 23: 553-555.
    • (2005) Immunity , vol.23 , pp. 553-555
    • Benedict, C.A.1    Ware, C.F.2
  • 126
    • 0032522593 scopus 로고    scopus 로고
    • Familial Mediterranean fever: The genetics of inflammation
    • Kastner DL. Familial Mediterranean fever: The genetics of inflammation. Hosp Pract (Minneapolis) 1998; 33: 131-146.
    • (1998) Hosp Pract (Minneapolis) , vol.33 , pp. 131-146
    • Kastner, D.L.1
  • 127
    • 0037349294 scopus 로고    scopus 로고
    • Targeted disruption of pyrin, the FMF protein, causes heightened sensitivity to endotoxin and a defect in macrophage apoptosis
    • Chae JJ, Komarow HD, Cheng J, Wood G, Raben N, Liu PP et al. Targeted disruption of pyrin, the FMF protein, causes heightened sensitivity to endotoxin and a defect in macrophage apoptosis. Mol Cell 2003; 11: 591-604.
    • (2003) Mol Cell , vol.11 , pp. 591-604
    • Chae, J.J.1    Komarow, H.D.2    Cheng, J.3    Wood, G.4    Raben, N.5    Liu, P.P.6
  • 128
  • 129
    • 33344476398 scopus 로고    scopus 로고
    • CATERPILLERs, pyrin and hereditary immunological disorders
    • Ting JP, Kastner DL, Hoffman HM. CATERPILLERs, pyrin and hereditary immunological disorders. Nat Rev Immunol 2006; 6: 183-195.
    • (2006) Nat Rev Immunol , vol.6 , pp. 183-195
    • Ting, J.P.1    Kastner, D.L.2    Hoffman, H.M.3
  • 130
    • 33749587661 scopus 로고    scopus 로고
    • The estrogen-responsive B box protein: A novel enhancer of interleukin-1beta secretion
    • (in press, doi: 10.1038/sj.cdd.4401896)
    • Munding C, Keller M, Niklaus G, Papin S, Tschopp J, Werner S et al. The estrogen-responsive B box protein: A novel enhancer of interleukin-1beta secretion. Cell Death Differ 2006; 31 (in press, doi: 10.1038/ sj.cdd.4401896).
    • (2006) Cell Death Differ , vol.31
    • Munding, C.1    Keller, M.2    Niklaus, G.3    Papin, S.4    Tschopp, J.5    Werner, S.6
  • 131
    • 29344469557 scopus 로고    scopus 로고
    • Structure of the PRYSPRY-domain: Implications for autoinflammatory diseases
    • Grutter C, Briand C, Capitani G, Mittl PR, Papin S, Tschopp J et al. Structure of the PRYSPRY-domain: Implications for autoinflammatory diseases. FEBS Lett 2006; 580: 99-106.
    • (2006) FEBS Lett , vol.580 , pp. 99-106
    • Grutter, C.1    Briand, C.2    Capitani, G.3    Mittl, P.R.4    Papin, S.5    Tschopp, J.6
  • 132
    • 30844432876 scopus 로고    scopus 로고
    • Cryopyrin and pyrin activate caspase-1, but not NF-kappaB, via ASC oligomerization
    • Yu JW, Wu J, Zhang Z, Datta P, Ibrahimi I, Taniguchi S et al. Cryopyrin and pyrin activate caspase-1, but not NF-kappaB, via ASC oligomerization. Cell Death Differ 2006; 13: 236-249.
    • (2006) Cell Death Differ , vol.13 , pp. 236-249
    • Yu, J.W.1    Wu, J.2    Zhang, Z.3    Datta, P.4    Ibrahimi, I.5    Taniguchi, S.6
  • 133
    • 0034091243 scopus 로고    scopus 로고
    • Higher than expected carrier rates for familial Mediterranean fever in various Jewish ethnic groups
    • Stoffman N, Magal N, Shohat T, Lotan R, Koman S, Oron A et al. Higher than expected carrier rates for familial Mediterranean fever in various Jewish ethnic groups. Eur J Hum Genet 2000; 8: 307-310.
    • (2000) Eur J Hum Genet , vol.8 , pp. 307-310
    • Stoffman, N.1    Magal, N.2    Shohat, T.3    Lotan, R.4    Koman, S.5    Oron, A.6
  • 134
    • 18244429610 scopus 로고    scopus 로고
    • Mutation and haplotype studies of familial Mediterranean fever reveal new ancestral relationships and evidence for a high carrier frequency with reduced penetrance in the Ashkenazi Jewish population
    • Aksentijevich I, Torosyan Y, Samuels J, Centola M, Pras E, Chae JJ et al. Mutation and haplotype studies of familial Mediterranean fever reveal new ancestral relationships and evidence for a high carrier frequency with reduced penetrance in the Ashkenazi Jewish population. Am J Hum Genet 1999; 64: 949-962.
    • (1999) Am J Hum Genet , vol.64 , pp. 949-962
    • Aksentijevich, I.1    Torosyan, Y.2    Samuels, J.3    Centola, M.4    Pras, E.5    Chae, J.J.6
  • 135
    • 0035091156 scopus 로고    scopus 로고
    • Episodic evolution of pyrin in primates: Human mutations recapitulate ancestral amino acid states
    • Schaner P, Richards N, Wadhwa A, Aksentijevich I, Kastner D, Tucker P et al. Episodic evolution of pyrin in primates: Human mutations recapitulate ancestral amino acid states. Nat Genet 2001; 27: 318-3211.
    • (2001) Nat Genet , vol.27 , pp. 318-321
    • Schaner, P.1    Richards, N.2    Wadhwa, A.3    Aksentijevich, I.4    Kastner, D.5    Tucker, P.6
  • 136
    • 0344823965 scopus 로고    scopus 로고
    • Pyrin binds the PSTPIP1/CD2BP1 protein, defining familial Mediterranean fever and PAPA syndrome as disorders in the same pathway
    • Shoham NG, Centola M, Mansfield E, Hull KM, Wood G, Wise CA et al. Pyrin binds the PSTPIP1/CD2BP1 protein, defining familial Mediterranean fever and PAPA syndrome as disorders in the same pathway. Proc Natl Acad Sci USA 2003; 100: 13501-13506.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13501-13506
    • Shoham, N.G.1    Centola, M.2    Mansfield, E.3    Hull, K.M.4    Wood, G.5    Wise, C.A.6
  • 137
    • 33645734214 scopus 로고    scopus 로고
    • Mutation of mouse Mayp/Pstpip2 causes a macrophage autoinflammatory disease
    • Grosse J, Chitu V, Marquardt A, Hanke P, Schmittwolf C, Zeitlmann L et al. Mutation of mouse Mayp/Pstpip2 causes a macrophage autoinflammatory disease. Blood 2006; 107: 3350-3358.
    • (2006) Blood , vol.107 , pp. 3350-3358
    • Grosse, J.1    Chitu, V.2    Marquardt, A.3    Hanke, P.4    Schmittwolf, C.5    Zeitlmann, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.