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Volumn 20, Issue 1, 2014, Pages 108-124

Inflammasome and atherogenesis

Author keywords

Atherosclerosis; Atherosgenesis; Autophagy; Caspase; Inflammasome

Indexed keywords

CASPASE 10; CASPASE 2; CASPASE 5; CASPASE 8; CASPASE RECRUITMENT DOMAIN PROTEIN 15; CASPASE RECRUITMENT DOMAIN PROTEIN 4; CRYOPYRIN; FAS ANTIGEN; FAS ASSOCIATED DEATH DOMAIN PROTEIN; IMIQUIMOD; INFLAMMASOME; INTERLEUKIN 1BETA CONVERTING ENZYME; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; PROTEIN ZO1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; RETINOIC ACID INDUCIBLE PROTEIN I; STEROL REGULATORY ELEMENT BINDING PROTEIN 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED DEATH DOMAIN PROTEIN; CELL RECEPTOR;

EID: 84907028666     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/13816128113199990586     Document Type: Article
Times cited : (26)

References (177)
  • 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: 417-26.
    • (2002) Mol Cell , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 2
  • 3
    • 58149287750 scopus 로고    scopus 로고
    • Targeted peptidecentric proteomics reveals caspase-7 as a substrate of the caspase-1 inflammasomes
    • Lamkanfi M, Kanneganti TD, Van Damme P, et al. Targeted peptidecentric proteomics reveals caspase-7 as a substrate of the caspase-1 inflammasomes. Mol Cell Proteomics 2008; 7: 2350-63.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 2350-2363
    • Lamkanfi, M.1    Kanneganti, T.D.2    Van Damme, P.3
  • 4
    • 33748598700 scopus 로고    scopus 로고
    • Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
    • Gurcel L, Abrami L, Girardin S, Tschopp J, van der Goot FG. Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival. Cell 2006; 126: 1135-45.
    • (2006) Cell , vol.126 , pp. 1135-1145
    • Gurcel, L.1    Abrami, L.2    Girardin, S.3    Tschopp, J.4    Van Der Goot, F.G.5
  • 5
    • 39749084641 scopus 로고    scopus 로고
    • Active caspase-1 is a regulator of unconventional protein secretion
    • Keller M, Rüegg A, Werner S, Beer HD. Active caspase-1 is a regulator of unconventional protein secretion. Cell 2008; 132: 818-31.
    • (2008) Cell , vol.132 , pp. 818-831
    • Keller, M.1    Rüegg, A.2    Werner, S.3    Beer, H.D.4
  • 6
    • 84867861468 scopus 로고    scopus 로고
    • Phosphorylation of NLRC4 is critical for inflammasome activation
    • Qu Y, Misaghi S, Izrael-Tomasevic A, et al. Phosphorylation of NLRC4 is critical for inflammasome activation. Nature 2012; 490: 539-42.
    • (2012) Nature , vol.490 , pp. 539-542
    • Qu, Y.1    Misaghi, S.2    Izrael-Tomasevic, A.3
  • 7
    • 79953315378 scopus 로고    scopus 로고
    • Differential requirements for NAIP5 in activation of the NLRC4 inflammasome
    • Lightfield KL, Persson J, Trinidad NJ, et al. Differential requirements for NAIP5 in activation of the NLRC4 inflammasome. Infect Immun 2011; 79: 1606-14.
    • (2011) Infect Immun , vol.79 , pp. 1606-1614
    • Lightfield, K.L.1    Persson, J.2    Trinidad, N.J.3
  • 8
    • 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 TH, 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: 38460-72.
    • (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.5    Huizinga, E.G.6
  • 9
    • 79951669207 scopus 로고    scopus 로고
    • The immune system in atherosclerosis
    • Hansson GK. & Hermansson A. The immune system in atherosclerosis. Nat Immunol 2011; 12: 204-12.
    • (2011) Nat Immunol , vol.12 , pp. 204-212
    • Hansson, G.K.1    Hermansson, A.2
  • 10
    • 79956319051 scopus 로고    scopus 로고
    • Progress and challenges in translating the biology of atherosclerosis
    • Libby P, Ridker PM, Hansson GK. Progress and challenges in translating the biology of atherosclerosis. Nature 2011; 473: 317-25.
    • (2011) Nature , vol.473 , pp. 317-325
    • Libby, P.1    Ridker, P.M.2    Hansson, G.K.3
  • 11
    • 81255188900 scopus 로고    scopus 로고
    • Atherosclerosis: Current pathogenesis and therapeutic options
    • Weber C, Noels H. Atherosclerosis: Current pathogenesis and therapeutic options. Nat Med 2011; 17: 1410-22.
    • (2011) Nat Med , vol.17 , pp. 1410-1422
    • Weber, C.1    Noels, H.2
  • 12
    • 66149086936 scopus 로고    scopus 로고
    • NOD-like receptors: Role in innate immunity and inflammatory disease
    • Chen G, Shaw MH, Kim YG, Nuñez G. NOD-like receptors: Role in innate immunity and inflammatory disease. Annu Rev Pathol. 2009; 4: 365-98.
    • (2009) Annu Rev Pathol , vol.4 , pp. 365-398
    • Chen, G.1    Shaw, M.H.2    Kim, Y.G.3    Nuñez, G.4
  • 13
    • 0042512008 scopus 로고    scopus 로고
    • Homology modeling provides insights into the binding mode of the PAAD/DAPIN/pyrin domain, a fourth member of the CARD/DD/DED domain family
    • Liu T, Rojas A, Ye Y, Godzik A. Homology modeling provides insights into the binding mode of the PAAD/DAPIN/pyrin domain, a fourth member of the CARD/DD/DED domain family. Protein Sci. 2003; 12: 1872-81.
    • (2003) Protein Sci , vol.12 , pp. 1872-1881
    • Liu, T.1    Rojas, A.2    Ye, Y.3    Godzik, A.4
  • 14
    • 84875445608 scopus 로고    scopus 로고
    • CDD: Conserved domains and protein three-dimensional structure
    • Marchler-Bauer A, Zheng C, Chitsaz F, et al. CDD: Conserved domains and protein three-dimensional structure. Nucleic Acids Res. 2013; 41: D348-52.
    • (2013) Nucleic Acids Res , vol.41 , pp. 348-352
    • Marchler-Bauer, A.1    Zheng, C.2    Chitsaz, F.3
  • 15
    • 0035425256 scopus 로고    scopus 로고
    • The death domain superfamily: A tale of two interfaces?
    • Weber CH, Vincenz C. The death domain superfamily: A tale of two interfaces? Trends Biochem Sci 2001; 26: 475-81.
    • (2001) Trends Biochem Sci , vol.26 , pp. 475-481
    • Weber, C.H.1    Vincenz, C.2
  • 16
    • 0028913550 scopus 로고
    • A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain
    • Boldin MP, Varfolomeev EE, Pancer Z, Mett IL, Camonis JH, Wallach D. A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain. J Biol Chem 1995; 270: 7795-8.
    • (1995) J Biol Chem , vol.270 , pp. 7795-7798
    • Boldin, M.P.1    Varfolomeev, E.E.2    Pancer, Z.3    Mett, I.L.4    Camonis, J.H.5    Wallach, D.6
  • 17
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan AM, O'Rourke K, Tewari M, Dixit VM. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 1995; 81: 505-12.
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 18
    • 10644296258 scopus 로고    scopus 로고
    • The C-terminal tails of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) and Fas receptors have opposing functions in Fasassociated death domain (FADD) recruitment and can regulate agonist-specific mechanisms of receptor activation
    • Thomas LR, Johnson RL, Reed JC, Thorburn A. The C-terminal tails of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) and Fas receptors have opposing functions in Fasassociated death domain (FADD) recruitment and can regulate agonist-specific mechanisms of receptor activation. J Biol Chem 2004; 279: 52479-86.
    • (2004) J Biol Chem , vol.279 , pp. 52479-52486
    • Thomas, L.R.1    Johnson, R.L.2    Reed, J.C.3    Thorburn, A.4
  • 19
    • 78549236456 scopus 로고    scopus 로고
    • The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations
    • Wang L, Yang JK, Kabaleeswaran V, et al. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nat Struct Mol Biol 2010; 17: 1324-9.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1324-1329
    • Wang, L.1    Yang, J.K.2    Kabaleeswaran, V.3
  • 20
    • 60549106191 scopus 로고    scopus 로고
    • The Fas-FADD death domain complex structure unravels signalling by receptor clustering
    • Scott FL, Stec B, Pop C, et al. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. Nature 2009; 457: 1019-22.
    • (2009) Nature , vol.457 , pp. 1019-1022
    • Scott, F.L.1    Stec, B.2    Pop, C.3
  • 21
    • 3543032779 scopus 로고    scopus 로고
    • Direct binding of Fas-associated death domain (FADD) to the tumor necrosis factor-related apoptosis-inducing ligand receptor DR5 is regulated by the death effector domain of FADD
    • Thomas LR, Henson A, Reed JC, Salsbury FR, Thorburn A. Direct binding of Fas-associated death domain (FADD) to the tumor necrosis factor-related apoptosis-inducing ligand receptor DR5 is regulated by the death effector domain of FADD. J Biol Chem 2004; 279: 32780-5.
    • (2004) J Biol Chem , vol.279 , pp. 32780-32785
    • Thomas, L.R.1    Henson, A.2    Reed, J.C.3    Salsbury, F.R.4    Thorburn, A.5
  • 22
    • 33744539048 scopus 로고    scopus 로고
    • The structure of FADD and its mode of interaction with procaspase-8
    • Carrington PE, Sandu C, Wei Y, et al. The structure of FADD and its mode of interaction with procaspase-8. Mol Cell 2006; 22: 599-610.
    • (2006) Mol Cell , vol.22 , pp. 599-610
    • Carrington, P.E.1    Sandu, C.2    Wei, Y.3
  • 23
    • 0033527064 scopus 로고    scopus 로고
    • PED/PEA-15: An antiapoptotic molecule that regulates FAS/TNFR1-induced apoptosis
    • Condorelli G, Vigliotta G, Cafieri A, et al. PED/PEA-15: An antiapoptotic molecule that regulates FAS/TNFR1-induced apoptosis. Oncogene 1999; 18: 4409-15.
    • (1999) Oncogene , vol.18 , pp. 4409-4415
    • Condorelli, G.1    Vigliotta, G.2    Cafieri, A.3
  • 24
    • 25844522837 scopus 로고    scopus 로고
    • Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
    • Renganathan H, Vaidyanathan H, Knapinska A, Ramos JW. Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD. Biochem J 2005; 390: 729-35
    • (2005) Biochem J , vol.390 , pp. 729-735
    • Renganathan, H.1    Vaidyanathan, H.2    Knapinska, A.3    Ramos, J.W.4
  • 25
    • 0037448684 scopus 로고    scopus 로고
    • DEDD and DEDD2 associate with caspase-8/10 and signal cell death
    • Alcivar A, Hu S, Tang J, Yang X. DEDD and DEDD2 associate with caspase-8/10 and signal cell death. Oncogene 2003; 22: 291-7.
    • (2003) Oncogene , vol.22 , pp. 291-297
    • Alcivar, A.1    Hu, S.2    Tang, J.3    Yang, X.4
  • 26
    • 0032580153 scopus 로고    scopus 로고
    • NMR structure and mutagenesis of the FADD (Mort1) death-effector domain
    • Eberstadt M, Huang B, Chen Z, et al. NMR structure and mutagenesis of the FADD (Mort1) death-effector domain. Nature 1998; 392: 941-5.
    • (1998) Nature , vol.392 , pp. 941-945
    • Eberstadt, M.1    Huang, B.2    Chen, Z.3
  • 27
    • 0032910169 scopus 로고    scopus 로고
    • Apoptosis control by death and decoy receptors
    • Ashkenazi A, Dixit VM. Apoptosis control by death and decoy receptors. Curr Opin Cell Biol 1999; 11: 255-60.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 255-260
    • Ashkenazi, A.1    Dixit, V.M.2
  • 29
    • 0027490172 scopus 로고
    • "Complementation cloning of an MHC class II transactivator mutated in hereditary MHC class II deficiency (or bare lymphocyte syndrome"
    • Steimle V, Otten LA, Zufferey M, Mach B. "Complementation cloning of an MHC class II transactivator mutated in hereditary MHC class II deficiency or bare lymphocyte syndrome". Cell 1993; 75: 135-46.
    • (1993) Cell , vol.75 , pp. 135-146
    • Steimle, V.1    Otten, L.A.2    Zufferey, M.3    Mach, B.4
  • 30
    • 0035106263 scopus 로고    scopus 로고
    • Transcriptional coactivator, CIITA, is an acetyltransferase that bypasses a promoter requirement for TAF(II)250
    • Raval A, Howcroft TK, Weissman JD, et al. Transcriptional coactivator, CIITA, is an acetyltransferase that bypasses a promoter requirement for TAF(II)250. Mol Cell 2001; 7: 105-15.
    • (2001) Mol Cell , vol.7 , pp. 105-115
    • Raval, A.1    Howcroft, T.K.2    Weissman, J.D.3
  • 31
    • 40449140937 scopus 로고    scopus 로고
    • The NLR gene family: A standard nomenclature
    • Ting JP, Lovering RC, Alnemri ES, et al. The NLR gene family: A standard nomenclature. Immunity 2008; 28: 285-7.
    • (2008) Immunity , vol.28 , pp. 285-287
    • Ting, J.P.1    Lovering, R.C.2    Alnemri, E.S.3
  • 32
    • 33847376042 scopus 로고    scopus 로고
    • Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation
    • Faustin B, Lartigue L, Bruey JM, et al. Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation. Mol Cell 2007; 25: 713-24.
    • (2007) Mol Cell , vol.25 , pp. 713-724
    • Faustin, B.1    Lartigue, L.2    Bruey, J.M.3
  • 33
    • 27644483812 scopus 로고    scopus 로고
    • A structure of the human apoptosome at 12.8 A resolution provides insights into this cell death platform
    • Yu X, Acehan D, Ménétret JF, et al. A structure of the human apoptosome at 12.8 A resolution provides insights into this cell death platform. Structure 2005; 13: 1725-35.
    • (2005) Structure , vol.13 , pp. 1725-1735
    • Yu, X.1    Acehan, D.2    Ménétret, J.F.3
  • 34
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome. Implications for assembly, procaspase-9 binding, and activation
    • Acehan D, Jiang X, Morgan DG, Heuser JE, Wang X, Akey CW. Three-dimensional structure of the apoptosome. Implications for assembly, procaspase-9 binding, and activation. Mol Cell 2002; 9: 423-32.
    • (2002) Mol Cell , vol.9 , pp. 423-432
    • Acehan, D.1    Jiang, X.2    Morgan, D.G.3    Heuser, J.E.4    Wang, X.5    Akey, C.W.6
  • 35
    • 78651241652 scopus 로고    scopus 로고
    • Structure of the Drosophila apoptosome at 6.9 Å resolution
    • Yuan S, Yu X, Topf M, et al. Structure of the Drosophila apoptosome at 6.9 Å resolution. Structure 1022; 19: 128-40.
    • Structure , vol.19 , pp. 128-140
    • Yuan, S.1    Yu, X.2    Topf, M.3
  • 36
    • 77951881456 scopus 로고    scopus 로고
    • Crystal structure of the Caenorhabditis elegans apoptosome reveals an octameric assembly of CED-4
    • Qi S, Pang Y, Hu Q, et al. Crystal structure of the Caenorhabditis elegans apoptosome reveals an octameric assembly of CED-4. Cell 2010; 41: 446-57.
    • (2010) Cell , vol.41 , pp. 446-457
    • Qi, S.1    Pang, Y.2    Hu, Q.3
  • 37
    • 28944443033 scopus 로고    scopus 로고
    • Three-dimensional structure of a double apoptosome formed by the Drosophila Apaf-1 related killer
    • Yu X, Wang L, Acehan D, Wang X, Akey CW. Three-dimensional structure of a double apoptosome formed by the Drosophila Apaf-1 related killer. J. Mol. Biol. 2006; 355: 577-89.
    • (2006) J. Mol. Biol , vol.355 , pp. 577-589
    • Yu, X.1    Wang, L.2    Acehan, D.3    Wang, X.4    Akey, C.W.5
  • 38
    • 78650321323 scopus 로고    scopus 로고
    • Oxidized low-density lipoprotein and atherosclerosis
    • Steinberg D, Witztum JL. Oxidized low-density lipoprotein and atherosclerosis. Arterioscler Thromb Vasc Biol 2010; 30: 2311-6.
    • (2010) Arterioscler Thromb Vasc Biol , vol.30 , pp. 2311-2316
    • Steinberg, D.1    Witztum, J.L.2
  • 39
    • 79955535643 scopus 로고    scopus 로고
    • Macrophages in the pathogenesis of atherosclerosis
    • Moore KJ, Tabas I. Macrophages in the pathogenesis of atherosclerosis. Cell 2011; 145: 341-55.
    • (2011) Cell , vol.145 , pp. 341-355
    • Moore, K.J.1    Tabas, I.2
  • 40
    • 34247494678 scopus 로고    scopus 로고
    • Elevated levels of interleukin-1beta-converting enzyme and caspase-cleaved cytokeratin-18 in acute myocardial infarction
    • Adlbrecht C, Hoetzenecker K, Posch M, et al. Elevated levels of interleukin-1beta-converting enzyme and caspase-cleaved cytokeratin-18 in acute myocardial infarction. Eur J Clin Invest 2007; 37: 372-80.
    • (2007) Eur J Clin Invest , vol.37 , pp. 372-380
    • Adlbrecht, C.1    Hoetzenecker, K.2    Posch, M.3
  • 41
    • 77951800951 scopus 로고    scopus 로고
    • NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals
    • Duewell P, Kono H, Rayner KJ, et al. NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals. Nature 2010; 464: 1357-61.
    • (2010) Nature , vol.464 , pp. 1357-1361
    • Duewell, P.1    Kono, H.2    Rayner, K.J.3
  • 42
    • 3142654767 scopus 로고    scopus 로고
    • Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf
    • Mariathasan S, Newton K, Monack D, et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 2004; 430: 213-8.
    • (2004) Nature , vol.430 , pp. 213-218
    • Mariathasan, S.1    Newton, K.2    Monack, D.3
  • 43
    • 79956303498 scopus 로고    scopus 로고
    • Regulation of the Antimicrobial Response by NLR Proteins
    • Elinav E, Strowig T, Henao-Mejia J, Flavell RA. Regulation of the Antimicrobial Response by NLR Proteins. Immunity 2011; 34: 665-79.
    • (2011) Immunity , vol.34 , pp. 665-679
    • Elinav, E.1    Strowig, T.2    Henao-Mejia, J.3    Flavell, R.A.4
  • 44
    • 79953046719 scopus 로고    scopus 로고
    • The inflammasome NLRs in immunity, inflammation, and associated diseases
    • Davis BK, Wen H, Ting JP. The inflammasome NLRs in immunity, inflammation, and associated diseases. Annu Rev Immunol 2011; 29: 707-35.
    • (2011) Annu Rev Immunol , vol.29 , pp. 707-735
    • Davis, B.K.1    Wen, H.2    Ting, J.P.3
  • 47
    • 79953219478 scopus 로고    scopus 로고
    • Genetic and molecular basis of inflammasome-mediated disease
    • Hoffman HM, Brydges SD. Genetic and molecular basis of inflammasome-mediated disease. J Biol Chem 2011; 286: 10889-96.
    • (2011) J Biol Chem , vol.286 , pp. 10889-10896
    • Hoffman, H.M.1    Brydges, S.D.2
  • 48
    • 34247574122 scopus 로고    scopus 로고
    • Inflammasome components NALP 1 and 3 show distinct but separate expression profiles in human tissues suggesting a site-specific role in the inflammatory response
    • Kummer JA, Broekhuizen R, Everett H, et al. Inflammasome components NALP 1 and 3 show distinct but separate expression profiles in human tissues suggesting a site-specific role in the inflammatory response. J Histochem Cytochem 2007; 55: 443-52.
    • (2007) J Histochem Cytochem , vol.55 , pp. 443-452
    • Kummer, J.A.1    Broekhuizen, R.2    Everett, H.3
  • 49
    • 84863469984 scopus 로고    scopus 로고
    • Interleukin-1, inflammasomes, autoinflammation and the skin
    • Contassot E, Beer HD, French LE. Interleukin-1, inflammasomes, autoinflammation and the skin. Swiss Med Wkly 2012; 142: W13590
    • (2012) Swiss Med Wkly , vol.142
    • Contassot, E.1    Beer, H.D.2    French, L.E.3
  • 50
    • 58049200723 scopus 로고    scopus 로고
    • Function of Nod-like receptors in microbial recognition and host defense
    • Franchi L, Warner N, Viani K & Nunez G. Function of Nod-like receptors in microbial recognition and host defense. Immunol Rev 2009; 227: 106-18.
    • (2009) Immunol Rev , vol.227 , pp. 106-118
    • Franchi, L.1    Warner, N.2    Viani, K.3    Nunez, G.4
  • 51
    • 58249112754 scopus 로고    scopus 로고
    • Autocrine role of endogenous interleukin-18 on inflammatory cytokine generation by human neutrophils
    • Fortin CF, Ear T, McDonald PP. Autocrine role of endogenous interleukin-18 on inflammatory cytokine generation by human neutrophils. FASEB J 2009; 23: 194-203
    • (2009) FASEB J , vol.23 , pp. 194-203
    • Fortin, C.F.1    Ear, T.2    McDonald, P.P.3
  • 53
    • 0345688077 scopus 로고    scopus 로고
    • Interleukin-18 and the risk of coronary heart disease in European men: The prospective epidemiological study of myocardial infarction (prime)
    • Blankenberg S, Luc G, Ducimetière P, et al. Interleukin-18 and the risk of coronary heart disease in European men: The prospective epidemiological study of myocardial infarction (prime). Circulation 2003; 108: 2453-59.
    • (2003) Circulation , vol.108 , pp. 2453-2459
    • Blankenberg, S.1    Luc, G.2    Ducimetière, P.3
  • 54
    • 84867712592 scopus 로고    scopus 로고
    • Interleukin-18: A potent pro-inflammatory cytokine in atherosclerosis: EXPERT'S PERSPECTIVE
    • Lina Badimon, Interleukin-18: A potent pro-inflammatory cytokine in atherosclerosis: EXPERT'S PERSPECTIVE. Cardiovasc Res 2012; 96: 172-5.
    • (2012) Cardiovasc Res , vol.96 , pp. 172-175
    • Badimon, L.1
  • 56
    • 0033048632 scopus 로고    scopus 로고
    • Cytokine expression in advanced human atherosclerotic plaques: Dominance of proinflammatory (Th1) and macrophage-stimulating cytokines
    • Frostegård J, Ulfgren AK, Nyberg P, et al. Cytokine expression in advanced human atherosclerotic plaques: Dominance of proinflammatory (Th1) and macrophage-stimulating cytokines. Atherosclerosis 1999; 145: 33-43.
    • (1999) Atherosclerosis , vol.145 , pp. 33-43
    • Frostegård, J.1    Ulfgren, A.K.2    Nyberg, P.3
  • 57
    • 0037388984 scopus 로고    scopus 로고
    • Lack of interleukin-1_decreases the severity of atherosclerosis in ApoE-deficient mice
    • Kirii H, Niwa T, Yamada Y, et al. Lack of interleukin-1_decreases the severity of atherosclerosis in ApoE-deficient mice. Arterioscler Thromb Vasc Biol. 2003; 23: 656-60.
    • (2003) Arterioscler Thromb Vasc Biol , vol.23 , pp. 656-660
    • Kirii, H.1    Niwa, T.2    Yamada, Y.3
  • 58
    • 77955356552 scopus 로고    scopus 로고
    • Cholesterol crystals activate the NLRP3 inflammasome in human macrophages: A novel link between cholesterol metabolism and inflammation
    • Rajamäki K, Lappalainen J, Oörni K, et al. Cholesterol crystals activate the NLRP3 inflammasome in human macrophages: A novel link between cholesterol metabolism and inflammation. PLOS ONE 2010; 5: E11765.
    • (2010) PLOS ONE , vol.5
    • Rajamäki, K.1    Lappalainen, J.2    Oörni, K.3
  • 59
    • 32944468985 scopus 로고    scopus 로고
    • Gout-associated uric acid crystals activate the NALP3 inflammasome
    • Petrilli V, Mayor A, Tardivel A, Tschopp J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 2006; 440: 237-41.
    • (2006) Nature , vol.440 , pp. 237-241
    • Petrilli, V.1    Mayor, A.2    Tardivel, A.3    Tschopp, J.4
  • 60
    • 79251587803 scopus 로고    scopus 로고
    • Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy
    • Egan DF, Shackelford DB, Mihaylova MM, et al. Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy. Science 2011; 331: 456-61.
    • (2011) Science , vol.331 , pp. 456-461
    • Egan, D.F.1    Shackelford, D.B.2    Mihaylova, M.M.3
  • 61
    • 61449193203 scopus 로고    scopus 로고
    • Critical role of apoptotic speck protein containing a caspase recruitment domain (ASC) and NLRP3 in causing necrosis and ASC speck formation induced by Porphyromonas gingivalis in human cells
    • Huang MT, Taxman DJ, Holley-Guthrie EA, et al. Critical role of apoptotic speck protein containing a caspase recruitment domain (ASC) and NLRP3 in causing necrosis and ASC speck formation induced by Porphyromonas gingivalis in human cells. J Immunol 2009; 182: 2395-404.
    • (2009) J Immunol , vol.182 , pp. 2395-2404
    • Huang, M.T.1    Taxman, D.J.2    Holley-Guthrie, E.A.3
  • 62
    • 48249134451 scopus 로고    scopus 로고
    • Critical role of bone marrow apoptosis-associated speck-like protein, an inflammasome adaptor molecule, in neointimal formation after vascular injury in mice
    • Yajima N, Takahashi M, Morimoto H, et al. Critical role of bone marrow apoptosis-associated speck-like protein, an inflammasome adaptor molecule, in neointimal formation after vascular injury in mice. Circulation 2008; 117: 3079-87.
    • (2008) Circulation , vol.117 , pp. 3079-3087
    • Yajima, N.1    Takahashi, M.2    Morimoto, H.3
  • 63
    • 0038094522 scopus 로고    scopus 로고
    • Reduced atherosclerosis in interleukin-18 deficient apolipoprotein E-knockout mice
    • Elhage R, Jawien J, Rudling M, et al. Reduced atherosclerosis in interleukin-18 deficient apolipoprotein E-knockout mice. Cardiovasc Res 2003; 59: 234-40.
    • (2003) Cardiovasc Res , vol.59 , pp. 234-240
    • Elhage, R.1    Jawien, J.2    Rudling, M.3
  • 64
    • 0037197992 scopus 로고    scopus 로고
    • Genetic alterations of IL-1 receptor antagonist in mice affect plasma cholesterol level and foam cell lesion size
    • Devlin CM, Kuriakose G, Hirsch E, Tabas I. Genetic alterations of IL-1 receptor antagonist in mice affect plasma cholesterol level and foam cell lesion size. Proc Natl Acad Sci USA 2002; 99: 6280-5.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6280-6285
    • Devlin, C.M.1    Kuriakose, G.2    Hirsch, E.3    Tabas, I.4
  • 65
    • 84861162164 scopus 로고    scopus 로고
    • U1-small nuclear ribonucleoprotein activates the NLRP3 inflammasome in human monocytes
    • Shin MS, Kang Y, Lee N, et al. U1-small nuclear ribonucleoprotein activates the NLRP3 inflammasome in human monocytes. J Immunol 2012; 188: 4769-77.
    • (2012) J Immunol , vol.188 , pp. 4769-4777
    • Shin, M.S.1    Kang, Y.2    Lee, N.3
  • 66
    • 84865820621 scopus 로고    scopus 로고
    • Activation of Nod-Like Receptor Protein 3 Inflammasomes Turns on Podocyte Injury and Glomerular Sclerosis in Hyperhomocysteinemia
    • Zhang C, Boini KM, Xia M, et al. Activation of Nod-Like Receptor Protein 3 Inflammasomes Turns on Podocyte Injury and Glomerular Sclerosis in Hyperhomocysteinemia. Hypertension 2012; 60: 154-62.
    • (2012) Hypertension , vol.60 , pp. 154-162
    • Zhang, C.1    Boini, K.M.2    Xia, M.3
  • 67
    • 84885598216 scopus 로고    scopus 로고
    • Nalp3 inflammasome is activated and required for vascular smooth muscle cell calcification
    • Wen C, Yang X, Yan Z, et al. Nalp3 inflammasome is activated and required for vascular smooth muscle cell calcification. Int J Cardiol 2013; doi:pii: S0167-5273(13)00271-4.
    • (2013) Int J Cardiol
    • Wen, C.1    Yang, X.2    Yan, Z.3
  • 69
    • 0033750522 scopus 로고    scopus 로고
    • A mouse model of vascular injury that induces rapid onset of medial cell apoptosis followed by reproducible neointimal hyperplasia
    • Sata M, Maejima Y, Adachi F, et al. A mouse model of vascular injury that induces rapid onset of medial cell apoptosis followed by reproducible neointimal hyperplasia. J Mol Cell Cardiol 2000; 32: 2097-104.
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 2097-2104
    • Sata, M.1    Maejima, Y.2    Adachi, F.3
  • 70
    • 0043075883 scopus 로고    scopus 로고
    • Deficiency of interleukin-1 receptor antagonist promotes neointimal formation after injury
    • Isoda K, Shiigai M, Ishigami N, et al. Deficiency of interleukin-1 receptor antagonist promotes neointimal formation after injury. Circulation 2003; 108: 516-8
    • (2003) Circulation , vol.108 , pp. 516-518
    • Isoda, K.1    Shiigai, M.2    Ishigami, N.3
  • 71
    • 33747091335 scopus 로고    scopus 로고
    • Neutralization of interleukin-18 inhibits neointimal formation in a rat model of vascular injury
    • Maffia P, Grassia G, Di Meglio P, et al. Neutralization of interleukin-18 inhibits neointimal formation in a rat model of vascular injury. Circulation 2006; 114: 430-7.
    • (2006) Circulation , vol.114 , pp. 430-437
    • Maffia, P.1    Grassia, G.2    Di Meglio, P.3
  • 72
    • 0027490174 scopus 로고
    • SREBP-1, a basic-helixloop-helix-leucine zipper protein that controls transcription of the low density lipoprotein receptor gene
    • Yokoyama C, Wang X, Briggs MR, et al. SREBP-1, a basic-helixloop-helix-leucine zipper protein that controls transcription of the low density lipoprotein receptor gene. Cell 1993; 75: 187-97.
    • (1993) Cell , vol.75 , pp. 187-197
    • Yokoyama, C.1    Wang, X.2    Briggs, M.R.3
  • 73
    • 84867393447 scopus 로고    scopus 로고
    • Regulation of the human prostacyclin receptor gene by the cholesterol-responsive SREBP1
    • Turner EC, Kinsella BT. Regulation of the human prostacyclin receptor gene by the cholesterol-responsive SREBP1. J Lipid Res 2012; 53: 2390-404.
    • (2012) J Lipid Res , vol.53 , pp. 2390-2404
    • Turner, E.C.1    Kinsella, B.T.2
  • 74
    • 65549140251 scopus 로고    scopus 로고
    • A phosphorylation cascade controls the degradation of active SREBP1
    • Bengoechea-Alonso MT, Ericsson J. A phosphorylation cascade controls the degradation of active SREBP1. J Biol Chem 2009; 284: 5885-95.
    • (2009) J Biol Chem , vol.284 , pp. 5885-5895
    • Bengoechea-Alonso, M.T.1    Ericsson, J.2
  • 75
    • 78049295975 scopus 로고    scopus 로고
    • MicroRNA-33 encoded by an intron of sterol regulatory element-binding protein 2 (Srebp2) regulates HDL in vivo
    • Horie T, Ono K, Horiguchi M, et al. MicroRNA-33 encoded by an intron of sterol regulatory element-binding protein 2 (Srebp2) regulates HDL in vivo. Proc Natl Acad Sci USA 2010; 107: 17321-6.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 17321-17326
    • Horie, T.1    Ono, K.2    Horiguchi, M.3
  • 76
    • 0033613147 scopus 로고    scopus 로고
    • A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood
    • Brown MS, Goldstein JL. A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood. Proc Natl Acad Sci USA 1999; 96: 11041-8.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11041-11048
    • Brown, M.S.1    Goldstein, J.L.2
  • 77
    • 37149021751 scopus 로고    scopus 로고
    • Atherosclerosis-prone hemodynamics differentially regulates endothelial and smooth muscle cell phenotypes and promotes pro-inflammatory priming
    • Hastings NE, Simmers MB, McDonald OG, Wamhoff BR, Blackman BR. Atherosclerosis-prone hemodynamics differentially regulates endothelial and smooth muscle cell phenotypes and promotes pro-inflammatory priming. Am J Physiol Cell Physiol 2007; 293: C1824-33.
    • (2007) Am J Physiol Cell Physiol , vol.293 , pp. 1824-1833
    • Hastings, N.E.1    Simmers, M.B.2    McDonald, O.G.3    Wamhoff, B.R.4    Blackman, B.R.5
  • 78
    • 84984808737 scopus 로고    scopus 로고
    • Srebp2 activation of nlrp3 nflammasome in endothelium mediates hemodynamic-induced atherosclerosis susceptibility
    • Xiao H, Lu M, Lin TY, et al. Srebp2 activation of nlrp3 nflammasome in endothelium mediates hemodynamic-induced atherosclerosis susceptibility. Circulation 2013;128: Doi: 10.1161
    • (2013) Circulation , vol.128
    • Xiao, H.1    Lu, M.2    Lin, T.Y.3
  • 80
    • 84880280093 scopus 로고    scopus 로고
    • Crystal structure of NLRC4 reveals its autoinhibition mechanism
    • Hu Z, Yan C, Liu P, et al. Crystal structure of NLRC4 reveals its autoinhibition mechanism. Science 2013; 341: 172-5.
    • (2013) Science , vol.341 , pp. 172-175
    • Hu, Z.1    Yan, C.2    Liu, P.3
  • 81
    • 0037228017 scopus 로고    scopus 로고
    • Birc1e is the gene within the Lgn1 locus associated with resistance to Legionella pneumophila
    • Diez E, Lee SH, Gauthier S, et al. Birc1e is the gene within the Lgn1 locus associated with resistance to Legionella pneumophila. Nat Genet 2003; 33: 55-60.
    • (2003) Nat Genet , vol.33 , pp. 55-60
    • Diez, E.1    Lee, S.H.2    Gauthier, S.3
  • 82
    • 45549092412 scopus 로고    scopus 로고
    • NAIP and Ipaf control Legionella pneumophila replication in human cells
    • Vinzing M, Eitel J, Lippmann J, et al. NAIP and Ipaf control Legionella pneumophila replication in human cells. J Immunol 2008; 180: 6808-15.
    • (2008) J Immunol , vol.180 , pp. 6808-6815
    • Vinzing, M.1    Eitel, J.2    Lippmann, J.3
  • 83
    • 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, et al. The Birc1e cytosolic pattern-recognition receptor contributes to the detection and control of Legionella pneumophila infection. Nat Immunol 2006; 7: 318-25
    • (2006) Nat Immunol , vol.7 , pp. 318-325
    • Zamboni, D.S.1    Kobayashi, K.S.2    Kohlsdorf, T.3
  • 85
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • Schroder K, Tschopp J. The inflammasomes. Cell 2010; 140: 821-32.
    • (2010) Cell , vol.140 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 86
    • 34548434775 scopus 로고    scopus 로고
    • Differential regulation of caspase-1 activation, pyroptosis, and autophagy via Ipaf and ASC in Shigella-infected macrophages
    • Suzuki T, Franchi L, Toma C, et al. Differential regulation of caspase-1 activation, pyroptosis, and autophagy via Ipaf and ASC in Shigella-infected macrophages. PLoS Pathog 2007; 3: E111.
    • (2007) Plos Pathog , vol.3
    • Suzuki, T.1    Franchi, L.2    Toma, C.3
  • 87
  • 88
    • 70249138036 scopus 로고    scopus 로고
    • Cutting edge: NFkappaB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP expression
    • Bauernfeind FG, Horvath G, Stutz A, et al. Cutting edge: NFkappaB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP expression. J Immunol 2009; 183: 7-38.
    • (2009) J Immunol , vol.183 , pp. 7-38
    • Bauernfeind, F.G.1    Horvath, G.2    Stutz, A.3
  • 90
    • 78651393239 scopus 로고    scopus 로고
    • A role for mitochondria in NLRP3 inflammasome activation
    • Zhou R, Yazdi AS, Menu P, Tschopp J. A role for mitochondria in NLRP3 inflammasome activation. Nature 2011; 469: 221-5.
    • (2011) Nature , vol.469 , pp. 221-225
    • Zhou, R.1    Yazdi, A.S.2    Menu, P.3    Tschopp, J.4
  • 91
    • 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, Haspel JA, Rathinam VA, et al. Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome. Nat Immunol 2011; 12: 222-30.
    • (2011) Nat Immunol , vol.12 , pp. 222-230
    • Nakahira, K.1    Haspel, J.A.2    Rathinam, V.A.3
  • 92
    • 33644607461 scopus 로고    scopus 로고
    • Pathophysiology and therapeutic potential of purinergic signaling
    • Burnstock G. Pathophysiology and therapeutic potential of purinergic signaling. Pharmacol Rev 2006; 58: 58-86.
    • (2006) Pharmacol Rev , vol.58 , pp. 58-86
    • Burnstock, G.1
  • 93
    • 33646072818 scopus 로고    scopus 로고
    • The p2x7 receptor: A key player in il-1 processing and release
    • Ferrari D, Pizzirani C, Adinolfi E, et al. The p2x7 receptor: A key player in il-1 processing and release. J Immunol 2006;176: 3877-83.
    • (2006) J Immunol , vol.176 , pp. 3877-3883
    • Ferrari, D.1    Pizzirani, C.2    Adinolfi, E.3
  • 94
    • 28244459680 scopus 로고    scopus 로고
    • Potentiation of caspase-1 activation by the P2X7 receptor is dependent on TLR signals and requires NF-kappaB-driven protein synthesis
    • Kahlenberg JM, Lundberg KC, Kertesy SB, Qu Y, Dubyak GR. Potentiation of caspase-1 activation by the P2X7 receptor is dependent on TLR signals and requires NF-kappaB-driven protein synthesis. Immunol 2001; 175: 7611-22.
    • (2001) Immunol , vol.175 , pp. 7611-7622
    • Kahlenberg, J.M.1    Lundberg, K.C.2    Kertesy, S.B.3    Qu, Y.4    Dubyak, G.R.5
  • 95
    • 34247118826 scopus 로고    scopus 로고
    • Pannexin-1-mediated recognition of bacterial molecules activates the cryopyrin inflammasome independent of Toll-like receptor signaling
    • Kanneganti TD, Lamkanfi M, Kim YG, et al. Pannexin-1-mediated recognition of bacterial molecules activates the cryopyrin inflammasome independent of Toll-like receptor signaling. Immunity 2007; 26: 433-43.
    • (2007) Immunity , vol.26 , pp. 433-443
    • Kanneganti, T.D.1    Lamkanfi, M.2    Kim, Y.G.3
  • 96
    • 47249144272 scopus 로고    scopus 로고
    • P2X7 receptor differentially couples to distinct release pathways for IL-1beta in mouse macrophage
    • Pelegrin P, Barroso-Gutierrez C, Surprenant A. P2X7 receptor differentially couples to distinct release pathways for IL-1beta in mouse macrophage. J Immunol 2008; 180: 7147-57.
    • (2008) J Immunol , vol.180 , pp. 7147-7157
    • Pelegrin, P.1    Barroso-Gutierrez, C.2    Surprenant, A.3
  • 97
    • 33750473352 scopus 로고    scopus 로고
    • Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor
    • Pelegrin, P. and Surprenant, A. Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor. EMBO J 2006; 25: 5071-82.
    • (2006) EMBO J , vol.25 , pp. 5071-5082
    • Pelegrin, P.1    Surprenant, A.2
  • 98
    • 44849136632 scopus 로고    scopus 로고
    • Pannexin-1-mediated intracellular delivery of muramyl dipeptide induces caspase-1 activation via cryopyrin/NLRP3 independently of Nod2
    • Marina-García N, Franchi L, Kim YG, et al. Pannexin-1-mediated intracellular delivery of muramyl dipeptide induces caspase-1 activation via cryopyrin/NLRP3 independently of Nod2. J. Immunol 2008; 180: 4050-7.
    • (2008) J. Immunol , vol.180 , pp. 4050-4057
    • Marina-García, N.1    Franchi, L.2    Kim, Y.G.3
  • 100
    • 47849097202 scopus 로고    scopus 로고
    • Sillic crystals and aluminum salts activate, the NALP3 inflammasome through phagosomal destabilization
    • Hornung V, Bauernfeind F, Halle A, et al. Sillic crystals and aluminum salts activate, the NALP3 inflammasome through phagosomal destabilization. Nat Immunol 2008; 9: 847-56.
    • (2008) Nat Immunol , vol.9 , pp. 847-856
    • Hornung, V.1    Bauernfeind, F.2    Halle, A.3
  • 101
    • 47849132947 scopus 로고    scopus 로고
    • The Nalp3 inflammasome is essential for the development of silicosis
    • Cassel SL, Eisenbarth SC, Iyer SS, et al. The Nalp3 inflammasome is essential for the development of silicosis. Proc Natl Acad Sci U S A. 2008; 105: 9035-9040.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9035-9040
    • Cassel, S.L.1    Eisenbarth, S.C.2    Iyer, S.S.3
  • 102
    • 79960542894 scopus 로고    scopus 로고
    • Cutting edge: Reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome
    • Bauernfeind F, Bartok E, Rieger A, Franchi L, Núñez G, Hornung V. Cutting edge: Reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome. J Immunol. 2011; 187: 613-7.
    • (2011) J Immunol , vol.187 , pp. 613-617
    • Bauernfeind, F.1    Bartok, E.2    Rieger, A.3    Franchi, L.4    Núñez, G.5    Hornung, V.6
  • 103
    • 63649133278 scopus 로고    scopus 로고
    • AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
    • Hornung V, Ablasser A, Charrel-Dennis M, et al. AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC. Nature. 2009; 458: 514-8.
    • (2009) Nature , vol.458 , pp. 514-518
    • Hornung, V.1    Ablasser, A.2    Charrel-Dennis, M.3
  • 104
    • 63649145255 scopus 로고    scopus 로고
    • AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
    • Fernandes-Alnemri T, Yu JW, Datta P, Wu J, Alnemri ES. AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA. Nature 2009; 458: 509-13.
    • (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
  • 105
    • 77951263260 scopus 로고    scopus 로고
    • The AIM2 inflammasome is critical for innate immunity to Francisella tularensis
    • Fernandes-Alnemri T, Yu JW, Juliana C, et al. The AIM2 inflammasome is critical for innate immunity to Francisella tularensis. Nat Immunol 2010; 11: 385-93.
    • (2010) Nat Immunol , vol.11 , pp. 385-393
    • Fernandes-Alnemri, T.1    Yu, J.W.2    Juliana, C.3
  • 106
    • 0037180771 scopus 로고    scopus 로고
    • Inflammation in atherosclerosis
    • Libby P. Inflammation in atherosclerosis. Nature 2002; 420: 868-74.
    • (2002) Nature , vol.420 , pp. 868-874
    • Libby, P.1
  • 107
    • 0141639811 scopus 로고    scopus 로고
    • Role of monocytes in atherogenesis
    • Osterud B, Bjorklid E. Role of monocytes in atherogenesis. Physiol Rev 2003; 83: 1069-112.
    • (2003) Physiol Rev , vol.83 , pp. 1069-1112
    • Osterud, B.1    Bjorklid, E.2
  • 108
    • 84862791715 scopus 로고    scopus 로고
    • Macrophage autophagy plays a protective role in advanced atherosclerosis
    • Liao X, Sluimer JC, Wang Y, et al. Macrophage autophagy plays a protective role in advanced atherosclerosis. Cell Metab 2012; 15: 545-53.
    • (2012) Cell Metab , vol.15 , pp. 545-553
    • Liao, X.1    Sluimer, J.C.2    Wang, Y.3
  • 109
    • 84875915764 scopus 로고    scopus 로고
    • Autophagy regulates TNF_-mediated joint destruction in experimental arthritis
    • Lin NY, Beyer C, Gießl A, et al. Autophagy regulates TNF_-mediated joint destruction in experimental arthritis. Ann Rheum Dis 2013; 72: 761-8.
    • (2013) Ann Rheum Dis , vol.72 , pp. 761-768
    • Lin, N.Y.1    Beyer, C.2    Gießl, A.3
  • 110
    • 84859448447 scopus 로고    scopus 로고
    • Autophagy links inflammasomes to atherosclerotic progression
    • Razani B, Feng C, Coleman T, et al. Autophagy links inflammasomes to atherosclerotic progression. Cell Metab 2012; 15: 34-544.
    • (2012) Cell Metab , vol.15 , pp. 34-544
    • Razani, B.1    Feng, C.2    Coleman, T.3
  • 111
    • 17844386319 scopus 로고    scopus 로고
    • IKKalpha limits macrophage NF-kappaB activation and contributes to the resolution of inflammation
    • Lawrence T, Bebien M, Liu GY, Nizet V, Karin M. IKKalpha limits macrophage NF-kappaB activation and contributes to the resolution of inflammation. Nature 2005; 434: 1138-43.
    • (2005) Nature , vol.434 , pp. 1138-1143
    • Lawrence, T.1    Bebien, M.2    Liu, G.Y.3    Nizet, V.4    Karin, M.5
  • 112
    • 13344261982 scopus 로고    scopus 로고
    • Activated transcription factor nuclear factor-kappa B is present in the atherosclerotic lesion
    • Brand K, Page S, Rogler G, et al. Activated transcription factor nuclear factor-kappa B is present in the atherosclerotic lesion. J Clin Invest 1996; 97: 1715-22.
    • (1996) J Clin Invest , vol.97 , pp. 1715-1722
    • Brand, K.1    Page, S.2    Rogler, G.3
  • 114
    • 33746895830 scopus 로고    scopus 로고
    • Toll-like receptors and atherosclerosis: Key contributors in disease and health?
    • Mullick AE, Tobias PS, Curtiss LK. Toll-like receptors and atherosclerosis: Key contributors in disease and health? Immunol Res 2006; 34:193-209.
    • (2006) Immunol Res , vol.34 , pp. 193-209
    • Mullick, A.E.1    Tobias, P.S.2    Curtiss, L.K.3
  • 115
    • 13444280215 scopus 로고    scopus 로고
    • CD36 is a sensor of diacylglycerides
    • Hoebe K, Georgel P, Rutschmann S, et al. CD36 is a sensor of diacylglycerides. Nature 2005; 433: 523-7.
    • (2005) Nature , vol.433 , pp. 523-527
    • Hoebe, K.1    Georgel, P.2    Rutschmann, S.3
  • 116
    • 23744514918 scopus 로고    scopus 로고
    • Response to Staphylococcus aureus requires CD36-mediated phagocytosis triggered by the COOH-terminal cytoplasmic domain
    • Stuart LM, Deng J, Silver JM, et al. Response to Staphylococcus aureus requires CD36-mediated phagocytosis triggered by the COOH-terminal cytoplasmic domain. J. Cell Biol 2005; 170: 477-85.
    • (2005) J. Cell Biol , vol.170 , pp. 477-485
    • Stuart, L.M.1    Deng, J.2    Silver, J.M.3
  • 117
    • 75649087741 scopus 로고    scopus 로고
    • CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer
    • Stewart CR, Stuart LM, Wilkinson K, et al. CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer. Nat Immunol 2010; 11: 155-61.
    • (2010) Nat Immunol , vol.11 , pp. 155-161
    • Stewart, C.R.1    Stuart, L.M.2    Wilkinson, K.3
  • 118
    • 3242728901 scopus 로고    scopus 로고
    • Reduced atherosclerosis in MyD88-null mice links elevated serum cholesterol levels to activation of innate immunity signaling pathways
    • Björkbacka H, Kunjathoor VV, Moore KJ, et al. Reduced atherosclerosis in MyD88-null mice links elevated serum cholesterol levels to activation of innate immunity signaling pathways. Nat Med 2004; 10: 416-21.
    • (2004) Nat Med , vol.10 , pp. 416-421
    • Björkbacka, H.1    Kunjathoor, V.V.2    Moore, K.J.3
  • 119
    • 34248209613 scopus 로고    scopus 로고
    • Macrophage-specific inhibition of NF-kappaB activation reduces foam-cell formation
    • Ferreira V, van Dijk KW, Groen AK, et al. Macrophage-specific inhibition of NF-kappaB activation reduces foam-cell formation. Atherosclerosis 2007; 192: 283-90.
    • (2007) Atherosclerosis , vol.192 , pp. 283-290
    • Ferreira, V.1    Van Dijk, K.W.2    Groen, A.K.3
  • 121
    • 56249090667 scopus 로고    scopus 로고
    • Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production
    • Saitoh T, Fujita N, Jang MH, et al. Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production. Nature 2008; 456: 264-8.
    • (2008) Nature , vol.456 , pp. 264-268
    • Saitoh, T.1    Fujita, N.2    Jang, M.H.3
  • 122
    • 56249135538 scopus 로고    scopus 로고
    • A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells
    • Cadwell K, Liu JY, Brown SL, et al. A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells. Nature 2008; 456: 259-63.
    • (2008) Nature , vol.456 , pp. 259-263
    • Cadwell, K.1    Liu, J.Y.2    Brown, S.L.3
  • 123
    • 0032563798 scopus 로고    scopus 로고
    • A protein conjugation system essential for autophagy
    • Mizushima N, Noda T, Yoshimori T, et al. A protein conjugation system essential for autophagy. Nature 1998; 395: 395-8.
    • (1998) Nature , vol.395 , pp. 395-398
    • Mizushima, N.1    Noda, T.2    Yoshimori, T.3
  • 124
    • 20144381544 scopus 로고    scopus 로고
    • Essential roles of Atg5 and FADD in autophagic cell death: Dissection of autophagic cell death into vacuole formation and cell death
    • Pyo JO, Jang MH, Kwon YK, et al. Essential roles of Atg5 and FADD in autophagic cell death: Dissection of autophagic cell death into vacuole formation and cell death. J Biol Chem 2005; 280: 20722-9.
    • (2005) J Biol Chem , vol.280 , pp. 20722-20729
    • Pyo, J.O.1    Jang, M.H.2    Kwon, Y.K.3
  • 125
    • 80053582762 scopus 로고    scopus 로고
    • A hippocampal insulin-growth factor 2 pathway regulates the extinction of fear memories
    • Agis-Balboa RC, Arcos-Diaz D, Wittnam J, et al. A hippocampal insulin-growth factor 2 pathway regulates the extinction of fear memories. EMBO J 2011; 30: 4701-11.
    • (2011) EMBO J , vol.30 , pp. 4701-4711
    • Agis-Balboa, R.C.1    Arcos-Diaz, D.2    Wittnam, J.3
  • 126
    • 84880376355 scopus 로고    scopus 로고
    • Emerging regulation and functions of autophagy
    • Boya P, Reggiori F, Codogno P. Emerging regulation and functions of autophagy. Nat Cell Biol 2013; 15: 713-20.
    • (2013) Nat Cell Biol , vol.15 , pp. 713-720
    • Boya, P.1    Reggiori, F.2    Codogno, P.3
  • 127
    • 0023972981 scopus 로고
    • George Lyman Duff memorial lecture. Progression and regression of atherosclerotic lesions. Insights from lipid physical biochemistry
    • Small DM. George Lyman Duff memorial lecture. Progression and regression of atherosclerotic lesions. Insights from lipid physical biochemistry. Arteriosclerosis 1988; 8: 103-29.
    • (1988) Arteriosclerosis , vol.8 , pp. 103-129
    • Small, D.M.1
  • 128
    • 47849085872 scopus 로고    scopus 로고
    • The NALP3 inflammasome is involved in the innate immune response to amyloid-β
    • Halle A, Hornung V, Petzold GC, et al. The NALP3 inflammasome is involved in the innate immune response to amyloid-β. Nat Immunol 2008; 9: 857-65.
    • (2008) Nat Immunol , vol.9 , pp. 857-865
    • Halle, A.1    Hornung, V.2    Petzold, G.C.3
  • 129
    • 79955038882 scopus 로고    scopus 로고
    • Fatty acid-induced NLRP3-ASC inflammasome activation interferes with insulin signaling
    • Wen H, Gris D, Lei Y, et al. Fatty acid-induced NLRP3-ASC inflammasome activation interferes with insulin signaling. Nat Immunol 2011; 12: 408-15.
    • (2011) Nat Immunol , vol.12 , pp. 408-415
    • Wen, H.1    Gris, D.2    Lei, Y.3
  • 130
    • 79953176280 scopus 로고    scopus 로고
    • Autophagy controls IL-1beta secretion by targeting pro-IL-1beta for degradation
    • Harris J, Hartman M, Roche C, et al. Autophagy controls IL-1beta secretion by targeting pro-IL-1beta for degradation. J Biol Chem 2011; 286: 9587-97.
    • (2011) J Biol Chem , vol.286 , pp. 9587-9597
    • Harris, J.1    Hartman, M.2    Roche, C.3
  • 131
    • 79955693448 scopus 로고    scopus 로고
    • The inflammasome in atherosclerosis and type 2 diabetes
    • Masters SL, Latz E, O'Neill LA. The inflammasome in atherosclerosis and type 2 diabetes. Sci Transl Med 2011; 3: 81-17. doi: 10.1126/scitranslmed.3001902
    • (2011) Sci Transl Med , vol.3 , pp. 81-117
    • Masters, S.L.1    Latz, E.2    O'neill, L.A.3
  • 132
    • 0027469584 scopus 로고
    • Functional expression of human cathepsin S in Saccharomyces cerevisiae: Purification and characterization of the recombinant enzyme
    • Bromme D, Bonneau PR, Lachance P, et al. Functional expression of human cathepsin S in Saccharomyces cerevisiae: Purification and characterization of the recombinant enzyme. J Biol Chem 1993; 268: 4832-8.
    • (1993) J Biol Chem , vol.268 , pp. 4832-4838
    • Bromme, D.1    Bonneau, P.R.2    Lachance, P.3
  • 133
    • 0028790929 scopus 로고
    • Mature cathepsin L is substantially active in the ionic milieu of the extracellular medium
    • Dehrmann FM, Coetzer TH, Pike RN, Dennison C. Mature cathepsin L is substantially active in the ionic milieu of the extracellular medium. Arch Biochem Biophys 1995; 324: 93-8.
    • (1995) Arch Biochem Biophys , vol.324 , pp. 93-98
    • Dehrmann, F.M.1    Coetzer, T.H.2    Pike, R.N.3    Dennison, C.4
  • 134
    • 0033610853 scopus 로고    scopus 로고
    • The collagenolytic activity of cathepsin K is unique among mammalian proteinases
    • Garnero P, Borel O, Byrjalsen I, et al. The collagenolytic activity of cathepsin K is unique among mammalian proteinases. J Biol Chem 1998; 273: 32347-52.
    • (1998) J Biol Chem , vol.273 , pp. 32347-32352
    • Garnero, P.1    Borel, O.2    Byrjalsen, I.3
  • 135
    • 0032145836 scopus 로고    scopus 로고
    • Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells
    • Sukhova GK, Shi GP, Simon DI, Chapman HA, Libby P. Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells. J Clin Invest 1998; 102: 576-83.
    • (1998) J Clin Invest , vol.102 , pp. 576-583
    • Sukhova, G.K.1    Shi, G.P.2    Simon, D.I.3    Chapman, H.A.4    Libby, P.5
  • 136
    • 33744957641 scopus 로고    scopus 로고
    • Advanced atherosclerotic foam cell formation has features of an acquired lysosomal storage disorder
    • Jerome WG. Advanced atherosclerotic foam cell formation has features of an acquired lysosomal storage disorder. Rejuvenation Res 2006; 9: 245-55.
    • (2006) Rejuvenation Res , vol.9 , pp. 245-255
    • Jerome, W.G.1
  • 137
    • 0033995604 scopus 로고    scopus 로고
    • Cholesterol and oxysterol metabolism and subcellular distribution in macrophage foam cells. Accumulation of oxidized esters in lysosomes
    • Brown AJ, Mander EL, Gelissen IC, Kritharides L, Dean RT, Jessup W. Cholesterol and oxysterol metabolism and subcellular distribution in macrophage foam cells. Accumulation of oxidized esters in lysosomes. J Lipid Res 2000; 41: 226-37.
    • (2000) J Lipid Res , vol.41 , pp. 226-237
    • Brown, A.J.1    Mander, E.L.2    Gelissen, I.C.3    Kritharides, L.4    Dean, R.T.5    Jessup, W.6
  • 138
    • 0033779272 scopus 로고    scopus 로고
    • Cholesterol delivered to macrophages by oxidized low density lipoprotein is sequestered in lysosomes and fails to efflux normally
    • Dhaliwal BS, Steinbrecher UP. Cholesterol delivered to macrophages by oxidized low density lipoprotein is sequestered in lysosomes and fails to efflux normally. J Lipid 2000; 1658-65.
    • (2000) J Lipid , pp. 1658-1665
    • Dhaliwal, B.S.1    Steinbrecher, U.P.2
  • 139
    • 25444481923 scopus 로고    scopus 로고
    • Aggregated LDL and lipid dispersions induce lysosomal cholesteryl ester accumulation in macrophage foam cells
    • Griffin EE, Ullery JC, Cox BE, Jerome WG. Aggregated LDL and lipid dispersions induce lysosomal cholesteryl ester accumulation in macrophage foam cells. J Lipid Res 2005; 46: 2052-60.
    • (2005) J Lipid Res , vol.46 , pp. 2052-2060
    • Griffin, E.E.1    Ullery, J.C.2    Cox, B.E.3    Jerome, W.G.4
  • 140
    • 0035064419 scopus 로고    scopus 로고
    • Lysosomal cholesterol derived from mildly oxidized low density lipoprotein is resistant to efflux
    • Yancey PG, Jerome WG. Lysosomal cholesterol derived from mildly oxidized low density lipoprotein is resistant to efflux. J Lipid Res 2001; 42: 317-27.
    • (2001) J Lipid Res , vol.42 , pp. 317-327
    • Yancey, P.G.1    Jerome, W.G.2
  • 141
    • 34248226770 scopus 로고    scopus 로고
    • Severely altered cholesterol homeostasis in macrophages lacking apoE and SR-BI
    • Yancey PG, Jerome WG, Yu H, et al. Severely altered cholesterol homeostasis in macrophages lacking apoE and SR-BI. J Lipid Res 2007; 48: 1140-9.
    • (2007) J Lipid Res , vol.48 , pp. 1140-1149
    • Yancey, P.G.1    Jerome, W.G.2    Yu, H.3
  • 142
    • 77649133500 scopus 로고    scopus 로고
    • Pathways by which reconstituted high-density lipoprotein mobilizes free cholesterol from whole body and from macrophages
    • Cuchel M, Lund-Katz S, dela Llera-Moya M, et al. Pathways by which reconstituted high-density lipoprotein mobilizes free cholesterol from whole body and from macrophages. Arterioscler Thromb Vasc Biol 2010; 30: 526-32.
    • (2010) Arterioscler Thromb Vasc Biol , vol.30 , pp. 526-532
    • Cuchel, M.1    Lund-Katz, S.2    Dela Llera-Moya, M.3
  • 143
    • 77954039619 scopus 로고    scopus 로고
    • ATP-binding cassette transporters and HDL suppress hematopoietic stem cell proliferation
    • Yvan-Charvet L, Pagler T, Gautier EL, et al. ATP-binding cassette transporters and HDL suppress hematopoietic stem cell proliferation. Science 2010; 328: 1689-93.
    • (2010) Science , vol.328 , pp. 1689-1693
    • Yvan-Charvet, L.1    Pagler, T.2    Gautier, E.L.3
  • 144
    • 84857057602 scopus 로고    scopus 로고
    • Antirestenotic mechanisms of everolimus on human coronary artery smooth muscle cells: Inhibition of human coronary artery smooth muscle cell proliferation, but not migration
    • Lavigne MC, Grimsby JL, Eppihimer MJ. Antirestenotic mechanisms of everolimus on human coronary artery smooth muscle cells: Inhibition of human coronary artery smooth muscle cell proliferation, but not migration. J Cardiovasc Pharmacol 2012; 59: 165-74.
    • (2012) J Cardiovasc Pharmacol , vol.59 , pp. 165-174
    • Lavigne, M.C.1    Grimsby, J.L.2    Eppihimer, M.J.3
  • 145
    • 59649088081 scopus 로고    scopus 로고
    • Everolimus inhibits monocyte/macrophage migration in vitro and their accumulation in carotid lesions of cholesterol-fed rabbits
    • Baetta R, Granata A, Canavesi M, et al. Everolimus inhibits monocyte/macrophage migration in vitro and their accumulation in carotid lesions of cholesterol-fed rabbits. J Pharmacol Exp Ther 2009; 328: 419-25.
    • (2009) J Pharmacol Exp Ther , vol.328 , pp. 419-425
    • Baetta, R.1    Granata, A.2    Canavesi, M.3
  • 146
    • 33846177854 scopus 로고    scopus 로고
    • The pharmacodynamic effects of sirolimus and sirolimuscalcineurin inhibitor combinations on macrophage scavenger and nuclear hormone receptors
    • Mathis AS, Jin S, Friedman GS, Peng F, Carl SM, Knipp GT The pharmacodynamic effects of sirolimus and sirolimuscalcineurin inhibitor combinations on macrophage scavenger and nuclear hormone receptors. J Pharm Sci 2007; 96: 209-22.
    • (2007) J Pharm Sci , vol.96 , pp. 209-222
    • Mathis, A.S.1    Jin, S.2    Friedman, G.S.3    Peng, F.4    Carl, S.M.5    Knipp, G.T.6
  • 147
    • 77952595127 scopus 로고    scopus 로고
    • Sirolimus inhibits endogenous cholesterol synthesis induced by inflammatory stress in human vascular smooth muscle cells
    • Ma KL, Varghese Z, Ku Y, et al. Sirolimus inhibits endogenous cholesterol synthesis induced by inflammatory stress in human vascular smooth muscle cells. Am J Physiol Heart Circ Physiol 2010; 298: H1646-H1651.
    • (2010) Am J Physiol Heart Circ Physiol , vol.298 , pp. 1646-1651
    • Ma, K.L.1    Varghese, Z.2    Ku, Y.3
  • 149
    • 84860153374 scopus 로고    scopus 로고
    • Toll-like receptor 7 stimulation by imiquimod induces macrophage autophagy and inflammation in atherosclerotic plaques
    • De Meyer I, Martinet W, Schrijvers DM, Timmermans J-P, Bult H, De Meyer GRY. Toll-like receptor 7 stimulation by imiquimod induces macrophage autophagy and inflammation in atherosclerotic plaques. Basic Res Cardiol 2012; 107: 269.
    • (2012) Basic Res Cardiol , vol.107
    • De Meyer, I.1    Martinet, W.2    Schrijvers, D.M.3    Timmermans, J.-P.4    Bult, H.5    De Meyer, G.6
  • 150
    • 0038204838 scopus 로고    scopus 로고
    • CD36 mediates the innate host response to_-amyloid
    • El-Khoury JB, Moore KJ, Means TK, et al. CD36 mediates the innate host response to_-amyloid. J Exp Med 2003; 197: 1657-66.
    • (2003) J Exp Med , vol.197 , pp. 1657-1666
    • El-Khoury, J.B.1    Moore, K.J.2    Means, T.K.3
  • 151
    • 0034101821 scopus 로고    scopus 로고
    • Targeted disruption of the class B scavenger receptor CD36 protects against atherosclerotic lesion development in mice
    • Febbraio M, Podrez EA, Smith JD, et al. Targeted disruption of the class B scavenger receptor CD36 protects against atherosclerotic lesion development in mice. J Clin Invest 2000; 105: 1049-56.
    • (2000) J Clin Invest , vol.105 , pp. 1049-1056
    • Febbraio, M.1    Podrez, E.A.2    Smith, J.D.3
  • 152
    • 23644435612 scopus 로고    scopus 로고
    • Loss of receptormediated lipid uptake via scavenger receptor A or CD36 pathways does not ameliorate atherosclerosis in hyperlipidemic mice
    • Moore KJ, Kunjathoor VV, Koehn SL, et al. Loss of receptormediated lipid uptake via scavenger receptor A or CD36 pathways does not ameliorate atherosclerosis in hyperlipidemic mice. J Clin Invest 2005; 115: 2192-201.
    • (2005) J Clin Invest , vol.115 , pp. 2192-2201
    • Moore, K.J.1    Kunjathoor, V.V.2    Koehn, S.L.3
  • 153
    • 84880777411 scopus 로고    scopus 로고
    • CD36 coordinates NLRP3 inflammasome activation by facilitating intracellular nucleation of soluble ligands into particulate ligands in sterile inflammation
    • Sheedy FJ, Grebe A, Rayner KJ, et al. CD36 coordinates NLRP3 inflammasome activation by facilitating intracellular nucleation of soluble ligands into particulate ligands in sterile inflammation. Nat Immunol 2013; 14: 812-20.
    • (2013) Nat Immunol , vol.14 , pp. 812-820
    • Sheedy, F.J.1    Grebe, A.2    Rayner, K.J.3
  • 154
    • 84863229387 scopus 로고    scopus 로고
    • COPDGene Investigators. Statins and pulmonary fibrosis: The potential role of NLRP3 inflammasome activation
    • Xu JF, Washko GR, Nakahira K, et al. COPDGene Investigators. Statins and pulmonary fibrosis: The potential role of NLRP3 inflammasome activation. Am J Respir Crit Care Med 2012; 185: 547-56.
    • (2012) Am J Respir Crit Care Med , vol.185 , pp. 547-556
    • Xu, J.F.1    Washko, G.R.2    Nakahira, K.3
  • 155
    • 84879582334 scopus 로고    scopus 로고
    • Alcohol-induced IL-1βin the brain is mediated by NLRP3/ASC inflammasome activation that amplifies neuroinflammation
    • Lippai D, Bala S, Petrasek J, et al. Alcohol-induced IL-1βin the brain is mediated by NLRP3/ASC inflammasome activation that amplifies neuroinflammation. J Leukoc Biol 2013; 94: 171-82.
    • (2013) J Leukoc Biol , vol.94 , pp. 171-182
    • Lippai, D.1    Bala, S.2    Petrasek, J.3
  • 156
    • 84881292306 scopus 로고    scopus 로고
    • MAVS Regulates Apoptotic Cell Death by Decreasing K48-linked Ubiquitination of VDAC1
    • Jun 10
    • Guan K, Zheng Z, Song T, et al. MAVS Regulates Apoptotic Cell Death by Decreasing K48-linked Ubiquitination of VDAC1. Mol Cell Biol 2013 Jun 10.
    • (2013) Mol Cell Biol
    • Guan, K.1    Zheng, Z.2    Song, T.3
  • 157
    • 84859911615 scopus 로고    scopus 로고
    • NLRC4-driven production of IL-1_discriminates between pathogenic and commensal bacteria and promotes host intestinal defense
    • Franchi L, Kamada N, Nakamura Y, et al. NLRC4-driven production of IL-1_discriminates between pathogenic and commensal bacteria and promotes host intestinal defense. Nat Immunol 2012; 13: 449-56.
    • (2012) Nat Immunol , vol.13 , pp. 449-456
    • Franchi, L.1    Kamada, N.2    Nakamura, Y.3
  • 158
    • 77951269392 scopus 로고    scopus 로고
    • The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses
    • Rathinam VA, Jiang Z, Waggoner SN, et al. The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses. Nat Immunol 2010; 11: 395-402.
    • (2010) Nat Immunol , vol.11 , pp. 395-402
    • Rathinam, V.A.1    Jiang, Z.2    Waggoner, S.N.3
  • 160
    • 84865389353 scopus 로고    scopus 로고
    • Critical role of caspase-1 in vascular inflammation and development of atherosclerosis in Western diet-fed apolipoprotein E-deficient mice
    • Usui F, Shirasuna K, Kimura H, et al. Critical role of caspase-1 in vascular inflammation and development of atherosclerosis in Western diet-fed apolipoprotein E-deficient mice. Biochem Biophys Res Commun 2012; 425: 162-8.
    • (2012) Biochem Biophys Res Commun , vol.425 , pp. 162-168
    • Usui, F.1    Shirasuna, K.2    Kimura, H.3
  • 161
    • 84855272667 scopus 로고    scopus 로고
    • Inflammasome-dependent pyroptosis and IL-18 protect against Burkholderia pseudomallei lung infection while IL-1_is deleterious
    • Ceballos-Olvera I, Sahoo M, Miller MA, Del Barrio L, Re F. Inflammasome-dependent pyroptosis and IL-18 protect against Burkholderia pseudomallei lung infection while IL-1_is deleterious. PLoS Pathog 2011; 7: E1002452.
    • (2011) Plos Pathog , vol.7
    • Ceballos-Olvera, I.1    Sahoo, M.2    Miller, M.A.3    Del Barrio, L.4    Re, F.5
  • 162
    • 76249115506 scopus 로고    scopus 로고
    • IL-1R1/MyD88 signaling is critical for elastase-induced lung inflammation and emphysema
    • Couillin I, Vasseur V, Charron S, et al. IL-1R1/MyD88 signaling is critical for elastase-induced lung inflammation and emphysema. J Immunol 2009; 183: 8195-202.
    • (2009) J Immunol , vol.183 , pp. 8195-8202
    • Couillin, I.1    Vasseur, V.2    Charron, S.3
  • 163
    • 75649096002 scopus 로고    scopus 로고
    • Thioredoxininteracting protein links oxidative stress to inflammasome activation
    • Zhou R, Tardivel A, Thorens B, Choi I, Tschopp J. Thioredoxininteracting protein links oxidative stress to inflammasome activation. Nat Immunol 2010; 11: 136-40
    • (2010) Nat Immunol , vol.11 , pp. 136-140
    • Zhou, R.1    Tardivel, A.2    Thorens, B.3    Choi, I.4    Tschopp, J.5
  • 164
    • 84881546504 scopus 로고    scopus 로고
    • A West Nile virus NS4B-P38G mutant strain induces adaptive immunity via TLR7-MyD88-dependent and independent signaling pathways
    • Xie G, Welte T, Wang J, et al. A West Nile virus NS4B-P38G mutant strain induces adaptive immunity via TLR7-MyD88-dependent and independent signaling pathways. Vaccine 2013; doi:pii: S0264-410X(13)00903-1. 10.1016
    • (2013) Vaccine
    • Xie, G.1    Welte, T.2    Wang, J.3
  • 165
    • 84875908991 scopus 로고    scopus 로고
    • TRPM2 links oxidative stress to NLRP3 inflammasome activation
    • Zhong Z, Zhai Y, Liang S, et al. TRPM2 links oxidative stress to NLRP3 inflammasome activation. Nat Commun 2013; 4: 1611.
    • (2013) Nat Commun , vol.4
    • Zhong, Z.1    Zhai, Y.2    Liang, S.3
  • 166
    • 84872736378 scopus 로고    scopus 로고
    • Long-term clinical course of patients carrying the Q703K mutation in the NLRP3 gene: A case series
    • Vitale A, Lucherini OM, Galeazzi M, Frediani B, Cantarini L. Long-term clinical course of patients carrying the Q703K mutation in the NLRP3 gene: A case series. Clin Exp Rheumatol 2012; 30: 943-6.
    • (2012) Clin Exp Rheumatol , vol.30 , pp. 943-946
    • Vitale, A.1    Lucherini, O.M.2    Galeazzi, M.3    Frediani, B.4    Cantarini, L.5
  • 167
    • 79951517164 scopus 로고    scopus 로고
    • Mutations in the autoinflammatory cryopyrin associated periodic syndrome gene: Epidemiological study and lessons from eight years of genetic analysis in France
    • Cuisset L, Jeru I, Dumont B, et al. Mutations in the autoinflammatory cryopyrin associated periodic syndrome gene: Epidemiological study and lessons from eight years of genetic analysis in France. Ann Rheum Dis 2011; 70: 495-9.
    • (2011) Ann Rheum Dis , vol.70 , pp. 495-499
    • Cuisset, L.1    Jeru, I.2    Dumont, B.3
  • 168
  • 169
    • 84875796225 scopus 로고    scopus 로고
    • Safety and efficacy of canakinumab in Japanese patients with phenotypes of cryopyrinassociated periodic syndrome as established in the first open-label, phase-3 pivotal study (24-week results)
    • Magawa T, Nishikomori R, Takada H, et al. Safety and efficacy of canakinumab in Japanese patients with phenotypes of cryopyrinassociated periodic syndrome as established in the first open-label, phase-3 pivotal study (24-week results). Clin Exp Rheumatol 2013; 31: 302-9.
    • (2013) Clin Exp Rheumatol , vol.31 , pp. 302-309
    • Magawa, T.1    Nishikomori, R.2    Takada, H.3
  • 170
    • 84877598469 scopus 로고    scopus 로고
    • Microarray-based gene expression profiling in patients with cryopyrin-associated periodic syndromes defines a disease-related signature and IL-1-responsive transcripts
    • Balow JE Jr, Ryan JG, Chae JJ, et al. Microarray-based gene expression profiling in patients with cryopyrin-associated periodic syndromes defines a disease-related signature and IL-1-responsive transcripts. Ann Rheum Dis 2013; 2: 1064-70.
    • (2013) Ann Rheum Dis , vol.2 , pp. 1064-1070
    • Balow, J.E.1    Ryan, J.G.2    Chae, J.J.3
  • 171
    • 35248883867 scopus 로고    scopus 로고
    • Differential role and tissue specificity of interleukin-1_gene expression in atherogenesis and lipid metabolism
    • Kamari Y, Werman-Venkert R, Shaish A, et al. Differential role and tissue specificity of interleukin-1_gene expression in atherogenesis and lipid metabolism. Atherosclerosis 2007; 195: 31-8.
    • (2007) Atherosclerosis , vol.195 , pp. 31-38
    • Kamari, Y.1    Werman-Venkert, R.2    Shaish, A.3
  • 172
    • 76349089146 scopus 로고    scopus 로고
    • Vascular smooth muscle cell apoptosis induces interleukin-1-directed inflammation: Effects of hyperlipidemia-mediated inhibition of phagocytosis
    • Clarke MC, Talib S, Figg NL, Bennett MR. Vascular smooth muscle cell apoptosis induces interleukin-1-directed inflammation: Effects of hyperlipidemia-mediated inhibition of phagocytosis. Circ Res 2010; 106: 363-72.
    • (2010) Circ Res , vol.106 , pp. 363-372
    • Clarke, M.C.1    Talib, S.2    Figg, N.L.3    Bennett, M.R.4
  • 173
    • 84883556030 scopus 로고    scopus 로고
    • Towards a role of interleukin-32 in atherosclerosis
    • Heinhuis B, Popa CD, van Tits BL, et al. Towards a role of interleukin-32 in atherosclerosis. Cytokine 2013; doi:pii: S1043-4666(13)00219-6.
    • (2013) Cytokine
    • Heinhuis, B.1    Popa, C.D.2    Van Tits, B.L.3
  • 175
    • 84883304324 scopus 로고    scopus 로고
    • NOD2-Mediated Innate Immune Signaling Regulates the Eicosanoids in Atherosclerosis
    • Jul 18, Epub ahead of print
    • Liu HQ, Zhang XY, Edfeldt K, et al. NOD2-Mediated Innate Immune Signaling Regulates the Eicosanoids in Atherosclerosis. Arterioscler Thromb Vasc Biol. 2013 Jul 18. [Epub ahead of print]
    • (2013) Arterioscler Thromb Vasc Biol
    • Liu, H.Q.1    Zhang, X.Y.2    Edfeldt, K.3
  • 176
    • 80052262707 scopus 로고    scopus 로고
    • Interaction of the inflammasome genes CARD8 and NLRP3 in abdominal aortic aneurysms
    • Roberts RL, Van Rij AM, Phillips LV, et al. Interaction of the inflammasome genes CARD8 and NLRP3 in abdominal aortic aneurysms. Atherosclerosis 2011; 218: 123-6.
    • (2011) Atherosclerosis , vol.218 , pp. 123-126
    • Roberts, R.L.1    Van Rij, A.M.2    Phillips, L.V.3
  • 177
    • 84876067752 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of novel antagonist compounds of Toll-like receptors 7, 8 and 9
    • Kandimalla ER, Bhagat L, Wang D, et al. Design, synthesis and biological evaluation of novel antagonist compounds of Toll-like receptors 7, 8 and 9. Nucleic Acids Res 2013; 41: 3947-61.
    • (2013) Nucleic Acids Res , vol.41 , pp. 3947-3961
    • Kandimalla, E.R.1    Bhagat, L.2    Wang, D.3


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