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Volumn 133, Issue 1, 2011, Pages 51-61

Cytoadherence-dependent induction of inflammatory responses by Mycoplasma pneumoniae

Author keywords

Cytoadherence; Inflammasome; Mycoplasma; THP 1; Toll like receptors

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYTOKINE; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; TUMOR NECROSIS FACTOR ALPHA;

EID: 79953297477     PISSN: 00192805     EISSN: 13652567     Source Type: Journal    
DOI: 10.1111/j.1365-2567.2011.03408.x     Document Type: Article
Times cited : (44)

References (62)
  • 1
    • 0027121315 scopus 로고
    • Peculiar properties of mycoplasmas: the smallest self-replicating prokaryotes
    • Razin S. Peculiar properties of mycoplasmas: the smallest self-replicating prokaryotes. FEMS Microbiol Lett 1992; 79:423-31.
    • (1992) FEMS Microbiol Lett , vol.79 , pp. 423-431
    • Razin, S.1
  • 2
    • 5644300391 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae and its role as a human pathogen
    • table of contents.
    • Waites KB, Talkington DF. Mycoplasma pneumoniae and its role as a human pathogen. Clin Microbiol Rev 2004; 17:697-728, table of contents.
    • (2004) Clin Microbiol Rev , vol.17 , pp. 697-728
    • Waites, K.B.1    Talkington, D.F.2
  • 5
    • 0002693276 scopus 로고
    • Pathgenic determinant and mechanisms
    • In: Maniloff J, McElhaney RN, Finch LR, Baseman JB, eds. Washington, D.C: American Society for Microbiology
    • Tryon VV, Baseman JB. Pathgenic determinant and mechanisms. In: Maniloff J, McElhaney RN, Finch LR, Baseman JB, eds. Mycoplasmas - Molecular Biology and Pathogenesis. Washington, D.C: American Society for Microbiology, 1992:457-89.
    • (1992) Mycoplasmas - Molecular Biology and Pathogenesis , pp. 457-489
    • Tryon, V.V.1    Baseman, J.B.2
  • 6
    • 37749005389 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae-derived lipopeptides induce acute inflammatory responses in the lungs of mice
    • Shimizu T, Kida Y, Kuwano K. Mycoplasma pneumoniae-derived lipopeptides induce acute inflammatory responses in the lungs of mice. Infect Immun 2008; 76:270-7.
    • (2008) Infect Immun , vol.76 , pp. 270-277
    • Shimizu, T.1    Kida, Y.2    Kuwano, K.3
  • 7
    • 25444505635 scopus 로고    scopus 로고
    • A dipalmitoylated lipoprotein from Mycoplasma pneumoniae activates NF-kappa B through TLR1, TLR2, and TLR6
    • Shimizu T, Kida Y, Kuwano K. A dipalmitoylated lipoprotein from Mycoplasma pneumoniae activates NF-kappa B through TLR1, TLR2, and TLR6. J Immunol 2005; 175:4641-6.
    • (2005) J Immunol , vol.175 , pp. 4641-4646
    • Shimizu, T.1    Kida, Y.2    Kuwano, K.3
  • 8
    • 34447108077 scopus 로고    scopus 로고
    • Triacylated lipoproteins derived from Mycoplasma pneumoniae activate nuclear factor-kappaB through toll-like receptors 1 and 2
    • Shimizu T, Kida Y, Kuwano K. Triacylated lipoproteins derived from Mycoplasma pneumoniae activate nuclear factor-kappaB through toll-like receptors 1 and 2. Immunology 2007; 121:473-83.
    • (2007) Immunology , vol.121 , pp. 473-483
    • Shimizu, T.1    Kida, Y.2    Kuwano, K.3
  • 9
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signaling
    • Akira S, Takeda K. Toll-like receptor signaling. Nat Rev Immunol 2004; 4:499-511.
    • (2004) Nat Rev Immunol , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 10
    • 0033067894 scopus 로고    scopus 로고
    • The toll-receptor family and control of innate immunity
    • Kopp EB, Medzhitov R. The toll-receptor family and control of innate immunity. Curr Opin Immunol 1999; 11:13-8.
    • (1999) Curr Opin Immunol , vol.11 , pp. 13-18
    • Kopp, E.B.1    Medzhitov, R.2
  • 11
    • 0033618630 scopus 로고    scopus 로고
    • Cell activation and apoptosis by bacterial lipoproteins through toll-like receptor-2
    • Aliprantis AO, Yang RB, Mark MR et al. Cell activation and apoptosis by bacterial lipoproteins through toll-like receptor-2. Science 1999; 285:736-9.
    • (1999) Science , vol.285 , pp. 736-739
    • Aliprantis, A.O.1    Yang, R.B.2    Mark, M.R.3
  • 12
    • 0033618562 scopus 로고    scopus 로고
    • Host defense mechanisms triggered by microbial lipoproteins through toll-like receptors
    • Brightbill HD, Libraty DH, Krutzik SR et al. Host defense mechanisms triggered by microbial lipoproteins through toll-like receptors. Science 1999; 285:732-6.
    • (1999) Science , vol.285 , pp. 732-736
    • Brightbill, H.D.1    Libraty, D.H.2    Krutzik, S.R.3
  • 13
    • 0033585011 scopus 로고    scopus 로고
    • Toll-like receptor 2 functions as a pattern recognition receptor for diverse bacterial products
    • Lien E, Sellati TJ, Yoshimura A et al. Toll-like receptor 2 functions as a pattern recognition receptor for diverse bacterial products. J Biol Chem 1999; 274:33419-25.
    • (1999) J Biol Chem , vol.274 , pp. 33419-33425
    • Lien, E.1    Sellati, T.J.2    Yoshimura, A.3
  • 14
    • 0032716031 scopus 로고    scopus 로고
    • The CD14 ligands lipoarabinomannan and lipopolysaccharide differ in their requirement for toll-like receptors
    • Means TK, Lien E, Yoshimura A, Wang S, Golenbock DT, Fenton MJ. The CD14 ligands lipoarabinomannan and lipopolysaccharide differ in their requirement for toll-like receptors. J Immunol 1999; 163:6748-55.
    • (1999) J Immunol , vol.163 , pp. 6748-6755
    • Means, T.K.1    Lien, E.2    Yoshimura, A.3    Wang, S.4    Golenbock, D.T.5    Fenton, M.J.6
  • 15
    • 0033213590 scopus 로고    scopus 로고
    • Differential roles of TLR2 and TLR4 in recognition of gram-negative and gram-positive bacterial cell wall components
    • Takeuchi O, Hoshino K, Kawai T, Sanjo H, Takada H, Ogawa T, Takeda K, Akira S. Differential roles of TLR2 and TLR4 in recognition of gram-negative and gram-positive bacterial cell wall components. Immunity 1999; 11:443-51.
    • (1999) Immunity , vol.11 , pp. 443-451
    • Takeuchi, O.1    Hoshino, K.2    Kawai, T.3    Sanjo, H.4    Takada, H.5    Ogawa, T.6    Takeda, K.7    Akira, S.8
  • 16
    • 0034650420 scopus 로고    scopus 로고
    • Preferentially the R-stereoisomer of the mycoplasmal lipopeptide macrophage-activating lipopeptide-2 activates immune cells through a toll-like receptor 2- and MyD88-dependent signaling pathway
    • Takeuchi O, Kaufmann A, Grote K, Kawai T, Hoshino K, Morr M, Muhlradt PF, Akira S. Preferentially the R-stereoisomer of the mycoplasmal lipopeptide macrophage-activating lipopeptide-2 activates immune cells through a toll-like receptor 2- and MyD88-dependent signaling pathway. J Immunol 2000; 164:554-7.
    • (2000) J Immunol , vol.164 , pp. 554-557
    • Takeuchi, O.1    Kaufmann, A.2    Grote, K.3    Kawai, T.4    Hoshino, K.5    Morr, M.6    Muhlradt, P.F.7    Akira, S.8
  • 18
    • 0035953543 scopus 로고    scopus 로고
    • The innate immune response to bacterial flagellin is mediated by toll-like receptor 5
    • Hayashi F, Smith KD, Ozinsky A et al. The innate immune response to bacterial flagellin is mediated by toll-like receptor 5. Nature 2001; 410:1099-103.
    • (2001) Nature , vol.410 , pp. 1099-1103
    • Hayashi, F.1    Smith, K.D.2    Ozinsky, A.3
  • 19
    • 0034619794 scopus 로고    scopus 로고
    • A toll-like receptor recognizes bacterial DNA
    • Hemmi H, Takeuchi O, Kawai T et al. A toll-like receptor recognizes bacterial DNA. Nature 2000; 408:740-5.
    • (2000) Nature , vol.408 , pp. 740-745
    • Hemmi, H.1    Takeuchi, O.2    Kawai, T.3
  • 20
    • 0033120081 scopus 로고    scopus 로고
    • Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: evidence for TLR4 as the Lps gene product
    • Hoshino K, Takeuchi O, Kawai T, Sanjo H, Ogawa T, Takeda Y, Takeda K, Akira S. Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: evidence for TLR4 as the Lps gene product. J Immunol 1999; 162:3749-52.
    • (1999) J Immunol , vol.162 , pp. 3749-3752
    • Hoshino, K.1    Takeuchi, O.2    Kawai, T.3    Sanjo, H.4    Ogawa, T.5    Takeda, Y.6    Takeda, K.7    Akira, S.8
  • 21
    • 0032509295 scopus 로고    scopus 로고
    • Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene
    • Poltorak A, He X, Smirnova I et al. Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene. Science 1998; 282:2085-8.
    • (1998) Science , vol.282 , pp. 2085-2088
    • Poltorak, A.1    He, X.2    Smirnova, I.3
  • 23
    • 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
  • 24
  • 25
    • 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; 38:240-4.
    • (2006) Nat Genet , vol.38 , pp. 240-244
    • Boyden, E.D.1    Dietrich, W.F.2
  • 26
    • 7944232105 scopus 로고    scopus 로고
    • Identification of bacterial muramyl dipeptide as activator of the NALP3/cryopyrin inflammasome
    • Martinon F, Agostini L, Meylan E, Tschopp J. Identification of bacterial muramyl dipeptide as activator of the NALP3/cryopyrin inflammasome. Curr Biol 2004; 14:1929-34.
    • (2004) Curr Biol , vol.14 , pp. 1929-1934
    • Martinon, F.1    Agostini, L.2    Meylan, E.3    Tschopp, J.4
  • 27
    • 34548679608 scopus 로고    scopus 로고
    • TLR5 and Ipaf: dual sensors of bacterial flagellin in the innate immune system
    • Miao EA, Andersen-Nissen E, Warren SE, Aderem A. TLR5 and Ipaf: dual sensors of bacterial flagellin in the innate immune system. Semin Immunopathol 2007; 29:275-88.
    • (2007) Semin Immunopathol , vol.29 , pp. 275-288
    • Miao, E.A.1    Andersen-Nissen, E.2    Warren, S.E.3    Aderem, A.4
  • 28
    • 32944470765 scopus 로고    scopus 로고
    • Cryopyrin activates the inflammasome in response to toxins and ATP
    • Mariathasan S, Weiss DS, Newton K et al. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 2006; 440:228-32.
    • (2006) Nature , vol.440 , pp. 228-232
    • Mariathasan, S.1    Weiss, D.S.2    Newton, K.3
  • 29
    • 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 et al. Critical role for NALP3/CIAS1/Cryopyrin in innate and adaptive immunity through its regulation of caspase-1. Immunity 2006; 24:317-27.
    • (2006) Immunity , vol.24 , pp. 317-327
    • Sutterwala, F.S.1    Ogura, Y.2    Szczepanik, M.3
  • 30
    • 32944462834 scopus 로고    scopus 로고
    • Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3
    • Kanneganti TD, Ozoren N, Body-Malapel M et al. Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3. Nature 2006; 440:233-6.
    • (2006) Nature , vol.440 , pp. 233-236
    • Kanneganti, T.D.1    Ozoren, N.2    Body-Malapel, M.3
  • 31
    • 34547101484 scopus 로고    scopus 로고
    • + for caspase-1 activation induced by intracellular and extracellular bacteria
    • + for caspase-1 activation induced by intracellular and extracellular bacteria. J Biol Chem 2007; 282:18810-8.
    • (2007) J Biol Chem , vol.282 , pp. 18810-18818
    • Franchi, L.1    Kanneganti, T.D.2    Dubyak, G.R.3    Nunez, G.4
  • 32
    • 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, Chen G, Park JH, Franchi L, Vandenabeele P, Nunez G. 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    Chen, G.4    Park, J.H.5    Franchi, L.6    Vandenabeele, P.7    Nunez, G.8
  • 34
    • 64049111768 scopus 로고    scopus 로고
    • The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA
    • Allen IC, Scull MA, Moore CB et al. The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA. Immunity 2009; 30:556-65.
    • (2009) Immunity , vol.30 , pp. 556-565
    • Allen, I.C.1    Scull, M.A.2    Moore, C.B.3
  • 35
    • 0035917471 scopus 로고    scopus 로고
    • Structure, function, and assembly of the terminal organelle of Mycoplasma pneumoniae
    • Krause DC, Balish MF. Structure, function, and assembly of the terminal organelle of Mycoplasma pneumoniae. FEMS Microbiol Lett 2001; 198:1-7.
    • (2001) FEMS Microbiol Lett , vol.198 , pp. 1-7
    • Krause, D.C.1    Balish, M.F.2
  • 36
    • 0002084168 scopus 로고    scopus 로고
    • Cytoadherence and the cytoskeleton
    • In: Razin S, Herrmann R, eds. New York: Kluwer Academic/Plenum Publishers
    • Balish MF, Krause DC. Cytoadherence and the cytoskeleton. In: Razin S, Herrmann R, eds. Molecular Biology and Pathogenicity of Mycoplasmas. New York: Kluwer Academic/Plenum Publishers, 2002:491-518.
    • (2002) Molecular Biology and Pathogenicity of Mycoplasmas , pp. 491-518
    • Balish, M.F.1    Krause, D.C.2
  • 37
    • 37749037745 scopus 로고    scopus 로고
    • Centipede and inchworm models to explain Mycoplasma gliding
    • Miyata M. Centipede and inchworm models to explain Mycoplasma gliding. Trends Microbiol 2008; 16:6-12.
    • (2008) Trends Microbiol , vol.16 , pp. 6-12
    • Miyata, M.1
  • 38
    • 64149110284 scopus 로고    scopus 로고
    • Molecular mechanism of mycoplasma gliding - a novel cell motility system
    • In: Lenz P, ed. New York: Springer Science
    • Miyata M. Molecular mechanism of mycoplasma gliding - a novel cell motility system. In: Lenz P, ed. Cell Motility. New York: Springer Science, 2008:137-75.
    • (2008) Cell Motility , pp. 137-175
    • Miyata, M.1
  • 39
    • 26244468736 scopus 로고    scopus 로고
    • A role for the Mycoplasma pneumoniae adhesin P1 in interleukin (IL)-4 synthesis and release from rodent mast cells
    • Hoek KL, Duffy LB, Cassell GH, Dai Y, Atkinson TP. A role for the Mycoplasma pneumoniae adhesin P1 in interleukin (IL)-4 synthesis and release from rodent mast cells. Microb Pathog 2005; 39:149-58.
    • (2005) Microb Pathog , vol.39 , pp. 149-158
    • Hoek, K.L.1    Duffy, L.B.2    Cassell, G.H.3    Dai, Y.4    Atkinson, T.P.5
  • 40
    • 0036081410 scopus 로고    scopus 로고
    • Regulation of proinflammatory cytokines in human lung epithelial cells infected with Mycoplasma pneumoniae
    • Yang J, Hooper WC, Phillips DJ, Talkington DF. Regulation of proinflammatory cytokines in human lung epithelial cells infected with Mycoplasma pneumoniae. Infect Immun 2002; 70:3649-55.
    • (2002) Infect Immun , vol.70 , pp. 3649-3655
    • Yang, J.1    Hooper, W.C.2    Phillips, D.J.3    Talkington, D.F.4
  • 41
    • 0037307792 scopus 로고    scopus 로고
    • Attachment organelle formation represented by localization of cytoadherence proteins and formation of the electron-dense core in wild-type and mutant strains of Mycoplasma pneumoniae
    • Seto S, Miyata M. Attachment organelle formation represented by localization of cytoadherence proteins and formation of the electron-dense core in wild-type and mutant strains of Mycoplasma pneumoniae. J Bacteriol 2003; 185:1082-91.
    • (2003) J Bacteriol , vol.185 , pp. 1082-1091
    • Seto, S.1    Miyata, M.2
  • 42
    • 0032922904 scopus 로고    scopus 로고
    • The 40- and 90-kDa membrane proteins (ORF6 gene product) of Mycoplasma pneumoniae are responsible for the tip structure formation and P1 (adhesin) association with the Triton shell
    • Layh-Schmitt G, Harkenthal M. The 40- and 90-kDa membrane proteins (ORF6 gene product) of Mycoplasma pneumoniae are responsible for the tip structure formation and P1 (adhesin) association with the Triton shell. FEMS Microbiol Lett 1999; 174:143-9.
    • (1999) FEMS Microbiol Lett , vol.174 , pp. 143-149
    • Layh-Schmitt, G.1    Harkenthal, M.2
  • 43
    • 0028932035 scopus 로고
    • A spontaneous hemadsorption-negative mutant of Mycoplasma pneumoniae exhibits a truncated adhesin-related 30-kilodalton protein and lacks the cytadherence-accessory protein HMW1
    • Layh-Schmitt G, Hilbert H, Pirkl E. A spontaneous hemadsorption-negative mutant of Mycoplasma pneumoniae exhibits a truncated adhesin-related 30-kilodalton protein and lacks the cytadherence-accessory protein HMW1. J Bacteriol 1995; 177:843-6.
    • (1995) J Bacteriol , vol.177 , pp. 843-846
    • Layh-Schmitt, G.1    Hilbert, H.2    Pirkl, E.3
  • 44
    • 0033057626 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae protein P30 is required for cytadherence and associated with proper cell development
    • Romero-Arroyo CE, Jordan J, Peacock SJ, Willby MJ, Farmer MA, Krause DC. Mycoplasma pneumoniae protein P30 is required for cytadherence and associated with proper cell development. J Bacteriol 1999; 181:1079-87.
    • (1999) J Bacteriol , vol.181 , pp. 1079-1087
    • Romero-Arroyo, C.E.1    Jordan, J.2    Peacock, S.J.3    Willby, M.J.4    Farmer, M.A.5    Krause, D.C.6
  • 45
    • 0035212227 scopus 로고    scopus 로고
    • Stability and subcellular localization of cytadherence-associated protein P65 in Mycoplasma pneumoniae
    • Jordan JL, Berry KM, Balish MF, Krause DC. Stability and subcellular localization of cytadherence-associated protein P65 in Mycoplasma pneumoniae. J Bacteriol 2001; 183:7387-91.
    • (2001) J Bacteriol , vol.183 , pp. 7387-7391
    • Jordan, J.L.1    Berry, K.M.2    Balish, M.F.3    Krause, D.C.4
  • 46
    • 0017079130 scopus 로고
    • Synergistic effect of colchicine and cytochalasin D on phagocytosis by peritoneal macrophages
    • Mimura N, Asano A. Synergistic effect of colchicine and cytochalasin D on phagocytosis by peritoneal macrophages. Nature 1976; 261:319-21.
    • (1976) Nature , vol.261 , pp. 319-321
    • Mimura, N.1    Asano, A.2
  • 47
    • 0011913143 scopus 로고
    • Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • Bowman EJ, Siebers A, Altendorf K. Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc Natl Acad Sci USA 1988; 85:7972-6.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 48
    • 15844393942 scopus 로고    scopus 로고
    • Activation of the native 45-kDa precursor form of interleukin-1-converting enzyme
    • Yamin TT, Ayala JM, Miller DK. Activation of the native 45-kDa precursor form of interleukin-1-converting enzyme. J Biol Chem 1996; 271:13273-82.
    • (1996) J Biol Chem , vol.271 , pp. 13273-13282
    • Yamin, T.T.1    Ayala, J.M.2    Miller, D.K.3
  • 50
    • 0035830853 scopus 로고    scopus 로고
    • ATP-stimulated release of interleukin (IL)-1beta and IL-18 requires priming by lipopolysaccharide and is independent of caspase-1 cleavage
    • Mehta VB, Hart J, Wewers MD. ATP-stimulated release of interleukin (IL)-1beta and IL-18 requires priming by lipopolysaccharide and is independent of caspase-1 cleavage. J Biol Chem 2001; 276:3820-6.
    • (2001) J Biol Chem , vol.276 , pp. 3820-3826
    • Mehta, V.B.1    Hart, J.2    Wewers, M.D.3
  • 51
    • 0036035454 scopus 로고    scopus 로고
    • Extracellular ATP regulates cell death of lymphocytes and monocytes induced by membrane-bound lipoproteins of Mycoplasma fermentans and Mycoplasma salivarium
    • Into T, Okada K, Inoue N, Yasuda M, Shibata K. Extracellular ATP regulates cell death of lymphocytes and monocytes induced by membrane-bound lipoproteins of Mycoplasma fermentans and Mycoplasma salivarium. Microbiol Immunol 2002; 46:667-75.
    • (2002) Microbiol Immunol , vol.46 , pp. 667-675
    • Into, T.1    Okada, K.2    Inoue, N.3    Yasuda, M.4    Shibata, K.5
  • 52
    • 0037593535 scopus 로고    scopus 로고
    • Colocalization of ATP release sites and ecto-ATPase activity at the extracellular surface of human astrocytes
    • Joseph SM, Buchakjian MR, Dubyak GR. Colocalization of ATP release sites and ecto-ATPase activity at the extracellular surface of human astrocytes. J Biol Chem 2003; 278:23331-42.
    • (2003) J Biol Chem , vol.278 , pp. 23331-23342
    • Joseph, S.M.1    Buchakjian, M.R.2    Dubyak, G.R.3
  • 54
    • 69549119940 scopus 로고    scopus 로고
    • Molecular mechanisms involved in inflammasome activation
    • Bryant C, Fitzgerald KA. Molecular mechanisms involved in inflammasome activation. Trends Cell Biol 2009; 19:455-64.
    • (2009) Trends Cell Biol , vol.19 , pp. 455-464
    • Bryant, C.1    Fitzgerald, K.A.2
  • 55
    • 74549206702 scopus 로고    scopus 로고
    • How the noninflammasome NLRs function in the innate immune system
    • Ting JP, Duncan JA, Lei Y. How the noninflammasome NLRs function in the innate immune system. Science 2010; 327:286-90.
    • (2010) Science , vol.327 , pp. 286-290
    • Ting, J.P.1    Duncan, J.A.2    Lei, Y.3
  • 59
    • 45849102043 scopus 로고    scopus 로고
    • ATP is released by monocytes stimulated with pathogen-sensing receptor ligands and induces IL-1beta and IL-18 secretion in an autocrine way
    • Piccini A, Carta S, Tassi S, Lasiglie D, Fossati G, Rubartelli A. ATP is released by monocytes stimulated with pathogen-sensing receptor ligands and induces IL-1beta and IL-18 secretion in an autocrine way. Proc Natl Acad Sci USA 2008; 105:8067-72.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8067-8072
    • Piccini, A.1    Carta, S.2    Tassi, S.3    Lasiglie, D.4    Fossati, G.5    Rubartelli, A.6
  • 60
    • 0029979369 scopus 로고    scopus 로고
    • Biologic basis for interleukin-1 in disease
    • Dinarello CA. Biologic basis for interleukin-1 in disease. Blood 1996; 87:2095-147.
    • (1996) Blood , vol.87 , pp. 2095-2147
    • Dinarello, C.A.1
  • 61
    • 0032989434 scopus 로고    scopus 로고
    • Converting enzyme-independent release of tumor necrosis factor alpha and IL-1beta from a stimulated human monocytic cell line in the presence of activated neutrophils or purified proteinase 3
    • Coeshott C, Ohnemus C, Pilyavskaya A, Ross S, Wieczorek M, Kroona H, Leimer AH, Cheronis J. Converting enzyme-independent release of tumor necrosis factor alpha and IL-1beta from a stimulated human monocytic cell line in the presence of activated neutrophils or purified proteinase 3. Proc Natl Acad Sci USA 1999; 96:6261-6.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6261-6266
    • Coeshott, C.1    Ohnemus, C.2    Pilyavskaya, A.3    Ross, S.4    Wieczorek, M.5    Kroona, H.6    Leimer, A.H.7    Cheronis, J.8
  • 62
    • 34548225362 scopus 로고    scopus 로고
    • NF-kappaB is a negative regulator of IL-1beta secretion as revealed by genetic and pharmacological inhibition of IKKbeta
    • Greten FR, Arkan MC, Bollrath J et al. NF-kappaB is a negative regulator of IL-1beta secretion as revealed by genetic and pharmacological inhibition of IKKbeta. Cell 2007; 130:918-31.
    • (2007) Cell , vol.130 , pp. 918-931
    • Greten, F.R.1    Arkan, M.C.2    Bollrath, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.