메뉴 건너뛰기




Volumn 63, Issue 9, 2008, Pages 1110-1123

How epithelial cells detect danger: Aiding the immune response

Author keywords

Allergy; Epithelium; Immune response; Receptors

Indexed keywords

CASPASE RECRUITMENT DOMAIN PROTEIN 15; CASPASE RECRUITMENT DOMAIN PROTEIN 4; CYTOPLASMIC RECEPTOR; PROTEINASE ACTIVATED RECEPTOR; PROTEINASE ACTIVATED RECEPTOR 1; PROTEINASE ACTIVATED RECEPTOR 2; PROTEINASE ACTIVATED RECEPTOR 3; PROTEINASE ACTIVATED RECEPTOR 4; TOLL LIKE RECEPTOR;

EID: 49249094671     PISSN: 01054538     EISSN: 13989995     Source Type: Journal    
DOI: 10.1111/j.1398-9995.2008.01785.x     Document Type: Review
Times cited : (66)

References (119)
  • 1
    • 0031765381 scopus 로고    scopus 로고
    • Role of fimbriae-mediated adherence for neutrophil migration across Escherichia coli-infected epithelial cell layers
    • Godaly G., Frendeus B, Proudfoot A, Svensson M, Klemm P, Svanborg C. Role of fimbriae-mediated adherence for neutrophil migration across Escherichia coli-infected epithelial cell layers. Mol Microbiol 1998 30: 725 735.
    • (1998) Mol Microbiol , vol.30 , pp. 725-735
    • Godaly, G.1    Frendeus, B.2    Proudfoot, A.3    Svensson, M.4    Klemm, P.5    Svanborg, C.6
  • 2
    • 0031461206 scopus 로고    scopus 로고
    • Epithelial cells as sensors for microbial infection
    • Kagnoff MF, Eckmann L. Epithelial cells as sensors for microbial infection. J Clin Invest 1997 100: 6 10.
    • (1997) J Clin Invest , vol.100 , pp. 6-10
    • Kagnoff, M.F.1    Eckmann, L.2
  • 3
    • 0030595339 scopus 로고    scopus 로고
    • The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults
    • Lemaitre B, Nicolas E, Michaut L, Reichhart JM, Hoffmann JA. The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 1996 86: 973 983.
    • (1996) Cell , vol.86 , pp. 973-983
    • Lemaitre, B.1    Nicolas, E.2    Michaut, L.3    Reichhart, J.M.4    Hoffmann, J.A.5
  • 4
    • 0024299087 scopus 로고
    • The Toll gene of Drosophila, required for dorsal-ventral embryonic polarity, appears to encode a transmembrane protein
    • Hashimoto C, Hudson KL, Anderson KV. The Toll gene of Drosophila, required for dorsal-ventral embryonic polarity, appears to encode a transmembrane protein. Cell 1988 52: 269 279.
    • (1988) Cell , vol.52 , pp. 269-279
    • Hashimoto, C.1    Hudson, K.L.2    Anderson, K.V.3
  • 5
    • 0036952124 scopus 로고    scopus 로고
    • Tissue and stage-specific expression of the Tolls in Drosophila embryos
    • Kambris Z, Hoffmann JA, Imler JL, Capovilla M. Tissue and stage-specific expression of the Tolls in Drosophila embryos. Gene Expr Patterns 2002 2: 311 317.
    • (2002) Gene Expr Patterns , vol.2 , pp. 311-317
    • Kambris, Z.1    Hoffmann, J.A.2    Imler, J.L.3    Capovilla, M.4
  • 6
    • 0031446642 scopus 로고    scopus 로고
    • Drosophila host defense: Differential induction of antimicrobial peptide genes after infection by various classes of microorganisms
    • Lemaitre B, Reichhart JM, Hoffmann JA. Drosophila host defense: differential induction of antimicrobial peptide genes after infection by various classes of microorganisms. Proc Natl Acad Sci USA 1997 94: 14614 14619.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14614-14619
    • Lemaitre, B.1    Reichhart, J.M.2    Hoffmann, J.A.3
  • 8
    • 0025774776 scopus 로고
    • Drosophila Toll and IL-1 receptor
    • Gay NJ, Keith FJ. Drosophila Toll and IL-1 receptor. Nature 1991 351: 355 356.
    • (1991) Nature , vol.351 , pp. 355-356
    • Gay, N.J.1    Keith, F.J.2
  • 9
    • 23044445303 scopus 로고    scopus 로고
    • Crystal structure of human toll-like receptor 3 (TLR3) ectodomain
    • Choe J, Kelker MS, Wilson IA. Crystal structure of human toll-like receptor 3 (TLR3) ectodomain. Science 2005 309: 581 585.
    • (2005) Science , vol.309 , pp. 581-585
    • Choe, J.1    Kelker, M.S.2    Wilson, I.A.3
  • 10
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe B, Kajava AV. The leucine-rich repeat as a protein recognition motif. Curr Opin Struct Biol 2001 11: 725 732.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 11
    • 2942627626 scopus 로고    scopus 로고
    • Hydrophobicity: An ancient damage-associated molecular pattern that initiates innate immune responses
    • Seong SY, Matzinger P. Hydrophobicity: an ancient damage-associated molecular pattern that initiates innate immune responses. Nat Rev Immunol 2004 4: 469 478.
    • (2004) Nat Rev Immunol , vol.4 , pp. 469-478
    • Seong, S.Y.1    Matzinger, P.2
  • 13
    • 0033532629 scopus 로고    scopus 로고
    • MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4
    • Shimazu R, Akashi S, Ogata H, Nagai Y, Fukudome K, Miyake K et al. MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J Exp Med 1999 189: 1777 1782.
    • (1999) J Exp Med , vol.189 , pp. 1777-1782
    • Shimazu, R.1    Akashi, S.2    Ogata, H.3    Nagai, Y.4    Fukudome, K.5    Miyake, K.6
  • 14
    • 0025166114 scopus 로고
    • CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein
    • Wright SD, Ramos RA, Tobias PS, Ulevitch RJ, Mathison JC. CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein. Science 1990 249: 1431 1433.
    • (1990) Science , vol.249 , pp. 1431-1433
    • Wright, S.D.1    Ramos, R.A.2    Tobias, P.S.3    Ulevitch, R.J.4    Mathison, J.C.5
  • 15
    • 0036672050 scopus 로고    scopus 로고
    • TLR4-dependent recognition of lipopolysaccharide by epithelial cells requires sCD14
    • Backhed F, Meijer L, Normark S, Richter-Dahlfors A. TLR4-dependent recognition of lipopolysaccharide by epithelial cells requires sCD14. Cell Microbiol 2002 4: 493 501.
    • (2002) Cell Microbiol , vol.4 , pp. 493-501
    • Backhed, F.1    Meijer, L.2    Normark, S.3    Richter-Dahlfors, A.4
  • 16
    • 4344627821 scopus 로고    scopus 로고
    • Endogenous ligands of Toll-like receptors
    • Tsan MF, Gao B. Endogenous ligands of Toll-like receptors. J Leukoc Biol 2004 76: 514 519.
    • (2004) J Leukoc Biol , vol.76 , pp. 514-519
    • Tsan, M.F.1    Gao, B.2
  • 17
    • 0034650427 scopus 로고    scopus 로고
    • Cutting edge: Heat shock protein 60 is a putative endogenous ligand of the toll-like receptor-4 complex
    • Ohashi K, Burkart V, Flohe S, Kolb H. Cutting edge: heat shock protein 60 is a putative endogenous ligand of the toll-like receptor-4 complex. J Immunol 2000 164: 558 561.
    • (2000) J Immunol , vol.164 , pp. 558-561
    • Ohashi, K.1    Burkart, V.2    Flohe, S.3    Kolb, H.4
  • 18
    • 0037177825 scopus 로고    scopus 로고
    • Novel signal transduction pathway utilized by extracellular HSP70: Role of toll-like receptor (TLR) 2 and TLR4
    • Asea A, Rehli M, Kabingu E, Boch JA, Bare O, Auron PE et al. Novel signal transduction pathway utilized by extracellular HSP70: role of toll-like receptor (TLR) 2 and TLR4. J Biol Chem 2002 277: 15028 15034.
    • (2002) J Biol Chem , vol.277 , pp. 15028-15034
    • Asea, A.1    Rehli, M.2    Kabingu, E.3    Boch, J.A.4    Bare, O.5    Auron, P.E.6
  • 19
    • 0037097672 scopus 로고    scopus 로고
    • Cutting edge: The immunostimulatory activity of the lung surfactant protein-A involves Toll-like receptor 4
    • Guillot L, Balloy V, McCormack FX, Golenbock DT, Chignard M, Si-Tahar M. Cutting edge: the immunostimulatory activity of the lung surfactant protein-A involves Toll-like receptor 4. J Immunol 2002 168: 5989 5992.
    • (2002) J Immunol , vol.168 , pp. 5989-5992
    • Guillot, L.1    Balloy, V.2    McCormack, F.X.3    Golenbock, D.T.4    Chignard, M.5    Si-Tahar, M.6
  • 20
    • 0034669971 scopus 로고    scopus 로고
    • Toll-like receptor 4, but not toll-like receptor 2, is a signaling receptor for Escherichia and Salmonella lipopolysaccharides
    • Tapping RI, Akashi S, Miyake K, Godowski PJ, Tobias PS. Toll-like receptor 4, but not toll-like receptor 2, is a signaling receptor for Escherichia and Salmonella lipopolysaccharides. J Immunol 2000 165: 5780 5787.
    • (2000) J Immunol , vol.165 , pp. 5780-5787
    • Tapping, R.I.1    Akashi, S.2    Miyake, K.3    Godowski, P.J.4    Tobias, P.S.5
  • 21
    • 0034662239 scopus 로고    scopus 로고
    • Cutting edge: Repurification of lipopolysaccharide eliminates signaling through both human and murine toll-like receptor 2
    • Hirschfeld M, Ma Y, Weis JH, Vogel SN, Weis JJ. Cutting edge: repurification of lipopolysaccharide eliminates signaling through both human and murine toll-like receptor 2. J Immunol 2000 165: 618 622.
    • (2000) J Immunol , vol.165 , pp. 618-622
    • Hirschfeld, M.1    Ma, Y.2    Weis, J.H.3    Vogel, S.N.4    Weis, J.J.5
  • 22
    • 7944220803 scopus 로고    scopus 로고
    • Toll-like receptor 2-dependent bacterial sensing does not occur via peptidoglycan recognition
    • Travassos LH, Girardin SE, Philpott DJ, Blanot D, Nahori MA, Werts C et al. Toll-like receptor 2-dependent bacterial sensing does not occur via peptidoglycan recognition. EMBO Rep 2004 5: 1000 1006.
    • (2004) EMBO Rep , vol.5 , pp. 1000-1006
    • Travassos, L.H.1    Girardin, S.E.2    Philpott, D.J.3    Blanot, D.4    Nahori, M.A.5    Werts, C.6
  • 23
    • 0031423761 scopus 로고    scopus 로고
    • MyD88: An adapter that recruits IRAK to the IL-1 receptor complex
    • Wesche H, Henzel WJ, Shillinglaw W, Li S, Cao Z. MyD88: an adapter that recruits IRAK to the IL-1 receptor complex. Immunity 1997 7: 837 847.
    • (1997) Immunity , vol.7 , pp. 837-847
    • Wesche, H.1    Henzel, W.J.2    Shillinglaw, W.3    Li, S.4    Cao, Z.5
  • 24
    • 0034597766 scopus 로고    scopus 로고
    • Structural basis for signal transduction by the Toll/interleukin-1 receptor domains
    • Xu Y, Tao X, Shen B, Horng T, Medzhitov R, Manley JL et al. Structural basis for signal transduction by the Toll/interleukin-1 receptor domains. Nature 2000 408: 111 115.
    • (2000) Nature , vol.408 , pp. 111-115
    • Xu, Y.1    Tao, X.2    Shen, B.3    Horng, T.4    Medzhitov, R.5    Manley, J.L.6
  • 25
    • 0034681434 scopus 로고    scopus 로고
    • Identification of two major sites in the type I interleukin-1 receptor cytoplasmic region responsible for coupling to pro-inflammatory signaling pathways
    • Slack JL, Schooley K, Bonnert TP, Mitcham JL, Qwarnstrom EE, Sims JE et al. Identification of two major sites in the type I interleukin-1 receptor cytoplasmic region responsible for coupling to pro-inflammatory signaling pathways. J Biol Chem 2000 275: 4670 4678.
    • (2000) J Biol Chem , vol.275 , pp. 4670-4678
    • Slack, J.L.1    Schooley, K.2    Bonnert, T.P.3    Mitcham, J.L.4    Qwarnstrom, E.E.5    Sims, J.E.6
  • 26
    • 0033583034 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharide activates nuclear factor-kappaB through interleukin-1 signaling mediators in cultured human dermal endothelial cells and mononuclear phagocytes
    • Zhang FX, Kirschning CJ, Mancinelli R, Xu XP, Jin Y, Faure E et al. Bacterial lipopolysaccharide activates nuclear factor-kappaB through interleukin-1 signaling mediators in cultured human dermal endothelial cells and mononuclear phagocytes. J Biol Chem 1999 274: 7611 7614.
    • (1999) J Biol Chem , vol.274 , pp. 7611-7614
    • Zhang, F.X.1    Kirschning, C.J.2    Mancinelli, R.3    Xu, X.P.4    Jin, Y.5    Faure, E.6
  • 27
    • 0036087432 scopus 로고    scopus 로고
    • CD40 ligation stimulates MCP-1 and IL-8 production, TRAF6 recruitment, and MAPK activation in proximal tubule cells
    • Li H, Nord EP. CD40 ligation stimulates MCP-1 and IL-8 production, TRAF6 recruitment, and MAPK activation in proximal tubule cells. Am J Physiol Renal Physiol 2002 282: F1020 F1033.
    • (2002) Am J Physiol Renal Physiol , vol.282
    • Li, H.1    Nord, E.P.2
  • 28
    • 0033634977 scopus 로고    scopus 로고
    • TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway
    • Takaesu G, Kishida S, Hiyama A, Yamaguchi K, Shibuya H, Irie K et al. TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway. Mol Cell 2000 5: 649 658.
    • (2000) Mol Cell , vol.5 , pp. 649-658
    • Takaesu, G.1    Kishida, S.2    Hiyama, A.3    Yamaguchi, K.4    Shibuya, H.5    Irie, K.6
  • 29
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng L, Wang C, Spencer E, Yang L, Braun A, You J et al. Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 2000 103: 351 361.
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6
  • 31
    • 0037153191 scopus 로고    scopus 로고
    • Essential role for TIRAP in activation of the signalling cascade shared by TLR2 and TLR4
    • Yamamoto M, Sato S, Hemmi H, Sanjo H, Uematsu S, Kaisho T et al. Essential role for TIRAP in activation of the signalling cascade shared by TLR2 and TLR4. Nature 2002 420: 324 329.
    • (2002) Nature , vol.420 , pp. 324-329
    • Yamamoto, M.1    Sato, S.2    Hemmi, H.3    Sanjo, H.4    Uematsu, S.5    Kaisho, T.6
  • 32
    • 0346157331 scopus 로고    scopus 로고
    • TIR domain-containing adaptors define the specificity of TLR signaling
    • Yamamoto M, Takeda K, Akira S. TIR domain-containing adaptors define the specificity of TLR signaling. Mol Immunol 2004 40: 861 868.
    • (2004) Mol Immunol , vol.40 , pp. 861-868
    • Yamamoto, M.1    Takeda, K.2    Akira, S.3
  • 33
    • 0033166472 scopus 로고    scopus 로고
    • Unresponsiveness of MyD88-deficient mice to endotoxin
    • Kawai T, Adachi O, Ogawa T, Takeda K, Akira S. Unresponsiveness of MyD88-deficient mice to endotoxin. Immunity 1999 11: 115 122.
    • (1999) Immunity , vol.11 , pp. 115-122
    • Kawai, T.1    Adachi, O.2    Ogawa, T.3    Takeda, K.4    Akira, S.5
  • 34
    • 0043176281 scopus 로고    scopus 로고
    • Role of adaptor TRIF in the MyD88-independent toll-like receptor signaling pathway
    • Yamamoto M, Sato S, Hemmi H, Hoshino K, Kaisho T, Sanjo H et al. Role of adaptor TRIF in the MyD88-independent toll-like receptor signaling pathway. Science 2003 301: 640 643.
    • (2003) Science , vol.301 , pp. 640-643
    • Yamamoto, M.1    Sato, S.2    Hemmi, H.3    Hoshino, K.4    Kaisho, T.5    Sanjo, H.6
  • 35
    • 0242624622 scopus 로고    scopus 로고
    • TRAM is specifically involved in the Toll-like receptor 4-mediated MyD88-independent signaling pathway
    • Yamamoto M, Sato S, Hemmi H, Uematsu S, Hoshino K, Kaisho T et al. TRAM is specifically involved in the Toll-like receptor 4-mediated MyD88-independent signaling pathway. Nat Immunol 2003 4: 1144 1150.
    • (2003) Nat Immunol , vol.4 , pp. 1144-1150
    • Yamamoto, M.1    Sato, S.2    Hemmi, H.3    Uematsu, S.4    Hoshino, K.5    Kaisho, T.6
  • 36
    • 0141959224 scopus 로고    scopus 로고
    • LPS-TLR4 signaling to IRF-3/7 and NF-{kappa}B involves the Toll adapters TRAM and TRIF
    • Fitzgerald KA, Rowe DC, Barnes BJ, Caffrey DR, Visintin A, Latz E et al. LPS-TLR4 signaling to IRF-3/7 and NF-{kappa}B involves the Toll adapters TRAM and TRIF. J Exp Med 2003 198: 1043 1055.
    • (2003) J Exp Med , vol.198 , pp. 1043-1055
    • Fitzgerald, K.A.1    Rowe, D.C.2    Barnes, B.J.3    Caffrey, D.R.4    Visintin, A.5    Latz, E.6
  • 37
    • 0037471003 scopus 로고    scopus 로고
    • Pyogenic bacterial infections in humans with IRAK-4 deficiency
    • Picard C, Puel A, Bonnet M, Ku CL, Bustamante J, Yang K et al. Pyogenic bacterial infections in humans with IRAK-4 deficiency. Science 2003 299: 2076 2079.
    • (2003) Science , vol.299 , pp. 2076-2079
    • Picard, C.1    Puel, A.2    Bonnet, M.3    Ku, C.L.4    Bustamante, J.5    Yang, K.6
  • 38
    • 0043281537 scopus 로고    scopus 로고
    • Distinct mutations in IRAK-4 confer hyporesponsiveness to lipopolysaccharide and interleukin-1 in a patient with recurrent bacterial infections
    • Medvedev AE, Lentschat A, Kuhns DB, Blanco JC, Salkowski C, Zhang S et al. Distinct mutations in IRAK-4 confer hyporesponsiveness to lipopolysaccharide and interleukin-1 in a patient with recurrent bacterial infections. J Exp Med 2003 198: 521 531.
    • (2003) J Exp Med , vol.198 , pp. 521-531
    • Medvedev, A.E.1    Lentschat, A.2    Kuhns, D.B.3    Blanco, J.C.4    Salkowski, C.5    Zhang, S.6
  • 39
    • 1042269515 scopus 로고    scopus 로고
    • The Arg753GLn polymorphism of the human toll-like receptor 2 gene in tuberculosis disease
    • Ogus AC, Yoldas B, Ozdemir T, Uguz A, Olcen S, Keser I et al. The Arg753GLn polymorphism of the human toll-like receptor 2 gene in tuberculosis disease. Eur Respir J 2004 23: 219 223.
    • (2004) Eur Respir J , vol.23 , pp. 219-223
    • Ogus, A.C.1    Yoldas, B.2    Ozdemir, T.3    Uguz, A.4    Olcen, S.5    Keser, I.6
  • 40
    • 33746895147 scopus 로고    scopus 로고
    • An autocrine loop involving ret and glial cell-derived neurotrophic factor mediates retinoic acid-induced neuroblastoma cell differentiation
    • Cerchia L, D'Alessio A, Amabile G, Duconge F, Pestourie C, Tavitian B et al. An autocrine loop involving ret and glial cell-derived neurotrophic factor mediates retinoic acid-induced neuroblastoma cell differentiation. Mol Cancer Res 2006 4: 481 488.
    • (2006) Mol Cancer Res , vol.4 , pp. 481-488
    • Cerchia, L.1    D'Alessio, A.2    Amabile, G.3    Duconge, F.4    Pestourie, C.5    Tavitian, B.6
  • 41
    • 0035818268 scopus 로고    scopus 로고
    • Exposure to farming in early life and development of asthma and allergy: A cross-sectional survey
    • Riedler J, Braun-Fahrlander C, Eder W, Schreuer M, Waser M, Maisch S et al. Exposure to farming in early life and development of asthma and allergy: a cross-sectional survey. Lancet 2001 358: 1129 1133.
    • (2001) Lancet , vol.358 , pp. 1129-1133
    • Riedler, J.1    Braun-Fahrlander, C.2    Eder, W.3    Schreuer, M.4    Waser, M.5    Maisch, S.6
  • 42
    • 21644434827 scopus 로고    scopus 로고
    • Expression of TLR2 and TLR4 messenger RNA in the epithelial cells of the nasal airway
    • Dong Z, Yang Z, Wang C. Expression of TLR2 and TLR4 messenger RNA in the epithelial cells of the nasal airway. Am J Rhinol 2005 19: 236 239.
    • (2005) Am J Rhinol , vol.19 , pp. 236-239
    • Dong, Z.1    Yang, Z.2    Wang, C.3
  • 46
    • 29144532165 scopus 로고    scopus 로고
    • Characterization of Toll-like receptors in primary lung epithelial cells: Strong impact of the TLR3 ligand poly(I:C) on the regulation of Toll-like receptors, adaptor proteins and inflammatory response
    • Ritter M, Mennerich D, Weith A, Seither P. Characterization of Toll-like receptors in primary lung epithelial cells: strong impact of the TLR3 ligand poly(I:C) on the regulation of Toll-like receptors, adaptor proteins and inflammatory response. J Inflamm (Lond) 2005 2: 16.
    • (2005) J Inflamm (Lond) , vol.2 , pp. 16
    • Ritter, M.1    Mennerich, D.2    Weith, A.3    Seither, P.4
  • 49
    • 0347362785 scopus 로고    scopus 로고
    • Respiratory syncytial virus up-regulates TLR4 and sensitizes airway epithelial cells to endotoxin
    • Monick MM, Yarovinsky TO, Powers LS, Butler NS, Carter AB, Gudmundsson G et al. Respiratory syncytial virus up-regulates TLR4 and sensitizes airway epithelial cells to endotoxin. J Biol Chem 2003 278: 53035 53044.
    • (2003) J Biol Chem , vol.278 , pp. 53035-53044
    • Monick, M.M.1    Yarovinsky, T.O.2    Powers, L.S.3    Butler, N.S.4    Carter, A.B.5    Gudmundsson, G.6
  • 51
    • 33846554134 scopus 로고    scopus 로고
    • Retinoic acid-inducible gene I mediates early antiviral response and Toll-like receptor 3 expression in respiratory syncytial virus-infected airway epithelial cells
    • Liu P, Jamaluddin M, Li K, Garofalo RP, Casola A, Brasier AR. Retinoic acid-inducible gene I mediates early antiviral response and Toll-like receptor 3 expression in respiratory syncytial virus-infected airway epithelial cells. J Virol 2007 81: 1401 1411.
    • (2007) J Virol , vol.81 , pp. 1401-1411
    • Liu, P.1    Jamaluddin, M.2    Li, K.3    Garofalo, R.P.4    Casola, A.5    Brasier, A.R.6
  • 52
    • 33845618496 scopus 로고    scopus 로고
    • H. influenzae potentiates airway epithelial cell responses to rhinovirus by increasing ICAM-1 and TLR3 expression
    • Sajjan US, Jia Y, Newcomb DC, Bentley JK, Lukacs NW, LiPuma JJ et al. H. influenzae potentiates airway epithelial cell responses to rhinovirus by increasing ICAM-1 and TLR3 expression. FASEB J 2006 20: 2121 2123.
    • (2006) FASEB J , vol.20 , pp. 2121-2123
    • Sajjan, U.S.1    Jia, Y.2    Newcomb, D.C.3    Bentley, J.K.4    Lukacs, N.W.5    Lipuma, J.J.6
  • 53
    • 49249104376 scopus 로고    scopus 로고
    • Mold allergen, pen C 13, induce inflammatory cytokines in human bronchial epithelial cells via activation of protease-activated receptor
    • Chow L, Chiu L, Yu C, Su S Mold allergen, pen C 13, induce inflammatory cytokines in human bronchial epithelial cells via activation of protease-activated receptor. J Allergy Clin Immunol 2006 117 (2, Suppl. 1 S254.
    • (2006) J Allergy Clin Immunol , vol.117 , Issue.2 SUPPL. 1
    • Chow, L.1    Chiu, L.2    Yu, C.3    Su, S.4
  • 55
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu TK, Hung DT, Wheaton VI, Coughlin SR. Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell 1991 64: 1057 1068.
    • (1991) Cell , vol.64 , pp. 1057-1068
    • Vu, T.K.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 56
    • 0029113121 scopus 로고
    • Molecular cloning and functional expression of the gene encoding the human proteinase-activated receptor 2
    • Nystedt S, Emilsson K, Larsson AK, Strombeck B, Sundelin J. Molecular cloning and functional expression of the gene encoding the human proteinase-activated receptor 2. Eur J Biochem 1995 232: 84 89.
    • (1995) Eur J Biochem , vol.232 , pp. 84-89
    • Nystedt, S.1    Emilsson, K.2    Larsson, A.K.3    Strombeck, B.4    Sundelin, J.5
  • 58
    • 0032510949 scopus 로고    scopus 로고
    • The human proteinase-activated receptor-3 (PAR-3) gene. Identification within a Par gene cluster and characterization in vascular endothelial cells and platelets
    • Schmidt VA, Nierman WC, Maglott DR, Cupit LD, Moskowitz KA, Wainer JA et al. The human proteinase-activated receptor-3 (PAR-3) gene. Identification within a Par gene cluster and characterization in vascular endothelial cells and platelets. J Biol Chem 1998 273: 15061 15068.
    • (1998) J Biol Chem , vol.273 , pp. 15061-15068
    • Schmidt, V.A.1    Nierman, W.C.2    Maglott, D.R.3    Cupit, L.D.4    Moskowitz, K.A.5    Wainer, J.A.6
  • 59
    • 0028814818 scopus 로고
    • Constitutive expression and modulation of the functional thrombin receptor in the human kidney
    • Xu Y, Zacharias U, Peraldi MN, He CJ, Lu C, Sraer JD et al. Constitutive expression and modulation of the functional thrombin receptor in the human kidney. Am J Pathol 1995 146: 101 110.
    • (1995) Am J Pathol , vol.146 , pp. 101-110
    • Xu, Y.1    Zacharias, U.2    Peraldi, M.N.3    He, C.J.4    Lu, C.5    Sraer, J.D.6
  • 60
    • 0027258993 scopus 로고
    • Chromosomal assignment of the human thrombin receptor gene: Localization to region q13 of chromosome 5
    • Bahou WF, Nierman WC, Durkin AS, Potter CL, Demetrick DJ. Chromosomal assignment of the human thrombin receptor gene: localization to region q13 of chromosome 5. Blood 1993 82: 1532 1537.
    • (1993) Blood , vol.82 , pp. 1532-1537
    • Bahou, W.F.1    Nierman, W.C.2    Durkin, A.S.3    Potter, C.L.4    Demetrick, D.J.5
  • 61
    • 0030946582 scopus 로고    scopus 로고
    • The human thrombin receptor and proteinase activated receptor-2 genes are tightly linked on chromosome 5q13
    • Schmidt VA, Nierman WC, Feldblyum TV, Maglott DR, Bahou WF. The human thrombin receptor and proteinase activated receptor-2 genes are tightly linked on chromosome 5q13. Br J Haematol 1997 97: 523 529.
    • (1997) Br J Haematol , vol.97 , pp. 523-529
    • Schmidt, V.A.1    Nierman, W.C.2    Feldblyum, T.V.3    Maglott, D.R.4    Bahou, W.F.5
  • 62
    • 0032483456 scopus 로고    scopus 로고
    • Gene and locus structure and chromosomal localization of the protease-activated receptor gene family
    • Kahn ML, Hammes SR, Botka C, Coughlin SR. Gene and locus structure and chromosomal localization of the protease-activated receptor gene family. J Biol Chem 1998 273: 23290 23296.
    • (1998) J Biol Chem , vol.273 , pp. 23290-23296
    • Kahn, M.L.1    Hammes, S.R.2    Botka, C.3    Coughlin, S.R.4
  • 63
    • 7944224566 scopus 로고    scopus 로고
    • The role of protease activation of inflammation in allergic respiratory diseases
    • Reed CE, Kita H. The role of protease activation of inflammation in allergic respiratory diseases. J Allergy Clin Immunol 2004 114: 997 1008.
    • (2004) J Allergy Clin Immunol , vol.114 , pp. 997-1008
    • Reed, C.E.1    Kita, H.2
  • 65
    • 0028797819 scopus 로고
    • Thrombin interaction with a recombinant N-terminal extracellular domain of the thrombin receptor in an acellular system
    • Bouton MC, Jandrot-Perrus M, Moog S, Cazenave JP, Guillin MC, Lanza F. Thrombin interaction with a recombinant N-terminal extracellular domain of the thrombin receptor in an acellular system. Biochem J 1995 305: 635 641.
    • (1995) Biochem J , vol.305 , pp. 635-641
    • Bouton, M.C.1    Jandrot-Perrus, M.2    Moog, S.3    Cazenave, J.P.4    Guillin, M.C.5    Lanza, F.6
  • 66
    • 0034624973 scopus 로고    scopus 로고
    • Tissue factor- and factor X-dependent activation of protease-activated receptor 2 by factor VIIa
    • Camerer E, Huang W, Coughlin SR. Tissue factor- and factor X-dependent activation of protease-activated receptor 2 by factor VIIa. Proc Natl Acad Sci USA 2000 97: 5255 5260.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5255-5260
    • Camerer, E.1    Huang, W.2    Coughlin, S.R.3
  • 68
    • 0034745133 scopus 로고    scopus 로고
    • Neutrophil proteases can inactivate human PAR3 and abolish the co-receptor function of PAR3 on murine platelets
    • Cumashi A, Ansuini H, Celli N, De Blasi A, O'Brien PJ, Brass LF et al. Neutrophil proteases can inactivate human PAR3 and abolish the co-receptor function of PAR3 on murine platelets. Thromb Haemost 2001 85: 533 538.
    • (2001) Thromb Haemost , vol.85 , pp. 533-538
    • Cumashi, A.1    Ansuini, H.2    Celli, N.3    De Blasi, A.4    O'Brien, P.J.5    Brass, L.F.6
  • 69
    • 0034748449 scopus 로고    scopus 로고
    • Glycosylation and the activation of proteinase-activated receptor 2 (PAR(2)) by human mast cell tryptase
    • Compton SJ, Renaux B, Wijesuriya SJ, Hollenberg MD. Glycosylation and the activation of proteinase-activated receptor 2 (PAR(2)) by human mast cell tryptase. Br J Pharmacol 2001 134: 705 718.
    • (2001) Br J Pharmacol , vol.134 , pp. 705-718
    • Compton, S.J.1    Renaux, B.2    Wijesuriya, S.J.3    Hollenberg, M.D.4
  • 70
    • 0029018204 scopus 로고
    • Proteolysis of the human platelet and endothelial cell thrombin receptor by neutrophil-derived cathepsin G
    • Molino M, Blanchard N, Belmonte E, Tarver AP, Abrams C, Hoxie JA et al. Proteolysis of the human platelet and endothelial cell thrombin receptor by neutrophil-derived cathepsin G. J Biol Chem 1995 270: 11168 11175.
    • (1995) J Biol Chem , vol.270 , pp. 11168-11175
    • Molino, M.1    Blanchard, N.2    Belmonte, E.3    Tarver, A.P.4    Abrams, C.5    Hoxie, J.A.6
  • 71
    • 0031850771 scopus 로고    scopus 로고
    • Reaction of mast cell proteases tryptase and chymase with protease activated receptors (PARs) on keratinocytes and fibroblasts
    • Schechter NM, Brass LF, Lavker RM, Jensen PJ. Reaction of mast cell proteases tryptase and chymase with protease activated receptors (PARs) on keratinocytes and fibroblasts. J Cell Physiol 1998 176: 365 373.
    • (1998) J Cell Physiol , vol.176 , pp. 365-373
    • Schechter, N.M.1    Brass, L.F.2    Lavker, R.M.3    Jensen, P.J.4
  • 72
    • 0031890089 scopus 로고    scopus 로고
    • Dual endothelium-dependent vascular activities of proteinase-activated receptor-2-activating peptides: Evidence for receptor heterogeneity
    • Roy SS, Saifeddine M, Loutzenhiser R, Triggle CR, Hollenberg MD. Dual endothelium-dependent vascular activities of proteinase-activated receptor-2-activating peptides: evidence for receptor heterogeneity. Br J Pharmacol 1998 123: 1434 1440.
    • (1998) Br J Pharmacol , vol.123 , pp. 1434-1440
    • Roy, S.S.1    Saifeddine, M.2    Loutzenhiser, R.3    Triggle, C.R.4    Hollenberg, M.D.5
  • 73
    • 0036895877 scopus 로고    scopus 로고
    • Proteinase-activated receptor-2 (PAR2): Vascular effects of a PAR2-derived activating peptide via a receptor different than PAR2
    • McGuire JJ, Dai J, Andrade-Gordon P, Triggle CR, Hollenberg MD. Proteinase-activated receptor-2 (PAR2): vascular effects of a PAR2-derived activating peptide via a receptor different than PAR2. J Pharmacol Exp Ther 2002 303: 985 992.
    • (2002) J Pharmacol Exp Ther , vol.303 , pp. 985-992
    • McGuire, J.J.1    Dai, J.2    Andrade-Gordon, P.3    Triggle, C.R.4    Hollenberg, M.D.5
  • 74
    • 0036078701 scopus 로고    scopus 로고
    • Proteinase-activated receptor (PAR)-1 and -2 agonists induce mediator release from mast cells by pathways distinct from PAR-1 and PAR-2
    • Stenton GR, Nohara O, Dery RE, Vliagoftis H, Gilchrist M, Johri A et al. Proteinase-activated receptor (PAR)-1 and -2 agonists induce mediator release from mast cells by pathways distinct from PAR-1 and PAR-2. J Pharmacol Exp Ther 2002 302: 466 474.
    • (2002) J Pharmacol Exp Ther , vol.302 , pp. 466-474
    • Stenton, G.R.1    Nohara, O.2    Dery, R.E.3    Vliagoftis, H.4    Gilchrist, M.5    Johri, A.6
  • 75
    • 0346788901 scopus 로고    scopus 로고
    • Protease-activated receptor 2: Activation, signalling and function
    • Cottrell GS, Amadesi S, Schmidlin F, Bunnett N. Protease-activated receptor 2: activation, signalling and function. Biochem Soc Trans 2003 31: 1191 1197.
    • (2003) Biochem Soc Trans , vol.31 , pp. 1191-1197
    • Cottrell, G.S.1    Amadesi, S.2    Schmidlin, F.3    Bunnett, N.4
  • 76
    • 0028923464 scopus 로고
    • The thrombin receptor in human platelets is coupled to a GTP binding protein of the G alpha q family
    • Benka ML, Lee M, Wang GR, Buckman S, Burlacu A, Cole L et al. The thrombin receptor in human platelets is coupled to a GTP binding protein of the G alpha q family. FEBS Lett 1995 363: 49 52.
    • (1995) FEBS Lett , vol.363 , pp. 49-52
    • Benka, M.L.1    Lee, M.2    Wang, G.R.3    Buckman, S.4    Burlacu, A.5    Cole, L.6
  • 77
    • 0030756508 scopus 로고    scopus 로고
    • Defective platelet activation in G alpha(q)-deficient mice
    • Offermanns S, Toombs CF, Hu YH, Simon MI. Defective platelet activation in G alpha(q)-deficient mice. Nature 1997 389: 183 186.
    • (1997) Nature , vol.389 , pp. 183-186
    • Offermanns, S.1    Toombs, C.F.2    Hu, Y.H.3    Simon, M.I.4
  • 78
    • 34547107639 scopus 로고    scopus 로고
    • Beta-Arrestin-dependent regulation of the cofilin pathway downstream of protease-activated receptor-2
    • Zoudilova M, Kumar P, Ge L, Wang P, Bokoch GM, DeFea KA. Beta-Arrestin-dependent regulation of the cofilin pathway downstream of protease-activated receptor-2. J Biol Chem 2007 282: 20634 20646.
    • (2007) J Biol Chem , vol.282 , pp. 20634-20646
    • Zoudilova, M.1    Kumar, P.2    Ge, L.3    Wang, P.4    Bokoch, G.M.5    Defea, K.A.6
  • 79
    • 0037136569 scopus 로고    scopus 로고
    • ADAM-33 surfaces as an asthma gene
    • Shapiro SD, Owen CA. ADAM-33 surfaces as an asthma gene. N Engl J Med 2002 347: 936 938.
    • (2002) N Engl J Med , vol.347 , pp. 936-938
    • Shapiro, S.D.1    Owen, C.A.2
  • 80
    • 1642313810 scopus 로고    scopus 로고
    • SPINK5: A gene for atopic dermatitis and asthma
    • Moffatt MF. SPINK5: a gene for atopic dermatitis and asthma. Clin Exp Allergy 2004 34: 325 327.
    • (2004) Clin Exp Allergy , vol.34 , pp. 325-327
    • Moffatt, M.F.1
  • 81
    • 0036533649 scopus 로고    scopus 로고
    • Activation of protease-activated receptor (PAR)-1, PAR-2, and PAR-4 stimulates IL-6, IL-8, and prostaglandin E2 release from human respiratory epithelial cells
    • Asokananthan N, Graham PT, Fink J, Knight DA, Bakker AJ, McWilliam AS et al. Activation of protease-activated receptor (PAR)-1, PAR-2, and PAR-4 stimulates IL-6, IL-8, and prostaglandin E2 release from human respiratory epithelial cells. J Immunol 2002 168: 3577 3585.
    • (2002) J Immunol , vol.168 , pp. 3577-3585
    • Asokananthan, N.1    Graham, P.T.2    Fink, J.3    Knight, D.A.4    Bakker, A.J.5    McWilliam, A.S.6
  • 82
    • 0037108373 scopus 로고    scopus 로고
    • House dust mite allergens induce proinflammatory cytokines from respiratory epithelial cells: The cysteine protease allergen, der p 1, activates protease-activated receptor (PAR)-2 and inactivates PAR-1
    • Asokananthan N, Graham PT, Stewart DJ, Bakker AJ, Eidne KA, Thompson PJ et al. House dust mite allergens induce proinflammatory cytokines from respiratory epithelial cells: the cysteine protease allergen, Der p 1, activates protease-activated receptor (PAR)-2 and inactivates PAR-1. J Immunol 2002 169: 4572.
    • (2002) J Immunol , vol.169 , pp. 4572
    • Asokananthan, N.1    Graham, P.T.2    Stewart, D.J.3    Bakker, A.J.4    Eidne, K.A.5    Thompson, P.J.6
  • 83
    • 1142285213 scopus 로고    scopus 로고
    • German cockroach extract activates protease-activated receptor 2 in human airway epithelial cells
    • Hong JH, Lee SI, Kim KE, Yong TS, Seo JT, Sohn MH et al. German cockroach extract activates protease-activated receptor 2 in human airway epithelial cells. J Allergy Clin Immunol 2004 113: 315 319.
    • (2004) J Allergy Clin Immunol , vol.113 , pp. 315-319
    • Hong, J.H.1    Lee, S.I.2    Kim, K.E.3    Yong, T.S.4    Seo, J.T.5    Sohn, M.H.6
  • 84
    • 0035575784 scopus 로고    scopus 로고
    • Trypsin induces activation and inflammatory mediator release from human eosinophils through protease-activated receptor-2
    • Miike S, McWilliam AS, Kita H. Trypsin induces activation and inflammatory mediator release from human eosinophils through protease-activated receptor-2. J Immunol 2001 167: 6615.
    • (2001) J Immunol , vol.167 , pp. 6615
    • Miike, S.1    McWilliam, A.S.2    Kita, H.3
  • 85
    • 0346995204 scopus 로고    scopus 로고
    • Cockroach proteases increase IL-8 expression in human bronchial epithelial cells via activation of protease-activated receptor (PAR)-2 and extracellular-signal-regulated kinase
    • Page K, Strunk VS, Hershenson MB. Cockroach proteases increase IL-8 expression in human bronchial epithelial cells via activation of protease-activated receptor (PAR)-2 and extracellular-signal-regulated kinase. J Allergy Clin Immunol 2003 112: 1112 1118.
    • (2003) J Allergy Clin Immunol , vol.112 , pp. 1112-1118
    • Page, K.1    Strunk, V.S.2    Hershenson, M.B.3
  • 87
    • 34648846307 scopus 로고    scopus 로고
    • Activation of protease-activated receptor-2 reduces airways inflammation in experimental allergic asthma
    • D'Agostino B, Roviezzo F, De Palma R, Terracciano S, De Nardo M, Gallelli L et al. Activation of protease-activated receptor-2 reduces airways inflammation in experimental allergic asthma. Clin Exp Allergy 2007 37: 1436 1443.
    • (2007) Clin Exp Allergy , vol.37 , pp. 1436-1443
    • D'Agostino, B.1    Roviezzo, F.2    De Palma, R.3    Terracciano, S.4    De Nardo, M.5    Gallelli, L.6
  • 89
    • 0035184146 scopus 로고    scopus 로고
    • Protease-activated receptors in human airways: Upregulation of PAR-2 in respiratory epithelium from patients with asthma
    • Knight D, Lim S, Scaffidi A, Roche N, Chung K, Stewart G et al. Protease-activated receptors in human airways: upregulation of PAR-2 in respiratory epithelium from patients with asthma. J Allergy Clin Immunol 2001 108: 797 803.
    • (2001) J Allergy Clin Immunol , vol.108 , pp. 797-803
    • Knight, D.1    Lim, S.2    Scaffidi, A.3    Roche, N.4    Chung, K.5    Stewart, G.6
  • 90
    • 33746713726 scopus 로고    scopus 로고
    • Gene and protein expression of protease-activated receptor 2 in structural and inflammatory cells in the nasal mucosa in seasonal allergic rhinitis
    • Dinh QT, Cryer A, Trevisani M, Dinh S, Wu S, Cifuentes LB et al. Gene and protein expression of protease-activated receptor 2 in structural and inflammatory cells in the nasal mucosa in seasonal allergic rhinitis. Clin Exp Allergy 2006 36: 1039 1048.
    • (2006) Clin Exp Allergy , vol.36 , pp. 1039-1048
    • Dinh, Q.T.1    Cryer, A.2    Trevisani, M.3    Dinh, S.4    Wu, S.5    Cifuentes, L.B.6
  • 92
    • 34250754475 scopus 로고    scopus 로고
    • PAR-2 activation regulates IL-8 and GRO-alpha synthesis by NF-kappaB, but not RANTES, IL-6, eotaxin or TARC expression in nasal epithelium
    • Rudack C, Steinhoff M, Mooren F, Buddenkotte J, Becker K, von Eiff C et al. PAR-2 activation regulates IL-8 and GRO-alpha synthesis by NF-kappaB, but not RANTES, IL-6, eotaxin or TARC expression in nasal epithelium. Clin Exp Allergy 2007 37: 1009 1022.
    • (2007) Clin Exp Allergy , vol.37 , pp. 1009-1022
    • Rudack, C.1    Steinhoff, M.2    Mooren, F.3    Buddenkotte, J.4    Becker, K.5    Von Eiff, C.6
  • 93
    • 0031037296 scopus 로고    scopus 로고
    • Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI 3-kinase gamma
    • Lopez-Ilasaca M, Crespo P, Pellici PG, Gutkind JS, Wetzker R. Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI 3-kinase gamma. Science 1997 275: 394 397.
    • (1997) Science , vol.275 , pp. 394-397
    • Lopez-Ilasaca, M.1    Crespo, P.2    Pellici, P.G.3    Gutkind, J.S.4    Wetzker, R.5
  • 94
    • 22444433175 scopus 로고    scopus 로고
    • NLRs join TLRs as innate sensors of pathogens
    • Martinon F, Tschopp J. NLRs join TLRs as innate sensors of pathogens. Trends Immunol 2005 26: 447 454.
    • (2005) Trends Immunol , vol.26 , pp. 447-454
    • Martinon, F.1    Tschopp, J.2
  • 95
    • 33344476398 scopus 로고    scopus 로고
    • CATERPILLERs, pyrin and hereditary immunological disorders
    • Ting JP, Kastner DL, Hoffman HM. CATERPILLERs, pyrin and hereditary immunological disorders. Nat Rev Immunol 2006 6: 183 195.
    • (2006) Nat Rev Immunol , vol.6 , pp. 183-195
    • Ting, J.P.1    Kastner, D.L.2    Hoffman, H.M.3
  • 96
    • 17644366913 scopus 로고    scopus 로고
    • NOD-LRR proteins: Role in host-microbial interactions and inflammatory disease
    • Inohara N, Chamaillard M, McDonald C, Nunez G. NOD-LRR proteins: role in host-microbial interactions and inflammatory disease. Annu Rev Biochem 2005 74: 355 383.
    • (2005) Annu Rev Biochem , vol.74 , pp. 355-383
    • Inohara, N.1    Chamaillard, M.2    McDonald, C.3    Nunez, G.4
  • 97
    • 33244472793 scopus 로고    scopus 로고
    • Signalling pathways and molecular interactions of NOD1 and NOD2
    • Strober W, Murray PJ, Kitani A, Watanabe T. Signalling pathways and molecular interactions of NOD1 and NOD2. Nat Rev Immunol 2006 6: 9 20.
    • (2006) Nat Rev Immunol , vol.6 , pp. 9-20
    • Strober, W.1    Murray, P.J.2    Kitani, A.3    Watanabe, T.4
  • 98
    • 11144289688 scopus 로고    scopus 로고
    • The Crohn's disease protein, NOD2, requires RIP2 in order to induce ubiquitinylation of a novel site on NEMO
    • Abbott DW, Wilkins A, Asara JM, Cantley LC. The Crohn's disease protein, NOD2, requires RIP2 in order to induce ubiquitinylation of a novel site on NEMO. Curr Biol 2004 14: 2217 2227.
    • (2004) Curr Biol , vol.14 , pp. 2217-2227
    • Abbott, D.W.1    Wilkins, A.2    Asara, J.M.3    Cantley, L.C.4
  • 99
    • 33645958613 scopus 로고    scopus 로고
    • TIR, CARD and PYRIN: Three domains for an antimicrobial triad
    • Werts C, Girardin SE, Philpott DJ. TIR, CARD and PYRIN: three domains for an antimicrobial triad. Cell Death Differ 2006 13: 798 815.
    • (2006) Cell Death Differ , vol.13 , pp. 798-815
    • Werts, C.1    Girardin, S.E.2    Philpott, D.J.3
  • 100
    • 13244292161 scopus 로고    scopus 로고
    • Nod2-dependent regulation of innate and adaptive immunity in the intestinal tract
    • Kobayashi KS, Chamaillard M, Ogura Y, Henegariu O, Inohara N, Nunez G et al. Nod2-dependent regulation of innate and adaptive immunity in the intestinal tract. Science 2005 307: 731 734.
    • (2005) Science , vol.307 , pp. 731-734
    • Kobayashi, K.S.1    Chamaillard, M.2    Ogura, Y.3    Henegariu, O.4    Inohara, N.5    Nunez, G.6
  • 101
    • 17944380130 scopus 로고    scopus 로고
    • CARD4/Nod1 mediates NF-kappaB and JNK activation by invasive Shigella flexneri
    • Girardin SE, Tournebize R, Mavris M, Page AL, Li X, Stark GR et al. CARD4/Nod1 mediates NF-kappaB and JNK activation by invasive Shigella flexneri. EMBO Rep 2001 2: 736 742.
    • (2001) EMBO Rep , vol.2 , pp. 736-742
    • Girardin, S.E.1    Tournebize, R.2    Mavris, M.3    Page, A.L.4    Li, X.5    Stark, G.R.6
  • 102
    • 23844521000 scopus 로고    scopus 로고
    • Synergistic stimulation of human monocytes and dendritic cells by Toll-like receptor 4 and NOD1- and NOD2-activating agonists
    • Fritz JH, Girardin SE, Fitting C, Werts C, Mengin-Lecreulx D, Caroff M et al. Synergistic stimulation of human monocytes and dendritic cells by Toll-like receptor 4 and NOD1- and NOD2-activating agonists. Eur J Immunol 2005 35: 2459 2470.
    • (2005) Eur J Immunol , vol.35 , pp. 2459-2470
    • Fritz, J.H.1    Girardin, S.E.2    Fitting, C.3    Werts, C.4    Mengin-Lecreulx, D.5    Caroff, M.6
  • 103
    • 28444471235 scopus 로고    scopus 로고
    • Synergistic effect of Nod1 and Nod2 agonists with Toll-like receptor agonists on human dendritic cells to generate interleukin-12 and T helper type 1 cells
    • Tada H, Aiba S, Shibata KI, Ohteki T, Takada H. Synergistic effect of Nod1 and Nod2 agonists with Toll-like receptor agonists on human dendritic cells to generate interleukin-12 and T helper type 1 cells. Infect Immun 2005 73: 7967 7976.
    • (2005) Infect Immun , vol.73 , pp. 7967-7976
    • Tada, H.1    Aiba, S.2    Shibata, K.I.3    Ohteki, T.4    Takada, H.5
  • 104
    • 27444433978 scopus 로고    scopus 로고
    • NOD2 regulation of Toll-like receptor responses and the pathogenesis of Crohn's disease
    • Watanabe T, Kitani A, Strober W. NOD2 regulation of Toll-like receptor responses and the pathogenesis of Crohn's disease. Gut 2005 54: 1515 1518.
    • (2005) Gut , vol.54 , pp. 1515-1518
    • Watanabe, T.1    Kitani, A.2    Strober, W.3
  • 105
    • 0037312509 scopus 로고    scopus 로고
    • NALPs: A novel protein family involved in inflammation
    • Tschopp J, Martinon F, Burns K. NALPs: a novel protein family involved in inflammation. Nat Rev Mol Cell Biol 2003 4: 95 104.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 95-104
    • Tschopp, J.1    Martinon, F.2    Burns, K.3
  • 106
    • 2542457495 scopus 로고    scopus 로고
    • Inflammatory caspases: Linking an intracellular innate immune system to autoinflammatory diseases
    • Martinon F, Tschopp J. Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases. Cell 2004 117: 561 574.
    • (2004) Cell , vol.117 , pp. 561-574
    • Martinon, F.1    Tschopp, J.2
  • 107
    • 33645770203 scopus 로고    scopus 로고
    • The Birc1e cytosolic pattern-recognition receptor contributes to the detection and control of Legionella pneumophila infection
    • Zamboni DS, Kobayashi KS, Kohlsdorf T, Ogura Y, Long EM, Vance RE et al. The Birc1e cytosolic pattern-recognition receptor contributes to the detection and control of Legionella pneumophila infection. Nat Immunol 2006 7: 318 325.
    • (2006) Nat Immunol , vol.7 , pp. 318-325
    • Zamboni, D.S.1    Kobayashi, K.S.2    Kohlsdorf, T.3    Ogura, Y.4    Long, E.M.5    Vance, R.E.6
  • 108
    • 26844452231 scopus 로고    scopus 로고
    • Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis
    • Mariathasan S, Weiss DS, Dixit VM, Monack DM. Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis. J Exp Med 2005 202: 1043 1049.
    • (2005) J Exp Med , vol.202 , pp. 1043-1049
    • Mariathasan, S.1    Weiss, D.S.2    Dixit, V.M.3    Monack, D.M.4
  • 109
    • 3142654767 scopus 로고    scopus 로고
    • Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf
    • Mariathasan S, Newton K, Monack DM, Vucic D, French DM, Lee WP et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 2004 430: 213 218.
    • (2004) Nature , vol.430 , pp. 213-218
    • Mariathasan, S.1    Newton, K.2    Monack, D.M.3    Vucic, D.4    French, D.M.5    Lee, W.P.6
  • 111
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • Martinon F, Burns K, Tschopp J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell 2002 10: 417 426.
    • (2002) Mol Cell , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 112
    • 32944462834 scopus 로고    scopus 로고
    • Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3
    • Kanneganti TD, Ozoren N, Body-Malapel M, Amer A, Park JH, Franchi L et al. Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3. Nature 2006 440: 233 236.
    • (2006) Nature , vol.440 , pp. 233-236
    • Kanneganti, T.D.1    Ozoren, N.2    Body-Malapel, M.3    Amer, A.4    Park, J.H.5    Franchi, L.6
  • 113
    • 32944468985 scopus 로고    scopus 로고
    • Gout-associated uric acid crystals activate the NALP3 inflammasome
    • Martinon F, Petrilli V, Mayor A, Tardivel A, Tschopp J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 2006 440: 237 241.
    • (2006) Nature , vol.440 , pp. 237-241
    • Martinon, F.1    Petrilli, V.2    Mayor, A.3    Tardivel, A.4    Tschopp, J.5
  • 114
    • 0035897904 scopus 로고    scopus 로고
    • Association between insertion mutation in NOD2 gene and Crohn's disease in German and British populations
    • Hampe J, Cuthbert A, Croucher PJ, Mirza MM, Mascheretti S, Fisher S et al. Association between insertion mutation in NOD2 gene and Crohn's disease in German and British populations. Lancet 2001 357: 925 928.
    • (2001) Lancet , vol.357 , pp. 925-928
    • Hampe, J.1    Cuthbert, A.2    Croucher, P.J.3    Mirza, M.M.4    Mascheretti, S.5    Fisher, S.6
  • 115
    • 34247239745 scopus 로고    scopus 로고
    • Various human epithelial cells express functional Toll-like receptors, NOD1 and NOD2 to produce anti-microbial peptides, but not proinflammatory cytokines
    • Uehara A, Fujimoto Y, Fukase K, Takada H. Various human epithelial cells express functional Toll-like receptors, NOD1 and NOD2 to produce anti-microbial peptides, but not proinflammatory cytokines. Mol Immunol 2007 44: 3100 3111.
    • (2007) Mol Immunol , vol.44 , pp. 3100-3111
    • Uehara, A.1    Fujimoto, Y.2    Fukase, K.3    Takada, H.4
  • 116
    • 3142581432 scopus 로고    scopus 로고
    • Regulation of Toll/IL-1-receptor-mediated gene expression by the inducible nuclear protein I[kappa]B[zeta]
    • Yamamoto M, Yamazaki S, Uematsu S, Sato S, Hemmi H, Hoshino K et al. Regulation of Toll/IL-1-receptor-mediated gene expression by the inducible nuclear protein I[kappa]B[zeta]. Nature 2004 430: 218 222.
    • (2004) Nature , vol.430 , pp. 218-222
    • Yamamoto, M.1    Yamazaki, S.2    Uematsu, S.3    Sato, S.4    Hemmi, H.5    Hoshino, K.6
  • 117
    • 14844293877 scopus 로고    scopus 로고
    • Positive and negative regulation of nuclear factor-{kappa}B-mediated transcription by I{kappa}B-{zeta}, an inducible nuclear protein
    • Motoyama M, Yamazaki S, Eto-Kimura A, Takeshige K, Muta T. Positive and negative regulation of nuclear factor-{kappa}B-mediated transcription by I{kappa}B-{zeta}, an inducible nuclear protein. J Biol Chem 2005 280: 7444 7451.
    • (2005) J Biol Chem , vol.280 , pp. 7444-7451
    • Motoyama, M.1    Yamazaki, S.2    Eto-Kimura, A.3    Takeshige, K.4    Muta, T.5
  • 118
    • 0347065364 scopus 로고    scopus 로고
    • Interferon regulatory factor-3-mediated activation of the interferon-sensitive response element by Toll-like receptor (TLR) 4 but Not TLR3 requires the p65 subunit of NF-{kappa}
    • Wietek C, Miggin SM, Jefferies CA, O'Neill LAJ. Interferon regulatory factor-3-mediated activation of the interferon-sensitive response element by Toll-like receptor (TLR) 4 but Not TLR3 requires the p65 subunit of NF-{kappa}. J Biol Chem 2003 278: 50923 50931.
    • (2003) J Biol Chem , vol.278 , pp. 50923-50931
    • Wietek, C.1    Miggin, S.M.2    Jefferies, C.A.3    O'Neill, L.A.J.4
  • 119
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu CD, Chinenov Y, Kerppola TK. Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol Cell 2002 9: 789 798.
    • (2002) Mol Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.