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Volumn 2, Issue 4, 2006, Pages 569-583

Pattern recognition receptors: An update

Author keywords

[No Author keywords available]

Indexed keywords

BETA INTERFERON; CASPASE RECRUITMENT DOMAIN PROTEIN 15; CD36 ANTIGEN; CELL SURFACE RECEPTOR; COLLECTIN; CYTOPLASMIC RECEPTOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1 RECEPTOR; JANUS KINASE; LECTIN; MITOGEN ACTIVATED PROTEIN KINASE P38; MYELOID DIFFERENTIATION FACTOR 88; PATTERN RECOGNITION RECEPTOR; RNA HELICASE; SCAVENGER RECEPTOR; STAT PROTEIN; TOLL LIKE RECEPTOR; TRANSFORMING GROWTH FACTOR BETA; TUMOR NECROSIS FACTOR RECEPTOR; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR;

EID: 33748499155     PISSN: 1744666X     EISSN: None     Source Type: Journal    
DOI: 10.1586/1744666X.2.4.569     Document Type: Review
Times cited : (5)

References (149)
  • 1
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Janeway CA Jr. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb. Symp. Quant. Biol. 54(Pt 1), 1-13 (1989).
    • (1989) Cold Spring Harb. Symp. Quant. Biol. , vol.54 , Issue.PART 1 , pp. 1-13
    • Janeway Jr., C.A.1
  • 2
    • 0022189558 scopus 로고
    • Establishment of dorsal-ventral polarity in the Drosophila embryo: The induction of polarity by the Toll gene product
    • Anderson KV, Bokla L, Nusslein-Volhard C. Establishment of dorsal-ventral polarity in the Drosophila embryo: the induction of polarity by the Toll gene product. Cell 42(3), 791-798 (1985).
    • (1985) Cell , vol.42 , Issue.3 , pp. 791-798
    • Anderson, K.V.1    Bokla, L.2    Nusslein-Volhard, C.3
  • 3
    • 0242581687 scopus 로고    scopus 로고
    • The immune response of Drosophila
    • Hoffmann JA. The immune response of Drosophila. Nature 426(6962), 33-38 (2003).
    • (2003) Nature , vol.426 , Issue.6962 , pp. 33-38
    • Hoffmann, J.A.1
  • 4
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • Medzhitov R, Preston-Hurlburt P, Janeway CA Jr. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 388(6640), 394-397 (1997).
    • (1997) Nature , vol.388 , Issue.6640 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway Jr., C.A.3
  • 5
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira S, Takeda K. Toll-like receptor signalling. Nat. Rev. Immunol. 4(7), 499-511 (2004).
    • (2004) Nat. Rev. Immunol. , vol.4 , Issue.7 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 6
    • 10744219675 scopus 로고    scopus 로고
    • TLR9 signals after translocating from the ER to CpG DNA in the lysosome
    • Latz E, Schoenemeyer A, Visintin A et al. TLR9 signals after translocating from the ER to CpG DNA in the lysosome. Nat. Immunol. 5(2), 190-198 (2004).
    • (2004) Nat. Immunol. , vol.5 , Issue.2 , pp. 190-198
    • Latz, E.1    Schoenemeyer, A.2    Visintin, A.3
  • 7
    • 29244450802 scopus 로고    scopus 로고
    • Intracellular localization of Toll-like receptor 9 prevents recognition of self DNA but facilitates access to viral DNA
    • Barton GM, Kagan JC, Medzhitov R. Intracellular localization of Toll-like receptor 9 prevents recognition of self DNA but facilitates access to viral DNA. Nat. Immunol. 7(1), 49-56 (2006).
    • (2006) Nat. Immunol. , vol.7 , Issue.1 , pp. 49-56
    • Barton, G.M.1    Kagan, J.C.2    Medzhitov, R.3
  • 8
    • 29244453937 scopus 로고    scopus 로고
    • Toll-erating self DNA
    • Bauer S. Toll-erating self DNA. Nat. Immunol. 7(1), 13-15 (2006).
    • (2006) Nat. Immunol. , vol.7 , Issue.1 , pp. 13-15
    • Bauer, S.1
  • 9
    • 0037465251 scopus 로고    scopus 로고
    • The interleukin-1 receptor/Toll-like receptor superfamily: Signal transduction during inflammation and host defense
    • Dunne A, O'Neill LA. The interleukin-1 receptor/Toll-like receptor superfamily: signal transduction during inflammation and host defense. Sci. STKE 2003(171), re3 (2003).
    • (2003) Sci. STKE , vol.2003 , Issue.171
    • Dunne, A.1    O'Neill, L.A.2
  • 11
    • 2142762520 scopus 로고    scopus 로고
    • TLRs: Differential adapter utilization by Toll-like receptors mediates TLR-specific patterns of gene expression
    • Vogel SN, Fitzgerald KA, Fenton MJ. TLRs: differential adapter utilization by Toll-like receptors mediates TLR-specific patterns of gene expression. Mol. Interv. 3(8), 466-477 (2003).
    • (2003) Mol. Interv. , vol.3 , Issue.8 , pp. 466-477
    • Vogel, S.N.1    Fitzgerald, K.A.2    Fenton, M.J.3
  • 12
    • 0030694108 scopus 로고    scopus 로고
    • IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling
    • Muzio M, Ni J, Feng P, Dixit VM. IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling. Science 278(5343), 1612-1615 (1997).
    • (1997) Science , vol.278 , Issue.5343 , pp. 612-1615
    • Muzio, M.1    Ni, J.2    Feng, P.3    Dixit, V.M.4
  • 13
    • 0035817925 scopus 로고    scopus 로고
    • Mal (MyD88-adapter-like) is required for Toll-like receptor-4 signal transduction
    • Fitzgerald KA, Palsson-McDermott EM, Bowie AG et al. Mal (MyD88-adapter-like) is required for Toll-like receptor-4 signal transduction. Nature 413(6851), 78-83 (2001).
    • (2001) Nature , vol.413 , Issue.6851 , pp. 78-83
    • Fitzgerald, K.A.1    Palsson-McDermott, E.M.2    Bowie, A.G.3
  • 14
    • 0035555301 scopus 로고    scopus 로고
    • TIRAP: An adapter molecule in the Toll signaling pathway
    • Horng T, Barton GM, Medzhitov R. TIRAP: an adapter molecule in the Toll signaling pathway. Nat. Immunol. 2(9), 835-841 (2001).
    • (2001) Nat. Immunol. , vol.2 , Issue.9 , pp. 835-841
    • Horng, T.1    Barton, G.M.2    Medzhitov, R.3
  • 15
    • 0037114185 scopus 로고    scopus 로고
    • Cutting edge: A novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-β promoter in the Toll-like receptor signaling
    • Yamamoto M, Sato S, Mori K et al. Cutting edge: a novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-β promoter in the Toll-like receptor signaling. J. Immunol. 169(12), 6668-6672 (2002).
    • (2002) J. Immunol. , vol.169 , Issue.12 , pp. 6668-6672
    • Yamamoto, M.1    Sato, S.2    Mori, K.3
  • 16
    • 0042679529 scopus 로고    scopus 로고
    • Identification of Lps2 as a key transducer of MyD88-independent TIR signalling
    • Hoebe K, Du X, Georgel P et al. Identification of Lps2 as a key transducer of MyD88-independent TIR signalling. Nature 424(6950), 743-748 (2003).
    • (2003) Nature , vol.424 , Issue.6950 , pp. 743-748
    • Hoebe, K.1    Du, X.2    Georgel, P.3
  • 17
    • 0037320451 scopus 로고    scopus 로고
    • TICAM-1, an adaptor molecule that participates in Toll-like receptor 3-mediated interferon-β induction
    • Oshiumi H, Matsumoto M, Funami K, Akazawa T, Seya T. TICAM-1, an adaptor molecule that participates in Toll-like receptor 3-mediated interferon-β induction. Nat. Immunol. 4(2), 161-167 (2003).
    • (2003) Nat. Immunol. , vol.4 , Issue.2 , pp. 161-167
    • Oshiumi, H.1    Matsumoto, M.2    Funami, K.3    Akazawa, T.4    Seya, T.5
  • 18
    • 0141959224 scopus 로고    scopus 로고
    • LPS-TLR4 signaling to IRF-3/7 and NF-κB involves the Toll adapters TRAM and TRIF
    • Fitzgerald KA, Rowe DC, Barnes BJ et al. LPS-TLR4 signaling to IRF-3/7 and NF-κB involves the Toll adapters TRAM and TRIF. J. Exp. Med. 198(7), 1043-1055 (2003).
    • (2003) J. Exp. Med. , vol.198 , Issue.7 , pp. 1043-1055
    • Fitzgerald, K.A.1    Rowe, D.C.2    Barnes, B.J.3
  • 19
    • 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 et al. TRAM is specifically involved in the Toll-like receptor 4-mediated MyD88-independent signaling pathway. Nat. Immunol. 4(11), 1144-1150 (2003).
    • (2003) Nat. Immunol. , vol.4 , Issue.11 , pp. 1144-1150
    • Yamamoto, M.1    Sato, S.2    Hemmi, H.3
  • 20
    • 0345991221 scopus 로고    scopus 로고
    • TICACM-2: A bridging adapter recruiting to Toll-like receptor 4 TICAM-1 that induces interferon-β
    • Oshiumi H, Sasai M, Shida K, Fujita T, Matsumoto M, Seya T. TICACM-2: a bridging adapter recruiting to Toll-like receptor 4 TICAM-1 that induces interferon-β. J. Biol. Chem. 278(50), 49751-49762 (2003).
    • (2003) J. Biol. Chem. , vol.278 , Issue.50 , pp. 49751-49762
    • Oshiumi, H.1    Sasai, M.2    Shida, K.3    Fujita, T.4    Matsumoto, M.5    Seya, T.6
  • 21
    • 2342475724 scopus 로고    scopus 로고
    • Requirement for a conserved Toll/interleukin-1 resistance domain protein in the Caenorhabditis elegans immune response
    • Liberati NT, Fitzgerald KA, Kim DH, Feinbaum R, Golenbock DT, Ausubel FM. Requirement for a conserved Toll/interleukin-1 resistance domain protein in the Caenorhabditis elegans immune response. Proc. Natl Acad. Sci. USA 101(17), 6593-6598 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , Issue.17 , pp. 6593-6598
    • Liberati, N.T.1    Fitzgerald, K.A.2    Kim, D.H.3    Feinbaum, R.4    Golenbock, D.T.5    Ausubel, F.M.6
  • 22
    • 0029865142 scopus 로고    scopus 로고
    • IRAK: A kinase associated with the interleukin-1 receptor
    • Cao Z, Henzel WJ, Gao X. IRAK: a kinase associated with the interleukin-1 receptor. Science 271(5252), 1128-1131 (1996).
    • (1996) Science , vol.271 , Issue.5252 , pp. 1128-1131
    • Cao, Z.1    Henzel, W.J.2    Gao, X.3
  • 23
    • 0037117543 scopus 로고    scopus 로고
    • IRAK-4: A novel member of the IRAK family with the properties of an IRAK-kinase
    • Li S, Strelow A, Fontana EJ, Wesche H. IRAK-4: a novel member of the IRAK family with the properties of an IRAK-kinase. Proc. Natl Acad. Sci. USA 99(8), 5567-5572 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , Issue.8 , pp. 5567-5572
    • Li, S.1    Strelow, A.2    Fontana, E.J.3    Wesche, H.4
  • 24
    • 2942748292 scopus 로고    scopus 로고
    • IRAK4 kinase activity is redundant for interleukin-1 (IL-1) receptor-associated kinase phosphorylation and IL-1 responsiveness
    • Qin J, Jiang Z, Qian Y, Casanova JL, Li X. IRAK4 kinase activity is redundant for interleukin-1 (IL-1) receptor-associated kinase phosphorylation and IL-1 responsiveness. J. Biol. Chem. 279(25), 26748-26753 (2004).
    • (2004) J. Biol. Chem. , vol.279 , Issue.25 , pp. 26748-26753
    • Qin, J.1    Jiang, Z.2    Qian, Y.3    Casanova, J.L.4    Li, X.5
  • 25
    • 0029761275 scopus 로고    scopus 로고
    • TRAF6 is a signal transducer for interleukin-1
    • Cao Z, Xiong J, Takeuchi M, Kurama T, Goeddel DV. TRAF6 is a signal transducer for interleukin-1. Nature 383(6599), 443-446 (1996).
    • (1996) Nature , vol.383 , Issue.6599 , pp. 443-446
    • Cao, Z.1    Xiong, J.2    Takeuchi, M.3    Kurama, T.4    Goeddel, D.V.5
  • 26
    • 0035913278 scopus 로고    scopus 로고
    • TAK1 is a ubiquitin-dependent kinase of MKK and IKK
    • Wang C, Deng L, Hong M, Akkaraju GR, Inoue J, Chen ZJ. TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature 412(6844), 346-351 (2001).
    • (2001) Nature , vol.412 , Issue.6844 , pp. 346-351
    • Wang, C.1    Deng, L.2    Hong, M.3    Akkaraju, G.R.4    Inoue, J.5    Chen, Z.J.6
  • 27
    • 2342629277 scopus 로고    scopus 로고
    • The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes
    • Sun L, Deng L, Ea CK, Xia ZP, Chen ZJ. The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes. Mol. Cell 14(3), 289-301 (2004).
    • (2004) Mol. Cell , vol.14 , Issue.3 , pp. 289-301
    • Sun, L.1    Deng, L.2    Ea, C.K.3    Xia, Z.P.4    Chen, Z.J.5
  • 28
    • 0035909372 scopus 로고    scopus 로고
    • Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3
    • Alexopoulou L, Holt AC, Medzhitov R, Flavell RA. Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3. Nature 413(6857), 732-738 (2001).
    • (2001) Nature , vol.413 , Issue.6857 , pp. 732-738
    • Alexopoulou, L.1    Holt, A.C.2    Medzhitov, R.3    Flavell, R.A.4
  • 29
    • 0043176281 scopus 로고    scopus 로고
    • Role of adaptor TRIF in the MyD88-independent Toll-like receptor signaling pathway
    • Yamamoto M, Sato S, Hemmi H et al. Role of adaptor TRIF in the MyD88-independent Toll-like receptor signaling pathway. Science 301(5633), 640-643 (2003).
    • (2003) Science , vol.301 , Issue.5633 , pp. 640-643
    • Yamamoto, M.1    Sato, S.2    Hemmi, H.3
  • 30
    • 2442642691 scopus 로고    scopus 로고
    • RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappa B activation
    • Meylan E, Burns K, Hofmann K et al. RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappa B activation. Nat. Immunol. 5(5), 503-507 (2004).
    • (2004) Nat. Immunol. , vol.5 , Issue.5 , pp. 503-507
    • Meylan, E.1    Burns, K.2    Hofmann, K.3
  • 31
    • 27744561393 scopus 로고    scopus 로고
    • Rip1 mediates the Trif-dependent Toll-like receptor 3- and 4-induced NF-{κ}B activation but does not contribute to interferon regulatory factor 3 activation
    • Cusson-Hermance N, Khurana S, Lee TH, Fitzgerald KA, Kelliher MA. Rip1 mediates the Trif-dependent Toll-like receptor 3- and 4-induced NF-{κ}B activation but does not contribute to interferon regulatory factor 3 activation. J. Biol. Chem. 280(44), 36560-36566 (2005).
    • (2005) J. Biol. Chem. , vol.280 , Issue.44 , pp. 36560-36566
    • Cusson-Hermance, N.1    Khurana, S.2    Lee, T.H.3    Fitzgerald, K.A.4    Kelliher, M.A.5
  • 32
    • 24944586285 scopus 로고    scopus 로고
    • Achieving stability of lipopolysaccharide-induced NF-κB activation
    • Covert MW, Leung TH, Gaston JE, Baltimore D. Achieving stability of lipopolysaccharide-induced NF-κB activation. Science 309(5742), 1854-1857 (2005).
    • (2005) Science , vol.309 , Issue.5742 , pp. 1854-1857
    • Covert, M.W.1    Leung, T.H.2    Gaston, J.E.3    Baltimore, D.4
  • 33
    • 24944489952 scopus 로고    scopus 로고
    • Stimulus specificity of gene expression programs determined by temporal control of IKK activity
    • Werner SL, Barken D, Hoffmann A. Stimulus specificity of gene expression programs determined by temporal control of IKK activity. Science 309(5742), 1857-1861 (2005).
    • (2005) Science , vol.309 , Issue.5742 , pp. 1857-1861
    • Werner, S.L.1    Barken, D.2    Hoffmann, A.3
  • 34
    • 0022829867 scopus 로고
    • Mechanisms of human β-interferon gene regulation
    • Maniatis T. Mechanisms of human β-interferon gene regulation. Harvey Lect. 82, 71-104 (1986).
    • (1986) Harvey Lect. , vol.82 , pp. 71-104
    • Maniatis, T.1
  • 35
    • 7444250116 scopus 로고    scopus 로고
    • Role of a transductional-transcriptional processor complex involving MyD88 and IRF-7 in Toll-like receptor signaling
    • Honda K, Yanai H, Mizutani T et al. Role of a transductional-transcriptional processor complex involving MyD88 and IRF-7 in Toll-like receptor signaling. Proc. Natl Acad. Sci. USA 101(43), 15416-15421 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , Issue.43 , pp. 15416-15421
    • Honda, K.1    Yanai, H.2    Mizutani, T.3
  • 36
    • 5444274514 scopus 로고    scopus 로고
    • Interferon-α induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6
    • Kawai T, Sato S, Ishii KJ et al. Interferon-α induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6. Nat. Immunol. 5(10), 1061-1068 (2004).
    • (2004) Nat. Immunol. , vol.5 , Issue.10 , pp. 1061-1068
    • Kawai, T.1    Sato, S.2    Ishii, K.J.3
  • 37
    • 20444380445 scopus 로고    scopus 로고
    • The interferon regulatory factor, IRF5, is a central mediator of Toll-like receptor 7 signaling
    • Schoenemeyer A, Barnes BJ, Mancl ME et al. The interferon regulatory factor, IRF5, is a central mediator of Toll-like receptor 7 signaling. J. Biol. Chem. 280(17), 17005-17012 (2005).
    • (2005) J. Biol. Chem. , vol.280 , Issue.17 , pp. 17005-17012
    • Schoenemeyer, A.1    Barnes, B.J.2    Mancl, M.E.3
  • 38
    • 30544451546 scopus 로고    scopus 로고
    • Specificity in Toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6
    • Hacker H, Redecke V, Blagoev B et al. Specificity in Toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6. Nature 439(7073), 204-207 (2006).
    • (2006) Nature , vol.439 , Issue.7073 , pp. 204-207
    • Hacker, H.1    Redecke, V.2    Blagoev, B.3
  • 39
    • 30544447047 scopus 로고    scopus 로고
    • Critical role of TRAF3 in the Toll-like receptor-dependent and -independent antiviral response
    • Oganesyan G, Saha SK, Guo B et al. Critical role of TRAF3 in the Toll-like receptor-dependent and -independent antiviral response. Nature 439(7073), 208-211 (2006).
    • (2006) Nature , vol.439 , Issue.7073 , pp. 208-211
    • Oganesyan, G.1    Saha, S.K.2    Guo, B.3
  • 40
    • 0038393016 scopus 로고    scopus 로고
    • IKKepsilon and TBK1 are essential components of the IRF3 signaling pathway
    • Fitzgerald KA, McWhirter SM, Faia KL et al. IKKepsilon and TBK1 are essential components of the IRF3 signaling pathway. Nat. Immunol. 4(5), 491-496 (2003).
    • (2003) Nat. Immunol. , vol.4 , Issue.5 , pp. 491-496
    • Fitzgerald, K.A.1    McWhirter, S.M.2    Faia, K.L.3
  • 41
    • 0038363463 scopus 로고    scopus 로고
    • Triggering the interferon antiviral response through an IKK-related pathway
    • Sharma S, tenOever BR, Grandvaux N, Zhou GP, Lin R, Hiscott J. Triggering the interferon antiviral response through an IKK-related pathway. Science 300(5622), 1148-1151 (2003).
    • (2003) Science , vol.300 , Issue.5622 , pp. 1148-1151
    • Sharma, S.1    tenOever, B.R.2    Grandvaux, N.3    Zhou, G.P.4    Lin, R.5    Hiscott, J.6
  • 43
    • 4344566281 scopus 로고    scopus 로고
    • The roles of two IκB kinase-related kinases in lipopolysaccharide and double stranded RNA signaling and viral infection
    • Hemmi H, Takeuchi O, Sato S et al. The roles of two IκB kinase-related kinases in lipopolysaccharide and double stranded RNA signaling and viral infection. J. Exp. Med. 199(12), 1641-1650 (2004).
    • (2004) J. Exp. Med. , vol.199 , Issue.12 , pp. 1641-1650
    • Hemmi, H.1    Takeuchi, O.2    Sato, S.3
  • 44
    • 3042647375 scopus 로고    scopus 로고
    • Differential requirement for TANK-binding kinase-1 in type I interferon responses to Toll-like receptor activation and viral infection
    • Perry AK, Chow EK, Goodnough JB, Yeh WC, Cheng G. Differential requirement for TANK-binding kinase-1 in type I interferon responses to Toll-like receptor activation and viral infection. J. Exp. Med. 199(12), 1651-1658 (2004).
    • (2004) J. Exp. Med. , vol.199 , Issue.12 , pp. 1651-1658
    • Perry, A.K.1    Chow, E.K.2    Goodnough, J.B.3    Yeh, W.C.4    Cheng, G.5
  • 45
    • 20244388983 scopus 로고    scopus 로고
    • Interleukin-1 receptor-associated kinase-1 plays an essential role for Toll-like receptor (TLR)7- and TLR9-mediated interferon-{alpha} induction
    • Uematsu S, Sato S, Yamamoto M et al. Interleukin-1 receptor-associated kinase-1 plays an essential role for Toll-like receptor (TLR)7- and TLR9-mediated interferon-{alpha} induction. J. Exp. Med. 201(6), 915-923 (2005).
    • (2005) J. Exp. Med. , vol.201 , Issue.6 , pp. 915-923
    • Uematsu, S.1    Sato, S.2    Yamamoto, M.3
  • 46
    • 0141919557 scopus 로고    scopus 로고
    • Interferon regulatory factor 5, a novel mediator of cell cycle arrest and cell death
    • Barnes BJ, Kellum MJ, Pinder KE, Frisancho JA, Pitha PM. Interferon regulatory factor 5, a novel mediator of cell cycle arrest and cell death. Cancer Res. 63(19), 6424-6431 (2003).
    • (2003) Cancer Res. , vol.63 , Issue.19 , pp. 6424-6431
    • Barnes, B.J.1    Kellum, M.J.2    Pinder, K.E.3    Frisancho, J.A.4    Pitha, P.M.5
  • 47
    • 15044345461 scopus 로고    scopus 로고
    • Integral role of IRF-5 in the gene induction programme activated by Toll-like receptors
    • Takaoka A, Yanai H, Kondo S et al. Integral role of IRF-5 in the gene induction programme activated by Toll-like receptors. Nature 434(7030), 243-249 (2005).
    • (2005) Nature , vol.434 , Issue.7030 , pp. 243-249
    • Takaoka, A.1    Yanai, H.2    Kondo, S.3
  • 48
    • 2942721674 scopus 로고    scopus 로고
    • ST2 is an inhibitor of interleukin 1 receptor and Toll-like receptor 4 signaling and maintains endotoxin tolerance
    • Brint EK, Xu D, Liu H et al. ST2 is an inhibitor of interleukin 1 receptor and Toll-like receptor 4 signaling and maintains endotoxin tolerance. Nat. Immunol. 5(4), 373-379 (2004).
    • (2004) Nat. Immunol. , vol.5 , Issue.4 , pp. 373-379
    • Brint, E.K.1    Xu, D.2    Liu, H.3
  • 49
    • 0042733592 scopus 로고    scopus 로고
    • SIGIRR, a negative regulator of Toll-like receptor-interleukin 1 receptor signaling
    • Wald D, Qin J, Zhao Z et al. SIGIRR, a negative regulator of Toll-like receptor-interleukin 1 receptor signaling. Nat. Immunol. 4(9), 920-927 (2003).
    • (2003) Nat. Immunol. , vol.4 , Issue.9 , pp. 920-927
    • Wald, D.1    Qin, J.2    Zhao, Z.3
  • 50
    • 20644450101 scopus 로고    scopus 로고
    • Negative regulation of Toll-like receptor 4 signaling by the Toll-like receptor homolog RP105
    • Divanovic S, Trompette A, Atabani SF et al. Negative regulation of Toll-like receptor 4 signaling by the Toll-like receptor homolog RP105. Nat. Immunol. 6(6), 571-578 (2005).
    • (2005) Nat. Immunol. , vol.6 , Issue.6 , pp. 571-578
    • Divanovic, S.1    Trompette, A.2    Atabani, S.F.3
  • 51
    • 10344260656 scopus 로고    scopus 로고
    • TRAIL-R as a negative regulator of innate immune cell responses
    • Diehl GE, Yue HH, Hsieh K et al. TRAIL-R as a negative regulator of innate immune cell responses. Immunity 21(6), 877-889 (2004).
    • (2004) Immunity , vol.21 , Issue.6 , pp. 877-889
    • Diehl, G.E.1    Yue, H.H.2    Hsieh, K.3
  • 52
    • 0842278645 scopus 로고    scopus 로고
    • Cutting edge: Toll-like receptor signaling in macrophages induces ligands for the NKG2D receptor
    • Hamerman JA Ogasawara K, Lanier LL. Cutting edge: Toll-like receptor signaling in macrophages induces ligands for the NKG2D receptor. J. Immunol. 172(4), 2001-2005 (2004).
    • (2004) J. Immunol. , vol.172 , Issue.4 , pp. 2001-2005
    • Hamerman, J.A.1    Ogasawara, K.2    Lanier, L.L.3
  • 53
    • 0042236366 scopus 로고    scopus 로고
    • MyD88S, a splice variant of MyD88, differentially modulates NF-κB- and AP-1-dependent gene expression
    • Janssens S, Burns K, Vercammen E, Tschopp J, Beyaert R. MyD88S, a splice variant of MyD88, differentially modulates NF-κB- and AP-1-dependent gene expression. FEBS Lett. 548(1-3), 103-107 (2003).
    • (2003) FEBS Lett. , vol.548 , Issue.1-3 , pp. 103-107
    • Janssens, S.1    Burns, K.2    Vercammen, E.3    Tschopp, J.4    Beyaert, R.5
  • 55
    • 27644548945 scopus 로고    scopus 로고
    • Negative regulation of Toll-like-receptor signaling by IRF-4
    • Negishi H, Ohba Y, Yanai H et al. Negative regulation of Toll-like-receptor signaling by IRF-4. Proc. Natl Acad. Sci. USA 102(44), 15989-15994 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , Issue.44 , pp. 15989-15994
    • Negishi, H.1    Ohba, Y.2    Yanai, H.3
  • 56
    • 11144233242 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling (SOCS) proteins indirectly regulate Toll-like receptor signaling in innate immune cells
    • Baetz A, Frey M, Heeg K, Dalpke AH. Suppressor of cytokine signaling (SOCS) proteins indirectly regulate Toll-like receptor signaling in innate immune cells. J. Biol. Chem. 279(52), 54708-54715 (2004).
    • (2004) J. Biol. Chem. , vol.279 , Issue.52 , pp. 54708-54715
    • Baetz, A.1    Frey, M.2    Heeg, K.3    Dalpke, A.H.4
  • 57
    • 31344467156 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling 1 negatively regulates Toll-like receptor signaling by mediating Mal degradation
    • Mansell A, Smith R, Doyle SL et al. Suppressor of cytokine signaling 1 negatively regulates Toll-like receptor signaling by mediating Mal degradation. Nat. Immunol. 7(2), 148-155 (2006).
    • (2006) Nat. Immunol. , vol.7 , Issue.2 , pp. 148-155
    • Mansell, A.1    Smith, R.2    Doyle, S.L.3
  • 58
    • 5444223519 scopus 로고    scopus 로고
    • The ubiquitin-modifying enzyme A20 is required for termination of Toll-like receptor responses
    • Boone DL, Turer EE, Lee EG et al. The ubiquitin-modifying enzyme A20 is required for termination of Toll-like receptor responses. Nat. Immunol. 5(10), 1052-1060 (2004).
    • (2004) Nat. Immunol. , vol.5 , Issue.10 , pp. 1052-1060
    • Boone, D.L.1    Turer, E.E.2    Lee, E.G.3
  • 59
    • 4444257589 scopus 로고    scopus 로고
    • A20 inhibits toll-like receptor 2- and 4-mediated interleukin-8 synthesis in airway epithelial cells
    • Gon Y, Asai Y, Hashimoto S et al. A20 inhibits toll-like receptor 2- and 4-mediated interleukin-8 synthesis in airway epithelial cells. Am. J. Respir. Cell Mol. Biol. 31(3), 330-336 (2004).
    • (2004) Am. J. Respir. Cell Mol. Biol. , vol.31 , Issue.3 , pp. 30-336
    • Gon, Y.1    Asai, Y.2    Hashimoto, S.3
  • 60
    • 0037418749 scopus 로고    scopus 로고
    • Regulation of Toll-like receptor 4 signalling by A20 zinc finger protein
    • O'Reilly SM, Moynagh PN. Regulation of Toll-like receptor 4 signalling by A20 zinc finger protein. Biochem. Biophys. Res. Commun. 303(2), 586-593 (2003).
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , Issue.2 , pp. 586-593
    • O'Reilly, S.M.1    Moynagh, P.N.2
  • 61
    • 0037629646 scopus 로고    scopus 로고
    • PI3K and negative regulation of TLR signaling
    • Fukao T, Koyasu S. PI3K and negative regulation of TLR signaling. Trends Immunol. 24(7), 358-363 (2003).
    • (2003) Trends Immunol. , vol.24 , Issue.7 , pp. 358-363
    • Fukao, T.1    Koyasu, S.2
  • 62
    • 20644450804 scopus 로고    scopus 로고
    • Negative regulation of Toll-like receptor-mediated immune responses
    • Liew FY, Xu D, Brint EK, O'Neill LA. Negative regulation of Toll-like receptor-mediated immune responses. Nat. Rev. Immunol. 5(6), 446-458 (2005).
    • (2005) Nat. Rev. Immunol. , vol.5 , Issue.6 , pp. 446-458
    • Liew, F.Y.1    Xu, D.2    Brint, E.K.3    O'Neill, L.A.4
  • 63
    • 1842607444 scopus 로고    scopus 로고
    • Primary immunodeficiency to pneumococcal infection due to a defect in Toll-like receptor signaling
    • Currie AJ, Davidson DJ, Reid GS et al. Primary immunodeficiency to pneumococcal infection due to a defect in Toll-like receptor signaling. J. Pediatr. 144(4), 512-518 (2004).
    • (2004) J. Pediatr. , vol.144 , Issue.4 , pp. 512-518
    • Currie, A.J.1    Davidson, D.J.2    Reid, G.S.3
  • 64
    • 18944391904 scopus 로고    scopus 로고
    • Cutting edge: Expression of IL-1 receptor-associated kinase-4 (IRAK-4) proteins with mutations identified in a patient with recurrent bacterial infections alters normal IRAK-4 interaction with components of the IL-1 receptor complex
    • Medvedev AE, Thomas K, Awomoyi A et al. Cutting edge: expression of IL-1 receptor-associated kinase-4 (IRAK-4) proteins with mutations identified in a patient with recurrent bacterial infections alters normal IRAK-4 interaction with components of the IL-1 receptor complex. J. Immunol. 174(11), 6587-6591 (2005).
    • (2005) J. Immunol. , vol.174 , Issue.11 , pp. 6587-6591
    • Medvedev, A.E.1    Thomas, K.2    Awomoyi, A.3
  • 65
    • 27744534928 scopus 로고    scopus 로고
    • Human TLR-7-, -8-, and -9-mediated induction of IFN-α/β and -λ. Is IRAK-4 dependent and redundant for protective immunity to viruses
    • Yang K, Puel A, Zhang S et al. Human TLR-7-, -8-, and -9-mediated induction of IFN-α/β and -λ. Is IRAK-4 dependent and redundant for protective immunity to viruses. Immunity 23(5), 465-478 (2005).
    • (2005) Immunity , vol.23 , Issue.5 , pp. 465-478
    • Yang, K.1    Puel, A.2    Zhang, S.3
  • 66
    • 5444254408 scopus 로고    scopus 로고
    • Toll-like receptors in the pathogenesis of human disease
    • Cook DN, Pisetsky DS, Schwartz DA. Toll-like receptors in the pathogenesis of human disease. Nat. Immunol. 5(10), 975-979 (2004).
    • (2004) Nat. Immunol. , vol.5 , Issue.10 , pp. 975-979
    • Cook, D.N.1    Pisetsky, D.S.2    Schwartz, D.A.3
  • 67
    • 0007568640 scopus 로고    scopus 로고
    • Genetic analysis of host responses in sepsis
    • Beutler B, Ulevitch RJ. Genetic analysis of host responses in sepsis. Curr. Infect. Dis. Rep. 3(5), 419-426 (2001).
    • (2001) Curr. Infect. Dis. Rep. , vol.3 , Issue.5 , pp. 419-426
    • Beutler, B.1    Ulevitch, R.J.2
  • 68
    • 3242728901 scopus 로고    scopus 로고
    • Reduced atherosclerosis in MyD88-null mice links elevated serum cholesterol levels to activation of innate immunity signaling pathways
    • Bjorkbacka 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. 10(4), 416-421 (2004).
    • (2004) Nat. Med. , vol.10 , Issue.4 , pp. 416-421
    • Bjorkbacka, H.1    Kunjathoor, V.V.2    Moore, K.J.3
  • 69
    • 0037130195 scopus 로고    scopus 로고
    • Toll-like receptor 4 polymorphisms and atherogenesis
    • Kiechl S, Lorenz E, Reindl M et al. Toll-like receptor 4 polymorphisms and atherogenesis. N. Engl. J. Med. 347(3), 185-192 (2002).
    • (2002) N. Engl. J. Med. , vol.347 , Issue.3 , pp. 185-192
    • Kiechl, S.1    Lorenz, E.2    Reindl, M.3
  • 70
    • 21844438276 scopus 로고    scopus 로고
    • A Toll for lupus
    • Anders HJ. A Toll for lupus. Lupus 14(6), 417-422 (2005).
    • (2005) Lupus , vol.14 , Issue.6 , pp. 417-422
    • Anders, H.J.1
  • 71
    • 1642275654 scopus 로고    scopus 로고
    • Signaling danger: Toll-like receptors and their potential roles in kidney disease
    • Anders HJ, Banas B, Schlondorff D. Signaling danger: Toll-like receptors and their potential roles in kidney disease. J. Am. Soc. Nephrol. 15(4), 854-867 (2004).
    • (2004) J. Am. Soc. Nephrol. , vol.15 , Issue.4 , pp. 854-867
    • Anders, H.J.1    Banas, B.2    Schlondorff, D.3
  • 72
    • 17644366913 scopus 로고    scopus 로고
    • NOD-LRR proteins: Role in host-microbial interactions and inflammatory disease
    • Inohara, Chamaillard, McDonald C, Nunez G. NOD-LRR proteins: role in host-microbial interactions and inflammatory disease. Annu. Rev. Biochem. 74, 355-383 (2005).
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 355-383
    • Inohara1    Chamaillard2    McDonald, C.3    Nunez, G.4
  • 73
    • 0038624558 scopus 로고    scopus 로고
    • NODS: Intracellular proteins involved in inflammation and apoptosis
    • Inohara N, Nunez G. NODS: intracellular proteins involved in inflammation and apoptosis. Nat. Rev. Immunol. 3(5), 371-382 (2003).
    • (2003) Nat. Rev. Immunol. , vol.3 , Issue.5 , pp. 371-382
    • Inohara, N.1    Nunez, G.2
  • 74
    • 0038615855 scopus 로고    scopus 로고
    • NOD1 detects a unique muropeptide from Gram-negative bacterial peptidoglycan
    • Girardin SE, Boneca IG, Carneiro LA et al. NOD1 detects a unique muropeptide from Gram-negative bacterial peptidoglycan. Science 300(5625), 1584-1587 (2003).
    • (2003) Science , vol.300 , Issue.5625 , pp. 584-1587
    • Girardin, S.E.1    Boneca, I.G.2    Carneiro, L.A.3
  • 75
    • 3442893287 scopus 로고    scopus 로고
    • Mini-review: The role of peptidoglycan recognition in innate immunity
    • Girardin SE, Philpott DJ. Mini-review: the role of peptidoglycan recognition in innate immunity. Eur. J. Immunol. 34(7), 1777-1182 (2004).
    • (2004) Eur. J. Immunol. , vol.34 , Issue.7 , pp. 1182-1777
    • Girardin, S.E.1    Philpott, D.J.2
  • 76
    • 2542466966 scopus 로고    scopus 로고
    • Innate immune recognition of microbes through Nod1 and Nod2: Implications for disease
    • Carneiro LA, Travassos LH, Philpott DJ. Innate immune recognition of microbes through Nod1 and Nod2: implications for disease. Microbes Infect. 6(6), 609-616 (2004).
    • (2004) Microbes Infect. , vol.6 , Issue.6 , pp. 609-616
    • Carneiro, L.A.1    Travassos, L.H.2    Philpott, D.J.3
  • 77
    • 2342583513 scopus 로고    scopus 로고
    • Regulatory regions and critical residues of NOD2 involved in muramyl dipeptide recognition
    • Tanabe T, Chamaillard M, Ogura Y et al. Regulatory regions and critical residues of NOD2 involved in muramyl dipeptide recognition. EMBO J. 23(7), 1587-1597 (2004).
    • (2004) EMBO J. , vol.23 , Issue.7 , pp. 1587-1597
    • Tanabe, T.1    Chamaillard, M.2    Ogura, Y.3
  • 78
    • 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. 14(21), 1929-1934 (2004).
    • (2004) Curr. Biol. , vol.14 , Issue.21 , pp. 1929-1934
    • Martinon, F.1    Agostini, L.2    Meylan, E.3    Tschopp, J.4
  • 79
    • 0141861083 scopus 로고    scopus 로고
    • Recognition of bacterial peptidoglycan by the innate immune system
    • Dziarski R. Recognition of bacterial peptidoglycan by the innate immune system. Cell. Mol. Life Sci. 60(9), 1793-1804 (2003).
    • (2003) Cell. Mol. Life Sci. , vol.60 , Issue.9 , pp. 1793-1804
    • Dziarski, R.1
  • 81
    • 3142654767 scopus 로고    scopus 로고
    • Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf
    • Mariathasan S, Newton K, Monack DM et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 430(6996), 213-218 (2004).
    • (2004) Nature , vol.430 , Issue.6996 , pp. 213-218
    • Mariathasan, S.1    Newton, K.2    Monack, D.M.3
  • 82
    • 0037425584 scopus 로고    scopus 로고
    • Naip5 affects host susceptibility to the intracellular pathogen Legionella pneumophila
    • Wright EK, Goodart SA, Growney JD et al. Naip5 affects host susceptibility to the intracellular pathogen Legionella pneumophila. Curr. Biol. 13(1), 27-36 (2003).
    • (2003) Curr. Biol. , vol.13 , Issue.1 , pp. 27-36
    • Wright, E.K.1    Goodart, S.A.2    Growney, J.D.3
  • 83
    • 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 410(6832), 1099-1103 (2001).
    • (2001) Nature , vol.410 , Issue.6832 , pp. 1099-1103
    • Hayashi, F.1    Smith, K.D.2    Ozinsky, A.3
  • 84
    • 0347776208 scopus 로고    scopus 로고
    • Toll-like receptor 5 recognizes a conserved site on flagellin required for protofilament formation and bacterial motility
    • Smith KD, Andersen-Nissen E, Hayashi F et al. Toll-like receptor 5 recognizes a conserved site on flagellin required for protofilament formation and bacterial motility. Nat. Immunol. 4(12), 1247-1253 (2003).
    • (2003) Nat. Immunol. , vol.4 , Issue.12 , pp. 1247-1253
    • Smith, K.D.1    Andersen-Nissen, E.2    Hayashi, F.3
  • 85
    • 0037075551 scopus 로고    scopus 로고
    • RICK/Rip2/CARDIAK mediates signalling for receptors of the innate and adaptive immune systems
    • Kobayashi K, Inohara N, Hernandez LD et al. RICK/Rip2/CARDIAK mediates signalling for receptors of the innate and adaptive immune systems. Nature 416(6877), 194-199 (2002).
    • (2002) Nature , vol.416 , Issue.6877 , pp. 194-199
    • Kobayashi, K.1    Inohara, N.2    Hernandez, L.D.3
  • 86
    • 0037075549 scopus 로고    scopus 로고
    • Involvement of receptor-interacting protein 2 in innate and adaptive immune responses
    • Chin AI, Dempsey PW, Bruhn K, Miller JF, Xu Y, Cheng G. Involvement of receptor-interacting protein 2 in innate and adaptive immune responses. Nature 416(6877), 190-194 (2002).
    • (2002) Nature , vol.416 , Issue.6877 , pp. 190-194
    • Chin, A.I.1    Dempsey, P.W.2    Bruhn, K.3    Miller, J.F.4    Xu, Y.5    Cheng, G.6
  • 87
    • 0346350694 scopus 로고    scopus 로고
    • Cutting edge: CIAS1/cryopyrin/PYPAF1/NALP3/CATE RPILLER 1.1 is an inducible inflammatory mediator with NF-κB suppressive properties
    • O'Connor W Jr, Harton JA, Zhu X, Linhoff MW, Ting JP. Cutting edge: CIAS1/cryopyrin/PYPAF1/NALP3/CATE RPILLER 1.1 is an inducible inflammatory mediator with NF-κB suppressive properties. J. Immunol. 171(12), 6329-6333 (2003).
    • (2003) J. Immunol. , vol.171 , Issue.12 , pp. 6329-6333
    • O'Connor Jr., W.1    Harton, J.A.2    Zhu, X.3    Linhoff, M.W.4    Ting, J.P.5
  • 89
    • 18644368579 scopus 로고    scopus 로고
    • Functional screening of five PYPAF family members identifies PYPAF5 as a novel regulator of NF-κB and caspase-1
    • Grenier JM, Wang L, Manji GA et al. Functional screening of five PYPAF family members identifies PYPAF5 as a novel regulator of NF-κB and caspase-1. FEBS Lett. 530(1-3), 73-78 (2002).
    • (2002) FEBS Lett. , vol.530 , Issue.1-3 , pp. 73-78
    • Grenier, J.M.1    Wang, L.2    Manji, G.A.3
  • 90
    • 0037470744 scopus 로고    scopus 로고
    • ASC is an activating adaptor for NF-κB and caspase-8-dependent apoptosis
    • Masumoto J, Dowds TA, Schaner P et al. ASC is an activating adaptor for NF-κB and caspase-8-dependent apoptosis. Biochem. Biophys. Res. Commun. 303(1), 69-73 (2003).
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , Issue.1 , pp. 69-73
    • Masumoto, J.1    Dowds, T.A.2    Schaner, P.3
  • 91
    • 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 440(7081), 237-241 (2006).
    • (2006) Nature , vol.440 , Issue.7081 , pp. 237-241
    • Martinon, F.1    Petrilli, V.2    Mayor, A.3    Tardivel, A.4    Tschopp, J.5
  • 92
    • 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 440(7081), 228-232 (2006).
    • (2006) Nature , vol.440 , Issue.7081 , pp. 228-232
    • Mariathasan, S.1    Weiss, D.S.2    Newton, K.3
  • 93
    • 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 440(7081), 233-236 (2006).
    • (2006) Nature , vol.440 , Issue.7081 , pp. 233-236
    • Kanneganti, T.D.1    Ozoren, N.2    Body-Malapel, M.3
  • 94
    • 30844432876 scopus 로고    scopus 로고
    • Cryopyrin and pyrin activate caspase-1, but not NF-κB, via ASC oligomerization
    • Yu JW, Wu J, Zhang Z et al. Cryopyrin and pyrin activate caspase-1, but not NF-κB, via ASC oligomerization. Cell Death Differ. 13(2), 236-249 (2006).
    • (2006) Cell Death Differ , vol.13 , Issue.2 , pp. 236-249
    • Yu, J.W.1    Wu, J.2    Zhang, Z.3
  • 96
    • 0141998606 scopus 로고    scopus 로고
    • Molecular identification of a danger signal that alerts the immune system to dying cells
    • Shi Y, Evans JE, Rock KL. Molecular identification of a danger signal that alerts the immune system to dying cells. Nature 425(6957), 516-521 (2003).
    • (2003) Nature , vol.425 , Issue.6957 , pp. 516-521
    • Shi, Y.1    Evans, J.E.2    Rock, K.L.3
  • 97
    • 0037221395 scopus 로고    scopus 로고
    • Crohn's disease-associated NOD2 variants share a signaling defect in response to lipopolysaccharide and peptidoglycan
    • Bonen DK, Ogura Y, Nicolae DL et al. Crohn's disease-associated NOD2 variants share a signaling defect in response to lipopolysaccharide and peptidoglycan. Gastroenterology 124(1), 140-146 (2003).
    • (2003) Gastroenterology , vol.124 , Issue.1 , pp. 140-146
    • Bonen, D.K.1    Ogura, Y.2    Nicolae, D.L.3
  • 98
    • 0036745064 scopus 로고    scopus 로고
    • Association of mutations in the NALP3/CIAS1/PYPAF1 gene with abroad phenotype including recurrent fever, cold sensitivity, sensorineural deafness, and AA amyloidosis
    • Aganna E, Martinon F, Hawkins PN et al. Association of mutations in the NALP3/CIAS1/PYPAF1 gene with abroad phenotype including recurrent fever, cold sensitivity, sensorineural deafness, and AA amyloidosis. Arthritis Rheum. 46(9), 2445-2452 (2002).
    • (2002) Arthritis Rheum. , vol.46 , Issue.9 , pp. 2445-2452
    • Aganna, E.1    Martinon, F.2    Hawkins, P.N.3
  • 99
    • 1642285783 scopus 로고    scopus 로고
    • NALP3 forms an IL-1β-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder
    • Agostini L, Martinon F, Burns K, McDermott MF, Hawkins PN, Tschopp J. NALP3 forms an IL-1β-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder. Immunity 20(3), 319-325 (2004).
    • (2004) Immunity , vol.20 , Issue.3 , pp. 319-325
    • Agostini, L.1    Martinon, F.2    Burns, K.3    McDermott, M.F.4    Hawkins, P.N.5    Tschopp, J.6
  • 100
    • 17144404177 scopus 로고    scopus 로고
    • IRF-7 is the master regulator of type-I interferon-dependent immune responses
    • Honda K, Yanai H, Negishi H et al. IRF-7 is the master regulator of type-I interferon-dependent immune responses. Nature 434(7034), 772-777 (2005).
    • (2005) Nature , vol.434 , Issue.7034 , pp. 772-777
    • Honda, K.1    Yanai, H.2    Negishi, H.3
  • 101
    • 0035978533 scopus 로고    scopus 로고
    • A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease
    • Ogura Y, Bonen DK, Inohara N et al. A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease. Nature 411(6837), 603-606 (2001).
    • (2001) Nature , vol.411 , Issue.6837 , pp. 603-606
    • Ogura, Y.1    Bonen, D.K.2    Inohara, N.3
  • 102
    • 0012135426 scopus 로고    scopus 로고
    • 3020insC mutation within the NOD2 gene in Crohn's disease: Frequency and association with clinical pattern in an Italian population
    • Vavassori P, Borgiani P, D'Apice MR et al. 3020insC mutation within the NOD2 gene in Crohn's disease: frequency and association with clinical pattern in an Italian population. Dig. Liver Dis. 34(2), 153 (2002).
    • (2002) Dig. Liver Dis. , vol.34 , Issue.2 , pp. 153
    • Vavassori, P.1    Borgiani, P.2    D'Apice, M.R.3
  • 103
    • 4444383817 scopus 로고    scopus 로고
    • The 3020insC mutation of the NOD2/CARD15 gene in patients with periodontal disease
    • Folwaczny M, Glas J, Torok HP, Mauermann D, Folwaczny C. The 3020insC mutation of the NOD2/CARD15 gene in patients with periodontal disease. Eur. J. Oral Sci. 112(4), 316-319 (2004).
    • (2004) Eur. J. Oral Sci. , vol.112 , Issue.4 , pp. 316-319
    • Folwaczny, M.1    Glas, J.2    Torok, H.P.3    Mauermann, D.4    Folwaczny, C.5
  • 104
    • 1842666807 scopus 로고    scopus 로고
    • NOD2 3020insC frameshift mutation is not associated with inflammatory bowel disease in Chinese patients of Han nationality
    • Guo QS, Xia B, Jiang Y, Qu Y, Li J. NOD2 3020insC frameshift mutation is not associated with inflammatory bowel disease in Chinese patients of Han nationality. World J. Gastroenterol. 10(7), 1069-1071 (2004).
    • (2004) World J. Gastroenterol. , vol.10 , Issue.7 , pp. 1069-1071
    • Guo, Q.S.1    Xia, B.2    Jiang, Y.3    Qu, Y.4    Li, J.5
  • 105
    • 12144287610 scopus 로고    scopus 로고
    • The NOD2 3020insC mutation and the risk of colorectal cancer
    • Kurzawski G, Suchy J, Kladny J. et al. The NOD2 3020insC mutation and the risk of colorectal cancer. Cancer Res. 64(5), 1604-1606 (2004).
    • (2004) Cancer Res. , vol.64 , Issue.5 , pp. 1604-1606
    • Kurzawski, G.1    Suchy, J.2    Kladny, J.3
  • 106
    • 3242813113 scopus 로고    scopus 로고
    • The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses
    • Yoneyama M, Kikuchi M, Natsukawa T et al. The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. Nat. Immunol. 5(7), 730-737 (2004).
    • (2004) Nat. Immunol. , vol.5 , Issue.7 , pp. 730-737
    • Yoneyama, M.1    Kikuchi, M.2    Natsukawa, T.3
  • 107
    • 1642348822 scopus 로고    scopus 로고
    • Expression analysis and genomic characterization of human melanoma differentiation associated gene-5, mda-5: A novel type I interferon-responsive apoptosis-inducing gene
    • Kang DC, Gopalkrishnan RV, Lin L et al. Expression analysis and genomic characterization of human melanoma differentiation associated gene-5, mda-5: a novel type I interferon-responsive apoptosis-inducing gene. Oncogene 23(9), 1789-1800 (2004).
    • (2004) Oncogene , vol.23 , Issue.9 , pp. 1789-1800
    • Kang, D.C.1    Gopalkrishnan, R.V.2    Lin, L.3
  • 108
    • 0037154176 scopus 로고    scopus 로고
    • mda-5: An interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties
    • Kang DC, Gopalkrishnan RV, Wu Q, Jankowsky E, Pyle AM, Fisher PB. mda-5: an interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties. Proc. Natl Acad. Sci. USA 99(2), 637-642 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , Issue.2 , pp. 637-642
    • Kang, D.C.1    Gopalkrishnan, R.V.2    Wu, Q.3    Jankowsky, E.4    Pyle, A.M.5    Fisher, P.B.6
  • 109
    • 13944253573 scopus 로고    scopus 로고
    • Regulating intracellular antiviral defense and permissiveness to hepatitis C virus RNA replication through a cellular RNA helicase, RIG-I
    • Sumpter R Jr, Loo YM, Foy E et al. Regulating intracellular antiviral defense and permissiveness to hepatitis C virus RNA replication through a cellular RNA helicase, RIG-I. J. Virol. 79(5), 2689-2699 (2005).
    • (2005) J. Virol. , vol.79 , Issue.5 , pp. 2689-2699
    • Sumpter Jr., R.1    Loo, Y.M.2    Foy, E.3
  • 110
    • 26844503987 scopus 로고    scopus 로고
    • The RNA helicase Lgp2 inhibits TLR-independent sensing of viral replication by retinoic acid-inducible gene-I
    • Rothenfusser S, Goutagny N, DiPerna G et al. The RNA helicase Lgp2 inhibits TLR-independent sensing of viral replication by retinoic acid-inducible gene-I. J. Immunol. 175(8), 5260-5268 (2005).
    • (2005) J. Immunol. , vol.175 , Issue.8 , pp. 5260-5268
    • Rothenfusser, S.1    Goutagny, N.2    DiPerna, G.3
  • 111
    • 22544455673 scopus 로고    scopus 로고
    • type-specific involvement of RIG-I in antiviral response
    • Kato H, Sato S, Yoneyama M et al. Cell type-specific involvement of RIG-I in antiviral response. Immunity 23(1), 19-28 (2005).
    • (2005) Immunity , vol.23 , Issue.1 , pp. 19-28
    • Kato, H.1    Sato, S.2    Yoneyama, M.3
  • 112
    • 27144440523 scopus 로고    scopus 로고
    • IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction
    • Kawai T, Takahashi K, Sato S et al. IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction. Nat. Immunol. 6(10), 981-988 (2005).
    • (2005) Nat. Immunol. , vol.6 , Issue.10 , pp. 981-988
    • Kawai, T.1    Takahashi, K.2    Sato, S.3
  • 113
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • Meylan E, Curran J, Hofmann K et al. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature 437(7062), 1167-1172 (2005).
    • (2005) Nature , vol.437 , Issue.7062 , pp. 1167-1172
    • Meylan, E.1    Curran, J.2    Hofmann, K.3
  • 114
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-κB and IRF3
    • Seth RB, Sun L, Ea CK, Chen ZJ. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-κB and IRF3. Cell 122(5), 669-682 (2005).
    • (2005) Cell , vol.122 , Issue.5 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.K.3    Chen, Z.J.4
  • 115
    • 24944538819 scopus 로고    scopus 로고
    • VISA is an adapter protein required for virus-triggered IFN-β signaling
    • Xu LG, Wang YY, Han KJ, Li LY, Zhai Z, Shu HB. VISA is an adapter protein required for virus-triggered IFN-β signaling. Mol. Cell 19(6), 727-740 (2005).
    • (2005) Mol. Cell , vol.19 , Issue.6 , pp. 727-740
    • Xu, L.G.1    Wang, Y.Y.2    Han, K.J.3    Li, L.Y.4    Zhai, Z.5    Shu, H.B.6
  • 116
    • 20044379559 scopus 로고    scopus 로고
    • Control of antiviral defenses through hepatitis C virus disruption of retinoic acid-inducible gene-I signaling
    • Foy E, Li K, Sumpter R Jr et al. Control of antiviral defenses through hepatitis C virus disruption of retinoic acid-inducible gene-I signaling. Proc. Natl Acad. Sci. USA 102(8), 2986-2991 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , Issue.8 , pp. 2986-2991
    • Foy, E.1    Li, K.2    Sumpter Jr., R.3
  • 117
    • 29144462494 scopus 로고    scopus 로고
    • Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity
    • Li XD, Sun L, Seth RB, Pineda G, Chen ZJ. Hepatitis C virus protease NS3/ 4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity. Proc. Natl Acad. Sci. USA 102(49), 17717-17722 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , Issue.49 , pp. 17717-17722
    • Li, X.D.1    Sun, L.2    Seth, R.B.3    Pineda, G.4    Chen, Z.J.5
  • 118
    • 10344259136 scopus 로고    scopus 로고
    • The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-β promoter
    • Andrejeva J, Childs KS, Young DF et al. The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-β promoter. Proc. Natl Acad. Sci. USA 101(49), 17264-17269 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , Issue.49 , pp. 17264-17269
    • Andrejeva, J.1    Childs, K.S.2    Young, D.F.3
  • 119
    • 0035885853 scopus 로고    scopus 로고
    • The Stat3/5 locus encodes novel endoplasmic reticulum and helicase-like proteins that are preferentially expressed in normal and neoplastic mammary tissue
    • Cui Y, Li M, Walton KD et al. The Stat3/5 locus encodes novel endoplasmic reticulum and helicase-like proteins that are preferentially expressed in normal and neoplastic mammary tissue. Genomics 78(3), 129-134 (2001).
    • (2001) Genomics , vol.78 , Issue.3 , pp. 129-134
    • Cui, Y.1    Li, M.2    Walton, K.D.3
  • 120
    • 23844438864 scopus 로고    scopus 로고
    • Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity
    • Yoneyama M, Kikuchi M, Matsumoto K et al. Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity. J. Immunol. 175(5), 2851-2858 (2005).
    • (2005) J. Immunol. , vol.175 , Issue.5 , pp. 2851-2858
    • Yoneyama, M.1    Kikuchi, M.2    Matsumoto, K.3
  • 121
    • 30444450839 scopus 로고    scopus 로고
    • Recognition of cytosolic DNA activates an IRF3-dependent innate immune response
    • Stetson DB, Medzhitov R. Recognition of cytosolic DNA activates an IRF3-dependent innate immune response. Immunity 24(1), 93-103 (2006).
    • (2006) Immunity , vol.24 , Issue.1 , pp. 93-103
    • Stetson, D.B.1    Medzhitov, R.2
  • 122
    • 29244471275 scopus 로고    scopus 로고
    • A Toll-like receptor-independent antiviral response induced by double-stranded B-form DNA
    • Ishii KJ, Coban C, Kato H et al. A Toll-like receptor-independent antiviral response induced by double-stranded B-form DNA. Nat. Immunol. 7(1), 40-48 (2006).
    • (2006) Nat. Immunol. , vol.7 , Issue.1 , pp. 40-48
    • Ishii, K.J.1    Coban, C.2    Kato, H.3
  • 123
    • 0032191166 scopus 로고    scopus 로고
    • The serum mannose-binding protein and the macrophage mannose receptor are pattern recognition molecules that link innate and adaptive immunity
    • Fraser IP, Koziel H, Ezekowitz RA. The serum mannose-binding protein and the macrophage mannose receptor are pattern recognition molecules that link innate and adaptive immunity. Semin. Immunol. 10(5), 363-372 (1998).
    • (1998) Semin. Immunol. , vol.10 , Issue.5 , pp. 363-372
    • Fraser, I.P.1    Koziel, H.2    Ezekowitz, R.A.3
  • 124
    • 5144222255 scopus 로고    scopus 로고
    • Complement: A unique innate immune sensor for danger signals
    • Gasque P. Complement: a unique innate immune sensor for danger signals. Mol. Immunol. 41(11), 1089-1098 (2004).
    • (2004) Mol. Immunol. , vol.41 , Issue.11 , pp. 1089-1098
    • Gasque, P.1
  • 125
    • 15944390196 scopus 로고    scopus 로고
    • How C-type lectins detect pathogens
    • Cambi A, Koopman M, Figdor CG. How C-type lectins detect pathogens. Cell. Microbiol. 7(4), 481-488 (2005).
    • (2005) Cell. Microbiol. , vol.7 , Issue.4 , pp. 481-488
    • Cambi, A.1    Koopman, M.2    Figdor, C.G.3
  • 126
    • 4544382185 scopus 로고    scopus 로고
    • The role of scavenger receptors in pathogen recognition and innate immunity
    • Mukhopadhyay S, Gordon S. The role of scavenger receptors in pathogen recognition and innate immunity. Immunobiology 209(1-2), 39-49 (2004).
    • (2004) Immunobiology , vol.209 , Issue.1-2 , pp. 39-49
    • Mukhopadhyay, S.1    Gordon, S.2
  • 127
    • 29144452851 scopus 로고    scopus 로고
    • The C-type lectin-like domain superfamily
    • Zelensky AN, Gready JE. The C-type lectin-like domain superfamily. FEBS J. 272(24), 6179-6217 (2005).
    • (2005) FEBS J. , vol.272 , Issue.24 , pp. 6179-6217
    • Zelensky, A.N.1    Gready, J.E.2
  • 128
    • 0037218327 scopus 로고    scopus 로고
    • Normal host defense during systemic candidiasis in mannose receptor-deficient mice
    • Lee SJ, Zheng NY, Clavijo M, Nussenzweig MC. Normal host defense during systemic candidiasis in mannose receptor-deficient mice. Infect. Immun. 71(1), 437-445 (2003).
    • (2003) Infect. Immun. , vol.71 , Issue.1 , pp. 437-445
    • Lee, S.J.1    Zheng, N.Y.2    Clavijo, M.3    Nussenzweig, M.C.4
  • 129
    • 0034304945 scopus 로고    scopus 로고
    • DC-SIGN-ICAM-2 interaction mediates dendritic cell trafficking
    • Geijtenbeek TB, Krooshoop DJ, Bleijs DA et al. DC-SIGN-ICAM-2 interaction mediates dendritic cell trafficking. Nat. Immunol. 1(4), 353-357 (2000).
    • (2000) Nat. Immunol. , vol.1 , Issue.4 , pp. 353-357
    • Geijtenbeek, T.B.1    Krooshoop, D.J.2    Bleijs, D.A.3
  • 130
    • 0034598934 scopus 로고    scopus 로고
    • Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor that supports primary immune responses
    • Geijtenbeek TB, Torensma R, van Vliet SJ et al. Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor that supports primary immune responses. Cell 100(5), 575-585 (2000).
    • (2000) Cell , vol.100 , Issue.5 , pp. 575-585
    • Geijtenbeek, T.B.1    Torensma, R.2    van Vliet, S.J.3
  • 131
    • 0141688292 scopus 로고    scopus 로고
    • DC-SIGN: Escape mechanism for pathogens
    • van Kooyk Y, Geijtenbeek TB. DC-SIGN: escape mechanism for pathogens. Nat. Rev. Immunol. 3(9), 697-709 (2003).
    • (2003) Nat. Rev. Immunol. , vol.3 , Issue.9 , pp. 697-709
    • van Kooyk, Y.1    Geijtenbeek, T.B.2
  • 132
    • 0034598905 scopus 로고    scopus 로고
    • DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells
    • Geijtenbeek TB, Kwon DS, Torensma R et al. DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells. Cell 100(5), 587-597 (2000).
    • (2000) Cell , vol.100 , Issue.5 , pp. 587-597
    • Geijtenbeek, T.B.1    Kwon, D.S.2    Torensma, R.3
  • 133
    • 0038407687 scopus 로고    scopus 로고
    • DC-SIGN: A novel HIV receptor on DCs that mediates HIV-1 transmission
    • Geijtenbeek TB, van Kooyk Y. DC-SIGN: a novel HIV receptor on DCs that mediates HIV-1 transmission. Curr. Top. Microbiol. Immunol. 276, 31-54 (2003).
    • (2003) Curr. Top. Microbiol. Immunol. , vol.276 , pp. 31-54
    • Geijtenbeek, T.B.1    van Kooyk, Y.2
  • 134
    • 0034979622 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells are highly susceptible to human immunodeficiency virus type 1 infection and release infectious virus
    • Patterson S, Rae A, Hockey N, Gilmour J, Gotch F. Plasmacytoid dendritic cells are highly susceptible to human immunodeficiency virus type 1 infection and release infectious virus. J. Virol. 75(14), 6710-6713 (2001).
    • (2001) J. Virol. , vol.75 , Issue.14 , pp. 6710-6713
    • Patterson, S.1    Rae, A.2    Hockey, N.3    Gilmour, J.4    Gotch, F.5
  • 135
    • 0034799379 scopus 로고    scopus 로고
    • DC-SIGN interactions with human immunodeficiency virus: Virus binding and transfer are dissociable functions
    • Pohlmann S, Leslie GJ, Edwards TG et al. DC-SIGN interactions with human immunodeficiency virus: virus binding and transfer are dissociable functions. J. Virol. 75(21), 10523-10526 (2001).
    • (2001) J. Virol. , vol.75 , Issue.21 , pp. 10523-10526
    • Pohlmann, S.1    Leslie, G.J.2    Edwards, T.G.3
  • 136
    • 22144493290 scopus 로고    scopus 로고
    • Mycobacterium bovis Bacillus Calmette-Guerin infects DC-SIGN-dendritic cell and causes the inhibition of IL-12 and the enhancement of IL-10 production
    • Gagliardi MC, Teloni R, Giannoni F et al. Mycobacterium bovis Bacillus Calmette-Guerin infects DC-SIGN-dendritic cell and causes the inhibition of IL-12 and the enhancement of IL-10 production. J. Leukoc. Biol. 78(1), 106-113 (2005).
    • (2005) J. Leukoc. Biol. , vol.78 , Issue.1 , pp. 106-113
    • Gagliardi, M.C.1    Teloni, R.2    Giannoni, F.3
  • 137
    • 33244497571 scopus 로고    scopus 로고
    • Dectin-1: A signalling non-TLR pattern-recognition receptor
    • Brown GD. Dectin-1: a signalling non-TLR pattern-recognition receptor. Nat. Rev. Immunol. 6(1), 33-43 (2005).
    • (2005) Nat. Rev. Immunol. , vol.6 , Issue.1 , pp. 33-43
    • Brown, G.D.1
  • 138
    • 0035817818 scopus 로고    scopus 로고
    • Immune recognition. A new receptor for β-glucans
    • Brown GD, Gordon S. Immune recognition. A new receptor for β-glucans. Nature 413(6851), 36-37 (2001).
    • (2001) Nature , vol.413 , Issue.6851 , pp. 36-37
    • Brown, G.D.1    Gordon, S.2
  • 140
    • 0033458799 scopus 로고    scopus 로고
    • Toll-like receptor-2 mediates mycobacteria-induced proinflammatory signaling in macrophages
    • Underhill DM, Ozinsky A, Smith KD, Aderem A. Toll-like receptor-2 mediates mycobacteria-induced proinflammatory signaling in macrophages. Proc. Natl Acad. Sci. USA 96(25), 14459-14463 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , Issue.25 , pp. 14459-14463
    • Underhill, D.M.1    Ozinsky, A.2    Smith, K.D.3    Aderem, A.4
  • 141
    • 27144521657 scopus 로고    scopus 로고
    • Dectin-1 activates Syk tyrosine kinase in a dynamic subset of macrophages for reactive oxygen production
    • Underhill DM, Rossnagle E, Lowell CA, Simmons RM. Dectin-1 activates Syk tyrosine kinase in a dynamic subset of macrophages for reactive oxygen production. Blood 106(7), 2543-2550 (2005).
    • (2005) Blood , vol.106 , Issue.7 , pp. 2543-2550
    • Underhill, D.M.1    Rossnagle, E.2    Lowell, C.A.3    Simmons, R.M.4
  • 142
    • 3242782480 scopus 로고    scopus 로고
    • The scavenger receptor MARCO is required for lung defense against pneumococcal pneumonia and inhaled particles
    • Arredouani M, Yang Z, Ning Y et al. The scavenger receptor MARCO is required for lung defense against pneumococcal pneumonia and inhaled particles. J. Exp. Med. 200(2), 267-272 (2004).
    • (2004) J. Exp. Med. , vol.200 , Issue.2 , pp. 267-272
    • Arredouani, M.1    Yang, Z.2    Ning, Y.3
  • 143
    • 18644378971 scopus 로고    scopus 로고
    • The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis C virus
    • Scarselli E, Ansuini H, Cerino R et al. The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis C virus. EMBO J. 21(19), 5017-5025 (2002).
    • (2002) EMBO J. , vol.21 , Issue.19 , pp. 5017-5025
    • Scarselli, E.1    Ansuini, H.2    Cerino, R.3
  • 144
    • 23844531867 scopus 로고    scopus 로고
    • Drosophila RNAi screen reveals CD36 family member required for mycobacterial infection
    • Philips JA, Rubin EJ, Perrimon N. Drosophila RNAi screen reveals CD36 family member required for mycobacterial infection. Science 309(5738), 1251-1253 (2005).
    • (2005) Science , vol.309 , Issue.5738 , pp. 1251-1253
    • Philips, J.A.1    Rubin, E.J.2    Perrimon, N.3
  • 145
    • 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. 170(3), 477-485 (2005).
    • (2005) J. Cell. Biol. , vol.170 , Issue.3 , pp. 477-485
    • Stuart, L.M.1    Deng, J.2    Silver, J.M.3
  • 146
    • 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 433(7025), 523-527 (2005).
    • (2005) Nature , vol.433 , Issue.7025 , pp. 523-527
    • Hoebe, K.1    Georgel, P.2    Rutschmann, S.3
  • 148
    • 0029918601 scopus 로고    scopus 로고
    • Plasmodium falciparum erythrocyte membrane protein 1 is a parasitized erythrocyte receptor for adherence to CD36, thrombospondin, and intercellular adhesion molecule 1
    • Baruch DI, Gormely JA, Ma C, Howard RJ, Pasloske BL. Plasmodium falciparum erythrocyte membrane protein 1 is a parasitized erythrocyte receptor for adherence to CD36, thrombospondin, and intercellular adhesion molecule 1. Proc. Natl Acad. Sci. USA 93(8), 3497-3502 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , Issue.8 , pp. 3497-3502
    • Baruch, D.I.1    Gormely, J.A.2    Ma, C.3    Howard, R.J.4    Pasloske, B.L.5
  • 149
    • 0034729792 scopus 로고    scopus 로고
    • Malaria susceptibility and CD36 mutation
    • Aitman TJ, Cooper LD, Norsworthy PJ et al. Malaria susceptibility and CD36 mutation. Nature 405(6790), 1015-1016 (2000).
    • (2000) Nature , vol.405 , Issue.6790 , pp. 1015-1016
    • Aitman, T.J.1    Cooper, L.D.2    Norsworthy, P.J.3


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