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Volumn 6, Issue 9, 2006, Pages 644-658

IRFs: Master regulators of signalling by Toll-like receptors and cytosolic pattern-recognition receptors

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CYCLOPHILIN B; INTERFERON; INTERFERON REGULATORY FACTOR; INTERFERON REGULATORY FACTOR 1; INTERFERON REGULATORY FACTOR 3; INTERFERON REGULATORY FACTOR 7; MYELOID DIFFERENTIATION FACTOR 88; PATTERN RECOGNITION RECEPTOR; SMALL NUCLEAR RIBONUCLEOPROTEIN; TOLL LIKE RECEPTOR; TRANSCRIPTION FACTOR; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR;

EID: 33748051738     PISSN: 14741733     EISSN: None     Source Type: Journal    
DOI: 10.1038/nri1900     Document Type: Review
Times cited : (1370)

References (148)
  • 1
    • 0028337542 scopus 로고
    • Transcriptional activation: A complex puzzle with few easy pieces
    • Tjian, R. & Maniatis, T. Transcriptional activation: a complex puzzle with few easy pieces. Cell 77, 5-8 (1994).
    • (1994) Cell , vol.77 , pp. 5-8
    • Tjian, R.1    Maniatis, T.2
  • 2
    • 0024516201 scopus 로고
    • The involvement of NF-κB in β-interferon gene regulation reveals its role as widely inducible mediator of signal transduction
    • Lenardo, M. J., Fan, C. M., Maniatis, T. & Baltimore, D. The involvement of NF-κB in β-interferon gene regulation reveals its role as widely inducible mediator of signal transduction. Cell 57, 287-294 (1989).
    • (1989) Cell , vol.57 , pp. 287-294
    • Lenardo, M.J.1    Fan, C.M.2    Maniatis, T.3    Baltimore, D.4
  • 3
    • 0036781052 scopus 로고    scopus 로고
    • NF-κB regulation in the immune system
    • Li, Q. & Verma, I. M. NF-κB regulation in the immune system. Nature Rev. Immunol. 2, 725-734 (2002).
    • (2002) Nature Rev. Immunol. , vol.2 , pp. 725-734
    • Li, Q.1    Verma, I.M.2
  • 4
    • 0035061538 scopus 로고    scopus 로고
    • IRF family of transcription factors as regulators of host defense
    • Taniguchi, T., Ogasawara, K., Takaoka, A. & Tanaka, N. IRF family of transcription factors as regulators of host defense. Annu. Rev. Immunol. 19, 623-655 (2001).
    • (2001) Annu. Rev. Immunol. , vol.19 , pp. 623-655
    • Taniguchi, T.1    Ogasawara, K.2    Takaoka, A.3    Tanaka, N.4
  • 5
    • 13444283466 scopus 로고    scopus 로고
    • Roles of interferon-regulatory factors in T-helper-cell differentiation
    • Lohoff, M. & Mak, T. W. Roles of interferon-regulatory factors in T-helper-cell differentiation. Nature Rev. Immunol. 5, 125-135 (2005).
    • (2005) Nature Rev. Immunol. , vol.5 , pp. 125-135
    • Lohoff, M.1    Mak, T.W.2
  • 6
    • 0035344461 scopus 로고    scopus 로고
    • A weak signal for strong responses: Interferon-α/β revisited
    • Taniguchi, T. & Takaoka, A. A weak signal for strong responses: interferon-α/β revisited. Nature Rev. Mol. Cell Biol. 2, 378-386 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 378-386
    • Taniguchi, T.1    Takaoka, A.2
  • 7
    • 18844457095 scopus 로고    scopus 로고
    • Mechanisms of type-I- and type-II-interferon-mediated signalling
    • Platanias, L. C. Mechanisms of type-I- and type-II-interferon-mediated signalling. Nature Rev. Immunol. 5, 375-386 (2005).
    • (2005) Nature Rev. Immunol. , vol.5 , pp. 375-386
    • Platanias, L.C.1
  • 8
    • 25444495693 scopus 로고    scopus 로고
    • The Yin and Yang of type I interferon activity in bacterial infection
    • Decker, T., Muller, M. & Stockinger, S. The Yin and Yang of type I interferon activity in bacterial infection. Nature Rev. Immunol. 5, 675-687 (2005).
    • (2005) Nature Rev. Immunol. , vol.5 , pp. 675-687
    • Decker, T.1    Muller, M.2    Stockinger, S.3
  • 9
    • 0032968759 scopus 로고    scopus 로고
    • Conserved transactivation domain shared by interferon regulatory factors and Smad morphogens
    • Eroshkin, A. & Mushegian, A. Conserved transactivation domain shared by interferon regulatory factors and Smad morphogens. J. Mol. Med. 77, 403-405 (1999).
    • (1999) J. Mol. Med. , vol.77 , pp. 403-405
    • Eroshkin, A.1    Mushegian, A.2
  • 10
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira, S., Uematsu, S. & Takeuchi, O. Pathogen recognition and innate immunity. Cell 124, 783-801 (2006).
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 12
    • 3242813113 scopus 로고    scopus 로고
    • The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses
    • Yoneyama, M. et al. The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. Nature Immunol. 5, 730-737 (2004).
    • (2004) Nature Immunol. , vol.5 , pp. 730-737
    • Yoneyama, M.1
  • 13
    • 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. et al. Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity. J. Immunol. 175, 2851-2858 (2005). References 12 and 13 were the first reports of the cytosolic PRR molecules involved in type I IFN gene induction by viruses or dsRNA.
    • (2005) J. Immunol. , vol.175 , pp. 2851-2858
    • Yoneyama, M.1
  • 14
    • 0032841028 scopus 로고    scopus 로고
    • Interferon regulatory factors: The next generation
    • Mamane, Y. et al. Interferon regulatory factors: the next generation. Gene 237, 1-14 (1999).
    • (1999) Gene , vol.237 , pp. 1-14
    • Mamane, Y.1
  • 15
    • 0032015647 scopus 로고    scopus 로고
    • Virus infection induces the assembly of coordinately activated transcription factors on the IFN-β enhancer in vivo
    • Wathelet, M. G. et al. Virus infection induces the assembly of coordinately activated transcription factors on the IFN-β enhancer in vivo. Mol. Cell 1, 507-518 (1998).
    • (1998) Mol. Cell , vol.1 , pp. 507-518
    • Wathelet, M.G.1
  • 16
    • 0023788435 scopus 로고
    • Regulated expression of a gene encoding a nuclear factor, IRF-1, that specifically binds to IFN-β gene regulatory elements
    • Miyamoto, M. et al. Regulated expression of a gene encoding a nuclear factor, IRF-1, that specifically binds to IFN-β gene regulatory elements. Cell 54, 903-913 (1988). This paper reports the discovery of the first IRF-family member, IRF1.
    • (1988) Cell , vol.54 , pp. 903-913
    • Miyamoto, M.1
  • 17
    • 0027361463 scopus 로고
    • Targeted disruption of IRF-1 or IRF-2 results in abnormal type I IFN gene induction and aberrant lymphocyte development
    • Matsuyama, T. et al. Targeted disruption of IRF-1 or IRF-2 results in abnormal type I IFN gene induction and aberrant lymphocyte development. Cell 75, 83-97 (1993).
    • (1993) Cell , vol.75 , pp. 83-97
    • Matsuyama, T.1
  • 18
    • 15044345461 scopus 로고    scopus 로고
    • Integral role of IRF-5 in the gene induction programme activated by Toll-like receptors
    • Takaoka, A. et al. Integral role of IRF-5 in the gene induction programme activated by Toll-like receptors. Nature 434, 243-249 (2005). This paper was the first report to show that IRF5 is essential for TLR-mediated induction of pro-inflammatory cytokine genes.
    • (2005) Nature , vol.434 , pp. 243-249
    • Takaoka, A.1
  • 19
    • 0031932892 scopus 로고    scopus 로고
    • Interferon regulatory factor 3 and CREB-binding protein/p300 are subunits of double-stranded RNA-activated transcription factor DRAF1
    • Weaver, B. K., Kumar, K. P. & Reich, N. C. Interferon regulatory factor 3 and CREB-binding protein/p300 are subunits of double-stranded RNA-activated transcription factor DRAF1. Mol. Cell. Biol. 18, 1359-1368 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1359-1368
    • Weaver, B.K.1    Kumar, K.P.2    Reich, N.C.3
  • 20
    • 0031893220 scopus 로고    scopus 로고
    • Virus-dependent phosphorylation of the IRF-3 transcription factor regulates nuclear translocation, transactivation potential, and proteasome-mediated degradation
    • Lin, R., Heylbroeck, C., Pitha, P. M. & Hiscott, J. Virus-dependent phosphorylation of the IRF-3 transcription factor regulates nuclear translocation, transactivation potential, and proteasome-mediated degradation. Mol. Cell. Biol. 18, 2986-2996 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2986-2996
    • Lin, R.1    Heylbroeck, C.2    Pitha, P.M.3    Hiscott, J.4
  • 21
    • 0032481352 scopus 로고    scopus 로고
    • Direct triggering of the type I interferon system by virus infection: Activation of a transcription factor complex containing IRF-3 and CBP/p300
    • Yoneyama, M. et al. Direct triggering of the type I interferon system by virus infection: activation of a transcription factor complex containing IRF-3 and CBP/p300. EMBO J. 17, 1087-1095 (1998).
    • (1998) EMBO J. , vol.17 , pp. 1087-1095
    • Yoneyama, M.1
  • 22
    • 0032549658 scopus 로고    scopus 로고
    • Involvement of the IRF family transcription factor IRF-3 in virus-induced activation of the IFN-β gene
    • Sato, M., Tanaka, N., Hata, N., Oda, E. & Taniguchi, T. Involvement of the IRF family transcription factor IRF-3 in virus-induced activation of the IFN-β gene. FEBS Lett. 425, 112-116 (1998). References 19-22 provide evidence for the phosphorylation-dependent activation of IRF3 during type I IFN gene induction.
    • (1998) FEBS Lett. , vol.425 , pp. 112-116
    • Sato, M.1    Tanaka, N.2    Hata, N.3    Oda, E.4    Taniguchi, T.5
  • 23
    • 0033858399 scopus 로고    scopus 로고
    • Analyses of virus-induced homomeric and heteromeric protein associations between IRF-3 and coactivator CBP/p300
    • Suhara, W. et al. Analyses of virus-induced homomeric and heteromeric protein associations between IRF-3 and coactivator CBP/p300. J. Biochem. (Tokyo) 128, 301-307 (2000).
    • (2000) J. Biochem. (Tokyo) , vol.128 , pp. 301-307
    • Suhara, W.1
  • 24
    • 0032434924 scopus 로고    scopus 로고
    • Positive feedback regulation of type I IFN genes by the IFN-inducible transcription factor IRF-7
    • Sato, M. et al. Positive feedback regulation of type I IFN genes by the IFN-inducible transcription factor IRF-7. FEBS Lett. 441, 106-110 (1998).
    • (1998) FEBS Lett. , vol.441 , pp. 106-110
    • Sato, M.1
  • 25
    • 0032538891 scopus 로고    scopus 로고
    • Differential viral induction of distinct interferon-α genes by positive feedback through interferon regulatory factor-7
    • Marie, I., Durbin, J. E. & Levy, D. E. Differential viral induction of distinct interferon-α genes by positive feedback through interferon regulatory factor-7. EMBO J. 17, 6660-6669 (1998). References 24 and 25 describe the positive-feedback regulation of type I IFN gene induction, which involves the expression and activation of IRF7.
    • (1998) EMBO J. , vol.17 , pp. 6660-6669
    • Marie, I.1    Durbin, J.E.2    Levy, D.E.3
  • 26
    • 0034602156 scopus 로고    scopus 로고
    • Multiple regulatory domains control IRF-7 activity in response to virus infection
    • Lin, R., Mamane, Y. & Hiscott, J. Multiple regulatory domains control IRF-7 activity in response to virus infection. J. Biol. Chem. 275, 34320-34327 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 34320-34327
    • Lin, R.1    Mamane, Y.2    Hiscott, J.3
  • 27
    • 0033680737 scopus 로고    scopus 로고
    • Distinct and essential roles of transcription factors IRF-3 and IRF-7 in response to viruses for IFN-α/β gene induction
    • Sato, M. et al. Distinct and essential roles of transcription factors IRF-3 and IRF-7 in response to viruses for IFN-α/β gene induction. Immunity 13, 539-548 (2000).
    • (2000) Immunity , vol.13 , pp. 539-548
    • Sato, M.1
  • 28
    • 17144404177 scopus 로고    scopus 로고
    • IRF-7 is the master regulator of type-I interferon-dependent immune responses
    • Honda, K. et al. IRF-7 is the master regulator of type-I interferon-dependent immune responses. Nature 434, 772-777 (2005). References 27 and 28 are gene-targeting studies of IRF3 and IRF7, respectively. Reference 28 provides definitive evidence that IRF7 is the main regulator of both cytosolic PRR- and TLR-mediated type I IFN gene induction.
    • (2005) Nature , vol.434 , pp. 772-777
    • Honda, K.1
  • 29
    • 0034801322 scopus 로고    scopus 로고
    • Gene induction pathways mediated by distinct IRFs during viral infection
    • Nakaya, T. et al. Gene induction pathways mediated by distinct IRFs during viral infection. Biochem. Biophys. Res. Commun. 283, 1150-1156 (2001).
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 1150-1156
    • Nakaya, T.1
  • 30
    • 0038363463 scopus 로고    scopus 로고
    • Triggering the interferon antiviral response through an IKK-related pathway
    • Sharma, S. et al. Triggering the interferon antiviral response through an IKK-related pathway. Science 300, 1148-1151 (2003).
    • (2003) Science , vol.300 , pp. 1148-1151
    • Sharma, S.1
  • 31
    • 0038393016 scopus 로고    scopus 로고
    • IKKε and TBK1 are essential components of the IRF3 signaling pathway
    • Fitzgerald, K. A. et al. IKKε and TBK1 are essential components of the IRF3 signaling pathway. Nature Immunol. 4, 491-496 (2003). References 30 and 31 were the first reports to identify that TBK1 and IKKε are the protein kinases that activate IRF3 and IRF7.
    • (2003) Nature Immunol. , vol.4 , pp. 491-496
    • Fitzgerald, K.A.1
  • 32
    • 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. et al. The roles of two IκB kinase-related kinases in lipopolysaccharide and double stranded RNA signaling and viral infection. J. Exp. Med. 199, 1641-1650 (2004).
    • (2004) J. Exp. Med. , vol.199 , pp. 1641-1650
    • Hemmi, H.1
  • 33
    • 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, A. K., Chow, E. K., Goodnough, J. B., Yeh, W. C. & 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, 1651-1658 (2004).
    • (2004) J. Exp. Med. , vol.199 , pp. 1651-1658
    • Perry, A.K.1    Chow, E.K.2    Goodnough, J.B.3    Yeh, W.C.4    Cheng, G.5
  • 34
    • 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-α induction
    • Uematsu, S. et al. Interleukin-1 receptor-associated kinase-1 plays an essential role for Toll-like receptor (TLR)7- and TLR9-mediated interferon-α induction. J. Exp. Med. 201, 915-923 (2005).
    • (2005) J. Exp. Med. , vol.201 , pp. 915-923
    • Uematsu, S.1
  • 35
    • 33645841633 scopus 로고    scopus 로고
    • IκB kinase-α is critical for interferon-α production induced by Toll-like receptors 7 and 9
    • Hoshino, K. et al. IκB kinase-α is critical for interferon-α production induced by Toll-like receptors 7 and 9. Nature 440, 949-953 (2006). References 34 and 35 show that IRAK1 and IKKα are involved in the activation of IRF7.
    • (2006) Nature , vol.440 , pp. 949-953
    • Hoshino, K.1
  • 36
    • 22244476202 scopus 로고    scopus 로고
    • Role of cyclophilin B in activation of interferon regulatory factor-3
    • Obata, Y. et al. Role of cyclophilin B in activation of interferon regulatory factor-3. J. Biol. Chem. 280, 18355-18360 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 18355-18360
    • Obata, Y.1
  • 37
    • 33744499683 scopus 로고    scopus 로고
    • Negative regulation of interferon-regulatory factor 3-dependent innate antiviral response by the prolyl isomerase Pin1
    • Saitoh, T. et al. Negative regulation of interferon-regulatory factor 3-dependent innate antiviral response by the prolyl isomerase Pin1. Nature Immunol. 7, 598-605 (2006).
    • (2006) Nature Immunol. , vol.7 , pp. 598-605
    • Saitoh, T.1
  • 38
    • 28644433321 scopus 로고    scopus 로고
    • SIKE is an IKKε/TBK1-associated suppressor of TLR3- and virus-triggered IRF-3 activation pathways
    • Huang, J. et al. SIKE is an IKKε/TBK1-associated suppressor of TLR3- and virus-triggered IRF-3 activation pathways. EMBO J. 24, 4018-4028 (2005).
    • (2005) EMBO J. , vol.24 , pp. 4018-4028
    • Huang, J.1
  • 39
    • 0141703238 scopus 로고    scopus 로고
    • Selective contribution of IFN-α/β signaling to the maturation of dendritic cells induced by double-stranded RNA or viral infection
    • Honda, K. et al. Selective contribution of IFN-α/β signaling to the maturation of dendritic cells induced by double-stranded RNA or viral infection. Proc. Natl Acad. Sci. USA 100, 10872-10877 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10872-10877
    • Honda, K.1
  • 40
    • 22544455673 scopus 로고    scopus 로고
    • Cell type-specific involvement of RIG-I in antiviral response
    • Kato, H. et al. Cell type-specific involvement of RIG-I in antiviral response. Immunity 23, 19-28 (2005).
    • (2005) Immunity , vol.23 , pp. 19-28
    • Kato, H.1
  • 41
    • 33646342149 scopus 로고    scopus 로고
    • Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses
    • Kato, H. et al. Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses. Nature 441, 101-105 (2006).
    • (2006) Nature , vol.441 , pp. 101-105
    • Kato, H.1
  • 42
    • 27144440523 scopus 로고    scopus 로고
    • IPS-1, an adaptor triggering RIG-Iand Mda5-mediated type I interferon induction
    • Kawai, T. et al. IPS-1, an adaptor triggering RIG-Iand Mda5-mediated type I interferon induction. Nature Immunol. 6, 981-988 (2005).
    • (2005) Nature Immunol. , vol.6 , pp. 981-988
    • Kawai, T.1
  • 43
    • 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. et al. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature 437, 1167-1172 (2005).
    • (2005) Nature , vol.437 , pp. 1167-1172
    • Meylan, E.1
  • 44
    • 24944538819 scopus 로고    scopus 로고
    • VISA is an adapter protein required for virus-triggered IFN-β signaling
    • Xu, L. G. et al. VISA is an adapter protein required for virus-triggered IFN-β signaling. Mol. Cell 19, 727-740 (2005).
    • (2005) Mol. Cell , vol.19 , pp. 727-740
    • Xu, L.G.1
  • 45
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-κB and IRF 3
    • Seth, R. B., Sun, L., Ea, C. K. & Chen, Z. J. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-κB and IRF 3. Cell 122, 669-682 (2005). References 42-45 report the discovery of the cytosolic adaptor molecule CARDIF/IPS1/MAVS/VISA.
    • (2005) Cell , vol.122 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.K.3    Chen, Z.J.4
  • 46
    • 33646592188 scopus 로고    scopus 로고
    • The specific and essential role of MAVS in antiviral innate immune responses
    • Sun, Q. et al. The specific and essential role of MAVS in antiviral innate immune responses. Immunity 24, 633-642 (2006).
    • (2006) Immunity , vol.24 , pp. 633-642
    • Sun, Q.1
  • 47
    • 33745814424 scopus 로고    scopus 로고
    • Essential role of IPS-1 in innate immune responses against RNA viruses
    • Kumar, H. et al. Essential role of IPS-1 in innate immune responses against RNA viruses. J. Exp. Med. 203, 1795-1803 (2006). References 46 and 47 describe gene-targeting studies of CARDIF/IPS1/MAVS/VISA and show that this adaptor has an essential role in the cytosolic pathway of type I IFN gene induction.
    • (2006) J. Exp. Med. , vol.203 , pp. 1795-1803
    • Kumar, H.1
  • 48
    • 30544447047 scopus 로고    scopus 로고
    • Critical role of TRAF3 in the Toll-like receptor-dependent and -independent antiviral response
    • Oganesyan, G. et al. Critical role of TRAF3 in the Toll-like receptor-dependent and -independent antiviral response. Nature 439, 208-211 (2006).
    • (2006) Nature , vol.439 , pp. 208-211
    • Oganesyan, G.1
  • 49
    • 10344252795 scopus 로고    scopus 로고
    • IFN regulatory factor 3-dependent induction of type I IFNs by intracellular bacteria is mediated by a TLR- and Nod2-independent mechanism
    • Stockinger, S. et al. IFN regulatory factor 3-dependent induction of type I IFNs by intracellular bacteria is mediated by a TLR- and Nod2-independent mechanism. J. Immunol. 173, 7416-7425 (2004).
    • (2004) J. Immunol. , vol.173 , pp. 7416-7425
    • Stockinger, S.1
  • 50
    • 4344627833 scopus 로고    scopus 로고
    • Type I interferon production enhances susceptibility to Listeria monocytogenes infection
    • O'Connell, R. M. et al. Type I interferon production enhances susceptibility to Listeria monocytogenes infection. J. Exp. Med. 200, 437-445 (2004).
    • (2004) J. Exp. Med. , vol.200 , pp. 437-445
    • O'Connell, R.M.1
  • 51
    • 30444450839 scopus 로고    scopus 로고
    • Recognition of cytosolic DNA activates an IRF3-dependent innate immune response
    • Stetson, D. B. & Medzhitov, R. Recognition of cytosolic DNA activates an IRF3-dependent innate immune response. Immunity 24, 93-103 (2006).
    • (2006) Immunity , vol.24 , pp. 93-103
    • Stetson, D.B.1    Medzhitov, R.2
  • 52
    • 29244471275 scopus 로고    scopus 로고
    • A Toll-like receptor-independent antiviral response induced by double-stranded B-form DNA
    • Ishii, K. J. et al. A Toll-like receptor-independent antiviral response induced by double-stranded B-form DNA. Nature Immunol. 7, 40-48 (2006).
    • (2006) Nature Immunol. , vol.7 , pp. 40-48
    • Ishii, K.J.1
  • 53
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • Medzhitov, R., Preston-Hurlburt, P. & Janeway, C. A. Jr. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 388, 394-397 (1997).
    • (1997) Nature , vol.388 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway Jr., C.A.3
  • 54
    • 5944261457 scopus 로고    scopus 로고
    • Pattern recognition receptors TLR4 and CD14 mediate response to respiratory syncytial virus
    • Kurt-Jones, E. A. et al. Pattern recognition receptors TLR4 and CD14 mediate response to respiratory syncytial virus. Nature Immunol. 1, 398-401 (2000).
    • (2000) Nature Immunol. , vol.1 , pp. 398-401
    • Kurt-Jones, E.A.1
  • 55
    • 0036796384 scopus 로고    scopus 로고
    • Differential involvement of IFN-β in Toll-like receptor-stimulated dendritic cell activation
    • Hoshino, K., Kaisho, T., Iwabe, T., Takeuchi, O. & Akira, S. Differential involvement of IFN-β in Toll-like receptor-stimulated dendritic cell activation. Int. Immunol. 14, 1225-1231 (2002).
    • (2002) Int. Immunol. , vol.14 , pp. 1225-1231
    • Hoshino, K.1    Kaisho, T.2    Iwabe, T.3    Takeuchi, O.4    Akira, S.5
  • 56
    • 0035889228 scopus 로고    scopus 로고
    • Lipopolysaccharide stimulates the MyD88-independent pathway and results in activation of IFN-regulatory factor 3 and the expression of a subset of lipopolysaccharide-inducible genes
    • Kawai, T. et al. Lipopolysaccharide stimulates the MyD88-independent pathway and results in activation of IFN-regulatory factor 3 and the expression of a subset of lipopolysaccharide-inducible genes. J. Immunol. 167, 5887-5894 (2001). This paper provides evidence that there is a MyD88-independent pathway for activation of IRF3.
    • (2001) J. Immunol. , vol.167 , pp. 5887-5894
    • Kawai, T.1
  • 57
    • 0038434274 scopus 로고    scopus 로고
    • Essential role of IRF-3 in lipopolysaccharide-induced interferon-β gene expression and endotoxin shock
    • Sakaguchi, S. et al. Essential role of IRF-3 in lipopolysaccharide- induced interferon-β gene expression and endotoxin shock. Biochem. Biophys. Res. Commun. 306, 860-866 (2003).
    • (2003) Biochem. Biophys. Res. Commun. , vol.306 , pp. 860-866
    • Sakaguchi, S.1
  • 58
    • 0347146027 scopus 로고    scopus 로고
    • Upregulation of costimulatory molecules induced by lipopolysaccharide and double-stranded RNA occurs by Trif-dependent and Trif-independent pathways
    • Hoebe, K. et al. Upregulation of costimulatory molecules induced by lipopolysaccharide and double-stranded RNA occurs by Trif-dependent and Trif-independent pathways. Nature Immunol. 4, 1223-1229 (2003).
    • (2003) Nature Immunol. , vol.4 , pp. 1223-1229
    • Hoebe, K.1
  • 59
    • 24944489952 scopus 로고    scopus 로고
    • Stimulus specificity of gene expression programs determined by temporal control of IKK activity
    • Werner, S. L., Barken, D. & Hoffmann, A. Stimulus specificity of gene expression programs determined by temporal control of IKK activity. Science 309, 1857-1861 (2005).
    • (2005) Science , vol.309 , pp. 1857-1861
    • Werner, S.L.1    Barken, D.2    Hoffmann, A.3
  • 60
    • 24144465889 scopus 로고    scopus 로고
    • Molecular determinants of crosstalk between nuclear receptors and Toll-like receptors
    • Ogawa, S. et al. Molecular determinants of crosstalk between nuclear receptors and Toll-like receptors. Cell 122, 707-721 (2005). Reference 60, together with references 101 and 102, provides evidence for the association of IRF3 with the NF-κB component p65.
    • (2005) Cell , vol.122 , pp. 707-721
    • Ogawa, S.1
  • 61
    • 0028348307 scopus 로고
    • Requirement for transcription factor IRF-1 in NO synthase induction in macrophages
    • Kamijo, R. et al. Requirement for transcription factor IRF-1 in NO synthase induction in macrophages. Science 263, 1612-1615 (1994).
    • (1994) Science , vol.263 , pp. 1612-1615
    • Kamijo, R.1
  • 62
    • 0035909372 scopus 로고    scopus 로고
    • Recognition of double-stranded RNA and activation of NF-κB by Toll-like receptor 3
    • Alexopoulou, L., Holt, A. C., Medzhitov, R. & Flavell, R. A. Recognition of double-stranded RNA and activation of NF-κB by Toll-like receptor 3. Nature 413, 732-738 (2001).
    • (2001) Nature , vol.413 , pp. 732-738
    • Alexopoulou, L.1    Holt, A.C.2    Medzhitov, R.3    Flavell, R.A.4
  • 63
    • 11144273976 scopus 로고    scopus 로고
    • Toll-like receptor 3 mediates West Nile virus entry into the brain causing lethal encephalitis
    • Wang, T. et al. Toll-like receptor 3 mediates West Nile virus entry into the brain causing lethal encephalitis. Nature Med. 10, 1366-1373 (2004). References 62 and 63 are the initial reports on the role of TLR3 in the recognition of virus-derived and synthetic dsRNA.
    • (2004) Nature Med. , vol.10 , pp. 1366-1373
    • Wang, T.1
  • 64
    • 31144451555 scopus 로고    scopus 로고
    • Deletion of TLR3 alters the pulmonary immune environment and mucus production during respiratory syncytial virus infection
    • Rudd, B. D. et al. Deletion of TLR3 alters the pulmonary immune environment and mucus production during respiratory syncytial virus infection. J. Immunol. 176, 1937-1942 (2006).
    • (2006) J. Immunol. , vol.176 , pp. 1937-1942
    • Rudd, B.D.1
  • 65
    • 12144286763 scopus 로고    scopus 로고
    • Toll-like receptors 9 and 3 as essential components of innate immune defense against mouse cytomegalovirus infection
    • Tabeta, K. et al. Toll-like receptors 9 and 3 as essential components of innate immune defense against mouse cytomegalovirus infection. Proc. Natl Acad. Sci. USA 101, 3516-3521 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3516-3521
    • Tabeta, K.1
  • 66
    • 32944481320 scopus 로고    scopus 로고
    • RNA interference reveals a role for TLR2 and TLR3 in the recognition of Leishmania donovani promastigotes by interferon-γ-primed macrophages
    • Flandin, J. F., Chano, F. & Descoteaux, A. RNA interference reveals a role for TLR2 and TLR3 in the recognition of Leishmania donovani promastigotes by interferon-γ-primed macrophages. Eur. J. Immunol. 36, 411-420 (2006).
    • (2006) Eur. J. Immunol. , vol.36 , pp. 411-420
    • Flandin, J.F.1    Chano, F.2    Descoteaux, A.3
  • 67
    • 19944432184 scopus 로고    scopus 로고
    • Double-stranded RNAs from the helminth parasite Schistosoma activate TLR3 in dendritic cells
    • Aksoy, E. et al. Double-stranded RNAs from the helminth parasite Schistosoma activate TLR3 in dendritic cells. J. Biol. Chem. 280, 277-283 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 277-283
    • Aksoy, E.1
  • 68
    • 0043176281 scopus 로고    scopus 로고
    • Role of adaptor TRIF in the MyD88-independent Toll-like receptor signaling pathway
    • Yamamoto, M. et al. Role of adaptor TRIF in the MyD88-independent Toll-like receptor signaling pathway. Science 301, 640-643 (2003).
    • (2003) Science , vol.301 , pp. 640-643
    • Yamamoto, M.1
  • 69
    • 7544225495 scopus 로고    scopus 로고
    • Novel roles of TLR3 tyrosine phosphorylation and PI3 kinase in double-stranded RNA signaling
    • Sarkar, S. N. et al. Novel roles of TLR3 tyrosine phosphorylation and PI3 kinase in double-stranded RNA signaling. Nature Struct. Mol. Biol. 11, 1060-1067 (2004).
    • (2004) Nature Struct. Mol. Biol. , vol.11 , pp. 1060-1067
    • Sarkar, S.N.1
  • 70
    • 0141923690 scopus 로고    scopus 로고
    • Toll/IL-1 receptor domain-containing adaptor inducing IFN-β (TRIF) associates with TNF receptor-associated factor 6 and TANK-binding kinase 1, and activates two distinct transcription factors, NF-κB and IFN-regulatory factor-3, in the Toll-like receptor signaling
    • Sato, S. et al. Toll/IL-1 receptor domain-containing adaptor inducing IFN-β (TRIF) associates with TNF receptor-associated factor 6 and TANK-binding kinase 1, and activates two distinct transcription factors, NF-κB and IFN-regulatory factor-3, in the Toll-like receptor signaling. J. Immunol. 171, 4304-4310 (2003).
    • (2003) J. Immunol. , vol.171 , pp. 4304-4310
    • Sato, S.1
  • 71
    • 4344613405 scopus 로고    scopus 로고
    • TNFR-associated factor (TRAF) 6 is essential for MyD88-dependent pathway but not Toll/IL-1 receptor domain-containing adaptor-inducing IFN-β (TRIF)-dependent pathway in TLR signaling
    • Gohda, J., Matsumura, T. & Inoue, J. TNFR-associated factor (TRAF) 6 is essential for MyD88-dependent pathway but not Toll/IL-1 receptor domain-containing adaptor-inducing IFN-β (TRIF)-dependent pathway in TLR signaling. J. Immunol. 173, 2913-2917 (2004).
    • (2004) J. Immunol. , vol.173 , pp. 2913-2917
    • Gohda, J.1    Matsumura, T.2    Inoue, J.3
  • 72
    • 30544451546 scopus 로고    scopus 로고
    • Specificity in Toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6
    • Hacker, H. et al. Specificity in Toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6. Nature 439, 204-207 (2006).
    • (2006) Nature , vol.439 , pp. 204-207
    • Hacker, H.1
  • 73
    • 23844461233 scopus 로고    scopus 로고
    • TRAF4 acts as a silencer in TLR-mediated signaling through the association with TRAF6 and TRIF
    • Takeshita, F. et al. TRAF4 acts as a silencer in TLR-mediated signaling through the association with TRAF6 and TRIF. Eur. J. Immunol. 35, 2477-2485 (2005).
    • (2005) Eur. J. Immunol. , vol.35 , pp. 2477-2485
    • Takeshita, F.1
  • 74
    • 30944431519 scopus 로고    scopus 로고
    • TNF receptor-associated factor-1 (TRAF1) negatively regulates Toll/IL-1 receptor domain-containing adaptor inducing IFN-β (TRIF)-mediated signaling
    • Su, X. et al. TNF receptor-associated factor-1 (TRAF1) negatively regulates Toll/IL-1 receptor domain-containing adaptor inducing IFN-β (TRIF)-mediated signaling. Eur. J. Immunol. 36, 199-206 (2006).
    • (2006) Eur. J. Immunol. , vol.36 , pp. 199-206
    • Su, X.1
  • 75
    • 10844219793 scopus 로고    scopus 로고
    • NF-κB-activating kinase-associated protein 1 participates in TLR3/Toll-IL-1 homology domain-containing adapter molecule-1-mediated IFN regulatory factor 3 activation
    • Sasai, M. et al. NF-κB-activating kinase-associated protein 1 participates in TLR3/Toll-IL-1 homology domain-containing adapter molecule-1-mediated IFN regulatory factor 3 activation. J. Immunol. 174, 27-30 (2005).
    • (2005) J. Immunol. , vol.174 , pp. 27-30
    • Sasai, M.1
  • 76
    • 0035887505 scopus 로고    scopus 로고
    • + cells in mouse lymph nodes and spleen display characteristics of plasmacytoid dendritic cells
    • + cells in mouse lymph nodes and spleen display characteristics of plasmacytoid dendritic cells. J. Exp. Med. 194, 1171-1178 (2001).
    • (2001) J. Exp. Med. , vol.194 , pp. 1171-1178
    • Nakano, H.1    Yanagita, M.2    Gunn, M.D.3
  • 77
    • 0035202483 scopus 로고    scopus 로고
    • Mouse type I IFN-producing cells are immature APCs with plasmacytoid morphology
    • Asselin-Paturel, C. et al. Mouse type I IFN-producing cells are immature APCs with plasmacytoid morphology. Nature Immunol. 2, 1144-1150 (2001).
    • (2001) Nature Immunol. , vol.2 , pp. 1144-1150
    • Asselin-Paturel, C.1
  • 78
    • 15244349785 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells in immunity
    • Colonna, M., Trinchieri, G. & Liu, Y. J. Plasmacytoid dendritic cells in immunity. Nature Immunol. 5, 1219-1226 (2004).
    • (2004) Nature Immunol. , vol.5 , pp. 1219-1226
    • Colonna, M.1    Trinchieri, G.2    Liu, Y.J.3
  • 79
    • 2942679083 scopus 로고    scopus 로고
    • The immunobiology of the TLR9 subfamily
    • Wagner, H. The immunobiology of the TLR9 subfamily. Trends Immunol. 25, 381-386 (2004).
    • (2004) Trends Immunol. , vol.25 , pp. 381-386
    • Wagner, H.1
  • 80
    • 1542317550 scopus 로고    scopus 로고
    • Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA
    • Diebold, S. S., Kaisho, T., Hemmi, H., Akira, S. & Reis e Sousa, C. Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA. Science 303, 1529-1531 (2004).
    • (2004) Science , vol.303 , pp. 1529-1531
    • Diebold, S.S.1    Kaisho, T.2    Hemmi, H.3    Akira, S.4    Reis E Sousa, C.5
  • 81
    • 0037443644 scopus 로고    scopus 로고
    • The roles of Toll-like receptor 9, MyD88, and DNA-dependent protein kinase catalytic subunit in the effects of two distinct CpG DNAs on dendritic cell subsets
    • Hemmi, H., Kaisho, T., Takeda, K. & Akira, S. The roles of Toll-like receptor 9, MyD88, and DNA-dependent protein kinase catalytic subunit in the effects of two distinct CpG DNAs on dendritic cell subsets. J. Immunol. 170, 3059-3064 (2003).
    • (2003) J. Immunol. , vol.170 , pp. 3059-3064
    • Hemmi, H.1    Kaisho, T.2    Takeda, K.3    Akira, S.4
  • 82
    • 0842328805 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 activates murine natural interferon-producing cells through Toll-like receptor 9
    • Krug, A. et al. Herpes simplex virus type 1 activates murine natural interferon-producing cells through Toll-like receptor 9. Blood 103, 1433-1437 (2004).
    • (2004) Blood , vol.103 , pp. 1433-1437
    • Krug, A.1
  • 83
    • 0042123694 scopus 로고    scopus 로고
    • Toll-like receptor 9-mediated recognition of herpes simplex virus-2 by plasmacytoid dendritic cells
    • Lund, J., Sato, A., Akira, S., Medzhitov, R. & Iwasaki, A. Toll-like receptor 9-mediated recognition of herpes simplex virus-2 by plasmacytoid dendritic cells. J. Exp. Med. 198, 513-520 (2003).
    • (2003) J. Exp. Med. , vol.198 , pp. 513-520
    • Lund, J.1    Sato, A.2    Akira, S.3    Medzhitov, R.4    Iwasaki, A.5
  • 84
    • 3142683548 scopus 로고    scopus 로고
    • TLR9-dependent recognition of MCMV by IPC and DC generates coordinated cytokine responses that activate antiviral NK cell function
    • Krug, A. et al. TLR9-dependent recognition of MCMV by IPC and DC generates coordinated cytokine responses that activate antiviral NK cell function. Immunity 21, 107-119 (2004).
    • (2004) Immunity , vol.21 , pp. 107-119
    • Krug, A.1
  • 85
    • 1542317578 scopus 로고    scopus 로고
    • Species-specific recognition of single-stranded RNA via Toll-like receptor 7 and 8
    • Heil, F. et al. Species-specific recognition of single-stranded RNA via Toll-like receptor 7 and 8. Science 303, 1526-1529 (2004).
    • (2004) Science , vol.303 , pp. 1526-1529
    • Heil, F.1
  • 86
    • 1842631428 scopus 로고    scopus 로고
    • Recognition of single-stranded RNA viruses by Toll-like receptor 7
    • Lund, J. M. et al. Recognition of single-stranded RNA viruses by Toll-like receptor 7. Proc. Natl Acad. Sci. USA 101, 5598-5603 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5598-5603
    • Lund, J.M.1
  • 87
    • 7444250116 scopus 로고    scopus 로고
    • Role of a transductional-transcriptional processor complex involving MyD88 and IRF-7 in Toll-like receptor signaling
    • Honda, K. 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, 15416-15421 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15416-15421
    • Honda, K.1
  • 88
    • 5444274514 scopus 로고    scopus 로고
    • Interferon-α induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6
    • Kawai, T. et al. Interferon-α induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6. Nature Immunol. 5, 1061-1068 (2004). References 87 and 88 report the evidence for a direct interaction between MyD88 and IRF7.
    • (2004) Nature Immunol. , vol.5 , pp. 1061-1068
    • Kawai, T.1
  • 89
    • 17844380477 scopus 로고    scopus 로고
    • Spatiotemporal regulation of MyD88-IRF-7 signalling for robust type-I interferon induction
    • Honda, K. et al. Spatiotemporal regulation of MyD88-IRF-7 signalling for robust type-I interferon induction. Nature 434, 1035-1040 (2005). This paper shows the importance of endosomal MyD88-IRF7 signalling for robust induction of type I IFN genes in pDCs.
    • (2005) Nature , vol.434 , pp. 1035-1040
    • Honda, K.1
  • 90
    • 0035865054 scopus 로고    scopus 로고
    • Human peripheral blood cells differentially recognize and respond to two distinct CpG motifs
    • Verthelyi, D., Ishii, K. J., Gursel, M., Takeshita, F. & Klinman, D. M. Human peripheral blood cells differentially recognize and respond to two distinct CpG motifs. J. Immunol. 166, 2372-2377 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 2372-2377
    • Verthelyi, D.1    Ishii, K.J.2    Gursel, M.3    Takeshita, F.4    Klinman, D.M.5
  • 91
    • 1842631153 scopus 로고    scopus 로고
    • Immunotherapeutic uses of CpG oligodeoxynucleotides
    • Klinman, D. M. Immunotherapeutic uses of CpG oligodeoxynucleotides. Nature Rev. Immunol. 4, 249-258 (2004).
    • (2004) Nature Rev. Immunol. , vol.4 , pp. 249-258
    • Klinman, D.M.1
  • 92
    • 33645963170 scopus 로고    scopus 로고
    • Osteopontin expression is essential for interferon-α production by plasmacytoid dendritic cells
    • Shinohara, M. L. et al. Osteopontin expression is essential for interferon-α production by plasmacytoid dendritic cells. Nature Immunol. 7, 498-506 (2006).
    • (2006) Nature Immunol. , vol.7 , pp. 498-506
    • Shinohara, M.L.1
  • 93
    • 33646460480 scopus 로고    scopus 로고
    • IRF family transcription factors in type I interferon induction
    • Yanai, H. et al. IRF family transcription factors in type I interferon induction. Int. Congr. Ser. 1285, 104-113 (2005).
    • (2005) Int. Congr. Ser. , vol.1285 , pp. 104-113
    • Yanai, H.1
  • 94
    • 0029143629 scopus 로고
    • Photolabeling identifies a putative fusion domain in the envelope glycoprotein of rabies and vesicular stomatitis viruses
    • Durrer, P., Gaudin, Y., Ruigrok, R. W., Graf, R. & Brunner, J. Photolabeling identifies a putative fusion domain in the envelope glycoprotein of rabies and vesicular stomatitis viruses. J. Biol. Chem. 270, 17575-17581 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 17575-17581
    • Durrer, P.1    Gaudin, Y.2    Ruigrok, R.W.3    Graf, R.4    Brunner, J.5
  • 95
    • 0031900543 scopus 로고    scopus 로고
    • Herpes simplex virus gD and virions accumulate in endosomes by mannose 6-phosphate-dependent and -independent mechanisms
    • Brunetti, C. R., Dingwell, K. S., Wale, C., Graham, F. L. & Johnson, D. C. Herpes simplex virus gD and virions accumulate in endosomes by mannose 6-phosphate-dependent and -independent mechanisms. J. Virol. 72, 3330-3339 (1998).
    • (1998) J. Virol. , vol.72 , pp. 3330-3339
    • Brunetti, C.R.1    Dingwell, K.S.2    Wale, C.3    Graham, F.L.4    Johnson, D.C.5
  • 96
    • 27644548945 scopus 로고    scopus 로고
    • Negative regulation of Toll-like-receptor signaling by IRF-4
    • Negishi, H. et al. Negative regulation of Toll-like-receptor signaling by IRF-4. Proc. Natl Acad. Sci. USA 102, 15989-15994 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15989-15994
    • Negishi, H.1
  • 97
    • 20444380445 scopus 로고    scopus 로고
    • The interferon regulatory factor, IRF5, is a central mediator of Toll-like receptor 7 signaling
    • Schoenemeyer, A. et al. The interferon regulatory factor, IRF5, is a central mediator of Toll-like receptor 7 signaling. J. Biol. Chem. 280, 17005-17012 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 17005-17012
    • Schoenemeyer, A.1
  • 98
    • 33744539146 scopus 로고    scopus 로고
    • IRF-8/interferon (IFN) consensus sequence-binding protein is involved in Toll-like receptor (TLR) signaling and contributes to the cross-talk between TLR and IFN-γ signaling pathways
    • Zhao, J. et al. IRF-8/interferon (IFN) consensus sequence-binding protein is involved in Toll-like receptor (TLR) signaling and contributes to the cross-talk between TLR and IFN-γ signaling pathways. J. Biol. Chem. 281, 10073-10080 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 10073-10080
    • Zhao, J.1
  • 99
    • 2442689141 scopus 로고    scopus 로고
    • Toll-like receptor 9 signaling activates NF-κB through IFN regulatory factor-8/IFN consensus sequence binding protein in dendritic cells
    • Tsujimura, H. et al. Toll-like receptor 9 signaling activates NF-κB through IFN regulatory factor-8/IFN consensus sequence binding protein in dendritic cells. J. Immunol. 172, 6820-6827 (2004).
    • (2004) J. Immunol. , vol.172 , pp. 6820-6827
    • Tsujimura, H.1
  • 100
    • 0036179505 scopus 로고    scopus 로고
    • The role of IRF-4 in transcriptional regulation
    • Marecki, S. & Fenton, M. J. The role of IRF-4 in transcriptional regulation. J. Interferon Cytokine Res. 22, 121-133 (2002).
    • (2002) J. Interferon Cytokine Res. , vol.22 , pp. 121-133
    • Marecki, S.1    Fenton, M.J.2
  • 101
    • 4644252538 scopus 로고    scopus 로고
    • One nucleotide in a κB site can determine cofactor specificity for NF-κB dimers
    • Leung, T. H., Hoffmann, A. & Baltimore, D. One nucleotide in a κB site can determine cofactor specificity for NF-κB dimers. Cell 118, 453-464 (2004).
    • (2004) Cell , vol.118 , pp. 453-464
    • Leung, T.H.1    Hoffmann, A.2    Baltimore, D.3
  • 102
    • 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-κB
    • Wietek, C., Miggin, S. M., Jefferies, C. A. & O'Neill, L. A. 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-κB. J. Biol. Chem. 278, 50923-50931 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 50923-50931
    • Wietek, C.1    Miggin, S.M.2    Jefferies, C.A.3    O'Neill, L.A.4
  • 103
    • 23844464444 scopus 로고    scopus 로고
    • Suppression of RNA recognition by Toll-like receptors: The impact of nucleoside modification and the evolutionary origin of RNA
    • Kariko, K., Buckstein, M., Ni, H. & Weissman, D. Suppression of RNA recognition by Toll-like receptors: the impact of nucleoside modification and the evolutionary origin of RNA. Immunity 23, 165-175 (2005).
    • (2005) Immunity , vol.23 , pp. 165-175
    • Kariko, K.1    Buckstein, M.2    Ni, H.3    Weissman, D.4
  • 104
    • 1642268316 scopus 로고    scopus 로고
    • Innate immune system discriminates between RNA containing bacterial versus eukaryotic structural features that prime for high-level IL-12 secretion by dendritic cells
    • Koski, G. K. et al. Innate immune system discriminates between RNA containing bacterial versus eukaryotic structural features that prime for high-level IL-12 secretion by dendritic cells. J. Immunol. 172, 3989-3993 (2004).
    • (2004) J. Immunol. , vol.172 , pp. 3989-3993
    • Koski, G.K.1
  • 105
    • 0036219195 scopus 로고    scopus 로고
    • CpG motifs in bacterial DNA and their immune effects
    • Krieg, A. M. CpG motifs in bacterial DNA and their immune effects. Annu. Rev. Immunol. 20, 709-760 (2002).
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 709-760
    • Krieg, A.M.1
  • 106
    • 28544449709 scopus 로고    scopus 로고
    • Immune stimulation mediated by autoantigen binding sites within small nuclear RNAs involves Toll-like receptors 7 and 8
    • Vollmer, J. et al. Immune stimulation mediated by autoantigen binding sites within small nuclear RNAs involves Toll-like receptors 7 and 8. J. Exp. Med. 202, 1575-1585 (2005).
    • (2005) J. Exp. Med. , vol.202 , pp. 1575-1585
    • Vollmer, J.1
  • 107
    • 27744444832 scopus 로고    scopus 로고
    • RNA-associated autoantigens activate B cells by combined B cell antigen receptor/Toll-like receptor 7 engagement
    • Lau, C. M. et al. RNA-associated autoantigens activate B cells by combined B cell antigen receptor/Toll-like receptor 7 engagement. J. Exp. Med. 202, 1171-1177 (2005).
    • (2005) J. Exp. Med. , vol.202 , pp. 1171-1177
    • Lau, C.M.1
  • 108
    • 0037061453 scopus 로고    scopus 로고
    • Chromatin-IgG complexes activate B cells by dual engagement of IgM and Toll-like receptors
    • Leadbetter, E. A. et al. Chromatin-IgG complexes activate B cells by dual engagement of IgM and Toll-like receptors. Nature 416, 603-607 (2002).
    • (2002) Nature , vol.416 , pp. 603-607
    • Leadbetter, E.A.1
  • 109
    • 0038639795 scopus 로고    scopus 로고
    • Systemic lupus erythematosus and the type I interferon system
    • Ronnblom, L. & Alm, G. V. Systemic lupus erythematosus and the type I interferon system. Arthritis Res. Ther. 5, 68-75 (2003).
    • (2003) Arthritis Res. Ther. , vol.5 , pp. 68-75
    • Ronnblom, L.1    Alm, G.V.2
  • 110
    • 3042548183 scopus 로고    scopus 로고
    • Toll-like receptor 9-dependent and -independent dendritic cell activation by chromatin-immunoglobulin G complexes
    • Boule, M. W. et al. Toll-like receptor 9-dependent and -independent dendritic cell activation by chromatin-immunoglobulin G complexes. J. Exp. Med. 199, 1631-1640 (2004).
    • (2004) J. Exp. Med. , vol.199 , pp. 1631-1640
    • Boule, M.W.1
  • 111
    • 0035900481 scopus 로고    scopus 로고
    • Induction of dendritic cell differentiation by IFN-α in systemic lupus erythematosus
    • Blanco, P., Palucka, A. K., Gill, M., Pascual, V. & Banchereau, J. Induction of dendritic cell differentiation by IFN-α in systemic lupus erythematosus. Science 294, 1540-1543 (2001).
    • (2001) Science , vol.294 , pp. 1540-1543
    • Blanco, P.1    Palucka, A.K.2    Gill, M.3    Pascual, V.4    Banchereau, J.5
  • 112
    • 18644383289 scopus 로고    scopus 로고
    • Endosomal translocation of vertebrate DNA activates dendritic cells via TLR9-dependent and -independent pathways
    • Yasuda, K. et al. Endosomal translocation of vertebrate DNA activates dendritic cells via TLR9-dependent and -independent pathways. J. Immunol. 174, 6129-6136 (2005).
    • (2005) J. Immunol. , vol.174 , pp. 6129-6136
    • Yasuda, K.1
  • 113
    • 9244234953 scopus 로고    scopus 로고
    • Targeting split vaccines to the endosome improves vaccination
    • Wagner, H., Heit, A., Schmitz, F. & Bauer, S. Targeting split vaccines to the endosome improves vaccination. Curr. Opin. Biotechnol. 15, 538-542 (2004).
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 538-542
    • Wagner, H.1    Heit, A.2    Schmitz, F.3    Bauer, S.4
  • 114
    • 33646368404 scopus 로고    scopus 로고
    • A common haplotype of interferon regulatory factor 5 (IRF5) regulates splicing and expression and is associated with increased risk of systemic lupus erythematosus
    • Graham, R. R. et al. A common haplotype of interferon regulatory factor 5 (IRF5) regulates splicing and expression and is associated with increased risk of systemic lupus erythematosus. Nature Genet. 38, 550-555 (2006). This paper reports that variants of IRF5 can confer risk of SLE.
    • (2006) Nature Genet. , vol.38 , pp. 550-555
    • Graham, R.R.1
  • 115
    • 0028146097 scopus 로고
    • Involvement of the IRF-1 transcription factor in antiviral responses to interferons
    • Kimura, T. et al. Involvement of the IRF-1 transcription factor in antiviral responses to interferons. Science 264, 1921-1924 (1994).
    • (1994) Science , vol.264 , pp. 1921-1924
    • Kimura, T.1
  • 116
    • 0036498798 scopus 로고    scopus 로고
    • Susceptibility of IFN regulatory factor-1 and IFN consensus sequence binding protein-deficient mice to brucellosis
    • Ko, J., Gendron-Fitzpatrick, A. & Splitter, G. A. Susceptibility of IFN regulatory factor-1 and IFN consensus sequence binding protein-deficient mice to brucellosis. J. Immunol. 168, 2433-2440 (2002).
    • (2002) J. Immunol. , vol.168 , pp. 2433-2440
    • Ko, J.1    Gendron-Fitzpatrick, A.2    Splitter, G.A.3
  • 117
    • 0030741433 scopus 로고    scopus 로고
    • H1-type immune responses by the transcription factor IRF-1
    • H1-type immune responses by the transcription factor IRF-1. Immunity 6, 673-679 (1997).
    • (1997) Immunity , vol.6 , pp. 673-679
    • Taki, S.1
  • 118
    • 0032510062 scopus 로고    scopus 로고
    • Requirement for IRF-1 in the microenvironment supporting development of natural killer cells
    • Ogasawara, K. et al. Requirement for IRF-1 in the microenvironment supporting development of natural killer cells. Nature 391, 700-703 (1998).
    • (1998) Nature , vol.391 , pp. 700-703
    • Ogasawara, K.1
  • 119
  • 120
    • 16044362508 scopus 로고    scopus 로고
    • Cooperation of the tumour suppressors IRF-1 and p53 in response to DNA damage
    • Tanaka, N. et al. Cooperation of the tumour suppressors IRF-1 and p53 in response to DNA damage. Nature 382, 816-818 (1996).
    • (1996) Nature , vol.382 , pp. 816-818
    • Tanaka, N.1
  • 121
    • 0029144891 scopus 로고
    • An IRF-1-dependent pathway of DNA damage-induced apoptosis in mitogen-activated T lymphocytes
    • Tamura, T. et al. An IRF-1-dependent pathway of DNA damage-induced apoptosis in mitogen-activated T lymphocytes. Nature 376, 596-599 (1995).
    • (1995) Nature , vol.376 , pp. 596-599
    • Tamura, T.1
  • 122
    • 0033635304 scopus 로고    scopus 로고
    • + T cell-mediated skin disease in mice lacking IRF-2, the transcriptional attenuator of interferon-α/β signaling
    • + T cell-mediated skin disease in mice lacking IRF-2, the transcriptional attenuator of interferon-α/β signaling. Immunity 13, 643-655 (2000).
    • (2000) Immunity , vol.13 , pp. 643-655
    • Hida, S.1
  • 123
    • 1442330451 scopus 로고    scopus 로고
    • Negative regulation of IFN-α/β signaling by IFN regulatory factor 2 for homeostatic development of dendritic cells
    • Honda, K., Mizutani, T. & Taniguchi, T. Negative regulation of IFN-α/β signaling by IFN regulatory factor 2 for homeostatic development of dendritic cells. Proc. Natl Acad. Sci. USA 101, 2416-2421 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2416-2421
    • Honda, K.1    Mizutani, T.2    Taniguchi, T.3
  • 124
    • 0034617994 scopus 로고    scopus 로고
    • Deficiency in the transcription factor interferon regulatory factor (IRF)-2 leads to severely compromised development of natural killer and T helper type 1 cells
    • Lohoff, M. et al. Deficiency in the transcription factor interferon regulatory factor (IRF)-2 leads to severely compromised development of natural killer and T helper type 1 cells. J. Exp. Med. 192, 325-336 (2000).
    • (2000) J. Exp. Med. , vol.192 , pp. 325-336
    • Lohoff, M.1
  • 125
    • 0037089575 scopus 로고    scopus 로고
    • Interferon regulatory factor 4 (IRF4) interacts with NFATc2 to modulate interleukin 4 gene expression
    • Rengarajan, J. et al. Interferon regulatory factor 4 (IRF4) interacts with NFATc2 to modulate interleukin 4 gene expression. J. Exp. Med. 195, 1003-1012 (2002).
    • (2002) J. Exp. Med. , vol.195 , pp. 1003-1012
    • Rengarajan, J.1
  • 126
    • 0037015052 scopus 로고    scopus 로고
    • Dysregulated T helper cell differentiation in the absence of interferon regulatory factor 4
    • Lohoff, M. et al. Dysregulated T helper cell differentiation in the absence of interferon regulatory factor 4. Proc. Natl Acad. Sci. USA 99, 11808-11812 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11808-11812
    • Lohoff, M.1
  • 127
    • 15444346834 scopus 로고    scopus 로고
    • Requirement for the transcription factor LSIRF/IRF4 for mature B and T lymphocyte function
    • Mittrucker, H. W. et al. Requirement for the transcription factor LSIRF/IRF4 for mature B and T lymphocyte function. Science 275, 540-543 (1997).
    • (1997) Science , vol.275 , pp. 540-543
    • Mittrucker, H.W.1
  • 128
    • 0038506030 scopus 로고    scopus 로고
    • IRF-4, 8 orchestrate the pre-B-to-B transition in lymphocyte development
    • Lu, R., Medina, K. L., Lancki, D. W. & Singh, H. IRF-4, 8 orchestrate the pre-B-to-B transition in lymphocyte development. Genes Dev. 17, 1703-1708 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 1703-1708
    • Lu, R.1    Medina, K.L.2    Lancki, D.W.3    Singh, H.4
  • 129
    • 14044270784 scopus 로고    scopus 로고
    • IFN regulatory factor-4 and -8 govern dendritic cell subset development and their functional diversity
    • Tamura, T. et al. IFN regulatory factor-4 and -8 govern dendritic cell subset development and their functional diversity. J. Immunol. 174, 2573-2581 (2005).
    • (2005) J. Immunol. , vol.174 , pp. 2573-2581
    • Tamura, T.1
  • 130
    • 0030896666 scopus 로고    scopus 로고
    • Crucial role of interferon consensus sequence binding protein, but neither of interferon regulatory factor 1 nor of nitric oxide synthesis for protection against murine listeriosis
    • Fehr, T. et al. Crucial role of interferon consensus sequence binding protein, but neither of interferon regulatory factor 1 nor of nitric oxide synthesis for protection against murine listeriosis. J. Exp. Med. 185, 921-931 (1997).
    • (1997) J. Exp. Med. , vol.185 , pp. 921-931
    • Fehr, T.1
  • 131
    • 0030670801 scopus 로고    scopus 로고
    • Interferon (IFN) consensus sequence-binding protein, a transcription factor of the IFN regulatory factor family, regulates immune responses in vivo through control of interleukin 12 expression
    • Giese, N. A. et al. Interferon (IFN) consensus sequence-binding protein, a transcription factor of the IFN regulatory factor family, regulates immune responses in vivo through control of interleukin 12 expression. J. Exp. Med. 186, 1535-1546 (1997).
    • (1997) J. Exp. Med. , vol.186 , pp. 1535-1546
    • Giese, N.A.1
  • 132
    • 0030664056 scopus 로고    scopus 로고
    • Interferon consensus sequence binding protein-deficient mice display impaired resistance to intracellular infection due to a primary defect in interleukin 12 p40 induction
    • Scharton-Kersten, T., Contursi, C., Masumi, A., Sher, A. & Ozato, K. Interferon consensus sequence binding protein-deficient mice display impaired resistance to intracellular infection due to a primary defect in interleukin 12 p40 induction. J. Exp. Med. 186, 1523-1534 (1997).
    • (1997) J. Exp. Med. , vol.186 , pp. 1523-1534
    • Scharton-Kersten, T.1    Contursi, C.2    Masumi, A.3    Sher, A.4    Ozato, K.5
  • 133
    • 16044369709 scopus 로고    scopus 로고
    • Immunodeficiency and chronic myelogenous leukemia-like syndrome in mice with a targeted mutation of the ICSBP gene
    • Holtschke, T. et al. Immunodeficiency and chronic myelogenous leukemia-like syndrome in mice with a targeted mutation of the ICSBP gene. Cell 87, 307-317 (1996).
    • (1996) Cell , vol.87 , pp. 307-317
    • Holtschke, T.1
  • 134
    • 0037011021 scopus 로고    scopus 로고
    • + dendritic cells
    • + dendritic cells. J. Exp. Med. 196, 1415-1425 (2002).
    • (2002) J. Exp. Med. , vol.196 , pp. 1415-1425
    • Schiavoni, G.1
  • 135
    • 17144466405 scopus 로고    scopus 로고
    • Regulation of IFN-α/β genes: Evidence for a dual function of the transcription factor complex ISGF3 in the production and action of IFN-β/α
    • Harada, H. et al. Regulation of IFN-α/β genes: evidence for a dual function of the transcription factor complex ISGF3 in the production and action of IFN-β/α. Genes Cells 1, 995-1005 (1996).
    • (1996) Genes Cells , vol.1 , pp. 995-1005
    • Harada, H.1
  • 136
    • 20044382430 scopus 로고    scopus 로고
    • Toll-like receptor 3 promotes cross-priming to virus-infected cells
    • Schulz, O. et al. Toll-like receptor 3 promotes cross-priming to virus-infected cells. Nature 433, 887-892 (2005).
    • (2005) Nature , vol.433 , pp. 887-892
    • Schulz, O.1
  • 137
    • 0038651180 scopus 로고    scopus 로고
    • Molecular basis for the immunostimulatory activity of guanine nucleoside analogs: Activation of Toll-like receptor 7
    • Lee, J. et al. Molecular basis for the immunostimulatory activity of guanine nucleoside analogs: activation of Toll-like receptor 7. Proc. Natl Acad. Sci. USA 100, 6646-6651 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6646-6651
    • Lee, J.1
  • 138
    • 20144389695 scopus 로고    scopus 로고
    • Sequence-specific potent induction of IFN-α by short interfering RNA in plasmacytoid dendritic cells through TLR7
    • Hornung, V. et al. Sequence-specific potent induction of IFN-α by short interfering RNA in plasmacytoid dendritic cells through TLR7. Nature Med. 11, 263-270 (2005).
    • (2005) Nature Med. , vol.11 , pp. 263-270
    • Hornung, V.1
  • 139
    • 22344454846 scopus 로고    scopus 로고
    • Sequence-dependent stimulation of the mammalian innate immune response by synthetic siRNA
    • Judge, A. D. et al. Sequence-dependent stimulation of the mammalian innate immune response by synthetic siRNA. Nature Biotechnol. 23, 457-462 (2005).
    • (2005) Nature Biotechnol. , vol.23 , pp. 457-462
    • Judge, A.D.1
  • 140
    • 0034619794 scopus 로고    scopus 로고
    • A Toll-like receptor recognizes bacterial DNA
    • Hemmi, H. et al. A Toll-like receptor recognizes bacterial DNA. Nature 408, 740-745 (2000). This paper reports on the discovery and function of TLR9.
    • (2000) Nature , vol.408 , pp. 740-745
    • Hemmi, H.1
  • 141
    • 0033000436 scopus 로고    scopus 로고
    • A role for casein kinase II phosphorylation in the regulation of IRF-1 transcriptional activity
    • Lin, R. & Hiscott, J. A role for casein kinase II phosphorylation in the regulation of IRF-1 transcriptional activity. Mol. Cell. Biochem. 191, 169-180 (1999).
    • (1999) Mol. Cell. Biochem. , vol.191 , pp. 169-180
    • Lin, R.1    Hiscott, J.2
  • 142
    • 0030930058 scopus 로고    scopus 로고
    • Identification and characterization of nucleophosmin/B23/numatrin which binds the anti-oncogenic transcription factor IRF-1 and manifests oncogenic activity
    • Kondo, T. et al. Identification and characterization of nucleophosmin/B23/numatrin which binds the anti-oncogenic transcription factor IRF-1 and manifests oncogenic activity. Oncogene 15, 1275-1281 (1997).
    • (1997) Oncogene , vol.15 , pp. 1275-1281
    • Kondo, T.1
  • 143
    • 7644223905 scopus 로고    scopus 로고
    • Interferon regulatory factor 1 binding to p300 stimulates DNA-dependent acetylation of p53
    • Dornan, D. et al. Interferon regulatory factor 1 binding to p300 stimulates DNA-dependent acetylation of p53. Mol. Cell. Biol. 24, 10083-10098 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10083-10098
    • Dornan, D.1
  • 144
    • 30444456366 scopus 로고    scopus 로고
    • The GRIP1:IRF3 interaction as a target for glucocorticoid receptor-mediated immunosuppression
    • Reily, M. M., Pantoja, C., Hu, X., Chinenov, Y. & Rogatsky, I. The GRIP1:IRF3 interaction as a target for glucocorticoid receptor-mediated immunosuppression. EMBO J. 25, 108-117 (2006).
    • (2006) EMBO J. , vol.25 , pp. 108-117
    • Reily, M.M.1    Pantoja, C.2    Hu, X.3    Chinenov, Y.4    Rogatsky, I.5
  • 145
    • 0034144377 scopus 로고    scopus 로고
    • Posttranslational regulation of IRF-4 activity by the immunophilin FKBP52
    • Mamane, Y., Sharma, S., Petropoulos, L., Lin, R. & Hiscott, J. Posttranslational regulation of IRF-4 activity by the immunophilin FKBP52. Immunity 12, 129-140 (2000).
    • (2000) Immunity , vol.12 , pp. 129-140
    • Mamane, Y.1    Sharma, S.2    Petropoulos, L.3    Lin, R.4    Hiscott, J.5
  • 146
    • 0033567084 scopus 로고    scopus 로고
    • Roles of IFN consensus sequence binding protein and PU.1 in regulating IL-18 gene expression
    • Kim, Y. M. et al. Roles of IFN consensus sequence binding protein and PU.1 in regulating IL-18 gene expression. J. Immunol. 163, 2000-2007 (1999).
    • (1999) J. Immunol. , vol.163 , pp. 2000-2007
    • Kim, Y.M.1
  • 147
    • 1642499349 scopus 로고    scopus 로고
    • Transforming growth factor β/Smad3 signaling regulates IRF-7 function and transcriptional activation of the β interferon promoter
    • Qing, J. et al. Transforming growth factor β/Smad3 signaling regulates IRF-7 function and transcriptional activation of the β interferon promoter. Mol. Cell. Biol. 24, 1411-1425 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1411-1425
    • Qing, J.1
  • 148
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • Darnell, J. E. Jr., Kerr, I. M. & Stark, G. R. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 264, 1415-1421 (1994).
    • (1994) Science , vol.264 , pp. 1415-1421
    • Darnell Jr., J.E.1    Kerr, I.M.2    Stark, G.R.3


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