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Volumn 25, Issue 7, 2017, Pages 573-584

Transcriptional Regulation of Antiviral Interferon-Stimulated Genes

Author keywords

IFN; ISG; transcription

Indexed keywords

CRK LIKE PROTEIN; INTERFERON; INTERFERON RECEPTOR; INTERFERON REGULATORY FACTOR 1; JANUS KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; RAC1 PROTEIN; RETINOIC ACID; STAT5 PROTEIN; TUMOR NECROSIS FACTOR; ANTIVIRUS AGENT;

EID: 85010867865     PISSN: 0966842X     EISSN: 18784380     Source Type: Journal    
DOI: 10.1016/j.tim.2017.01.001     Document Type: Review
Times cited : (149)

References (129)
  • 1
    • 84896958063 scopus 로고    scopus 로고
    • Innate immune sensing and signaling of cytosolic nucleic acids
    • Wu, J., Chen, Z.J., Innate immune sensing and signaling of cytosolic nucleic acids. Annu. Rev. Immunol. 32 (2014), 461–488.
    • (2014) Annu. Rev. Immunol. , vol.32 , pp. 461-488
    • Wu, J.1    Chen, Z.J.2
  • 2
    • 84896987305 scopus 로고    scopus 로고
    • Interferon-stimulated genes: a complex web of host defenses
    • Schneider, W.M., et al. Interferon-stimulated genes: a complex web of host defenses. Annu. Rev. Immunol. 32 (2014), 513–545.
    • (2014) Annu. Rev. Immunol. , vol.32 , pp. 513-545
    • Schneider, W.M.1
  • 3
    • 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. Nat. Rev. Immunol. 5 (2005), 375–386.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 375-386
    • Platanias, L.C.1
  • 4
    • 84859992161 scopus 로고    scopus 로고
    • The JAK–STAT pathway at twenty
    • Stark, G.R., Darnell, J.E. Jr, The JAK–STAT pathway at twenty. Immunity 36 (2012), 503–514.
    • (2012) Immunity , vol.36 , pp. 503-514
    • Stark, G.R.1    Darnell, J.E.2
  • 5
    • 84943815333 scopus 로고    scopus 로고
    • Cut, copy, move, delete: the study of human interferon genes reveal multiple mechanisms underlying their evolution in amniotes
    • Krause, C.D., Pestka, S., Cut, copy, move, delete: the study of human interferon genes reveal multiple mechanisms underlying their evolution in amniotes. Cytokine 76 (2015), 480–495.
    • (2015) Cytokine , vol.76 , pp. 480-495
    • Krause, C.D.1    Pestka, S.2
  • 7
    • 84940843590 scopus 로고    scopus 로고
    • Type III interferons (IFNs): emerging master regulators of immunity
    • Galani, I.E., et al. Type III interferons (IFNs): emerging master regulators of immunity. Adv. Exp. Med. Biol. 850 (2015), 1–15.
    • (2015) Adv. Exp. Med. Biol. , vol.850 , pp. 1-15
    • Galani, I.E.1
  • 8
    • 34848817968 scopus 로고    scopus 로고
    • Acetylation-dependent signal transduction for type I interferon receptor
    • Tang, X., et al. Acetylation-dependent signal transduction for type I interferon receptor. Cell 131 (2007), 93–105.
    • (2007) Cell , vol.131 , pp. 93-105
    • Tang, X.1
  • 9
    • 84869869682 scopus 로고    scopus 로고
    • HDAC inhibitor-based therapies: can we interpret the code?
    • New, M., et al. HDAC inhibitor-based therapies: can we interpret the code?. Mol. Oncol. 6 (2012), 637–656.
    • (2012) Mol. Oncol. , vol.6 , pp. 637-656
    • New, M.1
  • 10
    • 0842266786 scopus 로고    scopus 로고
    • Interferon-gamma: an overview of signals, mechanisms and functions
    • Schroder, K., et al. Interferon-gamma: an overview of signals, mechanisms and functions. J. Leukoc. Biol. 75 (2004), 163–189.
    • (2004) J. Leukoc. Biol. , vol.75 , pp. 163-189
    • Schroder, K.1
  • 11
    • 8744247500 scopus 로고    scopus 로고
    • Phosphorylation and specific ubiquitin acceptor sites are required for ubiquitination and degradation of the IFNAR1 subunit of type I interferon receptor
    • Kumar, K.G., et al. Phosphorylation and specific ubiquitin acceptor sites are required for ubiquitination and degradation of the IFNAR1 subunit of type I interferon receptor. J. Biol. Chem. 279 (2004), 46614–46620.
    • (2004) J. Biol. Chem. , vol.279 , pp. 46614-46620
    • Kumar, K.G.1
  • 12
    • 33745761009 scopus 로고    scopus 로고
    • UBP43 is a novel regulator of interferon signaling independent of its ISG15 isopeptidase activity
    • Malakhova, O.A., et al. UBP43 is a novel regulator of interferon signaling independent of its ISG15 isopeptidase activity. EMBO J. 25 (2006), 2358–2367.
    • (2006) EMBO J. , vol.25 , pp. 2358-2367
    • Malakhova, O.A.1
  • 13
    • 84922880395 scopus 로고    scopus 로고
    • Human intracellular ISG15 prevents interferon-alpha/beta over-amplification and auto-inflammation
    • Zhang, X., et al. Human intracellular ISG15 prevents interferon-alpha/beta over-amplification and auto-inflammation. Nature 517 (2015), 89–93.
    • (2015) Nature , vol.517 , pp. 89-93
    • Zhang, X.1
  • 14
    • 29244442569 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling 1 regulates the immune response to infection by a unique inhibition of type I interferon activity
    • Fenner, J.E., et al. Suppressor of cytokine signaling 1 regulates the immune response to infection by a unique inhibition of type I interferon activity. Nat. Immunol. 7 (2006), 33–39.
    • (2006) Nat. Immunol. , vol.7 , pp. 33-39
    • Fenner, J.E.1
  • 15
    • 84881218296 scopus 로고    scopus 로고
    • Suppression of cytokine signaling: the SOCS perspective
    • Linossi, E.M., et al. Suppression of cytokine signaling: the SOCS perspective. Cytokine Growth Factor Rev. 24 (2013), 241–248.
    • (2013) Cytokine Growth Factor Rev. , vol.24 , pp. 241-248
    • Linossi, E.M.1
  • 16
    • 70449698533 scopus 로고    scopus 로고
    • SOCS-1 binding to tyrosine 441 of IFN-gamma receptor subunit 1 contributes to the attenuation of IFN-gamma signaling in vivo
    • Starr, R., et al. SOCS-1 binding to tyrosine 441 of IFN-gamma receptor subunit 1 contributes to the attenuation of IFN-gamma signaling in vivo. J. Immunol. 183 (2009), 4537–4544.
    • (2009) J. Immunol. , vol.183 , pp. 4537-4544
    • Starr, R.1
  • 17
    • 0027411525 scopus 로고
    • The molecular cell biology of interferon-gamma and its receptor
    • Farrar, M.A., Schreiber, R.D., The molecular cell biology of interferon-gamma and its receptor. Annu. Rev. Immunol. 11 (1993), 571–611.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 571-611
    • Farrar, M.A.1    Schreiber, R.D.2
  • 18
    • 0035216135 scopus 로고    scopus 로고
    • Interferon-gamma receptor 2 expression as the deciding factor in human T, B, and myeloid cell proliferation or death
    • Bernabei, P., et al. Interferon-gamma receptor 2 expression as the deciding factor in human T, B, and myeloid cell proliferation or death. J. Leukoc. Biol. 70 (2001), 950–960.
    • (2001) J. Leukoc. Biol. , vol.70 , pp. 950-960
    • Bernabei, P.1
  • 19
    • 0028972504 scopus 로고
    • Ligand-induced autoregulation of IFN-gamma receptor beta chain expression in T helper cell subsets
    • Bach, E.A., et al. Ligand-induced autoregulation of IFN-gamma receptor beta chain expression in T helper cell subsets. Science 270 (1995), 1215–1218.
    • (1995) Science , vol.270 , pp. 1215-1218
    • Bach, E.A.1
  • 20
    • 84904638434 scopus 로고    scopus 로고
    • The molecular regulation of Janus kinase (JAK) activation
    • Babon, J.J., et al. The molecular regulation of Janus kinase (JAK) activation. Biochem. J. 462 (2014), 1–13.
    • (2014) Biochem. J. , vol.462 , pp. 1-13
    • Babon, J.J.1
  • 21
    • 84929283755 scopus 로고    scopus 로고
    • STAT2 phosphorylation and signaling
    • Steen, H.C., Gamero, A.M., STAT2 phosphorylation and signaling. JAKSTAT, 2, 2013, e25790.
    • (2013) JAKSTAT , vol.2 , pp. e25790
    • Steen, H.C.1    Gamero, A.M.2
  • 22
    • 0035930501 scopus 로고    scopus 로고
    • TYK2 and JAK2 are substrates of protein-tyrosine phosphatase 1B
    • Myers, M.P., et al. TYK2 and JAK2 are substrates of protein-tyrosine phosphatase 1B. J. Biol. Chem. 276 (2001), 47771–47774.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47771-47774
    • Myers, M.P.1
  • 23
    • 0035905767 scopus 로고    scopus 로고
    • CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling
    • Irie-Sasaki, J., et al. CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling. Nature 409 (2001), 349–354.
    • (2001) Nature , vol.409 , pp. 349-354
    • Irie-Sasaki, J.1
  • 24
    • 0037047335 scopus 로고    scopus 로고
    • CD45 controls interleukin-4-mediated IgE class switch recombination in human B cells through its function as a Janus kinase phosphatase
    • Yamada, T., et al. CD45 controls interleukin-4-mediated IgE class switch recombination in human B cells through its function as a Janus kinase phosphatase. J. Biol. Chem. 277 (2002), 28830–28835.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28830-28835
    • Yamada, T.1
  • 25
    • 0036006288 scopus 로고    scopus 로고
    • The T cell protein tyrosine phosphatase is a negative regulator of janus family kinases 1 and 3
    • Simoncic, P.D., et al. The T cell protein tyrosine phosphatase is a negative regulator of janus family kinases 1 and 3. Curr. Biol. 12 (2002), 446–453.
    • (2002) Curr. Biol. , vol.12 , pp. 446-453
    • Simoncic, P.D.1
  • 26
    • 0346101802 scopus 로고    scopus 로고
    • SHP-2 regulates SOCS-1-mediated Janus kinase-2 ubiquitination/degradation downstream of the prolactin receptor
    • Ali, S., et al. SHP-2 regulates SOCS-1-mediated Janus kinase-2 ubiquitination/degradation downstream of the prolactin receptor. J. Biol. Chem. 278 (2003), 52021–52031.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52021-52031
    • Ali, S.1
  • 27
    • 84876222093 scopus 로고    scopus 로고
    • Janus kinase inhibitors in autoimmune diseases
    • O'Shea, J.J., et al. Janus kinase inhibitors in autoimmune diseases. Ann. Rheum. Dis. 72:Suppl. 2 (2013), 111–115.
    • (2013) Ann. Rheum. Dis. , vol.72 , pp. 111-115
    • O'Shea, J.J.1
  • 28
    • 84855495283 scopus 로고    scopus 로고
    • IkappaB kinase epsilon (IKKε) regulates the balance between type I and type II interferon responses
    • Ng, S.L., et al. IkappaB kinase epsilon (IKKε) regulates the balance between type I and type II interferon responses. Proc. Natl. Acad. Sci. U. S. A. 108 (2011), 21170–21175.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 21170-21175
    • Ng, S.L.1
  • 29
    • 33847687659 scopus 로고    scopus 로고
    • Multiple functions of the IKK-related kinase IKKepsilon in interferon-mediated antiviral immunity
    • Tenoever, B.R., et al. Multiple functions of the IKK-related kinase IKKepsilon in interferon-mediated antiviral immunity. Science 315 (2007), 1274–1278.
    • (2007) Science , vol.315 , pp. 1274-1278
    • Tenoever, B.R.1
  • 30
    • 84872092694 scopus 로고    scopus 로고
    • Identification of STAT2 serine 287 as a novel regulatory phosphorylation site in type I interferon-induced cellular responses
    • Steen, H.C., et al. Identification of STAT2 serine 287 as a novel regulatory phosphorylation site in type I interferon-induced cellular responses. J. Biol. Chem. 288 (2013), 747–758.
    • (2013) J. Biol. Chem. , vol.288 , pp. 747-758
    • Steen, H.C.1
  • 31
    • 84893443507 scopus 로고    scopus 로고
    • Novel antiviral host factor, TNK1, regulates IFN signaling through serine phosphorylation of STAT1
    • Ooi, E.L., et al. Novel antiviral host factor, TNK1, regulates IFN signaling through serine phosphorylation of STAT1. Proc. Natl. Acad. Sci. U. S. A. 111 (2014), 1909–1914.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 1909-1914
    • Ooi, E.L.1
  • 32
    • 79952133903 scopus 로고    scopus 로고
    • RA-inducible gene-I induction augments STAT1 activation to inhibit leukemia cell proliferation
    • Jiang, L.J., et al. RA-inducible gene-I induction augments STAT1 activation to inhibit leukemia cell proliferation. Proc. Natl. Acad. Sci. U. S. A. 108 (2011), 1897–1902.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 1897-1902
    • Jiang, L.J.1
  • 33
    • 84892434546 scopus 로고    scopus 로고
    • Hepatic RIG-I predicts survival and interferon-alpha therapeutic response in hepatocellular carcinoma
    • Hou, J., et al. Hepatic RIG-I predicts survival and interferon-alpha therapeutic response in hepatocellular carcinoma. Cancer Cell 25 (2014), 49–63.
    • (2014) Cancer Cell , vol.25 , pp. 49-63
    • Hou, J.1
  • 34
    • 85007082176 scopus 로고    scopus 로고
    • CDK8 as the STAT1 serine 727 kinase?
    • Staab, J., et al. CDK8 as the STAT1 serine 727 kinase?. JAKSTAT, 2, 2013, e24275.
    • (2013) JAKSTAT , vol.2 , pp. e24275
    • Staab, J.1
  • 35
    • 84874282698 scopus 로고    scopus 로고
    • CDK8 kinase phosphorylates transcription factor STAT1 to selectively regulate the interferon response
    • Bancerek, J., et al. CDK8 kinase phosphorylates transcription factor STAT1 to selectively regulate the interferon response. Immunity 38 (2013), 250–262.
    • (2013) Immunity , vol.38 , pp. 250-262
    • Bancerek, J.1
  • 36
    • 3042648414 scopus 로고    scopus 로고
    • A linear signal transduction pathway involving phosphatidylinositol 3-kinase, protein kinase Cepsilon, and MAPK in mesangial cells regulates interferon-gamma-induced STAT1alpha transcriptional activation
    • Choudhury, G.G., A linear signal transduction pathway involving phosphatidylinositol 3-kinase, protein kinase Cepsilon, and MAPK in mesangial cells regulates interferon-gamma-induced STAT1alpha transcriptional activation. J. Biol. Chem. 279 (2004), 27399–27409.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27399-27409
    • Choudhury, G.G.1
  • 37
    • 0035823494 scopus 로고    scopus 로고
    • Roles of phosphatidylinositol 3-kinase in interferon-gamma-dependent phosphorylation of STAT1 on serine 727 and activation of gene expression
    • Nguyen, H., et al. Roles of phosphatidylinositol 3-kinase in interferon-gamma-dependent phosphorylation of STAT1 on serine 727 and activation of gene expression. J. Biol. Chem. 276 (2001), 33361–33368.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33361-33368
    • Nguyen, H.1
  • 38
    • 0037177813 scopus 로고    scopus 로고
    • Protein kinase C-delta (PKC-delta) is activated by type I interferons and mediates phosphorylation of Stat1 on serine 727
    • Uddin, S., et al. Protein kinase C-delta (PKC-delta) is activated by type I interferons and mediates phosphorylation of Stat1 on serine 727. J. Biol. Chem. 277 (2002), 14408–14416.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14408-14416
    • Uddin, S.1
  • 39
    • 0037530604 scopus 로고    scopus 로고
    • Activation of protein kinase C delta by IFN-gamma
    • Deb, D.K., et al. Activation of protein kinase C delta by IFN-gamma. J. Immunol. 171 (2003), 267–273.
    • (2003) J. Immunol. , vol.171 , pp. 267-273
    • Deb, D.K.1
  • 40
    • 0036789933 scopus 로고    scopus 로고
    • p38 MAPK enhances STAT1-dependent transcription independently of Ser-727 phosphorylation
    • Ramsauer, K., et al. p38 MAPK enhances STAT1-dependent transcription independently of Ser-727 phosphorylation. Proc. Natl. Acad. Sci. U. S. A. 99 (2002), 12859–12864.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12859-12864
    • Ramsauer, K.1
  • 41
    • 0037804774 scopus 로고    scopus 로고
    • Inhibition of coagulation, fibrinolysis, and endothelial cell activation by a p38 mitogen-activated protein kinase inhibitor during human endotoxemia
    • Branger, J., et al. Inhibition of coagulation, fibrinolysis, and endothelial cell activation by a p38 mitogen-activated protein kinase inhibitor during human endotoxemia. Blood 101 (2003), 4446–4448.
    • (2003) Blood , vol.101 , pp. 4446-4448
    • Branger, J.1
  • 42
    • 0037033046 scopus 로고    scopus 로고
    • SHP-2 is a dual-specificity phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues in nuclei
    • Wu, T.R., et al. SHP-2 is a dual-specificity phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues in nuclei. J. Biol. Chem. 277 (2002), 47572–47580.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47572-47580
    • Wu, T.R.1
  • 43
    • 42649118836 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in the JAK/STAT pathway
    • Xu, D., Qu, C.K., Protein tyrosine phosphatases in the JAK/STAT pathway. Front. Biosci. 13 (2008), 4925–4932.
    • (2008) Front. Biosci. , vol.13 , pp. 4925-4932
    • Xu, D.1    Qu, C.K.2
  • 44
    • 0036318564 scopus 로고    scopus 로고
    • Identification of a nuclear Stat1 protein tyrosine phosphatase
    • ten Hoeve, J., et al. Identification of a nuclear Stat1 protein tyrosine phosphatase. Mol. Cell. Biol. 22 (2002), 5662–5668.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5662-5668
    • ten Hoeve, J.1
  • 45
    • 0028972719 scopus 로고
    • Differential regulation of the alpha/beta interferon-stimulated Jak/Stat pathway by the SH2 domain-containing tyrosine phosphatase SHPTP1
    • David, M., et al. Differential regulation of the alpha/beta interferon-stimulated Jak/Stat pathway by the SH2 domain-containing tyrosine phosphatase SHPTP1. Mol. Cell. Biol. 15 (1995), 7050–7058.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 7050-7058
    • David, M.1
  • 46
    • 84908133543 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases as potential therapeutic targets
    • He, R.J., et al. Protein tyrosine phosphatases as potential therapeutic targets. Acta Pharmacol. Sin. 35 (2014), 1227–1246.
    • (2014) Acta Pharmacol. Sin. , vol.35 , pp. 1227-1246
    • He, R.J.1
  • 47
    • 22044431593 scopus 로고    scopus 로고
    • SUMO-1 conjugation selectively modulates STAT1-mediated gene responses
    • Ungureanu, D., et al. SUMO-1 conjugation selectively modulates STAT1-mediated gene responses. Blood 106 (2005), 224–226.
    • (2005) Blood , vol.106 , pp. 224-226
    • Ungureanu, D.1
  • 48
    • 0029061508 scopus 로고
    • Tyrosine-phosphorylated Stat1 and Stat2 plus a 48-kDa protein all contact DNA in forming interferon-stimulated-gene factor 3
    • Qureshi, S.A., et al. Tyrosine-phosphorylated Stat1 and Stat2 plus a 48-kDa protein all contact DNA in forming interferon-stimulated-gene factor 3. Proc. Natl. Acad. Sci. U. S. A. 92 (1995), 3829–3833.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 3829-3833
    • Qureshi, S.A.1
  • 49
    • 0025886837 scopus 로고
    • Isolation and characterization of a new mutant human cell line unresponsive to alpha and beta interferons
    • John, J., et al. Isolation and characterization of a new mutant human cell line unresponsive to alpha and beta interferons. Mol. Cell. Biol. 11 (1991), 4189–4195.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4189-4195
    • John, J.1
  • 50
    • 0029678749 scopus 로고    scopus 로고
    • Essential and non-redundant roles of p48 (ISGF3 gamma) and IRF-1 in both type I and type II interferon responses, as revealed by gene targeting studies
    • Kimura, T., et al. Essential and non-redundant roles of p48 (ISGF3 gamma) and IRF-1 in both type I and type II interferon responses, as revealed by gene targeting studies. Genes Cells 1 (1996), 115–124.
    • (1996) Genes Cells , vol.1 , pp. 115-124
    • Kimura, T.1
  • 51
    • 0025270456 scopus 로고
    • Synergistic interaction between interferon-alpha and interferon-gamma through induced synthesis of one subunit of the transcription factor ISGF3
    • Levy, D.E., et al. Synergistic interaction between interferon-alpha and interferon-gamma through induced synthesis of one subunit of the transcription factor ISGF3. EMBO J. 9 (1990), 1105–1111.
    • (1990) EMBO J. , vol.9 , pp. 1105-1111
    • Levy, D.E.1
  • 52
    • 79960563344 scopus 로고    scopus 로고
    • Determinants and dynamics of genome accessibility
    • Bell, O., et al. Determinants and dynamics of genome accessibility. Nat. Rev. Genet. 12 (2011), 554–564.
    • (2011) Nat. Rev. Genet. , vol.12 , pp. 554-564
    • Bell, O.1
  • 53
    • 2942592799 scopus 로고    scopus 로고
    • The chromatin-remodeling BAF complex mediates cellular antiviral activities by promoter priming
    • Cui, K., et al. The chromatin-remodeling BAF complex mediates cellular antiviral activities by promoter priming. Mol. Cell. Biol. 24 (2004), 4476–4486.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4476-4486
    • Cui, K.1
  • 54
    • 23044461703 scopus 로고    scopus 로고
    • PBAF chromatin-remodeling complex requires a novel specificity subunit, BAF200, to regulate expression of selective interferon-responsive genes
    • Yan, Z., et al. PBAF chromatin-remodeling complex requires a novel specificity subunit, BAF200, to regulate expression of selective interferon-responsive genes. Genes Dev. 19 (2005), 1662–1667.
    • (2005) Genes Dev. , vol.19 , pp. 1662-1667
    • Yan, Z.1
  • 55
    • 0036800352 scopus 로고    scopus 로고
    • Chromatin-remodelling factor BRG1 selectively activates a subset of interferon-alpha-inducible genes
    • Huang, M., et al. Chromatin-remodelling factor BRG1 selectively activates a subset of interferon-alpha-inducible genes. Nat. Cell. Biol. 4 (2002), 774–781.
    • (2002) Nat. Cell. Biol. , vol.4 , pp. 774-781
    • Huang, M.1
  • 56
    • 26844579129 scopus 로고    scopus 로고
    • Apical role for BRG1 in cytokine-induced promoter assembly
    • Ni, Z., et al. Apical role for BRG1 in cytokine-induced promoter assembly. Proc. Natl. Acad. Sci. U. S. A. 102 (2005), 14611–14616.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 14611-14616
    • Ni, Z.1
  • 57
    • 0029767462 scopus 로고    scopus 로고
    • Cooperation of Stat2 and p300/CBP in signalling induced by interferon-alpha
    • Bhattacharya, S., et al. Cooperation of Stat2 and p300/CBP in signalling induced by interferon-alpha. Nature 383 (1996), 344–347.
    • (1996) Nature , vol.383 , pp. 344-347
    • Bhattacharya, S.1
  • 58
    • 0036170183 scopus 로고    scopus 로고
    • IFN-Stimulated transcription through a TBP-free acetyltransferase complex escapes viral shutoff
    • Paulson, M., et al. IFN-Stimulated transcription through a TBP-free acetyltransferase complex escapes viral shutoff. Nat. Cell. Biol. 4 (2002), 140–147.
    • (2002) Nat. Cell. Biol. , vol.4 , pp. 140-147
    • Paulson, M.1
  • 59
    • 79959804516 scopus 로고    scopus 로고
    • Histone deacetylases as regulators of inflammation and immunity
    • Shakespear, M.R., et al. Histone deacetylases as regulators of inflammation and immunity. Trends Immunol. 32 (2011), 335–343.
    • (2011) Trends Immunol. , vol.32 , pp. 335-343
    • Shakespear, M.R.1
  • 60
    • 3042752799 scopus 로고    scopus 로고
    • Induction of interferon-stimulated gene expression and antiviral responses require protein deacetylase activity
    • Chang, H.M., et al. Induction of interferon-stimulated gene expression and antiviral responses require protein deacetylase activity. Proc. Natl. Acad. Sci. U. S. A. 101 (2004), 9578–9583.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9578-9583
    • Chang, H.M.1
  • 61
    • 84879614361 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase activity suppresses IFN-gamma induction of tripartite motif 22 via CHIP-mediated proteasomal degradation of IRF-1
    • Gao, B., et al. Inhibition of histone deacetylase activity suppresses IFN-gamma induction of tripartite motif 22 via CHIP-mediated proteasomal degradation of IRF-1. J. Immunol. 191 (2013), 464–471.
    • (2013) J. Immunol. , vol.191 , pp. 464-471
    • Gao, B.1
  • 62
    • 0344304443 scopus 로고    scopus 로고
    • Interferon-stimulated transcription and innate antiviral immunity require deacetylase activity and histone deacetylase 1
    • Nusinzon, I., Horvath, C.M., Interferon-stimulated transcription and innate antiviral immunity require deacetylase activity and histone deacetylase 1. Proc. Natl. Acad. Sci. U. S. A. 100 (2003), 14742–14747.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 14742-14747
    • Nusinzon, I.1    Horvath, C.M.2
  • 63
    • 84908265816 scopus 로고    scopus 로고
    • Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders
    • Falkenberg, K.J., Johnstone, R.W., Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders. Nat. Rev. Drug Discov. 13 (2014), 673–691.
    • (2014) Nat. Rev. Drug Discov. , vol.13 , pp. 673-691
    • Falkenberg, K.J.1    Johnstone, R.W.2
  • 64
    • 3142721913 scopus 로고    scopus 로고
    • Requirement of histone deacetylase activity for signaling by STAT1
    • Klampfer, L., et al. Requirement of histone deacetylase activity for signaling by STAT1. J. Biol. Chem. 279 (2004), 30358–30368.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30358-30368
    • Klampfer, L.1
  • 65
    • 4644366536 scopus 로고    scopus 로고
    • Histone deacetylase activity is required to recruit RNA polymerase II to the promoters of selected interferon-stimulated early response genes
    • Sakamoto, S., et al. Histone deacetylase activity is required to recruit RNA polymerase II to the promoters of selected interferon-stimulated early response genes. J. Biol. Chem. 279 (2004), 40362–40367.
    • (2004) J. Biol. Chem. , vol.279 , pp. 40362-40367
    • Sakamoto, S.1
  • 66
    • 84867688629 scopus 로고    scopus 로고
    • A FOXO3-IRF7 gene regulatory circuit limits inflammatory sequelae of antiviral responses
    • Litvak, V., et al. A FOXO3-IRF7 gene regulatory circuit limits inflammatory sequelae of antiviral responses. Nature 490 (2012), 421–425.
    • (2012) Nature , vol.490 , pp. 421-425
    • Litvak, V.1
  • 67
    • 0032401780 scopus 로고    scopus 로고
    • Ser727-dependent recruitment of MCM5 by Stat1alpha in IFN-gamma-induced transcriptional activation
    • Zhang, J.J., et al. Ser727-dependent recruitment of MCM5 by Stat1alpha in IFN-gamma-induced transcriptional activation. EMBO J. 17 (1998), 6963–6971.
    • (1998) EMBO J. , vol.17 , pp. 6963-6971
    • Zhang, J.J.1
  • 68
    • 0035853152 scopus 로고    scopus 로고
    • Identification of two residues in MCM5 critical for the assembly of MCM complexes and Stat1-mediated transcription activation in response to IFN-gamma
    • DaFonseca, C.J., et al. Identification of two residues in MCM5 critical for the assembly of MCM complexes and Stat1-mediated transcription activation in response to IFN-gamma. Proc. Natl. Acad. Sci. U. S. A. 98 (2001), 3034–3039.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 3034-3039
    • DaFonseca, C.J.1
  • 69
    • 0033534562 scopus 로고    scopus 로고
    • Functional association of Nmi with Stat5 and Stat1 in IL-2- and IFNgamma-mediated signaling
    • Zhu, M., et al. Functional association of Nmi with Stat5 and Stat1 in IL-2- and IFNgamma-mediated signaling. Cell 96 (1999), 121–130.
    • (1999) Cell , vol.96 , pp. 121-130
    • Zhu, M.1
  • 70
    • 0037222791 scopus 로고    scopus 로고
    • Role of metazoan mediator proteins in interferon-responsive transcription
    • Lau, J.F., et al. Role of metazoan mediator proteins in interferon-responsive transcription. Mol. Cell. Biol. 23 (2003), 620–628.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 620-628
    • Lau, J.F.1
  • 71
    • 84903977631 scopus 로고    scopus 로고
    • Silencing of IFN-stimulated gene transcription is regulated by histone H1 and its chaperone TAF-I
    • Kadota, S., Nagata, K., Silencing of IFN-stimulated gene transcription is regulated by histone H1 and its chaperone TAF-I. Nucleic Acids Res. 42 (2014), 7642–7653.
    • (2014) Nucleic Acids Res. , vol.42 , pp. 7642-7653
    • Kadota, S.1    Nagata, K.2
  • 72
    • 34547423214 scopus 로고    scopus 로고
    • Control of specificity and magnitude of NF-kappa B and STAT1-mediated gene activation through PIASy and PIAS1 cooperation
    • Tahk, S., et al. Control of specificity and magnitude of NF-kappa B and STAT1-mediated gene activation through PIASy and PIAS1 cooperation. Proc. Natl. Acad. Sci. U. S. A. 104 (2007), 11643–11648.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 11643-11648
    • Tahk, S.1
  • 73
    • 0035853098 scopus 로고    scopus 로고
    • A transcriptional corepressor of Stat1 with an essential LXXLL signature motif
    • Liu, B., et al. A transcriptional corepressor of Stat1 with an essential LXXLL signature motif. Proc. Natl. Acad. Sci. U. S. A. 98 (2001), 3203–3207.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 3203-3207
    • Liu, B.1
  • 74
    • 84955599188 scopus 로고    scopus 로고
    • Parsing the interferon transcriptional network and its disease associations
    • Mostafavi, S., et al. Parsing the interferon transcriptional network and its disease associations. Cell 164 (2016), 564–578.
    • (2016) Cell , vol.164 , pp. 564-578
    • Mostafavi, S.1
  • 75
    • 79251542671 scopus 로고    scopus 로고
    • A novel role for IFN-stimulated gene factor 3II in IFN-gamma signaling and induction of antiviral activity in human cells
    • Morrow, A.N., et al. A novel role for IFN-stimulated gene factor 3II in IFN-gamma signaling and induction of antiviral activity in human cells. J. Immunol. 186 (2011), 1685–1693.
    • (2011) J. Immunol. , vol.186 , pp. 1685-1693
    • Morrow, A.N.1
  • 76
    • 84903904112 scopus 로고    scopus 로고
    • STAT2 and IRF9: beyond ISGF3
    • Fink, K., Grandvaux, N., STAT2 and IRF9: beyond ISGF3. JAKSTAT, 2, 2013, e27521.
    • (2013) JAKSTAT , vol.2 , pp. e27521
    • Fink, K.1    Grandvaux, N.2
  • 77
    • 84885869823 scopus 로고    scopus 로고
    • IFNbeta-dependent increases in STAT1, STAT2, and IRF9 mediate resistance to viruses and DNA damage
    • Cheon, H., et al. IFNbeta-dependent increases in STAT1, STAT2, and IRF9 mediate resistance to viruses and DNA damage. EMBO J. 32 (2013), 2751–2763.
    • (2013) EMBO J. , vol.32 , pp. 2751-2763
    • Cheon, H.1
  • 78
    • 84939823954 scopus 로고    scopus 로고
    • Roles of unphosphorylated ISGF3 in HCV infection and interferon responsiveness
    • Sung, P.S., et al. Roles of unphosphorylated ISGF3 in HCV infection and interferon responsiveness. Proc. Natl. Acad. Sci. U. S. A. 112 (2015), 10443–10448.
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , pp. 10443-10448
    • Sung, P.S.1
  • 79
    • 0033534450 scopus 로고    scopus 로고
    • Activation of a CrkL–stat5 signaling complex by type I interferons
    • Fish, E.N., et al. Activation of a CrkL–stat5 signaling complex by type I interferons. J. Biol. Chem. 274 (1999), 571–573.
    • (1999) J. Biol. Chem. , vol.274 , pp. 571-573
    • Fish, E.N.1
  • 80
    • 84990843545 scopus 로고    scopus 로고
    • IFN regulatory factor 1 restricts hepatitis E virus replication by activating STAT1 to induce antiviral IFN-stimulated genes
    • Xu, L., et al. IFN regulatory factor 1 restricts hepatitis E virus replication by activating STAT1 to induce antiviral IFN-stimulated genes. FASEB J. 30 (2016), 3352–3367.
    • (2016) FASEB J. , vol.30 , pp. 3352-3367
    • Xu, L.1
  • 81
    • 0028032114 scopus 로고
    • Structure and regulation of the human interferon regulatory factor 1 (IRF-1) and IRF-2 genes: implications for a gene network in the interferon system
    • Harada, H., et al. Structure and regulation of the human interferon regulatory factor 1 (IRF-1) and IRF-2 genes: implications for a gene network in the interferon system. Mol. Cell. Biol. 14 (1994), 1500–1509.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1500-1509
    • Harada, H.1
  • 82
    • 84893075305 scopus 로고    scopus 로고
    • Regulation of type I interferon responses
    • Ivashkiv, L.B., Donlin, L.T., Regulation of type I interferon responses. Nat. Rev. Immunol. 14 (2014), 36–49.
    • (2014) Nat. Rev. Immunol. , vol.14 , pp. 36-49
    • Ivashkiv, L.B.1    Donlin, L.T.2
  • 83
    • 0036092049 scopus 로고    scopus 로고
    • Transcriptional profiling of interferon regulatory factor 3 target genes: direct involvement in the regulation of interferon-stimulated genes
    • Grandvaux, N., et al. Transcriptional profiling of interferon regulatory factor 3 target genes: direct involvement in the regulation of interferon-stimulated genes. J. Virol. 76 (2002), 5532–5539.
    • (2002) J. Virol. , vol.76 , pp. 5532-5539
    • Grandvaux, N.1
  • 84
    • 0842304532 scopus 로고    scopus 로고
    • Innate cellular response to virus particle entry requires IRF3 but not virus replication
    • Collins, S.E., et al. Innate cellular response to virus particle entry requires IRF3 but not virus replication. J. Virol. 78 (2004), 1706–1717.
    • (2004) J. Virol. , vol.78 , pp. 1706-1717
    • Collins, S.E.1
  • 85
    • 58149487691 scopus 로고    scopus 로고
    • The addition of tumor necrosis factor plus beta interferon induces a novel synergistic antiviral state against poxviruses in primary human fibroblasts
    • Bartee, E., et al. The addition of tumor necrosis factor plus beta interferon induces a novel synergistic antiviral state against poxviruses in primary human fibroblasts. J. Virol. 83 (2009), 498–511.
    • (2009) J. Virol. , vol.83 , pp. 498-511
    • Bartee, E.1
  • 86
    • 84966800365 scopus 로고    scopus 로고
    • Convergent transcription of interferon-stimulated genes by TNF-alpha and IFN-alpha augments antiviral activity against HCV and HEV
    • Wang, W., et al. Convergent transcription of interferon-stimulated genes by TNF-alpha and IFN-alpha augments antiviral activity against HCV and HEV. Sci. Rep., 6, 2016, 25482.
    • (2016) Sci. Rep. , vol.6 , pp. 25482
    • Wang, W.1
  • 87
    • 0024208751 scopus 로고
    • Antiviral activity of tumour necrosis factor. Synergism with interferons and induction of oligo-2′,5′-adenylate synthetase
    • Mestan, J., et al. Antiviral activity of tumour necrosis factor. Synergism with interferons and induction of oligo-2′,5′-adenylate synthetase. J. Gen. Virol. 69 (1988), 3113–3120.
    • (1988) J. Gen. Virol. , vol.69 , pp. 3113-3120
    • Mestan, J.1
  • 88
    • 84930320909 scopus 로고    scopus 로고
    • TNF-alpha induced by hepatitis C virus via TLR7 and TLR8 in hepatocytes supports interferon signaling via an autocrine mechanism
    • Lee, J., et al. TNF-alpha induced by hepatitis C virus via TLR7 and TLR8 in hepatocytes supports interferon signaling via an autocrine mechanism. PLoS Pathog., 11, 2015, e1004937.
    • (2015) PLoS Pathog. , vol.11 , pp. e1004937
    • Lee, J.1
  • 89
    • 0030722084 scopus 로고    scopus 로고
    • Antiviral activity of tumor necrosis factor (TNF) is mediated via p55 and p75 TNF receptors
    • Ruby, J., et al. Antiviral activity of tumor necrosis factor (TNF) is mediated via p55 and p75 TNF receptors. J. Exp. Med. 186 (1997), 1591–1596.
    • (1997) J. Exp. Med. , vol.186 , pp. 1591-1596
    • Ruby, J.1
  • 90
    • 0036147470 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha exerts powerful anti-influenza virus effects in lung epithelial cells
    • Seo, S.H., Webster, R.G., Tumor necrosis factor alpha exerts powerful anti-influenza virus effects in lung epithelial cells. J. Virol. 76 (2002), 1071–1076.
    • (2002) J. Virol. , vol.76 , pp. 1071-1076
    • Seo, S.H.1    Webster, R.G.2
  • 91
    • 0023035026 scopus 로고
    • Antiviral effects of recombinant tumour necrosis factor in vitro
    • Mestan, J., et al. Antiviral effects of recombinant tumour necrosis factor in vitro. Nature 323 (1986), 816–819.
    • (1986) Nature , vol.323 , pp. 816-819
    • Mestan, J.1
  • 92
    • 0034623132 scopus 로고    scopus 로고
    • The Rac1/p38 mitogen-activated protein kinase pathway is required for interferon alpha-dependent transcriptional activation but not serine phosphorylation of Stat proteins
    • Uddin, S., et al. The Rac1/p38 mitogen-activated protein kinase pathway is required for interferon alpha-dependent transcriptional activation but not serine phosphorylation of Stat proteins. J. Biol. Chem. 275 (2000), 27634–27640.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27634-27640
    • Uddin, S.1
  • 93
    • 15444367336 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinase kinase (MKK) 3 and MKK6 by type I interferons
    • Li, Y., et al. Activation of mitogen-activated protein kinase kinase (MKK) 3 and MKK6 by type I interferons. J. Biol. Chem. 280 (2005), 10001–10010.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10001-10010
    • Li, Y.1
  • 94
    • 0028177001 scopus 로고
    • Interferon-gamma induces the synthesis and activation of cytosolic phospholipase A2
    • Wu, T., et al. Interferon-gamma induces the synthesis and activation of cytosolic phospholipase A2. J. Clin. Invest. 93 (1994), 571–577.
    • (1994) J. Clin. Invest. , vol.93 , pp. 571-577
    • Wu, T.1
  • 95
    • 0029063584 scopus 로고
    • Rac mediates growth factor-induced arachidonic acid release
    • Peppelenbosch, M.P., Rac mediates growth factor-induced arachidonic acid release. Cell 81 (1995), 849–856.
    • (1995) Cell , vol.81 , pp. 849-856
    • Peppelenbosch, M.P.1
  • 96
    • 84887890762 scopus 로고    scopus 로고
    • Perspective on the discovery and scientific impact of p38 MAP kinase
    • Young, P.R., Perspective on the discovery and scientific impact of p38 MAP kinase. J. Biomol. Screen. 18 (2013), 1156–1163.
    • (2013) J. Biomol. Screen. , vol.18 , pp. 1156-1163
    • Young, P.R.1
  • 97
    • 0347723965 scopus 로고    scopus 로고
    • Role of p38alpha Map kinase in type I interferon signaling
    • Li, Y., et al. Role of p38alpha Map kinase in type I interferon signaling. J. Biol. Chem. 279 (2004), 970–979.
    • (2004) J. Biol. Chem. , vol.279 , pp. 970-979
    • Li, Y.1
  • 98
    • 0033569766 scopus 로고    scopus 로고
    • Activation of the p38 mitogen-activated protein kinase by type I interferons
    • Uddin, S., et al. Activation of the p38 mitogen-activated protein kinase by type I interferons. J. Biol. Chem. 274 (1999), 30127–30131.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30127-30131
    • Uddin, S.1
  • 99
    • 0033911179 scopus 로고    scopus 로고
    • p38 map kinase regulates TNF-alpha production in human astrocytes and microglia by multiple mechanisms
    • Lee, Y.B., et al. p38 map kinase regulates TNF-alpha production in human astrocytes and microglia by multiple mechanisms. Cytokine 12 (2000), 874–880.
    • (2000) Cytokine , vol.12 , pp. 874-880
    • Lee, Y.B.1
  • 100
    • 0035808316 scopus 로고    scopus 로고
    • ERK1 and ERK2 activate CCAAAT/enhancer-binding protein-beta-dependent gene transcription in response to interferon-gamma
    • Hu, J., et al. ERK1 and ERK2 activate CCAAAT/enhancer-binding protein-beta-dependent gene transcription in response to interferon-gamma. J. Biol. Chem. 276 (2001), 287–297.
    • (2001) J. Biol. Chem. , vol.276 , pp. 287-297
    • Hu, J.1
  • 101
    • 84887297004 scopus 로고    scopus 로고
    • Inhibition of pyrimidine biosynthesis pathway suppresses viral growth through innate immunity
    • Lucas-Hourani, M., Inhibition of pyrimidine biosynthesis pathway suppresses viral growth through innate immunity. PLoS Pathog., 9, 2013, e1003678.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003678
    • Lucas-Hourani, M.1
  • 102
    • 84861578651 scopus 로고    scopus 로고
    • Mycophenolic acid augments interferon-stimulated gene expression and inhibits hepatitis C virus infection in vitro and in vivo
    • Pan, Q., et al. Mycophenolic acid augments interferon-stimulated gene expression and inhibits hepatitis C virus infection in vitro and in vivo. Hepatology 55 (2012), 1673–1683.
    • (2012) Hepatology , vol.55 , pp. 1673-1683
    • Pan, Q.1
  • 103
    • 84979582494 scopus 로고    scopus 로고
    • Discovery of a broad-spectrum antiviral compound that inhibits pyrimidine biosynthesis and establishes a type 1 interferon-independent antiviral state
    • Chung, D.H., et al. Discovery of a broad-spectrum antiviral compound that inhibits pyrimidine biosynthesis and establishes a type 1 interferon-independent antiviral state. Antimicrob. Agents Chemother. 60 (2016), 4552–4562.
    • (2016) Antimicrob. Agents Chemother. , vol.60 , pp. 4552-4562
    • Chung, D.H.1
  • 104
    • 84964978281 scopus 로고    scopus 로고
    • Cross talk between nucleotide synthesis pathways with cellular immunity in constraining hepatitis E virus replication
    • Wang, Y., et al. Cross talk between nucleotide synthesis pathways with cellular immunity in constraining hepatitis E virus replication. Antimicrob. Agents Chemother. 60 (2016), 2834–2848.
    • (2016) Antimicrob. Agents Chemother. , vol.60 , pp. 2834-2848
    • Wang, Y.1
  • 105
    • 84932625135 scopus 로고    scopus 로고
    • Ribavirin restores IFNalpha responsiveness in HCV-infected livers by epigenetic remodelling at interferon stimulated genes
    • Testoni, B., et al. Ribavirin restores IFNalpha responsiveness in HCV-infected livers by epigenetic remodelling at interferon stimulated genes. Gut 65 (2016), 672–682.
    • (2016) Gut , vol.65 , pp. 672-682
    • Testoni, B.1
  • 106
    • 0029037420 scopus 로고
    • Safety and pharmacokinetics of vitamin A therapy for infants with respiratory syncytial virus infections
    • Neuzil, K.M., et al. Safety and pharmacokinetics of vitamin A therapy for infants with respiratory syncytial virus infections. Antimicrob. Agents Chemother. 39 (1995), 1191–1193.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1191-1193
    • Neuzil, K.M.1
  • 107
    • 39549107777 scopus 로고    scopus 로고
    • All-trans retinoic acid for treatment of chronic hepatitis C
    • Bocher, W.O., et al. All-trans retinoic acid for treatment of chronic hepatitis C. Liver Int. 28 (2008), 347–354.
    • (2008) Liver Int. , vol.28 , pp. 347-354
    • Bocher, W.O.1
  • 108
    • 84978229814 scopus 로고    scopus 로고
    • Retinoid regulation of antiviral innate immunity in hepatocytes
    • Cho, N.E., et al. Retinoid regulation of antiviral innate immunity in hepatocytes. Hepatology 63 (2016), 1783–1795.
    • (2016) Hepatology , vol.63 , pp. 1783-1795
    • Cho, N.E.1
  • 109
    • 85042249412 scopus 로고    scopus 로고
    • Vitamin A deficiency is associated with hepatitis C virus chronic infection and with unresponsiveness to interferon-based antiviral therapy
    • Bitetto, D., et al. Vitamin A deficiency is associated with hepatitis C virus chronic infection and with unresponsiveness to interferon-based antiviral therapy. Hepatology 57 (2013), 925–933.
    • (2013) Hepatology , vol.57 , pp. 925-933
    • Bitetto, D.1
  • 110
    • 84892429717 scopus 로고    scopus 로고
    • Antiviral strategies for hepatitis E virus
    • Debing, Y., Neyts, J., Antiviral strategies for hepatitis E virus. Antiviral Res. 102 (2014), 106–118.
    • (2014) Antiviral Res. , vol.102 , pp. 106-118
    • Debing, Y.1    Neyts, J.2
  • 111
    • 0348136783 scopus 로고    scopus 로고
    • Interferon alfacon-1 plus corticosteroids in severe acute respiratory syndrome: a preliminary study
    • Loutfy, M.R., et al. Interferon alfacon-1 plus corticosteroids in severe acute respiratory syndrome: a preliminary study. JAMA 290 (2003), 3222–3228.
    • (2003) JAMA , vol.290 , pp. 3222-3228
    • Loutfy, M.R.1
  • 112
    • 84960262412 scopus 로고    scopus 로고
    • IFN-lambda therapy: current status and future perspectives
    • Lasfar, A., et al. IFN-lambda therapy: current status and future perspectives. Drug Discov. Today 21 (2016), 167–171.
    • (2016) Drug Discov. Today , vol.21 , pp. 167-171
    • Lasfar, A.1
  • 113
    • 73849120349 scopus 로고    scopus 로고
    • Clinical use of interferon-gamma
    • Miller, C.H., et al. Clinical use of interferon-gamma. Ann. N. Y. Acad. Sci. 1182 (2009), 69–79.
    • (2009) Ann. N. Y. Acad. Sci. , vol.1182 , pp. 69-79
    • Miller, C.H.1
  • 114
    • 0025916176 scopus 로고
    • A randomised controlled trial of recombinant interferon-gamma in Chinese patients with chronic hepatitis B virus infection
    • Lau, J.Y., et al. A randomised controlled trial of recombinant interferon-gamma in Chinese patients with chronic hepatitis B virus infection. J. Med. Virol. 34 (1991), 184–187.
    • (1991) J. Med. Virol. , vol.34 , pp. 184-187
    • Lau, J.Y.1
  • 115
    • 33646011268 scopus 로고    scopus 로고
    • Interferon gamma-1b for the treatment of fibrosis in chronic hepatitis C infection
    • Muir, A.J., et al. Interferon gamma-1b for the treatment of fibrosis in chronic hepatitis C infection. J. Viral. Hepat. 13 (2006), 322–328.
    • (2006) J. Viral. Hepat. , vol.13 , pp. 322-328
    • Muir, A.J.1
  • 116
    • 84984590312 scopus 로고    scopus 로고
    • Peginterferon lambda for the treatment of HBeAg-positive chronic hepatitis B: a randomized phase 2b study (LIRA-B)
    • Chan, H.L., et al. Peginterferon lambda for the treatment of HBeAg-positive chronic hepatitis B: a randomized phase 2b study (LIRA-B). J. Hepatol. 64 (2016), 1011–1019.
    • (2016) J. Hepatol. , vol.64 , pp. 1011-1019
    • Chan, H.L.1
  • 117
    • 84922813934 scopus 로고    scopus 로고
    • A randomized phase 2b study of peginterferon lambda-1a for the treatment of chronic HCV infection
    • Muir, A.J., et al. A randomized phase 2b study of peginterferon lambda-1a for the treatment of chronic HCV infection. J. Hepatol. 61 (2014), 1238–1246.
    • (2014) J. Hepatol. , vol.61 , pp. 1238-1246
    • Muir, A.J.1
  • 118
    • 84931569282 scopus 로고    scopus 로고
    • Interferon-lambda and interleukin 22 act synergistically for the induction of interferon-stimulated genes and control of rotavirus infection
    • Hernandez, P.P., et al. Interferon-lambda and interleukin 22 act synergistically for the induction of interferon-stimulated genes and control of rotavirus infection. Nat. Immunol. 16 (2015), 698–707.
    • (2015) Nat. Immunol. , vol.16 , pp. 698-707
    • Hernandez, P.P.1
  • 119
    • 79956353201 scopus 로고    scopus 로고
    • IFN-lambda determines the intestinal epithelial antiviral host defense
    • Pott, J., et al. IFN-lambda determines the intestinal epithelial antiviral host defense. Proc. Natl. Acad. Sci. U. S. A. 108 (2011), 7944–7949.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 7944-7949
    • Pott, J.1
  • 120
    • 79955542915 scopus 로고    scopus 로고
    • A diverse range of gene products are effectors of the type I interferon antiviral response
    • Schoggins, J.W., et al. A diverse range of gene products are effectors of the type I interferon antiviral response. Nature 472 (2011), 481–485.
    • (2011) Nature , vol.472 , pp. 481-485
    • Schoggins, J.W.1
  • 121
    • 41149156316 scopus 로고    scopus 로고
    • Liver gene expression signature to predict response to pegylated interferon plus ribavirin combination therapy in patients with chronic hepatitis C
    • Asselah, T., et al. Liver gene expression signature to predict response to pegylated interferon plus ribavirin combination therapy in patients with chronic hepatitis C. Gut 57 (2008), 516–524.
    • (2008) Gut , vol.57 , pp. 516-524
    • Asselah, T.1
  • 122
    • 84865460821 scopus 로고    scopus 로고
    • Interferon-gamma-stimulated genes, but not USP18, are expressed in livers of patients with acute hepatitis C
    • Dill, M.T., et al. Interferon-gamma-stimulated genes, but not USP18, are expressed in livers of patients with acute hepatitis C. Gastroenterology 143 (2012), 777–786.
    • (2012) Gastroenterology , vol.143 , pp. 777-786
    • Dill, M.T.1
  • 123
    • 84933279572 scopus 로고    scopus 로고
    • Aicardi-Goutières syndrome and the type I interferonopathies
    • Crow, Y.J., Manel, N., Aicardi-Goutières syndrome and the type I interferonopathies. Nat. Rev. Immunol. 15 (2015), 429–440.
    • (2015) Nat. Rev. Immunol. , vol.15 , pp. 429-440
    • Crow, Y.J.1    Manel, N.2
  • 124
    • 0037451167 scopus 로고    scopus 로고
    • Interferon and granulopoiesis signatures in systemic lupus erythematosus blood
    • Bennett, L., et al. Interferon and granulopoiesis signatures in systemic lupus erythematosus blood. J. Exp. Med. 197 (2003), 711–723.
    • (2003) J. Exp. Med. , vol.197 , pp. 711-723
    • Bennett, L.1
  • 125
    • 53549103852 scopus 로고    scopus 로고
    • Divergent TLR7 and TLR9 signaling and type I interferon production distinguish pathogenic and nonpathogenic AIDS virus infections
    • Mandl, J.N., et al. Divergent TLR7 and TLR9 signaling and type I interferon production distinguish pathogenic and nonpathogenic AIDS virus infections. Nat. Med. 14 (2008), 1077–1087.
    • (2008) Nat. Med. , vol.14 , pp. 1077-1087
    • Mandl, J.N.1
  • 126
    • 84930210177 scopus 로고    scopus 로고
    • Pattern recognition receptors as potential therapeutic targets in inflammatory rheumatic disease
    • Mullen, L.M., et al. Pattern recognition receptors as potential therapeutic targets in inflammatory rheumatic disease. Arthritis Res. Ther., 17, 2015, 122.
    • (2015) Arthritis Res. Ther. , vol.17 , pp. 122
    • Mullen, L.M.1
  • 127
    • 0029671421 scopus 로고    scopus 로고
    • Identification of an interferon-gamma receptor alpha chain sequence required for JAK-1 binding
    • Kaplan, D.H., et al. Identification of an interferon-gamma receptor alpha chain sequence required for JAK-1 binding. J. Biol. Chem. 271 (1996), 9–12.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9-12
    • Kaplan, D.H.1
  • 128
    • 12444347845 scopus 로고    scopus 로고
    • Role of tyrosine 441 of interferon-gamma receptor subunit 1 in SOCS-1-mediated attenuation of STAT1 activation
    • Qing, Y., et al. Role of tyrosine 441 of interferon-gamma receptor subunit 1 in SOCS-1-mediated attenuation of STAT1 activation. J. Biol. Chem. 280 (2005), 1849–1853.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1849-1853
    • Qing, Y.1
  • 129
    • 48249138503 scopus 로고    scopus 로고
    • Recruitment of Stat1 to chromatin is required for interferon-induced serine phosphorylation of Stat1 transactivation domain
    • Sadzak, I., et al. Recruitment of Stat1 to chromatin is required for interferon-induced serine phosphorylation of Stat1 transactivation domain. Proc. Natl. Acad. Sci. U. S. A. 105 (2008), 8944–8949.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 8944-8949
    • Sadzak, I.1


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