메뉴 건너뛰기




Volumn 27, Issue 2, 2015, Pages 85-101

Early IFN type I response: Larning from microbial evasion strategies

Author keywords

Bacteria; Evasion mechanism; IFN stimulated genes; Interferon; Signaling; Virus

Indexed keywords

INDUCIBLE NITRIC OXIDE SYNTHASE; INTERFERON; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PROTEIN KINASE R; UBIQUITIN;

EID: 84931570382     PISSN: 10445323     EISSN: 10963618     Source Type: Journal    
DOI: 10.1016/j.smim.2015.03.005     Document Type: Review
Times cited : (43)

References (260)
  • 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. 2014, 32:461-488.
    • (2014) Annu. Rev. Immunol. , vol.32 , pp. 461-488
    • Wu, J.1    Chen, Z.J.2
  • 2
    • 84859405717 scopus 로고    scopus 로고
    • Signaling by myeloid C-type lectin receptors in immunity and homeostasis
    • Sancho D., Reis e Sousa C. Signaling by myeloid C-type lectin receptors in immunity and homeostasis. Annu. Rev. Immunol. 2012, 30:491-529.
    • (2012) Annu. Rev. Immunol. , vol.30 , pp. 491-529
    • Sancho, D.1    Reis e Sousa, C.2
  • 3
    • 84878190840 scopus 로고    scopus 로고
    • Immune sensing of DNA
    • Paludan S.R., Bowie A.G. Immune sensing of DNA. Immunity 2013, 38:870-880.
    • (2013) Immunity , vol.38 , pp. 870-880
    • Paludan, S.R.1    Bowie, A.G.2
  • 4
    • 77949940198 scopus 로고    scopus 로고
    • Intracellular toll-like receptors
    • Blasius A.L., Beutler B. Intracellular toll-like receptors. Immunity 2010, 32:305-315.
    • (2010) Immunity , vol.32 , pp. 305-315
    • Blasius, A.L.1    Beutler, B.2
  • 6
    • 84884138508 scopus 로고    scopus 로고
    • The interferon response to intracellular DNA: why so many receptors?
    • Unterholzner L. The interferon response to intracellular DNA: why so many receptors?. Immunobiology 2013, 218:1312-1321.
    • (2013) Immunobiology , vol.218 , pp. 1312-1321
    • Unterholzner, L.1
  • 8
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira S., Uematsu S., Takeuchi O. Pathogen recognition and innate immunity. Cell 2006, 124:783-801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 9
    • 33748051738 scopus 로고    scopus 로고
    • IRFs: master regulators of signalling by Toll-like receptors and cytosolic pattern-recognition receptors
    • Honda K., Taniguchi T. IRFs: master regulators of signalling by Toll-like receptors and cytosolic pattern-recognition receptors. Nat. Rev. Immunol. 2006, 6:644-658.
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 644-658
    • Honda, K.1    Taniguchi, T.2
  • 10
    • 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. 2014, 14:36-49.
    • (2014) Nat. Rev. Immunol. , vol.14 , pp. 36-49
    • Ivashkiv, L.B.1    Donlin, L.T.2
  • 11
    • 84896987305 scopus 로고    scopus 로고
    • Interferon-stimulated genes: a complex web of host defenses
    • Schneider W.M., Chevillotte M.D., Rice C.M. Interferon-stimulated genes: a complex web of host defenses. Annu. Rev. Immunol. 2014, 32:513-545.
    • (2014) Annu. Rev. Immunol. , vol.32 , pp. 513-545
    • Schneider, W.M.1    Chevillotte, M.D.2    Rice, C.M.3
  • 12
    • 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. 2005, 5:375-386.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 375-386
    • Platanias, L.C.1
  • 13
    • 84906850729 scopus 로고    scopus 로고
    • Type I and III interferon production in response to RNA viruses
    • Reid E., Charleston B. Type I and III interferon production in response to RNA viruses. J. Interferon Cytokine Res. 2014, 34:649-658.
    • (2014) J. Interferon Cytokine Res. , vol.34 , pp. 649-658
    • Reid, E.1    Charleston, B.2
  • 15
    • 84859992161 scopus 로고    scopus 로고
    • The JAK-STAT pathway at twenty
    • Stark G.R., Darnell J.E. The JAK-STAT pathway at twenty. Immunity 2012, 36:503-514.
    • (2012) Immunity , vol.36 , pp. 503-514
    • Stark, G.R.1    Darnell, J.E.2
  • 16
    • 33748455338 scopus 로고    scopus 로고
    • Type I interferons in host defense
    • Stetson D.B., Medzhitov R. Type I interferons in host defense. Immunity 2006, 25:373-381.
    • (2006) Immunity , vol.25 , pp. 373-381
    • Stetson, D.B.1    Medzhitov, R.2
  • 17
    • 38849154155 scopus 로고    scopus 로고
    • IFN regulation and functions in myeloid dendritic cells
    • Coccia E.M. IFN regulation and functions in myeloid dendritic cells. Cytokine Growth Factor Rev. 2008, 19:21-32.
    • (2008) Cytokine Growth Factor Rev. , vol.19 , pp. 21-32
    • Coccia, E.M.1
  • 18
    • 84888799401 scopus 로고    scopus 로고
    • Confounding roles for type I interferons during bacterial and viral pathogenesis
    • Carrero J.A. Confounding roles for type I interferons during bacterial and viral pathogenesis. Int. Immunol. 2013, 25:663-669.
    • (2013) Int. Immunol. , vol.25 , pp. 663-669
    • Carrero, J.A.1
  • 19
    • 84899134307 scopus 로고    scopus 로고
    • Bacteria fighting back: how pathogens target and subvert the host innate immune system
    • Reddick L.E., Alto N.M. Bacteria fighting back: how pathogens target and subvert the host innate immune system. Mol. Cell 2014, 54:321-328.
    • (2014) Mol. Cell , vol.54 , pp. 321-328
    • Reddick, L.E.1    Alto, N.M.2
  • 20
    • 32944462309 scopus 로고    scopus 로고
    • Anti-immunology: evasion of the host immune system by bacterial and viral pathogens
    • Finlay B.B., McFadden G. Anti-immunology: evasion of the host immune system by bacterial and viral pathogens. Cell 2006, 124:767-782.
    • (2006) Cell , vol.124 , pp. 767-782
    • Finlay, B.B.1    McFadden, G.2
  • 21
    • 84877610008 scopus 로고    scopus 로고
    • Bacterial subversion of host innate immune pathways
    • Baxt L.A., Garza-Mayers A.C., Goldberg M.B. Bacterial subversion of host innate immune pathways. Science 2013, 340:697-701.
    • (2013) Science , vol.340 , pp. 697-701
    • Baxt, L.A.1    Garza-Mayers, A.C.2    Goldberg, M.B.3
  • 22
    • 11144240264 scopus 로고    scopus 로고
    • Inverse interference: how viruses fight the interferon system
    • Weber F., Kochs G., Haller O. Inverse interference: how viruses fight the interferon system. Viral Immunol. 2004, 17:498-515.
    • (2004) Viral Immunol. , vol.17 , pp. 498-515
    • Weber, F.1    Kochs, G.2    Haller, O.3
  • 23
    • 77955413296 scopus 로고    scopus 로고
    • Viral tricks to grid-lock the type I interferon system
    • Versteeg G.A., Garcia-Sastre A. Viral tricks to grid-lock the type I interferon system. Curr. Opin. Microbiol. 2010, 13:508-516.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 508-516
    • Versteeg, G.A.1    Garcia-Sastre, A.2
  • 24
    • 56749133272 scopus 로고    scopus 로고
    • Viral evasion and subversion of pattern-recognition receptor signalling
    • Bowie A.G., Unterholzner L. Viral evasion and subversion of pattern-recognition receptor signalling. Nat. Rev. Immunol. 2008, 8:911-922.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 911-922
    • Bowie, A.G.1    Unterholzner, L.2
  • 25
    • 84907515304 scopus 로고    scopus 로고
    • Cellular sensing of viral DNA and viral evasion mechanisms
    • Orzalli M.H., Knipe D.M. Cellular sensing of viral DNA and viral evasion mechanisms. Annu. Rev. Microbiol. 2014, 68:477-492.
    • (2014) Annu. Rev. Microbiol. , vol.68 , pp. 477-492
    • Orzalli, M.H.1    Knipe, D.M.2
  • 26
    • 84921463388 scopus 로고    scopus 로고
    • Microbial strategies for antagonizing Toll-like-receptor signal transduction
    • Rosadini C.V., Kagan J.C. Microbial strategies for antagonizing Toll-like-receptor signal transduction. Curr. Opin. Immunol. 2015, 32C:61-70.
    • (2015) Curr. Opin. Immunol. , vol.32C , pp. 61-70
    • Rosadini, C.V.1    Kagan, J.C.2
  • 27
    • 79956300649 scopus 로고    scopus 로고
    • Toll-like receptors and their crosstalk with other innate receptors in infection and immunity
    • Kawai T., Akira S. Toll-like receptors and their crosstalk with other innate receptors in infection and immunity. Immunity 2011, 34:637-650.
    • (2011) Immunity , vol.34 , pp. 637-650
    • Kawai, T.1    Akira, S.2
  • 28
    • 84872259257 scopus 로고    scopus 로고
    • A virological view of innate immune recognition
    • Iwasaki A. A virological view of innate immune recognition. Annu. Rev. Microbiol. 2012, 66:177-196.
    • (2012) Annu. Rev. Microbiol. , vol.66 , pp. 177-196
    • Iwasaki, A.1
  • 29
    • 84941755669 scopus 로고    scopus 로고
    • Microbial sensing by toll-like receptors and intracellular nucleic acid sensors
    • Pandey S., Kawai T., Akira S. Microbial sensing by toll-like receptors and intracellular nucleic acid sensors. Cold Spring Harb. Perspect. Biol. 2015, 7a016246.
    • (2015) Cold Spring Harb. Perspect. Biol. , pp. 7a016246
    • Pandey, S.1    Kawai, T.2    Akira, S.3
  • 30
    • 46949097299 scopus 로고    scopus 로고
    • Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5
    • Kato H., Takeuchi O., Mikamo-Satoh E., Hirai R., Kawai T., Matsushita K., et al. Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5. J. Exp. Med. 2008, 205:1601-1610.
    • (2008) J. Exp. Med. , vol.205 , pp. 1601-1610
    • Kato, H.1    Takeuchi, O.2    Mikamo-Satoh, E.3    Hirai, R.4    Kawai, T.5    Matsushita, K.6
  • 31
    • 33750984771 scopus 로고    scopus 로고
    • RIG-I-mediated antiviral responses to single-stranded RNA bearing 5'-phosphates
    • Pichlmair A., Schulz O., Tan C.P., Naslund T.I., Liljestrom P., Weber F., et al. RIG-I-mediated antiviral responses to single-stranded RNA bearing 5'-phosphates. Science 2006, 314:997-1001.
    • (2006) Science , vol.314 , pp. 997-1001
    • Pichlmair, A.1    Schulz, O.2    Tan, C.P.3    Naslund, T.I.4    Liljestrom, P.5    Weber, F.6
  • 33
    • 84868569570 scopus 로고    scopus 로고
    • RIG-I detects infection with live Listeria by sensing secreted bacterial nucleic acids
    • Abdullah Z., Schlee M., Roth S., Mraheil M.A., Barchet W., Bottcher J., et al. RIG-I detects infection with live Listeria by sensing secreted bacterial nucleic acids. EMBO J. 2012, 31:4153-4164.
    • (2012) EMBO J. , vol.31 , pp. 4153-4164
    • Abdullah, Z.1    Schlee, M.2    Roth, S.3    Mraheil, M.A.4    Barchet, W.5    Bottcher, J.6
  • 34
    • 80054810643 scopus 로고    scopus 로고
    • Mitochondrial antiviral signaling protein (MAVS) monitors commensal bacteria and induces an immune response that prevents experimental colitis
    • Li X.D., Chiu Y.H., Ismail A.S., Behrendt C.L., Wight-Carter M., Hooper L.V., et al. Mitochondrial antiviral signaling protein (MAVS) monitors commensal bacteria and induces an immune response that prevents experimental colitis. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:17390-17395.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 17390-17395
    • Li, X.D.1    Chiu, Y.H.2    Ismail, A.S.3    Behrendt, C.L.4    Wight-Carter, M.5    Hooper, L.V.6
  • 35
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB 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-kappaB and IRF 3. Cell 2005, 122:669-682.
    • (2005) Cell , vol.122 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.K.3    Chen, Z.J.4
  • 36
    • 53349178089 scopus 로고    scopus 로고
    • STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling
    • Ishikawa H., Barber G.N. STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling. Nature 2008, 455:674-678.
    • (2008) Nature , vol.455 , pp. 674-678
    • Ishikawa, H.1    Barber, G.N.2
  • 37
    • 53349168904 scopus 로고    scopus 로고
    • The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation
    • Zhong B., Yang Y., Li S., Wang Y.Y., Li Y., Diao F., et al. The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation. Immunity 2008, 29:538-550.
    • (2008) Immunity , vol.29 , pp. 538-550
    • Zhong, B.1    Yang, Y.2    Li, S.3    Wang, Y.Y.4    Li, Y.5    Diao, F.6
  • 38
    • 84918775897 scopus 로고    scopus 로고
    • MITA/STING: a central and multifaceted mediator in innate immune response
    • Ran Y., Shu H.B., Wang Y.Y. MITA/STING: a central and multifaceted mediator in innate immune response. Cytokine Growth Factor Rev. 2014, 25:631-639.
    • (2014) Cytokine Growth Factor Rev. , vol.25 , pp. 631-639
    • Ran, Y.1    Shu, H.B.2    Wang, Y.Y.3
  • 39
    • 84870623251 scopus 로고    scopus 로고
    • DsRNA-dependent protein kinase PKR and its role in stress, signaling and HCV infection
    • Dabo S., Meurs E.F. dsRNA-dependent protein kinase PKR and its role in stress, signaling and HCV infection. Viruses 2012, 4:2598-2635.
    • (2012) Viruses , vol.4 , pp. 2598-2635
    • Dabo, S.1    Meurs, E.F.2
  • 40
    • 84908309281 scopus 로고    scopus 로고
    • IFIT1: a dual sensor and effector molecule that detects non-2'-O methylated viral RNA and inhibits its translation
    • Diamond M.S. IFIT1: a dual sensor and effector molecule that detects non-2'-O methylated viral RNA and inhibits its translation. Cytokine Growth Factor Rev. 2014.
    • (2014) Cytokine Growth Factor Rev.
    • Diamond, M.S.1
  • 42
  • 43
    • 4344641279 scopus 로고    scopus 로고
    • Advancements in the battle against severe acute respiratory syndrome
    • Hui D.S., Wong G.W. Advancements in the battle against severe acute respiratory syndrome. Expert Opin. Pharmacother. 2004, 5:1687-1693.
    • (2004) Expert Opin. Pharmacother. , vol.5 , pp. 1687-1693
    • Hui, D.S.1    Wong, G.W.2
  • 44
    • 84878966726 scopus 로고    scopus 로고
    • Middle East respiratory syndrome coronavirus (MERS-CoV): announcement of the Coronavirus Study Group
    • de Groot R.J., Baker S.C., Baric R.S., Brown C.S., Drosten C., Enjuanes L., et al. Middle East respiratory syndrome coronavirus (MERS-CoV): announcement of the Coronavirus Study Group. J. Virol. 2013, 87:7790-7792.
    • (2013) J. Virol. , vol.87 , pp. 7790-7792
    • de Groot, R.J.1    Baker, S.C.2    Baric, R.S.3    Brown, C.S.4    Drosten, C.5    Enjuanes, L.6
  • 45
    • 84899122287 scopus 로고    scopus 로고
    • Coronaviruses: important emerging human pathogens
    • Coleman C.M., Frieman M.B. Coronaviruses: important emerging human pathogens. J. Virol. 2014, 88:5209-5212.
    • (2014) J. Virol. , vol.88 , pp. 5209-5212
    • Coleman, C.M.1    Frieman, M.B.2
  • 46
    • 84884515347 scopus 로고    scopus 로고
    • From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses
    • Hilgenfeld R., Peiris M. From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses. Antiviral Res. 2013, 100:286-295.
    • (2013) Antiviral Res. , vol.100 , pp. 286-295
    • Hilgenfeld, R.1    Peiris, M.2
  • 47
    • 84897578593 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome vs. the Middle East respiratory syndrome
    • Hui D.S., Memish Z.A., Zumla A. Severe acute respiratory syndrome vs. the Middle East respiratory syndrome. Curr. Opin. Pulm. Med. 2014, 20:233-241.
    • (2014) Curr. Opin. Pulm. Med. , vol.20 , pp. 233-241
    • Hui, D.S.1    Memish, Z.A.2    Zumla, A.3
  • 48
    • 84876310574 scopus 로고    scopus 로고
    • Human cell tropism and innate immune system interactions of human respiratory coronavirus EMC compared to those of severe acute respiratory syndrome coronavirus
    • Zielecki F., Weber M., Eickmann M., Spiegelberg L., Zaki A.M., Matrosovich M., et al. Human cell tropism and innate immune system interactions of human respiratory coronavirus EMC compared to those of severe acute respiratory syndrome coronavirus. J. Virol. 2013, 87:5300-5304.
    • (2013) J. Virol. , vol.87 , pp. 5300-5304
    • Zielecki, F.1    Weber, M.2    Eickmann, M.3    Spiegelberg, L.4    Zaki, A.M.5    Matrosovich, M.6
  • 49
    • 84874606884 scopus 로고    scopus 로고
    • Efficient replication of the novel human betacoronavirus EMC on primary human epithelium highlights its zoonotic potential
    • Kindler E., Jonsdottir H.R., Muth D., Hamming O.J., Hartmann R., Rodriguez R., et al. Efficient replication of the novel human betacoronavirus EMC on primary human epithelium highlights its zoonotic potential. MBio 2013, 4:e00611-e00612.
    • (2013) MBio , vol.4 , pp. e00611-e00612
    • Kindler, E.1    Jonsdottir, H.R.2    Muth, D.3    Hamming, O.J.4    Hartmann, R.5    Rodriguez, R.6
  • 50
    • 84901999946 scopus 로고    scopus 로고
    • To sense or not to sense viral RNA - essentials of coronavirus innate immune evasion
    • Kindler E., Thiel V. To sense or not to sense viral RNA - essentials of coronavirus innate immune evasion. Curr. Opin. Microbiol. 2014, 20:69-75.
    • (2014) Curr. Opin. Microbiol. , vol.20 , pp. 69-75
    • Kindler, E.1    Thiel, V.2
  • 51
    • 84862895252 scopus 로고    scopus 로고
    • SARS coronavirus pathogenesis: host innate immune responses and viral antagonism of interferon
    • Totura A.L., Baric R.S. SARS coronavirus pathogenesis: host innate immune responses and viral antagonism of interferon. Curr. Opin. Virol. 2012, 2:264-275.
    • (2012) Curr. Opin. Virol. , vol.2 , pp. 264-275
    • Totura, A.L.1    Baric, R.S.2
  • 52
    • 78751637122 scopus 로고    scopus 로고
    • Ribose 2'-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5
    • Zust R., Cervantes-Barragan L., Habjan M., Maier R., Neuman B.W., Ziebuhr J., et al. Ribose 2'-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5. Nat. Immunol. 2011, 12:137-143.
    • (2011) Nat. Immunol. , vol.12 , pp. 137-143
    • Zust, R.1    Cervantes-Barragan, L.2    Habjan, M.3    Maier, R.4    Neuman, B.W.5    Ziebuhr, J.6
  • 53
    • 84920574962 scopus 로고    scopus 로고
    • Coronavirus non-structural protein 16: evasion, attenuation, and possible treatments
    • Menachery V.D., Debbink K., Baric R.S. Coronavirus non-structural protein 16: evasion, attenuation, and possible treatments. Virus Res. 2014.
    • (2014) Virus Res.
    • Menachery, V.D.1    Debbink, K.2    Baric, R.S.3
  • 54
    • 78549284909 scopus 로고    scopus 로고
    • 2'-O methylation of the viral mRNA cap evades host restriction by IFIT family members
    • Daffis S., Szretter K.J., Schriewer J., Li J., Youn S., Errett J., et al. 2'-O methylation of the viral mRNA cap evades host restriction by IFIT family members. Nature 2010, 468:452-456.
    • (2010) Nature , vol.468 , pp. 452-456
    • Daffis, S.1    Szretter, K.J.2    Schriewer, J.3    Li, J.4    Youn, S.5    Errett, J.6
  • 55
    • 84896981937 scopus 로고    scopus 로고
    • Attenuation and restoration of severe acute respiratory syndrome coronavirus mutant lacking 2'-O-methyltransferase activity
    • Menachery V.D., Yount B.L., Josset L., Gralinski L.E., Scobey T., Agnihothram S., et al. Attenuation and restoration of severe acute respiratory syndrome coronavirus mutant lacking 2'-O-methyltransferase activity. J. Virol. 2014, 88:4251-4264.
    • (2014) J. Virol. , vol.88 , pp. 4251-4264
    • Menachery, V.D.1    Yount, B.L.2    Josset, L.3    Gralinski, L.E.4    Scobey, T.5    Agnihothram, S.6
  • 56
    • 84862203582 scopus 로고    scopus 로고
    • RNA 3'-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex
    • Bouvet M., Imbert I., Subissi L., Gluais L., Canard B., Decroly E. RNA 3'-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:9372-9377.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 9372-9377
    • Bouvet, M.1    Imbert, I.2    Subissi, L.3    Gluais, L.4    Canard, B.5    Decroly, E.6
  • 57
    • 79957805839 scopus 로고    scopus 로고
    • Endoribonuclease activities of porcine reproductive and respiratory syndrome virus nsp11 was essential for nsp11 to inhibit IFN-beta induction
    • Shi X., Wang L., Li X., Zhang G., Guo J., Zhao D., et al. Endoribonuclease activities of porcine reproductive and respiratory syndrome virus nsp11 was essential for nsp11 to inhibit IFN-beta induction. Mol. Immunol. 2011, 48:1568-1572.
    • (2011) Mol. Immunol. , vol.48 , pp. 1568-1572
    • Shi, X.1    Wang, L.2    Li, X.3    Zhang, G.4    Guo, J.5    Zhao, D.6
  • 58
    • 54749157085 scopus 로고    scopus 로고
    • SARS-coronavirus replication is supported by a reticulovesicular network of modified endoplasmic reticulum
    • Knoops K., Kikkert M., Worm S.H., Zevenhoven-Dobbe J.C., van der Meer Y., Koster A.J., et al. SARS-coronavirus replication is supported by a reticulovesicular network of modified endoplasmic reticulum. PLoS Biol. 2008, 6:e226.
    • (2008) PLoS Biol. , vol.6 , pp. e226
    • Knoops, K.1    Kikkert, M.2    Worm, S.H.3    Zevenhoven-Dobbe, J.C.4    van der Meer, Y.5    Koster, A.J.6
  • 59
    • 84880177352 scopus 로고    scopus 로고
    • MERS-coronavirus replication induces severe in vitro cytopathology and is strongly inhibited by cyclosporin A or interferon-alpha treatment
    • de Wilde A.H., Raj V.S., Oudshoorn D., Bestebroer T.M., van Nieuwkoop S., Limpens R.W., et al. MERS-coronavirus replication induces severe in vitro cytopathology and is strongly inhibited by cyclosporin A or interferon-alpha treatment. J. Gen. Virol. 2013, 94:1749-1760.
    • (2013) J. Gen. Virol. , vol.94 , pp. 1749-1760
    • de Wilde, A.H.1    Raj, V.S.2    Oudshoorn, D.3    Bestebroer, T.M.4    van Nieuwkoop, S.5    Limpens, R.W.6
  • 60
    • 79960315021 scopus 로고    scopus 로고
    • SARS-CoV nucleocapsid protein antagonizes IFN-beta response by targeting initial step of IFN-beta induction pathway, and its C-terminal region is critical for the antagonism
    • Lu X., Pan J., Tao J., Guo D. SARS-CoV nucleocapsid protein antagonizes IFN-beta response by targeting initial step of IFN-beta induction pathway, and its C-terminal region is critical for the antagonism. Virus Genes 2011, 42:37-45.
    • (2011) Virus Genes , vol.42 , pp. 37-45
    • Lu, X.1    Pan, J.2    Tao, J.3    Guo, D.4
  • 61
    • 33846104528 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus open reading frame (ORF) 3b, ORF 6, and nucleocapsid proteins function as interferon antagonists
    • Kopecky-Bromberg S.A., Martinez-Sobrido L., Frieman M., Baric R.A., Palese P. Severe acute respiratory syndrome coronavirus open reading frame (ORF) 3b, ORF 6, and nucleocapsid proteins function as interferon antagonists. J. Virol. 2007, 81:548-557.
    • (2007) J. Virol. , vol.81 , pp. 548-557
    • Kopecky-Bromberg, S.A.1    Martinez-Sobrido, L.2    Frieman, M.3    Baric, R.A.4    Palese, P.5
  • 62
    • 67449102609 scopus 로고    scopus 로고
    • Molecular determinants for subcellular localization of the severe acute respiratory syndrome coronavirus open reading frame 3b protein
    • Freundt E.C., Yu L., Park E., Lenardo M.J., Xu X.N. Molecular determinants for subcellular localization of the severe acute respiratory syndrome coronavirus open reading frame 3b protein. J. Virol. 2009, 83:6631-6640.
    • (2009) J. Virol. , vol.83 , pp. 6631-6640
    • Freundt, E.C.1    Yu, L.2    Park, E.3    Lenardo, M.J.4    Xu, X.N.5
  • 63
    • 67650230347 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus M protein inhibits type I interferon production by impeding the formation of TRAF3.TANK.TBK1/IKKepsilon complex
    • Siu K.L., Kok K.H., Ng M.H., Poon V.K., Yuen K.Y., Zheng B.J., et al. Severe acute respiratory syndrome coronavirus M protein inhibits type I interferon production by impeding the formation of TRAF3.TANK.TBK1/IKKepsilon complex. J. Biol. Chem. 2009, 284:16202-16209.
    • (2009) J. Biol. Chem. , vol.284 , pp. 16202-16209
    • Siu, K.L.1    Kok, K.H.2    Ng, M.H.3    Poon, V.K.4    Yuen, K.Y.5    Zheng, B.J.6
  • 64
    • 84899584959 scopus 로고    scopus 로고
    • SARS coronavirus papain-like protease inhibits the type I interferon signaling pathway through interaction with the STING-TRAF3-TBK1 complex
    • Chen X., Yang X., Zheng Y., Yang Y., Xing Y., Chen Z. SARS coronavirus papain-like protease inhibits the type I interferon signaling pathway through interaction with the STING-TRAF3-TBK1 complex. Protein Cell. 2014, 5:369-381.
    • (2014) Protein Cell. , vol.5 , pp. 369-381
    • Chen, X.1    Yang, X.2    Zheng, Y.3    Yang, Y.4    Xing, Y.5    Chen, Z.6
  • 65
    • 84856501373 scopus 로고    scopus 로고
    • Coronavirus papain-like proteases negatively regulate antiviral innate immune response through disruption of STING-mediated signaling
    • Sun L., Xing Y., Chen X., Zheng Y., Yang Y., Nichols D.B., et al. Coronavirus papain-like proteases negatively regulate antiviral innate immune response through disruption of STING-mediated signaling. PLoS One 2012, 7:e30802.
    • (2012) PLoS One , vol.7 , pp. e30802
    • Sun, L.1    Xing, Y.2    Chen, X.3    Zheng, Y.4    Yang, Y.5    Nichols, D.B.6
  • 66
    • 67449088510 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus papain-like protease ubiquitin-like domain and catalytic domain regulate antagonism of IRF3 and NF-kappaB signaling
    • Frieman M., Ratia K., Johnston R.E., Mesecar A.D., Baric R.S. Severe acute respiratory syndrome coronavirus papain-like protease ubiquitin-like domain and catalytic domain regulate antagonism of IRF3 and NF-kappaB signaling. J. Virol. 2009, 83:6689-6705.
    • (2009) J. Virol. , vol.83 , pp. 6689-6705
    • Frieman, M.1    Ratia, K.2    Johnston, R.E.3    Mesecar, A.D.4    Baric, R.S.5
  • 67
    • 84886731532 scopus 로고    scopus 로고
    • Strategies of highly pathogenic RNA viruses to block dsRNA detection by RIG-I-like receptors: hide, mask, hit
    • Zinzula L., Tramontano E. Strategies of highly pathogenic RNA viruses to block dsRNA detection by RIG-I-like receptors: hide, mask, hit. Antiviral Res. 2013, 100:615-635.
    • (2013) Antiviral Res. , vol.100 , pp. 615-635
    • Zinzula, L.1    Tramontano, E.2
  • 68
    • 84910073473 scopus 로고    scopus 로고
    • Message in a bottle: lessons learned from antagonism of STING signalling during RNA virus infection
    • Maringer K., Fernandez-Sesma A. Message in a bottle: lessons learned from antagonism of STING signalling during RNA virus infection. Cytokine Growth Factor Rev. 2014.
    • (2014) Cytokine Growth Factor Rev.
    • Maringer, K.1    Fernandez-Sesma, A.2
  • 69
    • 79955075657 scopus 로고    scopus 로고
    • The double-stranded RNA-binding protein PACT functions as a cellular activator of RIG-I to facilitate innate antiviral response
    • Kok K.H., Lui P.Y., Ng M.H., Siu K.L., Au S.W., Jin D.Y. The double-stranded RNA-binding protein PACT functions as a cellular activator of RIG-I to facilitate innate antiviral response. Cell Host Microbe. 2011, 9:299-309.
    • (2011) Cell Host Microbe. , vol.9 , pp. 299-309
    • Kok, K.H.1    Lui, P.Y.2    Ng, M.H.3    Siu, K.L.4    Au, S.W.5    Jin, D.Y.6
  • 70
    • 84895534920 scopus 로고    scopus 로고
    • Middle east respiratory syndrome coronavirus 4a protein is a double-stranded RNA-binding protein that suppresses PACT-induced activation of RIG-I and MDA5 in the innate antiviral response
    • Siu K.L., Yeung M.L., Kok K.H., Yuen K.S., Kew C., Lui P.Y., et al. Middle east respiratory syndrome coronavirus 4a protein is a double-stranded RNA-binding protein that suppresses PACT-induced activation of RIG-I and MDA5 in the innate antiviral response. J. Virol. 2014, 88:4866-4876.
    • (2014) J. Virol. , vol.88 , pp. 4866-4876
    • Siu, K.L.1    Yeung, M.L.2    Kok, K.H.3    Yuen, K.S.4    Kew, C.5    Lui, P.Y.6
  • 71
    • 84897055458 scopus 로고    scopus 로고
    • The ORF4b-encoded accessory proteins of Middle East respiratory syndrome coronavirus and two related bat coronaviruses localize to the nucleus and inhibit innate immune signalling
    • Matthews K.L., Coleman C.M., van der Meer Y., Snijder E.J., Frieman M.B. The ORF4b-encoded accessory proteins of Middle East respiratory syndrome coronavirus and two related bat coronaviruses localize to the nucleus and inhibit innate immune signalling. J. Gen. Virol. 2014, 95:874-882.
    • (2014) J. Gen. Virol. , vol.95 , pp. 874-882
    • Matthews, K.L.1    Coleman, C.M.2    van der Meer, Y.3    Snijder, E.J.4    Frieman, M.B.5
  • 72
    • 84905902848 scopus 로고    scopus 로고
    • Flaviviral RNAs: weapons and targets in the war between virus and host
    • Bidet K., Garcia-Blanco M.A. Flaviviral RNAs: weapons and targets in the war between virus and host. Biochem. J. 2014, 462:215-230.
    • (2014) Biochem. J. , vol.462 , pp. 215-230
    • Bidet, K.1    Garcia-Blanco, M.A.2
  • 73
    • 84871654982 scopus 로고    scopus 로고
    • Immune evasion strategies of flaviviruses
    • Ye J., Zhu B., Fu Z.F., Chen H., Cao S. Immune evasion strategies of flaviviruses. Vaccine 2013, 31:461-471.
    • (2013) Vaccine , vol.31 , pp. 461-471
    • Ye, J.1    Zhu, B.2    Fu, Z.F.3    Chen, H.4    Cao, S.5
  • 74
    • 77956126053 scopus 로고    scopus 로고
    • Flavivirus RNA cap methyltransferase: structure, function, and inhibition
    • Liu L., Dong H., Chen H., Zhang J., Ling H., Li Z., et al. Flavivirus RNA cap methyltransferase: structure, function, and inhibition. Front. Biol. (Beijing) 2010, 5:286-303.
    • (2010) Front. Biol. (Beijing) , vol.5 , pp. 286-303
    • Liu, L.1    Dong, H.2    Chen, H.3    Zhang, J.4    Ling, H.5    Li, Z.6
  • 75
    • 84861978036 scopus 로고    scopus 로고
    • Flaviviruses and flavivirus vaccines
    • Heinz F.X., Stiasny K. Flaviviruses and flavivirus vaccines. Vaccine 2012, 30:4301-4306.
    • (2012) Vaccine , vol.30 , pp. 4301-4306
    • Heinz, F.X.1    Stiasny, K.2
  • 79
    • 50049109958 scopus 로고    scopus 로고
    • Flavivirus methyltransferase: a novel antiviral target
    • Dong H., Zhang B., Shi P.Y. Flavivirus methyltransferase: a novel antiviral target. Antiviral Res. 2008, 80:1-10.
    • (2008) Antiviral Res. , vol.80 , pp. 1-10
    • Dong, H.1    Zhang, B.2    Shi, P.Y.3
  • 80
    • 84863711523 scopus 로고    scopus 로고
    • 2'-O methylation of the viral mRNA cap by West Nile virus evades ifit1-dependent and -independent mechanisms of host restriction in vivo
    • Szretter K.J., Daniels B.P., Cho H., Gainey M.D., Yokoyama W.M., Gale M., et al. 2'-O methylation of the viral mRNA cap by West Nile virus evades ifit1-dependent and -independent mechanisms of host restriction in vivo. PLoS Pathog. 2012, 8:e1002698.
    • (2012) PLoS Pathog. , vol.8 , pp. e1002698
    • Szretter, K.J.1    Daniels, B.P.2    Cho, H.3    Gainey, M.D.4    Yokoyama, W.M.5    Gale, M.6
  • 81
    • 84883310180 scopus 로고    scopus 로고
    • Ifit1 inhibits Japanese encephalitis virus replication through binding to 5' capped 2'-O unmethylated RNA
    • Kimura T., Katoh H., Kayama H., Saiga H., Okuyama M., Okamoto T., et al. Ifit1 inhibits Japanese encephalitis virus replication through binding to 5' capped 2'-O unmethylated RNA. J. Virol. 2013, 87:9997-10003.
    • (2013) J. Virol. , vol.87 , pp. 9997-10003
    • Kimura, T.1    Katoh, H.2    Kayama, H.3    Saiga, H.4    Okuyama, M.5    Okamoto, T.6
  • 82
    • 77957201605 scopus 로고    scopus 로고
    • The endoplasmic reticulum provides the membrane platform for biogenesis of the flavivirus replication complex
    • Gillespie L.K., Hoenen A., Morgan G., Mackenzie J.M. The endoplasmic reticulum provides the membrane platform for biogenesis of the flavivirus replication complex. J. Virol. 2010, 84:10438-10447.
    • (2010) J. Virol. , vol.84 , pp. 10438-10447
    • Gillespie, L.K.1    Hoenen, A.2    Morgan, G.3    Mackenzie, J.M.4
  • 83
    • 64649097038 scopus 로고    scopus 로고
    • Composition and three-dimensional architecture of the dengue virus replication and assembly sites
    • Welsch S., Miller S., Romero-Brey I., Merz A., Bleck C.K., Walther P., et al. Composition and three-dimensional architecture of the dengue virus replication and assembly sites. Cell Host Microbe. 2009, 5:365-375.
    • (2009) Cell Host Microbe. , vol.5 , pp. 365-375
    • Welsch, S.1    Miller, S.2    Romero-Brey, I.3    Merz, A.4    Bleck, C.K.5    Walther, P.6
  • 84
    • 77950824984 scopus 로고    scopus 로고
    • Dengue virus inhibits the production of type I interferon in primary human dendritic cells
    • Rodriguez-Madoz J.R., Bernal-Rubio D., Kaminski D., Boyd K., Fernandez-Sesma A. Dengue virus inhibits the production of type I interferon in primary human dendritic cells. J. Virol. 2010, 84:4845-4850.
    • (2010) J. Virol. , vol.84 , pp. 4845-4850
    • Rodriguez-Madoz, J.R.1    Bernal-Rubio, D.2    Kaminski, D.3    Boyd, K.4    Fernandez-Sesma, A.5
  • 85
    • 77956859036 scopus 로고    scopus 로고
    • Inhibition of the type I interferon response in human dendritic cells by dengue virus infection requires a catalytically active NS2B3 complex
    • Rodriguez-Madoz J.R., Belicha-Villanueva A., Bernal-Rubio D., Ashour J., Ayllon J., Fernandez-Sesma A. Inhibition of the type I interferon response in human dendritic cells by dengue virus infection requires a catalytically active NS2B3 complex. J. Virol. 2010, 84:9760-9774.
    • (2010) J. Virol. , vol.84 , pp. 9760-9774
    • Rodriguez-Madoz, J.R.1    Belicha-Villanueva, A.2    Bernal-Rubio, D.3    Ashour, J.4    Ayllon, J.5    Fernandez-Sesma, A.6
  • 86
    • 84868102239 scopus 로고    scopus 로고
    • DENV inhibits type I IFN production in infected cells by cleaving human STING
    • Aguirre S., Maestre A.M., Pagni S., Patel J.R., Savage T., Gutman D., et al. DENV inhibits type I IFN production in infected cells by cleaving human STING. PLoS Pathog. 2012, 8:e1002934.
    • (2012) PLoS Pathog. , vol.8 , pp. e1002934
    • Aguirre, S.1    Maestre, A.M.2    Pagni, S.3    Patel, J.R.4    Savage, T.5    Gutman, D.6
  • 87
    • 84864036246 scopus 로고    scopus 로고
    • Dengue virus targets the adaptor protein MITA to subvert host innate immunity
    • Yu C.Y., Chang T.H., Liang J.J., Chiang R.L., Lee Y.L., Liao C.L., et al. Dengue virus targets the adaptor protein MITA to subvert host innate immunity. PLoS Pathog. 2012, 8:e1002780.
    • (2012) PLoS Pathog. , vol.8 , pp. e1002780
    • Yu, C.Y.1    Chang, T.H.2    Liang, J.J.3    Chiang, R.L.4    Lee, Y.L.5    Liao, C.L.6
  • 88
    • 84896690188 scopus 로고    scopus 로고
    • Activation and evasion of antiviral innate immunity by hepatitis C virus
    • Horner S.M. Activation and evasion of antiviral innate immunity by hepatitis C virus. J. Mol. Biol. 2014, 426:1198-1209.
    • (2014) J. Mol. Biol. , vol.426 , pp. 1198-1209
    • Horner, S.M.1
  • 89
    • 59149085501 scopus 로고    scopus 로고
    • The global burden of hepatitis C
    • Lavanchy D. The global burden of hepatitis C. Liver Int. 2009, 29(Suppl. 1):74-81.
    • (2009) Liver Int. , vol.29 , pp. 74-81
    • Lavanchy, D.1
  • 90
    • 84887993940 scopus 로고    scopus 로고
    • Interferon-stimulated genes and their role in controlling hepatitis C virus
    • Metz P., Reuter A., Bender S., Bartenschlager R. Interferon-stimulated genes and their role in controlling hepatitis C virus. J. Hepatol. 2013, 59:1331-1341.
    • (2013) J. Hepatol. , vol.59 , pp. 1331-1341
    • Metz, P.1    Reuter, A.2    Bender, S.3    Bartenschlager, R.4
  • 92
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • Meylan E., Curran J., Hofmann K., Moradpour D., Binder M., Bartenschlager R., et al. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature 2005, 437:1167-1172.
    • (2005) Nature , vol.437 , pp. 1167-1172
    • Meylan, E.1    Curran, J.2    Hofmann, K.3    Moradpour, D.4    Binder, M.5    Bartenschlager, R.6
  • 93
    • 29144462494 scopus 로고    scopus 로고
    • Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity
    • Li X.D., Sun L., Seth R.B., Pineda G., Chen Z.J. Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:17717-17722.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 17717-17722
    • Li, X.D.1    Sun, L.2    Seth, R.B.3    Pineda, G.4    Chen, Z.J.5
  • 94
    • 80052281413 scopus 로고    scopus 로고
    • Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus
    • Horner S.M., Liu H.M., Park H.S., Briley J., Gale M. Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:14590-14595.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 14590-14595
    • Horner, S.M.1    Liu, H.M.2    Park, H.S.3    Briley, J.4    Gale, M.5
  • 95
    • 33744913266 scopus 로고    scopus 로고
    • Dissociation of a MAVS/IPS-1/VISA/Cardif-IKKepsilon molecular complex from the mitochondrial outer membrane by hepatitis C virus NS3-4A proteolytic cleavage
    • Lin R., Lacoste J., Nakhaei P., Sun Q., Yang L., Paz S., et al. Dissociation of a MAVS/IPS-1/VISA/Cardif-IKKepsilon molecular complex from the mitochondrial outer membrane by hepatitis C virus NS3-4A proteolytic cleavage. J. Virol. 2006, 80:6072-6083.
    • (2006) J. Virol. , vol.80 , pp. 6072-6083
    • Lin, R.1    Lacoste, J.2    Nakhaei, P.3    Sun, Q.4    Yang, L.5    Paz, S.6
  • 96
    • 77950603105 scopus 로고    scopus 로고
    • Cleavage of mitochondrial antiviral signaling protein in the liver of patients with chronic hepatitis C correlates with a reduced activation of the endogenous interferon system
    • Bellecave P., Sarasin-Filipowicz M., Donze O., Kennel A., Gouttenoire J., Meylan E., et al. Cleavage of mitochondrial antiviral signaling protein in the liver of patients with chronic hepatitis C correlates with a reduced activation of the endogenous interferon system. Hepatology 2010, 51:1127-1136.
    • (2010) Hepatology , vol.51 , pp. 1127-1136
    • Bellecave, P.1    Sarasin-Filipowicz, M.2    Donze, O.3    Kennel, A.4    Gouttenoire, J.5    Meylan, E.6
  • 97
    • 84872163319 scopus 로고    scopus 로고
    • Hepatitis C virus NS4B protein targets STING and abrogates RIG-I-mediated type I interferon-dependent innate immunity
    • Nitta S., Sakamoto N., Nakagawa M., Kakinuma S., Mishima K., Kusano-Kitazume A., et al. Hepatitis C virus NS4B protein targets STING and abrogates RIG-I-mediated type I interferon-dependent innate immunity. Hepatology 2013, 57:46-58.
    • (2013) Hepatology , vol.57 , pp. 46-58
    • Nitta, S.1    Sakamoto, N.2    Nakagawa, M.3    Kakinuma, S.4    Mishima, K.5    Kusano-Kitazume, A.6
  • 98
    • 84879173207 scopus 로고    scopus 로고
    • Hepatitis C virus NS4B blocks the interaction of STING and TBK1 to evade host innate immunity
    • Ding Q., Cao X., Lu J., Huang B., Liu Y.J., Kato N., et al. Hepatitis C virus NS4B blocks the interaction of STING and TBK1 to evade host innate immunity. J. Hepatol. 2013, 59:52-58.
    • (2013) J. Hepatol. , vol.59 , pp. 52-58
    • Ding, Q.1    Cao, X.2    Lu, J.3    Huang, B.4    Liu, Y.J.5    Kato, N.6
  • 99
    • 14544280209 scopus 로고    scopus 로고
    • Immune evasion by hepatitis C virus NS3/4A protease-mediated cleavage of the Toll-like receptor 3 adaptor protein TRIF
    • Li K., Foy E., Ferreon J.C., Nakamura M., Ferreon A.C., Ikeda M., et al. Immune evasion by hepatitis C virus NS3/4A protease-mediated cleavage of the Toll-like receptor 3 adaptor protein TRIF. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:2992-2997.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 2992-2997
    • Li, K.1    Foy, E.2    Ferreon, J.C.3    Nakamura, M.4    Ferreon, A.C.5    Ikeda, M.6
  • 100
    • 84876858736 scopus 로고    scopus 로고
    • HCV-induced miR-21 contributes to evasion of host immune system by targeting MyD88 and IRAK1
    • Chen Y., Chen J., Wang H., Shi J., Wu K., Liu S., et al. HCV-induced miR-21 contributes to evasion of host immune system by targeting MyD88 and IRAK1. PLoS Pathog. 2013, 9:e1003248.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003248
    • Chen, Y.1    Chen, J.2    Wang, H.3    Shi, J.4    Wu, K.5    Liu, S.6
  • 101
    • 34548178194 scopus 로고    scopus 로고
    • Hepatitis C virus nonstructural protein 5A modulates the toll-like receptor-MyD88-dependent signaling pathway in macrophage cell lines
    • Abe T., Kaname Y., Hamamoto I., Tsuda Y., Wen X., Taguwa S., et al. Hepatitis C virus nonstructural protein 5A modulates the toll-like receptor-MyD88-dependent signaling pathway in macrophage cell lines. J. Virol. 2007, 81:8953-8966.
    • (2007) J. Virol. , vol.81 , pp. 8953-8966
    • Abe, T.1    Kaname, Y.2    Hamamoto, I.3    Tsuda, Y.4    Wen, X.5    Taguwa, S.6
  • 103
    • 84898844083 scopus 로고    scopus 로고
    • Distinct toll-like receptor 3 and 7 expression in peripheral blood mononuclear cells from patients with chronic hepatitis C infection
    • Motavaf M., Noorbakhsh F., Alavian S.M., Sharifi Z. Distinct toll-like receptor 3 and 7 expression in peripheral blood mononuclear cells from patients with chronic hepatitis C infection. Hepat. Mon. 2014, 14:e16421.
    • (2014) Hepat. Mon. , vol.14 , pp. e16421
    • Motavaf, M.1    Noorbakhsh, F.2    Alavian, S.M.3    Sharifi, Z.4
  • 104
    • 84919397221 scopus 로고    scopus 로고
    • Hepatitis C virus infection decreases the expression of Toll-like receptors 3 and 7 via upregulation of miR-758
    • Yang Q., Fu S., Wang J. Hepatitis C virus infection decreases the expression of Toll-like receptors 3 and 7 via upregulation of miR-758. Arch. Virol. 2014, 159:2997-3003.
    • (2014) Arch. Virol. , vol.159 , pp. 2997-3003
    • Yang, Q.1    Fu, S.2    Wang, J.3
  • 105
    • 77952127743 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells sense hepatitis C virus-infected cells, produce interferon, and inhibit infection
    • Takahashi K., Asabe S., Wieland S., Garaigorta U., Gastaminza P., Isogawa M., et al. Plasmacytoid dendritic cells sense hepatitis C virus-infected cells, produce interferon, and inhibit infection. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:7431-7436.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 7431-7436
    • Takahashi, K.1    Asabe, S.2    Wieland, S.3    Garaigorta, U.4    Gastaminza, P.5    Isogawa, M.6
  • 106
    • 0033932001 scopus 로고    scopus 로고
    • Recovery, persistence, and sequelae in hepatitis C virus infection: a perspective on long-term outcome
    • Alter H.J., Seeff L.B. Recovery, persistence, and sequelae in hepatitis C virus infection: a perspective on long-term outcome. Semin. Liver Dis. 2000, 20:17-35.
    • (2000) Semin. Liver Dis. , vol.20 , pp. 17-35
    • Alter, H.J.1    Seeff, L.B.2
  • 107
    • 79952305174 scopus 로고    scopus 로고
    • Interferon-induced gene expression is a stronger predictor of treatment response than IL28B genotype in patients with hepatitis C
    • Dill M.T., Duong F.H., Vogt J.E., Bibert S., Bochud P.Y., Terracciano L., et al. Interferon-induced gene expression is a stronger predictor of treatment response than IL28B genotype in patients with hepatitis C. Gastroenterology 2011, 140:1021-1031.
    • (2011) Gastroenterology , vol.140 , pp. 1021-1031
    • Dill, M.T.1    Duong, F.H.2    Vogt, J.E.3    Bibert, S.4    Bochud, P.Y.5    Terracciano, L.6
  • 108
    • 84901703352 scopus 로고    scopus 로고
    • HIV and HCV activate the inflammasome in monocytes and macrophages via endosomal Toll-like receptors without induction of type 1 interferon
    • Chattergoon M.A., Latanich R., Quinn J., Winter M.E., Buckheit R.W., Blankson J.N., et al. HIV and HCV activate the inflammasome in monocytes and macrophages via endosomal Toll-like receptors without induction of type 1 interferon. PLoS Pathog. 2014, 10:e1004082.
    • (2014) PLoS Pathog. , vol.10 , pp. e1004082
    • Chattergoon, M.A.1    Latanich, R.2    Quinn, J.3    Winter, M.E.4    Buckheit, R.W.5    Blankson, J.N.6
  • 109
    • 84904978754 scopus 로고    scopus 로고
    • Sex-specific association between X-linked Toll-like receptor 7 with the outcomes of hepatitis C virus infection
    • Yue M., Feng L., Tang S.D., Wang J.J., Xue X.X., Ding W.L., et al. Sex-specific association between X-linked Toll-like receptor 7 with the outcomes of hepatitis C virus infection. Gene 2014, 548:244-250.
    • (2014) Gene , vol.548 , pp. 244-250
    • Yue, M.1    Feng, L.2    Tang, S.D.3    Wang, J.J.4    Xue, X.X.5    Ding, W.L.6
  • 111
    • 84866498069 scopus 로고    scopus 로고
    • Redefining the viral reservoirs that prevent HIV-1 eradication
    • Eisele E., Siliciano R.F. Redefining the viral reservoirs that prevent HIV-1 eradication. Immunity 2012, 37:377-388.
    • (2012) Immunity , vol.37 , pp. 377-388
    • Eisele, E.1    Siliciano, R.F.2
  • 112
    • 84885075354 scopus 로고    scopus 로고
    • Therapeutics for HIV-1 reactivation from latency
    • Sgarbanti M., Battistini A. Therapeutics for HIV-1 reactivation from latency. Curr. Opin. Virol. 2013, 3:394-401.
    • (2013) Curr. Opin. Virol. , vol.3 , pp. 394-401
    • Sgarbanti, M.1    Battistini, A.2
  • 113
    • 84899461396 scopus 로고    scopus 로고
    • HIV-1 latency: an update of molecular mechanisms and therapeutic strategies
    • Battistini A., Sgarbanti M. HIV-1 latency: an update of molecular mechanisms and therapeutic strategies. Viruses 2014, 6:1715-1758.
    • (2014) Viruses , vol.6 , pp. 1715-1758
    • Battistini, A.1    Sgarbanti, M.2
  • 114
    • 84864911121 scopus 로고    scopus 로고
    • HIV-1, interferon and the interferon regulatory factor system: an interplay between induction, antiviral responses and viral evasion
    • Marsili G., Remoli A.L., Sgarbanti M., Perrotti E., Fragale A., Battistini A. HIV-1, interferon and the interferon regulatory factor system: an interplay between induction, antiviral responses and viral evasion. Cytokine Growth Factor Rev. 2012, 23:255-270.
    • (2012) Cytokine Growth Factor Rev. , vol.23 , pp. 255-270
    • Marsili, G.1    Remoli, A.L.2    Sgarbanti, M.3    Perrotti, E.4    Fragale, A.5    Battistini, A.6
  • 115
    • 84894523250 scopus 로고    scopus 로고
    • Innate antiviral immune signaling, viral evasion and modulation by HIV-1
    • Rustagi A., Gale M. Innate antiviral immune signaling, viral evasion and modulation by HIV-1. J. Mol. Biol. 2014, 426:1161-1177.
    • (2014) J. Mol. Biol. , vol.426 , pp. 1161-1177
    • Rustagi, A.1    Gale, M.2
  • 116
    • 84866488122 scopus 로고    scopus 로고
    • Innate immune recognition of HIV-1
    • Iwasaki A. Innate immune recognition of HIV-1. Immunity 2012, 37:389-398.
    • (2012) Immunity , vol.37 , pp. 389-398
    • Iwasaki, A.1
  • 117
    • 78651387934 scopus 로고    scopus 로고
    • The interface between the innate interferon response and expression of host retroviral restriction factors
    • Douville R.N., Hiscott J. The interface between the innate interferon response and expression of host retroviral restriction factors. Cytokine 2010, 52:108-115.
    • (2010) Cytokine , vol.52 , pp. 108-115
    • Douville, R.N.1    Hiscott, J.2
  • 118
    • 84918539112 scopus 로고    scopus 로고
    • Unmasking immune sensing of retroviruses: interplay between innate sensors and host effectors
    • van Montfoort N., Olagnier D., Hiscott J. Unmasking immune sensing of retroviruses: interplay between innate sensors and host effectors. Cytokine Growth Factor Rev. 2014.
    • (2014) Cytokine Growth Factor Rev.
    • van Montfoort, N.1    Olagnier, D.2    Hiscott, J.3
  • 120
    • 84904200114 scopus 로고    scopus 로고
    • Interactions between HIV-1 and the cell-autonomous innate immune system
    • Towers G.J., Noursadeghi M. Interactions between HIV-1 and the cell-autonomous innate immune system. Cell Host Microbe. 2014, 16:10-18.
    • (2014) Cell Host Microbe. , vol.16 , pp. 10-18
    • Towers, G.J.1    Noursadeghi, M.2
  • 121
    • 84867654572 scopus 로고    scopus 로고
    • Innate immune sensing of HIV-1 by dendritic cells
    • Luban J. Innate immune sensing of HIV-1 by dendritic cells. Cell Host Microbe. 2012, 12:408-418.
    • (2012) Cell Host Microbe. , vol.12 , pp. 408-418
    • Luban, J.1
  • 122
    • 84905732218 scopus 로고    scopus 로고
    • The ribonuclease activity of SAMHD1 is required for HIV-1 restriction
    • Ryoo J., Choi J., Oh C., Kim S., Seo M., Kim S.Y., et al. The ribonuclease activity of SAMHD1 is required for HIV-1 restriction. Nat. Med. 2014, 20:936-941.
    • (2014) Nat. Med. , vol.20 , pp. 936-941
    • Ryoo, J.1    Choi, J.2    Oh, C.3    Kim, S.4    Seo, M.5    Kim, S.Y.6
  • 123
    • 84887988228 scopus 로고    scopus 로고
    • SAMHD1 host restriction factor: a link with innate immune sensing of retrovirus infection
    • Sze A., Olagnier D., Lin R., van Grevenynghe J., Hiscott J. SAMHD1 host restriction factor: a link with innate immune sensing of retrovirus infection. J. Mol. Biol. 2013, 425:4981-4994.
    • (2013) J. Mol. Biol. , vol.425 , pp. 4981-4994
    • Sze, A.1    Olagnier, D.2    Lin, R.3    van Grevenynghe, J.4    Hiscott, J.5
  • 124
    • 79959843617 scopus 로고    scopus 로고
    • SAMHD1 is the dendritic- and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx
    • Laguette N., Sobhian B., Casartelli N., Ringeard M., Chable-Bessia C., Segeral E., et al. SAMHD1 is the dendritic- and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx. Nature 2011, 474:654-657.
    • (2011) Nature , vol.474 , pp. 654-657
    • Laguette, N.1    Sobhian, B.2    Casartelli, N.3    Ringeard, M.4    Chable-Bessia, C.5    Segeral, E.6
  • 125
    • 79959858243 scopus 로고    scopus 로고
    • Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein
    • Hrecka K., Hao C., Gierszewska M., Swanson S.K., Kesik-Brodacka M., Srivastava S., et al. Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein. Nature 2011, 474:658-661.
    • (2011) Nature , vol.474 , pp. 658-661
    • Hrecka, K.1    Hao, C.2    Gierszewska, M.3    Swanson, S.K.4    Kesik-Brodacka, M.5    Srivastava, S.6
  • 126
    • 84894435407 scopus 로고    scopus 로고
    • Dendritic cells in progression and pathology of HIV infection
    • Manches O., Frleta D., Bhardwaj N. Dendritic cells in progression and pathology of HIV infection. Trends Immunol. 2014, 35:114-122.
    • (2014) Trends Immunol. , vol.35 , pp. 114-122
    • Manches, O.1    Frleta, D.2    Bhardwaj, N.3
  • 128
    • 78651401005 scopus 로고    scopus 로고
    • RIG-I-mediated antiviral signaling is inhibited in HIV-1 infection by a protease-mediated sequestration of RIG-I
    • Solis M., Nakhaei P., Jalalirad M., Lacoste J., Douville R., Arguello M., et al. RIG-I-mediated antiviral signaling is inhibited in HIV-1 infection by a protease-mediated sequestration of RIG-I. J. Virol. 2011, 85:1224-1236.
    • (2011) J. Virol. , vol.85 , pp. 1224-1236
    • Solis, M.1    Nakhaei, P.2    Jalalirad, M.3    Lacoste, J.4    Douville, R.5    Arguello, M.6
  • 130
    • 77958114725 scopus 로고    scopus 로고
    • The cytosolic exonuclease TREX1 inhibits the innate immune response to human immunodeficiency virus type 1
    • Yan N., Regalado-Magdos A.D., Stiggelbout B., Lee-Kirsch M.A., Lieberman J. The cytosolic exonuclease TREX1 inhibits the innate immune response to human immunodeficiency virus type 1. Nat. Immunol. 2010, 11:1005-1013.
    • (2010) Nat. Immunol. , vol.11 , pp. 1005-1013
    • Yan, N.1    Regalado-Magdos, A.D.2    Stiggelbout, B.3    Lee-Kirsch, M.A.4    Lieberman, J.5
  • 131
    • 84892739389 scopus 로고    scopus 로고
    • Cell death by pyroptosis drives CD4 T-cell depletion in HIV-1 infection
    • Doitsh G., Galloway N.L., Geng X., Yang Z., Monroe K.M., Zepeda O., et al. Cell death by pyroptosis drives CD4 T-cell depletion in HIV-1 infection. Nature 2014, 505:509-514.
    • (2014) Nature , vol.505 , pp. 509-514
    • Doitsh, G.1    Galloway, N.L.2    Geng, X.3    Yang, Z.4    Monroe, K.M.5    Zepeda, O.6
  • 132
    • 84890215093 scopus 로고    scopus 로고
    • The capsids of HIV-1 and HIV-2 determine immune detection of the viral cDNA by the innate sensor cGAS in dendritic cells
    • Lahaye X., Satoh T., Gentili M., Cerboni S., Conrad C., Hurbain I., et al. The capsids of HIV-1 and HIV-2 determine immune detection of the viral cDNA by the innate sensor cGAS in dendritic cells. Immunity 2013, 39:1132-1142.
    • (2013) Immunity , vol.39 , pp. 1132-1142
    • Lahaye, X.1    Satoh, T.2    Gentili, M.3    Cerboni, S.4    Conrad, C.5    Hurbain, I.6
  • 133
    • 84888054227 scopus 로고    scopus 로고
    • HIV-1 evades innate immune recognition through specific cofactor recruitment
    • Rasaiyaah J., Tan C.P., Fletcher A.J., Price A.J., Blondeau C., Hilditch L., et al. HIV-1 evades innate immune recognition through specific cofactor recruitment. Nature 2013, 503:402-405.
    • (2013) Nature , vol.503 , pp. 402-405
    • Rasaiyaah, J.1    Tan, C.P.2    Fletcher, A.J.3    Price, A.J.4    Blondeau, C.5    Hilditch, L.6
  • 134
    • 84964315701 scopus 로고    scopus 로고
    • Transmission dynamics and control of Ebola virus disease (EVD): a review
    • Chowell G., Nishiura H. Transmission dynamics and control of Ebola virus disease (EVD): a review. BMC Med. 2014, 12:196.
    • (2014) BMC Med. , vol.12 , pp. 196
    • Chowell, G.1    Nishiura, H.2
  • 135
    • 84901068339 scopus 로고    scopus 로고
    • Characterization of host immune responses in Ebola virus infections
    • Wong G., Kobinger G.P., Qiu X. Characterization of host immune responses in Ebola virus infections. Expert Rev. Clin. Immunol. 2014, 10:781-790.
    • (2014) Expert Rev. Clin. Immunol. , vol.10 , pp. 781-790
    • Wong, G.1    Kobinger, G.P.2    Qiu, X.3
  • 136
    • 0034993883 scopus 로고    scopus 로고
    • The role of the Type I interferon response in the resistance of mice to filovirus infection
    • Bray M. The role of the Type I interferon response in the resistance of mice to filovirus infection. J. Gen. Virol. 2001, 82:1365-1373.
    • (2001) J. Gen. Virol. , vol.82 , pp. 1365-1373
    • Bray, M.1
  • 137
    • 70349255932 scopus 로고    scopus 로고
    • Evasion of interferon responses by Ebola and Marburg viruses
    • Basler C.F., Amarasinghe G.K. Evasion of interferon responses by Ebola and Marburg viruses. J. Interferon Cytokine Res. 2009, 29:511-520.
    • (2009) J. Interferon Cytokine Res. , vol.29 , pp. 511-520
    • Basler, C.F.1    Amarasinghe, G.K.2
  • 139
    • 84866939048 scopus 로고    scopus 로고
    • Marburg virus VP35 can both fully coat the backbone and cap the ends of dsRNA for interferon antagonism
    • Bale S., Julien J.P., Bornholdt Z.A., Kimberlin C.R., Halfmann P., Zandonatti M.A., et al. Marburg virus VP35 can both fully coat the backbone and cap the ends of dsRNA for interferon antagonism. PLoS Pathog. 2012, 8:e1002916.
    • (2012) PLoS Pathog. , vol.8 , pp. e1002916
    • Bale, S.1    Julien, J.P.2    Bornholdt, Z.A.3    Kimberlin, C.R.4    Halfmann, P.5    Zandonatti, M.A.6
  • 141
    • 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. Nat. Rev. Immunol. 2005, 5:675-687.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 675-687
    • Decker, T.1    Muller, M.2    Stockinger, S.3
  • 142
    • 84883809384 scopus 로고    scopus 로고
    • Structural modifications of bacterial lipopolysaccharide that facilitate gram-negative bacteria evasion of host innate immunity
    • Matsuura M. Structural modifications of bacterial lipopolysaccharide that facilitate gram-negative bacteria evasion of host innate immunity. Front. Immunol. 2013, 4:109.
    • (2013) Front. Immunol. , vol.4 , pp. 109
    • Matsuura, M.1
  • 143
    • 84887431806 scopus 로고    scopus 로고
    • Intracellular Shigella remodels its LPS to dampen the innate immune recognition and evade inflammasome activation
    • Paciello I., Silipo A., Lembo-Fazio L., Curcuru L., Zumsteg A., Noel G., et al. Intracellular Shigella remodels its LPS to dampen the innate immune recognition and evade inflammasome activation. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:E4345-E4354.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. E4345-E4354
    • Paciello, I.1    Silipo, A.2    Lembo-Fazio, L.3    Curcuru, L.4    Zumsteg, A.5    Noel, G.6
  • 144
    • 34848831208 scopus 로고    scopus 로고
    • YopJ targets TRAF proteins to inhibit TLR-mediated NF-kappaB, MAPK and IRF3 signal transduction
    • Sweet C.R., Conlon J., Golenbock D.T., Goguen J., Silverman N. YopJ targets TRAF proteins to inhibit TLR-mediated NF-kappaB, MAPK and IRF3 signal transduction. Cell. Microbiol. 2007, 9:2700-2715.
    • (2007) Cell. Microbiol. , vol.9 , pp. 2700-2715
    • Sweet, C.R.1    Conlon, J.2    Golenbock, D.T.3    Goguen, J.4    Silverman, N.5
  • 145
    • 84862818454 scopus 로고    scopus 로고
    • The Shigella flexneri effector OspI deamidates UBC13 to dampen the inflammatory response
    • Sanada T., Kim M., Mimuro H., Suzuki M., Ogawa M., Oyama A., et al. The Shigella flexneri effector OspI deamidates UBC13 to dampen the inflammatory response. Nature 2012, 483:623-626.
    • (2012) Nature , vol.483 , pp. 623-626
    • Sanada, T.1    Kim, M.2    Mimuro, H.3    Suzuki, M.4    Ogawa, M.5    Oyama, A.6
  • 146
    • 84867746584 scopus 로고    scopus 로고
    • Inhibition of TLR signaling by a bacterial protein containing immunoreceptor tyrosine-based inhibitory motifs
    • Yan D., Wang X., Luo L., Cao X., Ge B. Inhibition of TLR signaling by a bacterial protein containing immunoreceptor tyrosine-based inhibitory motifs. Nat. Immunol. 2012, 13:1063-1071.
    • (2012) Nat. Immunol. , vol.13 , pp. 1063-1071
    • Yan, D.1    Wang, X.2    Luo, L.3    Cao, X.4    Ge, B.5
  • 147
    • 0038363463 scopus 로고    scopus 로고
    • Triggering the interferon antiviral response through an IKK-related pathway
    • Sharma S., tenOever B.R., Grandvaux N., Zhou G.P., Lin R., Hiscott J. Triggering the interferon antiviral response through an IKK-related pathway. Science 2003, 300:1148-1151.
    • (2003) Science , vol.300 , pp. 1148-1151
    • Sharma, S.1    tenOever, B.R.2    Grandvaux, N.3    Zhou, G.P.4    Lin, R.5    Hiscott, J.6
  • 149
    • 77449101221 scopus 로고    scopus 로고
    • Regulation of immunity and oncogenesis by the IRF transcription factor family
    • Savitsky D., Tamura T., Yanai H., Taniguchi T. Regulation of immunity and oncogenesis by the IRF transcription factor family. Cancer Immunol. Immunother. 2010, 59:489-510.
    • (2010) Cancer Immunol. Immunother. , vol.59 , pp. 489-510
    • Savitsky, D.1    Tamura, T.2    Yanai, H.3    Taniguchi, T.4
  • 151
    • 33750064259 scopus 로고    scopus 로고
    • Evidence for licensing of IFN-gamma-induced IFN regulatory factor 1 transcription factor by MyD88 in Toll-like receptor-dependent gene induction program
    • Negishi H., Fujita Y., Yanai H., Sakaguchi S., Ouyang X., Shinohara M., et al. Evidence for licensing of IFN-gamma-induced IFN regulatory factor 1 transcription factor by MyD88 in Toll-like receptor-dependent gene induction program. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:15136-15141.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 15136-15141
    • Negishi, H.1    Fujita, Y.2    Yanai, H.3    Sakaguchi, S.4    Ouyang, X.5    Shinohara, M.6
  • 152
    • 77952503750 scopus 로고    scopus 로고
    • Peroxisomes are signaling platforms for antiviral innate immunity
    • Dixit E., Boulant S., Zhang Y., Lee A.S., Odendall C., Shum B., et al. Peroxisomes are signaling platforms for antiviral innate immunity. Cell 2010, 141:668-681.
    • (2010) Cell , vol.141 , pp. 668-681
    • Dixit, E.1    Boulant, S.2    Zhang, Y.3    Lee, A.S.4    Odendall, C.5    Shum, B.6
  • 153
    • 79955542915 scopus 로고    scopus 로고
    • A diverse range of gene products are effectors of the type I interferon antiviral response
    • Schoggins J.W., Wilson S.J., Panis M., Murphy M.Y., Jones C.T., Bieniasz P., et al. A diverse range of gene products are effectors of the type I interferon antiviral response. Nature 2011, 472:481-485.
    • (2011) Nature , vol.472 , pp. 481-485
    • Schoggins, J.W.1    Wilson, S.J.2    Panis, M.3    Murphy, M.Y.4    Jones, C.T.5    Bieniasz, P.6
  • 154
    • 36148979683 scopus 로고    scopus 로고
    • Regulation of IRF-3-dependent innate immunity by the papain-like protease domain of the severe acute respiratory syndrome coronavirus
    • Devaraj S.G., Wang N., Chen Z., Chen Z., Tseng M., Barretto N., et al. Regulation of IRF-3-dependent innate immunity by the papain-like protease domain of the severe acute respiratory syndrome coronavirus. J. Biol. Chem. 2007, 282:32208-32221.
    • (2007) J. Biol. Chem. , vol.282 , pp. 32208-32221
    • Devaraj, S.G.1    Wang, N.2    Chen, Z.3    Chen, Z.4    Tseng, M.5    Barretto, N.6
  • 155
    • 84894076838 scopus 로고    scopus 로고
    • Proteolytic processing, deubiquitinase and interferon antagonist activities of Middle East respiratory syndrome coronavirus papain-like protease
    • Yang X., Chen X., Bian G., Tu J., Xing Y., Wang Y., et al. Proteolytic processing, deubiquitinase and interferon antagonist activities of Middle East respiratory syndrome coronavirus papain-like protease. J. Gen. Virol. 2014, 95:614-626.
    • (2014) J. Gen. Virol. , vol.95 , pp. 614-626
    • Yang, X.1    Chen, X.2    Bian, G.3    Tu, J.4    Xing, Y.5    Wang, Y.6
  • 156
    • 28544435897 scopus 로고    scopus 로고
    • Immunity by ubiquitylation: a reversible process of modification
    • Liu Y.C., Penninger J., Karin M. Immunity by ubiquitylation: a reversible process of modification. Nat. Rev. Immunol. 2005, 5:941-952.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 941-952
    • Liu, Y.C.1    Penninger, J.2    Karin, M.3
  • 157
    • 50149084681 scopus 로고    scopus 로고
    • West Nile virus nonstructural protein 1 inhibits TLR3 signal transduction
    • Wilson J.R., de Sessions P.F., Leon M.A., Scholle F. West Nile virus nonstructural protein 1 inhibits TLR3 signal transduction. J. Virol. 2008, 82:8262-8271.
    • (2008) J. Virol. , vol.82 , pp. 8262-8271
    • Wilson, J.R.1    de Sessions, P.F.2    Leon, M.A.3    Scholle, F.4
  • 158
    • 84897378080 scopus 로고    scopus 로고
    • Abrogation of TLR3 inhibition by discrete amino acid changes in the C-terminal half of the West Nile virus NS1 protein
    • Morrison C.R., Scholle F. Abrogation of TLR3 inhibition by discrete amino acid changes in the C-terminal half of the West Nile virus NS1 protein. Virology 2014, 456-457:96-107.
    • (2014) Virology , pp. 96-107
    • Morrison, C.R.1    Scholle, F.2
  • 159
    • 84900399883 scopus 로고    scopus 로고
    • Modulation of innate immune signaling by the secreted form of the West Nile virus NS1 glycoprotein
    • Crook K.R., Miller-Kittrell M., Morrison C.R., Scholle F. Modulation of innate immune signaling by the secreted form of the West Nile virus NS1 glycoprotein. Virology 2014, 458-459:172-182.
    • (2014) Virology , pp. 172-182
    • Crook, K.R.1    Miller-Kittrell, M.2    Morrison, C.R.3    Scholle, F.4
  • 160
    • 84892164414 scopus 로고    scopus 로고
    • Dengue virus subverts the interferon induction pathway via NS2B/3 protease-IkappaB kinase epsilon interaction
    • Anglero-Rodriguez Y.I., Pantoja P., Sariol C.A. Dengue virus subverts the interferon induction pathway via NS2B/3 protease-IkappaB kinase epsilon interaction. Clin. Vaccine Immunol. 2014, 21:29-38.
    • (2014) Clin. Vaccine Immunol. , vol.21 , pp. 29-38
    • Anglero-Rodriguez, Y.I.1    Pantoja, P.2    Sariol, C.A.3
  • 161
    • 84897516567 scopus 로고    scopus 로고
    • Tick-borne flaviviruses antagonize both IRF-1 and type I IFN signaling to inhibit dendritic cell function
    • Robertson S.J., Lubick K.J., Freedman B.A., Carmody A.B., Best S.M. Tick-borne flaviviruses antagonize both IRF-1 and type I IFN signaling to inhibit dendritic cell function. J. Immunol. 2014, 192:2744-2755.
    • (2014) J. Immunol. , vol.192 , pp. 2744-2755
    • Robertson, S.J.1    Lubick, K.J.2    Freedman, B.A.3    Carmody, A.B.4    Best, S.M.5
  • 162
    • 17844395681 scopus 로고    scopus 로고
    • Interaction between the HCV NS3 protein and the host TBK1 protein leads to inhibition of cellular antiviral responses
    • Otsuka M., Kato N., Moriyama M., Taniguchi H., Wang Y., Dharel N., et al. Interaction between the HCV NS3 protein and the host TBK1 protein leads to inhibition of cellular antiviral responses. Hepatology 2005, 41:1004-1012.
    • (2005) Hepatology , vol.41 , pp. 1004-1012
    • Otsuka, M.1    Kato, N.2    Moriyama, M.3    Taniguchi, H.4    Wang, Y.5    Dharel, N.6
  • 163
    • 84869208689 scopus 로고    scopus 로고
    • Hepatitis C virus NS2 protease inhibits host cell antiviral response by inhibiting IKKepsilon and TBK1 functions
    • Kaukinen P., Sillanpaa M., Nousiainen L., Melen K., Julkunen I. Hepatitis C virus NS2 protease inhibits host cell antiviral response by inhibiting IKKepsilon and TBK1 functions. J. Med. Virol. 2013, 85:71-82.
    • (2013) J. Med. Virol. , vol.85 , pp. 71-82
    • Kaukinen, P.1    Sillanpaa, M.2    Nousiainen, L.3    Melen, K.4    Julkunen, I.5
  • 164
    • 84870341699 scopus 로고    scopus 로고
    • Impairment of interferon regulatory factor-3 activation by hepatitis C virus core protein basic amino acid region 1
    • Inoue K., Tsukiyama-Kohara K., Matsuda C., Yoneyama M., Fujita T., Kuge S., et al. Impairment of interferon regulatory factor-3 activation by hepatitis C virus core protein basic amino acid region 1. Biochem. Biophys. Res. Commun. 2012, 428:494-499.
    • (2012) Biochem. Biophys. Res. Commun. , vol.428 , pp. 494-499
    • Inoue, K.1    Tsukiyama-Kohara, K.2    Matsuda, C.3    Yoneyama, M.4    Fujita, T.5    Kuge, S.6
  • 165
    • 77951044335 scopus 로고    scopus 로고
    • DEAD/H BOX 3 (DDX3) helicase binds the RIG-I adaptor IPS-1 to up-regulate IFN-beta-inducing potential
    • Oshiumi H., Sakai K., Matsumoto M., Seya T. DEAD/H BOX 3 (DDX3) helicase binds the RIG-I adaptor IPS-1 to up-regulate IFN-beta-inducing potential. Eur. J. Immunol. 2010, 40:940-948.
    • (2010) Eur. J. Immunol. , vol.40 , pp. 940-948
    • Oshiumi, H.1    Sakai, K.2    Matsumoto, M.3    Seya, T.4
  • 166
    • 78650127763 scopus 로고    scopus 로고
    • Hepatitis C virus core protein abrogates the DDX3 function that enhances IPS-1-mediated IFN-beta induction
    • Oshiumi H., Ikeda M., Matsumoto M., Watanabe A., Takeuchi O., Akira S., et al. Hepatitis C virus core protein abrogates the DDX3 function that enhances IPS-1-mediated IFN-beta induction. PLoS One 2010, 5:e14258.
    • (2010) PLoS One , vol.5 , pp. e14258
    • Oshiumi, H.1    Ikeda, M.2    Matsumoto, M.3    Watanabe, A.4    Takeuchi, O.5    Akira, S.6
  • 167
    • 33845724693 scopus 로고    scopus 로고
    • Repression of interferon regulatory factor 1 by hepatitis C virus core protein results in inhibition of antiviral and immunomodulatory genes
    • Ciccaglione A.R., Stellacci E., Marcantonio C., Muto V., Equestre M., Marsili G., et al. Repression of interferon regulatory factor 1 by hepatitis C virus core protein results in inhibition of antiviral and immunomodulatory genes. J. Virol. 2007, 81:202-214.
    • (2007) J. Virol. , vol.81 , pp. 202-214
    • Ciccaglione, A.R.1    Stellacci, E.2    Marcantonio, C.3    Muto, V.4    Equestre, M.5    Marsili, G.6
  • 168
    • 84900385674 scopus 로고    scopus 로고
    • Hepatitis C virus core protein inhibits interferon production by a human plasmacytoid dendritic cell line and dysregulates interferon regulatory factor-7 and signal transducer and activator of transcription (STAT) 1 protein expression
    • Stone A.E., Mitchell A., Brownell J., Miklin D.J., Golden-Mason L., Polyak S.J., et al. Hepatitis C virus core protein inhibits interferon production by a human plasmacytoid dendritic cell line and dysregulates interferon regulatory factor-7 and signal transducer and activator of transcription (STAT) 1 protein expression. PLoS One 2014, 9:e95627.
    • (2014) PLoS One , vol.9 , pp. e95627
    • Stone, A.E.1    Mitchell, A.2    Brownell, J.3    Miklin, D.J.4    Golden-Mason, L.5    Polyak, S.J.6
  • 170
    • 70349748582 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 mediates global disruption of innate antiviral signaling and immune defenses within infected cells
    • Doehle B.P., Hladik F., McNevin J.P., McElrath M.J., Gale M. Human immunodeficiency virus type 1 mediates global disruption of innate antiviral signaling and immune defenses within infected cells. J. Virol. 2009, 83:10395-10405.
    • (2009) J. Virol. , vol.83 , pp. 10395-10405
    • Doehle, B.P.1    Hladik, F.2    McNevin, J.P.3    McElrath, M.J.4    Gale, M.5
  • 171
    • 40649114040 scopus 로고    scopus 로고
    • HIV-1 accessory proteins VPR and Vif modulate antiviral response by targeting IRF-3 for degradation
    • Okumura A., Alce T., Lubyova B., Ezelle H., Strebel K., Pitha P.M. HIV-1 accessory proteins VPR and Vif modulate antiviral response by targeting IRF-3 for degradation. Virology 2008, 373:85-97.
    • (2008) Virology , vol.373 , pp. 85-97
    • Okumura, A.1    Alce, T.2    Lubyova, B.3    Ezelle, H.4    Strebel, K.5    Pitha, P.M.6
  • 172
    • 84865069404 scopus 로고    scopus 로고
    • Vpu-deficient HIV strains stimulate innate immune signaling responses in target cells
    • Doehle B.P., Chang K., Fleming L., McNevin J., Hladik F., McElrath M.J., et al. Vpu-deficient HIV strains stimulate innate immune signaling responses in target cells. J. Virol. 2012, 86:8499-8506.
    • (2012) J. Virol. , vol.86 , pp. 8499-8506
    • Doehle, B.P.1    Chang, K.2    Fleming, L.3    McNevin, J.4    Hladik, F.5    McElrath, M.J.6
  • 174
    • 0038725688 scopus 로고    scopus 로고
    • Apoptosis as an HIV strategy to escape immune attack
    • Gougeon M.L. Apoptosis as an HIV strategy to escape immune attack. Nat. Rev. Immunol. 2003, 3:392-404.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 392-404
    • Gougeon, M.L.1
  • 175
    • 79957998255 scopus 로고    scopus 로고
    • HIV infection of dendritic cells subverts the IFN induction pathway via IRF-1 and inhibits type 1 IFN production
    • Harman A.N., Lai J., Turville S., Samarajiwa S., Gray L., Marsden V., et al. HIV infection of dendritic cells subverts the IFN induction pathway via IRF-1 and inhibits type 1 IFN production. Blood 2011, 118:298-308.
    • (2011) Blood , vol.118 , pp. 298-308
    • Harman, A.N.1    Lai, J.2    Turville, S.3    Samarajiwa, S.4    Gray, L.5    Marsden, V.6
  • 176
    • 41149122048 scopus 로고    scopus 로고
    • IRF-1 is required for full NF-kappaB transcriptional activity at the human immunodeficiency virus type 1 long terminal repeat enhancer
    • Sgarbanti M., Remoli A.L., Marsili G., Ridolfi B., Borsetti A., Perrotti E., et al. IRF-1 is required for full NF-kappaB transcriptional activity at the human immunodeficiency virus type 1 long terminal repeat enhancer. J. Virol. 2008, 82:3632-3641.
    • (2008) J. Virol. , vol.82 , pp. 3632-3641
    • Sgarbanti, M.1    Remoli, A.L.2    Marsili, G.3    Ridolfi, B.4    Borsetti, A.5    Perrotti, E.6
  • 177
    • 0037141146 scopus 로고    scopus 로고
    • Modulation of human immunodeficiency virus 1 replication by interferon regulatory factors
    • Sgarbanti M., Borsetti A., Moscufo N., Bellocchi M.C., Ridolfi B., Nappi F., et al. Modulation of human immunodeficiency virus 1 replication by interferon regulatory factors. J. Exp. Med. 2002, 195:1359-1370.
    • (2002) J. Exp. Med. , vol.195 , pp. 1359-1370
    • Sgarbanti, M.1    Borsetti, A.2    Moscufo, N.3    Bellocchi, M.C.4    Ridolfi, B.5    Nappi, F.6
  • 178
    • 33744819439 scopus 로고    scopus 로고
    • Intracellular HIV-1 Tat protein represses constitutive LMP2 transcription increasing proteasome activity by interfering with the binding of IRF-1 to STAT1
    • Remoli A.L., Marsili G., Perrotti E., Gallerani E., Ilari R., Nappi F., et al. Intracellular HIV-1 Tat protein represses constitutive LMP2 transcription increasing proteasome activity by interfering with the binding of IRF-1 to STAT1. Biochem. J. 2006, 396:371-380.
    • (2006) Biochem. J. , vol.396 , pp. 371-380
    • Remoli, A.L.1    Marsili, G.2    Perrotti, E.3    Gallerani, E.4    Ilari, R.5    Nappi, F.6
  • 179
    • 84894284462 scopus 로고    scopus 로고
    • IkappaB kinase epsilon targets interferon regulatory factor 1 in activated T lymphocytes
    • Sgarbanti M., Marsili G., Remoli A.L., Stellacci E., Mai A., Rotili D., et al. IkappaB kinase epsilon targets interferon regulatory factor 1 in activated T lymphocytes. Mol. Cell. Biol. 2014, 34:1054-1065.
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 1054-1065
    • Sgarbanti, M.1    Marsili, G.2    Remoli, A.L.3    Stellacci, E.4    Mai, A.5    Rotili, D.6
  • 181
    • 63149113399 scopus 로고    scopus 로고
    • Ebola virus protein VP35 impairs the function of interferon regulatory factor-activating kinases IKKepsilon and TBK-1
    • Prins K.C., Cardenas W.B., Basler C.F. Ebola virus protein VP35 impairs the function of interferon regulatory factor-activating kinases IKKepsilon and TBK-1. J. Virol. 2009, 83:3069-3077.
    • (2009) J. Virol. , vol.83 , pp. 3069-3077
    • Prins, K.C.1    Cardenas, W.B.2    Basler, C.F.3
  • 182
    • 77957189097 scopus 로고    scopus 로고
    • Basic residues within the ebolavirus VP35 protein are required for its viral polymerase cofactor function
    • Prins K.C., Binning J.M., Shabman R.S., Leung D.W., Amarasinghe G.K., Basler C.F. Basic residues within the ebolavirus VP35 protein are required for its viral polymerase cofactor function. J. Virol. 2010, 84:10581-10591.
    • (2010) J. Virol. , vol.84 , pp. 10581-10591
    • Prins, K.C.1    Binning, J.M.2    Shabman, R.S.3    Leung, D.W.4    Amarasinghe, G.K.5    Basler, C.F.6
  • 183
    • 67650866693 scopus 로고    scopus 로고
    • Ebola Zaire virus blocks type I interferon production by exploiting the host SUMO modification machinery
    • Chang T.H., Kubota T., Matsuoka M., Jones S., Bradfute S.B., Bray M., et al. Ebola Zaire virus blocks type I interferon production by exploiting the host SUMO modification machinery. PLoS Pathog. 2009, 5:e1000493.
    • (2009) PLoS Pathog. , vol.5 , pp. e1000493
    • Chang, T.H.1    Kubota, T.2    Matsuoka, M.3    Jones, S.4    Bradfute, S.B.5    Bray, M.6
  • 184
    • 54449099430 scopus 로고    scopus 로고
    • Virus infection triggers SUMOylation of IRF3 and IRF7, leading to the negative regulation of type I interferon gene expression
    • Kubota T., Matsuoka M., Chang T.H., Tailor P., Sasaki T., Tashiro M., et al. Virus infection triggers SUMOylation of IRF3 and IRF7, leading to the negative regulation of type I interferon gene expression. J. Biol. Chem. 2008, 283:25660-25670.
    • (2008) J. Biol. Chem. , vol.283 , pp. 25660-25670
    • Kubota, T.1    Matsuoka, M.2    Chang, T.H.3    Tailor, P.4    Sasaki, T.5    Tashiro, M.6
  • 185
    • 84889673409 scopus 로고    scopus 로고
    • Beneficial innate signaling interference for antibacterial responses by a Toll-like receptor-mediated enhancement of the MKP-IRF3 axis
    • Negishi H., Matsuki K., Endo N., Sarashina H., Miki S., Matsuda A., et al. Beneficial innate signaling interference for antibacterial responses by a Toll-like receptor-mediated enhancement of the MKP-IRF3 axis. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:19884-19889.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 19884-19889
    • Negishi, H.1    Matsuki, K.2    Endo, N.3    Sarashina, H.4    Miki, S.5    Matsuda, A.6
  • 186
    • 77949519531 scopus 로고    scopus 로고
    • The SARS Coronavirus 3a protein causes endoplasmic reticulum stress and induces ligand-independent downregulation of the type 1 interferon receptor
    • Minakshi R., Padhan K., Rani M., Khan N., Ahmad F., Jameel S. The SARS Coronavirus 3a protein causes endoplasmic reticulum stress and induces ligand-independent downregulation of the type 1 interferon receptor. PLoS One 2009, 4:e8342.
    • (2009) PLoS One , vol.4 , pp. e8342
    • Minakshi, R.1    Padhan, K.2    Rani, M.3    Khan, N.4    Ahmad, F.5    Jameel, S.6
  • 187
    • 79955624337 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus papain-like protease suppressed alpha interferon-induced responses through downregulation of extracellular signal-regulated kinase 1-mediated signalling pathways
    • Li S.W., Lai C.C., Ping J.F., Tsai F.J., Wan L., Lin Y.J., et al. Severe acute respiratory syndrome coronavirus papain-like protease suppressed alpha interferon-induced responses through downregulation of extracellular signal-regulated kinase 1-mediated signalling pathways. J. Gen. Virol. 2011, 92:1127-1140.
    • (2011) J. Gen. Virol. , vol.92 , pp. 1127-1140
    • Li, S.W.1    Lai, C.C.2    Ping, J.F.3    Tsai, F.J.4    Wan, L.5    Lin, Y.J.6
  • 188
    • 35348845802 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 function by sequestering nuclear import factors on the rough endoplasmic reticulum/Golgi membrane
    • Frieman M., Yount B., Heise M., Kopecky-Bromberg S.A., Palese P., Baric R.S. Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 function by sequestering nuclear import factors on the rough endoplasmic reticulum/Golgi membrane. J. Virol. 2007, 81:9812-9824.
    • (2007) J. Virol. , vol.81 , pp. 9812-9824
    • Frieman, M.1    Yount, B.2    Heise, M.3    Kopecky-Bromberg, S.A.4    Palese, P.5    Baric, R.S.6
  • 189
    • 58249084172 scopus 로고    scopus 로고
    • Virus-induced unfolded protein response attenuates antiviral defenses via phosphorylation-dependent degradation of the type I interferon receptor
    • Liu J., HuangFu W.C., Kumar K.G., Qian J., Casey J.P., Hamanaka R.B., et al. Virus-induced unfolded protein response attenuates antiviral defenses via phosphorylation-dependent degradation of the type I interferon receptor. Cell Host Microbe. 2009, 5:72-83.
    • (2009) Cell Host Microbe. , vol.5 , pp. 72-83
    • Liu, J.1    HuangFu, W.C.2    Kumar, K.G.3    Qian, J.4    Casey, J.P.5    Hamanaka, R.B.6
  • 190
    • 80055114110 scopus 로고    scopus 로고
    • A conserved peptide in West Nile virus NS4A protein contributes to proteolytic processing and is essential for replication
    • Ambrose R.L., Mackenzie J.M. A conserved peptide in West Nile virus NS4A protein contributes to proteolytic processing and is essential for replication. J. Virol. 2011, 85:11274-11282.
    • (2011) J. Virol. , vol.85 , pp. 11274-11282
    • Ambrose, R.L.1    Mackenzie, J.M.2
  • 191
    • 26444489068 scopus 로고    scopus 로고
    • Inhibition of interferon-stimulated JAK-STAT signaling by a tick-borne flavivirus and identification of NS5 as an interferon antagonist
    • Best S.M., Morris K.L., Shannon J.G., Robertson S.J., Mitzel D.N., Park G.S., et al. Inhibition of interferon-stimulated JAK-STAT signaling by a tick-borne flavivirus and identification of NS5 as an interferon antagonist. J. Virol. 2005, 79:12828-12839.
    • (2005) J. Virol. , vol.79 , pp. 12828-12839
    • Best, S.M.1    Morris, K.L.2    Shannon, J.G.3    Robertson, S.J.4    Mitzel, D.N.5    Park, G.S.6
  • 192
    • 34250827756 scopus 로고    scopus 로고
    • Identification of residues critical for the interferon antagonist function of Langat virus NS5 reveals a role for the RNA-dependent RNA polymerase domain
    • Park G.S., Morris K.L., Hallett R.G., Bloom M.E., Best S.M. Identification of residues critical for the interferon antagonist function of Langat virus NS5 reveals a role for the RNA-dependent RNA polymerase domain. J. Virol. 2007, 81:6936-6946.
    • (2007) J. Virol. , vol.81 , pp. 6936-6946
    • Park, G.S.1    Morris, K.L.2    Hallett, R.G.3    Bloom, M.E.4    Best, S.M.5
  • 194
    • 70349432365 scopus 로고    scopus 로고
    • Dengue virus NS5 inhibits interferon-alpha signaling by blocking signal transducer and activator of transcription 2 phosphorylation
    • Mazzon M., Jones M., Davidson A., Chain B., Jacobs M. Dengue virus NS5 inhibits interferon-alpha signaling by blocking signal transducer and activator of transcription 2 phosphorylation. J. Infect. Dis. 2009, 200:1261-1270.
    • (2009) J. Infect. Dis. , vol.200 , pp. 1261-1270
    • Mazzon, M.1    Jones, M.2    Davidson, A.3    Chain, B.4    Jacobs, M.5
  • 195
    • 66149146738 scopus 로고    scopus 로고
    • NS5 of dengue virus mediates STAT2 binding and degradation
    • Ashour J., Laurent-Rolle M., Shi P.Y., Garcia-Sastre A. NS5 of dengue virus mediates STAT2 binding and degradation. J. Virol. 2009, 83:5408-5418.
    • (2009) J. Virol. , vol.83 , pp. 5408-5418
    • Ashour, J.1    Laurent-Rolle, M.2    Shi, P.Y.3    Garcia-Sastre, A.4
  • 197
    • 33744943788 scopus 로고    scopus 로고
    • Blocking of interferon-induced Jak-Stat signaling by Japanese encephalitis virus NS5 through a protein tyrosine phosphatase-mediated mechanism
    • Lin R.J., Chang B.L., Yu H.P., Liao C.L., Lin Y.L. Blocking of interferon-induced Jak-Stat signaling by Japanese encephalitis virus NS5 through a protein tyrosine phosphatase-mediated mechanism. J. Virol. 2006, 80:5908-5918.
    • (2006) J. Virol. , vol.80 , pp. 5908-5918
    • Lin, R.J.1    Chang, B.L.2    Yu, H.P.3    Liao, C.L.4    Lin, Y.L.5
  • 198
    • 38849166538 scopus 로고    scopus 로고
    • Tick-borne encephalitis virus NS5 associates with membrane protein scribble and impairs interferon-stimulated JAK-STAT signalling
    • Werme K., Wigerius M., Johansson M. Tick-borne encephalitis virus NS5 associates with membrane protein scribble and impairs interferon-stimulated JAK-STAT signalling. Cell. Microbiol. 2008, 10:696-712.
    • (2008) Cell. Microbiol. , vol.10 , pp. 696-712
    • Werme, K.1    Wigerius, M.2    Johansson, M.3
  • 199
    • 84863158653 scopus 로고    scopus 로고
    • Activation of the Ras/Raf/MEK pathway facilitates hepatitis C virus replication via attenuation of the interferon-JAK-STAT pathway
    • Zhang Q., Gong R., Qu J., Zhou Y., Liu W., Chen M., et al. Activation of the Ras/Raf/MEK pathway facilitates hepatitis C virus replication via attenuation of the interferon-JAK-STAT pathway. J. Virol. 2012, 86:1544-1554.
    • (2012) J. Virol. , vol.86 , pp. 1544-1554
    • Zhang, Q.1    Gong, R.2    Qu, J.3    Zhou, Y.4    Liu, W.5    Chen, M.6
  • 200
    • 0032824134 scopus 로고    scopus 로고
    • Expression of hepatitis C virus proteins inhibits signal transduction through the Jak-STAT pathway
    • Heim M.H., Moradpour D., Blum H.E. Expression of hepatitis C virus proteins inhibits signal transduction through the Jak-STAT pathway. J. Virol. 1999, 73:8469-8475.
    • (1999) J. Virol. , vol.73 , pp. 8469-8475
    • Heim, M.H.1    Moradpour, D.2    Blum, H.E.3
  • 201
    • 0037362931 scopus 로고    scopus 로고
    • IFN-alpha antagonistic activity of HCV core protein involves induction of suppressor of cytokine signaling-3
    • Bode J.G., Ludwig S., Ehrhardt C., Albrecht U., Erhardt A., Schaper F., et al. IFN-alpha antagonistic activity of HCV core protein involves induction of suppressor of cytokine signaling-3. FASEB J. 2003, 17:488-490.
    • (2003) FASEB J. , vol.17 , pp. 488-490
    • Bode, J.G.1    Ludwig, S.2    Ehrhardt, C.3    Albrecht, U.4    Erhardt, A.5    Schaper, F.6
  • 202
    • 34548648264 scopus 로고    scopus 로고
    • HCV structural proteins interfere with interferon-alpha Jak/STAT signalling pathway
    • Luquin E., Larrea E., Civeira M.P., Prieto J., Aldabe R. HCV structural proteins interfere with interferon-alpha Jak/STAT signalling pathway. Antiviral Res. 2007, 76:194-197.
    • (2007) Antiviral Res. , vol.76 , pp. 194-197
    • Luquin, E.1    Larrea, E.2    Civeira, M.P.3    Prieto, J.4    Aldabe, R.5
  • 203
    • 0036435567 scopus 로고    scopus 로고
    • Expression of HCV structural proteins impairs IFN-mediated antiviral response
    • Keskinen P., Melen K., Julkunen I. Expression of HCV structural proteins impairs IFN-mediated antiviral response. Virology 2002, 299:164-171.
    • (2002) Virology , vol.299 , pp. 164-171
    • Keskinen, P.1    Melen, K.2    Julkunen, I.3
  • 204
    • 61449133987 scopus 로고    scopus 로고
    • Identification of the nonstructural protein 4B of hepatitis C virus as a factor that inhibits the antiviral activity of interferon-alpha
    • Xu J., Liu S., Xu Y., Tien P., Gao G. Identification of the nonstructural protein 4B of hepatitis C virus as a factor that inhibits the antiviral activity of interferon-alpha. Virus Res. 2009, 141:55-62.
    • (2009) Virus Res. , vol.141 , pp. 55-62
    • Xu, J.1    Liu, S.2    Xu, Y.3    Tien, P.4    Gao, G.5
  • 205
    • 0346100572 scopus 로고    scopus 로고
    • Hepatitis C virus inhibits interferon signaling through up-regulation of protein phosphatase 2A
    • Duong F.H., Filipowicz M., Tripodi M., La Monica N., Heim M.H. Hepatitis C virus inhibits interferon signaling through up-regulation of protein phosphatase 2A. Gastroenterology 2004, 126:263-277.
    • (2004) Gastroenterology , vol.126 , pp. 263-277
    • Duong, F.H.1    Filipowicz, M.2    Tripodi, M.3    La Monica, N.4    Heim, M.H.5
  • 206
    • 70349245146 scopus 로고    scopus 로고
    • Intracellular innate immune cascades and interferon defenses that control hepatitis C virus
    • Horner S.M., Gale M. Intracellular innate immune cascades and interferon defenses that control hepatitis C virus. J. Interferon Cytokine Res. 2009, 29:489-498.
    • (2009) J. Interferon Cytokine Res. , vol.29 , pp. 489-498
    • Horner, S.M.1    Gale, M.2
  • 207
    • 34047174776 scopus 로고    scopus 로고
    • HCV NS5A inhibits interferon-alpha signaling through suppression of STAT1 phosphorylation in hepatocyte-derived cell lines
    • Lan K.H., Lan K.L., Lee W.P., Sheu M.L., Chen M.Y., Lee Y.L., et al. HCV NS5A inhibits interferon-alpha signaling through suppression of STAT1 phosphorylation in hepatocyte-derived cell lines. J. Hepatol. 2007, 46:759-767.
    • (2007) J. Hepatol. , vol.46 , pp. 759-767
    • Lan, K.H.1    Lan, K.L.2    Lee, W.P.3    Sheu, M.L.4    Chen, M.Y.5    Lee, Y.L.6
  • 208
    • 37149040796 scopus 로고    scopus 로고
    • Ebola virus VP24 proteins inhibit the interaction of NPI-1 subfamily karyopherin alpha proteins with activated STAT1
    • Reid S.P., Valmas C., Martinez O., Sanchez F.M., Basler C.F. Ebola virus VP24 proteins inhibit the interaction of NPI-1 subfamily karyopherin alpha proteins with activated STAT1. J. Virol. 2007, 81:13469-13477.
    • (2007) J. Virol. , vol.81 , pp. 13469-13477
    • Reid, S.P.1    Valmas, C.2    Martinez, O.3    Sanchez, F.M.4    Basler, C.F.5
  • 209
    • 73849109409 scopus 로고    scopus 로고
    • Ebolavirus VP24 binding to karyopherins is required for inhibition of interferon signaling
    • Mateo M., Reid S.P., Leung L.W., Basler C.F., Volchkov V.E. Ebolavirus VP24 binding to karyopherins is required for inhibition of interferon signaling. J. Virol. 2010, 84:1169-1175.
    • (2010) J. Virol. , vol.84 , pp. 1169-1175
    • Mateo, M.1    Reid, S.P.2    Leung, L.W.3    Basler, C.F.4    Volchkov, V.E.5
  • 210
    • 84908332680 scopus 로고    scopus 로고
    • Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to selectively compete with nuclear import of phosphorylated STAT1
    • Xu W., Edwards M.R., Borek D.M., Feagins A.R., Mittal A., Alinger J.B., et al. Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to selectively compete with nuclear import of phosphorylated STAT1. Cell Host Microbe. 2014, 16:187-200.
    • (2014) Cell Host Microbe. , vol.16 , pp. 187-200
    • Xu, W.1    Edwards, M.R.2    Borek, D.M.3    Feagins, A.R.4    Mittal, A.5    Alinger, J.B.6
  • 211
    • 84860903741 scopus 로고    scopus 로고
    • The ebola virus interferon antagonist VP24 directly binds STAT1 and has a novel, pyramidal fold
    • Zhang A.P., Bornholdt Z.A., Liu T., Abelson D.M., Lee D.E., Li S., et al. The ebola virus interferon antagonist VP24 directly binds STAT1 and has a novel, pyramidal fold. PLoS Pathog. 2012, 8:e1002550.
    • (2012) PLoS Pathog. , vol.8 , pp. e1002550
    • Zhang, A.P.1    Bornholdt, Z.A.2    Liu, T.3    Abelson, D.M.4    Lee, D.E.5    Li, S.6
  • 212
    • 77649195743 scopus 로고    scopus 로고
    • Marburg virus evades interferon responses by a mechanism distinct from ebola virus
    • Valmas C., Grosch M.N., Schumann M., Olejnik J., Martinez O., Best S.M., et al. Marburg virus evades interferon responses by a mechanism distinct from ebola virus. PLoS Pathog. 2010, 6:e1000721.
    • (2010) PLoS Pathog. , vol.6 , pp. e1000721
    • Valmas, C.1    Grosch, M.N.2    Schumann, M.3    Olejnik, J.4    Martinez, O.5    Best, S.M.6
  • 213
    • 84979854929 scopus 로고    scopus 로고
    • Super-infection with Staphylococcus aureus inhibits influenza virus-induced type I IFN signaling through impaired STAT1-STAT2 dimerization
    • Warnking K., Klemm C., Loffler B., Niemann S., van Kruchten A., Peters G., et al. Super-infection with Staphylococcus aureus inhibits influenza virus-induced type I IFN signaling through impaired STAT1-STAT2 dimerization. Cell. Microbiol. 2014.
    • (2014) Cell. Microbiol.
    • Warnking, K.1    Klemm, C.2    Loffler, B.3    Niemann, S.4    van Kruchten, A.5    Peters, G.6
  • 215
    • 0034177513 scopus 로고    scopus 로고
    • Lactobacilli and Streptococci activate NF-kappa B and STAT signaling pathways in human macrophages
    • Miettinen M., Lehtonen A., Julkunen I., Matikainen S. Lactobacilli and Streptococci activate NF-kappa B and STAT signaling pathways in human macrophages. J. Immunol. 2000, 164:3733-3740.
    • (2000) J. Immunol. , vol.164 , pp. 3733-3740
    • Miettinen, M.1    Lehtonen, A.2    Julkunen, I.3    Matikainen, S.4
  • 216
    • 84898728217 scopus 로고    scopus 로고
    • Interferon-stimulated genes: roles in viral pathogenesis
    • Schoggins J.W. Interferon-stimulated genes: roles in viral pathogenesis. Curr. Opin. Virol. 2014, 6:40-46.
    • (2014) Curr. Opin. Virol. , vol.6 , pp. 40-46
    • Schoggins, J.W.1
  • 217
    • 84871253668 scopus 로고    scopus 로고
    • Host restriction factors in retroviral infection: promises in virus-host interaction
    • Zheng Y.H., Jeang K.T., Tokunaga K. Host restriction factors in retroviral infection: promises in virus-host interaction. Retrovirology 2012, 9:112.
    • (2012) Retrovirology , vol.9 , pp. 112
    • Zheng, Y.H.1    Jeang, K.T.2    Tokunaga, K.3
  • 218
    • 84863115198 scopus 로고    scopus 로고
    • Intrinsic antiviral immunity
    • Yan N., Chen Z.J. Intrinsic antiviral immunity. Nat. Immunol. 2012, 13:214-222.
    • (2012) Nat. Immunol. , vol.13 , pp. 214-222
    • Yan, N.1    Chen, Z.J.2
  • 219
    • 84866740475 scopus 로고    scopus 로고
    • Evolutionary conflicts between viruses and restriction factors shape immunity
    • Duggal N.K., Emerman M. Evolutionary conflicts between viruses and restriction factors shape immunity. Nat. Rev. Immunol. 2012, 12:687-695.
    • (2012) Nat. Rev. Immunol. , vol.12 , pp. 687-695
    • Duggal, N.K.1    Emerman, M.2
  • 220
    • 80053616925 scopus 로고    scopus 로고
    • Protein kinase PKR and RNA adenosine deaminase ADAR1: new roles for old players as modulators of the interferon response
    • Pfaller C.K., Li Z., George C.X., Samuel C.E. Protein kinase PKR and RNA adenosine deaminase ADAR1: new roles for old players as modulators of the interferon response. Curr. Opin. Immunol. 2011, 23:573-582.
    • (2011) Curr. Opin. Immunol. , vol.23 , pp. 573-582
    • Pfaller, C.K.1    Li, Z.2    George, C.X.3    Samuel, C.E.4
  • 221
    • 34347225099 scopus 로고    scopus 로고
    • The dsRNA protein kinase PKR: virus and cell control
    • Garcia M.A., Meurs E.F., Esteban M. The dsRNA protein kinase PKR: virus and cell control. Biochimie 2007, 89:799-811.
    • (2007) Biochimie , vol.89 , pp. 799-811
    • Garcia, M.A.1    Meurs, E.F.2    Esteban, M.3
  • 223
    • 77954947916 scopus 로고    scopus 로고
    • Activation of the antiviral kinase PKR and viral countermeasures
    • Dauber B., Wolff T. Activation of the antiviral kinase PKR and viral countermeasures. Viruses 2009, 1:523-544.
    • (2009) Viruses , vol.1 , pp. 523-544
    • Dauber, B.1    Wolff, T.2
  • 226
    • 75149139029 scopus 로고    scopus 로고
    • Hepatitis C virus blocks interferon effector function by inducing protein kinase R phosphorylation
    • Garaigorta U., Chisari F.V. Hepatitis C virus blocks interferon effector function by inducing protein kinase R phosphorylation. Cell Host Microbe. 2009, 6:513-522.
    • (2009) Cell Host Microbe. , vol.6 , pp. 513-522
    • Garaigorta, U.1    Chisari, F.V.2
  • 227
    • 84859432807 scopus 로고    scopus 로고
    • Failure of innate and adaptive immune responses in controlling hepatitis C virus infection
    • Thimme R., Binder M., Bartenschlager R. Failure of innate and adaptive immune responses in controlling hepatitis C virus infection. FEMS Microbiol. Rev. 2012, 36:663-683.
    • (2012) FEMS Microbiol. Rev. , vol.36 , pp. 663-683
    • Thimme, R.1    Binder, M.2    Bartenschlager, R.3
  • 228
    • 84869015272 scopus 로고    scopus 로고
    • Blocking double-stranded RNA-activated protein kinase PKR by Japanese encephalitis virus nonstructural protein 2A
    • Tu Y.C., Yu C.Y., Liang J.J., Lin E., Liao C.L., Lin Y.L. Blocking double-stranded RNA-activated protein kinase PKR by Japanese encephalitis virus nonstructural protein 2A. J. Virol. 2012, 86:10347-10358.
    • (2012) J. Virol. , vol.86 , pp. 10347-10358
    • Tu, Y.C.1    Yu, C.Y.2    Liang, J.J.3    Lin, E.4    Liao, C.L.5    Lin, Y.L.6
  • 229
    • 69249205651 scopus 로고    scopus 로고
    • Ebola virus VP35 antagonizes PKR activity through its C-terminal interferon inhibitory domain
    • Schumann M., Gantke T., Muhlberger E. Ebola virus VP35 antagonizes PKR activity through its C-terminal interferon inhibitory domain. J. Virol. 2009, 83:8993-8997.
    • (2009) J. Virol. , vol.83 , pp. 8993-8997
    • Schumann, M.1    Gantke, T.2    Muhlberger, E.3
  • 230
    • 33845728488 scopus 로고    scopus 로고
    • The VP35 protein of Ebola virus inhibits the antiviral effect mediated by double-stranded RNA-dependent protein kinase PKR
    • Feng Z., Cerveny M., Yan Z., He B. The VP35 protein of Ebola virus inhibits the antiviral effect mediated by double-stranded RNA-dependent protein kinase PKR. J. Virol. 2007, 81:182-192.
    • (2007) J. Virol. , vol.81 , pp. 182-192
    • Feng, Z.1    Cerveny, M.2    Yan, Z.3    He, B.4
  • 231
    • 33646748294 scopus 로고    scopus 로고
    • Ebola virus VP35 protein binds double-stranded RNA and inhibits alpha/beta interferon production induced by RIG-I signaling
    • Cardenas W.B., Loo Y.M., Gale M., Hartman A.L., Kimberlin C.R., Martinez-Sobrido L., et al. Ebola virus VP35 protein binds double-stranded RNA and inhibits alpha/beta interferon production induced by RIG-I signaling. J. Virol. 2006, 80:5168-5178.
    • (2006) J. Virol. , vol.80 , pp. 5168-5178
    • Cardenas, W.B.1    Loo, Y.M.2    Gale, M.3    Hartman, A.L.4    Kimberlin, C.R.5    Martinez-Sobrido, L.6
  • 232
    • 84880445500 scopus 로고    scopus 로고
    • Mutual antagonism between the Ebola virus VP35 protein and the RIG-I activator PACT determines infection outcome
    • Luthra P., Ramanan P., Mire C.E., Weisend C., Tsuda Y., Yen B., et al. Mutual antagonism between the Ebola virus VP35 protein and the RIG-I activator PACT determines infection outcome. Cell Host Microbe. 2013, 14:74-84.
    • (2013) Cell Host Microbe. , vol.14 , pp. 74-84
    • Luthra, P.1    Ramanan, P.2    Mire, C.E.3    Weisend, C.4    Tsuda, Y.5    Yen, B.6
  • 233
    • 79551616928 scopus 로고    scopus 로고
    • Multiple levels of PKR inhibition during HIV-1 replication
    • Clerzius G., Gelinas J.F., Gatignol A. Multiple levels of PKR inhibition during HIV-1 replication. Rev. Med. Virol. 2011, 21:42-53.
    • (2011) Rev. Med. Virol. , vol.21 , pp. 42-53
    • Clerzius, G.1    Gelinas, J.F.2    Gatignol, A.3
  • 234
    • 84883652077 scopus 로고    scopus 로고
    • The PKR activator, PACT, becomes a PKR inhibitor during HIV-1 replication
    • Clerzius G., Shaw E., Daher A., Burugu S., Gelinas J.F., Ear T., et al. The PKR activator, PACT, becomes a PKR inhibitor during HIV-1 replication. Retrovirology 2013, 10:96.
    • (2013) Retrovirology , vol.10 , pp. 96
    • Clerzius, G.1    Shaw, E.2    Daher, A.3    Burugu, S.4    Gelinas, J.F.5    Ear, T.6
  • 235
    • 84914176391 scopus 로고    scopus 로고
    • HIV-1 translation and its regulation by cellular factors PKR and PACT
    • Burugu S., Daher A., Meurs E.F., Gatignol A. HIV-1 translation and its regulation by cellular factors PKR and PACT. Virus Res. 2014.
    • (2014) Virus Res.
    • Burugu, S.1    Daher, A.2    Meurs, E.F.3    Gatignol, A.4
  • 236
    • 84888016188 scopus 로고    scopus 로고
    • The antiviral activities of ISG15
    • Morales D.J., Lenschow D.J. The antiviral activities of ISG15. J. Mol. Biol. 2013, 425:4995-5008.
    • (2013) J. Mol. Biol. , vol.425 , pp. 4995-5008
    • Morales, D.J.1    Lenschow, D.J.2
  • 237
    • 84875854073 scopus 로고    scopus 로고
    • Interferon-induced ISG15 pathway: an ongoing virus-host battle
    • Zhao C., Collins M.N., Hsiang T.Y., Krug R.M. Interferon-induced ISG15 pathway: an ongoing virus-host battle. Trends Microbiol. 2013, 21:181-186.
    • (2013) Trends Microbiol. , vol.21 , pp. 181-186
    • Zhao, C.1    Collins, M.N.2    Hsiang, T.Y.3    Krug, R.M.4
  • 238
    • 77951991690 scopus 로고    scopus 로고
    • Positive regulation of interferon regulatory factor 3 activation by Herc5 via ISG15 modification
    • Shi H.X., Yang K., Liu X., Liu X.Y., Wei B., Shan Y.F., et al. Positive regulation of interferon regulatory factor 3 activation by Herc5 via ISG15 modification. Mol. Cell. Biol. 2010, 30:2424-2436.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 2424-2436
    • Shi, H.X.1    Yang, K.2    Liu, X.3    Liu, X.Y.4    Wei, B.5    Shan, Y.F.6
  • 239
    • 77953114765 scopus 로고    scopus 로고
    • The ISG15 conjugation system broadly targets newly synthesized proteins: implications for the antiviral function of ISG15
    • Durfee L.A., Lyon N., Seo K., Huibregtse J.M. The ISG15 conjugation system broadly targets newly synthesized proteins: implications for the antiviral function of ISG15. Mol. Cell 2010, 38:722-732.
    • (2010) Mol. Cell , vol.38 , pp. 722-732
    • Durfee, L.A.1    Lyon, N.2    Seo, K.3    Huibregtse, J.M.4
  • 240
    • 41649084195 scopus 로고    scopus 로고
    • ISG15 inhibits Ebola VP40 VLP budding in an L-domain-dependent manner by blocking Nedd4 ligase activity
    • Okumura A., Pitha P.M., Harty R.N. ISG15 inhibits Ebola VP40 VLP budding in an L-domain-dependent manner by blocking Nedd4 ligase activity. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:3974-3979.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 3974-3979
    • Okumura, A.1    Pitha, P.M.2    Harty, R.N.3
  • 241
    • 31944435603 scopus 로고    scopus 로고
    • Innate antiviral response targets HIV-1 release by the induction of ubiquitin-like protein ISG15
    • Okumura A., Lu G., Pitha-Rowe I., Pitha P.M. Innate antiviral response targets HIV-1 release by the induction of ubiquitin-like protein ISG15. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:1440-1445.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 1440-1445
    • Okumura, A.1    Lu, G.2    Pitha-Rowe, I.3    Pitha, P.M.4
  • 242
    • 29744463886 scopus 로고    scopus 로고
    • The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme
    • Lindner H.A., Fotouhi-Ardakani N., Lytvyn V., Lachance P., Sulea T., Menard R. The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme. J. Virol. 2005, 79:15199-15208.
    • (2005) J. Virol. , vol.79 , pp. 15199-15208
    • Lindner, H.A.1    Fotouhi-Ardakani, N.2    Lytvyn, V.3    Lachance, P.4    Sulea, T.5    Menard, R.6
  • 243
    • 77950806384 scopus 로고    scopus 로고
    • Deubiquitinating and interferon antagonism activities of coronavirus papain-like proteases
    • Clementz M.A., Chen Z., Banach B.S., Wang Y., Sun L., Ratia K., et al. Deubiquitinating and interferon antagonism activities of coronavirus papain-like proteases. J. Virol. 2010, 84:4619-4629.
    • (2010) J. Virol. , vol.84 , pp. 4619-4629
    • Clementz, M.A.1    Chen, Z.2    Banach, B.S.3    Wang, Y.4    Sun, L.5    Ratia, K.6
  • 244
    • 84901670584 scopus 로고    scopus 로고
    • Structural basis for the ubiquitin-linkage specificity and deISGylating activity of SARS-CoV papain-like protease
    • Ratia K., Kilianski A., Baez-Santos Y.M., Baker S.C., Mesecar A. Structural basis for the ubiquitin-linkage specificity and deISGylating activity of SARS-CoV papain-like protease. PLoS Pathog. 2014, 10:e1004113.
    • (2014) PLoS Pathog. , vol.10 , pp. e1004113
    • Ratia, K.1    Kilianski, A.2    Baez-Santos, Y.M.3    Baker, S.C.4    Mesecar, A.5
  • 245
    • 77958142546 scopus 로고    scopus 로고
    • Inhibition of hepatitis C virus replication by IFN-mediated ISGylation of HCV-NS5A
    • Kim M.J., Yoo J.Y. Inhibition of hepatitis C virus replication by IFN-mediated ISGylation of HCV-NS5A. J. Immunol. 2010, 185:4311-4318.
    • (2010) J. Immunol. , vol.185 , pp. 4311-4318
    • Kim, M.J.1    Yoo, J.Y.2
  • 246
    • 77954726570 scopus 로고    scopus 로고
    • The interferon stimulated gene 15 functions as a proviral factor for the hepatitis C virus and as a regulator of the IFN response
    • Broering R., Zhang X., Kottilil S., Trippler M., Jiang M., Lu M., et al. The interferon stimulated gene 15 functions as a proviral factor for the hepatitis C virus and as a regulator of the IFN response. Gut 2010, 59:1111-1119.
    • (2010) Gut , vol.59 , pp. 1111-1119
    • Broering, R.1    Zhang, X.2    Kottilil, S.3    Trippler, M.4    Jiang, M.5    Lu, M.6
  • 247
    • 76249129136 scopus 로고    scopus 로고
    • ISG15, a ubiquitin-like interferon-stimulated gene, promotes hepatitis C virus production in vitro: implications for chronic infection and response to treatment
    • Chen L., Sun J., Meng L., Heathcote J., Edwards A.M., McGilvray I.D. ISG15, a ubiquitin-like interferon-stimulated gene, promotes hepatitis C virus production in vitro: implications for chronic infection and response to treatment. J. Gen. Virol. 2010, 91:382-388.
    • (2010) J. Gen. Virol. , vol.91 , pp. 382-388
    • Chen, L.1    Sun, J.2    Meng, L.3    Heathcote, J.4    Edwards, A.M.5    McGilvray, I.D.6
  • 249
    • 84910640644 scopus 로고    scopus 로고
    • Activation of endogenous type I IFN signaling contributes to persistent HCV infection
    • Li Y., Li S., Duan X., Liu B., Yang C., Zeng P., et al. Activation of endogenous type I IFN signaling contributes to persistent HCV infection. Rev. Med. Virol. 2014, 24:332-342.
    • (2014) Rev. Med. Virol. , vol.24 , pp. 332-342
    • Li, Y.1    Li, S.2    Duan, X.3    Liu, B.4    Yang, C.5    Zeng, P.6
  • 250
    • 84905049001 scopus 로고    scopus 로고
    • Contribution of increased ISG15, ISGylation and deregulated type I IFN signaling in Usp18 mutant mice during the course of bacterial infections
    • Dauphinee S.M., Richer E., Eva M.M., McIntosh F., Paquet M., Dangoor D., et al. Contribution of increased ISG15, ISGylation and deregulated type I IFN signaling in Usp18 mutant mice during the course of bacterial infections. Genes Immun. 2014, 15:282-292.
    • (2014) Genes Immun. , vol.15 , pp. 282-292
    • Dauphinee, S.M.1    Richer, E.2    Eva, M.M.3    McIntosh, F.4    Paquet, M.5    Dangoor, D.6
  • 251
    • 84906088413 scopus 로고    scopus 로고
    • Type I IFN signaling triggers immunopathology in tuberculosis-susceptible mice by modulating lung phagocyte dynamics
    • Dorhoi A., Yeremeev V., Nouailles G., Weiner J., Jorg S., Heinemann E., et al. Type I IFN signaling triggers immunopathology in tuberculosis-susceptible mice by modulating lung phagocyte dynamics. Eur. J. Immunol. 2014, 44:2380-2393.
    • (2014) Eur. J. Immunol. , vol.44 , pp. 2380-2393
    • Dorhoi, A.1    Yeremeev, V.2    Nouailles, G.3    Weiner, J.4    Jorg, S.5    Heinemann, E.6
  • 252
    • 84866686896 scopus 로고    scopus 로고
    • Genome-wide expression profiling identifies type 1 interferon response pathways in active tuberculosis
    • Ottenhoff T.H., Dass R.H., Yang N., Zhang M.M., Wong H.E., Sahiratmadja E., et al. Genome-wide expression profiling identifies type 1 interferon response pathways in active tuberculosis. PloS One 2012, 7:e45839.
    • (2012) PloS One , vol.7 , pp. e45839
    • Ottenhoff, T.H.1    Dass, R.H.2    Yang, N.3    Zhang, M.M.4    Wong, H.E.5    Sahiratmadja, E.6
  • 253
    • 77955894773 scopus 로고    scopus 로고
    • An interferon-inducible neutrophil-driven blood transcriptional signature in human tuberculosis
    • Berry M.P., Graham C.M., McNab F.W., Xu Z., Bloch S.A., Oni T., et al. An interferon-inducible neutrophil-driven blood transcriptional signature in human tuberculosis. Nature 2010, 466:973-977.
    • (2010) Nature , vol.466 , pp. 973-977
    • Berry, M.P.1    Graham, C.M.2    McNab, F.W.3    Xu, Z.4    Bloch, S.A.5    Oni, T.6
  • 255
    • 0038392936 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase and control of intracellular bacterial pathogens
    • Chakravortty D., Hensel M. Inducible nitric oxide synthase and control of intracellular bacterial pathogens. Microbes Infect. 2003, 5:621-627.
    • (2003) Microbes Infect. , vol.5 , pp. 621-627
    • Chakravortty, D.1    Hensel, M.2
  • 256
    • 84919603264 scopus 로고    scopus 로고
    • NADPH oxidases: an overview from structure to innate immunity-associated pathologies
    • Panday A., Sahoo M.K., Osorio D., Batra S. NADPH oxidases: an overview from structure to innate immunity-associated pathologies. Cell. Mol. Immunol. 2014.
    • (2014) Cell. Mol. Immunol.
    • Panday, A.1    Sahoo, M.K.2    Osorio, D.3    Batra, S.4
  • 257
    • 0034095005 scopus 로고    scopus 로고
    • Salmonella pathogenicity island 2-dependent evasion of the phagocyte NADPH oxidase
    • Vazquez-Torres A., Xu Y., Jones-Carson J., Holden D.W., Lucia S.M., Dinauer M.C., et al. Salmonella pathogenicity island 2-dependent evasion of the phagocyte NADPH oxidase. Science 2000, 287:1655-1658.
    • (2000) Science , vol.287 , pp. 1655-1658
    • Vazquez-Torres, A.1    Xu, Y.2    Jones-Carson, J.3    Holden, D.W.4    Lucia, S.M.5    Dinauer, M.C.6
  • 258
    • 0036839654 scopus 로고    scopus 로고
    • Modulation of inducible nitric oxide synthase expression by the attaching and effacing bacterial pathogen Citrobacter rodentium in infected mice
    • Vallance B.A., Deng W., De Grado M., Chan C., Jacobson K., Finlay B.B. Modulation of inducible nitric oxide synthase expression by the attaching and effacing bacterial pathogen Citrobacter rodentium in infected mice. Infect. Immun. 2002, 70:6424-6435.
    • (2002) Infect. Immun. , vol.70 , pp. 6424-6435
    • Vallance, B.A.1    Deng, W.2    De Grado, M.3    Chan, C.4    Jacobson, K.5    Finlay, B.B.6
  • 259
    • 84883398813 scopus 로고    scopus 로고
    • Rational design of a live attenuated dengue vaccine: 2'-O-methyltransferase mutants are highly attenuated and immunogenic in mice and macaques
    • Zust R., Dong H., Li X.F., Chang D.C., Zhang B., Balakrishnan T., et al. Rational design of a live attenuated dengue vaccine: 2'-O-methyltransferase mutants are highly attenuated and immunogenic in mice and macaques. PLoS Pathog. 2013, 9:e1003521.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003521
    • Zust, R.1    Dong, H.2    Li, X.F.3    Chang, D.C.4    Zhang, B.5    Balakrishnan, T.6
  • 260
    • 84899039853 scopus 로고    scopus 로고
    • Role of type I interferons in inflammasome activation, cell death, and disease during microbial infection
    • Malireddi R.K., Kanneganti T.D. Role of type I interferons in inflammasome activation, cell death, and disease during microbial infection. Front. Cell. Infect. Microbiol. 2013, 3:77.
    • (2013) Front. Cell. Infect. Microbiol. , vol.3 , pp. 77
    • Malireddi, R.K.1    Kanneganti, T.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.