메뉴 건너뛰기




Volumn 86, Issue 17, 2012, Pages 9311-9322

Foot-and-mouth disease virus 3C protease cleaves NEMO to impair innate immune signaling

Author keywords

[No Author keywords available]

Indexed keywords

2',5' OLIGOADENYLATE SYNTHETASE; ALPHA1 INTERFERON; BETA INTERFERON; DOUBLE STRANDED RNA; GAMMA INTERFERON INDUCIBLE PROTEIN 10; I KAPPA B KINASE GAMMA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON REGULATORY FACTOR 3; INTERFERON STIMULATED GENE 54 PROTEIN; INTERLEUKIN 1BETA; INTERLEUKIN 6; MESSENGER RNA; PROTEINASE; PROTEINASE 3C; RANTES; RETINOIC ACID INDUCIBLE PROTEIN I; TRANSCRIPTION FACTOR; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN;

EID: 84866144289     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00722-12     Document Type: Article
Times cited : (131)

References (61)
  • 1
    • 77955109451 scopus 로고    scopus 로고
    • A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response
    • Ashida H, et al. 2010. A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response. Nat. Cell Biol. 12: 66-73.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 66-73
    • Ashida, H.1
  • 2
    • 34247127075 scopus 로고    scopus 로고
    • MDA-5 is cleaved in poliovirus-infected cells
    • Barral PM, et al. 2007. MDA-5 is cleaved in poliovirus-infected cells. J. Virol. 81: 3677-3684.
    • (2007) J. Virol. , vol.81 , pp. 3677-3684
    • Barral, P.M.1
  • 4
    • 0037744789 scopus 로고    scopus 로고
    • The Ebola virus VP35 protein inhibits activation of interferon regulatory factor 3
    • Basler CF, et al. 2003. The Ebola virus VP35 protein inhibits activation of interferon regulatory factor 3. J. Virol. 77: 7945-7956.
    • (2003) J. Virol. , vol.77 , pp. 7945-7956
    • Basler, C.F.1
  • 5
    • 0033988512 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells
    • Belsham GJ, McInerney GM, Ross-Smith N. 2000. Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells. J. Virol. 74: 272-280.
    • (2000) J. Virol. , vol.74 , pp. 272-280
    • Belsham, G.J.1    McInerney, G.M.2    Ross-Smith, N.3
  • 6
    • 15744372994 scopus 로고    scopus 로고
    • Crystal structure of foot-and-mouth disease virus 3C protease. New insights into catalytic mechanism and cleavage specificity
    • Birtley JR, et al. 2005. Crystal structure of foot-and-mouth disease virus 3C protease. New insights into catalytic mechanism and cleavage specificity. J. Biol. Chem. 280: 11520-11527.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11520-11527
    • Birtley, J.R.1
  • 7
    • 39549103042 scopus 로고    scopus 로고
    • Signal processing by its coil zipper domain activates IKK gamma
    • Bloor S, et al. 2008. Signal processing by its coil zipper domain activates IKK gamma. Proc. Natl. Acad. Sci. U. S. A. 105: 1279-1284.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 1279-1284
    • Bloor, S.1
  • 8
    • 34548566398 scopus 로고    scopus 로고
    • Ubiquitination and proteasomal degradation of interferon regulatory factor-3 induced by Npro from a cytopathic bovine viral diarrhea virus
    • Chen Z, et al. 2007. Ubiquitination and proteasomal degradation of interferon regulatory factor-3 induced by Npro from a cytopathic bovine viral diarrhea virus. Virology 366: 277-292.
    • (2007) Virology , vol.366 , pp. 277-292
    • Chen, Z.1
  • 9
    • 0032731093 scopus 로고    scopus 로고
    • Ability of foot-andmouth disease virus to form plaques in cell culture is associated with suppression of alpha/beta interferon
    • Chinsangaram J, Piccone ME, Grubman MJ. 1999. Ability of foot-andmouth disease virus to form plaques in cell culture is associated with suppression of alpha/beta interferon. J. Virol. 73: 9891-9898.
    • (1999) J. Virol. , vol.73 , pp. 9891-9898
    • Chinsangaram, J.1    Piccone, M.E.2    Grubman, M.J.3
  • 10
    • 77950806384 scopus 로고    scopus 로고
    • Deubiquitinating and interferon antagonism activities of coronavirus papain-like proteases
    • Clementz MA, et al. 2010. Deubiquitinating and interferon antagonism activities of coronavirus papain-like proteases. J. Virol. 84: 4619-4629.
    • (2010) J. Virol , vol.84 , pp. 4619-4629
    • Clementz, M.A.1
  • 11
    • 32444446676 scopus 로고    scopus 로고
    • The leader proteinase of foot-and-mouth disease virus inhibits the induction of beta interferon mRNA and blocks the host innate immune response
    • de Los Santos T, de Avila Botton S, Weiblen R, Grubman MJ. 2006. The leader proteinase of foot-and-mouth disease virus inhibits the induction of beta interferon mRNA and blocks the host innate immune response. J. Virol. 80: 1906-1914.
    • (2006) J. Virol , vol.80 , pp. 1906-1914
    • de Los Santos, T.1    de Avila Botton, S.2    Weiblen, R.3    Grubman, M.J.4
  • 12
    • 36349008785 scopus 로고    scopus 로고
    • Degradation of nuclear factor kappa B during foot-and-mouth disease virus infection
    • de Los Santos T, Diaz-San Segundo F, Grubman MJ. 2007. Degradation of nuclear factor kappa B during foot-and-mouth disease virus infection. J. Virol. 81: 12803-12815.
    • (2007) J. Virol , vol.81 , pp. 12803-12815
    • de Los Santos, T.1    Diaz-San Segundo, F.2    Grubman, M.J.3
  • 13
    • 59649103610 scopus 로고    scopus 로고
    • A conserved domain in the leader proteinase of foot-and-mouth disease virus is required for proper subcellular localization and function
    • de los Santos T, Segundo FD, Zhu J, Koster M, Dias CC, Grubman MJ. 2009. A conserved domain in the leader proteinase of foot-and-mouth disease virus is required for proper subcellular localization and function. J. Virol. 83: 1800-1810.
    • (2009) J. Virol , vol.83 , pp. 1800-1810
    • de los Santos, T.1    Segundo, F.D.2    Zhu, J.3    Koster, M.4    Dias, C.C.5    Grubman, M.J.6
  • 14
    • 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 SG, et al. 2007. Regulation of IRF-3-dependent innate immunity by the papain-like protease domain of the severe acute respiratory syndrome coronavirus. J. Biol. Chem. 282: 32208-32221.
    • (2007) J. Biol. Chem. , vol.282 , pp. 32208-32221
    • Devaraj, S.G.1
  • 15
    • 79951815029 scopus 로고    scopus 로고
    • Porcine type I interferon rapidly protects swine against challenge with multiple serotypes of foot-and-mouth disease virus
    • Dias CC, Moraes MP, Segundo FD, de los Santos T, Grubman MJ. 2011. Porcine type I interferon rapidly protects swine against challenge with multiple serotypes of foot-and-mouth disease virus. J. Interferon Cytokine Res. 31: 227-236.
    • (2011) J. Interferon Cytokine Res , vol.31 , pp. 227-236
    • Dias, C.C.1    Moraes, M.P.2    Segundo, F.D.3    de los Santos, T.4    Grubman, M.J.5
  • 16
    • 79954629155 scopus 로고    scopus 로고
    • Antiviral activity of bovine type III interferon against foot-and-mouth disease virus
    • Diaz-San Segundo F, et al. 2011. Antiviral activity of bovine type III interferon against foot-and-mouth disease virus. Virology 413: 283-292.
    • (2011) Virology , vol.413 , pp. 283-292
    • Diaz-San Segundo, F.1
  • 17
    • 67449093056 scopus 로고    scopus 로고
    • Biological effect of Muller's Ratchet: distant capsid site can affect picornavirus protein processing
    • Escarmis C, Perales C, Domingo E. 2009. Biological effect of Muller's Ratchet: distant capsid site can affect picornavirus protein processing. J. Virol. 83: 6748-6756.
    • (2009) J. Virol , vol.83 , pp. 6748-6756
    • Escarmis, C.1    Perales, C.2    Domingo, E.3
  • 18
    • 84860901212 scopus 로고    scopus 로고
    • Viral mediated redirection of NEMO/IKKgamma to autophagosomes curtails the inflammatory cascade
    • doi:10.1371/journal.ppat.1002517
    • Fliss PM, et al. 2012. Viral mediated redirection of NEMO/IKKgamma to autophagosomes curtails the inflammatory cascade. PLoS Pathog. 8: e1002517. doi:10.1371/journal.ppat.1002517.
    • (2012) PLoS Pathog , vol.8
    • Fliss, P.M.1
  • 19
    • 0037113946 scopus 로고    scopus 로고
    • Recognition of eukaryotic initiation factor 4G isoforms by picornaviral proteinases
    • Foeger N, Glaser W, Skern T. 2002. Recognition of eukaryotic initiation factor 4G isoforms by picornaviral proteinases. J. Biol. Chem. 277: 44300-44309.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44300-44309
    • Foeger, N.1    Glaser, W.2    Skern, T.3
  • 20
    • 33744791510 scopus 로고    scopus 로고
    • Essential role of mda-5 in type I IFN responses to polyriboinosinic:polyribocytidylic acid and encephalomyocarditis picornavirus
    • Gitlin L, et al. 2006. Essential role of mda-5 in type I IFN responses to polyriboinosinic:polyribocytidylic acid and encephalomyocarditis picornavirus. Proc. Natl. Acad. Sci. U. S. A. 103: 8459-8464.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 8459-8464
    • Gitlin, L.1
  • 21
    • 52049112977 scopus 로고    scopus 로고
    • Immune evasion during foot-andmouth disease virus infection of swine
    • Golde WT, Nfon CK, Toka FN. 2008. Immune evasion during foot-andmouth disease virus infection of swine. Immunol. Rev. 225: 85-95.
    • (2008) Immunol. Rev. , vol.225 , pp. 85-95
    • Golde, W.T.1    Nfon, C.K.2    Toka, F.N.3
  • 24
    • 0028802290 scopus 로고
    • Identification of the active-site residues of the 3C proteinase of foot-andmouth disease virus
    • Grubman MJ, Zellner M, Bablanian G, Mason PW, Piccone ME. 1995. Identification of the active-site residues of the 3C proteinase of foot-andmouth disease virus. Virology 213: 581-589.
    • (1995) Virology , vol.213 , pp. 581-589
    • Grubman, M.J.1    Zellner, M.2    Bablanian, G.3    Mason, P.W.4    Piccone, M.E.5
  • 25
    • 79957604087 scopus 로고    scopus 로고
    • Identification of the role of RIG-I, MDA-5 and TLR3 in sensing RNA viruses in porcine epithelial cells using lentivirus-driven RNA interference
    • Husser L, Alves MP, Ruggli N, Summerfield A. 2011. Identification of the role of RIG-I, MDA-5 and TLR3 in sensing RNA viruses in porcine epithelial cells using lentivirus-driven RNA interference. Virus Res. 159: 9-16.
    • (2011) Virus Res , vol.159 , pp. 9-16
    • Husser, L.1    Alves, M.P.2    Ruggli, N.3    Summerfield, A.4
  • 26
    • 80052143412 scopus 로고    scopus 로고
    • RIG-I-like receptors: cytoplasmic sensors for non-self RNA
    • Kato H, Takahasi K, Fujita T. 2011. RIG-I-like receptors: cytoplasmic sensors for non-self RNA. Immunol. Rev. 243: 91-98.
    • (2011) Immunol. Rev. , vol.243 , pp. 91-98
    • Kato, H.1    Takahasi, K.2    Fujita, T.3
  • 27
    • 33646342149 scopus 로고    scopus 로고
    • Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses
    • Kato H, et al. 2006. Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses. Nature 441: 101-105.
    • (2006) Nature , vol.441 , pp. 101-105
    • Kato, H.1
  • 28
    • 31344461659 scopus 로고    scopus 로고
    • Innate immune recognition of viral infection
    • Kawai T, Akira S. 2006. Innate immune recognition of viral infection. Nat. Immunol. 7: 131-137.
    • (2006) Nat. Immunol. , vol.7 , pp. 131-137
    • Kawai, T.1    Akira, S.2
  • 29
    • 27144440523 scopus 로고    scopus 로고
    • IPS-1, an adaptor triggering RIG-I- and Mda5- mediated type I interferon induction
    • Kawai T, et al. 2005. IPS-1, an adaptor triggering RIG-I- and Mda5- mediated type I interferon induction. Nat. Immunol. 6: 981-988.
    • (2005) Nat. Immunol. , vol.6 , pp. 981-988
    • Kawai, T.1
  • 30
    • 77953028825 scopus 로고    scopus 로고
    • Modulation of type I interferon induction by porcine reproductive and respiratory syndrome virus and degradation of CREB-binding protein by non-structural protein 1 in MARC-145 and HeLa cells
    • Kim O, Sun Y, Lai FW, Song C, Yoo D. 2010. Modulation of type I interferon induction by porcine reproductive and respiratory syndrome virus and degradation of CREB-binding protein by non-structural protein 1 in MARC-145 and HeLa cells. Virology 402: 315-326.
    • (2010) Virology , vol.402 , pp. 315-326
    • Kim, O.1    Sun, Y.2    Lai, F.W.3    Song, C.4    Yoo, D.5
  • 31
    • 0021236936 scopus 로고
    • Biologically active protease of foot and mouth disease virus is expressed from cloned viral cDNA in Escherichia coli
    • Klump W, Marquardt O, Hofschneider PH. 1984. Biologically active protease of foot and mouth disease virus is expressed from cloned viral cDNA in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 81: 3351-3355.
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 3351-3355
    • Klump, W.1    Marquardt, O.2    Hofschneider, P.H.3
  • 32
    • 77955006559 scopus 로고    scopus 로고
    • The 3C protein of enterovirus 71 inhibits retinoid acid-inducible gene I-mediated interferon regulatory factor 3 activation and type I interferon responses
    • Lei X, et al. 2010. The 3C protein of enterovirus 71 inhibits retinoid acid-inducible gene I-mediated interferon regulatory factor 3 activation and type I interferon responses. J. Virol. 84: 8051-8061.
    • (2010) J. Virol , vol.84 , pp. 8051-8061
    • Lei, X.1
  • 33
    • 80052278508 scopus 로고    scopus 로고
    • Cleavage of the adaptor protein TRIF by enterovirus 71 3C inhibits antiviral responses mediated by Toll-like receptor 3
    • Lei X, et al. 2011. Cleavage of the adaptor protein TRIF by enterovirus 71 3C inhibits antiviral responses mediated by Toll-like receptor 3. J. Virol. 85: 8811-8818.
    • (2011) J. Virol , vol.85 , pp. 8811-8818
    • Lei, X.1
  • 34
    • 0036724051 scopus 로고    scopus 로고
    • The carboxyl-terminal region of IkappaB kinase gamma (IKKgamma) is required for full IKK activation
    • Makris C, Roberts JL, Karin M. 2002. The carboxyl-terminal region of IkappaB kinase gamma (IKKgamma) is required for full IKK activation. Mol. Cell. Biol. 22: 6573-6581.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6573-6581
    • Makris, C.1    Roberts, J.L.2    Karin, M.3
  • 35
    • 0037232731 scopus 로고    scopus 로고
    • Molecular basis of pathogenesis of FMDV
    • Mason PW, Grubman MJ, Baxt B. 2003. Molecular basis of pathogenesis of FMDV. Virus Res. 91: 9-32.
    • (2003) Virus Res , vol.91 , pp. 9-32
    • Mason, P.W.1    Grubman, M.J.2    Baxt, B.3
  • 36
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • Meylan E, et al. 2005. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature 437: 1167-1172.
    • (2005) Nature , vol.437 , pp. 1167-1172
    • Meylan, E.1
  • 37
    • 34250840521 scopus 로고    scopus 로고
    • Enhanced antiviral activity against foot-andmouth disease virus by a combination of type I and II porcine interferons
    • Moraes MP, et al. 2007. Enhanced antiviral activity against foot-andmouth disease virus by a combination of type I and II porcine interferons. J. Virol. 81: 7124-7135.
    • (2007) J. Virol , vol.81 , pp. 7124-7135
    • Moraes, M.P.1
  • 38
    • 79953279338 scopus 로고    scopus 로고
    • The coxsackievirus B 3C protease cleaves MAVS and TRIF to attenuate host type I interferon and apoptotic signaling
    • doi:10.1371/journal.ppat.1001311
    • Mukherjee A, et al. 2011. The coxsackievirus B 3C protease cleaves MAVS and TRIF to attenuate host type I interferon and apoptotic signaling. PLoS Pathog. 7: e1001311. doi:10.1371/journal.ppat.1001311.
    • (2011) PLoS Pathog , vol.7
    • Mukherjee, A.1
  • 39
    • 70349807812 scopus 로고    scopus 로고
    • The viral RNA recognition sensor RIG-I is degraded during encephalomyocarditis virus (EMCV) infection
    • Papon L, et al. 2009. The viral RNA recognition sensor RIG-I is degraded during encephalomyocarditis virus (EMCV) infection. Virology 393: 311-318.
    • (2009) Virology , vol.393 , pp. 311-318
    • Papon, L.1
  • 40
    • 79960598740 scopus 로고    scopus 로고
    • Disruption of TLR3 signaling due to cleavage of TRIF by the hepatitis A virus protease-polymerase processing intermediate, 3CD
    • doi:10.1371/journal.ppat.1002169
    • Qu L, et al. 2011. Disruption of TLR3 signaling due to cleavage of TRIF by the hepatitis A virus protease-polymerase processing intermediate, 3CD. PLoS Pathog. 7:e1002169. doi:10.1371/journal.ppat.1002169.
    • (2011) PLoS Pathog , vol.7
    • Qu, L.1
  • 41
    • 33750443289 scopus 로고    scopus 로고
    • IkappaB kinase complexes: gateways to NF-kappaB activation and transcription
    • Scheidereit C. 2006. IkappaB kinase complexes: gateways to NF-kappaB activation and transcription. Oncogene 25: 6685-6705.
    • (2006) Oncogene , vol.25 , pp. 6685-6705
    • Scheidereit, C.1
  • 42
    • 70349750273 scopus 로고    scopus 로고
    • IRF3 inhibition by rotavirus NSP1 is host cell and virus strain dependent but independent of NSP1 proteasomal degradation
    • Sen A, Feng N, Ettayebi K, Hardy ME, Greenberg HB. 2009. IRF3 inhibition by rotavirus NSP1 is host cell and virus strain dependent but independent of NSP1 proteasomal degradation. J. Virol. 83: 10322-10335.
    • (2009) J. Virol , vol.83 , pp. 10322-10335
    • Sen, A.1    Feng, N.2    Ettayebi, K.3    Hardy, M.E.4    Greenberg, H.B.5
  • 43
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3
    • Seth RB, Sun L, Ea CK, Chen ZJ. 2005. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3. Cell 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
  • 44
    • 79958224016 scopus 로고    scopus 로고
    • The nonstructural protein 1 papain-like cysteine protease was necessary for porcine reproductive and respiratory syndrome virus nonstructural protein 1 to inhibit interferon-beta induction
    • Shi X, et al. 2011. The nonstructural protein 1 papain-like cysteine protease was necessary for porcine reproductive and respiratory syndrome virus nonstructural protein 1 to inhibit interferon-beta induction. DNA Cell Biol. 30: 355-362
    • (2011) DNA Cell Biol , vol.30 , pp. 355-362
    • Shi, X.1
  • 45
    • 77957674435 scopus 로고    scopus 로고
    • Nonstructural protein 1alpha subunitbased inhibition of NF-kappaB activation and suppression of interferonbeta production by porcine reproductive and respiratory syndrome virus
    • Song C, Krell P, Yoo D. 2010. Nonstructural protein 1alpha subunitbased inhibition of NF-kappaB activation and suppression of interferonbeta production by porcine reproductive and respiratory syndrome virus. Virology 407: 268-280.
    • (2010) Virology , vol.407 , pp. 268-280
    • Song, C.1    Krell, P.2    Yoo, D.3
  • 46
    • 60549104769 scopus 로고    scopus 로고
    • Innate immune responses against foot-and-mouth disease virus: current understanding and future directions
    • Summerfield A, Guzylack-Piriou L, Harwood L, McCullough KC. 2009. Innate immune responses against foot-and-mouth disease virus: current understanding and future directions. Vet. Immunol. Immunopathol. 128: 205-210.
    • (2009) Vet. Immunol. Immunopathol , vol.128 , pp. 205-210
    • Summerfield, A.1    Guzylack-Piriou, L.2    Harwood, L.3    McCullough, K.C.4
  • 47
    • 77954461006 scopus 로고    scopus 로고
    • The cysteine protease domain of porcine reproductive and respiratory syndrome virus nonstructural protein 2 possesses deubiquitinating and interferon antagonism functions
    • Sun Z, Chen Z, Lawson SR, Fang Y. 2010. The cysteine protease domain of porcine reproductive and respiratory syndrome virus nonstructural protein 2 possesses deubiquitinating and interferon antagonism functions. J. Virol. 84: 7832-7846.
    • (2010) J. Virol , vol.84 , pp. 7832-7846
    • Sun, Z.1    Chen, Z.2    Lawson, S.R.3    Fang, Y.4
  • 48
    • 0023197987 scopus 로고
    • Proteolytic processing of foot-and-mouth disease virus polyproteins expressed in a cell-free system from clone-derived transcripts
    • Vakharia VN, Devaney MA, Moore DM, Dunn JJ, Grubman MJ. 1987. Proteolytic processing of foot-and-mouth disease virus polyproteins expressed in a cell-free system from clone-derived transcripts. J. Virol. 61: 3199-3207.
    • (1987) J. Virol , vol.61 , pp. 3199-3207
    • Vakharia, V.N.1    Devaney, M.A.2    Moore, D.M.3    Dunn, J.J.4    Grubman, M.J.5
  • 49
    • 79952837091 scopus 로고    scopus 로고
    • The leader proteinase of foot-and-mouth disease virus negatively regulates the type I interferon pathway by acting as a viral deubiquitinase
    • Wang D, et al. 2011. The leader proteinase of foot-and-mouth disease virus negatively regulates the type I interferon pathway by acting as a viral deubiquitinase. J. Virol. 85: 3758-3766.
    • (2011) J. Virol , vol.85 , pp. 3758-3766
    • Wang, D.1
  • 50
    • 51549111359 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of porcine IFN-beta promoter stimulator 1 (IPS-1)
    • Wang D, et al. 2008. Molecular cloning and functional characterization of porcine IFN-beta promoter stimulator 1 (IPS-1). Vet. Immunol. Immunopathol. 125: 344-353.
    • (2008) Vet. Immunol. Immunopathol , vol.125 , pp. 344-353
    • Wang, D.1
  • 51
    • 82455218948 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus (FMDV) leader proteinase negatively regulates the porcine interferon-lambda1 pathway
    • Wang D, et al. 2011. Foot-and-mouth disease virus (FMDV) leader proteinase negatively regulates the porcine interferon-lambda1 pathway. Mol. Immunol. 49: 407-412.
    • (2011) Mol. Immunol , vol.49 , pp. 407-412
    • Wang, D.1
  • 52
    • 77955565711 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus leader proteinase inhibits dsRNA-induced type I interferon transcription by decreasing interferon regulatory factor 3/7 in protein levels
    • Wang D, et al. 2010. Foot-and-mouth disease virus leader proteinase inhibits dsRNA-induced type I interferon transcription by decreasing interferon regulatory factor 3/7 in protein levels. Biochem. Biophys. Res. Commun. 399: 72-78.
    • (2010) Biochem. Biophys. Res. Commun. , vol.399 , pp. 72-78
    • Wang, D.1
  • 53
    • 69249212250 scopus 로고    scopus 로고
    • Expression of exogenous IFN-alpha by bypassing the translation block protects cells against FMDV infection
    • Xiong Y, Lin M, Yuan B, Yuan T, Zheng C. 2009. Expression of exogenous IFN-alpha by bypassing the translation block protects cells against FMDV infection. Antiviral Res. 84: 60-66.
    • (2009) Antiviral Res. , vol.84 , pp. 60-66
    • Xiong, Y.1    Lin, M.2    Yuan, B.3    Yuan, T.4    Zheng, C.5
  • 54
    • 24944538819 scopus 로고    scopus 로고
    • VISA is an adapter protein required for virus-triggered IFN-beta signaling
    • Xu LG, et al. 2005. VISA is an adapter protein required for virus-triggered IFN-beta signaling. Mol. Cell 19: 727-740.
    • (2005) Mol. Cell , vol.19 , pp. 727-740
    • Xu, L.G.1
  • 55
    • 0842321781 scopus 로고    scopus 로고
    • The zinc finger mutation C417R of I-kappa B kinase gamma impairs lipopolysaccharide- and TNF-mediated NF-kappa B activation through inhibiting phosphorylation of the I-kappa B kinase beta activation loop
    • Yang F, et al. 2004. The zinc finger mutation C417R of I-kappa B kinase gamma impairs lipopolysaccharide- and TNF-mediated NF-kappa B activation through inhibiting phosphorylation of the I-kappa B kinase beta activation loop. J. Immunol. 172: 2446-2452.
    • (2004) J. Immunol , vol.172 , pp. 2446-2452
    • Yang, F.1
  • 56
    • 34249855382 scopus 로고    scopus 로고
    • Disruption of innate immunity due to mitochondrial targeting of a picornaviral protease precursor
    • Yang Y, et al. 2007. Disruption of innate immunity due to mitochondrial targeting of a picornaviral protease precursor. Proc. Natl. Acad. Sci. U. S. A. 104: 7253-7258.
    • (2007) Proc. Natl. Acad. Sci. U. S. A , vol.104 , pp. 7253-7258
    • Yang, Y.1
  • 57
    • 40949113624 scopus 로고    scopus 로고
    • Porcine interferongamma protects swine from foot-and-mouth disease virus (FMDV)
    • Yao Q, Huang Q, Cao Y, Qian P, Chen H. 2008. Porcine interferongamma protects swine from foot-and-mouth disease virus (FMDV). Vet. Immunol. Immunopathol. 122: 309-311.
    • (2008) Vet. Immunol. Immunopathol , vol.122 , pp. 309-311
    • Yao, Q.1    Huang, Q.2    Cao, Y.3    Qian, P.4    Chen, H.5
  • 58
    • 34548126512 scopus 로고    scopus 로고
    • RIG-I family RNA helicases: cytoplasmic sensor for antiviral innate immunity
    • Yoneyama M, Fujita T. 2007. RIG-I family RNA helicases: cytoplasmic sensor for antiviral innate immunity. Cytokine Growth Factor Rev. 18: 545-551.
    • (2007) Cytokine Growth Factor Rev. , vol.18 , pp. 545-551
    • Yoneyama, M.1    Fujita, T.2
  • 59
    • 77955290279 scopus 로고    scopus 로고
    • Hepatitis B virus polymerase inhibits RIG-I- and Tolllike receptor 3-mediated beta interferon induction in human hepatocytes through interference with interferon regulatory factor 3 activation and dampening of the interaction between TBK1/IKKepsilon and DDX3
    • Yu S, et al. 2010. Hepatitis B virus polymerase inhibits RIG-I- and Tolllike receptor 3-mediated beta interferon induction in human hepatocytes through interference with interferon regulatory factor 3 activation and dampening of the interaction between TBK1/IKKepsilon and DDX3. J. Gen. Virol. 91: 2080-2090.
    • (2010) J. Gen. Virol. , vol.91 , pp. 2080-2090
    • Yu, S.1
  • 60
    • 34249058119 scopus 로고    scopus 로고
    • The NEMO adaptor bridges the nuclear factorkappaB and interferon regulatory factor signaling pathways
    • Zhao T, et al. 2007. The NEMO adaptor bridges the nuclear factorkappaB and interferon regulatory factor signaling pathways. Nat. Immunol. 8: 592-600.
    • (2007) Nat. Immunol , vol.8 , pp. 592-600
    • Zhao, T.1
  • 61
    • 55549102621 scopus 로고    scopus 로고
    • PLP2, a potent deubiquitinase from murine hepatitis virus, strongly inhibits cellular type I interferon production
    • Zheng D, Chen G, Guo B, Cheng G, Tang H. 2008. PLP2, a potent deubiquitinase from murine hepatitis virus, strongly inhibits cellular type I interferon production. Cell Res. 18: 1105-1113.
    • (2008) Cell Res. , vol.18 , pp. 1105-1113
    • Zheng, D.1    Chen, G.2    Guo, B.3    Cheng, G.4    Tang, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.