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Volumn 9, Issue 7, 2013, Pages

Myxoma Virus Protein M029 Is a Dual Function Immunomodulator that Inhibits PKR and Also Conscripts RHA/DHX9 to Promote Expanded Host Tropism and Viral Replication

Author keywords

[No Author keywords available]

Indexed keywords

M029 PROTEIN; PROTEIN KINASE R; RNA HELICASE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84884733748     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1003465     Document Type: Article
Times cited : (54)

References (66)
  • 1
    • 70349260534 scopus 로고    scopus 로고
    • The interferon system and vaccinia virus evasion mechanisms
    • Perdiguero B, Esteban M, (2009) The interferon system and vaccinia virus evasion mechanisms. J Interferon Cytokine Res 29: 581-598.
    • (2009) J Interferon Cytokine Res , vol.29 , pp. 581-598
    • Perdiguero, B.1    Esteban, M.2
  • 3
    • 79957999765 scopus 로고    scopus 로고
    • How vaccinia virus has evolved to subvert the host immune response
    • Bahar MW, Graham SC, Chen RA, Cooray S, Smith GL, et al. (2011) How vaccinia virus has evolved to subvert the host immune response. J Struct Biol 175: 127-134.
    • (2011) J Struct Biol , vol.175 , pp. 127-134
    • Bahar, M.W.1    Graham, S.C.2    Chen, R.A.3    Cooray, S.4    Smith, G.L.5
  • 4
    • 0026751682 scopus 로고
    • The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNA-dependent protein kinase
    • Chang HW, Watson JC, Jacobs BL, (1992) The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNA-dependent protein kinase. Proc Natl Acad Sci U S A 89: 4825-4829.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 4825-4829
    • Chang, H.W.1    Watson, J.C.2    Jacobs, B.L.3
  • 5
    • 0027407080 scopus 로고
    • The E3L and K3L vaccinia virus gene products stimulate translation through inhibition of the double-stranded RNA-dependent protein kinase by different mechanisms
    • Davies MV, Chang HW, Jacobs BL, Kaufman RJ, (1993) The E3L and K3L vaccinia virus gene products stimulate translation through inhibition of the double-stranded RNA-dependent protein kinase by different mechanisms. J Virol 67: 1688-1692.
    • (1993) J Virol , vol.67 , pp. 1688-1692
    • Davies, M.V.1    Chang, H.W.2    Jacobs, B.L.3    Kaufman, R.J.4
  • 6
    • 0032502728 scopus 로고    scopus 로고
    • Vaccinia virus E3L protein is an inhibitor of the interferon (i.f.n.)-induced 2-5A synthetase enzyme
    • Rivas C, Gil J, Melkova Z, Esteban M, Diaz-Guerra M, (1998) Vaccinia virus E3L protein is an inhibitor of the interferon (i.f.n.)-induced 2-5A synthetase enzyme. Virology 243: 406-414.
    • (1998) Virology , vol.243 , pp. 406-414
    • Rivas, C.1    Gil, J.2    Melkova, Z.3    Esteban, M.4    Diaz-Guerra, M.5
  • 7
    • 78650070662 scopus 로고    scopus 로고
    • Roles of vaccinia virus genes E3L and K3L and host genes PKR and RNase L during intratracheal infection of C57BL/6 mice
    • Rice AD, Turner PC, Embury JE, Moldawer LL, Baker HV, et al. (2011) Roles of vaccinia virus genes E3L and K3L and host genes PKR and RNase L during intratracheal infection of C57BL/6 mice. J Virol 85: 550-567.
    • (2011) J Virol , vol.85 , pp. 550-567
    • Rice, A.D.1    Turner, P.C.2    Embury, J.E.3    Moldawer, L.L.4    Baker, H.V.5
  • 8
    • 0035937802 scopus 로고    scopus 로고
    • IRF3 and IRF7 phosphorylation in virus-infected cells does not require double-stranded RNA-dependent protein kinase R or Ikappa B kinase but is blocked by Vaccinia virus E3L protein
    • Smith EJ, Marie I, Prakash A, Garcia-Sastre A, Levy DE, (2001) IRF3 and IRF7 phosphorylation in virus-infected cells does not require double-stranded RNA-dependent protein kinase R or Ikappa B kinase but is blocked by Vaccinia virus E3L protein. J Biol Chem 276: 8951-8957.
    • (2001) J Biol Chem , vol.276 , pp. 8951-8957
    • Smith, E.J.1    Marie, I.2    Prakash, A.3    Garcia-Sastre, A.4    Levy, D.E.5
  • 9
    • 0036232802 scopus 로고    scopus 로고
    • Blockade of interferon induction and action by the E3L double-stranded RNA binding proteins of vaccinia virus
    • Xiang Y, Condit RC, Vijaysri S, Jacobs B, Williams BR, et al. (2002) Blockade of interferon induction and action by the E3L double-stranded RNA binding proteins of vaccinia virus. J Virol 76: 5251-5259.
    • (2002) J Virol , vol.76 , pp. 5251-5259
    • Xiang, Y.1    Condit, R.C.2    Vijaysri, S.3    Jacobs, B.4    Williams, B.R.5
  • 10
    • 67449107496 scopus 로고    scopus 로고
    • Vaccinia virus E3 suppresses expression of diverse cytokines through inhibition of the PKR, NF-kappaB, and IRF3 pathways
    • Myskiw C, Arsenio J, van Bruggen R, Deschambault Y, Cao J, (2009) Vaccinia virus E3 suppresses expression of diverse cytokines through inhibition of the PKR, NF-kappaB, and IRF3 pathways. J Virol 83: 6757-6768.
    • (2009) J Virol , vol.83 , pp. 6757-6768
    • Myskiw, C.1    Arsenio, J.2    van Bruggen, R.3    Deschambault, Y.4    Cao, J.5
  • 12
    • 0027163047 scopus 로고
    • Identification of a conserved motif that is necessary for binding of the vaccinia virus E3L gene products to double-stranded RNA
    • Chang HW, Jacobs BL, (1993) Identification of a conserved motif that is necessary for binding of the vaccinia virus E3L gene products to double-stranded RNA. Virology 194: 537-547.
    • (1993) Virology , vol.194 , pp. 537-547
    • Chang, H.W.1    Jacobs, B.L.2
  • 13
    • 0035158662 scopus 로고    scopus 로고
    • Both carboxy- and amino-terminal domains of the vaccinia virus interferon resistance gene, E3L, are required for pathogenesis in a mouse model
    • Brandt TA, Jacobs BL, (2001) Both carboxy- and amino-terminal domains of the vaccinia virus interferon resistance gene, E3L, are required for pathogenesis in a mouse model. J Virol 75: 850-856.
    • (2001) J Virol , vol.75 , pp. 850-856
    • Brandt, T.A.1    Jacobs, B.L.2
  • 14
    • 13844252090 scopus 로고    scopus 로고
    • The N-terminal domain of the vaccinia virus E3L-protein is required for neurovirulence, but not induction of a protective immune response
    • Brandt T, Heck MC, Vijaysri S, Jentarra GM, Cameron JM, et al. (2005) The N-terminal domain of the vaccinia virus E3L-protein is required for neurovirulence, but not induction of a protective immune response. Virology 333: 263-270.
    • (2005) Virology , vol.333 , pp. 263-270
    • Brandt, T.1    Heck, M.C.2    Vijaysri, S.3    Jentarra, G.M.4    Cameron, J.M.5
  • 15
    • 84861313238 scopus 로고    scopus 로고
    • The amino terminus of the vaccinia virus E3 protein is necessary to inhibit the interferon response
    • White SD, Jacobs BL, (2012) The amino terminus of the vaccinia virus E3 protein is necessary to inhibit the interferon response. J Virol 86: 5895-5904.
    • (2012) J Virol , vol.86 , pp. 5895-5904
    • White, S.D.1    Jacobs, B.L.2
  • 16
    • 0036037388 scopus 로고    scopus 로고
    • The role of the PKR-inhibitory genes, E3L and K3L, in determining vaccinia virus host range
    • Langland JO, Jacobs BL, (2002) The role of the PKR-inhibitory genes, E3L and K3L, in determining vaccinia virus host range. Virology 299: 133-141.
    • (2002) Virology , vol.299 , pp. 133-141
    • Langland, J.O.1    Jacobs, B.L.2
  • 18
    • 70350022721 scopus 로고    scopus 로고
    • The double-stranded RNA binding domain of the vaccinia virus E3L protein inhibits both RNA- and DNA-induced activation of interferon beta
    • Marq JB, Hausmann S, Luban J, Kolakofsky D, Garcin D, (2009) The double-stranded RNA binding domain of the vaccinia virus E3L protein inhibits both RNA- and DNA-induced activation of interferon beta. J Biol Chem 284: 25471-25478.
    • (2009) J Biol Chem , vol.284 , pp. 25471-25478
    • Marq, J.B.1    Hausmann, S.2    Luban, J.3    Kolakofsky, D.4    Garcin, D.5
  • 19
    • 77956275377 scopus 로고    scopus 로고
    • Inhibition of the RNA polymerase III-mediated dsDNA-sensing pathway of innate immunity by vaccinia virus protein E3
    • Valentine R, Smith GL, (2010) Inhibition of the RNA polymerase III-mediated dsDNA-sensing pathway of innate immunity by vaccinia virus protein E3. J Gen Virol 91: 2221-2229.
    • (2010) J Gen Virol , vol.91 , pp. 2221-2229
    • Valentine, R.1    Smith, G.L.2
  • 20
    • 84861009411 scopus 로고    scopus 로고
    • Innate immune response of human plasmacytoid dendritic cells to poxvirus infection is subverted by vaccinia E3 via its Z-DNA/RNA binding domain
    • Cao H, Dai P, Wang W, Li H, Yuan J, et al. (2012) Innate immune response of human plasmacytoid dendritic cells to poxvirus infection is subverted by vaccinia E3 via its Z-DNA/RNA binding domain. PLoS One 7: e36823.
    • (2012) PLoS One , vol.7
    • Cao, H.1    Dai, P.2    Wang, W.3    Li, H.4    Yuan, J.5
  • 21
    • 0028936838 scopus 로고
    • Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene
    • Beattie E, Denzler KL, Tartaglia J, Perkus ME, Paoletti E, et al. (1995) Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene. J Virol 69: 499-505.
    • (1995) J Virol , vol.69 , pp. 499-505
    • Beattie, E.1    Denzler, K.L.2    Tartaglia, J.3    Perkus, M.E.4    Paoletti, E.5
  • 22
    • 0031555657 scopus 로고    scopus 로고
    • Complementation of deletion of the vaccinia virus E3L gene by the Escherichia coli RNase III gene
    • Shors T, Jacobs BL, (1997) Complementation of deletion of the vaccinia virus E3L gene by the Escherichia coli RNase III gene. Virology 227: 77-87.
    • (1997) Virology , vol.227 , pp. 77-87
    • Shors, T.1    Jacobs, B.L.2
  • 23
    • 0141568807 scopus 로고    scopus 로고
    • The Orf virus E3L homologue is able to complement deletion of the vaccinia virus E3L gene in vitro but not in vivo
    • Vijaysri S, Talasela L, Mercer AA, McInnes CJ, Jacobs BL, et al. (2003) The Orf virus E3L homologue is able to complement deletion of the vaccinia virus E3L gene in vitro but not in vivo. Virology 314: 305-314.
    • (2003) Virology , vol.314 , pp. 305-314
    • Vijaysri, S.1    Talasela, L.2    Mercer, A.A.3    McInnes, C.J.4    Jacobs, B.L.5
  • 24
    • 83255192959 scopus 로고    scopus 로고
    • Host-range restriction of vaccinia virus E3L deletion mutant can be overcome in vitro, but not in vivo, by expression of the influenza virus NS1 protein
    • Guerra S, Abaitua F, Martinez-Sobrido L, Esteban M, Garcia-Sastre A, et al. (2011) Host-range restriction of vaccinia virus E3L deletion mutant can be overcome in vitro, but not in vivo, by expression of the influenza virus NS1 protein. PLoS One 6: e28677.
    • (2011) PLoS One , vol.6
    • Guerra, S.1    Abaitua, F.2    Martinez-Sobrido, L.3    Esteban, M.4    Garcia-Sastre, A.5
  • 25
    • 81255184409 scopus 로고    scopus 로고
    • Comparative analysis of poxvirus orthologues of the vaccinia virus E3 protein: modulation of protein kinase R activity, cytokine responses, and virus pathogenicity
    • Myskiw C, Arsenio J, Hammett C, van Bruggen R, Deschambault Y, et al. (2011) Comparative analysis of poxvirus orthologues of the vaccinia virus E3 protein: modulation of protein kinase R activity, cytokine responses, and virus pathogenicity. J Virol 85: 12280-12291.
    • (2011) J Virol , vol.85 , pp. 12280-12291
    • Myskiw, C.1    Arsenio, J.2    Hammett, C.3    van Bruggen, R.4    Deschambault, Y.5
  • 27
    • 0030862430 scopus 로고    scopus 로고
    • Compact, synthetic, vaccinia virus early/late promoter for protein expression
    • Chakrabarti S, Sisler JR, Moss B, (1997) Compact, synthetic, vaccinia virus early/late promoter for protein expression. Biotechniques 23: 1094-1097.
    • (1997) Biotechniques , vol.23 , pp. 1094-1097
    • Chakrabarti, S.1    Sisler, J.R.2    Moss, B.3
  • 28
    • 0038709512 scopus 로고    scopus 로고
    • Role of the serine-threonine kinase PAK-1 in myxoma virus replication
    • Johnston JB, Barrett JW, Chang W, Chung CS, Zeng W, et al. (2003) Role of the serine-threonine kinase PAK-1 in myxoma virus replication. J Virol 77: 5877-5888.
    • (2003) J Virol , vol.77 , pp. 5877-5888
    • Johnston, J.B.1    Barrett, J.W.2    Chang, W.3    Chung, C.S.4    Zeng, W.5
  • 29
    • 37549034204 scopus 로고    scopus 로고
    • Identification of host range mutants of myxoma virus with altered oncolytic potential in human glioma cells
    • Barrett JW, Alston LR, Wang F, Stanford MM, Gilbert PA, et al. (2007) Identification of host range mutants of myxoma virus with altered oncolytic potential in human glioma cells. J Neurovirol 13: 549-560.
    • (2007) J Neurovirol , vol.13 , pp. 549-560
    • Barrett, J.W.1    Alston, L.R.2    Wang, F.3    Stanford, M.M.4    Gilbert, P.A.5
  • 30
    • 48149085568 scopus 로고    scopus 로고
    • Myxoma virus is oncolytic for human pancreatic adenocarcinoma cells
    • Woo Y, Kelly KJ, Stanford MM, Galanis C, Chun YS, et al. (2008) Myxoma virus is oncolytic for human pancreatic adenocarcinoma cells. Ann Surg Oncol 15: 2329-2335.
    • (2008) Ann Surg Oncol , vol.15 , pp. 2329-2335
    • Woo, Y.1    Kelly, K.J.2    Stanford, M.M.3    Galanis, C.4    Chun, Y.S.5
  • 31
    • 84859579201 scopus 로고    scopus 로고
    • Myxoma virus-mediated oncolysis of ascites-derived human ovarian cancer cells and spheroids is impacted by differential AKT activity
    • Correa RJ, Komar M, Tong JG, Sivapragasam M, Rahman MM, et al. (2012) Myxoma virus-mediated oncolysis of ascites-derived human ovarian cancer cells and spheroids is impacted by differential AKT activity. Gynecol Oncol 125: 441-450.
    • (2012) Gynecol Oncol , vol.125 , pp. 441-450
    • Correa, R.J.1    Komar, M.2    Tong, J.G.3    Sivapragasam, M.4    Rahman, M.M.5
  • 33
    • 34548714237 scopus 로고    scopus 로고
    • Targeting human medulloblastoma: oncolytic virotherapy with myxoma virus is enhanced by rapamycin
    • Lun XQ, Zhou H, Alain T, Sun B, Wang L, et al. (2007) Targeting human medulloblastoma: oncolytic virotherapy with myxoma virus is enhanced by rapamycin. Cancer Res 67: 8818-8827.
    • (2007) Cancer Res , vol.67 , pp. 8818-8827
    • Lun, X.Q.1    Zhou, H.2    Alain, T.3    Sun, B.4    Wang, L.5
  • 34
    • 37548998947 scopus 로고    scopus 로고
    • Myxoma virus oncolysis of primary and metastatic B16F10 mouse tumors in vivo
    • Stanford MM, Shaban M, Barrett JW, Werden SJ, Gilbert PA, et al. (2008) Myxoma virus oncolysis of primary and metastatic B16F10 mouse tumors in vivo. Mol Ther 16: 52-59.
    • (2008) Mol Ther , vol.16 , pp. 52-59
    • Stanford, M.M.1    Shaban, M.2    Barrett, J.W.3    Werden, S.J.4    Gilbert, P.A.5
  • 35
    • 27544508998 scopus 로고    scopus 로고
    • Myxoma virus is a novel oncolytic virus with significant antitumor activity against experimental human gliomas
    • Lun X, Yang W, Alain T, Shi ZQ, Muzik H, et al. (2005) Myxoma virus is a novel oncolytic virus with significant antitumor activity against experimental human gliomas. Cancer Res 65: 9982-9990.
    • (2005) Cancer Res , vol.65 , pp. 9982-9990
    • Lun, X.1    Yang, W.2    Alain, T.3    Shi, Z.Q.4    Muzik, H.5
  • 36
    • 84862820881 scopus 로고    scopus 로고
    • Myxoma virus sensitizes cancer cells to gemcitabine and is an effective oncolytic virotherapeutic in models of disseminated pancreatic cancer
    • Wennier ST, Liu J, Li S, Rahman MM, Mona M, et al. (2012) Myxoma virus sensitizes cancer cells to gemcitabine and is an effective oncolytic virotherapeutic in models of disseminated pancreatic cancer. Mol Ther 20: 759-768.
    • (2012) Mol Ther , vol.20 , pp. 759-768
    • Wennier, S.T.1    Liu, J.2    Li, S.3    Rahman, M.M.4    Mona, M.5
  • 37
    • 34548168389 scopus 로고    scopus 로고
    • Vaccinia virus temperature-sensitive mutants in the A28 gene produce non-infectious virions that bind to cells but are defective in entry
    • Turner PC, Dilling BP, Prins C, Cresawn SG, Moyer RW, et al. (2007) Vaccinia virus temperature-sensitive mutants in the A28 gene produce non-infectious virions that bind to cells but are defective in entry. Virology 366: 62-72.
    • (2007) Virology , vol.366 , pp. 62-72
    • Turner, P.C.1    Dilling, B.P.2    Prins, C.3    Cresawn, S.G.4    Moyer, R.W.5
  • 38
    • 32344443865 scopus 로고    scopus 로고
    • Characterization of the major capsid proteins of myxoma virus particles using MALDI-TOF mass spectrometry
    • Zachertowska A, Brewer D, Evans DH, (2006) Characterization of the major capsid proteins of myxoma virus particles using MALDI-TOF mass spectrometry. J Virol Methods 132: 1-12.
    • (2006) J Virol Methods , vol.132 , pp. 1-12
    • Zachertowska, A.1    Brewer, D.2    Evans, D.H.3
  • 39
    • 0027255150 scopus 로고
    • Nuclear localization of a double-stranded RNA-binding protein encoded by the vaccinia virus E3L gene
    • Yuwen H, Cox JH, Yewdell JW, Bennink JR, Moss B, (1993) Nuclear localization of a double-stranded RNA-binding protein encoded by the vaccinia virus E3L gene. Virology 195: 732-744.
    • (1993) Virology , vol.195 , pp. 732-744
    • Yuwen, H.1    Cox, J.H.2    Yewdell, J.W.3    Bennink, J.R.4    Moss, B.5
  • 40
    • 68949163770 scopus 로고    scopus 로고
    • Human cancer cells have specifically lost the ability to induce the synergistic state caused by tumor necrosis factor plus interferon-beta
    • Bartee E, McFadden G, (2009) Human cancer cells have specifically lost the ability to induce the synergistic state caused by tumor necrosis factor plus interferon-beta. Cytokine 47: 199-205.
    • (2009) Cytokine , vol.47 , pp. 199-205
    • Bartee, E.1    McFadden, G.2
  • 42
    • 0029133407 scopus 로고
    • Rescue of vaccinia virus lacking the E3L gene by mutants of E3L
    • Chang HW, Uribe LH, Jacobs BL, (1995) Rescue of vaccinia virus lacking the E3L gene by mutants of E3L. J Virol 69: 6605-6608.
    • (1995) J Virol , vol.69 , pp. 6605-6608
    • Chang, H.W.1    Uribe, L.H.2    Jacobs, B.L.3
  • 43
    • 37849041929 scopus 로고    scopus 로고
    • Loss of protein kinase PKR expression in human HeLa cells complements the vaccinia virus E3L deletion mutant phenotype by restoration of viral protein synthesis
    • Zhang P, Jacobs BL, Samuel CE, (2008) Loss of protein kinase PKR expression in human HeLa cells complements the vaccinia virus E3L deletion mutant phenotype by restoration of viral protein synthesis. J Virol 82: 840-848.
    • (2008) J Virol , vol.82 , pp. 840-848
    • Zhang, P.1    Jacobs, B.L.2    Samuel, C.E.3
  • 45
    • 0032566917 scopus 로고    scopus 로고
    • The vaccinia virus E3L gene product interacts with both the regulatory and the substrate binding regions of PKR: implications for PKR autoregulation
    • Sharp TV, Moonan F, Romashko A, Joshi B, Barber GN, et al. (1998) The vaccinia virus E3L gene product interacts with both the regulatory and the substrate binding regions of PKR: implications for PKR autoregulation. Virology 250: 302-315.
    • (1998) Virology , vol.250 , pp. 302-315
    • Sharp, T.V.1    Moonan, F.2    Romashko, A.3    Joshi, B.4    Barber, G.N.5
  • 46
    • 0031723958 scopus 로고    scopus 로고
    • Inhibition of double-stranded RNA-dependent protein kinase PKR by vaccinia virus E3: role of complex formation and the E3 N-terminal domain
    • Romano PR, Zhang F, Tan SL, Garcia-Barrio MT, Katze MG, et al. (1998) Inhibition of double-stranded RNA-dependent protein kinase PKR by vaccinia virus E3: role of complex formation and the E3 N-terminal domain. Mol Cell Biol 18: 7304-7316.
    • (1998) Mol Cell Biol , vol.18 , pp. 7304-7316
    • Romano, P.R.1    Zhang, F.2    Tan, S.L.3    Garcia-Barrio, M.T.4    Katze, M.G.5
  • 47
    • 0030945449 scopus 로고    scopus 로고
    • Domain structure of human nuclear DNA helicase II (RNA helicase A)
    • Zhang S, Grosse F, (1997) Domain structure of human nuclear DNA helicase II (RNA helicase A). J Biol Chem 272: 11487-11494.
    • (1997) J Biol Chem , vol.272 , pp. 11487-11494
    • Zhang, S.1    Grosse, F.2
  • 48
    • 0037736816 scopus 로고    scopus 로고
    • RNA helicase A interacts with dsDNA and topoisomerase IIalpha
    • Zhou K, Choe KT, Zaidi Z, Wang Q, Mathews MB, et al. (2003) RNA helicase A interacts with dsDNA and topoisomerase IIalpha. Nucleic Acids Res 31: 2253-2260.
    • (2003) Nucleic Acids Res , vol.31 , pp. 2253-2260
    • Zhou, K.1    Choe, K.T.2    Zaidi, Z.3    Wang, Q.4    Mathews, M.B.5
  • 49
    • 33749134437 scopus 로고    scopus 로고
    • DExD/H box RNA helicases: multifunctional proteins with important roles in transcriptional regulation
    • Fuller-Pace FV, (2006) DExD/H box RNA helicases: multifunctional proteins with important roles in transcriptional regulation. Nucleic Acids Res 34: 4206-4215.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4206-4215
    • Fuller-Pace, F.V.1
  • 50
    • 34748885125 scopus 로고    scopus 로고
    • Nuclear factors are involved in hepatitis C virus RNA replication
    • Isken O, Baroth M, Grassmann CW, Weinlich S, Ostareck DH, et al. (2007) Nuclear factors are involved in hepatitis C virus RNA replication. RNA 13: 1675-1692.
    • (2007) RNA , vol.13 , pp. 1675-1692
    • Isken, O.1    Baroth, M.2    Grassmann, C.W.3    Weinlich, S.4    Ostareck, D.H.5
  • 51
    • 70350328597 scopus 로고    scopus 로고
    • Identification of RNA helicase A as a new host factor in the replication cycle of foot-and-mouth disease virus
    • Lawrence P, Rieder E, (2009) Identification of RNA helicase A as a new host factor in the replication cycle of foot-and-mouth disease virus. J Virol 83: 11356-11366.
    • (2009) J Virol , vol.83 , pp. 11356-11366
    • Lawrence, P.1    Rieder, E.2
  • 52
    • 77950493743 scopus 로고    scopus 로고
    • RNA helicase A modulates translation of HIV-1 and infectivity of progeny virions
    • Bolinger C, Sharma A, Singh D, Yu L, Boris-Lawrie K, (2010) RNA helicase A modulates translation of HIV-1 and infectivity of progeny virions. Nucleic Acids Res 38: 1686-1696.
    • (2010) Nucleic Acids Res , vol.38 , pp. 1686-1696
    • Bolinger, C.1    Sharma, A.2    Singh, D.3    Yu, L.4    Boris-Lawrie, K.5
  • 53
    • 84863116521 scopus 로고    scopus 로고
    • Identification of RNA helicase A as a cellular factor that interacts with influenza A virus NS1 protein and its role in the virus life cycle
    • Lin L, Li Y, Pyo HM, Lu X, Raman SN, et al. (2012) Identification of RNA helicase A as a cellular factor that interacts with influenza A virus NS1 protein and its role in the virus life cycle. J Virol 86: 1942-1954.
    • (2012) J Virol , vol.86 , pp. 1942-1954
    • Lin, L.1    Li, Y.2    Pyo, H.M.3    Lu, X.4    Raman, S.N.5
  • 54
    • 33744965939 scopus 로고    scopus 로고
    • Association of RNA helicase a with human immunodeficiency virus type 1 particles
    • Roy BB, Hu J, Guo X, Russell RS, Guo F, et al. (2006) Association of RNA helicase a with human immunodeficiency virus type 1 particles. J Biol Chem 281: 12625-12635.
    • (2006) J Biol Chem , vol.281 , pp. 12625-12635
    • Roy, B.B.1    Hu, J.2    Guo, X.3    Russell, R.S.4    Guo, F.5
  • 55
    • 80555133355 scopus 로고    scopus 로고
    • DHX9 pairs with IPS-1 to sense double-stranded RNA in myeloid dendritic cells
    • Zhang Z, Yuan B, Lu N, Facchinetti V, Liu YJ, (2011) DHX9 pairs with IPS-1 to sense double-stranded RNA in myeloid dendritic cells. J Immunol 187: 4501-4508.
    • (2011) J Immunol , vol.187 , pp. 4501-4508
    • Zhang, Z.1    Yuan, B.2    Lu, N.3    Facchinetti, V.4    Liu, Y.J.5
  • 56
    • 70349931825 scopus 로고    scopus 로고
    • Analysis of vaccinia virus-host protein-protein interactions: validations of yeast two-hybrid screenings
    • Zhang L, Villa NY, Rahman MM, Smallwood S, Shattuck D, et al. (2009) Analysis of vaccinia virus-host protein-protein interactions: validations of yeast two-hybrid screenings. J Proteome Res 8: 4311-4318.
    • (2009) J Proteome Res , vol.8 , pp. 4311-4318
    • Zhang, L.1    Villa, N.Y.2    Rahman, M.M.3    Smallwood, S.4    Shattuck, D.5
  • 57
    • 0031010760 scopus 로고    scopus 로고
    • The purified myxoma virus gamma interferon receptor homolog M-T7 interacts with the heparin-binding domains of chemokines
    • Lalani AS, Graham K, Mossman K, Rajarathnam K, Clark-Lewis I, et al. (1997) The purified myxoma virus gamma interferon receptor homolog M-T7 interacts with the heparin-binding domains of chemokines. J Virol 71: 4356-4363.
    • (1997) J Virol , vol.71 , pp. 4356-4363
    • Lalani, A.S.1    Graham, K.2    Mossman, K.3    Rajarathnam, K.4    Clark-Lewis, I.5
  • 58
    • 33645819161 scopus 로고    scopus 로고
    • A chemokine-binding domain in the tumor necrosis factor receptor from variola (smallpox) virus
    • Alejo A, Ruiz-Arguello MB, Ho Y, Smith VP, Saraiva M, et al. (2006) A chemokine-binding domain in the tumor necrosis factor receptor from variola (smallpox) virus. Proc Natl Acad Sci U S A 103: 5995-6000.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 5995-6000
    • Alejo, A.1    Ruiz-Arguello, M.B.2    Ho, Y.3    Smith, V.P.4    Saraiva, M.5
  • 59
    • 70450202877 scopus 로고    scopus 로고
    • The myxoma virus m-t5 ankyrin repeat host range protein is a novel adaptor that coordinately links the cellular signaling pathways mediated by Akt and Skp1 in virus-infected cells
    • Werden SJ, Lanchbury J, Shattuck D, Neff C, Dufford M, et al. (2009) The myxoma virus m-t5 ankyrin repeat host range protein is a novel adaptor that coordinately links the cellular signaling pathways mediated by Akt and Skp1 in virus-infected cells. J Virol 83: 12068-12083.
    • (2009) J Virol , vol.83 , pp. 12068-12083
    • Werden, S.J.1    Lanchbury, J.2    Shattuck, D.3    Neff, C.4    Dufford, M.5
  • 60
    • 73449119324 scopus 로고    scopus 로고
    • Co-regulation of NF-kappaB and inflammasome-mediated inflammatory responses by myxoma virus pyrin domain-containing protein M013
    • Rahman MM, Mohamed MR, Kim M, Smallwood S, McFadden G, (2009) Co-regulation of NF-kappaB and inflammasome-mediated inflammatory responses by myxoma virus pyrin domain-containing protein M013. PLoS Pathog 5: e1000635.
    • (2009) PLoS Pathog , vol.5
    • Rahman, M.M.1    Mohamed, M.R.2    Kim, M.3    Smallwood, S.4    McFadden, G.5
  • 61
    • 0030048279 scopus 로고    scopus 로고
    • Myxoma virus M-T7, a secreted homolog of the interferon-gamma receptor, is a critical virulence factor for the development of myxomatosis in European rabbits
    • Mossman K, Nation P, Macen J, Garbutt M, Lucas A, et al. (1996) Myxoma virus M-T7, a secreted homolog of the interferon-gamma receptor, is a critical virulence factor for the development of myxomatosis in European rabbits. Virology 215: 17-30.
    • (1996) Virology , vol.215 , pp. 17-30
    • Mossman, K.1    Nation, P.2    Macen, J.3    Garbutt, M.4    Lucas, A.5
  • 62
    • 0034655379 scopus 로고    scopus 로고
    • Post-translational modification of the myxoma-virus anti-inflammatory serpin SERP-1 by a virally encoded sialyltransferase
    • Nash P, Barry M, Seet BT, Veugelers K, Hota S, et al. (2000) Post-translational modification of the myxoma-virus anti-inflammatory serpin SERP-1 by a virally encoded sialyltransferase. Biochem J 347: 375-382.
    • (2000) Biochem J , vol.347 , pp. 375-382
    • Nash, P.1    Barry, M.2    Seet, B.T.3    Veugelers, K.4    Hota, S.5
  • 63
    • 33845762303 scopus 로고    scopus 로고
    • M135R is a novel cell surface virulence factor of myxoma virus
    • Barrett JW, Sypula J, Wang F, Alston LR, Shao Z, et al. (2007) M135R is a novel cell surface virulence factor of myxoma virus. J Virol 81: 106-114.
    • (2007) J Virol , vol.81 , pp. 106-114
    • Barrett, J.W.1    Sypula, J.2    Wang, F.3    Alston, L.R.4    Shao, Z.5
  • 64
    • 81255123292 scopus 로고    scopus 로고
    • Myxoma virus lacking the pyrin-like protein M013 is sensed in human myeloid cells by both NLRP3 and multiple Toll-like receptors, which independently activate the inflammasome and NF-kappaB innate response pathways
    • Rahman MM, McFadden G, (2011) Myxoma virus lacking the pyrin-like protein M013 is sensed in human myeloid cells by both NLRP3 and multiple Toll-like receptors, which independently activate the inflammasome and NF-kappaB innate response pathways. J Virol 85: 12505-12517.
    • (2011) J Virol , vol.85 , pp. 12505-12517
    • Rahman, M.M.1    McFadden, G.2
  • 65
    • 69449103056 scopus 로고    scopus 로고
    • Cowpox virus expresses a novel ankyrin repeat NF-kappaB inhibitor that controls inflammatory cell influx into virus-infected tissues and is critical for virus pathogenesis
    • Mohamed MR, Rahman MM, Rice A, Moyer RW, Werden SJ, et al. (2009) Cowpox virus expresses a novel ankyrin repeat NF-kappaB inhibitor that controls inflammatory cell influx into virus-infected tissues and is critical for virus pathogenesis. J Virol 83: 9223-9236.
    • (2009) J Virol , vol.83 , pp. 9223-9236
    • Mohamed, M.R.1    Rahman, M.M.2    Rice, A.3    Moyer, R.W.4    Werden, S.J.5
  • 66
    • 79952586504 scopus 로고    scopus 로고
    • M062 is a host range factor essential for myxoma virus pathogenesis and functions as an antagonist of host SAMD9 in human cells
    • Liu J, Wennier S, Zhang L, McFadden G, (2011) M062 is a host range factor essential for myxoma virus pathogenesis and functions as an antagonist of host SAMD9 in human cells. J Virol 85: 3270-3282.
    • (2011) J Virol , vol.85 , pp. 3270-3282
    • Liu, J.1    Wennier, S.2    Zhang, L.3    McFadden, G.4


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