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Volumn 25, Issue 5, 2014, Pages 621-628

RIG-I-like receptors and negative-strand RNA viruses: RLRly bird catches some worms

Author keywords

Genome segmentation; Negative strand RNA virus; Panhandle; RIG I like receptors; Viral countermeasures

Indexed keywords

GENOMIC RNA; RECEPTOR; RIG I LIKE RECEPTOR; RNA HELICASE; SINGLE STRANDED RNA; UNCLASSIFIED DRUG; DDX58 PROTEIN, HUMAN; DEAD BOX PROTEIN;

EID: 84908353501     PISSN: 13596101     EISSN: 18790305     Source Type: Journal    
DOI: 10.1016/j.cytogfr.2014.05.004     Document Type: Short Survey
Times cited : (24)

References (119)
  • 2
    • 80053590435 scopus 로고    scopus 로고
    • Orchestrating the interferon antiviral response through the mitochondrial antiviral signaling (MAVS) adapter
    • Belgnaoui S.M., Paz S., Hiscott J. Orchestrating the interferon antiviral response through the mitochondrial antiviral signaling (MAVS) adapter. Curr Opin Immunol 2011, 23:564-572.
    • (2011) Curr Opin Immunol , vol.23 , pp. 564-572
    • Belgnaoui, S.M.1    Paz, S.2    Hiscott, J.3
  • 3
    • 84885117922 scopus 로고    scopus 로고
    • Non-structural proteins of arthropod-borne bunyaviruses: roles and functions
    • Eifan S., Schnettler E., Dietrich I., Kohl A., Blomstrom A.L. Non-structural proteins of arthropod-borne bunyaviruses: roles and functions. Viruses 2013, 5:2447-2468.
    • (2013) Viruses , vol.5 , pp. 2447-2468
    • Eifan, S.1    Schnettler, E.2    Dietrich, I.3    Kohl, A.4    Blomstrom, A.L.5
  • 4
    • 84899125345 scopus 로고    scopus 로고
    • Mechanisms of RIG-I-like receptor activation and manipulation by viral pathogens
    • Gack M.U. Mechanisms of RIG-I-like receptor activation and manipulation by viral pathogens. J Virol 2014, 88:5213-5216.
    • (2014) J Virol , vol.88 , pp. 5213-5216
    • Gack, M.U.1
  • 5
    • 81555200097 scopus 로고    scopus 로고
    • Induction and evasion of type I interferon responses by influenza viruses
    • Garcia-Sastre A. Induction and evasion of type I interferon responses by influenza viruses. Virus Res 2011, 162:12-18.
    • (2011) Virus Res , vol.162 , pp. 12-18
    • Garcia-Sastre, A.1
  • 6
    • 80052705992 scopus 로고    scopus 로고
    • Interplay between innate immunity and negative-strand RNA viruses: towards a rational model
    • [second page of table of contents]
    • Gerlier D., Lyles D.S. Interplay between innate immunity and negative-strand RNA viruses: towards a rational model. Microbiol Mol Biol Rev MMBR 2011, 75:468-490. [second page of table of contents].
    • (2011) Microbiol Mol Biol Rev MMBR , vol.75 , pp. 468-490
    • Gerlier, D.1    Lyles, D.S.2
  • 8
    • 54449099369 scopus 로고    scopus 로고
    • The multifunctional NS1 protein of influenza A viruses
    • Hale B.G., Randall R.E., Ortin J., Jackson D. The multifunctional NS1 protein of influenza A viruses. J Gen Virol 2008, 89:2359-2376.
    • (2008) J Gen Virol , vol.89 , pp. 2359-2376
    • Hale, B.G.1    Randall, R.E.2    Ortin, J.3    Jackson, D.4
  • 9
    • 84869845792 scopus 로고    scopus 로고
    • A structure-based model of RIG-I activation
    • Kolakofsky D., Kowalinski E., Cusack S. A structure-based model of RIG-I activation. RNA 2012, 18:2118-2127.
    • (2012) RNA , vol.18 , pp. 2118-2127
    • Kolakofsky, D.1    Kowalinski, E.2    Cusack, S.3
  • 10
    • 84870359715 scopus 로고    scopus 로고
    • Recognition of viruses in the cytoplasm by RLRs and other helicases - how conformational changes, mitochondrial dynamics and ubiquitination control innate immune responses
    • Ng C.S., Kato H., Fujita T. Recognition of viruses in the cytoplasm by RLRs and other helicases - how conformational changes, mitochondrial dynamics and ubiquitination control innate immune responses. Int Immunol 2012, 24:739-749.
    • (2012) Int Immunol , vol.24 , pp. 739-749
    • Ng, C.S.1    Kato, H.2    Fujita, T.3
  • 11
    • 84887992816 scopus 로고    scopus 로고
    • Paramyxovirus activation and inhibition of innate immune responses
    • Parks G.D., Alexander-Miller M.A. Paramyxovirus activation and inhibition of innate immune responses. J Mol Biol 2013, 425:4872-4892.
    • (2013) J Mol Biol , vol.425 , pp. 4872-4892
    • Parks, G.D.1    Alexander-Miller, M.A.2
  • 12
    • 82955187705 scopus 로고    scopus 로고
    • Interferon-stimulated genes and their antiviral effector functions
    • Schoggins J.W., Rice C.M. Interferon-stimulated genes and their antiviral effector functions. Curr Opin Virol 2011, 1:519-525.
    • (2011) Curr Opin Virol , vol.1 , pp. 519-525
    • Schoggins, J.W.1    Rice, C.M.2
  • 13
    • 84884157315 scopus 로고    scopus 로고
    • Master sensors of pathogenic RNA - RIG-I like receptors
    • Schlee M. Master sensors of pathogenic RNA - RIG-I like receptors. Immunobiology 2013, 218:1322-1335.
    • (2013) Immunobiology , vol.218 , pp. 1322-1335
    • Schlee, M.1
  • 14
    • 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
  • 15
    • 84883488816 scopus 로고    scopus 로고
    • Defining the functional determinants for RNA surveillance by RIG-I
    • Kohlway A., Luo D., Rawling D.C., Ding S.C., Pyle A.M. Defining the functional determinants for RNA surveillance by RIG-I. EMBO Rep 2013, 14:772-779.
    • (2013) EMBO Rep , vol.14 , pp. 772-779
    • Kohlway, A.1    Luo, D.2    Rawling, D.C.3    Ding, S.C.4    Pyle, A.M.5
  • 16
    • 80054703126 scopus 로고    scopus 로고
    • Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA
    • Kowalinski E., Lunardi T., McCarthy A.A., Louber J., Brunel J., Grigorov B., et al. Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. Cell 2011, 147:423-435.
    • (2011) Cell , vol.147 , pp. 423-435
    • Kowalinski, E.1    Lunardi, T.2    McCarthy, A.A.3    Louber, J.4    Brunel, J.5    Grigorov, B.6
  • 17
    • 84877326407 scopus 로고    scopus 로고
    • LGP2 plays a critical role in sensitizing MDA-5 to activation by double-stranded RNA
    • Childs K.S., Randall R.E., Goodbourn S. LGP2 plays a critical role in sensitizing MDA-5 to activation by double-stranded RNA. PLoS ONE 2013, 8:e64202.
    • (2013) PLoS ONE , vol.8 , pp. e64202
    • Childs, K.S.1    Randall, R.E.2    Goodbourn, S.3
  • 19
    • 34247341367 scopus 로고    scopus 로고
    • TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity
    • Gack M.U., Shin Y.C., Joo C.H., Urano T., Liang C., Sun L., et al. TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity. Nature 2007, 446:916-920.
    • (2007) Nature , vol.446 , pp. 916-920
    • Gack, M.U.1    Shin, Y.C.2    Joo, C.H.3    Urano, T.4    Liang, C.5    Sun, L.6
  • 20
    • 84883487585 scopus 로고    scopus 로고
    • ATPase-driven oligomerization of RIG-I on RNA allows optimal activation of type-I interferon
    • Patel J.R., Jain A., Chou Y.Y., Baum A., Ha T., Garcia-Sastre A. ATPase-driven oligomerization of RIG-I on RNA allows optimal activation of type-I interferon. EMBO Rep 2013, 14:780-787.
    • (2013) EMBO Rep , vol.14 , pp. 780-787
    • Patel, J.R.1    Jain, A.2    Chou, Y.Y.3    Baum, A.4    Ha, T.5    Garcia-Sastre, A.6
  • 21
    • 84899957213 scopus 로고    scopus 로고
    • Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I
    • Peisley A., Wu B., Xu H., Chen Z.J., Hur S. Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I. Nature 2014.
    • (2014) Nature
    • Peisley, A.1    Wu, B.2    Xu, H.3    Chen, Z.J.4    Hur, S.5
  • 22
    • 84875542059 scopus 로고    scopus 로고
    • Dephosphorylation of the RNA sensors RIG-I and MDA5 by the phosphatase PP1 is essential for innate immune signaling
    • Wies E., Wang M.K., Maharaj N.P., Chen K., Zhou S., Finberg R.W., et al. Dephosphorylation of the RNA sensors RIG-I and MDA5 by the phosphatase PP1 is essential for innate immune signaling. Immunity 2013, 38:437-449.
    • (2013) Immunity , vol.38 , pp. 437-449
    • Wies, E.1    Wang, M.K.2    Maharaj, N.P.3    Chen, K.4    Zhou, S.5    Finberg, R.W.6
  • 23
    • 77951708374 scopus 로고    scopus 로고
    • Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity
    • Zeng W.W., Sun L.J., Jiang X.M., Chen X., Hou F.J., Adhikari A., et al. Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity. Cell 2010, 141:315-330.
    • (2010) Cell , vol.141 , pp. 315-330
    • Zeng, W.W.1    Sun, L.J.2    Jiang, X.M.3    Chen, X.4    Hou, F.J.5    Adhikari, A.6
  • 24
    • 79960990301 scopus 로고    scopus 로고
    • Molecular mechanism of signal perception and integration by the innate immune sensor retinoic acid-inducible Gene-I (RIG-I)
    • Binder M., Eberle F., Seitz S., Mucke N., Huber C.M., Kiani N., et al. Molecular mechanism of signal perception and integration by the innate immune sensor retinoic acid-inducible Gene-I (RIG-I). J Biol Chem 2011, 286:27278-27287.
    • (2011) J Biol Chem , vol.286 , pp. 27278-27287
    • Binder, M.1    Eberle, F.2    Seitz, S.3    Mucke, N.4    Huber, C.M.5    Kiani, N.6
  • 25
    • 84872604349 scopus 로고    scopus 로고
    • Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5
    • Wu B., Peisley A., Richards C., Yao H., Zeng X., Lin C., et al. Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5. Cell 2013, 152:276-289.
    • (2013) Cell , vol.152 , pp. 276-289
    • Wu, B.1    Peisley, A.2    Richards, C.3    Yao, H.4    Zeng, X.5    Lin, C.6
  • 26
    • 68049089651 scopus 로고    scopus 로고
    • Recognition of 5' triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus
    • Schlee M., Roth A., Hornung V., Hagmann C.A., Wimmenauer V., Barchet W., et al. Recognition of 5' triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus. Immunity 2009, 31:25-34.
    • (2009) Immunity , vol.31 , pp. 25-34
    • Schlee, M.1    Roth, A.2    Hornung, V.3    Hagmann, C.A.4    Wimmenauer, V.5    Barchet, W.6
  • 27
    • 67749133995 scopus 로고    scopus 로고
    • 5'-Triphosphate RNA requires base-paired structures to activate antiviral signaling via RIG-I
    • Schmidt A., Schwerd T., Hamm W., Hellmuth J.C., Cui S., Wenzel M., et al. 5'-Triphosphate RNA requires base-paired structures to activate antiviral signaling via RIG-I. Proc Natl Acad Sci U S A 2009, 106:12067-12072.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 12067-12072
    • Schmidt, A.1    Schwerd, T.2    Hamm, W.3    Hellmuth, J.C.4    Cui, S.5    Wenzel, M.6
  • 28
    • 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
  • 30
    • 47949092573 scopus 로고    scopus 로고
    • Innate immunity induced by composition-dependent RIG-I recognition of hepatitis C virus RNA
    • Saito T., Owen D.M., Jiang F., Marcotrigiano J., Gale M. Innate immunity induced by composition-dependent RIG-I recognition of hepatitis C virus RNA. Nature 2008, 454:523-527.
    • (2008) Nature , vol.454 , pp. 523-527
    • Saito, T.1    Owen, D.M.2    Jiang, F.3    Marcotrigiano, J.4    Gale, M.5
  • 31
    • 70349728538 scopus 로고    scopus 로고
    • Activation of MDA5 requires higher-order RNA structures generated during virus infection
    • Pichlmair A., Schulz O., Tan C.P., Rehwinkel J., Kato H., Takeuchi O., et al. Activation of MDA5 requires higher-order RNA structures generated during virus infection. J Virol 2009, 83:10761-10769.
    • (2009) J Virol , vol.83 , pp. 10761-10769
    • Pichlmair, A.1    Schulz, O.2    Tan, C.P.3    Rehwinkel, J.4    Kato, H.5    Takeuchi, O.6
  • 32
    • 79952125382 scopus 로고    scopus 로고
    • Activation of IFN-beta expression by a viral mRNA through RNase L and MDA5
    • Luthra P., Sun D., Silverman R.H., He B. Activation of IFN-beta expression by a viral mRNA through RNase L and MDA5. Proc Natl Acad Sci U S A 2011, 108:2118-2123.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 2118-2123
    • Luthra, P.1    Sun, D.2    Silverman, R.H.3    He, B.4
  • 34
    • 84863421511 scopus 로고    scopus 로고
    • The 3' untranslated regions of influenza genomic sequences are 5'ppp-independent ligands for RIG-I
    • Davis W.G., Bowzard J.B., Sharma S.D., Wiens M.E., Ranjan P., Gangappa S., et al. The 3' untranslated regions of influenza genomic sequences are 5'ppp-independent ligands for RIG-I. PLoS ONE 2012, 7:e32661.
    • (2012) PLoS ONE , vol.7 , pp. e32661
    • Davis, W.G.1    Bowzard, J.B.2    Sharma, S.D.3    Wiens, M.E.4    Ranjan, P.5    Gangappa, S.6
  • 35
    • 80051781196 scopus 로고    scopus 로고
    • Nucleoproteins and nucleocapsids of negative-strand RNA viruses
    • Ruigrok R.W., Crepin T., Kolakofsky D. Nucleoproteins and nucleocapsids of negative-strand RNA viruses. Curr Opin Microbiol 2011, 14:504-510.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 504-510
    • Ruigrok, R.W.1    Crepin, T.2    Kolakofsky, D.3
  • 36
    • 33646453915 scopus 로고    scopus 로고
    • Double-stranded RNA is produced by positive-strand RNA viruses and DNA viruses but not in detectable amounts by negative-strand RNA viruses
    • Weber F., Wagner V., Rasmussen S.B., Hartmann R., Paludan S.R. Double-stranded RNA is produced by positive-strand RNA viruses and DNA viruses but not in detectable amounts by negative-strand RNA viruses. J Virol 2006, 80:5059-5064.
    • (2006) J Virol , vol.80 , pp. 5059-5064
    • Weber, F.1    Wagner, V.2    Rasmussen, S.B.3    Hartmann, R.4    Paludan, S.R.5
  • 37
    • 84875167118 scopus 로고    scopus 로고
    • Incoming RNA virus nucleocapsids containing a 5'-triphosphorylated genome activate RIG-I and antiviral signaling
    • Weber M., Gawanbacht A., Habjan M., Rang A., Borner C., Schmidt A.M., et al. Incoming RNA virus nucleocapsids containing a 5'-triphosphorylated genome activate RIG-I and antiviral signaling. Cell Host Microbe 2013, 13:336-346.
    • (2013) Cell Host Microbe , vol.13 , pp. 336-346
    • Weber, M.1    Gawanbacht, A.2    Habjan, M.3    Rang, A.4    Borner, C.5    Schmidt, A.M.6
  • 38
    • 77957997708 scopus 로고    scopus 로고
    • Preference of RIG-I for short viral RNA molecules in infected cells revealed by next-generation sequencing
    • Baum A., Sachidanandam R., Garcia-Sastre A. Preference of RIG-I for short viral RNA molecules in infected cells revealed by next-generation sequencing. Proc Natl Acad Sci U S AV 107 2010, 16303-16308.
    • (2010) Proc Natl Acad Sci U S AV 107 , pp. 16303-16308
    • Baum, A.1    Sachidanandam, R.2    Garcia-Sastre, A.3
  • 39
    • 49149128081 scopus 로고    scopus 로고
    • Cellular La protein shields nonsegmented negative-strand RNA viral leader RNA from RIG-I and enhances virus growth by diverse mechanisms
    • Bitko V., Musiyenko A., Bayfield M.A., Maraia R.J., Barik S. Cellular La protein shields nonsegmented negative-strand RNA viral leader RNA from RIG-I and enhances virus growth by diverse mechanisms. J Virol 2008, 82:7977-7987.
    • (2008) J Virol , vol.82 , pp. 7977-7987
    • Bitko, V.1    Musiyenko, A.2    Bayfield, M.A.3    Maraia, R.J.4    Barik, S.5
  • 40
    • 72849147109 scopus 로고    scopus 로고
    • Both RIG-I and MDA5 RNA helicases contribute to the induction of alpha/beta interferon in measles virus-infected human cells
    • Ikegame S., Takeda M., Ohno S., Nakatsu Y., Nakanishi Y., Yanagi Y. Both RIG-I and MDA5 RNA helicases contribute to the induction of alpha/beta interferon in measles virus-infected human cells. J Virol 2010, 84:372-379.
    • (2010) J Virol , vol.84 , pp. 372-379
    • Ikegame, S.1    Takeda, M.2    Ohno, S.3    Nakatsu, Y.4    Nakanishi, Y.5    Yanagi, Y.6
  • 41
    • 34547157869 scopus 로고    scopus 로고
    • Cytosolic 5'-triphosphate ended viral leader transcript of measles virus as activator of the RIG I-mediated interferon response
    • Plumet S., Herschke F., Bourhis J.M., Valentin H., Longhi S., Gerlier D. Cytosolic 5'-triphosphate ended viral leader transcript of measles virus as activator of the RIG I-mediated interferon response. PLoS ONE 2007, 2:e279.
    • (2007) PLoS ONE , vol.2 , pp. e279
    • Plumet, S.1    Herschke, F.2    Bourhis, J.M.3    Valentin, H.4    Longhi, S.5    Gerlier, D.6
  • 42
    • 0019343549 scopus 로고
    • Origin and replication of defective interfering particles
    • Perrault J. Origin and replication of defective interfering particles. Curr Top Microbiol Immunol 1981, 93:151-207.
    • (1981) Curr Top Microbiol Immunol , vol.93 , pp. 151-207
    • Perrault, J.1
  • 43
    • 33745839246 scopus 로고    scopus 로고
    • Sendai virus defective-interfering genomes and the activation of interferon-beta
    • Strahle L., Garcin D., Kolakofsky D. Sendai virus defective-interfering genomes and the activation of interferon-beta. Virology 2006, 351:101-111.
    • (2006) Virology , vol.351 , pp. 101-111
    • Strahle, L.1    Garcin, D.2    Kolakofsky, D.3
  • 44
    • 84896950946 scopus 로고    scopus 로고
    • Activation of the interferon induction cascade by influenza a viruses requires viral RNA synthesis and nuclear export
    • Killip M.J., Smith M., Jackson D., Randall R.E. Activation of the interferon induction cascade by influenza a viruses requires viral RNA synthesis and nuclear export. J Virol 2014, 88:3942-3952.
    • (2014) J Virol , vol.88 , pp. 3942-3952
    • Killip, M.J.1    Smith, M.2    Jackson, D.3    Randall, R.E.4
  • 45
    • 84897515363 scopus 로고    scopus 로고
    • An unbiased genetic screen reveals the polygenic nature of the influenza virus anti-interferon response
    • Perez-Cidoncha M., Killip M.J., Oliveros J.C., Asensio V.J., Fernandez Y., Bengoechea J.A., et al. An unbiased genetic screen reveals the polygenic nature of the influenza virus anti-interferon response. J Virol 2014, 88:4632-4646.
    • (2014) J Virol , vol.88 , pp. 4632-4646
    • Perez-Cidoncha, M.1    Killip, M.J.2    Oliveros, J.C.3    Asensio, V.J.4    Fernandez, Y.5    Bengoechea, J.A.6
  • 46
    • 75749140581 scopus 로고    scopus 로고
    • RIG-I detects viral genomic RNA during negative-strand RNA virus infection
    • Rehwinkel J., Tan C.P., Goubau D., Schulz O., Pichlmair A., Bier K., et al. RIG-I detects viral genomic RNA during negative-strand RNA virus infection. Cell 2010, 140:397-408.
    • (2010) Cell , vol.140 , pp. 397-408
    • Rehwinkel, J.1    Tan, C.P.2    Goubau, D.3    Schulz, O.4    Pichlmair, A.5    Bier, K.6
  • 47
    • 84884503975 scopus 로고    scopus 로고
    • Viruses of the family Bunyaviridae: are all available isolates reassortants?
    • Briese T., Calisher C.H., Higgs S. Viruses of the family Bunyaviridae: are all available isolates reassortants?. Virology 2013, 446:207-216.
    • (2013) Virology , vol.446 , pp. 207-216
    • Briese, T.1    Calisher, C.H.2    Higgs, S.3
  • 48
    • 0021220003 scopus 로고
    • Divided genomes and intrinsic noise
    • Pressing J., Reanney D.C. Divided genomes and intrinsic noise. J Mol Evolution 1984, 20:135-146.
    • (1984) J Mol Evolution , vol.20 , pp. 135-146
    • Pressing, J.1    Reanney, D.C.2
  • 49
    • 79953795976 scopus 로고    scopus 로고
    • Viral genome segmentation can result from a trade-off between genetic content and particle stability
    • Ojosnegros S., Garcia-Arriaza J., Escarmis C., Manrubia S.C., Perales C., Arias A., et al. Viral genome segmentation can result from a trade-off between genetic content and particle stability. PLoS Genetics 2011, 7:e1001344.
    • (2011) PLoS Genetics , vol.7 , pp. e1001344
    • Ojosnegros, S.1    Garcia-Arriaza, J.2    Escarmis, C.3    Manrubia, S.C.4    Perales, C.5    Arias, A.6
  • 50
    • 80052047427 scopus 로고    scopus 로고
    • Replication-coupled and host factor-mediated encapsidation of the influenza virus genome by viral nucleoprotein
    • Kawaguchi A., Momose F., Nagata K. Replication-coupled and host factor-mediated encapsidation of the influenza virus genome by viral nucleoprotein. J Virol 2011, 85:6197-6204.
    • (2011) J Virol , vol.85 , pp. 6197-6204
    • Kawaguchi, A.1    Momose, F.2    Nagata, K.3
  • 51
    • 80052285645 scopus 로고    scopus 로고
    • The cellular RNA helicase UAP56 is required for prevention of double-stranded RNA formation during influenza A virus infection
    • Wisskirchen C., Ludersdorfer T.H., Muller D.A., Moritz E., Pavlovic J. The cellular RNA helicase UAP56 is required for prevention of double-stranded RNA formation during influenza A virus infection. J Virol 2011, 85:8646-8655.
    • (2011) J Virol , vol.85 , pp. 8646-8655
    • Wisskirchen, C.1    Ludersdorfer, T.H.2    Muller, D.A.3    Moritz, E.4    Pavlovic, J.5
  • 52
    • 78951490665 scopus 로고    scopus 로고
    • The C proteins of human parainfluenza virus type 1 limit double-stranded RNA accumulation that would otherwise trigger activation of MDA5 and protein kinase R
    • Boonyaratanakornkit J., Bartlett E., Schomacker H., Surman S., Akira S., Bae Y.S., et al. The C proteins of human parainfluenza virus type 1 limit double-stranded RNA accumulation that would otherwise trigger activation of MDA5 and protein kinase R. J Virol 2011, 85:1495-1506.
    • (2011) J Virol , vol.85 , pp. 1495-1506
    • Boonyaratanakornkit, J.1    Bartlett, E.2    Schomacker, H.3    Surman, S.4    Akira, S.5    Bae, Y.S.6
  • 53
    • 35148862077 scopus 로고    scopus 로고
    • Role for the phosphoprotein P subunit of the paramyxovirus polymerase in limiting induction of host cell antiviral responses
    • Dillon P.J., Parks G.D. Role for the phosphoprotein P subunit of the paramyxovirus polymerase in limiting induction of host cell antiviral responses. J Virol 2007, 81:11116-11127.
    • (2007) J Virol , vol.81 , pp. 11116-11127
    • Dillon, P.J.1    Parks, G.D.2
  • 54
    • 69449092124 scopus 로고    scopus 로고
    • Role for the paramyxovirus genomic promoter in limiting host cell antiviral responses and cell killing
    • Manuse M.J., Parks G.D. Role for the paramyxovirus genomic promoter in limiting host cell antiviral responses and cell killing. J Virol 2009, 83:9057-9067.
    • (2009) J Virol , vol.83 , pp. 9057-9067
    • Manuse, M.J.1    Parks, G.D.2
  • 55
    • 33751248250 scopus 로고    scopus 로고
    • Translational inhibition and increased interferon induction in cells infected with C protein-deficient measles virus
    • Nakatsu Y., Takeda M., Ohno S., Koga R., Yanagi Y. Translational inhibition and increased interferon induction in cells infected with C protein-deficient measles virus. J Virol 2006, 80:11861-11867.
    • (2006) J Virol , vol.80 , pp. 11861-11867
    • Nakatsu, Y.1    Takeda, M.2    Ohno, S.3    Koga, R.4    Yanagi, Y.5
  • 56
    • 84890883651 scopus 로고    scopus 로고
    • Measles virus C protein impairs production of defective copyback double-stranded viral RNA and activation of protein kinase R
    • Pfaller C.K., Radeke M.J., Cattaneo R., Samuel C.E. Measles virus C protein impairs production of defective copyback double-stranded viral RNA and activation of protein kinase R. J Virol 2014, 88:456-468.
    • (2014) J Virol , vol.88 , pp. 456-468
    • Pfaller, C.K.1    Radeke, M.J.2    Cattaneo, R.3    Samuel, C.E.4
  • 57
    • 53749086902 scopus 로고    scopus 로고
    • Sendai virus C protein plays a role in restricting PKR activation by limiting the generation of intracellular double-stranded RNA
    • Takeuchi K., Komatsu T., Kitagawa Y., Sada K., Gotoh B. Sendai virus C protein plays a role in restricting PKR activation by limiting the generation of intracellular double-stranded RNA. J Virol 2008, 82:10102-10110.
    • (2008) J Virol , vol.82 , pp. 10102-10110
    • Takeuchi, K.1    Komatsu, T.2    Kitagawa, Y.3    Sada, K.4    Gotoh, B.5
  • 58
    • 84869034587 scopus 로고    scopus 로고
    • Incoming influenza A virus evades early host recognition, while influenza B virus induces interferon expression directly upon entry
    • Osterlund P., Strengell M., Sarin L.P., Poranen M.M., Fagerlund R., Melen K., et al. Incoming influenza A virus evades early host recognition, while influenza B virus induces interferon expression directly upon entry. J Virol 2012, 86:11183-11193.
    • (2012) J Virol , vol.86 , pp. 11183-11193
    • Osterlund, P.1    Strengell, M.2    Sarin, L.P.3    Poranen, M.M.4    Fagerlund, R.5    Melen, K.6
  • 59
    • 0027102716 scopus 로고
    • Binding of influenza A virus NS1 protein to dsRNA in vitro
    • Hatada E., Fukuda R. Binding of influenza A virus NS1 protein to dsRNA in vitro. J Gen Virol 1992, 73(Pt 12):3325-3329.
    • (1992) J Gen Virol , vol.73 , pp. 3325-3329
    • Hatada, E.1    Fukuda, R.2
  • 62
    • 0029400032 scopus 로고
    • An amino-terminal polypeptide fragment of the influenza virus NS1 protein possesses specific RNA-binding activity and largely helical backbone structure
    • Qian X.Y., Chien C.Y., Lu Y., Montelione G.T., Krug R.M. An amino-terminal polypeptide fragment of the influenza virus NS1 protein possesses specific RNA-binding activity and largely helical backbone structure. RNA 1995, 1:948-956.
    • (1995) RNA , vol.1 , pp. 948-956
    • Qian, X.Y.1    Chien, C.Y.2    Lu, Y.3    Montelione, G.T.4    Krug, R.M.5
  • 63
    • 65549164536 scopus 로고    scopus 로고
    • Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I
    • Gack M.U., Albrecht R.A., Urano T., Inn K.S., Huang I.C., Carnero E., et al. Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I. Cell Host Microbe 2009, 5:439-449.
    • (2009) Cell Host Microbe , vol.5 , pp. 439-449
    • Gack, M.U.1    Albrecht, R.A.2    Urano, T.3    Inn, K.S.4    Huang, I.C.5    Carnero, E.6
  • 64
    • 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
  • 65
    • 0037444193 scopus 로고    scopus 로고
    • Cellular antiviral responses against influenza A virus are countered at the posttranscriptional level by the viral NS1A protein via its binding to a cellular protein required for the 3' end processing of cellular pre-mRNAS
    • Noah D.L., Twu K.Y., Krug R.M. Cellular antiviral responses against influenza A virus are countered at the posttranscriptional level by the viral NS1A protein via its binding to a cellular protein required for the 3' end processing of cellular pre-mRNAS. Virology 2003, 307:386-395.
    • (2003) Virology , vol.307 , pp. 386-395
    • Noah, D.L.1    Twu, K.Y.2    Krug, R.M.3
  • 66
    • 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
  • 67
    • 44349143815 scopus 로고    scopus 로고
    • Processing of genome 5' termini as a strategy of negative-strand RNA viruses to avoid RIG-I-dependent interferon induction
    • Habjan M., Andersson I., Klingstrom J., Schumann M., Martin A., Zimmermann P., et al. Processing of genome 5' termini as a strategy of negative-strand RNA viruses to avoid RIG-I-dependent interferon induction. PLoS ONE 2008, 3:e2032.
    • (2008) PLoS ONE , vol.3 , pp. e2032
    • Habjan, M.1    Andersson, I.2    Klingstrom, J.3    Schumann, M.4    Martin, A.5    Zimmermann, P.6
  • 68
    • 79955605785 scopus 로고    scopus 로고
    • Old world hantaviruses do not produce detectable amounts of dsRNA in infected cells and the 5' termini of their genomic RNAs are monophosphorylated
    • Wang H., Vaheri A., Weber F., Plyusnin A. Old world hantaviruses do not produce detectable amounts of dsRNA in infected cells and the 5' termini of their genomic RNAs are monophosphorylated. J Gen Virol 2011, 92:1199-1204.
    • (2011) J Gen Virol , vol.92 , pp. 1199-1204
    • Wang, H.1    Vaheri, A.2    Weber, F.3    Plyusnin, A.4
  • 69
    • 80051775478 scopus 로고    scopus 로고
    • RNA helicase retinoic acid-inducible gene I as a sensor of Hantaan virus replication
    • Lee M.H., Lalwani P., Raftery M.J., Matthaei M., Lutteke N., Kirsanovs S., et al. RNA helicase retinoic acid-inducible gene I as a sensor of Hantaan virus replication. J Gen Virol 2011, 92:2191-2200.
    • (2011) J Gen Virol , vol.92 , pp. 2191-2200
    • Lee, M.H.1    Lalwani, P.2    Raftery, M.J.3    Matthaei, M.4    Lutteke, N.5    Kirsanovs, S.6
  • 70
    • 66149095145 scopus 로고    scopus 로고
    • Efficient reverse genetics generation of infectious junin viruses differing in glycoprotein processing
    • Albarino C.G., Bergeron E., Erickson B.R., Khristova M.L., Rollin P.E., Nichol S.T. Efficient reverse genetics generation of infectious junin viruses differing in glycoprotein processing. J Virol 2009, 83:5606-5614.
    • (2009) J Virol , vol.83 , pp. 5606-5614
    • Albarino, C.G.1    Bergeron, E.2    Erickson, B.R.3    Khristova, M.L.4    Rollin, P.E.5    Nichol, S.T.6
  • 71
    • 79953166075 scopus 로고    scopus 로고
    • Short double-stranded RNAs with an overhanging 5'ppp-nucleotide, as found in arenavirus genomes, act as RIG-I decoys
    • Marq J.B., Hausmann S., Veillard N., Kolakofsky D., Garcin D. Short double-stranded RNAs with an overhanging 5'ppp-nucleotide, as found in arenavirus genomes, act as RIG-I decoys. J Biol Chem 2011, 286:6108-6116.
    • (2011) J Biol Chem , vol.286 , pp. 6108-6116
    • Marq, J.B.1    Hausmann, S.2    Veillard, N.3    Kolakofsky, D.4    Garcin, D.5
  • 72
    • 79952303123 scopus 로고    scopus 로고
    • Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3' to 5' exonuclease activity essential for immune suppression
    • Hastie K.M., Kimberlin C.R., Zandonatti M.A., MacRae I.J., Saphire E.O. Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3' to 5' exonuclease activity essential for immune suppression. Proc Natl Acad Sci U S A 2011, 108:2396-2401.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 2396-2401
    • Hastie, K.M.1    Kimberlin, C.R.2    Zandonatti, M.A.3    MacRae, I.J.4    Saphire, E.O.5
  • 73
    • 78650132935 scopus 로고    scopus 로고
    • Cap binding and immune evasion revealed by Lassa nucleoprotein structure
    • Qi X., Lan S., Wang W., Schelde L.M., Dong H., Wallat G.D., et al. Cap binding and immune evasion revealed by Lassa nucleoprotein structure. Nature 2010, 468:779-783.
    • (2010) Nature , vol.468 , pp. 779-783
    • Qi, X.1    Lan, S.2    Wang, W.3    Schelde, L.M.4    Dong, H.5    Wallat, G.D.6
  • 74
    • 75449114628 scopus 로고    scopus 로고
    • Z proteins of New World arenaviruses bind RIG-I and interfere with type I interferon induction
    • Fan L., Briese T., Lipkin W.I. Z proteins of New World arenaviruses bind RIG-I and interfere with type I interferon induction. J Virol 2010, 84:1785-1791.
    • (2010) J Virol , vol.84 , pp. 1785-1791
    • Fan, L.1    Briese, T.2    Lipkin, W.I.3
  • 75
    • 64049090424 scopus 로고    scopus 로고
    • Human respiratory syncytial virus nonstructural protein NS2 antagonizes the activation of beta interferon transcription by interacting with RIG-I
    • Ling Z., Tran K.C., Teng M.N. Human respiratory syncytial virus nonstructural protein NS2 antagonizes the activation of beta interferon transcription by interacting with RIG-I. J Virol 2009, 83:3734-3742.
    • (2009) J Virol , vol.83 , pp. 3734-3742
    • Ling, Z.1    Tran, K.C.2    Teng, M.N.3
  • 76
  • 77
    • 84856844697 scopus 로고    scopus 로고
    • Arterivirus and nairovirus ovarian tumor domain-containing Deubiquitinases target activated RIG-I to control innate immune signaling
    • van Kasteren P.B., Beugeling C., Ninaber D.K., Frias-Staheli N., van Boheemen S., Garcia-Sastre A., et al. Arterivirus and nairovirus ovarian tumor domain-containing Deubiquitinases target activated RIG-I to control innate immune signaling. J Virol 2012, 86:773-785.
    • (2012) J Virol , vol.86 , pp. 773-785
    • van Kasteren, P.B.1    Beugeling, C.2    Ninaber, D.K.3    Frias-Staheli, N.4    van Boheemen, S.5    Garcia-Sastre, A.6
  • 78
    • 10344259136 scopus 로고    scopus 로고
    • The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-beta promoter
    • Andrejeva J., Childs K.S., Young D.F., Carlos T.S., Stock N., Goodbourn S., et al. The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-beta promoter. Proc Natl Acad Sci U S A 2004, 101:17264-17269.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17264-17269
    • Andrejeva, J.1    Childs, K.S.2    Young, D.F.3    Carlos, T.S.4    Stock, N.5    Goodbourn, S.6
  • 79
    • 84873523444 scopus 로고    scopus 로고
    • Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling
    • Motz C., Schuhmann K.M., Kirchhofer A., Moldt M., Witte G., Conzelmann K.K., et al. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science 2013, 339:690-693.
    • (2013) Science , vol.339 , pp. 690-693
    • Motz, C.1    Schuhmann, K.M.2    Kirchhofer, A.3    Moldt, M.4    Witte, G.5    Conzelmann, K.K.6
  • 80
    • 84861304915 scopus 로고    scopus 로고
    • Proteins interact with the RNA helicase LGP2 to inhibit RIG-I-dependent interferon induction
    • Childs K., Randall R., Goodbourn S., Paramyxovirus V. proteins interact with the RNA helicase LGP2 to inhibit RIG-I-dependent interferon induction. J Virol 2012, 86:3411-3421.
    • (2012) J Virol , vol.86 , pp. 3411-3421
    • Childs, K.1    Randall, R.2    Goodbourn, S.3    Paramyxovirus, V.4
  • 81
    • 84873320976 scopus 로고    scopus 로고
    • Induction of Siglec-G by RNA viruses inhibits the innate immune response by promoting RIG-I degradation
    • Chen W., Han C., Xie B., Hu X., Yu Q., Shi L., et al. Induction of Siglec-G by RNA viruses inhibits the innate immune response by promoting RIG-I degradation. Cell 2013, 152:467-478.
    • (2013) Cell , vol.152 , pp. 467-478
    • Chen, W.1    Han, C.2    Xie, B.3    Hu, X.4    Yu, Q.5    Shi, L.6
  • 82
    • 84878608456 scopus 로고    scopus 로고
    • Toscana virus NSs protein inhibits the induction of type I interferon by interacting with RIG-I
    • Gori-Savellini G., Valentini M., Cusi M.G. Toscana virus NSs protein inhibits the induction of type I interferon by interacting with RIG-I. J Virol 2013, 87:6660-6667.
    • (2013) J Virol , vol.87 , pp. 6660-6667
    • Gori-Savellini, G.1    Valentini, M.2    Cusi, M.G.3
  • 83
    • 84864391552 scopus 로고    scopus 로고
    • Human respiratory syncytial virus nucleoprotein and inclusion bodies antagonize the innate immune response mediated by MDA5 and MAVS
    • Lifland A.W., Jung J., Alonas E., Zurla C., Crowe J.E., Santangelo P.J. Human respiratory syncytial virus nucleoprotein and inclusion bodies antagonize the innate immune response mediated by MDA5 and MAVS. J Virol 2012, 86:8245-8258.
    • (2012) J Virol , vol.86 , pp. 8245-8258
    • Lifland, A.W.1    Jung, J.2    Alonas, E.3    Zurla, C.4    Crowe, J.E.5    Santangelo, P.J.6
  • 84
    • 84896930327 scopus 로고    scopus 로고
    • Hijacking of RIG-I signaling proteins into virus-induced cytoplasmic structures correlates with the inhibition of Type I interferon responses
    • Santiago F.W., Covaleda L.M., Sanchez-Aparicio M.T., Silvas J.A., Diaz-Vizarreta A.C., Patel J.R., et al. Hijacking of RIG-I signaling proteins into virus-induced cytoplasmic structures correlates with the inhibition of Type I interferon responses. J Virol 2014, 88:4572-4585.
    • (2014) J Virol , vol.88 , pp. 4572-4585
    • Santiago, F.W.1    Covaleda, L.M.2    Sanchez-Aparicio, M.T.3    Silvas, J.A.4    Diaz-Vizarreta, A.C.5    Patel, J.R.6
  • 85
    • 84894576199 scopus 로고    scopus 로고
    • Evasion of antiviral immunity through sequestering of TBK1/IKKepsilon/IRF3 into viral inclusion bodies
    • Wu X., Qi X., Qu B., Zhang Z., Liang M., Li C., et al. Evasion of antiviral immunity through sequestering of TBK1/IKKepsilon/IRF3 into viral inclusion bodies. J Virol 2014, 88:3067-3076.
    • (2014) J Virol , vol.88 , pp. 3067-3076
    • Wu, X.1    Qi, X.2    Qu, B.3    Zhang, Z.4    Liang, M.5    Li, C.6
  • 87
    • 77956634918 scopus 로고    scopus 로고
    • The PB2 subunit of the influenza virus RNA polymerase affects virulence by interacting with the mitochondrial antiviral signaling protein and inhibiting expression of beta interferon
    • Graef K.M., Vreede F.T., Lau Y.F., McCall A.W., Carr S.M., Subbarao K., et al. The PB2 subunit of the influenza virus RNA polymerase affects virulence by interacting with the mitochondrial antiviral signaling protein and inhibiting expression of beta interferon. J Virol 2010, 84:8433-8445.
    • (2010) J Virol , vol.84 , pp. 8433-8445
    • Graef, K.M.1    Vreede, F.T.2    Lau, Y.F.3    McCall, A.W.4    Carr, S.M.5    Subbarao, K.6
  • 88
    • 77957757095 scopus 로고    scopus 로고
    • Influenza A virus polymerase inhibits type I interferon induction by binding to interferon beta promoter stimulator 1
    • Iwai A., Shiozaki T., Kawai T., Akira S., Kawaoka Y., Takada A., et al. Influenza A virus polymerase inhibits type I interferon induction by binding to interferon beta promoter stimulator 1. J Biol Chem 2010, 285:32064-32074.
    • (2010) J Biol Chem , vol.285 , pp. 32064-32074
    • Iwai, A.1    Shiozaki, T.2    Kawai, T.3    Akira, S.4    Kawaoka, Y.5    Takada, A.6
  • 89
    • 80755169631 scopus 로고    scopus 로고
    • The influenza virus PB1-F2 protein has interferon antagonistic activity
    • Dudek S.E., Wixler L., Nordhoff C., Nordmann A., Anhlan D., Wixler V., et al. The influenza virus PB1-F2 protein has interferon antagonistic activity. Biol Chem 2011, 392:1135-1144.
    • (2011) Biol Chem , vol.392 , pp. 1135-1144
    • Dudek, S.E.1    Wixler, L.2    Nordhoff, C.3    Nordmann, A.4    Anhlan, D.5    Wixler, V.6
  • 90
    • 84877941530 scopus 로고    scopus 로고
    • The influenza virus protein PB1-F2 interacts with IKKbeta and modulates NF-kappaB signalling
    • Reis A.L., McCauley J.W. The influenza virus protein PB1-F2 interacts with IKKbeta and modulates NF-kappaB signalling. PLoS ONE 2013, 8:e63852.
    • (2013) PLoS ONE , vol.8 , pp. e63852
    • Reis, A.L.1    McCauley, J.W.2
  • 91
    • 79959823372 scopus 로고    scopus 로고
    • The influenza virus protein PB1-F2 inhibits the induction of type I interferon at the level of the MAVS adaptor protein
    • Varga Z.T., Ramos I., Hai R., Schmolke M., Garcia-Sastre A., Fernandez-Sesma A., et al. The influenza virus protein PB1-F2 inhibits the induction of type I interferon at the level of the MAVS adaptor protein. PLoS Pathogens 2011, 7:e1002067.
    • (2011) PLoS Pathogens , vol.7 , pp. e1002067
    • Varga, Z.T.1    Ramos, I.2    Hai, R.3    Schmolke, M.4    Garcia-Sastre, A.5    Fernandez-Sesma, A.6
  • 92
    • 19944370132 scopus 로고    scopus 로고
    • Identification of the rabies virus alpha/beta interferon antagonist: phosphoprotein P interferes with phosphorylation of interferon regulatory factor 3
    • Brzozka K., Finke S., Conzelmann K.K. Identification of the rabies virus alpha/beta interferon antagonist: phosphoprotein P interferes with phosphorylation of interferon regulatory factor 3. J Virol 2005, 79:7673-7681.
    • (2005) J Virol , vol.79 , pp. 7673-7681
    • Brzozka, K.1    Finke, S.2    Conzelmann, K.K.3
  • 93
    • 84903362017 scopus 로고    scopus 로고
    • An innate immunity-regulating virulence determinant is uniquely encoded by the Andes virus nucleocapsid protein
    • Cimica V., Dalrymple N.A., Roth E., Nasonov A., Mackow E.R. An innate immunity-regulating virulence determinant is uniquely encoded by the Andes virus nucleocapsid protein. mBio 2014, 5.
    • (2014) mBio , pp. 5
    • Cimica, V.1    Dalrymple, N.A.2    Roth, E.3    Nasonov, A.4    Mackow, E.R.5
  • 94
    • 47249132062 scopus 로고    scopus 로고
    • Select paramyxoviral V proteins inhibit IRF3 activation by acting as alternative substrates for inhibitor of kappaB kinase epsilon (IKKe)/TBK1
    • Lu L.L., Puri M., Horvath C.M., Sen G.C. Select paramyxoviral V proteins inhibit IRF3 activation by acting as alternative substrates for inhibitor of kappaB kinase epsilon (IKKe)/TBK1. J Biol Chem 2008, 283:14269-14276.
    • (2008) J Biol Chem , vol.283 , pp. 14269-14276
    • Lu, L.L.1    Puri, M.2    Horvath, C.M.3    Sen, G.C.4
  • 95
    • 84893458405 scopus 로고    scopus 로고
    • Hantavirus GnT elements mediate TRAF3 binding and inhibit RIG-I/TBK1-directed beta interferon transcription by blocking IRF3 phosphorylation
    • Matthys V.S., Cimica V., Dalrymple N.A., Glennon N.B., Bianco C., Mackow E.R. Hantavirus GnT elements mediate TRAF3 binding and inhibit RIG-I/TBK1-directed beta interferon transcription by blocking IRF3 phosphorylation. J Virol 2014, 88:2246-2259.
    • (2014) J Virol , vol.88 , pp. 2246-2259
    • Matthys, V.S.1    Cimica, V.2    Dalrymple, N.A.3    Glennon, N.B.4    Bianco, C.5    Mackow, E.R.6
  • 97
    • 26444475464 scopus 로고    scopus 로고
    • Viral targeting of the interferon-{beta}-inducing Traf family member-associated NF-{kappa}B activator (TANK)-binding kinase-1
    • Unterstab G., Ludwig S., Anton A., Planz O., Dauber B., Krappmann D., et al. Viral targeting of the interferon-{beta}-inducing Traf family member-associated NF-{kappa}B activator (TANK)-binding kinase-1. Proc Natl Acad Sci U S A 2005, 102:13640-13645.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 13640-13645
    • Unterstab, G.1    Ludwig, S.2    Anton, A.3    Planz, O.4    Dauber, B.5    Krappmann, D.6
  • 98
    • 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 Pathogens 2009, 5:e1000493.
    • (2009) PLoS Pathogens , vol.5 , pp. e1000493
    • Chang, T.H.1    Kubota, T.2    Matsuoka, M.3    Jones, S.4    Bradfute, S.B.5    Bray, M.6
  • 99
    • 73149114616 scopus 로고    scopus 로고
    • Thogoto virus ML protein is a potent inhibitor of the interferon regulatory factor-7 transcription factor
    • Buettner N., Vogt C., Martinez-Sobrido L., Weber F., Waibler Z., Kochs G. Thogoto virus ML protein is a potent inhibitor of the interferon regulatory factor-7 transcription factor. J Gen Virol 2010, 91:220-227.
    • (2010) J Gen Virol , vol.91 , pp. 220-227
    • Buettner, N.1    Vogt, C.2    Martinez-Sobrido, L.3    Weber, F.4    Waibler, Z.5    Kochs, G.6
  • 100
    • 55549139493 scopus 로고    scopus 로고
    • The interferon antagonist ML protein of thogoto virus targets general transcription factor IIB
    • Vogt C., Preuss E., Mayer D., Weber F., Schwemmle M., Kochs G. The interferon antagonist ML protein of thogoto virus targets general transcription factor IIB. J Virol 2008, 82:11446-11453.
    • (2008) J Virol , vol.82 , pp. 11446-11453
    • Vogt, C.1    Preuss, E.2    Mayer, D.3    Weber, F.4    Schwemmle, M.5    Kochs, G.6
  • 101
    • 84864118573 scopus 로고    scopus 로고
    • Inhibition of interferon regulatory factor 3 activation by paramyxovirus V protein
    • Irie T., Kiyotani K., Igarashi T., Yoshida A., Sakaguchi T. Inhibition of interferon regulatory factor 3 activation by paramyxovirus V protein. J Virol 2012, 86:7136-7145.
    • (2012) J Virol , vol.86 , pp. 7136-7145
    • Irie, T.1    Kiyotani, K.2    Igarashi, T.3    Yoshida, A.4    Sakaguchi, T.5
  • 102
    • 18144378011 scopus 로고    scopus 로고
    • Nuclear localization of the Nipah virus W protein allows for inhibition of both virus- and toll-like receptor 3-triggered signaling pathways
    • Shaw M.L., Cardenas W.B., Zamarin D., Palese P., Basler C.F. Nuclear localization of the Nipah virus W protein allows for inhibition of both virus- and toll-like receptor 3-triggered signaling pathways. J Virol 2005, 79:6078-6088.
    • (2005) J Virol , vol.79 , pp. 6078-6088
    • Shaw, M.L.1    Cardenas, W.B.2    Zamarin, D.3    Palese, P.4    Basler, C.F.5
  • 103
    • 38949091131 scopus 로고    scopus 로고
    • A SAP30 complex inhibits IFN-beta expression in Rift Valley fever virus infected cells
    • Le May N., Mansuroglu Z., Leger P., Josse T., Blot G., Billecocq A., et al. A SAP30 complex inhibits IFN-beta expression in Rift Valley fever virus infected cells. PLoS Pathogens 2008, 4:e13.
    • (2008) PLoS Pathogens , vol.4 , pp. e13
    • Le May, N.1    Mansuroglu, Z.2    Leger, P.3    Josse, T.4    Blot, G.5    Billecocq, A.6
  • 105
    • 34248333002 scopus 로고    scopus 로고
    • La Crosse bunyavirus nonstructural protein NSs serves to suppress the type I interferon system of mammalian hosts
    • Blakqori G., Delhaye S., Habjan M., Blair C.D., Sanchez-Vargas I., Olson K.E., et al. La Crosse bunyavirus nonstructural protein NSs serves to suppress the type I interferon system of mammalian hosts. J Virol 2007, 81:4991-4999.
    • (2007) J Virol , vol.81 , pp. 4991-4999
    • Blakqori, G.1    Delhaye, S.2    Habjan, M.3    Blair, C.D.4    Sanchez-Vargas, I.5    Olson, K.E.6
  • 106
    • 0035152344 scopus 로고    scopus 로고
    • Genetic evidence for an interferon-antagonistic function of rift valley fever virus nonstructural protein NSs
    • Bouloy M., Janzen C., Vialat P., Khun H., Pavlovic J., Huerre M., et al. Genetic evidence for an interferon-antagonistic function of rift valley fever virus nonstructural protein NSs. J Virol 2001, 75:1371-1377.
    • (2001) J Virol , vol.75 , pp. 1371-1377
    • Bouloy, M.1    Janzen, C.2    Vialat, P.3    Khun, H.4    Pavlovic, J.5    Huerre, M.6
  • 107
    • 10744223476 scopus 로고    scopus 로고
    • VSV strains with defects in their ability to shutdown innate immunity are potent systemic anti-cancer agents
    • Stojdl D.F., Lichty B.D., tenOever B.R., Paterson J.M., Power A.T., Knowles S., et al. VSV strains with defects in their ability to shutdown innate immunity are potent systemic anti-cancer agents. Cancer Cell 2003, 4:263-275.
    • (2003) Cancer Cell , vol.4 , pp. 263-275
    • Stojdl, D.F.1    Lichty, B.D.2    tenOever, B.R.3    Paterson, J.M.4    Power, A.T.5    Knowles, S.6
  • 108
    • 13944264963 scopus 로고    scopus 로고
    • Interferon induction and/or production and its suppression by influenza A viruses
    • Marcus P.I., Rojek J.M., Sekellick M.J. Interferon induction and/or production and its suppression by influenza A viruses. J Virol 2005, 79:2880-2890.
    • (2005) J Virol , vol.79 , pp. 2880-2890
    • Marcus, P.I.1    Rojek, J.M.2    Sekellick, M.J.3
  • 109
    • 84863754680 scopus 로고    scopus 로고
    • An overlapping protein-coding region in influenza A virus segment 3 modulates the host response
    • Jagger B.W., Wise H.M., Kash J.C., Walters K.A., Wills N.M., Xiao Y.L., et al. An overlapping protein-coding region in influenza A virus segment 3 modulates the host response. Science 2012, 337:199-204.
    • (2012) Science , vol.337 , pp. 199-204
    • Jagger, B.W.1    Wise, H.M.2    Kash, J.C.3    Walters, K.A.4    Wills, N.M.5    Xiao, Y.L.6
  • 110
    • 84866932844 scopus 로고    scopus 로고
    • Complexes of vesicular stomatitis virus matrix protein with host Rae1 and Nup98 involved in inhibition of host transcription
    • Rajani K.R., Pettit Kneller E.L., McKenzie M.O., Horita D.A., Chou J.W., Lyles D.S. Complexes of vesicular stomatitis virus matrix protein with host Rae1 and Nup98 involved in inhibition of host transcription. PLoS Pathogens 2012, 8:e1002929.
    • (2012) PLoS Pathogens , vol.8 , pp. e1002929
    • Rajani, K.R.1    Pettit Kneller, E.L.2    McKenzie, M.O.3    Horita, D.A.4    Chou, J.W.5    Lyles, D.S.6
  • 111
    • 1342264311 scopus 로고    scopus 로고
    • TFIIH transcription factor, a target for the Rift Valley hemorrhagic fever virus
    • Le May N., Dubaele S., De Santis L.P., Billecocq A., Bouloy M., Egly J.M. TFIIH transcription factor, a target for the Rift Valley hemorrhagic fever virus. Cell 2004, 116:541-550.
    • (2004) Cell , vol.116 , pp. 541-550
    • Le May, N.1    Dubaele, S.2    De Santis, L.P.3    Billecocq, A.4    Bouloy, M.5    Egly, J.M.6
  • 112
    • 84894536027 scopus 로고    scopus 로고
    • Virulence factor NSs of rift valley fever virus recruits the F-box protein FBXO3 to degrade subunit p62 of general transcription factor TFIIH
    • Kainulainen M., Habjan M., Hubel P., Busch L., Lau S., Colinge J., et al. Virulence factor NSs of rift valley fever virus recruits the F-box protein FBXO3 to degrade subunit p62 of general transcription factor TFIIH. J Virol 2014, 88:3464-3473.
    • (2014) J Virol , vol.88 , pp. 3464-3473
    • Kainulainen, M.1    Habjan, M.2    Hubel, P.3    Busch, L.4    Lau, S.5    Colinge, J.6
  • 113
    • 80052073169 scopus 로고    scopus 로고
    • NSs protein of rift valley fever virus promotes posttranslational downregulation of the TFIIH subunit p62
    • Kalveram B., Lihoradova O., Ikegami T. NSs protein of rift valley fever virus promotes posttranslational downregulation of the TFIIH subunit p62. J Virol 2011, 85:6234-6243.
    • (2011) J Virol , vol.85 , pp. 6234-6243
    • Kalveram, B.1    Lihoradova, O.2    Ikegami, T.3
  • 114
    • 3843130779 scopus 로고    scopus 로고
    • Inhibition of RNA polymerase II phosphorylation by a viral interferon antagonist
    • Thomas D., Blakqori G., Wagner V., Banholzer M., Kessler N., Elliott R.M., et al. Inhibition of RNA polymerase II phosphorylation by a viral interferon antagonist. J Biol Chem 2004, 279:31471-31477.
    • (2004) J Biol Chem , vol.279 , pp. 31471-31477
    • Thomas, D.1    Blakqori, G.2    Wagner, V.3    Banholzer, M.4    Kessler, N.5    Elliott, R.M.6
  • 115
    • 79952792593 scopus 로고    scopus 로고
    • Interferon antagonist NSs of La Crosse virus triggers a DNA damage response-like degradation of transcribing RNA polymerase II
    • Verbruggen P., Ruf M., Blakqori G., Overby A.K., Heidemann M., Eick D., et al. Interferon antagonist NSs of La Crosse virus triggers a DNA damage response-like degradation of transcribing RNA polymerase II. J Biol Chem 2011, 286:3681-3692.
    • (2011) J Biol Chem , vol.286 , pp. 3681-3692
    • Verbruggen, P.1    Ruf, M.2    Blakqori, G.3    Overby, A.K.4    Heidemann, M.5    Eick, D.6
  • 116
    • 3242813113 scopus 로고    scopus 로고
    • The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses
    • Yoneyama M., Kikuchi M., Natsukawa T., Shinobu N., Imaizumi T., Miyagishi M., et al. The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. Nat Immunol 2004, 5:730-737.
    • (2004) Nat Immunol , vol.5 , pp. 730-737
    • Yoneyama, M.1    Kikuchi, M.2    Natsukawa, T.3    Shinobu, N.4    Imaizumi, T.5    Miyagishi, M.6
  • 117
    • 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
  • 118
    • 34547960175 scopus 로고    scopus 로고
    • Small self-RNA generated by RNase L amplifies antiviral innate immunity
    • Malathi K., Dong B., Gale M., Silverman R.H. Small self-RNA generated by RNase L amplifies antiviral innate immunity. Nature 2007, 448:816-819.
    • (2007) Nature , vol.448 , pp. 816-819
    • Malathi, K.1    Dong, B.2    Gale, M.3    Silverman, R.H.4
  • 119
    • 84897407806 scopus 로고    scopus 로고
    • DHX36 enhances RIG-I signaling by facilitating PKR-mediated antiviral stress granule formation
    • Yoo J.S., Takahasi K., Ng C.S., Ouda R., Onomoto K., Yoneyama M., et al. DHX36 enhances RIG-I signaling by facilitating PKR-mediated antiviral stress granule formation. PLoS Pathogens 2014, 10:e1004012.
    • (2014) PLoS Pathogens , vol.10 , pp. e1004012
    • Yoo, J.S.1    Takahasi, K.2    Ng, C.S.3    Ouda, R.4    Onomoto, K.5    Yoneyama, M.6


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