메뉴 건너뛰기




Volumn 6, Issue 12, 2014, Pages 4999-5027

Interferon induction by RNA viruses and antagonism by viral pathogens

Author keywords

Interferon induction; RLR; TLR; Viral antagonism

Indexed keywords

ALPHA INTERFERON; ALPHA INTERFERON RECEPTOR; ALPHA INTERFERON RECEPTOR 1; ALPHA INTERFERON RECEPTOR 2; BETA INTERFERON; CD4 ANTIGEN; DEUBIQUITINASE; GAMMA INTERFERON; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON REGULATORY FACTOR 3; INTERFERON REGULATORY FACTOR 7; INTERLEUKIN 1 RECEPTOR ASSOCIATED KINASE 1; MYELOID DIFFERENTIATION FACTOR 88; PATTERN RECOGNITION RECEPTOR; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; RETINOIC ACID INDUCIBLE PROTEIN I; SUMO 2 PROTEIN; SUMO 3 PROTEIN; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 11; TOLL LIKE RECEPTOR 20; TOLL LIKE RECEPTOR 4; TOLL LIKE RECEPTOR 7; TOLL LIKE RECEPTOR 8; TOLL LIKE RECEPTOR ADAPTOR MOLECULE 1; TOLL LIKE RECEPTOR ADAPTOR MOLECULE 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 3; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; UNCLASSIFIED DRUG; UNINDEXED DRUG; INTERFERON;

EID: 84917693019     PISSN: None     EISSN: 19994915     Source Type: Journal    
DOI: 10.3390/v6124999     Document Type: Review
Times cited : (54)

References (189)
  • 1
    • 0020002134 scopus 로고
    • Biochemistry of interferons and their actions
    • Lengyel, P. Biochemistry of interferons and their actions. Annu. Rev. Biochem. 1982, 51, 251-282.
    • (1982) Annu. Rev. Biochem , vol.51 , pp. 251-282
    • Lengyel, P.1
  • 3
    • 34547099363 scopus 로고    scopus 로고
    • The interferons: 50 years after their discovery, there is much more to learn
    • Pestka, S. The interferons: 50 years after their discovery, there is much more to learn. J. Biol. Chem. 2007, 282, 20047-20051.
    • (2007) J. Biol. Chem , vol.282 , pp. 20047-20051
    • Pestka, S.1
  • 5
    • 9644262469 scopus 로고    scopus 로고
    • Interferons, interferon-like cytokines, and their receptors
    • Pestka, S.; Krause, C. D.; Walter, M. R. Interferons, interferon-like cytokines, and their receptors. Immunol. Rev. 2004, 202, 8-32.
    • (2004) Immunol. Rev , vol.202 , pp. 8-32
    • Pestka, S.1    Krause, C.D.2    Walter, M.R.3
  • 8
    • 3442888513 scopus 로고    scopus 로고
    • The expanded family of class II cytokines that share the IL-10 receptor-2 (IL-10R2) chain
    • Donnelly, R. P.; Sheikh, F.; Kotenko, S. V.; Dickensheets, H. The expanded family of class II cytokines that share the IL-10 receptor-2 (IL-10R2) chain. J. Leukoc. Biol 2004, 76, 314-321.
    • (2004) J. Leukoc. Biol , vol.76 , pp. 314-321
    • Donnelly, R.P.1    Sheikh, F.2    Kotenko, S.V.3    Dickensheets, H.4
  • 9
    • 2342444617 scopus 로고    scopus 로고
    • Full house: 12 receptors for 27 cytokines
    • Kotenko, S. V.; Langer, J. A. Full house: 12 receptors for 27 cytokines. Int. Immunopharmacol. 2004, 4, 593-608.
    • (2004) Int. Immunopharmacol , vol.4 , pp. 593-608
    • Kotenko, S.V.1    Langer, J.A.2
  • 10
    • 65549165903 scopus 로고    scopus 로고
    • Interferons and viral infections
    • Fensterl, V.; Sen, G. C. Interferons and viral infections. Biofactors 2009, 35, 14-20.
    • (2009) Biofactors , vol.35 , pp. 14-20
    • Fensterl, V.1    Sen, G.C.2
  • 12
    • 17644372733 scopus 로고    scopus 로고
    • IPC: Professional type 1 interferon-producing cells and plasmacytoid dendritic cell precursors
    • Liu, Y. J. IPC: Professional type 1 interferon-producing cells and plasmacytoid dendritic cell precursors. Annu. Rev. Immunol. 2005, 23, 275-306.
    • (2005) Annu. Rev. Immunol , vol.23 , pp. 275-306
    • Liu, Y.J.1
  • 14
    • 68849114353 scopus 로고    scopus 로고
    • Receptor density is key to the alpha2/beta interferon differential activities
    • Moraga, I.; Harari, D.; Schreiber, G.; Uze, G.; Pellegrini, S. Receptor density is key to the alpha2/beta interferon differential activities. Mol. Cell. Biol. 2009, 29, 4778-4787.
    • (2009) Mol. Cell. Biol , vol.29 , pp. 4778-4787
    • Moraga, I.1    Harari, D.2    Schreiber, G.3    Uze, G.4    Pellegrini, S.5
  • 15
    • 33644522358 scopus 로고    scopus 로고
    • Inquiring into the differential action of interferons (IFNs): An IFN-alpha2 mutant with enhanced affinity to IFNAR1 is functionally similar to IFN-beta
    • Jaitin, D. A.; Roisman, L. C.; Jaks, E.; Gavutis, M.; Piehler, J.; van der Heyden, J.; Uze, G.; Schreiber, G. Inquiring into the differential action of interferons (IFNs): An IFN-alpha2 mutant with enhanced affinity to IFNAR1 is functionally similar to IFN-beta. Mol. Cell. Biol. 2006, 26, 1888-1897.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 1888-1897
    • Jaitin, D.A.1    Roisman, L.C.2    Jaks, E.3    Gavutis, M.4    Piehler, J.5    van der Heyden, J.6    Uze, G.7    Schreiber, G.8
  • 16
    • 57749092917 scopus 로고    scopus 로고
    • The stability of the ternary interferon-receptor complex rather than the affinity to the individual subunits dictates differential biological activities
    • Kalie, E.; Jaitin, D. A.; Podoplelova, Y.; Piehler, J.; Schreiber, G. The stability of the ternary interferon-receptor complex rather than the affinity to the individual subunits dictates differential biological activities. J. Biol. Chem. 2008, 283, 32925-32936.
    • (2008) J. Biol. Chem , vol.283 , pp. 32925-32936
    • Kalie, E.1    Jaitin, D.A.2    Podoplelova, Y.3    Piehler, J.4    Schreiber, G.5
  • 19
    • 0024449635 scopus 로고
    • Interactions of alpha-and gamma-interferon in the transcriptional regulation of the gene encoding a guanylate-binding protein
    • Decker, T.; Lew, D. J.; Cheng, Y. S.; Levy, D. E.; Darnell, J. E., Jr. Interactions of alpha-and gamma-interferon in the transcriptional regulation of the gene encoding a guanylate-binding protein. EMBO J. 1989, 8, 2009-2014.
    • (1989) EMBO J , vol.8 , pp. 2009-2014
    • Decker, T.1    Lew, D.J.2    Cheng, Y.S.3    Levy, D.E.4    Darnell, J.E.5
  • 20
    • 0024388159 scopus 로고
    • Alpha interferon and gamma interferon stimulate transcription of a single gene through different signal transduction pathways
    • Lew, D. J.; Decker, T.; Darnell, J. E., Jr. Alpha interferon and gamma interferon stimulate transcription of a single gene through different signal transduction pathways. Mol. Cell. Biol. 1989, 9, 5404-5411.
    • (1989) Mol. Cell. Biol , vol.9 , pp. 5404-5411
    • Lew, D.J.1    Decker, T.2    Darnell, J.E.3
  • 22
    • 77954754505 scopus 로고    scopus 로고
    • Induction of type I interferon by RNA viruses: Cellular receptors and their substrates
    • Baum, A.; Garcia-Sastre, A. Induction of type I interferon by RNA viruses: Cellular receptors and their substrates. Amino Acids 2010, 38, 1283-1299.
    • (2010) Amino Acids , vol.38 , pp. 1283-1299
    • Baum, A.1    Garcia-Sastre, A.2
  • 23
    • 0029730738 scopus 로고    scopus 로고
    • A conserved signaling pathway: The Drosophila toll-dorsal pathway
    • Belvin, M. P.; Anderson, K. V. A conserved signaling pathway: The Drosophila toll-dorsal pathway. Annu. Rev. Cell Dev. Biol. 1996, 12, 393-416.
    • (1996) Annu. Rev. Cell Dev. Biol , vol.12 , pp. 393-416
    • Belvin, M.P.1    Anderson, K.V.2
  • 24
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • Medzhitov, R.; Preston-Hurlburt, P.; Janeway, C. A., Jr. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 1997, 388, 394-397.
    • (1997) Nature , vol.388 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway, C.A.3
  • 25
    • 35349016235 scopus 로고    scopus 로고
    • Recognition of microorganisms and activation of the immune response
    • Medzhitov, R. Recognition of microorganisms and activation of the immune response. Nature 2007, 449, 819-826.
    • (2007) Nature , vol.449 , pp. 819-826
    • Medzhitov, R.1
  • 27
    • 0019133661 scopus 로고
    • Mutations affecting segment number and polarity in Drosophila
    • Nusslein-Volhard, C.; Wieschaus, E. Mutations affecting segment number and polarity in Drosophila. Nature 1980, 287, 795-801.
    • (1980) Nature , vol.287 , pp. 795-801
    • Nusslein-Volhard, C.1    Wieschaus, E.2
  • 28
    • 0031890394 scopus 로고    scopus 로고
    • Drosophila immune responses as models for human immunity
    • Dushay, M. S.; Eldon, E. D. Drosophila immune responses as models for human immunity. Am. J. Hum. Genet. 1998, 62, 10-14.
    • (1998) Am. J. Hum. Genet , vol.62 , pp. 10-14
    • Dushay, M.S.1    Eldon, E.D.2
  • 29
    • 0013655342 scopus 로고
    • Periodicity of leucine and tandem repetition of a 24-amino acid segment in the primary structure of leucine-rich alpha 2-glycoprotein of human serum
    • Takahashi, N.; Takahashi, Y.; Putnam, F. W. Periodicity of leucine and tandem repetition of a 24-amino acid segment in the primary structure of leucine-rich alpha 2-glycoprotein of human serum. Proc. Natl. Acad. Sci. USA 1985, 82, 1906-1910.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1906-1910
    • Takahashi, N.1    Takahashi, Y.2    Putnam, F.W.3
  • 30
    • 0025774776 scopus 로고
    • Drosophila Toll and IL-1 receptor
    • Gay, N. J.; Keith, F. J. Drosophila Toll and IL-1 receptor. Nature 1991, 351, 355-356.
    • (1991) Nature , vol.351 , pp. 355-356
    • Gay, N.J.1    Keith, F.J.2
  • 31
    • 0025804653 scopus 로고
    • Dominant and recessive mutations define functional domains of Toll, a transmembrane protein required for dorsal-ventral polarity in the Drosophila embryo
    • Schneider, D. S.; Hudson, K. L.; Lin, T. Y.; Anderson, K. V. Dominant and recessive mutations define functional domains of Toll, a transmembrane protein required for dorsal-ventral polarity in the Drosophila embryo. Genes Dev. 1991, 5, 797-807.
    • (1991) Genes Dev , vol.5 , pp. 797-807
    • Schneider, D.S.1    Hudson, K.L.2    Lin, T.Y.3    Anderson, K.V.4
  • 32
    • 0028167111 scopus 로고
    • The spatzle gene encodes a component of the extracellular signaling pathway establishing the dorsal-ventral pattern of the Drosophila embryo
    • Morisato, D.; Anderson, K. V. The spatzle gene encodes a component of the extracellular signaling pathway establishing the dorsal-ventral pattern of the Drosophila embryo. Cell 1994, 76, 677-688.
    • (1994) Cell , vol.76 , pp. 677-688
    • Morisato, D.1    Anderson, K.V.2
  • 33
    • 0028922245 scopus 로고
    • Signals from the IL-1 receptor homolog, Toll, can activate an immune response in a Drosophila hemocyte cell line
    • Rosetto, M.; Engstrom, Y.; Baldari, C. T.; Telford, J. L.; Hultmark, D. Signals from the IL-1 receptor homolog, Toll, can activate an immune response in a Drosophila hemocyte cell line. Biochem. Biophys. Res. Commun. 1995, 209, 111-116.
    • (1995) Biochem. Biophys. Res. Commun , vol.209 , pp. 111-116
    • Rosetto, M.1    Engstrom, Y.2    Baldari, C.T.3    Telford, J.L.4    Hultmark, D.5
  • 34
    • 0030595339 scopus 로고    scopus 로고
    • The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults
    • Lemaitre, B.; Nicolas, E.; Michaut, L.; Reichhart, J. M.; Hoffmann, J. A. The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 1996, 86, 973-983.
    • (1996) Cell , vol.86 , pp. 973-983
    • Lemaitre, B.1    Nicolas, E.2    Michaut, L.3    Reichhart, J.M.4    Hoffmann, J.A.5
  • 35
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Janeway, C. A., Jr. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb. Symp. Quant. Biol 1989, 54, 1-13.
    • (1989) Cold Spring Harb. Symp. Quant. Biol , vol.54 , pp. 1-13
    • Janeway, C.A.1
  • 37
    • 0028038271 scopus 로고
    • Expression of a novel Toll-like gene spans the parasegment boundary and contributes to hedgehog function in the adult eye of Drosophila
    • Chiang, C.; Beachy, P. A. Expression of a novel Toll-like gene spans the parasegment boundary and contributes to hedgehog function in the adult eye of Drosophila. Mech. Dev. 1994, 47, 225-239.
    • (1994) Mech. Dev , vol.47 , pp. 225-239
    • Chiang, C.1    Beachy, P.A.2
  • 39
    • 0034457684 scopus 로고    scopus 로고
    • Cloning and characterization of a sub-family of human toll-like receptors: HTLR7, hTLR8 and hTLR9
    • Chuang, T. H.; Ulevitch, R. J. Cloning and characterization of a sub-family of human toll-like receptors: hTLR7, hTLR8 and hTLR9. Eur. Cytokine Netw. 2000, 11, 372-378.
    • (2000) Eur. Cytokine Netw , vol.11 , pp. 372-378
    • Chuang, T.H.1    Ulevitch, R.J.2
  • 40
    • 0035911644 scopus 로고    scopus 로고
    • Identification of hTLR10: A novel human Toll-like receptor preferentially expressed in immune cells
    • Chuang, T.; Ulevitch, R. J. Identification of hTLR10: A novel human Toll-like receptor preferentially expressed in immune cells. Biochim. Biophys. Acta 2001, 1518, 157-161.
    • (2001) Biochim. Biophys. Acta , vol.1518 , pp. 157-161
    • Chuang, T.1    Ulevitch, R.J.2
  • 41
    • 24744459433 scopus 로고    scopus 로고
    • Of mice and man: TLR11 (finally) finds profilin
    • Lauw, F. N.; Caffrey, D. R.; Golenbock, D. T. Of mice and man: TLR11 (finally) finds profilin. Trends Immunol. 2005, 26, 509-511.
    • (2005) Trends Immunol , vol.26 , pp. 509-511
    • Lauw, F.N.1    Caffrey, D.R.2    Golenbock, D.T.3
  • 43
    • 0346157290 scopus 로고    scopus 로고
    • Innate immunity: An overview
    • Beutler, B. Innate immunity: An overview. Mol. Immunol. 2004, 40, 845-859.
    • (2004) Mol. Immunol , vol.40 , pp. 845-859
    • Beutler, B.1
  • 44
    • 20044368019 scopus 로고    scopus 로고
    • Human TLR10 is a functional receptor, expressed by B cells and plasmacytoid dendritic cells, which activates gene transcription through MyD88
    • Hasan, U.; Chaffois, C.; Gaillard, C.; Saulnier, V.; Merck, E.; Tancredi, S.; Guiet, C.; Briere, F.; Vlach, J.; Lebecque, S.; et al. Human TLR10 is a functional receptor, expressed by B cells and plasmacytoid dendritic cells, which activates gene transcription through MyD88. J. Immunol. 2005, 174, 2942-2950.
    • (2005) J. Immunol , vol.174 , pp. 2942-2950
    • Hasan, U.1    Chaffois, C.2    Gaillard, C.3    Saulnier, V.4    Merck, E.5    Tancredi, S.6    Guiet, C.7    Briere, F.8    Vlach, J.9    Lebecque, S.10
  • 46
    • 35748935892 scopus 로고    scopus 로고
    • Divergent Toll-like receptors in catfish (Ictalurus punctatus): TLR5S, TLR20, TLR21
    • Baoprasertkul, P.; Xu, P.; Peatman, E.; Kucuktas, H.; Liu, Z. Divergent Toll-like receptors in catfish (Ictalurus punctatus): TLR5S, TLR20, TLR21. Fish Shellfish Immunol. 2007, 23, 1218-1230.
    • (2007) Fish Shellfish Immunol , vol.23 , pp. 1218-1230
    • Baoprasertkul, P.1    Xu, P.2    Peatman, E.3    Kucuktas, H.4    Liu, Z.5
  • 47
    • 80455168991 scopus 로고    scopus 로고
    • Toll-like receptors in bony fish: From genomics to function
    • Palti, Y. Toll-like receptors in bony fish: From genomics to function. Dev. Comp. Immunol. 2011, 35, 1263-1272.
    • (2011) Dev. Comp. Immunol , vol.35 , pp. 1263-1272
    • Palti, Y.1
  • 48
    • 56549116047 scopus 로고    scopus 로고
    • Toll-like receptor and RIG-I-like receptor signaling
    • Kawai, T.; Akira, S. Toll-like receptor and RIG-I-like receptor signaling. Ann. N. Y. Acad. Sci. 2008, 1143, 1-20.
    • (2008) Ann. N.Y. Acad. Sci , vol.1143 , pp. 1-20
    • Kawai, T.1    Akira, S.2
  • 49
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtues of a nonclonal system of recognition
    • Medzhitov, R.; Janeway, C. A., Jr. Innate immunity: The virtues of a nonclonal system of recognition. Cell 1997, 91, 295-298.
    • (1997) Cell , vol.91 , pp. 295-298
    • Medzhitov, R.1    Janeway, C.A.2
  • 52
    • 0014425756 scopus 로고
    • Genetic control of leucocyte responses to endotoxin
    • Sultzer, B. M. Genetic control of leucocyte responses to endotoxin. Nature 1968, 219, 1253-1254.
    • (1968) Nature , vol.219 , pp. 1253-1254
    • Sultzer, B.M.1
  • 54
    • 0017752368 scopus 로고
    • Genetic analysis of generation of serum interferon by bacterial lipopolysaccharide
    • Apte, R. N.; Ascher, O.; Pluznik, D. H. Genetic analysis of generation of serum interferon by bacterial lipopolysaccharide. J. Immunol. 1977, 119, 1898-1902.
    • (1977) J. Immunol , vol.119 , pp. 1898-1902
    • Apte, R.N.1    Ascher, O.2    Pluznik, D.H.3
  • 55
    • 0018858071 scopus 로고
    • The primary role of lymphoreticular cells in the mediation of host responses to bacterial endotoxim
    • Michalek, S. M.; Moore, R. N.; McGhee, J. R.; Rosenstreich, D. L.; Mergenhagen, S. E. The primary role of lymphoreticular cells in the mediation of host responses to bacterial endotoxim. J. Infect. Dis. 1980, 141, 55-63.
    • (1980) J. Infect. Dis , vol.141 , pp. 55-63
    • Michalek, S.M.1    Moore, R.N.2    McGhee, J.R.3    Rosenstreich, D.L.4    Mergenhagen, S.E.5
  • 56
    • 0033120081 scopus 로고    scopus 로고
    • Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: Evidence for TLR4 as the Lps gene product
    • Hoshino, K.; Takeuchi, O.; Kawai, T.; Sanjo, H.; Ogawa, T.; Takeda, Y.; Takeda, K.; Akira, S. Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: Evidence for TLR4 as the Lps gene product. J. Immunol. 1999, 162, 3749-3752.
    • (1999) J. Immunol , vol.162 , pp. 3749-3752
    • Hoshino, K.1    Takeuchi, O.2    Kawai, T.3    Sanjo, H.4    Ogawa, T.5    Takeda, Y.6    Takeda, K.7    Akira, S.8
  • 57
    • 0033532629 scopus 로고    scopus 로고
    • MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4
    • Shimazu, R.; Akashi, S.; Ogata, H.; Nagai, Y.; Fukudome, K.; Miyake, K.; Kimoto, M. MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J. Exp. Med. 1999, 189, 1777-1782.
    • (1999) J. Exp. Med , vol.189 , pp. 1777-1782
    • Shimazu, R.1    Akashi, S.2    Ogata, H.3    Nagai, Y.4    Fukudome, K.5    Miyake, K.6    Kimoto, M.7
  • 59
    • 34548608447 scopus 로고    scopus 로고
    • Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide
    • Jin, M. S.; Kim, S. E.; Heo, J. Y.; Lee, M. E.; Kim, H. M.; Paik, S. G.; Lee, H.; Lee, J. O. Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide. Cell 2007, 130, 1071-1082.
    • (2007) Cell , vol.130 , pp. 1071-1082
    • Jin, M.S.1    Kim, S.E.2    Heo, J.Y.3    Lee, M.E.4    Kim, H.M.5    Paik, S.G.6    Lee, H.7    Lee, J.O.8
  • 60
    • 0033580949 scopus 로고    scopus 로고
    • Peptidoglycan-and lipoteichoic acid-induced cell activation is mediated by toll-like receptor 2
    • Schwandner, R.; Dziarski, R.; Wesche, H.; Rothe, M.; Kirschning, C. J. Peptidoglycan-and lipoteichoic acid-induced cell activation is mediated by toll-like receptor 2. J. Biol. Chem. 1999, 274, 17406-17409.
    • (1999) J. Biol. Chem , vol.274 , pp. 17406-17409
    • Schwandner, R.1    Dziarski, R.2    Wesche, H.3    Rothe, M.4    Kirschning, C.J.5
  • 61
    • 0035909372 scopus 로고    scopus 로고
    • Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3
    • Alexopoulou, L.; Holt, A. C.; Medzhitov, R.; Flavell, R. A. Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3. Nature 2001, 413, 732-738.
    • (2001) Nature , vol.413 , pp. 732-738
    • Alexopoulou, L.1    Holt, A.C.2    Medzhitov, R.3    Flavell, R.A.4
  • 63
    • 1542317550 scopus 로고    scopus 로고
    • Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA
    • Diebold, S. S.; Kaisho, T.; Hemmi, H.; Akira, S.; Reis E Sousa, C. Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA. Science 2004, 303, 1529-1531.
    • (2004) Science , vol.303 , pp. 1529-1531
    • Diebold, S.S.1    Kaisho, T.2    Hemmi, H.3    Akira, S.4    Reis, E.5    Sousa, C.6
  • 68
    • 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
  • 71
    • 84861558147 scopus 로고    scopus 로고
    • The origin and properties of extracellular DNA: From PAMP to DAMP
    • Pisetsky, D. S. The origin and properties of extracellular DNA: From PAMP to DAMP. Clin. Immunol. 2012, 144, 32-40.
    • (2012) Clin. Immunol , vol.144 , pp. 32-40
    • Pisetsky, D.S.1
  • 72
    • 23744454577 scopus 로고    scopus 로고
    • TLR signalling and activation of IRFs: Revisiting old friends from the NF-kappaB pathway
    • Moynagh, P. N. TLR signalling and activation of IRFs: Revisiting old friends from the NF-kappaB pathway. Trends Immunol. 2005, 26, 469-476.
    • (2005) Trends Immunol , vol.26 , pp. 469-476
    • Moynagh, P.N.1
  • 73
    • 36049033394 scopus 로고    scopus 로고
    • Signaling to NF-kappaB by Toll-like receptors
    • Kawai, T.; Akira, S. Signaling to NF-kappaB by Toll-like receptors. Trends Mol. Med. 2007, 13, 460-469.
    • (2007) Trends Mol. Med , vol.13 , pp. 460-469
    • Kawai, T.1    Akira, S.2
  • 74
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira, S.; Takeda, K. Toll-like receptor signalling. Nat. Rev. Immunol. 2004, 4, 499-511.
    • (2004) Nat. Rev. Immunol , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 77
    • 34248570795 scopus 로고    scopus 로고
    • Ubiquitin-mediated activation of TAK1 and IKK
    • Adhikari, A.; Xu, M.; Chen, Z. J. Ubiquitin-mediated activation of TAK1 and IKK. Oncogene 2007, 26, 3214-3226.
    • (2007) Oncogene , vol.26 , pp. 3214-3226
    • Adhikari, A.1    Xu, M.2    Chen, Z.J.3
  • 78
    • 77951260924 scopus 로고    scopus 로고
    • The role of pattern-recognition receptors in innate immunity: Update on Toll-like receptors
    • Kawai, T.; Akira, S. The role of pattern-recognition receptors in innate immunity: Update on Toll-like receptors. Nat. Immunol. 2010, 11, 373-384.
    • (2010) Nat. Immunol , vol.11 , pp. 373-384
    • Kawai, T.1    Akira, S.2
  • 79
    • 15244349785 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells in immunity
    • Colonna, M.; Trinchieri, G.; Liu, Y. J. Plasmacytoid dendritic cells in immunity. Nat. Immunol. 2004, 5, 1219-1226.
    • (2004) Nat. Immunol , vol.5 , pp. 1219-1226
    • Colonna, M.1    Trinchieri, G.2    Liu, Y.J.3
  • 80
    • 5444274514 scopus 로고    scopus 로고
    • Interferon-alpha induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6
    • Kawai, T.; Sato, S.; Ishii, K. J.; Coban, C.; Hemmi, H.; Yamamoto, M.; Terai, K.; Matsuda, M.; Inoue, J.; Uematsu, S.; et al. Interferon-alpha induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6. Nat. Immunol. 2004, 5, 1061-1068.
    • (2004) Nat. Immunol , vol.5 , pp. 1061-1068
    • Kawai, T.1    Sato, S.2    Ishii, K.J.3    Coban, C.4    Hemmi, H.5    Yamamoto, M.6    Terai, K.7    Matsuda, M.8    Inoue, J.9    Uematsu, S.10
  • 82
    • 0037320451 scopus 로고    scopus 로고
    • TICAM-1, an adaptor molecule that participates in Toll-like receptor 3-mediated interferon-beta induction
    • Oshiumi, H.; Matsumoto, M.; Funami, K.; Akazawa, T.; Seya, T. TICAM-1, an adaptor molecule that participates in Toll-like receptor 3-mediated interferon-beta induction. Nat. Immunol. 2003, 4, 161-167.
    • (2003) Nat. Immunol , vol.4 , pp. 161-167
    • Oshiumi, H.1    Matsumoto, M.2    Funami, K.3    Akazawa, T.4    Seya, T.5
  • 83
    • 0141923690 scopus 로고    scopus 로고
    • Toll/IL-1 receptor domain-containing adaptor inducing IFN-beta (TRIF) associates with TNF receptor-associated factor 6 and TANK-binding kinase 1, and activates two distinct transcription factors, NF-kappa B and IFN-regulatory factor-3, in the Toll-like receptor signaling
    • Sato, S.; Sugiyama, M.; Yamamoto, M.; Watanabe, Y.; Kawai, T.; Takeda, K.; Akira, S. Toll/IL-1 receptor domain-containing adaptor inducing IFN-beta (TRIF) associates with TNF receptor-associated factor 6 and TANK-binding kinase 1, and activates two distinct transcription factors, NF-kappa B and IFN-regulatory factor-3, in the Toll-like receptor signaling. J. Immunol. 2003, 171, 4304-4310.
    • (2003) J. Immunol , vol.171 , pp. 4304-4310
    • Sato, S.1    Sugiyama, M.2    Yamamoto, M.3    Watanabe, Y.4    Kawai, T.5    Takeda, K.6    Akira, S.7
  • 84
    • 10844219793 scopus 로고    scopus 로고
    • Cutting Edge: NF-kappaB-activating kinase-associated protein 1 participates in TLR3/Toll-IL-1 homology domain-containing adapter molecule-1-mediated IFN regulatory factor 3 activation
    • Sasai, M.; Oshiumi, H.; Matsumoto, M.; Inoue, N.; Fujita, F.; Nakanishi, M.; Seya, T. Cutting Edge: NF-kappaB-activating kinase-associated protein 1 participates in TLR3/Toll-IL-1 homology domain-containing adapter molecule-1-mediated IFN regulatory factor 3 activation. J. Immunol. 2005, 174, 27-30.
    • (2005) J. Immunol , vol.174 , pp. 27-30
    • Sasai, M.1    Oshiumi, H.2    Matsumoto, M.3    Inoue, N.4    Fujita, F.5    Nakanishi, M.6    Seya, T.7
  • 85
    • 0038363463 scopus 로고    scopus 로고
    • Triggering the interferon antiviral response through an IKK-related pathway
    • Sharma, S.; tenOever, B. R.; Grandvaux, N.; Zhou, G. P.; Lin, R.; Hiscott, J. Triggering the interferon antiviral response through an IKK-related pathway. Science 2003, 300, 1148-1151.
    • (2003) Science , vol.300 , pp. 1148-1151
    • Sharma, S.1    tenOever, B.R.2    Grandvaux, N.3    Zhou, G.P.4    Lin, R.5    Hiscott, J.6
  • 86
    • 0345991221 scopus 로고    scopus 로고
    • TIR-containing adapter molecule (TICAM)-2, a bridging adapter recruiting to toll-like receptor 4 TICAM-1 that induces interferon-beta
    • Oshiumi, H.; Sasai, M.; Shida, K.; Fujita, T.; Matsumoto, M.; Seya, T. TIR-containing adapter molecule (TICAM)-2, a bridging adapter recruiting to toll-like receptor 4 TICAM-1 that induces interferon-beta. J. Biol. Chem. 2003, 278, 49751-49762.
    • (2003) J. Biol. Chem , vol.278 , pp. 49751-49762
    • Oshiumi, H.1    Sasai, M.2    Shida, K.3    Fujita, T.4    Matsumoto, M.5    Seya, T.6
  • 87
    • 33646908228 scopus 로고    scopus 로고
    • Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling
    • Kagan, J. C.; Medzhitov, R. Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling. Cell 2006, 125, 943-955.
    • (2006) Cell , vol.125 , pp. 943-955
    • Kagan, J.C.1    Medzhitov, R.2
  • 88
    • 0037153130 scopus 로고    scopus 로고
    • The adaptor molecule TIRAP provides signalling specificity for Toll-like receptors
    • Horng, T.; Barton, G. M.; Flavell, R. A.; Medzhitov, R. The adaptor molecule TIRAP provides signalling specificity for Toll-like receptors. Nature 2002, 420, 329-333.
    • (2002) Nature , vol.420 , pp. 329-333
    • Horng, T.1    Barton, G.M.2    Flavell, R.A.3    Medzhitov, R.4
  • 90
    • 0024344173 scopus 로고
    • Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes
    • Gorbalenya, A. E.; Koonin, E. V.; Donchenko, A. P.; Blinov, V. M. Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 1989, 17, 4713-4730.
    • (1989) Nucleic Acids Res , vol.17 , pp. 4713-4730
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 91
    • 78650048628 scopus 로고    scopus 로고
    • Function and regulation of retinoic acid-inducible gene-I
    • Matsumiya, T.; Stafforini, D. M. Function and regulation of retinoic acid-inducible gene-I. Crit. Rev. Immunol. 2010, 30, 489-513.
    • (2010) Crit. Rev. Immunol , vol.30 , pp. 489-513
    • Matsumiya, T.1    Stafforini, D.M.2
  • 93
    • 0033816530 scopus 로고    scopus 로고
    • An RNA helicase, RHIV-1, induced by porcine reproductive and respiratory syndrome virus (PRRSV) is mapped on porcine chromosome 10q13
    • Zhang, X.; Wang, C.; Schook, L. B.; Hawken, R. J.; Rutherford, M. S. An RNA helicase, RHIV-1, induced by porcine reproductive and respiratory syndrome virus (PRRSV) is mapped on porcine chromosome 10q13. Microb. Pathog. 2000, 28, 267-278.
    • (2000) Microb. Pathog , vol.28 , pp. 267-278
    • Zhang, X.1    Wang, C.2    Schook, L.B.3    Hawken, R.J.4    Rutherford, M.S.5
  • 94
    • 0034663166 scopus 로고    scopus 로고
    • Gene expression networks underlying retinoic acid-induced differentiation of acute promyelocytic leukemia cells
    • Liu, T. X.; Zhang, J. W.; Tao, J.; Zhang, R. B.; Zhang, Q. H.; Zhao, C. J.; Tong, J. H.; Lanotte, M.; Waxman, S.; Chen, S. J.; et al. Gene expression networks underlying retinoic acid-induced differentiation of acute promyelocytic leukemia cells. Blood 2000, 96, 1496-1504.
    • (2000) Blood , vol.96 , pp. 1496-1504
    • Liu, T.X.1    Zhang, J.W.2    Tao, J.3    Zhang, R.B.4    Zhang, Q.H.5    Zhao, C.J.6    Tong, J.H.7    Lanotte, M.8    Waxman, S.9    Chen, S.J.10
  • 96
    • 3843122128 scopus 로고    scopus 로고
    • Retinoic acid-inducible gene-I is induced by interferon-gamma and regulates the expression of interferon-gamma stimulated gene 15 in MCF-7 cells
    • Cui, X. F.; Imaizumi, T.; Yoshida, H.; Borden, E. C.; Satoh, K. Retinoic acid-inducible gene-I is induced by interferon-gamma and regulates the expression of interferon-gamma stimulated gene 15 in MCF-7 cells. Biochem. Cell Biol. 2004, 82, 401-405.
    • (2004) Biochem. Cell Biol , vol.82 , pp. 401-405
    • Cui, X.F.1    Imaizumi, T.2    Yoshida, H.3    Borden, E.C.4    Satoh, K.5
  • 99
    • 0032769247 scopus 로고    scopus 로고
    • Differentiation induction subtraction hybridization (DISH): A strategy for cloning genes displaying differential expression during growth arrest and terminal differentiation
    • Huang, F.; Adelman, J.; Jiang, H.; Goldstein, N. I.; Fisher, P. B. Differentiation induction subtraction hybridization (DISH): A strategy for cloning genes displaying differential expression during growth arrest and terminal differentiation. Gene 1999, 236, 125-131.
    • (1999) Gene , vol.236 , pp. 125-131
    • Huang, F.1    Adelman, J.2    Jiang, H.3    Goldstein, N.I.4    Fisher, P.B.5
  • 100
    • 0033542378 scopus 로고    scopus 로고
    • Identification and temporal expression pattern of genes modulated during irreversible growth arrest and terminal differentiation in human melanoma cells
    • Huang, F.; Adelman, J.; Jiang, H.; Goldstein, N. I.; Fisher, P. B. Identification and temporal expression pattern of genes modulated during irreversible growth arrest and terminal differentiation in human melanoma cells. Oncogene 1999, 18, 3546-3552.
    • (1999) Oncogene , vol.18 , pp. 3546-3552
    • Huang, F.1    Adelman, J.2    Jiang, H.3    Goldstein, N.I.4    Fisher, P.B.5
  • 101
    • 0037154176 scopus 로고    scopus 로고
    • mda-5: An interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties
    • Kang, D. C.; Gopalkrishnan, R. V.; Wu, Q.; Jankowsky, E.; Pyle, A. M.; Fisher, P. B. mda-5: An interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties. Proc. Natl. Acad. Sci. USA 2002, 99, 637-642.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 637-642
    • Kang, D.C.1    Gopalkrishnan, R.V.2    Wu, Q.3    Jankowsky, E.4    Pyle, A.M.5    Fisher, P.B.6
  • 102
    • 0035969246 scopus 로고    scopus 로고
    • Signal transducer and activator of transcription (Stat) 5 controls the proliferation and differentiation of mammary alveolar epithelium
    • Miyoshi, K.; Shillingford, J. M.; Smith, G. H.; Grimm, S. L.; Wagner, K. U.; Oka, T.; Rosen, J. M.; Robinson, G. W.; Hennighausen, L. Signal transducer and activator of transcription (Stat) 5 controls the proliferation and differentiation of mammary alveolar epithelium. J. Cell Biol. 2001, 155, 531-542.
    • (2001) J. Cell Biol , vol.155 , pp. 531-542
    • Miyoshi, K.1    Shillingford, J.M.2    Smith, G.H.3    Grimm, S.L.4    Wagner, K.U.5    Oka, T.6    Rosen, J.M.7    Robinson, G.W.8    Hennighausen, L.9
  • 103
    • 0035885853 scopus 로고    scopus 로고
    • The Stat3/5 locus encodes novel endoplasmic reticulum and helicase-like proteins that are preferentially expressed in normal and neoplastic mammary tissue
    • Cui, Y.; Li, M.; Walton, K. D.; Sun, K.; Hanover, J. A.; Furth, P. A.; Hennighausen, L. The Stat3/5 locus encodes novel endoplasmic reticulum and helicase-like proteins that are preferentially expressed in normal and neoplastic mammary tissue. Genomics 2001, 78, 129-134.
    • (2001) Genomics , vol.78 , pp. 129-134
    • Cui, Y.1    Li, M.2    Walton, K.D.3    Sun, K.4    Hanover, J.A.5    Furth, P.A.6    Hennighausen, L.7
  • 104
    • 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
  • 107
    • 1542306855 scopus 로고    scopus 로고
    • Interferon induction by siRNAs and ssRNAs synthesized by phage polymerase
    • Kim, D. H.; Longo, M.; Han, Y.; Lundberg, P.; Cantin, E.; Rossi, J. J. Interferon induction by siRNAs and ssRNAs synthesized by phage polymerase. Nat. Biotechnol. 2004, 22, 321-325.
    • (2004) Nat. Biotechnol , vol.22 , pp. 321-325
    • Kim, D.H.1    Longo, M.2    Han, Y.3    Lundberg, P.4    Cantin, E.5    Rossi, J.J.6
  • 108
    • 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
  • 109
    • 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.; Coch, C.; Janke, M.; Mihailovic, A.; Wardle, G.; 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    Coch, C.7    Janke, M.8    Mihailovic, A.9    Wardle, G.10
  • 110
    • 77954242369 scopus 로고    scopus 로고
    • The Chase for the RIG-I Ligand-Recent Advances
    • Schlee, M.; Hartmann, G. The Chase for the RIG-I Ligand-Recent Advances. Mol. Ther. 2010, 18, 1254-1262.
    • (2010) Mol. Ther , vol.18 , pp. 1254-1262
    • Schlee, M.1    Hartmann, G.2
  • 111
    • 68049092912 scopus 로고    scopus 로고
    • RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway
    • Chiu, Y. H.; Macmillan, J. B.; Chen, Z. J. RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell 2009, 138, 576-591.
    • (2009) Cell , vol.138 , pp. 576-591
    • Chiu, Y.H.1    Macmillan, J.B.2    Chen, Z.J.3
  • 113
    • 33744791510 scopus 로고    scopus 로고
    • Essential role of mda-5 in type I IFN responses to polyriboinosinic: Polyribocytidylic acid and encephalomyocarditis picornavirus
    • Gitlin, L.; Barchet, W.; Gilfillan, S.; Cella, M.; Beutler, B.; Flavell, R. A.; Diamond, M. S.; Colonna, M. Essential role of mda-5 in type I IFN responses to polyriboinosinic: Polyribocytidylic acid and encephalomyocarditis picornavirus. Proc. Natl. Acad. Sci. USA 2006, 103, 8459-8464.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8459-8464
    • Gitlin, L.1    Barchet, W.2    Gilfillan, S.3    Cella, M.4    Beutler, B.5    Flavell, R.A.6    Diamond, M.S.7    Colonna, M.8
  • 115
    • 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.; Hiiragi, A.; Dermody, T. S.; Fujita, T.; Akira, S. 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, 601-610.
    • (2008) J. Exp. Med , vol.205 , pp. 601-610
    • Kato, H.1    Takeuchi, O.2    Mikamo-Satoh, E.3    Hirai, R.4    Kawai, T.5    Matsushita, K.6    Hiiragi, A.7    Dermody, T.S.8    Fujita, T.9    Akira, S.10
  • 116
    • 79952125382 scopus 로고    scopus 로고
    • Activation of IFN-β; expression by a viral mRNA through RNase L and MDA5
    • Luthra, P.; Sun, D.; Silverman, R. H.; He, B. Activation of IFN-β; expression by a viral mRNA through RNase L and MDA5. Proc. Natl. Acad. Sci. USA 2011, 108, 2118-2123.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 2118-2123
    • Luthra, P.1    Sun, D.2    Silverman, R.H.3    He, B.4
  • 117
    • 33845431988 scopus 로고    scopus 로고
    • RNA-and virus-independent inhibition of antiviral signaling by RNA helicase LGP2
    • Komuro, A.; Horvath, C. M. RNA-and virus-independent inhibition of antiviral signaling by RNA helicase LGP2. J. Virol. 2006, 80, 12332-12342.
    • (2006) J. Virol , vol.80 , pp. 12332-12342
    • Komuro, A.1    Horvath, C.M.2
  • 125
    • 24944538819 scopus 로고    scopus 로고
    • VISA is an adapter protein required for virus-triggered IFN-beta signaling
    • Xu, L. G.; Wang, Y. Y.; Han, K. J.; Li, L. Y.; Zhai, Z.; Shu, H. B. VISA is an adapter protein required for virus-triggered IFN-beta signaling. Mol. Cell 2005, 19, 727-740.
    • (2005) Mol. Cell , vol.19 , pp. 727-740
    • Xu, L.G.1    Wang, Y.Y.2    Han, K.J.3    Li, L.Y.4    Zhai, Z.5    Shu, H.B.6
  • 126
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • Meylan, E.; Curran, J.; Hofmann, K.; Moradpour, D.; Binder, M.; Bartenschlager, R.; Tschopp, J. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature 2005, 437, 1167-1172.
    • (2005) Nature , vol.437 , pp. 1167-1172
    • Meylan, E.1    Curran, J.2    Hofmann, K.3    Moradpour, D.4    Binder, M.5    Bartenschlager, R.6    Tschopp, J.7
  • 127
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3
    • Seth, R. B.; Sun, L.; Ea, C. K.; Chen, Z. J. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3. Cell 2005, 122, 669-682.
    • (2005) Cell , vol.122 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.K.3    Chen, Z.J.4
  • 131
    • 79961133270 scopus 로고    scopus 로고
    • MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response
    • Hou, F.; Sun, L.; Zheng, H.; Skaug, B.; Jiang, Q. X.; Chen, Z. J. MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell 2011, 146, 448-461.
    • (2011) Cell , vol.146 , pp. 448-461
    • Hou, F.1    Sun, L.2    Zheng, H.3    Skaug, B.4    Jiang, Q.X.5    Chen, Z.J.6
  • 132
    • 24144475528 scopus 로고    scopus 로고
    • Connecting mitochondria and innate immunity
    • McWhirter, S. M.; Tenoever, B. R.; Maniatis, T. Connecting mitochondria and innate immunity. Cell 2005, 122, 645-647.
    • (2005) Cell , vol.122 , pp. 645-647
    • McWhirter, S.M.1    Tenoever, B.R.2    Maniatis, T.3
  • 134
    • 84904703858 scopus 로고    scopus 로고
    • Peroxisomal MAVS activates IRF1-mediated IFN-lambda production
    • Ding, S.; Robek, M. D. Peroxisomal MAVS activates IRF1-mediated IFN-lambda production. Nat. Immunol. 2014, 15, 700-701.
    • (2014) Nat. Immunol , vol.15 , pp. 700-701
    • Ding, S.1    Robek, M.D.2
  • 135
    • 9244236078 scopus 로고    scopus 로고
    • A FADD-dependent innate immune mechanism in mammalian cells
    • Balachandran, S.; Thomas, E.; Barber, G. N. A FADD-dependent innate immune mechanism in mammalian cells. Nature 2004, 432, 401-405.
    • (2004) Nature , vol.432 , pp. 401-405
    • Balachandran, S.1    Thomas, E.2    Barber, G.N.3
  • 136
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng, L.; Wang, C.; Spencer, E.; Yang, L.; Braun, A.; You, J.; Slaughter, C.; Pickart, C.; Chen, Z. J. Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 2000, 103, 51-61.
    • (2000) Cell , vol.103 , pp. 51-61
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 138
    • 84892606477 scopus 로고    scopus 로고
    • TRIM14 is a mitochondrial adaptor that facilitates retinoic acid-inducible gene-I-like receptor-mediated innate immune response
    • Zhou, Z.; Jia, X.; Xue, Q.; Dou, Z.; Ma, Y.; Zhao, Z.; Jiang, Z.; He, B.; Jin, Q.; Wang, J. TRIM14 is a mitochondrial adaptor that facilitates retinoic acid-inducible gene-I-like receptor-mediated innate immune response. Proc. Natl. Acad. Sci. USA 2014, 111, E245-E254.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. E245-E254
    • Zhou, Z.1    Jia, X.2    Xue, Q.3    Dou, Z.4    Ma, Y.5    Zhao, Z.6    Jiang, Z.7    He, B.8    Jin, Q.9    Wang, J.10
  • 139
    • 21344465240 scopus 로고    scopus 로고
    • TLR signalling and the function of dendritic cells
    • Hemmi, H.; Akira, S. TLR signalling and the function of dendritic cells. Chem. Immunol. Allergy 2005, 86, 120-135.
    • (2005) Chem. Immunol. Allergy , vol.86 , pp. 120-135
    • Hemmi, H.1    Akira, S.2
  • 140
    • 0742272509 scopus 로고    scopus 로고
    • Toll-like receptors and dendritic cells: For whom the bug tolls
    • Reis E Sousa, C. Toll-like receptors and dendritic cells: For whom the bug tolls. Semin. Immunol. 2004, 16, 27-34.
    • (2004) Semin. Immunol , vol.16 , pp. 27-34
    • Reis, E.1    Sousa, C.2
  • 141
    • 27744558575 scopus 로고    scopus 로고
    • The role of Toll-like receptors in the regulation of neutrophil migration, activation, and apoptosis
    • Sabroe, I.; Dower, S. K.; Whyte, M. K. The role of Toll-like receptors in the regulation of neutrophil migration, activation, and apoptosis. Clin. Infect. Dis. 2005, 41 (Suppl. 7), S421-S426.
    • (2005) Clin. Infect. Dis , vol.41 , pp. S421-S426
    • Sabroe, I.1    Dower, S.K.2    Whyte, M.K.3
  • 142
    • 34548411427 scopus 로고    scopus 로고
    • Regulating B-cell activation and survival in response to TLR signals
    • Gerondakis, S.; Grumont, R. J.; Banerjee, A. Regulating B-cell activation and survival in response to TLR signals. Immunol. Cell Biol. 2007, 85, 471-475.
    • (2007) Immunol. Cell Biol , vol.85 , pp. 471-475
    • Gerondakis, S.1    Grumont, R.J.2    Banerjee, A.3
  • 144
  • 145
    • 75649093343 scopus 로고    scopus 로고
    • Toll-like receptor signalling in the intestinal epithelium: How bacterial recognition shapes intestinal function
    • Abreu, M. T. Toll-like receptor signalling in the intestinal epithelium: How bacterial recognition shapes intestinal function. Nat. Rev. Immunol. 2010, 10, 131-144.
    • (2010) Nat. Rev. Immunol , vol.10 , pp. 131-144
    • Abreu, M.T.1
  • 149
    • 33846061693 scopus 로고    scopus 로고
    • Inhibition of retinoic acid-inducible gene I-mediated induction of beta interferon by the NS1 protein of influenza A virus
    • Mibayashi, M.; Martinez-Sobrido, L.; Loo, Y. M.; Cardenas, W. B.; Gale, M., Jr.; Garcia-Sastre, A. Inhibition of retinoic acid-inducible gene I-mediated induction of beta interferon by the NS1 protein of influenza A virus. J. Virol. 2007, 81, 514-524.
    • (2007) J. Virol , vol.81 , pp. 514-524
    • Mibayashi, M.1    Martinez-Sobrido, L.2    Loo, Y.M.3    Cardenas, W.B.4    Gale, M.5    Garcia-Sastre, A.6
  • 150
    • 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.; Randall, R. E. 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. USA 2004, 101, 17264-17269.
    • (2004) Proc. Natl. Acad. Sci. USA , 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    Randall, R.E.7
  • 151
    • 84857603541 scopus 로고    scopus 로고
    • Respiratory syncytial virus NS1 protein colocalizes with mitochondrial antiviral signaling protein MAVS following infection
    • Boyapalle, S.; Wong, T.; Garay, J.; Teng, M.; San Juan-Vergara, H.; Mohapatra, S. Respiratory syncytial virus NS1 protein colocalizes with mitochondrial antiviral signaling protein MAVS following infection. PLoS One 2012, 7, e29386.
    • (2012) PLoS One , vol.7
    • Boyapalle, S.1    Wong, T.2    Garay, J.3    Teng, M.4    San Juan-Vergara, H.5    Mohapatra, S.6
  • 152
    • 59449109932 scopus 로고    scopus 로고
    • Control of TANK-binding kinase 1-mediated signaling by the gamma(1)34. 5 protein of herpes simplex virus 1
    • Verpooten, D.; Ma, Y.; Hou, S.; Yan, Z.; He, B. Control of TANK-binding kinase 1-mediated signaling by the gamma(1)34. 5 protein of herpes simplex virus 1. J. Biol. Chem. 2009, 284, 1097-1105.
    • (2009) J. Biol. Chem , vol.284 , pp. 1097-1105
    • Verpooten, D.1    Ma, Y.2    Hou, S.3    Yan, Z.4    He, B.5
  • 153
    • 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
  • 154
    • 84892164414 scopus 로고    scopus 로고
    • Dengue virus subverts the interferon induction pathway via NS2B/3 protease-IkappaB kinase epsilon interaction
    • Anglero-Rodriguez, Y. I.; Pantoja, P.; Sariol, C. A. Dengue virus subverts the interferon induction pathway via NS2B/3 protease-IkappaB kinase epsilon interaction. Clin. Vaccine Immunol. 2014, 21, 29-38.
    • (2014) Clin. Vaccine Immunol , vol.21 , pp. 29-38
    • Anglero-Rodriguez, Y.I.1    Pantoja, P.2    Sariol, C.A.3
  • 155
    • 0032128003 scopus 로고    scopus 로고
    • Human papillomavirus 16 E6 oncoprotein binds to interferon regulatory factor-3 and inhibits its transcriptional activity
    • Ronco, L. V.; Karpova, A. Y.; Vidal, M.; Howley, P. M. Human papillomavirus 16 E6 oncoprotein binds to interferon regulatory factor-3 and inhibits its transcriptional activity. Genes Dev. 1998, 12, 2061-2072.
    • (1998) Genes Dev , vol.12 , pp. 2061-2072
    • Ronco, L.V.1    Karpova, A.Y.2    Vidal, M.3    Howley, P.M.4
  • 156
    • 70349807812 scopus 로고    scopus 로고
    • The viral RNA recognition sensor RIG-I is degraded during encephalomyocarditis virus (EMCV) infection
    • Papon, L.; Oteiza, A.; Imaizumi, T.; Kato, H.; Brocchi, E.; Lawson, T. G.; Akira, S.; Mechti, N. The viral RNA recognition sensor RIG-I is degraded during encephalomyocarditis virus (EMCV) infection. Virology 2009, 393, 311-318.
    • (2009) Virology , vol.393 , pp. 311-318
    • Papon, L.1    Oteiza, A.2    Imaizumi, T.3    Kato, H.4    Brocchi, E.5    Lawson, T.G.6    Akira, S.7    Mechti, N.8
  • 157
    • 79960598740 scopus 로고    scopus 로고
    • Disruption of TLR3 signaling due to cleavage of TRIF by the hepatitis A virus protease-polymerase processing intermediate, 3CD
    • Qu, L.; Feng, Z.; Yamane, D.; Liang, Y.; Lanford, R. E.; Li, K.; Lemon, S. M. Disruption of TLR3 signaling due to cleavage of TRIF by the hepatitis A virus protease-polymerase processing intermediate, 3CD. PLoS Pathog. 2011, 7, e1002169.
    • (2011) PLoS Pathog , vol.7
    • Qu, L.1    Feng, Z.2    Yamane, D.3    Liang, Y.4    Lanford, R.E.5    Li, K.6    Lemon, S.M.7
  • 160
    • 33947382185 scopus 로고    scopus 로고
    • Classical swine fever virus Npro interacts with interferon regulatory factor 3 and induces its proteasomal degradation
    • Bauhofer, O.; Summerfield, A.; Sakoda, Y.; Tratschin, J. D.; Hofmann, M. A.; Ruggli, N. Classical swine fever virus Npro interacts with interferon regulatory factor 3 and induces its proteasomal degradation. J. Virol. 2007, 81, 3087-3096.
    • (2007) J. Virol , vol.81 , pp. 3087-3096
    • Bauhofer, O.1    Summerfield, A.2    Sakoda, Y.3    Tratschin, J.D.4    Hofmann, M.A.5    Ruggli, N.6
  • 161
    • 73949087536 scopus 로고    scopus 로고
    • Porcine reproductive and respiratory syndrome virus nonstructural protein 1beta modulates host innate immune response by antagonizing IRF3 activation
    • Beura, L. K.; Sarkar, S. N.; Kwon, B.; Subramaniam, S.; Jones, C.; Pattnaik, A. K.; Osorio, F. A. Porcine reproductive and respiratory syndrome virus nonstructural protein 1beta modulates host innate immune response by antagonizing IRF3 activation. J. Virol. 2010, 84, 1574-1584.
    • (2010) J. Virol , vol.84 , pp. 1574-1584
    • Beura, L.K.1    Sarkar, S.N.2    Kwon, B.3    Subramaniam, S.4    Jones, C.5    Pattnaik, A.K.6    Osorio, F.A.7
  • 162
    • 0037687422 scopus 로고    scopus 로고
    • Regulation of interferon regulatory factor-3 by the hepatitis C virus serine protease
    • Foy, E.; Li, K.; Wang, C.; Sumpter, R., Jr.; Ikeda, M.; Lemon, S. M.; Gale, M., Jr. Regulation of interferon regulatory factor-3 by the hepatitis C virus serine protease. Science 2003, 300, 1145-1148.
    • (2003) Science , vol.300 , pp. 1145-1148
    • Foy, E.1    Li, K.2    Wang, C.3    Sumpter, R.4    Ikeda, M.5    Lemon, S.M.6    Gale, M.7
  • 163
    • 77955290279 scopus 로고    scopus 로고
    • Hepatitis B virus polymerase inhibits RIG-I-and Toll-like 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.; Chen, J.; Wu, M.; Chen, H.; Kato, N.; Yuan, Z. Hepatitis B virus polymerase inhibits RIG-I-and Toll-like 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. 2010, 91, 2080-2090.
    • (2010) J. Gen. Virol , vol.91 , pp. 2080-2090
    • Yu, S.1    Chen, J.2    Wu, M.3    Chen, H.4    Kato, N.5    Yuan, Z.6
  • 164
    • 49149113373 scopus 로고    scopus 로고
    • Viral targeting of DEAD box protein 3 reveals its role in TBK1/IKKepsilon-mediated IRF activation
    • Schroder, M.; Baran, M.; Bowie, A. G. Viral targeting of DEAD box protein 3 reveals its role in TBK1/IKKepsilon-mediated IRF activation. EMBO J. 2008, 27, 2147-2157.
    • (2008) EMBO J , vol.27 , pp. 2147-2157
    • Schroder, M.1    Baran, M.2    Bowie, A.G.3
  • 166
    • 77956044074 scopus 로고    scopus 로고
    • Varicella-zoster virus immediate-early protein 62 blocks interferon regulatory factor 3 (IRF3) phosphorylation at key serine residues: A novel mechanism of IRF3 inhibition among herpesviruses
    • Sen, N.; Sommer, M.; Che, X.; White, K.; Ruyechan, W. T.; Arvin, A. M. Varicella-zoster virus immediate-early protein 62 blocks interferon regulatory factor 3 (IRF3) phosphorylation at key serine residues: A novel mechanism of IRF3 inhibition among herpesviruses. J. Virol. 2010, 84, 9240-9253.
    • (2010) J. Virol , vol.84 , pp. 9240-9253
    • Sen, N.1    Sommer, M.2    Che, X.3    White, K.4    Ruyechan, W.T.5    Arvin, A.M.6
  • 167
    • 33947627724 scopus 로고    scopus 로고
    • Recruitment of activated IRF-3 and CBP/p300 to herpes simplex virus ICP0 nuclear foci: Potential role in blocking IFN-beta induction
    • Melroe, G. T.; Silva, L.; Schaffer, P. A.; Knipe, D. M. Recruitment of activated IRF-3 and CBP/p300 to herpes simplex virus ICP0 nuclear foci: Potential role in blocking IFN-beta induction. Virology 2007, 360, 305-321.
    • (2007) Virology , vol.360 , pp. 305-321
    • Melroe, G.T.1    Silva, L.2    Schaffer, P.A.3    Knipe, D.M.4
  • 168
    • 70350004240 scopus 로고    scopus 로고
    • Key role of Ubc5 and lysine-63 polyubiquitination in viral activation of IRF3
    • Zeng, W.; Xu, M.; Liu, S.; Sun, L.; Chen, Z. J. Key role of Ubc5 and lysine-63 polyubiquitination in viral activation of IRF3. Mol. Cell 2009, 36, 315-325.
    • (2009) Mol. Cell , vol.36 , pp. 315-325
    • Zeng, W.1    Xu, M.2    Liu, S.3    Sun, L.4    Chen, Z.J.5
  • 169
    • 77951247349 scopus 로고    scopus 로고
    • Virus-triggered ubiquitination of TRAF3/6 by cIAP1/2 is essential for induction of interferon-beta (IFN-beta) and cellular antiviral response
    • Mao, A. P.; Li, S.; Zhong, B.; Li, Y.; Yan, J.; Li, Q.; Teng, C.; Shu, H. B. Virus-triggered ubiquitination of TRAF3/6 by cIAP1/2 is essential for induction of interferon-beta (IFN-beta) and cellular antiviral response. J. Biol. Chem. 2010, 285, 9470-9476.
    • (2010) J. Biol. Chem , vol.285 , pp. 9470-9476
    • Mao, A.P.1    Li, S.2    Zhong, B.3    Li, Y.4    Yan, J.5    Li, Q.6    Teng, C.7    Shu, H.B.8
  • 170
    • 84888292851 scopus 로고    scopus 로고
    • Dynamic regulation of innate immunity by ubiquitin and ubiquitin-like proteins
    • Liu, X.; Wang, Q.; Chen, W.; Wang, C. Dynamic regulation of innate immunity by ubiquitin and ubiquitin-like proteins. Cytokine Growth Factor Rev. 2013, 24, 559-570.
    • (2013) Cytokine Growth Factor Rev , vol.24 , pp. 559-570
    • Liu, X.1    Wang, Q.2    Chen, W.3    Wang, C.4
  • 171
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • Amerik, A. Y.; Hochstrasser, M. Mechanism and function of deubiquitinating enzymes. Biochim. Biophys. Acta 2004, 1695, 189-207.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 189-207
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 173
    • 78650053747 scopus 로고    scopus 로고
    • The cysteine protease domain of porcine reproductive and respiratory syndrome virus non-structural protein 2 antagonizes interferon regulatory factor 3 activation
    • Li, H.; Zheng, Z.; Zhou, P.; Zhang, B.; Shi, Z.; Hu, Q.; Wang, H. The cysteine protease domain of porcine reproductive and respiratory syndrome virus non-structural protein 2 antagonizes interferon regulatory factor 3 activation. J. Gen. Virol. 2010, 91, 2947-2958.
    • (2010) J. Gen. Virol , vol.91 , pp. 2947-2958
    • Li, H.1    Zheng, Z.2    Zhou, P.3    Zhang, B.4    Shi, Z.5    Hu, Q.6    Wang, H.7
  • 174
    • 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, S. R.; Fang, Y. The cysteine protease domain of porcine reproductive and respiratory syndrome virus nonstructural protein 2 possesses deubiquitinating and interferon antagonism functions. J. Virol. 2010, 84, 7832-7846.
    • (2010) J. Virol , vol.84 , pp. 7832-7846
    • Sun, Z.1    Chen, Z.2    Lawson, S.R.3    Fang, Y.4
  • 175
    • 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.; Fang, L.; Li, P.; Sun, L.; Fan, J.; Zhang, Q.; Luo, R.; Liu, X.; Li, K.; Chen, H.; et al. The leader proteinase of foot-and-mouth disease virus negatively regulates the type I interferon pathway by acting as a viral deubiquitinase. J. Virol. 2011, 85, 3758-3766.
    • (2011) J. Virol , vol.85 , pp. 3758-3766
    • Wang, D.1    Fang, L.2    Li, P.3    Sun, L.4    Fan, J.5    Zhang, Q.6    Luo, R.7    Liu, X.8    Li, K.9    Chen, H.10
  • 176
    • 84907445220 scopus 로고    scopus 로고
    • Hepatitis E Virus Inhibits Type I Interferon Induction by ORF1 Product
    • Nan, Y.; Yu, Y.; Ma, Z.; Khattar, S. K.; Fredericksen, B.; Zhang, Y. J. Hepatitis E Virus Inhibits Type I Interferon Induction by ORF1 Product. J. Virol. 2014, 88, 11924-11932.
    • (2014) J. Virol , vol.88 , pp. 11924-11932
    • Nan, Y.1    Yu, Y.2    Ma, Z.3    Khattar, S.K.4    Fredericksen, B.5    Zhang, Y.J.6
  • 177
    • 54449099430 scopus 로고    scopus 로고
    • Virus infection triggers SUMOylation of IRF3 and IRF7, leading to the negative regulation of type I interferon gene expression
    • Kubota, T.; Matsuoka, M.; Chang, T. H.; Tailor, P.; Sasaki, T.; Tashiro, M.; Kato, A.; Ozato, K. Virus infection triggers SUMOylation of IRF3 and IRF7, leading to the negative regulation of type I interferon gene expression. J. Biol. Chem. 2008, 283, 25660-25670.
    • (2008) J. Biol. Chem , vol.283 , pp. 25660-25670
    • Kubota, T.1    Matsuoka, M.2    Chang, T.H.3    Tailor, P.4    Sasaki, T.5    Tashiro, M.6    Kato, A.7    Ozato, K.8
  • 178
  • 181
    • 84871975770 scopus 로고    scopus 로고
    • The viral interferon regulatory factors of KSHV: Immunosuppressors or oncogenes?
    • Jacobs, S. R.; Damania, B. The viral interferon regulatory factors of KSHV: Immunosuppressors or oncogenes? Front. Immunol. 2011, 2, e19.
    • (2011) Front. Immunol , vol.2
    • Jacobs, S.R.1    Damania, B.2
  • 183
    • 0035864786 scopus 로고    scopus 로고
    • HHV-8 encoded vIRF-1 represses the interferon antiviral response by blocking IRF-3 recruitment of the CBP/p300 coactivators
    • Lin, R.; Genin, P.; Mamane, Y.; Sgarbanti, M.; Battistini, A.; Harrington, W. J., Jr.; Barber, G. N.; Hiscott, J. HHV-8 encoded vIRF-1 represses the interferon antiviral response by blocking IRF-3 recruitment of the CBP/p300 coactivators. Oncogene 2001, 20, 800-811.
    • (2001) Oncogene , vol.20 , pp. 800-811
    • Lin, R.1    Genin, P.2    Mamane, Y.3    Sgarbanti, M.4    Battistini, A.5    Harrington, W.J.6    Barber, G.N.7    Hiscott, J.8
  • 184
    • 0344564198 scopus 로고    scopus 로고
    • Functional analysis of human herpesvirus 8-encoded viral interferon regulatory factor 1 and its association with cellular interferon regulatory factors and p300
    • Burysek, L.; Yeow, W. S.; Lubyova, B.; Kellum, M.; Schafer, S. L.; Huang, Y. Q.; Pitha, P. M. Functional analysis of human herpesvirus 8-encoded viral interferon regulatory factor 1 and its association with cellular interferon regulatory factors and p300. J. Virol. 1999, 73, 7334-7342.
    • (1999) J. Virol , vol.73 , pp. 7334-7342
    • Burysek, L.1    Yeow, W.S.2    Lubyova, B.3    Kellum, M.4    Schafer, S.L.5    Huang, Y.Q.6    Pitha, P.M.7
  • 185
    • 0033508091 scopus 로고    scopus 로고
    • Unique properties of a second human herpesvirus 8-encoded interferon regulatory factor (vIRF-2)
    • Burysek, L.; Yeow, W. S.; Pitha, P. M. Unique properties of a second human herpesvirus 8-encoded interferon regulatory factor (vIRF-2). J. Hum. Virol. 1999, 2, 19-32.
    • (1999) J. Hum. Virol , vol.2 , pp. 19-32
    • Burysek, L.1    Yeow, W.S.2    Pitha, P.M.3
  • 186
    • 69949181061 scopus 로고    scopus 로고
    • Identification of caspase-mediated decay of interferon regulatory factor-3, exploited by a Kaposi sarcoma-associated herpesvirus immunoregulatory protein
    • Areste, C.; Mutocheluh, M.; Blackbourn, D. J. Identification of caspase-mediated decay of interferon regulatory factor-3, exploited by a Kaposi sarcoma-associated herpesvirus immunoregulatory protein. J. Biol. Chem. 2009, 284, 23272-23285.
    • (2009) J. Biol. Chem , vol.284 , pp. 23272-23285
    • Areste, C.1    Mutocheluh, M.2    Blackbourn, D.J.3
  • 187
    • 1542289919 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus-encoded vIRF-3 stimulates the transcriptional activity of cellular IRF-3 and IRF-7
    • Lubyova, B.; Kellum, M. J.; Frisancho, A. J.; Pitha, P. M. Kaposi's sarcoma-associated herpesvirus-encoded vIRF-3 stimulates the transcriptional activity of cellular IRF-3 and IRF-7. J. Biol. Chem. 2004, 279, 7643-7654.
    • (2004) J. Biol. Chem , vol.279 , pp. 7643-7654
    • Lubyova, B.1    Kellum, M.J.2    Frisancho, A.J.3    Pitha, P.M.4
  • 188
    • 34547135460 scopus 로고    scopus 로고
    • Inhibition of interferon regulatory factor 7 (IRF7)-mediated interferon signal transduction by the Kaposi's sarcoma-associated herpesvirus viral IRF homolog vIRF3
    • Joo, C. H.; Shin, Y. C.; Gack, M.; Wu, L.; Levy, D.; Jung, J. U. Inhibition of interferon regulatory factor 7 (IRF7)-mediated interferon signal transduction by the Kaposi's sarcoma-associated herpesvirus viral IRF homolog vIRF3. J. Virol. 2007, 81, 8282-8292.
    • (2007) J. Virol , vol.81 , pp. 8282-8292
    • Joo, C.H.1    Shin, Y.C.2    Gack, M.3    Wu, L.4    Levy, D.5    Jung, J.U.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.