메뉴 건너뛰기




Volumn 5, Issue JUN, 2014, Pages

Can't RIDD off viruses

Author keywords

IRE1; OAS; RIDD pathway; RNaseL; Unfolded protein response; UPR; Xbp1

Indexed keywords

2', 5' OLIGOADENYLATE SYNTHETASE; DOUBLE STRANDED RNA; ENZYME; INOSITOL REQUIRING ENZYME 1; INTERFERON; MESSENGER RNA; PATTERN RECOGNITION RECEPTOR; RIBONUCLEASE; RIBONUCLEASE L; RNA DIRECTED RNA POLYMERASE; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG; UNTRANSLATED RNA; VIRUS RNA;

EID: 84904887792     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2014.00292     Document Type: Review
Times cited : (14)

References (143)
  • 1
    • 33646826348 scopus 로고    scopus 로고
    • Parallels among positive-strand RNA viruses, reverse-transcribing viruses and double-stranded RNA viruses
    • doi: 10.1038/nrmicro1389
    • Ahlquist, P. (2006). Parallels among positive-strand RNA viruses, reverse-transcribing viruses and double-stranded RNA viruses. Nat. Rev. Microbiol. 4, 371-382. doi: 10.1038/nrmicro1389
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 371-382
    • Ahlquist, P.1
  • 2
    • 65049090018 scopus 로고    scopus 로고
    • Downmodulation of the RNA-binding protein, HuR, and cellular growth
    • doi: 10.1038/onc.2009.16
    • Al-Ahmadi, W., Al-Haj, L., Al-Mohanna, F. A., Silverman, R. H., and Khabar, K. S. (2009). Downmodulation of the RNA-binding protein, HuR, and cellular growth. Oncogene 28, 1782-1791. doi: 10.1038/onc.2009.16
    • (2009) Oncogene , vol.28 , pp. 1782-1791
    • Al-Ahmadi, W.1    Al-Haj, L.2    Al-Mohanna, F.A.3    Silverman, R.H.4    Khabar, K.S.5
  • 3
    • 84860529490 scopus 로고    scopus 로고
    • UU/UA dinucleotide frequency reduction in coding regions results in increased mRNA stability and protein expression
    • doi: 10.1038/mt.2012.29
    • Al-Saif, M., and Khabar, K. S. (2012). UU/UA dinucleotide frequency reduction in coding regions results in increased mRNA stability and protein expression. Mol. Ther. 20, 954-959. doi: 10.1038/mt.2012.29
    • (2012) Mol. Ther. , vol.20 , pp. 954-959
    • Al-Saif, M.1    Khabar, K.S.2
  • 4
    • 67650472415 scopus 로고    scopus 로고
    • Ribosomal protein mRNAs are primary targets of regulation in RNase-L-induced senescence
    • doi: 10.4161/rna.6.3.8526
    • Andersen, J. B., Mazan-Mamczarz, K., Zhan, M., Gorospe, M., and Hassel, B. A. (2009). Ribosomal protein mRNAs are primary targets of regulation in RNase-L-induced senescence. RNA Biol. 6, 305-315. doi: 10.4161/rna.6.3.8526
    • (2009) RNA Biol. , vol.6 , pp. 305-315
    • Andersen, J.B.1    Mazan-Mamczarz, K.2    Zhan, M.3    Gorospe, M.4    Hassel, B.A.5
  • 5
    • 82255164455 scopus 로고    scopus 로고
    • Nucleoside modifications in RNA limit activation of 2'-5'-oligoadenylate synthetase and increase resistance to cleavage by RNase L
    • doi: 10.1093/nar/gkr586
    • Anderson, B. R., Muramatsu, H., Jha, B. K., Silverman, R. H., Weissman, D., and Kariko, K. (2011). Nucleoside modifications in RNA limit activation of 2'-5'-oligoadenylate synthetase and increase resistance to cleavage by RNase L. Nucleic Acids Res. 39, 9329-9338. doi: 10.1093/nar/gkr586
    • (2011) Nucleic Acids Res. , vol.39 , pp. 9329-9338
    • Anderson, B.R.1    Muramatsu, H.2    Jha, B.K.3    Silverman, R.H.4    Weissman, D.5    Kariko, K.6
  • 6
    • 80053353462 scopus 로고    scopus 로고
    • Innate and adaptive immune responses to viral infection and vaccination
    • doi: 10.1016/j.coviro.2011.07.002
    • Aoshi, T., Koyama, S., Kobiyama, K., Akira, S., and Ishii, K. J. (2011). Innate and adaptive immune responses to viral infection and vaccination. Curr. Opin. Virol. 1, 226-232. doi: 10.1016/j.coviro.2011.07.002
    • (2011) Curr. Opin. Virol. , vol.1 , pp. 226-232
    • Aoshi, T.1    Koyama, S.2    Kobiyama, K.3    Akira, S.4    Ishii, K.J.5
  • 7
    • 59649092854 scopus 로고    scopus 로고
    • Messenger RNA targeting to endoplasmic reticulum stress signalling sites
    • doi: 10.1038/nature07641
    • Aragon, T., Van Anken, E., Pincus, D., Serafimova, I. M., Korennykh, A. V., Rubio, C. A., et al. (2009). Messenger RNA targeting to endoplasmic reticulum stress signalling sites. Nature 457, 736-740. doi: 10.1038/nature07641
    • (2009) Nature , vol.457 , pp. 736-740
    • Aragon, T.1    Van Anken, E.2    Pincus, D.3    Serafimova, I.M.4    Korennykh, A.V.5    Rubio, C.A.6
  • 8
    • 0028936838 scopus 로고
    • Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene
    • Beattie, E., Denzler, K. L., Tartaglia, J., Perkus, M. E., Paoletti, E., and Jacobs, B. L. (1995). Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene. J. Virol. 69, 499-505.
    • (1995) J. Virol. , vol.69 , pp. 499-505
    • Beattie, E.1    Denzler, K.L.2    Tartaglia, J.3    Perkus, M.E.4    Paoletti, E.5    Jacobs, B.L.6
  • 9
    • 84890288780 scopus 로고    scopus 로고
    • Regulated IRE1-dependent decay pathway is activated during Japanese encephalitis virus-induced unfolded protein response
    • doi: 10.1099/vir.0.057265-0
    • Bhattacharyya, S., Sen, U., and Vrati, S. (2014). Regulated IRE1-dependent decay pathway is activated during Japanese encephalitis virus-induced unfolded protein response and benefits viral replication. J. Gen. Virol. 95(Pt 1), 71-79. doi: 10.1099/vir.0.057265-0
    • (2014) benefits viral replication. J. Gen. Virol , vol.95 , Issue.1 , pp. 71-79
    • Bhattacharyya, S.1    Sen, U.2    Vrati, S.3
  • 11
    • 0033919776 scopus 로고    scopus 로고
    • The 2'-5' oligoadenylate/RNase L/RNase L inhibitor pathway regulates both MyoD mRNA stability and muscle cell differentiation
    • doi: 10.1128/MCB.20.14.4959-4969.2000
    • Bisbal, C., Silhol, M., Laubenthal, H., Kaluza, T., Carnac, G., Milligan, L., et al. (2000). The 2'-5' oligoadenylate/RNase L/RNase L inhibitor pathway regulates both MyoD mRNA stability and muscle cell differentiation. Mol. Cell. Biol. 20, 4959-4969. doi: 10.1128/MCB.20.14.4959-4969.2000
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4959-4969
    • Bisbal, C.1    Silhol, M.2    Laubenthal, H.3    Kaluza, T.4    Carnac, G.5    Milligan, L.6
  • 13
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • doi: 10.1038/415092a
    • Calfon, M., Zeng, H., Urano, F., Till, J. H., Hubbard, S. R., Harding, H. P., et al. (2002). IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415, 92-96. doi: 10.1038/415092a
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5    Harding, H.P.6
  • 14
    • 0031870271 scopus 로고    scopus 로고
    • The role of 2'-5' oligoadenylate-activated ribonuclease L in apoptosis
    • doi: 10.1038/sj.cdd.4400352
    • Castelli, J. C., Hassel, B. A., Maran, A., Paranjape, J., Hewitt, J. A., Li, X. L., et al. (1998). The role of 2'-5' oligoadenylate-activated ribonuclease L in apoptosis. Cell Death Differ. 5, 313-320. doi: 10.1038/sj.cdd.4400352
    • (1998) Cell Death Differ. , vol.5 , pp. 313-320
    • Castelli, J.C.1    Hassel, B.A.2    Maran, A.3    Paranjape, J.4    Hewitt, J.A.5    Li, X.L.6
  • 15
    • 0030924144 scopus 로고    scopus 로고
    • A study of the interferon antiviral mechanism: apoptosis activation by the 2-5A system
    • doi: 10.1084/jem.186.6.967
    • Castelli, J. C., Hassel, B. A., Wood, K. A., Li, X. L., Amemiya, K., Dalakas, M. C., et al. (1997). A study of the interferon antiviral mechanism: apoptosis activation by the 2-5A system. J. Exp. Med. 186, 967-972. doi: 10.1084/jem.186.6.967
    • (1997) J. Exp. Med. , vol.186 , pp. 967-972
    • Castelli, J.C.1    Hassel, B.A.2    Wood, K.A.3    Li, X.L.4    Amemiya, K.5    Dalakas, M.C.6
  • 16
    • 0021164485 scopus 로고
    • Activation of the ppp(A2'p)nA system in interferon-treated, herpes simplex virus-infected cells and evidence for novel inhibitors of the ppp(A2'p)nA-dependent RNase
    • doi: 10.1111/j.1432-1033.1984.tb08355.x
    • Cayley, P. J., Davies, J. A., Mccullagh, K. G., and Kerr, I. M. (1984). Activation of the ppp(A2'p)nA system in interferon-treated, herpes simplex virus-infected cells and evidence for novel inhibitors of the ppp(A2'p)nA-dependent RNase. Eur. J. Biochem. 143, 165-174. doi: 10.1111/j.1432-1033.1984.tb08355.x
    • (1984) Eur. J. Biochem. , vol.143 , pp. 165-174
    • Cayley, P.J.1    Davies, J.A.2    Mccullagh, K.G.3    Kerr, I.M.4
  • 17
    • 84869057548 scopus 로고    scopus 로고
    • RNase L triggers autophagy in response to viral infections
    • doi: 10.1128/JVI.00270-12
    • Chakrabarti, A., Ghosh, P. K., Banerjee, S., Gaughan, C., and Silverman, R. H. (2012). RNase L triggers autophagy in response to viral infections. J. Virol. 86, 11311-11321. doi: 10.1128/JVI.00270-12
    • (2012) J. Virol. , vol.86 , pp. 11311-11321
    • Chakrabarti, A.1    Ghosh, P.K.2    Banerjee, S.3    Gaughan, C.4    Silverman, R.H.5
  • 18
    • 84886749523 scopus 로고    scopus 로고
    • IRE1: ER stress sensor and cell fate executor
    • doi: 10.1016/j.tcb.2013.06.005
    • Chen, Y., and Brandizzi, F. (2013). IRE1: ER stress sensor and cell fate executor. Trends Cell Biol. 23, 547-555. doi: 10.1016/j.tcb.2013.06.005
    • (2013) Trends Cell Biol. , vol.23 , pp. 547-555
    • Chen, Y.1    Brandizzi, F.2
  • 19
    • 0346995213 scopus 로고    scopus 로고
    • Evasion of cellular antiviral responses by human cytomegalovirus TRS1 and IRS1
    • doi: 10.1128/JVI.78.1.197-205.2004
    • Child, S. J., Hakki, M., De Niro, K. L., and Geballe, A. P. (2004). Evasion of cellular antiviral responses by human cytomegalovirus TRS1 and IRS1. J. Virol. 78, 197-205. doi: 10.1128/JVI.78.1.197-205.2004
    • (2004) J. Virol. , vol.78 , pp. 197-205
    • Child, S.J.1    Hakki, M.2    De Niro, K.L.3    Geballe, A.P.4
  • 20
    • 84880609359 scopus 로고    scopus 로고
    • A role for Ifit2 in restricting West Nile virus infection in the brain
    • doi: 10.1128/JVI.01097-13
    • Cho, H., Shrestha, B., Sen, G. C., and Diamond, M. S. (2013a). A role for Ifit2 in restricting West Nile virus infection in the brain. J. Virol. 87, 8363-8371. doi: 10.1128/JVI.01097-13
    • (2013) J. Virol. , vol.87 , pp. 8363-8371
    • Cho, H.1    Shrestha, B.2    Sen, G.C.3    Diamond, M.S.4
  • 21
    • 84877870687 scopus 로고    scopus 로고
    • The unfolded protein response element IRE1alpha senses bacterial proteins invading the ER to activate RIG-I and innate immune signaling
    • doi: 10.1016/j.chom.2013.03.011
    • Cho, J. A., Lee, A. H., Platzer, B., Cross, B. C., Gardner, B. M., De Luca, H., et al. (2013b). The unfolded protein response element IRE1alpha senses bacterial proteins invading the ER to activate RIG-I and innate immune signaling. Cell Host Microbe 13, 558-569. doi: 10.1016/j.chom.2013.03.011
    • (2013) Cell Host Microbe , vol.13 , pp. 558-569
    • Cho, J.A.1    Lee, A.H.2    Platzer, B.3    Cross, B.C.4    Gardner, B.M.5    De Luca, H.6
  • 22
    • 33751254102 scopus 로고    scopus 로고
    • Recent advances in deciphering viral and host determinants of dengue virus replication and pathogenesis
    • doi: 10.1128/JVI.01257-06
    • Clyde, K., Kyle, J. L., and Harris, E. (2006). Recent advances in deciphering viral and host determinants of dengue virus replication and pathogenesis. J. Virol. 80, 11418-11431. doi: 10.1128/JVI.01257-06
    • (2006) J. Virol. , vol.80 , pp. 11418-11431
    • Clyde, K.1    Kyle, J.L.2    Harris, E.3
  • 23
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • doi: 10.1016/S0092-8674(00)81360-4
    • Cox, J. S., and Walter, P. (1996). A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 87, 391-404. doi: 10.1016/S0092-8674(00)81360-4
    • (1996) Cell , vol.87 , pp. 391-404
    • Cox, J.S.1    Walter, P.2
  • 24
    • 30044432596 scopus 로고    scopus 로고
    • On the mechanism of sensing unfolded protein in the endoplasmic reticulum
    • doi: 10.1073/pnas.0509487102
    • Credle, J. J., Finer-Moore, J. S., Papa, F. R., Stroud, R. M., and Walter, P. (2005). On the mechanism of sensing unfolded protein in the endoplasmic reticulum. Proc. Natl. Acad. Sci. U.S.A. 102, 18773-18784. doi: 10.1073/pnas.0509487102
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 18773-18784
    • Credle, J.J.1    Finer-Moore, J.S.2    Papa, F.R.3    Stroud, R.M.4    Walter, P.5
  • 25
    • 84861534927 scopus 로고    scopus 로고
    • p180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulum
    • doi: 10.1371/journal.pbio.1001336
    • Cui, X. A., Zhang, H., and Palazzo, A. F. (2012). p180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulum. PLoS Biol. 10:e1001336. doi: 10.1371/journal.pbio.1001336
    • (2012) PLoS Biol. , vol.10
    • Cui, X.A.1    Zhang, H.2    Palazzo, A.F.3
  • 27
    • 78549284909 scopus 로고    scopus 로고
    • 2'-O methylation of the viral mRNA cap evades host restriction by IFIT family members
    • doi: 10.1038/nature09489
    • Daffis, S., Szretter, K. J., Schriewer, J., Li, J., Youn, S., Errett, J., et al. (2010). 2'-O methylation of the viral mRNA cap evades host restriction by IFIT family members. Nature 468, 452-456. doi: 10.1038/nature09489
    • (2010) Nature , vol.468 , pp. 452-456
    • Daffis, S.1    Szretter, K.J.2    Schriewer, J.3    Li, J.4    Youn, S.5    Errett, J.6
  • 28
    • 77958176122 scopus 로고    scopus 로고
    • Cytoplasmic viral replication complexes
    • doi: 10.1016/j.chom.2010.06.010
    • den Boon, J. A., Diaz, A., and Ahlquist, P. (2010). Cytoplasmic viral replication complexes. Cell Host Microbe 8, 77-85. doi: 10.1016/j.chom.2010.06.010
    • (2010) Cell Host Microbe , vol.8 , pp. 77-85
    • Den Boon, J.A.1    Diaz, A.2    Ahlquist, P.3
  • 29
    • 54949149143 scopus 로고    scopus 로고
    • Seeking membranes: positive-strand RNA virus replication complexes
    • doi: 10.1371/journal.pbio.0060270
    • Denison, M. R. (2008). Seeking membranes: positive-strand RNA virus replication complexes. PLoS Biol. 6:e270. doi: 10.1371/journal.pbio.0060270
    • (2008) PLoS Biol , vol.6
    • Denison, M.R.1
  • 30
    • 54249119561 scopus 로고    scopus 로고
    • JNK signaling in apoptosis
    • doi: 10.1038/onc.2008.301
    • Dhanasekaran, D. N., and Reddy, E. P. (2008). JNK signaling in apoptosis. Oncogene 27, 6245-6251. doi: 10.1038/onc.2008.301
    • (2008) Oncogene , vol.27 , pp. 6245-6251
    • Dhanasekaran, D.N.1    Reddy, E.P.2
  • 31
    • 0030799121 scopus 로고    scopus 로고
    • A bipartite model of 2-5A-dependent RNase L
    • doi: 10.1074/jbc.272.35.22236
    • Dong, B., and Silverman, R. H. (1997). A bipartite model of 2-5A-dependent RNase L. J. Biol. Chem. 272, 22236-22242. doi: 10.1074/jbc.272.35.22236
    • (1997) J. Biol. Chem. , vol.272 , pp. 22236-22242
    • Dong, B.1    Silverman, R.H.2
  • 32
    • 0033555353 scopus 로고    scopus 로고
    • Alternative function of a protein kinase homology domain in 2', 5'-oligoadenylate dependent RNase L
    • doi: 10.1093/nar/27.2.439
    • Dong, B., and Silverman, R. H. (1999). Alternative function of a protein kinase homology domain in 2', 5'-oligoadenylate dependent RNase L. Nucleic Acids Res. 27, 439-445. doi: 10.1093/nar/27.2.439
    • (1999) Nucleic Acids Res. , vol.27 , pp. 439-445
    • Dong, B.1    Silverman, R.H.2
  • 33
    • 0028302105 scopus 로고
    • Intrinsic molecular activities of the interferon-induced 2-5A-dependent RNase
    • Dong, B., Xu, L., Zhou, A., Hassel, B. A., Lee, X., Torrence, P. F., et al. (1994). Intrinsic molecular activities of the interferon-induced 2-5A-dependent RNase. J. Biol. Chem. 269, 14153-14158.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14153-14158
    • Dong, B.1    Xu, L.2    Zhou, A.3    Hassel, B.A.4    Lee, X.5    Torrence, P.F.6
  • 34
    • 33644778763 scopus 로고    scopus 로고
    • Dengue virus utilizes a novel strategy for translation initiation when cap-dependent translation is inhibited
    • doi: 10.1128/JVI.80.6.2976-2986.2006
    • Edgil, D., Polacek, C., and Harris, E. (2006). Dengue virus utilizes a novel strategy for translation initiation when cap-dependent translation is inhibited. J. Virol. 80, 2976-2986. doi: 10.1128/JVI.80.6.2976-2986.2006
    • (2006) J. Virol. , vol.80 , pp. 2976-2986
    • Edgil, D.1    Polacek, C.2    Harris, E.3
  • 35
    • 0033919961 scopus 로고    scopus 로고
    • Formation of the poliovirus replication complex requires coupled viral translation, vesicle production, and viral RNA synthesis
    • doi: 10.1128/JVI.74.14.6570-6580.2000
    • Egger, D., Teterina, N., Ehrenfeld, E., and Bienz, K. (2000). Formation of the poliovirus replication complex requires coupled viral translation, vesicle production, and viral RNA synthesis. J. Virol. 74, 6570-6580. doi: 10.1128/JVI.74.14.6570-6580.2000
    • (2000) J. Virol. , vol.74 , pp. 6570-6580
    • Egger, D.1    Teterina, N.2    Ehrenfeld, E.3    Bienz, K.4
  • 36
    • 0019794540 scopus 로고
    • Interferon action: RNA cleavage pattern of a (2'-5')oligoadenylate-dependent endonuclease
    • doi: 10.1126/science.6165080
    • Floyd-Smith, G., Slattery, E., and Lengyel, P. (1981). Interferon action: RNA cleavage pattern of a (2'-5')oligoadenylate-dependent endonuclease. Science 212, 1030-1032. doi: 10.1126/science.6165080
    • (1981) Science , vol.212 , pp. 1030-1032
    • Floyd-Smith, G.1    Slattery, E.2    Lengyel, P.3
  • 37
    • 84871911924 scopus 로고    scopus 로고
    • Comparison of mRNA localization and regulation during endoplasmic reticulum stress in Drosophila cells
    • doi: 10.1091/mbc.E12-06-0491
    • Gaddam, D., Stevens, N., and Hollien, J. (2013). Comparison of mRNA localization and regulation during endoplasmic reticulum stress in Drosophila cells. Mol. Biol. Cell 24, 14-20. doi: 10.1091/mbc.E12-06-0491
    • (2013) Mol. Biol. Cell , vol.24 , pp. 14-20
    • Gaddam, D.1    Stevens, N.2    Hollien, J.3
  • 38
    • 0037031709 scopus 로고    scopus 로고
    • Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein
    • doi: 10.1126/science.1074276
    • Gao, G., Guo, X., and Goff, S. P. (2002). Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein. Science 297, 1703-1706. doi: 10.1126/science.1074276
    • (2002) Science , vol.297 , pp. 1703-1706
    • Gao, G.1    Guo, X.2    Goff, S.P.3
  • 39
    • 33846083772 scopus 로고    scopus 로고
    • The zinc-finger antiviral protein recruits the RNA processing exosome to degrade the target mRNA
    • doi: 10.1073/pnas.0607063104
    • Guo, X., Ma, J., Sun, J., and Gao, G. (2007). The zinc-finger antiviral protein recruits the RNA processing exosome to degrade the target mRNA. Proc. Natl. Acad. Sci. U.S.A. 104, 151-156. doi: 10.1073/pnas.0607063104
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 151-156
    • Guo, X.1    Ma, J.2    Sun, J.3    Gao, G.4
  • 40
    • 68049110633 scopus 로고    scopus 로고
    • IRE1alpha kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates
    • doi: 10.1016/j.cell.2009.07.017
    • Han, D., Lerner, A. G., Vande Walle, L., Upton, J. P., Xu, W., Hagen, A., et al. (2009). IRE1alpha kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates. Cell 138, 562-575. doi: 10.1016/j.cell.2009.07.017
    • (2009) Cell , vol.138 , pp. 562-575
    • Han, D.1    Lerner, A.G.2    Vande Walle, L.3    Upton, J.P.4    Xu, W.5    Hagen, A.6
  • 41
    • 0036233219 scopus 로고    scopus 로고
    • Activation and evasion of the antiviral 2'-5' oligoadenylate synthetase/ribonuclease L pathway by hepatitis C virus mRNA
    • doi: 10.1017/S1355838202020617
    • Han, J. Q., and Barton, D. J. (2002). Activation and evasion of the antiviral 2'-5' oligoadenylate synthetase/ribonuclease L pathway by hepatitis C virus mRNA. RNA 8, 512-525. doi: 10.1017/S1355838202020617
    • (2002) RNA , vol.8 , pp. 512-525
    • Han, J.Q.1    Barton, D.J.2
  • 42
    • 84896045262 scopus 로고    scopus 로고
    • Structure of human RNase L reveals the basis for regulated RNA decay in the IFN response
    • doi: 10.1126/science.1249845
    • Han, Y., Donovan, J., Rath, S., Whitney, G., Chitrakar, A., and Korennykh, A. (2014). Structure of human RNase L reveals the basis for regulated RNA decay in the IFN response. Science 343, 1244-1248. doi: 10.1126/science.1249845
    • (2014) Science , vol.343 , pp. 1244-1248
    • Han, Y.1    Donovan, J.2    Rath, S.3    Whitney, G.4    Chitrakar, A.5    Korennykh, A.6
  • 43
    • 84868152934 scopus 로고    scopus 로고
    • Innate immune messenger 2-5A tethers human RNase L into active high-order complexes
    • doi: 10.1016/j.celrep.2012.09.004
    • Han, Y., Whitney, G., Donovan, J., and Korennykh, A. (2012). Innate immune messenger 2-5A tethers human RNase L into active high-order complexes. Cell Rep. 2, 902-913. doi: 10.1016/j.celrep.2012.09.004
    • (2012) Cell Rep. , vol.2 , pp. 902-913
    • Han, Y.1    Whitney, G.2    Donovan, J.3    Korennykh, A.4
  • 44
    • 0344413485 scopus 로고    scopus 로고
    • Crystal structure of the 2'-specific and double-stranded RNA-activated interferon-induced antiviral protein 2'-5'-oligoadenylate synthetase
    • doi: 10.1016/S1097-2765(03)00433-7
    • Hartmann, R., Justesen, J., Sarkar, S. N., Sen, G. C., and Yee, V. C. (2003). Crystal structure of the 2'-specific and double-stranded RNA-activated interferon-induced antiviral protein 2'-5'-oligoadenylate synthetase. Mol. Cell 12, 1173-1185. doi: 10.1016/S1097-2765(03)00433-7
    • (2003) Mol. Cell , vol.12 , pp. 1173-1185
    • Hartmann, R.1    Justesen, J.2    Sarkar, S.N.3    Sen, G.C.4    Yee, V.C.5
  • 45
    • 84863149924 scopus 로고    scopus 로고
    • Influenza A viral replication is blocked by inhibition of the inositol-requiring enzyme 1 (IRE1) stress pathway
    • doi: 10.1074/jbc.M111.284695
    • Hassan, I. H., Zhang, M. S., Powers, L. S., Shao, J. Q., Baltrusaitis, J., Rutkowski, D. T., et al. (2012). Influenza A viral replication is blocked by inhibition of the inositol-requiring enzyme 1 (IRE1) stress pathway. J. Biol. Chem. 287, 4679-4689. doi: 10.1074/jbc.M111.284695
    • (2012) J. Biol. Chem. , vol.287 , pp. 4679-4689
    • Hassan, I.H.1    Zhang, M.S.2    Powers, L.S.3    Shao, J.Q.4    Baltrusaitis, J.5    Rutkowski, D.T.6
  • 46
    • 0027270867 scopus 로고
    • A dominant negative mutant of 2-5A-dependent RNase suppresses antiproliferative and antiviral effects of interferon
    • Hassel, B. A., Zhou, A., Sotomayor, C., Maran, A., and Silverman, R. H. (1993). A dominant negative mutant of 2-5A-dependent RNase suppresses antiproliferative and antiviral effects of interferon. EMBO J. 12, 3297-3304.
    • (1993) EMBO J. , vol.12 , pp. 3297-3304
    • Hassel, B.A.1    Zhou, A.2    Sotomayor, C.3    Maran, A.4    Silverman, R.H.5
  • 47
    • 33645142635 scopus 로고    scopus 로고
    • Viruses, endoplasmic reticulum stress, and interferon responses
    • doi: 10.1038/sj.cdd.4401833
    • He, B. (2006). Viruses, endoplasmic reticulum stress, and interferon responses. Cell Death Differ. 13, 393-403. doi: 10.1038/sj.cdd.4401833
    • (2006) Cell Death Differ. , vol.13 , pp. 393-403
    • He, B.1
  • 48
    • 0021349750 scopus 로고
    • Simian virus 40-infected, interferon-treated cells contain 2',5'-oligoadenylates which do not activate cleavage of RNA
    • Hersh, C. L., Brown, R. E., Roberts, W. K., Swyryd, E. A., Kerr, I. M., and Stark, G. R. (1984). Simian virus 40-infected, interferon-treated cells contain 2',5'-oligoadenylates which do not activate cleavage of RNA. J. Biol. Chem. 259, 1731-1737.
    • (1984) J. Biol. Chem. , vol.259 , pp. 1731-1737
    • Hersh, C.L.1    Brown, R.E.2    Roberts, W.K.3    Swyryd, E.A.4    Kerr, I.M.5    Stark, G.R.6
  • 49
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: controlling cell fate decisions under ER stress and beyond
    • Hetz, C. (2012). The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat. Rev. Mol. Cell Biol. 13, 89-102.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 89-102
    • Hetz, C.1
  • 50
    • 33745893809 scopus 로고    scopus 로고
    • Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response
    • doi: 10.1126/science.1129631
    • Hollien, J., and Weissman, J. S. (2006). Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Science 313, 104-107. doi: 10.1126/science.1129631
    • (2006) Science , vol.313 , pp. 104-107
    • Hollien, J.1    Weissman, J.S.2
  • 51
    • 42649125586 scopus 로고    scopus 로고
    • IRE1beta inhibits chylomicron production by selectively degrading MTP mRNA
    • doi: 10.1016/j.cmet.2008.03.005
    • Iqbal, J., Dai, K., Seimon, T., Jungreis, R., Oyadomari, M., Kuriakose, G., et al. (2008). IRE1beta inhibits chylomicron production by selectively degrading MTP mRNA. Cell Metab. 7, 445-455. doi: 10.1016/j.cmet.2008.03.005
    • (2008) Cell Metab. , vol.7 , pp. 445-455
    • Iqbal, J.1    Dai, K.2    Seimon, T.3    Jungreis, R.4    Oyadomari, M.5    Kuriakose, G.6
  • 52
    • 18844419215 scopus 로고    scopus 로고
    • Human cytomegalovirus infection activates and regulates the unfolded protein response
    • doi: 10.1128/JVI.79.11.6890-6899.2005
    • Isler, J. A., Skalet, A. H., and Alwine, J. C. (2005). Human cytomegalovirus infection activates and regulates the unfolded protein response. J. Virol. 79, 6890-6899. doi: 10.1128/JVI.79.11.6890-6899.2005
    • (2005) J. Virol. , vol.79 , pp. 6890-6899
    • Isler, J.A.1    Skalet, A.H.2    Alwine, J.C.3
  • 53
    • 0035147411 scopus 로고    scopus 로고
    • Translational control by the ER transmembrane kinase/ribonuclease IRE1 under ER stress
    • doi: 10.1038/35055065
    • Iwawaki, T., Hosoda, A., Okuda, T., Kamigori, Y., Nomura-Furuwatari, C., Kimata, Y., et al. (2001). Translational control by the ER transmembrane kinase/ribonuclease IRE1 under ER stress. Nat. Cell Biol. 3, 158-164. doi: 10.1038/35055065
    • (2001) Nat. Cell Biol. , vol.3 , pp. 158-164
    • Iwawaki, T.1    Hosoda, A.2    Okuda, T.3    Kamigori, Y.4    Nomura-Furuwatari, C.5    Kimata, Y.6
  • 54
    • 0030585155 scopus 로고    scopus 로고
    • When two strands are better than one: the mediators and modulators of the cellular responses to double-stranded RNA
    • doi: 10.1006/viro.1996.0259
    • Jacobs, B. L., and Langland, J. O. (1996). When two strands are better than one: the mediators and modulators of the cellular responses to double-stranded RNA. Virology 219, 339-349. doi: 10.1006/viro.1996.0259
    • (1996) Virology , vol.219 , pp. 339-349
    • Jacobs, B.L.1    Langland, J.O.2
  • 55
    • 84857969026 scopus 로고    scopus 로고
    • Sensing of RNA viruses: a review of innate immune receptors involved in recognizing RNA virus invasion
    • doi: 10.1128/JVI.05738-11
    • Jensen, S., and Thomsen, A. R. (2012). Sensing of RNA viruses: a review of innate immune receptors involved in recognizing RNA virus invasion. J. Virol. 86, 2900-2910. doi: 10.1128/JVI.05738-11
    • (2012) J. Virol. , vol.86 , pp. 2900-2910
    • Jensen, S.1    Thomsen, A.R.2
  • 56
    • 0023655215 scopus 로고
    • Purification and characterization of a 2'-phosphodiesterase from bovine spleen
    • Johnston, M. I., and Hearl, W. G. (1987). Purification and characterization of a 2'-phosphodiesterase from bovine spleen. J. Biol. Chem. 262, 8377-8382.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8377-8382
    • Johnston, M.I.1    Hearl, W.G.2
  • 57
    • 84879711466 scopus 로고    scopus 로고
    • Gap junctional communication promotes apoptosis in a connexin-type-dependent manner
    • doi: 10.1038/cddis.2013.105
    • Kameritsch, P., Khandoga, N., Pohl, U., and Pogoda, K. (2013). Gap junctional communication promotes apoptosis in a connexin-type-dependent manner. Cell Death Dis. 4:e584. doi: 10.1038/cddis.2013.105
    • (2013) Cell Death Dis. , vol.4
    • Kameritsch, P.1    Khandoga, N.2    Pohl, U.3    Pogoda, K.4
  • 58
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls
    • doi: 10.1101/gad.13.10.1211
    • Kaufman, R. J. (1999). Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13, 1211-1233. doi: 10.1101/gad.13.10.1211
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 59
    • 0038504114 scopus 로고    scopus 로고
    • RNase L mediates transient control of the interferon response through modulation of the double-stranded RNA-dependent protein kinase PKR
    • doi: 10.1074/jbc.M208766200
    • Khabar, K. S., Siddiqui, Y. M., Al-Zoghaibi, F., Al-Haj, L., Dhalla, M., Zhou, A., et al. (2003). RNase L mediates transient control of the interferon response through modulation of the double-stranded RNA-dependent protein kinase PKR. J. Biol. Chem. 278, 20124-20132. doi: 10.1074/jbc.M208766200
    • (2003) J. Biol. Chem. , vol.278 , pp. 20124-20132
    • Khabar, K.S.1    Siddiqui, Y.M.2    Al-Zoghaibi, F.3    Al-Haj, L.4    Dhalla, M.5    Zhou, A.6
  • 60
    • 35348967427 scopus 로고    scopus 로고
    • Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins
    • doi: 10.1083/jcb.200704166
    • Kimata, Y., Ishiwata-Kimata, Y., Ito, T., Hirata, A., Suzuki, T., Oikawa, D., et al. (2007). Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins. J. Cell Biol. 179, 75-86. doi: 10.1083/jcb.200704166
    • (2007) J. Cell Biol. , vol.179 , pp. 75-86
    • Kimata, Y.1    Ishiwata-Kimata, Y.2    Ito, T.3    Hirata, A.4    Suzuki, T.5    Oikawa, D.6
  • 61
    • 0019200844 scopus 로고
    • Radioimmune, radiobinding and HPLC analysis of 2-5A and related oligonucleotides from intact cells
    • doi: 10.1038/288189a0
    • Knight, M., Cayley, P. J., Silverman, R. H., Wreschner, D. H., Gilbert, C. S., Brown, R. E., et al. (1980). Radioimmune, radiobinding and HPLC analysis of 2-5A and related oligonucleotides from intact cells. Nature 288, 189-192. doi: 10.1038/288189a0
    • (1980) Nature , vol.288 , pp. 189-192
    • Knight, M.1    Cayley, P.J.2    Silverman, R.H.3    Wreschner, D.H.4    Gilbert, C.S.5    Brown, R.E.6
  • 62
    • 59649111087 scopus 로고    scopus 로고
    • The unfolded protein response signals through high-order assembly of Ire1
    • doi: 10.1038/nature07661
    • Korennykh, A. V., Egea, P. F., Korostelev, A. A., Finer-Moore, J., Zhang, C., Shokat, K. M., et al. (2009). The unfolded protein response signals through high-order assembly of Ire1. Nature 457, 687-693. doi: 10.1038/nature07661
    • (2009) Nature , vol.457 , pp. 687-693
    • Korennykh, A.V.1    Egea, P.F.2    Korostelev, A.A.3    Finer-Moore, J.4    Zhang, C.5    Shokat, K.M.6
  • 64
    • 4444248697 scopus 로고    scopus 로고
    • Identification of 2'-phosphodiesterase, which plays a role in the 2-5A system regulated by interferon
    • doi: 10.1074/jbc.M400089200
    • Kubota, K., Nakahara, K., Ohtsuka, T., Yoshida, S., Kawaguchi, J., Fujita, Y., et al. (2004). Identification of 2'-phosphodiesterase, which plays a role in the 2-5A system regulated by interferon. J. Biol. Chem. 279, 37832-37841. doi: 10.1074/jbc.M400089200
    • (2004) J. Biol. Chem. , vol.279 , pp. 37832-37841
    • Kubota, K.1    Nakahara, K.2    Ohtsuka, T.3    Yoshida, S.4    Kawaguchi, J.5    Fujita, Y.6
  • 65
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • doi: 10.1128/MCB.23.21.7448-7459.2003
    • Lee, A. H., Iwakoshi, N. N., and Glimcher, L. H. (2003). XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell. Biol. 23, 7448-7459. doi: 10.1128/MCB.23.21.7448-7459.2003
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 66
    • 37649004940 scopus 로고    scopus 로고
    • Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing
    • doi: 10.1016/j.cell.2007.10.057
    • Lee, K. P., Dey, M., Neculai, D., Cao, C., Dever, T. E., and Sicheri, F. (2008). Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing. Cell 132, 89-100. doi: 10.1016/j.cell.2007.10.057
    • (2008) Cell , vol.132 , pp. 89-100
    • Lee, K.P.1    Dey, M.2    Neculai, D.3    Cao, C.4    Dever, T.E.5    Sicheri, F.6
  • 67
    • 84873619956 scopus 로고    scopus 로고
    • Regulation of human RNase-L by the miR-29 family reveals a novel oncogenic role in chronic myelogenous leukemia
    • doi: 10.1089/jir.2012.0062
    • Lee, T. Y., Ezelle, H. J., Venkataraman, T., Lapidus, R. G., Scheibner, K. A., and Hassel, B. A. (2013). Regulation of human RNase-L by the miR-29 family reveals a novel oncogenic role in chronic myelogenous leukemia. J. Interferon Cytokine Res. 33, 34-42. doi: 10.1089/jir.2012.0062
    • (2013) J. Interferon Cytokine Res. , vol.33 , pp. 34-42
    • Lee, T.Y.1    Ezelle, H.J.2    Venkataraman, T.3    Lapidus, R.G.4    Scheibner, K.A.5    Hassel, B.A.6
  • 68
    • 0041832111 scopus 로고    scopus 로고
    • Partitioning and translation of mRNAs encoding soluble proteins on membrane-bound ribosomes
    • doi: 10.1261/rna.5610403
    • Lerner, R. S., Seiser, R. M., Zheng, T., Lager, P. J., Reedy, M. C., Keene, J. D., et al. (2003). Partitioning and translation of mRNAs encoding soluble proteins on membrane-bound ribosomes. RNA 9, 1123-1137. doi: 10.1261/rna.5610403
    • (2003) RNA , vol.9 , pp. 1123-1137
    • Lerner, R.S.1    Seiser, R.M.2    Zheng, T.3    Lager, P.J.4    Reedy, M.C.5    Keene, J.D.6
  • 69
    • 0347093362 scopus 로고    scopus 로고
    • An apoptotic signaling pathway in the interferon antiviral response mediated by RNase L and c-Jun NH2-terminal kinase
    • doi: 10.1074/jbc.M305893200
    • Li, G., Xiang, Y., Sabapathy, K., and Silverman, R. H. (2004). An apoptotic signaling pathway in the interferon antiviral response mediated by RNase L and c-Jun NH2-terminal kinase. J. Biol. Chem. 279, 1123-1131. doi: 10.1074/jbc.M305893200
    • (2004) J. Biol. Chem. , vol.279 , pp. 1123-1131
    • Li, G.1    Xiang, Y.2    Sabapathy, K.3    Silverman, R.H.4
  • 70
    • 77958016968 scopus 로고    scopus 로고
    • Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering
    • doi: 10.1073/pnas.1010580107
    • Li, H., Korennykh, A. V., Behrman, S. L., and Walter, P. (2010). Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering. Proc. Natl. Acad. Sci. U.S.A. 107, 16113-16118. doi: 10.1073/pnas.1010580107
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 16113-16118
    • Li, H.1    Korennykh, A.V.2    Behrman, S.L.3    Walter, P.4
  • 71
    • 0031901636 scopus 로고    scopus 로고
    • RNase L mediates the antiviral effect of interferon through a selective reduction in viral RNA during encephalomyocarditis virus infection
    • Li, X. L., Blackford, J. A., and Hassel, B. A. (1998). RNase L mediates the antiviral effect of interferon through a selective reduction in viral RNA during encephalomyocarditis virus infection. J. Virol. 72, 2752-2759.
    • (1998) J. Virol. , vol.72 , pp. 2752-2759
    • Li, X.L.1    Blackford, J.A.2    Hassel, B.A.3
  • 73
    • 36049049392 scopus 로고    scopus 로고
    • IRE1 signaling affects cell fate during the unfolded protein response
    • doi: 10.1126/science.1146361
    • Lin, J. H., Li, H., Yasumura, D., Cohen, H. R., Zhang, C., Panning, B., et al. (2007). IRE1 signaling affects cell fate during the unfolded protein response. Science 318, 944-949. doi: 10.1126/science.1146361
    • (2007) Science , vol.318 , pp. 944-949
    • Lin, J.H.1    Li, H.2    Yasumura, D.3    Cohen, H.R.4    Zhang, C.5    Panning, B.6
  • 74
    • 84876383987 scopus 로고    scopus 로고
    • MCPIP1 ribonuclease exhibits broad-spectrum antiviral effects through viral RNA binding and degradation
    • doi: 10.1093/nar/gkt019
    • Lin, R. J., Chien, H. L., Lin, S. Y., Chang, B. L., Yu, H. P., Tang, W. C., et al. (2013). MCPIP1 ribonuclease exhibits broad-spectrum antiviral effects through viral RNA binding and degradation. Nucleic Acids Res. 41, 3314-3326. doi: 10.1093/nar/gkt019
    • (2013) Nucleic Acids Res. , vol.41 , pp. 3314-3326
    • Lin, R.J.1    Chien, H.L.2    Lin, S.Y.3    Chang, B.L.4    Yu, H.P.5    Tang, W.C.6
  • 75
    • 76249133498 scopus 로고    scopus 로고
    • Distinct antiviral roles for human 2',5'-oligoadenylate synthetase family members against dengue virus infection
    • doi: 10.4049/jimmunol.0902728
    • Lin, R. J., Yu, H. P., Chang, B. L., Tang, W. C., Liao, C. L., and Lin, Y. L. (2009). Distinct antiviral roles for human 2',5'-oligoadenylate synthetase family members against dengue virus infection. J. Immunol. 183, 8035-8043. doi: 10.4049/jimmunol.0902728
    • (2009) J. Immunol. , vol.183 , pp. 8035-8043
    • Lin, R.J.1    Yu, H.P.2    Chang, B.L.3    Tang, W.C.4    Liao, C.L.5    Lin, Y.L.6
  • 76
    • 45749114525 scopus 로고    scopus 로고
    • The role of IRE1alpha in the degradation of insulin mRNA in pancreatic beta-cells
    • doi: 10.1371/journal.pone.0001648
    • Lipson, K. L., Ghosh, R., and Urano, F. (2008). The role of IRE1alpha in the degradation of insulin mRNA in pancreatic beta-cells. PLoS ONE 3:e1648. doi: 10.1371/journal.pone.0001648
    • (2008) PLoS ONE , vol.3
    • Lipson, K.L.1    Ghosh, R.2    Urano, F.3
  • 77
    • 16844387124 scopus 로고    scopus 로고
    • Role of JNK activation in apoptosis: a double-edged sword
    • doi: 10.1038/sj.cr.7290262
    • Liu, J., and Lin, A. (2005). Role of JNK activation in apoptosis: a double-edged sword. Cell Res. 15, 36-42. doi: 10.1038/sj.cr.7290262
    • (2005) Cell Res. , vol.15 , pp. 36-42
    • Liu, J.1    Lin, A.2
  • 78
    • 0028042337 scopus 로고
    • HIV-1 TAR RNA has an intrinsic ability to activate interferon-inducible enzymes
    • doi: 10.1006/viro.1994.1601
    • Maitra, R. K., Mcmillan, N. A., Desai, S., Mcswiggen, J., Hovanessian, A. G., Sen, G., et al. (1994). HIV-1 TAR RNA has an intrinsic ability to activate interferon-inducible enzymes. Virology 204, 823-827. doi: 10.1006/viro.1994.1601
    • (1994) Virology , vol.204 , pp. 823-827
    • Maitra, R.K.1    Mcmillan, N.A.2    Desai, S.3    Mcswiggen, J.4    Hovanessian, A.G.5    Sen, G.6
  • 79
    • 34547960175 scopus 로고    scopus 로고
    • Small self-RNA generated by RNase L amplifies antiviral innate immunity
    • doi: 10.1038/nature06042
    • Malathi, K., Dong, B., Gale, M. Jr., and Silverman, R. H. (2007). Small self-RNA generated by RNase L amplifies antiviral innate immunity. Nature 448, 816-819. doi: 10.1038/nature06042
    • (2007) Nature , vol.448 , pp. 816-819
    • Malathi, K.1    Dong, B.2    Gale Jr., M.3    Silverman, R.H.4
  • 80
    • 26844496280 scopus 로고    scopus 로고
    • A transcriptional signaling pathway in the IFN system mediated by 2'-5'-oligoadenylate activation of RNase L
    • doi: 10.1073/pnas.0507551102
    • Malathi, K., Paranjape, J. M., Bulanova, E., Shim, M., Guenther-Johnson, J. M., Faber, P. W., et al. (2005). A transcriptional signaling pathway in the IFN system mediated by 2'-5'-oligoadenylate activation of RNase L. Proc. Natl. Acad. Sci. U.S.A. 102, 14533-14538. doi: 10.1073/pnas.0507551102
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 14533-14538
    • Malathi, K.1    Paranjape, J.M.2    Bulanova, E.3    Shim, M.4    Guenther-Johnson, J.M.5    Faber, P.W.6
  • 81
    • 78149324490 scopus 로고    scopus 로고
    • RNase L releases a small RNA from HCV RNA that refolds into a potent PAMP
    • doi: 10.1261/rna.2244210
    • Malathi, K., Saito, T., Crochet, N., Barton, D. J., Gale, M. Jr., and Silverman, R. H. (2010). RNase L releases a small RNA from HCV RNA that refolds into a potent PAMP. RNA 16, 2108-2119. doi: 10.1261/rna.2244210
    • (2010) RNA , vol.16 , pp. 2108-2119
    • Malathi, K.1    Saito, T.2    Crochet, N.3    Barton, D.J.4    Gale Jr., M.5    Silverman, R.H.6
  • 82
    • 0025187878 scopus 로고
    • Differential expression and distinct structure of 69- and 100-kDa forms of 2-5A synthetase in human cells treated with interferon
    • Marie, I., Svab, J., Robert, N., Galabru, J., and Hovanessian, A. G. (1990). Differential expression and distinct structure of 69- and 100-kDa forms of 2-5A synthetase in human cells treated with interferon. J. Biol. Chem. 265, 18601-18607.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18601-18607
    • Marie, I.1    Svab, J.2    Robert, N.3    Galabru, J.4    Hovanessian, A.G.5
  • 83
    • 0032889556 scopus 로고    scopus 로고
    • RNase L inhibitor is induced during human immunodeficiency virus type 1 infection and down regulates the 2-5A/RNase L pathway in human T cells
    • Martinand, C., Montavon, C., Salehzada, T., Silhol, M., Lebleu, B., and Bisbal, C. (1999). RNase L inhibitor is induced during human immunodeficiency virus type 1 infection and down regulates the 2-5A/RNase L pathway in human T cells. J. Virol. 73, 290-296.
    • (1999) J. Virol. , vol.73 , pp. 290-296
    • Martinand, C.1    Montavon, C.2    Salehzada, T.3    Silhol, M.4    Lebleu, B.5    Bisbal, C.6
  • 84
    • 0032103209 scopus 로고    scopus 로고
    • RNase L inhibitor (RLI) antisense constructions block partially the down regulation of the 2-5A/RNase L pathway in encephalomyocarditis-virus-(EMCV)-infected cells
    • doi: 10.1046/j.1432-1327.1998.2540248.x
    • Martinand, C., Salehzada, T., Silhol, M., Lebleu, B., and Bisbal, C. (1998). RNase L inhibitor (RLI) antisense constructions block partially the down regulation of the 2-5A/RNase L pathway in encephalomyocarditis-virus-(EMCV)-infected cells. Eur. J. Biochem. 254, 248-255. doi: 10.1046/j.1432-1327.1998.2540248.x
    • (1998) Eur. J. Biochem. , vol.254 , pp. 248-255
    • Martinand, C.1    Salehzada, T.2    Silhol, M.3    Lebleu, B.4    Bisbal, C.5
  • 85
    • 35148894008 scopus 로고    scopus 로고
    • West Nile virus infection activates the unfolded protein response, leading to CHOP induction and apoptosis
    • doi: 10.1128/JVI.01151-07
    • Medigeshi, G. R., Lancaster, A. M., Hirsch, A. J., Briese, T., Lipkin, W. I., Defilippis, V., et al. (2007). West Nile virus infection activates the unfolded protein response, leading to CHOP induction and apoptosis. J. Virol. 81, 10849-10860. doi: 10.1128/JVI.01151-07
    • (2007) J. Virol. , vol.81 , pp. 10849-10860
    • Medigeshi, G.R.1    Lancaster, A.M.2    Hirsch, A.J.3    Briese, T.4    Lipkin, W.I.5    Defilippis, V.6
  • 87
    • 42349086670 scopus 로고    scopus 로고
    • Modification of intracellular membrane structures for virus replication
    • doi: 10.1038/nrmicro1890
    • Miller, S., and Krijnse-Locker, J. (2008). Modification of intracellular membrane structures for virus replication. Nat. Rev. Microbiol. 6, 363-374. doi: 10.1038/nrmicro1890
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 363-374
    • Miller, S.1    Krijnse-Locker, J.2
  • 88
    • 33646478272 scopus 로고    scopus 로고
    • The primary function of RNA binding by the influenza A virus NS1 protein in infected cells: Inhibiting the 2'-5' oligo (A) synthetase/RNase L pathway
    • doi: 10.1073/pnas.0602184103
    • Min, J. Y., and Krug, R. M. (2006). The primary function of RNA binding by the influenza A virus NS1 protein in infected cells: Inhibiting the 2'-5' oligo (A) synthetase/RNase L pathway. Proc. Natl. Acad. Sci. U.S.A. 103, 7100-7105. doi: 10.1073/pnas.0602184103
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 7100-7105
    • Min, J.Y.1    Krug, R.M.2
  • 89
    • 0018801485 scopus 로고
    • Structural requirements of double-stranded RNA for the activation of 2',5'-oligo(A) polymerase and protein kinase of interferon-treated HeLa cells
    • Minks, M. A., West, D. K., Benvin, S., and Baglioni, C. (1979). Structural requirements of double-stranded RNA for the activation of 2',5'-oligo(A) polymerase and protein kinase of interferon-treated HeLa cells. J. Biol. Chem. 254, 10180-10183.
    • (1979) J. Biol. Chem. , vol.254 , pp. 10180-10183
    • Minks, M.A.1    West, D.K.2    Benvin, S.3    Baglioni, C.4
  • 90
    • 84878209731 scopus 로고    scopus 로고
    • Three-dimensional architecture of tick-borne encephalitis virus replication sites and trafficking of the replicated RNA
    • doi: 10.1128/JVI.03456-12
    • Miorin, L., Romero-Brey, I., Maiuri, P., Hoppe, S., Krijnse-Locker, J., Bartenschlager, R., et al. (2013). Three-dimensional architecture of tick-borne encephalitis virus replication sites and trafficking of the replicated RNA. J. Virol. 87, 6469-6481. doi: 10.1128/JVI.03456-12
    • (2013) J. Virol. , vol.87 , pp. 6469-6481
    • Miorin, L.1    Romero-Brey, I.2    Maiuri, P.3    Hoppe, S.4    Krijnse-Locker, J.5    Bartenschlager, R.6
  • 91
    • 19544367765 scopus 로고    scopus 로고
    • 2-5A induces a conformational change in the ankyrin-repeat domain of RNase L
    • doi: 10.1002/prot.20474
    • Nakanishi, M., Goto, Y., and Kitade, Y. (2005). 2-5A induces a conformational change in the ankyrin-repeat domain of RNase L. Proteins 60, 131-138. doi: 10.1002/prot.20474
    • (2005) Proteins , vol.60 , pp. 131-138
    • Nakanishi, M.1    Goto, Y.2    Kitade, Y.3
  • 92
    • 77956016131 scopus 로고    scopus 로고
    • Identification of a consensus element recognized and cleaved by IRE1 alpha
    • doi: 10.1093/nar/gkq452
    • Oikawa, D., Tokuda, M., Hosoda, A., and Iwawaki, T. (2010). Identification of a consensus element recognized and cleaved by IRE1 alpha. Nucleic Acids Res. 38, 6265-6273. doi: 10.1093/nar/gkq452
    • (2010) Nucleic Acids Res. , vol.38 , pp. 6265-6273
    • Oikawa, D.1    Tokuda, M.2    Hosoda, A.3    Iwawaki, T.4
  • 93
    • 34250882716 scopus 로고    scopus 로고
    • Site-specific cleavage of CD59 mRNA by endoplasmic reticulum-localized ribonuclease, IRE1
    • doi: 10.1016/j.bbrc.2007.06.020
    • Oikawa, D., Tokuda, M., and Iwawaki, T. (2007). Site-specific cleavage of CD59 mRNA by endoplasmic reticulum-localized ribonuclease, IRE1. Biochem. Biophys. Res. Commun. 360, 122-127. doi: 10.1016/j.bbrc.2007.06.020
    • (2007) Biochem. Biophys. Res. Commun. , vol.360 , pp. 122-127
    • Oikawa, D.1    Tokuda, M.2    Iwawaki, T.3
  • 94
    • 0344395603 scopus 로고    scopus 로고
    • Bypassing a kinase activity with an ATP-competitive drug
    • doi: 10.1126/science.1090031
    • Papa, F. R., Zhang, C., Shokat, K., and Walter, P. (2003). Bypassing a kinase activity with an ATP-competitive drug. Science 302, 1533-1537. doi: 10.1126/science.1090031
    • (2003) Science , vol.302 , pp. 1533-1537
    • Papa, F.R.1    Zhang, C.2    Shokat, K.3    Walter, P.4
  • 95
    • 36348940608 scopus 로고    scopus 로고
    • Interferons and viruses: an interplay between induction, signalling, antiviral responses and virus countermeasures
    • doi: 10.1099/vir.0.83391-0
    • Randall, R. E., and Goodbourn, S. (2008). Interferons and viruses: an interplay between induction, signalling, antiviral responses and virus countermeasures. J. Gen. Virol. 89, 1-47. doi: 10.1099/vir.0.83391-0
    • (2008) J. Gen. Virol. , vol.89 , pp. 1-47
    • Randall, R.E.1    Goodbourn, S.2
  • 96
    • 0022396831 scopus 로고
    • Novel 2',5'-oligoadenylates synthesized in interferon-treated, vaccinia virus-infected cells
    • Rice, A. P., Kerr, S. M., Roberts, W. K., Brown, R. E., and Kerr, I. M. (1985). Novel 2',5'-oligoadenylates synthesized in interferon-treated, vaccinia virus-infected cells. J. Virol. 56, 1041-1044.
    • (1985) J. Virol. , vol.56 , pp. 1041-1044
    • Rice, A.P.1    Kerr, S.M.2    Roberts, W.K.3    Brown, R.E.4    Kerr, I.M.5
  • 97
    • 0032502728 scopus 로고    scopus 로고
    • Vaccinia virus E3L protein is an inhibitor of the interferon (i.f.n.)-induced 2-5A synthetase enzyme
    • doi: 10.1006/viro.1998.9072
    • Rivas, C., Gil, J., Melkova, Z., Esteban, M., and Diaz-Guerra, M. (1998). Vaccinia virus E3L protein is an inhibitor of the interferon (i.f.n.)-induced 2-5A synthetase enzyme. Virology 243, 406-414. doi: 10.1006/viro.1998.9072
    • (1998) Virology , vol.243 , pp. 406-414
    • Rivas, C.1    Gil, J.2    Melkova, Z.3    Esteban, M.4    Diaz-Guerra, M.5
  • 98
    • 0032746471 scopus 로고    scopus 로고
    • Viruses and apoptosis
    • doi: 10.1146/annurev.micro.53.1.577
    • Roulston, A., Marcellus, R. C., and Branton, P. E. (1999). Viruses and apoptosis. Annu. Rev. Microbiol. 53, 577-628. doi: 10.1146/annurev.micro.53.1.577
    • (1999) Annu. Rev. Microbiol. , vol.53 , pp. 577-628
    • Roulston, A.1    Marcellus, R.C.2    Branton, P.E.3
  • 99
    • 80054828840 scopus 로고    scopus 로고
    • Role of the endoplasmic reticulum-associated degradation (ERAD) pathway in degradation of hepatitis C virus envelope proteins and production of virus particles
    • doi: 10.1074/jbc.M111.259085
    • Saeed, M., Suzuki, R., Watanabe, N., Masaki, T., Tomonaga, M., Muhammad, A., et al. (2011). Role of the endoplasmic reticulum-associated degradation (ERAD) pathway in degradation of hepatitis C virus envelope proteins and production of virus particles. J. Biol. Chem. 286, 37264-37273. doi: 10.1074/jbc.M111.259085
    • (2011) J. Biol. Chem. , vol.286 , pp. 37264-37273
    • Saeed, M.1    Suzuki, R.2    Watanabe, N.3    Masaki, T.4    Tomonaga, M.5    Muhammad, A.6
  • 100
    • 0026047523 scopus 로고
    • Polyclonal antibodies against RNase L Subcellular localization of this enzyme in mouse cells
    • Salehzada, T., Silhol, M., Lebleu, B., and Bisbal, C. (1991). Polyclonal antibodies against RNase L. Subcellular localization of this enzyme in mouse cells. J. Biol. Chem. 266, 5808-5813.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5808-5813
    • Salehzada, T.1    Silhol, M.2    Lebleu, B.3    Bisbal, C.4
  • 101
    • 33947357710 scopus 로고    scopus 로고
    • Inhibition of cellular 2'-5' oligoadenylate synthetase by the herpes simplex virus type 1 Us11 protein
    • doi: 10.1128/JVI.02520-06
    • Sanchez, R., and Mohr, I. (2007). Inhibition of cellular 2'-5' oligoadenylate synthetase by the herpes simplex virus type 1 Us11 protein. J. Virol. 81, 3455-3464. doi: 10.1128/JVI.02520-06
    • (2007) J. Virol. , vol.81 , pp. 3455-3464
    • Sanchez, R.1    Mohr, I.2
  • 102
    • 0033556388 scopus 로고    scopus 로고
    • Enzymatic characteristics of recombinant medium isozyme of 2'-5' oligoadenylate synthetase
    • doi: 10.1074/jbc.274.3.1848
    • Sarkar, S. N., Bandyopadhyay, S., Ghosh, A., and Sen, G. C. (1999). Enzymatic characteristics of recombinant medium isozyme of 2'-5' oligoadenylate synthetase. J. Biol. Chem. 274, 1848-1855. doi: 10.1074/jbc.274.3.1848
    • (1999) J. Biol. Chem. , vol.274 , pp. 1848-1855
    • Sarkar, S.N.1    Bandyopadhyay, S.2    Ghosh, A.3    Sen, G.C.4
  • 103
    • 79960765634 scopus 로고    scopus 로고
    • Sensing of viral nucleic acids by RIG-I: from translocation to translation
    • doi: 10.1016/j.ejcb.2011.01.015
    • Schmidt, A., Rothenfusser, S., and Hopfner, K. P. (2012). Sensing of viral nucleic acids by RIG-I: from translocation to translation. Eur. J. Cell Biol. 91, 78-85. doi: 10.1016/j.ejcb.2011.01.015
    • (2012) Eur. J. Cell Biol. , vol.91 , pp. 78-85
    • Schmidt, A.1    Rothenfusser, S.2    Hopfner, K.P.3
  • 104
    • 82955187705 scopus 로고    scopus 로고
    • Interferon-stimulated genes and their antiviral effector functions
    • doi: 10.1016/j.coviro.2011.10.008
    • Schoggins, J. W., and Rice, C. M. (2011). Interferon-stimulated genes and their antiviral effector functions. Curr. Opin. Virol. 1, 519-525. doi: 10.1016/j.coviro.2011.10.008
    • (2011) Curr. Opin. Virol. , vol.1 , pp. 519-525
    • Schoggins, J.W.1    Rice, C.M.2
  • 105
    • 10444226462 scopus 로고    scopus 로고
    • ER stress and the unfolded protein response
    • doi: 10.1016/j.mrfmmm.2004.06.056
    • Schroder, M., and Kaufman, R. J. (2005). ER stress and the unfolded protein response. Mutat. Res. 569, 29-63. doi: 10.1016/j.mrfmmm.2004.06.056
    • (2005) Mutat. Res. , vol.569 , pp. 29-63
    • Schroder, M.1    Kaufman, R.J.2
  • 106
    • 38449085054 scopus 로고    scopus 로고
    • The interferon-stimulated genes: targets of direct signaling by interferons, double-stranded RNA, and viruses
    • doi: 10.1007/978-3-540-71329-6_12
    • Sen, G. C., and Sarkar, S. N. (2007). The interferon-stimulated genes: targets of direct signaling by interferons, double-stranded RNA, and viruses. Curr. Top. Microbiol. Immunol. 316, 233-250. doi: 10.1007/978-3-540-71329-6_12
    • (2007) Curr. Top. Microbiol. Immunol. , vol.316 , pp. 233-250
    • Sen, G.C.1    Sarkar, S.N.2
  • 107
    • 0029903049 scopus 로고    scopus 로고
    • Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
    • Shamu, C. E., and Walter, P. (1996). Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 15, 3028-3039.
    • (1996) EMBO J. , vol.15 , pp. 3028-3039
    • Shamu, C.E.1    Walter, P.2
  • 108
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • doi: 10.1038/nature00939
    • Sheehy, A. M., Gaddis, N. C., Choi, J. D., and Malim, M. H. (2002). Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418, 646-650. doi: 10.1038/nature00939
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 109
    • 77952314490 scopus 로고    scopus 로고
    • Endogenous antiviral mechanisms of RNA interference: a comparative biology perspective
    • doi: 10.1007/978-1-60761-588-0_1
    • Sidahmed, A. M., and Wilkie, B. (2010). Endogenous antiviral mechanisms of RNA interference: a comparative biology perspective. Methods Mol. Biol. 623, 3-19. doi: 10.1007/978-1-60761-588-0_1
    • (2010) Methods Mol. Biol. , vol.623 , pp. 3-19
    • Sidahmed, A.M.1    Wilkie, B.2
  • 110
    • 84871601752 scopus 로고    scopus 로고
    • RNase L induces autophagy via c-Jun N-terminal kinase and double-stranded RNA-dependent protein kinase signaling pathways
    • doi: 10.1074/jbc.M112.399964
    • Siddiqui, M. A., and Malathi, K. (2012). RNase L induces autophagy via c-Jun N-terminal kinase and double-stranded RNA-dependent protein kinase signaling pathways. J. Biol. Chem. 287, 43651-43664. doi: 10.1074/jbc.M112.399964
    • (2012) J. Biol. Chem. , vol.287 , pp. 43651-43664
    • Siddiqui, M.A.1    Malathi, K.2
  • 111
    • 0030954870 scopus 로고    scopus 로고
    • The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response
    • doi: 10.1016/S0092-8674(00)80369-4
    • Sidrauski, C., and Walter, P. (1997). The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response. Cell 90, 1031-1039. doi: 10.1016/S0092-8674(00)80369-4
    • (1997) Cell , vol.90 , pp. 1031-1039
    • Sidrauski, C.1    Walter, P.2
  • 112
    • 0037465342 scopus 로고    scopus 로고
    • Implications for RNase L in prostate cancer biology
    • doi: 10.1021/bi027147i
    • Silverman, R. H. (2003). Implications for RNase L in prostate cancer biology. Biochemistry 42, 1805-1812. doi: 10.1021/bi027147i
    • (2003) Biochemistry , vol.42 , pp. 1805-1812
    • Silverman, R.H.1
  • 113
    • 36348987303 scopus 로고    scopus 로고
    • Viral encounters with 2',5'-oligoadenylate synthetase and RNase L during the interferon antiviral response
    • doi: 10.1128/JVI.01471-07
    • Silverman, R. H. (2007). Viral encounters with 2',5'-oligoadenylate synthetase and RNase L during the interferon antiviral response. J. Virol. 81, 12720-12729. doi: 10.1128/JVI.01471-07
    • (2007) J. Virol. , vol.81 , pp. 12720-12729
    • Silverman, R.H.1
  • 114
    • 0020535757 scopus 로고
    • rRNA cleavage as an index of ppp(A2'p)nA activity in interferon-treated encephalomyocarditis virus-infected cells
    • Silverman, R. H., Skehel, J. J., James, T. C., Wreschner, D. H., and Kerr, I. M. (1983). rRNA cleavage as an index of ppp(A2'p)nA activity in interferon-treated encephalomyocarditis virus-infected cells. J. Virol. 46, 1051-1055.
    • (1983) J. Virol. , vol.46 , pp. 1051-1055
    • Silverman, R.H.1    Skehel, J.J.2    James, T.C.3    Wreschner, D.H.4    Kerr, I.M.5
  • 115
    • 0019882453 scopus 로고
    • Synthesis, characterization and properties of ppp(A2'p)nApCp and related high-specific-activity 32P-labelled derivatives of ppp(A2'p)nA
    • doi: 10.1111/j.1432-1033.1981.tb06200.x
    • Silverman, R. H., Wreschner, D. H., Gilbert, C. S., and Kerr, I. M. (1981). Synthesis, characterization and properties of ppp(A2'p)nApCp and related high-specific-activity 32P-labelled derivatives of ppp(A2'p)nA. Eur. J. Biochem. 115, 79-85. doi: 10.1111/j.1432-1033.1981.tb06200.x
    • (1981) Eur. J. Biochem. , vol.115 , pp. 79-85
    • Silverman, R.H.1    Wreschner, D.H.2    Gilbert, C.S.3    Kerr, I.M.4
  • 116
    • 84879534664 scopus 로고    scopus 로고
    • Evasion of antiviral innate immunity by Theiler's virus L protein through direct inhibition of RNase L.
    • doi: 10.1371/journal.ppat.1003474
    • Sorgeloos, F., Jha, B. K., Silverman, R. H., and Michiels, T. (2013). Evasion of antiviral innate immunity by Theiler's virus L protein through direct inhibition of RNase L. PLoS Pathog. 9:e1003474. doi: 10.1371/journal.ppat.1003474
    • (2013) PLoS Pathog. , vol.9
    • Sorgeloos, F.1    Jha, B.K.2    Silverman, R.H.3    Michiels, T.4
  • 117
    • 84883312419 scopus 로고    scopus 로고
    • Cytomegalovirus downregulates IRE1 to repress the unfolded protein response
    • doi: 10.1371/journal.ppat.1003544
    • Stahl, S., Burkhart, J. M., Hinte, F., Tirosh, B., Mohr, H., Zahedi, R. P., et al. (2013). Cytomegalovirus downregulates IRE1 to repress the unfolded protein response. PLoS Pathog. 9:e1003544. doi: 10.1371/journal.ppat.1003544
    • (2013) PLoS Pathog. , vol.9
    • Stahl, S.1    Burkhart, J.M.2    Hinte, F.3    Tirosh, B.4    Mohr, H.5    Zahedi, R.P.6
  • 118
    • 0036223410 scopus 로고    scopus 로고
    • Japanese encephalitis virus infection initiates endoplasmic reticulum stress and an unfolded protein response
    • doi: 10.1128/JVI.76.9.4162-4171.2002
    • Su, H. L., Liao, C. L., and Lin, Y. L. (2002). Japanese encephalitis virus infection initiates endoplasmic reticulum stress and an unfolded protein response. J. Virol. 76, 4162-4171. doi: 10.1128/JVI.76.9.4162-4171.2002
    • (2002) J. Virol. , vol.76 , pp. 4162-4171
    • Su, H.L.1    Liao, C.L.2    Lin, Y.L.3
  • 119
    • 8144225873 scopus 로고    scopus 로고
    • Structural basis for recognition of 2',5'-linked oligoadenylates by human ribonuclease L
    • doi: 10.1038/sj.emboj.7600420
    • Tanaka, N., Nakanishi, M., Kusakabe, Y., Goto, Y., Kitade, Y., and Nakamura, K. T. (2004). Structural basis for recognition of 2',5'-linked oligoadenylates by human ribonuclease L. EMBO J. 23, 3929-3938. doi: 10.1038/sj.emboj.7600420
    • (2004) EMBO J. , vol.23 , pp. 3929-3938
    • Tanaka, N.1    Nakanishi, M.2    Kusakabe, Y.3    Goto, Y.4    Kitade, Y.5    Nakamura, K.T.6
  • 120
    • 2342435179 scopus 로고    scopus 로고
    • Hepatitis C virus suppresses the IRE1-XBP1 pathway of the unfolded protein response
    • doi: 10.1074/jbc.M312144200
    • Tardif, K. D., Mori, K., Kaufman, R. J., and Siddiqui, A. (2004). Hepatitis C virus suppresses the IRE1-XBP1 pathway of the unfolded protein response. J. Biol. Chem. 279, 17158-17164. doi: 10.1074/jbc.M312144200
    • (2004) J. Biol. Chem. , vol.279 , pp. 17158-17164
    • Tardif, K.D.1    Mori, K.2    Kaufman, R.J.3    Siddiqui, A.4
  • 121
    • 0036314483 scopus 로고    scopus 로고
    • Hepatitis C virus subgenomic replicons induce endoplasmic reticulum stress activating an intracellular signaling pathway
    • doi: 10.1128/JVI.76.15.7453-7459.2002
    • Tardif, K. D., Mori, K., and Siddiqui, A. (2002). Hepatitis C virus subgenomic replicons induce endoplasmic reticulum stress activating an intracellular signaling pathway. J. Virol. 76, 7453-7459. doi: 10.1128/JVI.76.15.7453-7459.2002
    • (2002) J. Virol. , vol.76 , pp. 7453-7459
    • Tardif, K.D.1    Mori, K.2    Siddiqui, A.3
  • 122
    • 79959634861 scopus 로고    scopus 로고
    • Pattern recognition receptors and the innate immune response to viral infection
    • doi: 10.3390/v3060920
    • Thompson, M. R., Kaminski, J. J., Kurt-Jones, E. A., and Fitzgerald, K. A. (2011). Pattern recognition receptors and the innate immune response to viral infection. Viruses 3, 920-940. doi: 10.3390/v3060920
    • (2011) Viruses , vol.3 , pp. 920-940
    • Thompson, M.R.1    Kaminski, J.J.2    Kurt-Jones, E.A.3    Fitzgerald, K.A.4
  • 123
    • 0034312290 scopus 로고    scopus 로고
    • The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response
    • doi: 10.1101/gad.839400
    • Tirasophon, W., Lee, K., Callaghan, B., Welihinda, A., and Kaufman, R. J. (2000). The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response. Genes Dev. 14, 2725-2736. doi: 10.1101/gad.839400
    • (2000) Genes Dev. , vol.14 , pp. 2725-2736
    • Tirasophon, W.1    Lee, K.2    Callaghan, B.3    Welihinda, A.4    Kaufman, R.J.5
  • 124
    • 0032525990 scopus 로고    scopus 로고
    • A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells
    • doi: 10.1101/gad.12.12.1812
    • Tirasophon, W., Welihinda, A. A., and Kaufman, R. J. (1998). A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. Genes Dev. 12, 1812-1824. doi: 10.1101/gad.12.12.1812
    • (1998) Genes Dev. , vol.12 , pp. 1812-1824
    • Tirasophon, W.1    Welihinda, A.A.2    Kaufman, R.J.3
  • 125
    • 44149099332 scopus 로고    scopus 로고
    • A viral RNA competitively inhibits the antiviral endoribonuclease domain of RNase L
    • doi: 10.1261/rna.958908
    • Townsend, H. L., Jha, B. K., Han, J. Q., Maluf, N. K., Silverman, R. H., and Barton, D. J. (2008). A viral RNA competitively inhibits the antiviral endoribonuclease domain of RNase L. RNA 14, 1026-1036. doi: 10.1261/rna.958908
    • (2008) RNA , vol.14 , pp. 1026-1036
    • Townsend, H.L.1    Jha, B.K.2    Han, J.Q.3    Maluf, N.K.4    Silverman, R.H.5    Barton, D.J.6
  • 127
    • 24644508371 scopus 로고    scopus 로고
    • The spread of apoptosis through gap-junctional channels in BHK cells transfected with Cx32
    • doi: 10.1007/s10495-005-0776-8
    • Udawatte, C., and Ripps, H. (2005). The spread of apoptosis through gap-junctional channels in BHK cells transfected with Cx32. Apoptosis 10, 1019-1029. doi: 10.1007/s10495-005-0776-8
    • (2005) Apoptosis , vol.10 , pp. 1019-1029
    • Udawatte, C.1    Ripps, H.2
  • 128
    • 84868525253 scopus 로고    scopus 로고
    • IRE1alpha cleaves select microRNAs during ER stress to derepress translation of proapoptotic Caspase-2
    • doi: 10.1126/science.1226191
    • Upton, J. P., Wang, L., Han, D., Wang, E. S., Huskey, N. E., Lim, L., et al. (2012). IRE1alpha cleaves select microRNAs during ER stress to derepress translation of proapoptotic Caspase-2. Science 338, 818-822. doi: 10.1126/science.1226191
    • (2012) Science , vol.338 , pp. 818-822
    • Upton, J.P.1    Wang, L.2    Han, D.3    Wang, E.S.4    Huskey, N.E.5    Lim, L.6
  • 129
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • doi: 10.1126/science.287.5453.664
    • Urano, F., Wang, X., Bertolotti, A., Zhang, Y., Chung, P., Harding, H. P., et al. (2000). Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287, 664-666. doi: 10.1126/science.287.5453.664
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6
  • 130
    • 84892173964 scopus 로고    scopus 로고
    • Sensing microbial RNA in the cytosol
    • doi: 10.3389/fimmu.2013.00468
    • Vabret, N., and Blander, J. M. (2013). Sensing microbial RNA in the cytosol. Front. Immunol. 4:468. doi: 10.3389/fimmu.2013.00468
    • (2013) Front. Immunol. , vol.4 , pp. 468
    • Vabret, N.1    Blander, J.M.2
  • 131
    • 35748972351 scopus 로고    scopus 로고
    • Hepatitis C virus RNA: dinucleotide frequencies and cleavage by RNase L
    • doi: 10.1016/j.virusres.2007.05.020
    • Washenberger, C. L., Han, J. Q., Kechris, K. J., Jha, B. K., Silverman, R. H., and Barton, D. J. (2007). Hepatitis C virus RNA: dinucleotide frequencies and cleavage by RNase L. Virus Res. 130, 85-95. doi: 10.1016/j.virusres.2007.05.020
    • (2007) Virus Res. , vol.130 , pp. 85-95
    • Washenberger, C.L.1    Han, J.Q.2    Kechris, K.J.3    Jha, B.K.4    Silverman, R.H.5    Barton, D.J.6
  • 132
    • 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
    • doi: 10.1128/JVI.80.10.5059-5064.2006
    • Weber, F., Wagner, V., Rasmussen, S. B., Hartmann, R., and Paludan, S. R. (2006). 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. 80, 5059-5064. doi: 10.1128/JVI.80.10.5059-5064.2006
    • (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
  • 133
    • 0019389403 scopus 로고
    • Ribosomal RNA cleavage, nuclease activation and 2-5A(ppp(A2'p)nA) in interferon-treated cells
    • doi: 10.1093/nar/9.7.1571
    • Wreschner, D. H., James, T. C., Silverman, R. H., and Kerr, I. M. (1981a). Ribosomal RNA cleavage, nuclease activation and 2-5A(ppp(A2'p)nA) in interferon-treated cells. Nucleic Acids Res. 9, 1571-1581. doi: 10.1093/nar/9.7.1571
    • (1981) Nucleic Acids Res , vol.9 , pp. 1571-1581
    • Wreschner, D.H.1    James, T.C.2    Silverman, R.H.3    Kerr, I.M.4
  • 134
    • 0019423024 scopus 로고
    • Interferon action-sequence specificity of the ppp(A2'p)nA-dependent ribonuclease
    • doi: 10.1038/289414a0
    • Wreschner, D. H., Mccauley, J. W., Skehel, J. J., and Kerr, I. M. (1981b). Interferon action-sequence specificity of the ppp(A2'p)nA-dependent ribonuclease. Nature 289, 414-417. doi: 10.1038/289414a0
    • (1981) Nature , vol.289 , pp. 414-417
    • Wreschner, D.H.1    Mccauley, J.W.2    Skehel, J.J.3    Kerr, I.M.4
  • 135
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • doi: 10.1016/S0092-8674(01)00611-0
    • Yoshida, H., Matsui, T., Yamamoto, A., Okada, T., and Mori, K. (2001). XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107, 881-891. doi: 10.1016/S0092-8674(01)00611-0
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 136
    • 84888204980 scopus 로고    scopus 로고
    • Tick-borne encephalitis virus triggers inositol-requiring enzyme 1 (IRE1) and transcription factor 6 (ATF6) pathways of unfolded protein response
    • doi: 10.1016/j.virusres.2013.10.012
    • Yu, C., Achazi, K., and Niedrig, M. (2013). Tick-borne encephalitis virus triggers inositol-requiring enzyme 1 (IRE1) and transcription factor 6 (ATF6) pathways of unfolded protein response. Virus Res. 178, 471-477. doi: 10.1016/j.virusres.2013.10.012
    • (2013) Virus Res. , vol.178 , pp. 471-477
    • Yu, C.1    Achazi, K.2    Niedrig, M.3
  • 137
    • 33751247922 scopus 로고    scopus 로고
    • Flavivirus infection activates the XBP1 pathway of the unfolded protein response to cope with endoplasmic reticulum stress
    • doi: 10.1128/JVI.00879-06
    • Yu, C. Y., Hsu, Y. W., Liao, C. L., and Lin, Y. L. (2006). Flavivirus infection activates the XBP1 pathway of the unfolded protein response to cope with endoplasmic reticulum stress. J. Virol. 80, 11868-11880. doi: 10.1128/JVI.00879-06
    • (2006) J. Virol. , vol.80 , pp. 11868-11880
    • Yu, C.Y.1    Hsu, Y.W.2    Liao, C.L.3    Lin, Y.L.4
  • 138
    • 77956642651 scopus 로고    scopus 로고
    • Coxsackievirus B3 infection activates the unfolded protein response and induces apoptosis through downregulation of p58IPK and activation of CHOP and SREBP1
    • doi: 10.1128/JVI.01416-09
    • Zhang, H. M., Ye, X., Su, Y., Yuan, J., Liu, Z., Stein, D. A., et al. (2010). Coxsackievirus B3 infection activates the unfolded protein response and induces apoptosis through downregulation of p58IPK and activation of CHOP and SREBP1. J. Virol. 84, 8446-8459. doi: 10.1128/JVI.01416-09
    • (2010) J. Virol. , vol.84 , pp. 8446-8459
    • Zhang, H.M.1    Ye, X.2    Su, Y.3    Yuan, J.4    Liu, Z.5    Stein, D.A.6
  • 139
    • 84881415860 scopus 로고    scopus 로고
    • Homologous 2',5'-phosphodiesterases from disparate RNA viruses antagonize antiviral innate immunity
    • doi: 10.1073/pnas.1306917110
    • Zhang, R., Jha, B. K., Ogden, K. M., Dong, B., Zhao, L., Elliott, R., et al. (2013). Homologous 2',5'-phosphodiesterases from disparate RNA viruses antagonize antiviral innate immunity. Proc. Natl. Acad. Sci. U.S.A. 110, 13114-13119. doi: 10.1073/pnas.1306917110
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 13114-13119
    • Zhang, R.1    Jha, B.K.2    Ogden, K.M.3    Dong, B.4    Zhao, L.5    Elliott, R.6
  • 140
    • 84862297105 scopus 로고    scopus 로고
    • Antagonism of the interferon-induced OAS-RNase L pathway by murine coronavirus ns2 protein is required for virus replication and liver pathology
    • doi: 10.1016/j.chom.2012.04.011
    • Zhao, L., Jha, B. K., Wu, A., Elliott, R., Ziebuhr, J., Gorbalenya, A. E., et al. (2012). Antagonism of the interferon-induced OAS-RNase L pathway by murine coronavirus ns2 protein is required for virus replication and liver pathology. Cell Host Microbe 11, 607-616. doi: 10.1016/j.chom.2012.04.011
    • (2012) Cell Host Microbe , vol.11 , pp. 607-616
    • Zhao, L.1    Jha, B.K.2    Wu, A.3    Elliott, R.4    Ziebuhr, J.5    Gorbalenya, A.E.6
  • 141
    • 0027510449 scopus 로고
    • Expression cloning of 2-5A-dependent RNAase: a uniquely regulated mediator of interferon action
    • doi: 10.1016/0092-8674(93)90403-D
    • Zhou, A., Hassel, B. A., and Silverman, R. H. (1993). Expression cloning of 2-5A-dependent RNAase: a uniquely regulated mediator of interferon action. Cell 72, 753-765. doi: 10.1016/0092-8674(93)90403-D
    • (1993) Cell , vol.72 , pp. 753-765
    • Zhou, A.1    Hassel, B.A.2    Silverman, R.H.3
  • 142
    • 27144545445 scopus 로고    scopus 로고
    • Mapping of the human RNASEL promoter and expression in cancer and normal cells
    • doi: 10.1089/jir.2005.25.595
    • Zhou, A., Molinaro, R. J., Malathi, K., and Silverman, R. H. (2005). Mapping of the human RNASEL promoter and expression in cancer and normal cells. J. Interferon Cytokine Res. 25, 595-603. doi: 10.1089/jir.2005.25.595
    • (2005) J. Interferon Cytokine Res. , vol.25 , pp. 595-603
    • Zhou, A.1    Molinaro, R.J.2    Malathi, K.3    Silverman, R.H.4
  • 143
    • 0030817251 scopus 로고    scopus 로고
    • Interferon action and apoptosis are defective in mice devoid of 2',5'-oligoadenylate-dependent RNase L
    • doi: 10.1093/emboj/16.21.6355
    • Zhou, A., Paranjape, J., Brown, T. L., Nie, H., Naik, S., Dong, B., et al. (1997). Interferon action and apoptosis are defective in mice devoid of 2',5'-oligoadenylate-dependent RNase L. EMBO J. 16, 6355-6363. doi: 10.1093/emboj/16.21.6355
    • (1997) EMBO J. , vol.16 , pp. 6355-6363
    • Zhou, A.1    Paranjape, J.2    Brown, T.L.3    Nie, H.4    Naik, S.5    Dong, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.