메뉴 건너뛰기




Volumn 27, Issue 7, 2011, Pages 286-293

Strategies for viral RNA stability: Live long and prosper

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; NUCLEASE; VIRUS RNA;

EID: 79959368183     PISSN: 01689525     EISSN: 01689525     Source Type: Journal    
DOI: 10.1016/j.tig.2011.04.003     Document Type: Review
Times cited : (39)

References (88)
  • 1
    • 33847771442 scopus 로고    scopus 로고
    • The highways and byways of mRNA decay
    • Garneau N.L., et al. The highways and byways of mRNA decay. Nat. Rev. Mol. Cell Biol. 2007, 8:113-126.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 113-126
    • Garneau, N.L.1
  • 2
    • 41149138114 scopus 로고    scopus 로고
    • Multifunctional deadenylase complexes diversify mRNA control
    • Goldstrohm A.C., Wickens M. Multifunctional deadenylase complexes diversify mRNA control. Nat. Rev. Mol. Cell Biol. 2008, 9:337-344.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 337-344
    • Goldstrohm, A.C.1    Wickens, M.2
  • 3
    • 33745869788 scopus 로고    scopus 로고
    • RNA-quality control by the exosome
    • Houseley J., et al. RNA-quality control by the exosome. Nat. Rev. Mol. Cell Biol. 2006, 9:529-539.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 529-539
    • Houseley, J.1
  • 4
    • 79952362044 scopus 로고    scopus 로고
    • Structural and biochemical studies of the 5'→3' exoribonuclease Xrn1
    • Chang J.H., et al. Structural and biochemical studies of the 5'→3' exoribonuclease Xrn1. Nat. Struct. Mol. Biol. 2011, 18:270-276.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 270-276
    • Chang, J.H.1
  • 5
    • 78149426485 scopus 로고    scopus 로고
    • Multiple mRNA decapping enzymes in mammalian cells
    • Song M.G., et al. Multiple mRNA decapping enzymes in mammalian cells. Mol. Cell 2010, 40:423-432.
    • (2010) Mol. Cell , vol.40 , pp. 423-432
    • Song, M.G.1
  • 6
    • 70450182086 scopus 로고    scopus 로고
    • Gene expression networks: competing mRNA decay pathways in mammalian cells
    • Maquat L.E., Gong C. Gene expression networks: competing mRNA decay pathways in mammalian cells. Biochem. Soc. Trans. 2009, 37:1287-1292.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 1287-1292
    • Maquat, L.E.1    Gong, C.2
  • 7
    • 78649839805 scopus 로고    scopus 로고
    • Dissection of Dom34-Hbs1 reveals independent functions in two RNA quality control pathways
    • van den Elzen A.M., et al. Dissection of Dom34-Hbs1 reveals independent functions in two RNA quality control pathways. Nat. Struct. Mol. Biol. 2010, 17:1446-1452.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1446-1452
    • van den Elzen, A.M.1
  • 8
    • 79952304472 scopus 로고    scopus 로고
    • Different nuclease requirements for exosome-mediated degradation of normal and nonstop mRNAs
    • Schaeffer D., van Hoof A. Different nuclease requirements for exosome-mediated degradation of normal and nonstop mRNAs. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:2366-2371.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 2366-2371
    • Schaeffer, D.1    van Hoof, A.2
  • 9
    • 78751504841 scopus 로고    scopus 로고
    • Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment
    • Clement S.L., et al. Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment. Mol. Cell. Biol. 2011, 31:256-266.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 256-266
    • Clement, S.L.1
  • 10
    • 78649865439 scopus 로고    scopus 로고
    • Alternatively expressed domains of AU-rich element RNA-binding protein 1 (AUF1) regulate RNA-binding affinity, RNA-induced protein oligomerization, and the local conformation of bound RNA ligands
    • Zucconi B.E., et al. Alternatively expressed domains of AU-rich element RNA-binding protein 1 (AUF1) regulate RNA-binding affinity, RNA-induced protein oligomerization, and the local conformation of bound RNA ligands. J. Biol. Chem. 2010, 285:39127-39139.
    • (2010) J. Biol. Chem. , vol.285 , pp. 39127-39139
    • Zucconi, B.E.1
  • 11
    • 84862833318 scopus 로고    scopus 로고
    • The role of KSRP in mRNA decay and microRNA precursor maturation
    • Gherzi R., et al. The role of KSRP in mRNA decay and microRNA precursor maturation. Wiley Interdisciplinary Rev.: RNA 2010, 1:230-239.
    • (2010) Wiley Interdisciplinary Rev.: RNA , vol.1 , pp. 230-239
    • Gherzi, R.1
  • 12
    • 77956170809 scopus 로고    scopus 로고
    • RNA-based antiviral immunity
    • Ding S.W. RNA-based antiviral immunity. Nat. Rev. Immunol. 2010, 10:632-644.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 632-644
    • Ding, S.W.1
  • 13
    • 77956034926 scopus 로고    scopus 로고
    • Novel endoribonucleases as central players in various pathways of eukaryotic RNA metabolism
    • Tomecki R., Dziembowski A. Novel endoribonucleases as central players in various pathways of eukaryotic RNA metabolism. RNA 2010, 16:1692-1724.
    • (2010) RNA , vol.16 , pp. 1692-1724
    • Tomecki, R.1    Dziembowski, A.2
  • 14
    • 25444484963 scopus 로고    scopus 로고
    • Control of gene expression during T cell activation: alternate regulation of mRNA transcription and mRNA stability
    • Cheadle C., et al. Control of gene expression during T cell activation: alternate regulation of mRNA transcription and mRNA stability. BMC Genomics 2005, 6:75.
    • (2005) BMC Genomics , vol.6 , pp. 75
    • Cheadle, C.1
  • 15
    • 77952218796 scopus 로고    scopus 로고
    • Salmonella-mediated delivery of RNase P-based ribozymes for inhibition of viral gene expression and replication in human cells
    • Bai Y., et al. Salmonella-mediated delivery of RNase P-based ribozymes for inhibition of viral gene expression and replication in human cells. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:7269-7274.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 7269-7274
    • Bai, Y.1
  • 16
    • 33646590585 scopus 로고    scopus 로고
    • Tethering KSRP, a decay-promoting AU-rich element-binding protein, to mRNAs elicits mRNA decay
    • Chou C.F., et al. Tethering KSRP, a decay-promoting AU-rich element-binding protein, to mRNAs elicits mRNA decay. Mol. Cell. Biol. 2006, 26:3695-3706.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3695-3706
    • Chou, C.F.1
  • 17
    • 78549284909 scopus 로고    scopus 로고
    • 2'-O methylation of the viral mRNA cap evades host restriction by IFIT family members
    • Daffis S., et al. 2'-O methylation of the viral mRNA cap evades host restriction by IFIT family members. Nature 2010, 2468:452-456.
    • (2010) Nature , vol.2468 , pp. 452-456
    • Daffis, S.1
  • 18
    • 77956286560 scopus 로고    scopus 로고
    • The cytoplasmic fate of an mRNP is determined cotranscriptionally: exception or rule?
    • Trcek T., Singer R.H. The cytoplasmic fate of an mRNP is determined cotranscriptionally: exception or rule?. Genes Dev. 2010, 24:1827-1831.
    • (2010) Genes Dev. , vol.24 , pp. 1827-1831
    • Trcek, T.1    Singer, R.H.2
  • 19
    • 77950839519 scopus 로고    scopus 로고
    • Identification of a dominant negative inhibitor of human zinc finger antiviral protein reveals a functional endogenous pool and critical homotypic interactions
    • Law L.M., et al. Identification of a dominant negative inhibitor of human zinc finger antiviral protein reveals a functional endogenous pool and critical homotypic interactions. J. Virol. 2010, 84:4504-4512.
    • (2010) J. Virol. , vol.84 , pp. 4504-4512
    • Law, L.M.1
  • 20
    • 77949899515 scopus 로고    scopus 로고
    • Viral induction of the zinc finger antiviral protein is IRF3-dependent but NF-kappaB-independent
    • Wang N., et al. Viral induction of the zinc finger antiviral protein is IRF3-dependent but NF-kappaB-independent. J. Biol. Chem. 2010, 285:6080-6090.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6080-6090
    • Wang, N.1
  • 21
    • 0037031709 scopus 로고    scopus 로고
    • Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein
    • Gao G., et al. Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein. Science 2002, 297:1703-1706.
    • (2002) Science , vol.297 , pp. 1703-1706
    • Gao, G.1
  • 22
    • 38849094611 scopus 로고    scopus 로고
    • A premature termination codon mutation at the C terminus of foamy virus Gag downregulates the levels of spliced pol mRNA
    • Lee E.G., et al. A premature termination codon mutation at the C terminus of foamy virus Gag downregulates the levels of spliced pol mRNA. J. Virol. 2008, 82:1656-1664.
    • (2008) J. Virol. , vol.82 , pp. 1656-1664
    • Lee, E.G.1
  • 23
    • 79954611142 scopus 로고    scopus 로고
    • Endogenous ribosomal frameshift signals operate as mRNA destabilizing elements through at least two molecular pathways in yeast
    • Belew A.T., et al. Endogenous ribosomal frameshift signals operate as mRNA destabilizing elements through at least two molecular pathways in yeast. Nucleic Acids Res. 2011, 39:2799-2808.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 2799-2808
    • Belew, A.T.1
  • 24
    • 44449098281 scopus 로고    scopus 로고
    • SARS-coronavirus replication/transcription complexes are membrane-protected and need a host factor for activity in vitro
    • van Hemert M.J., et al. SARS-coronavirus replication/transcription complexes are membrane-protected and need a host factor for activity in vitro. PLoS Pathog. 2008, 4:e1000054.
    • (2008) PLoS Pathog. , vol.4
    • van Hemert, M.J.1
  • 25
    • 34547510230 scopus 로고    scopus 로고
    • Mutational analysis of a viral RNA element that counteracts rapid RNA decay by interaction with the polyadenylate tail
    • Conrad N.K., et al. Mutational analysis of a viral RNA element that counteracts rapid RNA decay by interaction with the polyadenylate tail. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:10412-10417.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 10412-10417
    • Conrad, N.K.1
  • 26
    • 78649422018 scopus 로고    scopus 로고
    • Poly(A) tail recognition by a viral RNA element through assembly of a triple helix
    • Mitton-Fry R.M., et al. Poly(A) tail recognition by a viral RNA element through assembly of a triple helix. Science 2010, 330:1244-1247.
    • (2010) Science , vol.330 , pp. 1244-1247
    • Mitton-Fry, R.M.1
  • 27
    • 0033557214 scopus 로고    scopus 로고
    • 3'-Terminal RNA structures and poly(U) tracts inhibit initiation by a 3'-->5' exonuclease in vitro
    • Ford L.P., Wilusz J. 3'-Terminal RNA structures and poly(U) tracts inhibit initiation by a 3'-->5' exonuclease in vitro. Nucleic Acids Res. 1999, 27:1159-1167.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1159-1167
    • Ford, L.P.1    Wilusz, J.2
  • 28
    • 77950939771 scopus 로고    scopus 로고
    • Structural and functional properties of the vesicular stomatitis virus nucleoprotein-RNA complex as revealed by proteolytic digestion
    • Sarkar A., et al. Structural and functional properties of the vesicular stomatitis virus nucleoprotein-RNA complex as revealed by proteolytic digestion. Virology 2010, 401:61-69.
    • (2010) Virology , vol.401 , pp. 61-69
    • Sarkar, A.1
  • 29
    • 77950439778 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus ORF57 protein binds and protects a nuclear noncoding RNA from cellular RNA decay pathways
    • Sahin B.B., et al. Kaposi's sarcoma-associated herpesvirus ORF57 protein binds and protects a nuclear noncoding RNA from cellular RNA decay pathways. PLoS Pathog. 2010, 6:e1000799.
    • (2010) PLoS Pathog. , vol.6
    • Sahin, B.B.1
  • 31
    • 77956312311 scopus 로고    scopus 로고
    • Sindbis virus usurps the cellular HuR protein to stabilize its transcripts and promote productive infections in mammalian and mosquito cells
    • Sokoloski K.J., et al. Sindbis virus usurps the cellular HuR protein to stabilize its transcripts and promote productive infections in mammalian and mosquito cells. Cell Host Microbe 2010, 8:196-207.
    • (2010) Cell Host Microbe , vol.8 , pp. 196-207
    • Sokoloski, K.J.1
  • 32
    • 21844438516 scopus 로고    scopus 로고
    • Inhibition of hepatitis C virus translation and subgenomic replication by siRNAs directed against highly conserved HCV sequence and cellular HCV cofactors
    • Korf M., et al. Inhibition of hepatitis C virus translation and subgenomic replication by siRNAs directed against highly conserved HCV sequence and cellular HCV cofactors. J. Hepatol. 2005, 43:225-234.
    • (2005) J. Hepatol. , vol.43 , pp. 225-234
    • Korf, M.1
  • 33
    • 57049151268 scopus 로고    scopus 로고
    • The RNA stability regulator HuR regulates L1 protein expression in vivo in differentiating cervical epithelial cells
    • Cumming S.A., et al. The RNA stability regulator HuR regulates L1 protein expression in vivo in differentiating cervical epithelial cells. Virology 2009, 383:142-149.
    • (2009) Virology , vol.383 , pp. 142-149
    • Cumming, S.A.1
  • 34
    • 79551708353 scopus 로고    scopus 로고
    • Foamy virus nuclear RNA export is distinct from that of other retroviruses
    • Bodem J., et al. Foamy virus nuclear RNA export is distinct from that of other retroviruses. J. Virol. 2011, 85:2333-2341.
    • (2011) J. Virol. , vol.85 , pp. 2333-2341
    • Bodem, J.1
  • 35
    • 79959821564 scopus 로고    scopus 로고
    • Viral-mediated stabilization of AU-rich element containing mRNA contributes to cell transformation
    • Kuroshima T., et al. Viral-mediated stabilization of AU-rich element containing mRNA contributes to cell transformation. Oncogene 2011, 10.1038/onc.2011.14.
    • (2011) Oncogene
    • Kuroshima, T.1
  • 36
    • 34247617164 scopus 로고    scopus 로고
    • The 3' untranslated region complex involved in stabilization of human alpha-globin mRNA assembles in the nucleus and serves an independent role as a splice enhancer
    • Ji X., et al. The 3' untranslated region complex involved in stabilization of human alpha-globin mRNA assembles in the nucleus and serves an independent role as a splice enhancer. Mol. Cell. Biol. 2007, 27:3290-3302.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3290-3302
    • Ji, X.1
  • 37
    • 66149143922 scopus 로고    scopus 로고
    • Depletion of the poly(C)-binding proteins alphaCP1 and alphaCP2 from K562 cells leads to p53-independent induction of cyclin-dependent kinase inhibitor (CDKN1A) and G1 arrest
    • Waggoner S.A., et al. Depletion of the poly(C)-binding proteins alphaCP1 and alphaCP2 from K562 cells leads to p53-independent induction of cyclin-dependent kinase inhibitor (CDKN1A) and G1 arrest. J. Biol. Chem. 2009, 284:9039-9049.
    • (2009) J. Biol. Chem. , vol.284 , pp. 9039-9049
    • Waggoner, S.A.1
  • 38
    • 67349238700 scopus 로고    scopus 로고
    • Altered interactions between stem-loop IV within the 5' noncoding region of coxsackievirus RNA and poly(rC) binding protein 2: effects on IRES-mediated translation and viral infectivity
    • Sean P., et al. Altered interactions between stem-loop IV within the 5' noncoding region of coxsackievirus RNA and poly(rC) binding protein 2: effects on IRES-mediated translation and viral infectivity. Virology 2009, 389:45-58.
    • (2009) Virology , vol.389 , pp. 45-58
    • Sean, P.1
  • 39
    • 42649123361 scopus 로고    scopus 로고
    • Protein-RNA tethering: the role of poly(C) binding protein 2 in poliovirus RNA replication
    • Spear A., et al. Protein-RNA tethering: the role of poly(C) binding protein 2 in poliovirus RNA replication. Virology 2008, 374:280-291.
    • (2008) Virology , vol.374 , pp. 280-291
    • Spear, A.1
  • 40
    • 78650852496 scopus 로고    scopus 로고
    • Expression of IMP1 enhances production of murine leukemia virus vector by facilitating viral genomic RNA packaging
    • Mai Y., Gao G. Expression of IMP1 enhances production of murine leukemia virus vector by facilitating viral genomic RNA packaging. PLoS ONE 2010, 5:e15881.
    • (2010) PLoS ONE , vol.5
    • Mai, Y.1    Gao, G.2
  • 41
    • 77955186506 scopus 로고    scopus 로고
    • Structural features in the Rous sarcoma virus RNA stability element are necessary for sensing the correct termination codon
    • Withers J.B., Beemon K.L. Structural features in the Rous sarcoma virus RNA stability element are necessary for sensing the correct termination codon. Retrovirology 2010, 7:65.
    • (2010) Retrovirology , vol.7 , pp. 65
    • Withers, J.B.1    Beemon, K.L.2
  • 42
    • 78149353044 scopus 로고    scopus 로고
    • Bunyaviridae RNA polymerases (L-protein) have an N-terminal, influenza-like endonuclease domain, essential for viral cap-dependent transcription
    • Reguera J., et al. Bunyaviridae RNA polymerases (L-protein) have an N-terminal, influenza-like endonuclease domain, essential for viral cap-dependent transcription. PLoS Pathog. 2010, 6:e1001101.
    • (2010) PLoS Pathog. , vol.6
    • Reguera, J.1
  • 43
    • 77954856078 scopus 로고    scopus 로고
    • Protein kinase R contributes to immunity against specific viruses by regulating interferon mRNA integrity
    • Schulz O., et al. Protein kinase R contributes to immunity against specific viruses by regulating interferon mRNA integrity. Cell Host Microbe 2010, 7:354-361.
    • (2010) Cell Host Microbe , vol.7 , pp. 354-361
    • Schulz, O.1
  • 44
    • 77956937785 scopus 로고    scopus 로고
    • Magnesium-dependent interaction of PKR with adenovirus VAI
    • Launer-Felty K., et al. Magnesium-dependent interaction of PKR with adenovirus VAI. J. Mol. Biol. 2010, 402:638-644.
    • (2010) J. Mol. Biol. , vol.402 , pp. 638-644
    • Launer-Felty, K.1
  • 45
    • 78751543984 scopus 로고    scopus 로고
    • Dcp1 links coactivators of mRNA decapping to Dcp2 by proline recognition
    • Borja M.S., et al. Dcp1 links coactivators of mRNA decapping to Dcp2 by proline recognition. RNA 2011, 17:278-290.
    • (2011) RNA , vol.17 , pp. 278-290
    • Borja, M.S.1
  • 46
    • 78650069922 scopus 로고    scopus 로고
    • Poliovirus-mediated disruption of cytoplasmic processing bodies
    • Dougherty J.D., et al. Poliovirus-mediated disruption of cytoplasmic processing bodies. J. Virol. 2011, 85:64-75.
    • (2011) J. Virol. , vol.85 , pp. 64-75
    • Dougherty, J.D.1
  • 47
    • 52649167373 scopus 로고    scopus 로고
    • Cleavage of poly(A)-binding protein by poliovirus 3C proteinase inhibits viral internal ribosome entry site-mediated translation
    • Bonderoff J.M., et al. Cleavage of poly(A)-binding protein by poliovirus 3C proteinase inhibits viral internal ribosome entry site-mediated translation. J. Virol. 2008, 82:9389-9399.
    • (2008) J. Virol. , vol.82 , pp. 9389-9399
    • Bonderoff, J.M.1
  • 48
    • 77956378342 scopus 로고    scopus 로고
    • Combined agonist-antagonist genome-wide functional screening identifies broadly active antiviral microRNAs
    • Santhakumar D., et al. Combined agonist-antagonist genome-wide functional screening identifies broadly active antiviral microRNAs. Proc. Natl. Acad. Sci. U.S.A. 2010, 2107:13830-13835.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.2107 , pp. 13830-13835
    • Santhakumar, D.1
  • 49
    • 77953798171 scopus 로고    scopus 로고
    • Down-regulation of a host microRNA by a Herpesvirus saimiri noncoding RNA
    • Cazalla D., et al. Down-regulation of a host microRNA by a Herpesvirus saimiri noncoding RNA. Science 2010, 328:1563-1566.
    • (2010) Science , vol.328 , pp. 1563-1566
    • Cazalla, D.1
  • 50
    • 0346995213 scopus 로고    scopus 로고
    • Evasion of cellular antiviral responses by human cytomegalovirus TRS1 and IRS1
    • Child S.J., et al. Evasion of cellular antiviral responses by human cytomegalovirus TRS1 and IRS1. J. Virol. 2004, 78:197-205.
    • (2004) J. Virol. , vol.78 , pp. 197-205
    • Child, S.J.1
  • 51
    • 77952585622 scopus 로고    scopus 로고
    • T2 Family ribonucleases: ancient enzymes with diverse roles
    • Luhtala N., Parker R. T2 Family ribonucleases: ancient enzymes with diverse roles. Trends Biochem. Sci. 2010, 35:253-259.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 253-259
    • Luhtala, N.1    Parker, R.2
  • 52
    • 67649881103 scopus 로고    scopus 로고
    • RNASET2-deficient cystic leukoencephalopathy resembles congenital cytomegalovirus brain infection
    • Henneke M., et al. RNASET2-deficient cystic leukoencephalopathy resembles congenital cytomegalovirus brain infection. Nat. Genet. 2009, 41:773-775.
    • (2009) Nat. Genet. , vol.41 , pp. 773-775
    • Henneke, M.1
  • 53
    • 78651507445 scopus 로고    scopus 로고
    • Adenosine deaminases acting on RNA, RNA editing, and interferon action
    • George C.X., et al. Adenosine deaminases acting on RNA, RNA editing, and interferon action. J. Interferon Cytokine Res. 2011, 31:99-117.
    • (2011) J. Interferon Cytokine Res. , vol.31 , pp. 99-117
    • George, C.X.1
  • 54
    • 79959362665 scopus 로고    scopus 로고
    • Crystal structure of a KSHV-SOX-DNA complex: insights into the molecular mechanisms underlying DNase activity and host shutoff
    • Bagnéris C., et al. Crystal structure of a KSHV-SOX-DNA complex: insights into the molecular mechanisms underlying DNase activity and host shutoff. Nucleic Acids Res. 2011, 10.1093/nar/gkr111.
    • (2011) Nucleic Acids Res.
    • Bagnéris, C.1
  • 55
    • 66249138088 scopus 로고    scopus 로고
    • Aberrant herpesvirus-induced polyadenylation correlates with cellular messenger RNA destruction
    • Lee Y.J., Glaunsinger B.A. Aberrant herpesvirus-induced polyadenylation correlates with cellular messenger RNA destruction. PLoS Biol. 2009, 7:e1000107.
    • (2009) PLoS Biol. , vol.7
    • Lee, Y.J.1    Glaunsinger, B.A.2
  • 56
    • 77957853228 scopus 로고    scopus 로고
    • Nuclear import of cytoplasmic poly(A) binding protein restricts gene expression via hyperadenylation and nuclear retention of mRNA
    • Kumar G.R., Glaunsinger B.A. Nuclear import of cytoplasmic poly(A) binding protein restricts gene expression via hyperadenylation and nuclear retention of mRNA. Mol. Cell. Biol. 2010, 30:4996-5008.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 4996-5008
    • Kumar, G.R.1    Glaunsinger, B.A.2
  • 57
    • 77952702091 scopus 로고    scopus 로고
    • Evidence for translational regulation by the herpes simplex virus virion host shutoff protein
    • Saffran H.A., et al. Evidence for translational regulation by the herpes simplex virus virion host shutoff protein. J. Virol. 2010, 84:6041-6049.
    • (2010) J. Virol. , vol.84 , pp. 6041-6049
    • Saffran, H.A.1
  • 58
    • 68149163563 scopus 로고    scopus 로고
    • A bridge crosses the active-site canyon of the Epstein-Barr virus nuclease with DNase and RNase activities
    • Buisson M., et al. A bridge crosses the active-site canyon of the Epstein-Barr virus nuclease with DNase and RNase activities. J. Mol. Biol. 2009, 391:717-728.
    • (2009) J. Mol. Biol. , vol.391 , pp. 717-728
    • Buisson, M.1
  • 59
    • 33847779501 scopus 로고    scopus 로고
    • Vaccinia virus D10 protein has mRNA decapping activity, providing a mechanism for control of host and viral gene expression
    • Parrish S., et al. Vaccinia virus D10 protein has mRNA decapping activity, providing a mechanism for control of host and viral gene expression. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:2139-2144.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 2139-2144
    • Parrish, S.1
  • 60
    • 36348981668 scopus 로고    scopus 로고
    • Characterization of a second vaccinia virus mRNA-decapping enzyme conserved in poxviruses
    • Parrish S., Moss B. Characterization of a second vaccinia virus mRNA-decapping enzyme conserved in poxviruses. J. Virol. 2007, 81:12973-12978.
    • (2007) J. Virol. , vol.81 , pp. 12973-12978
    • Parrish, S.1    Moss, B.2
  • 61
    • 78649827255 scopus 로고    scopus 로고
    • Insights into the molecular determinants involved in cap recognition by the vaccinia virus D10 decapping enzyme
    • Soulière M.F., et al. Insights into the molecular determinants involved in cap recognition by the vaccinia virus D10 decapping enzyme. Nucleic Acids Res. 2010, 38:7599-7610.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 7599-7610
    • Soulière, M.F.1
  • 62
    • 78149308100 scopus 로고    scopus 로고
    • The N-terminal domain of the arenavirus L protein is an RNA endonuclease essential in mRNA transcription
    • Morin B., et al. The N-terminal domain of the arenavirus L protein is an RNA endonuclease essential in mRNA transcription. PLoS Pathog. 2010, 6:e1001038.
    • (2010) PLoS Pathog. , vol.6
    • Morin, B.1
  • 63
    • 14744304265 scopus 로고    scopus 로고
    • The structural basis of recognition and removal of cellular mRNA 7-methyl G 'caps' by a viral capsid protein: a unique viral response to host defense
    • Tang J., et al. The structural basis of recognition and removal of cellular mRNA 7-methyl G 'caps' by a viral capsid protein: a unique viral response to host defense. J. Mol. Recognit. 2005, 18:158-168.
    • (2005) J. Mol. Recognit. , vol.18 , pp. 158-168
    • Tang, J.1
  • 64
    • 77954902027 scopus 로고    scopus 로고
    • Yeast double-stranded RNA virus L-A deliberately synthesizes RNA transcripts with 5'-diphosphate
    • Fujimura T., Esteban R. Yeast double-stranded RNA virus L-A deliberately synthesizes RNA transcripts with 5'-diphosphate. J. Biol. Chem. 2010, 285:22911-22918.
    • (2010) J. Biol. Chem. , vol.285 , pp. 22911-22918
    • Fujimura, T.1    Esteban, R.2
  • 65
    • 70350768988 scopus 로고    scopus 로고
    • A two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein
    • Kamitani W., et al. A two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein. Nat. Struct. Mol. Biol. 2009, 16:1134-1140.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1134-1140
    • Kamitani, W.1
  • 66
    • 79952303123 scopus 로고    scopus 로고
    • Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3' to 5' exonuclease activity essential for immune suppression
    • Hastie K.M., et al. Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3' to 5' exonuclease activity essential for immune suppression. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:2396-2401.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 2396-2401
    • Hastie, K.M.1
  • 67
    • 78650132935 scopus 로고    scopus 로고
    • Cap binding and immune evasion revealed by Lassa nucleoprotein structure
    • Qi L., et al. Cap binding and immune evasion revealed by Lassa nucleoprotein structure. Nature 2010, 468:779-783.
    • (2010) Nature , vol.468 , pp. 779-783
    • Qi, L.1
  • 68
    • 33645518839 scopus 로고    scopus 로고
    • Discovery of an RNA virus 3'->5' exoribonuclease that is critically involved in coronavirus RNA synthesis
    • Minskaia E., et al. Discovery of an RNA virus 3'->5' exoribonuclease that is critically involved in coronavirus RNA synthesis. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:5108-5113.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 5108-5113
    • Minskaia, E.1
  • 69
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • Steitz T.A., Steitz J.A. A general two-metal-ion mechanism for catalytic RNA. Proc. Natl. Acad. Sci. U.S.A. 1993, 90:6498-6502.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 70
    • 57049096375 scopus 로고    scopus 로고
    • A highly structured, nuclease-resistant, noncoding RNA produced by flaviviruses is required for pathogenicity
    • Pijlman G.P., et al. A highly structured, nuclease-resistant, noncoding RNA produced by flaviviruses is required for pathogenicity. Cell Host Microbe 2008, 4:579-591.
    • (2008) Cell Host Microbe , vol.4 , pp. 579-591
    • Pijlman, G.P.1
  • 71
    • 77957966906 scopus 로고    scopus 로고
    • RNA structures required for production of subgenomic flavivirus RNA
    • Funk A., et al. RNA structures required for production of subgenomic flavivirus RNA. J. Virol. 2010, 84:11407-11417.
    • (2010) J. Virol. , vol.84 , pp. 11407-11417
    • Funk, A.1
  • 72
    • 77957935535 scopus 로고    scopus 로고
    • An RNA pseudoknot is required for production of yellow fever virus subgenomic RNA by the host nuclease XRN1
    • Silva P.A., et al. An RNA pseudoknot is required for production of yellow fever virus subgenomic RNA by the host nuclease XRN1. J. Virol. 2010, 284:11395-11406.
    • (2010) J. Virol. , vol.284 , pp. 11395-11406
    • Silva, P.A.1
  • 73
    • 46749124698 scopus 로고    scopus 로고
    • Position-dependent function for a tandem microRNA miR-122-binding site located in the hepatitis C virus RNA genome
    • Jopling C.L., et al. Position-dependent function for a tandem microRNA miR-122-binding site located in the hepatitis C virus RNA genome. Cell Host Microbe 2008, 4:77-85.
    • (2008) Cell Host Microbe , vol.4 , pp. 77-85
    • Jopling, C.L.1
  • 74
    • 74249112787 scopus 로고    scopus 로고
    • Therapeutic silencing of microRNA-122 in primates with chronic hepatitis C virus infection
    • Lanford R.E., et al. Therapeutic silencing of microRNA-122 in primates with chronic hepatitis C virus infection. Science 2010, 327:198-201.
    • (2010) Science , vol.327 , pp. 198-201
    • Lanford, R.E.1
  • 75
    • 79952768199 scopus 로고    scopus 로고
    • Masking the 5' terminal nucleotides of the hepatitis C virus genome by an unconventional microRNA-target RNA complex
    • Machlin E.S., et al. Masking the 5' terminal nucleotides of the hepatitis C virus genome by an unconventional microRNA-target RNA complex. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:3193-3198.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 3193-3198
    • Machlin, E.S.1
  • 76
    • 77954055072 scopus 로고    scopus 로고
    • Infidelity of SARS-CoV Nsp14-exonuclease mutant virus replication is revealed by complete genome sequencing
    • Eckerle L.D., et al. Infidelity of SARS-CoV Nsp14-exonuclease mutant virus replication is revealed by complete genome sequencing. PLoS Pathog. 2010, 6:e1000896.
    • (2010) PLoS Pathog. , vol.6
    • Eckerle, L.D.1
  • 77
    • 36048969246 scopus 로고    scopus 로고
    • High fidelity of murine hepatitis virus replication is decreased in nsp14 exoribonuclease mutants
    • Eckerle L.D., et al. High fidelity of murine hepatitis virus replication is decreased in nsp14 exoribonuclease mutants. J. Virol. 2007, 81:12135-12144.
    • (2007) J. Virol. , vol.81 , pp. 12135-12144
    • Eckerle, L.D.1
  • 78
    • 69249217786 scopus 로고    scopus 로고
    • Identification of RNA instability elements in Borna disease virus
    • Siemetzki U., et al. Identification of RNA instability elements in Borna disease virus. Virus Res. 2009, 144:27-34.
    • (2009) Virus Res. , vol.144 , pp. 27-34
    • Siemetzki, U.1
  • 79
    • 2442666665 scopus 로고    scopus 로고
    • Transcription and replication of nonsegmented negative-strand RNA viruses
    • Whelan S.P., et al. Transcription and replication of nonsegmented negative-strand RNA viruses. Curr. Top. Microbiol. Immunol. 2004, 283:61-119.
    • (2004) Curr. Top. Microbiol. Immunol. , vol.283 , pp. 61-119
    • Whelan, S.P.1
  • 80
    • 77951489100 scopus 로고    scopus 로고
    • 5' to 3' mRNA decay factors colocalize with Ty1 gag and human APOBEC3G and promote Ty1 retrotransposition
    • Dutko J.A., et al. 5' to 3' mRNA decay factors colocalize with Ty1 gag and human APOBEC3G and promote Ty1 retrotransposition. J. Virol. 2010, 84:5052-5066.
    • (2010) J. Virol. , vol.84 , pp. 5052-5066
    • Dutko, J.A.1
  • 81
    • 42449143475 scopus 로고    scopus 로고
    • Unexpected roles for UPF1 in HIV-1 RNA metabolism and translation
    • Ajamian L., et al. Unexpected roles for UPF1 in HIV-1 RNA metabolism and translation. RNA 2008, 14:914-927.
    • (2008) RNA , vol.14 , pp. 914-927
    • Ajamian, L.1
  • 82
    • 28544442127 scopus 로고    scopus 로고
    • Eukaryotic Lsm proteins: lessons from bacteria
    • Wilusz C.J., Wilusz J. Eukaryotic Lsm proteins: lessons from bacteria. Nat. Struct. Mol. Biol. 2005, 12:1031-1036.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 1031-1036
    • Wilusz, C.J.1    Wilusz, J.2
  • 83
    • 38449123517 scopus 로고    scopus 로고
    • Mammalian stress granules and processing bodies
    • Kedersha N., Anderson P. Mammalian stress granules and processing bodies. Methods Enzymol. 2007, 431:61-81.
    • (2007) Methods Enzymol. , vol.431 , pp. 61-81
    • Kedersha, N.1    Anderson, P.2
  • 84
    • 78649722117 scopus 로고    scopus 로고
    • The human Pat1b protein: a novel mRNA deadenylation factor identified by a new immunoprecipitation technique
    • Totaro A., et al. The human Pat1b protein: a novel mRNA deadenylation factor identified by a new immunoprecipitation technique. Nucleic Acids Res. 2011, 39:635-647.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 635-647
    • Totaro, A.1
  • 85
    • 77950260836 scopus 로고    scopus 로고
    • LSm1-7 complexes bind to specific sites in viral RNA genomes and regulate their translation and replication
    • Galão R.P., et al. LSm1-7 complexes bind to specific sites in viral RNA genomes and regulate their translation and replication. RNA 2010, 16:817-827.
    • (2010) RNA , vol.16 , pp. 817-827
    • Galão, R.P.1
  • 86
    • 69449087208 scopus 로고    scopus 로고
    • Translation and replication of hepatitis C virus genomic RNA depends on ancient cellular proteins that control mRNA fates
    • Scheller N., et al. Translation and replication of hepatitis C virus genomic RNA depends on ancient cellular proteins that control mRNA fates. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:13517-13522.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 13517-13522
    • Scheller, N.1
  • 87
    • 77953319069 scopus 로고    scopus 로고
    • DDX6 (Rck/p54) is required for efficient hepatitis C virus replication but not for internal ribosome entry site-directed translation
    • Jangra R.K., et al. DDX6 (Rck/p54) is required for efficient hepatitis C virus replication but not for internal ribosome entry site-directed translation. J. Virol. 2010, 84:6810-6824.
    • (2010) J. Virol. , vol.84 , pp. 6810-6824
    • Jangra, R.K.1
  • 88
    • 34548472407 scopus 로고    scopus 로고
    • Lsm proteins bind and stabilize RNAs containing 5' poly(A) tracts
    • Bergman N., et al. Lsm proteins bind and stabilize RNAs containing 5' poly(A) tracts. Nat. Struct. Mol. Biol. 2007, 14:824-831.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 824-831
    • Bergman, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.