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Volumn 1, Issue 1, 2014, Pages 111-132

Thinking outside the triangle: Replication fidelity of the largest RNA viruses

Author keywords

Coronavirus; Exoribonuclease; Proofreading; Quasispecies; Virus evolution

Indexed keywords

DNA POLYMERASE; EXORIBONUCLEASE; FLUOROURACIL; LIVE VACCINE; RIBAVIRIN; RNA; RNA DIRECTED RNA POLYMERASE; RNA POLYMERASE; VIRUS PROTEIN; VIRUS RNA;

EID: 85016934946     PISSN: 2327056X     EISSN: 23270578     Source Type: Journal    
DOI: 10.1146/annurev-virology-031413-085507     Document Type: Article
Times cited : (95)

References (122)
  • 1
    • 0015133749 scopus 로고
    • Selforganization of matter and the evolution of biological macromolecules
    • Eigen M. 1971. Selforganization of matter and the evolution of biological macromolecules. Naturwissenschaften 58:465-523
    • (1971) Naturwissenschaften , vol.58 , pp. 465-523
    • Eigen, M.1
  • 3
    • 84883774875 scopus 로고    scopus 로고
    • Correlation between mutation rate and genome size in riboviruses: Mutation rate of bacteriophage Qβ
    • Bradwell K, Combe M, Domingo-Calap P, Sanjuán R. 2013. Correlation between mutation rate and genome size in riboviruses: mutation rate of bacteriophage Qβ. Genetics 195:243-51
    • (2013) Genetics , vol.195 , pp. 243-251
    • Bradwell, K.1    Combe, M.2    Domingo-Calap, P.3    Sanjuán, R.4
  • 4
    • 84888011629 scopus 로고    scopus 로고
    • A decade after SARS: Strategies for controlling emerging coronaviruses
    • Graham RL, Donaldson EF, Baric RS. 2013. A decade after SARS: strategies for controlling emerging coronaviruses. Nat. Rev. Microbiol. 11:836-48
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 836-848
    • Graham, R.L.1    Donaldson, E.F.2    Baric, R.S.3
  • 5
    • 84889573658 scopus 로고    scopus 로고
    • Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor
    • Ge XY,Li JL, Yang XL,Chmura AA, ZhuG, et al. 2013. Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor. Nature 503:535-38
    • (2013) Nature , vol.503 , pp. 535-538
    • Ge, X.Y.1    Li, J.L.2    Yang, X.L.3    Chmura, A.A.4    Zhu, G.5
  • 6
    • 84869225041 scopus 로고    scopus 로고
    • Evidence supporting a zoonotic origin of human coronavirus strain NL63
    • Huynh J, Li S, Yount B, Smith A, Sturges L, et al. 2012. Evidence supporting a zoonotic origin of human coronavirus strain NL63. J. Virol. 86:12816-25
    • (2012) J. Virol. , vol.86 , pp. 12816-12825
    • Huynh, J.1    Li, S.2    Yount, B.3    Smith, A.4    Sturges, L.5
  • 7
    • 70249102165 scopus 로고    scopus 로고
    • Distant relatives of severe acute respiratory syndrome coronavirus and close relatives of human coronavirus 229E in bats, Ghana
    • Pfefferle S, Oppong S, Drexler JF, Gloza-Rausch F, Ipsen A, et al. 2009. Distant relatives of severe acute respiratory syndrome coronavirus and close relatives of human coronavirus 229E in bats, Ghana. Emerg. Infect. Dis. 15:1377-84
    • (2009) Emerg. Infect. Dis. , vol.15 , pp. 1377-1384
    • Pfefferle, S.1    Oppong, S.2    Drexler, J.F.3    Gloza-Rausch, F.4    Ipsen, A.5
  • 8
    • 84871866829 scopus 로고    scopus 로고
    • Identification and characterization of a novel alpaca respiratory coronavirus most closely related to the human coronavirus 229E
    • Crossley BM, Mock RE, Callison SA, Hietala SK. 2012. Identification and characterization of a novel alpaca respiratory coronavirus most closely related to the human coronavirus 229E. Viruses 4:3689-700
    • (2012) Viruses , vol.4 , pp. 3689-3700
    • Crossley, B.M.1    Mock, R.E.2    Callison, S.A.3    Hietala, S.K.4
  • 9
    • 13744252665 scopus 로고    scopus 로고
    • Complete genomic sequence of human coronavirus OC43: Molecular clock analysis suggests a relatively recent zoonotic coronavirus transmission event
    • Vijgen L, Keyaerts E, Moës E, Thoelen I, Wollants E, et al. 2005. Complete genomic sequence of human coronavirus OC43: molecular clock analysis suggests a relatively recent zoonotic coronavirus transmission event. J. Virol. 79:1595-604
    • (2005) J. Virol. , vol.79 , pp. 1595-1604
    • Vijgen, L.1    Keyaerts, E.2    Moës, E.3    Thoelen, I.4    Wollants, E.5
  • 10
    • 26844532049 scopus 로고    scopus 로고
    • Phylogenetic and recombination analysis of coronavirus HKU1, a novel coronavirus from patients with pneumonia
    • Woo PCY, Lau SKP, Huang Y, Tsoi HW, Chan KH, Yuen KY. 2005. Phylogenetic and recombination analysis of coronavirus HKU1, a novel coronavirus from patients with pneumonia. Arch. Virol. 150:2299-311
    • (2005) Arch. Virol. , vol.150 , pp. 2299-2311
    • Woo, P.C.Y.1    Lau, S.K.P.2    Huang, Y.3    Tsoi, H.W.4    Chan, K.H.5    Yuen, K.Y.6
  • 11
    • 0242717589 scopus 로고    scopus 로고
    • Coronavirus as a possible cause of severe acute respiratory syndrome
    • Peiris JSM, Lai ST, Poon LLM, Guan Y, Yam LYC, et al. 2003. Coronavirus as a possible cause of severe acute respiratory syndrome. Lancet 361:1319-25
    • (2003) Lancet , vol.361 , pp. 1319-1325
    • Peiris, J.S.M.1    Lai, S.T.2    Poon, L.L.M.3    Guan, Y.4    Yam, L.Y.C.5
  • 13
    • 70349669409 scopus 로고    scopus 로고
    • Coronavirus diversity, phylogeny and interspecies jumping
    • Woo PCY, Lau SKP, Huang Y, Yuen KY. 2009. Coronavirus diversity, phylogeny and interspecies jumping. Exp. Biol. Med. 234:1117-27
    • (2009) Exp. Biol. Med. , vol.234 , pp. 1117-1127
    • Woo, P.C.Y.1    Lau, S.K.P.2    Huang, Y.3    Yuen, K.Y.4
  • 14
    • 84888115990 scopus 로고    scopus 로고
    • Ecology, evolution and classification of bat coronaviruses in the aftermath of SARS
    • Drexler JF, Corman VM, Drosten C. 2013. Ecology, evolution and classification of bat coronaviruses in the aftermath of SARS. Antivir. Res. 101:45-56
    • (2013) Antivir. Res. , vol.101 , pp. 45-56
    • Drexler, J.F.1    Corman, V.M.2    Drosten, C.3
  • 17
    • 84884515347 scopus 로고    scopus 로고
    • From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses
    • Hilgenfeld R, Peiris M. 2013. From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses. Antivir. Res. 100:286-95
    • (2013) Antivir. Res. , vol.100 , pp. 286-295
    • Hilgenfeld, R.1    Peiris, M.2
  • 19
    • 84899641194 scopus 로고    scopus 로고
    • Middle East respiratory syndrome coronavirus infection in dromedary camels in Saudi Arabia
    • Alagaili AN, Briese T,MishraN, Kapoor V, Sameroff SC, et al. 2014. Middle East respiratory syndrome coronavirus infection in dromedary camels in Saudi Arabia. mBio 5:e00884-14
    • (2014) MBio , vol.5 , pp. e00884-e00914
    • Alagaili, A.N.1    Briese, T.2    Mishra, N.3    Kapoor, V.4    Sameroff, S.C.5
  • 20
    • 84890433761 scopus 로고    scopus 로고
    • Middle East respiratory syndrome coronavirus: Quantification of the extent of the epidemic, surveillance biases, and transmissibility
    • Cauchemez S, Fraser C, Van Kerkhove MD, Donnelly CA, Riley S, et al. 2014. Middle East respiratory syndrome coronavirus: quantification of the extent of the epidemic, surveillance biases, and transmissibility. Lancet Infect. Dis. 14:50-56
    • (2014) Lancet Infect. Dis. , vol.14 , pp. 50-56
    • Cauchemez, S.1    Fraser, C.2    Van Kerkhove, M.D.3    Donnelly, C.A.4    Riley, S.5
  • 21
    • 84882918127 scopus 로고    scopus 로고
    • Interhuman transmissibility of Middle East respiratory syndrome coronavirus: Estimation of pandemic risk
    • Breban R, Riou J, Fontanet A. 2013. Interhuman transmissibility of Middle East respiratory syndrome coronavirus: estimation of pandemic risk. Lancet 382:694-99
    • (2013) Lancet , vol.382 , pp. 694-699
    • Breban, R.1    Riou, J.2    Fontanet, A.3
  • 22
    • 67349158649 scopus 로고    scopus 로고
    • Coronaviruses post-SARS: Update on replication and pathogenesis
    • Perlman S, Netland J. 2009. Coronaviruses post-SARS: update on replication and pathogenesis. Nat. Rev. Microbiol. 7:439-50
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 439-450
    • Perlman, S.1    Netland, J.2
  • 23
    • 0023512767 scopus 로고
    • An efficient ribosomal frameshifting signal in the polymerase-encoding region of the coronavirus IBV
    • Brierley I, Boursnell ME, Binns MM, Bilimoria B, Blok VC, et al. 1987. An efficient ribosomal frameshifting signal in the polymerase-encoding region of the coronavirus IBV. EMBO J. 6:3779-85
    • (1987) EMBO J. , vol.6 , pp. 3779-3785
    • Brierley, I.1    Boursnell, M.E.2    Binns, M.M.3    Bilimoria, B.4    Blok, V.C.5
  • 25
    • 0042164218 scopus 로고    scopus 로고
    • Unique and conserved features of genome and proteome of SARS-coronavirus, an early split-off from the coronavirus group 2 lineage
    • Snijder EJ, Bredenbeek PJ, Dobbe JC, Thiel V, Ziebuhr J, et al. 2003. Unique and conserved features of genome and proteome of SARS-coronavirus, an early split-off from the coronavirus group 2 lineage. J. Mol. Biol. 331:991-1004
    • (2003) J. Mol. Biol. , vol.331 , pp. 991-1004
    • Snijder, E.J.1    Bredenbeek, P.J.2    Dobbe, J.C.3    Thiel, V.4    Ziebuhr, J.5
  • 26
    • 0034072633 scopus 로고    scopus 로고
    • Virus-encoded proteinases and proteolytic processing in the Nidovirales
    • Ziebuhr J, Snijder EJ, Gorbalenya AE. 2000. Virus-encoded proteinases and proteolytic processing in the Nidovirales. J. Gen. Virol. 81:853-79
    • (2000) J. Gen. Virol. , vol.81 , pp. 853-879
    • Ziebuhr, J.1    Snijder, E.J.2    Gorbalenya, A.E.3
  • 27
    • 77955462625 scopus 로고    scopus 로고
    • Subgenomic messenger RNA amplification in coronaviruses
    • Wu HY, Brian DA. 2010. Subgenomic messenger RNA amplification in coronaviruses. Proc. Natl. Acad. Sci. USA 107:12257-62
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 12257-12262
    • Wu, H.Y.1    Brian, D.A.2
  • 28
    • 33750218147 scopus 로고    scopus 로고
    • A second, non-canonical RNAdependent RNA polymerase in SARS coronavirus
    • Imbert I, Guillemot JC, Bourhis JM, Bussetta C, Coutard B, et al. 2006. A second, non-canonical RNAdependent RNA polymerase in SARS coronavirus. EMBO J. 25:4933-42
    • (2006) EMBO J. , vol.25 , pp. 4933-4942
    • Imbert, I.1    Guillemot, J.C.2    Bourhis, J.M.3    Bussetta, C.4    Coutard, B.5
  • 29
    • 84857837587 scopus 로고    scopus 로고
    • The SARS-coronavirus nsp7+nsp8 complex is a unique multimeric RNA polymerase capable of both de novo initiation and primer extension
    • te Velthuis AJW, van denWorm SHE, Snijder EJ. 2012. The SARS-coronavirus nsp7+nsp8 complex is a unique multimeric RNA polymerase capable of both de novo initiation and primer extension. Nucleic Acids Res. 40:1737-47
    • (2012) Nucleic Acids Res. , vol.40 , pp. 1737-1747
    • Te Velthuis, A.J.W.1    Van Den Worm, S.H.E.2    Snijder, E.J.3
  • 31
    • 17444431570 scopus 로고    scopus 로고
    • Expression, purification, and characterization of SARS coronavirus RNA polymerase
    • Cheng A, Zhang W, Xie Y, JiangW, Arnold E, et al. 2005. Expression, purification, and characterization of SARS coronavirus RNA polymerase. Virology 335:165-76
    • (2005) Virology , vol.335 , pp. 165-176
    • Cheng, A.1    Zhang, W.2    Xie, Y.3    Jiang, W.4    Arnold, E.5
  • 32
    • 84868492015 scopus 로고    scopus 로고
    • Biochemical characterization of a recombinant SARS coronavirus nsp12 RNA-dependent RNA polymerase capable of copying viral RNA templates
    • Ahn DG, Choi JK, Taylor DR, Oh JW. 2012. Biochemical characterization of a recombinant SARS coronavirus nsp12 RNA-dependent RNA polymerase capable of copying viral RNA templates. Arch. Virol. 157:2095-104
    • (2012) Arch. Virol. , vol.157 , pp. 2095-2104
    • Ahn, D.G.1    Choi, J.K.2    Taylor, D.R.3    Oh, J.W.4
  • 33
    • 0033941814 scopus 로고    scopus 로고
    • The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5'-to-3' polarity
    • Seybert A, Hegyi A, Siddell SG, Ziebuhr J. 2000. The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5'-to-3' polarity. RNA 6:1056-68
    • (2000) RNA , vol.6 , pp. 1056-1068
    • Seybert, A.1    Hegyi, A.2    Siddell, S.G.3    Ziebuhr, J.4
  • 34
    • 3142689813 scopus 로고    scopus 로고
    • Human coronavirus 229E nonstructural protein 13: Characterization of duplex-unwinding, nucleoside triphosphatase, and RNA 5'-triphosphatase activities
    • Ivanov KA, Ziebuhr J. 2004. Human coronavirus 229E nonstructural protein 13: characterization of duplex-unwinding, nucleoside triphosphatase, and RNA 5'-triphosphatase activities. J. Virol. 78:7833-38
    • (2004) J. Virol. , vol.78 , pp. 7833-7838
    • Ivanov, K.A.1    Ziebuhr, J.2
  • 35
    • 62549159638 scopus 로고    scopus 로고
    • Functional screen reveals SARS coronavirus nonstructural protein nsp14 as a novel cap N7 methyltransferase
    • Chen Y, Cai H, Pan J, Xiang N, Tien P, et al. 2009. Functional screen reveals SARS coronavirus nonstructural protein nsp14 as a novel cap N7 methyltransferase. Proc. Natl. Acad. Sci. USA 106:3484-89
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3484-3489
    • Chen, Y.1    Cai, H.2    Pan, J.3    Xiang, N.4    Tien, P.5
  • 36
    • 33645518839 scopus 로고    scopus 로고
    • Discovery of an RNA virus 3'→5' exoribonuclease that is critically involved in coronavirus RNA synthesis
    • Minskaia E, Hertzig T, Gorbalenya AE, Campanacci V, Cambillau C, et al. 2006. Discovery of an RNA virus 3'→5' exoribonuclease that is critically involved in coronavirus RNA synthesis. Proc. Natl. Acad. Sci. USA 103:5108-13
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 5108-5113
    • Minskaia, E.1    Hertzig, T.2    Gorbalenya, A.E.3    Campanacci, V.4    Cambillau, C.5
  • 38
    • 47749138964 scopus 로고    scopus 로고
    • Coronavirus nonstructural protein 16 is a cap-0 binding enzyme possessing (nucleoside-2'O)-methyltransferase activity
    • Decroly E, Imbert I, Coutard B, Bouvet M, Selisko B, et al. 2008. Coronavirus nonstructural protein 16 is a cap-0 binding enzyme possessing (nucleoside-2'O)-methyltransferase activity. J. Virol. 82:8071-84
    • (2008) J. Virol. , vol.82 , pp. 8071-8084
    • Decroly, E.1    Imbert, I.2    Coutard, B.3    Bouvet, M.4    Selisko, B.5
  • 39
    • 33645000761 scopus 로고    scopus 로고
    • Insights into SARS-CoV transcription and replication from the structure of the nsp7-nsp8 hexadecamer
    • Zhai Y, Sun F, Li X, Pang H, Xu X, et al. 2005. Insights into SARS-CoV transcription and replication from the structure of the nsp7-nsp8 hexadecamer. Nat. Struct. Mol. Biol. 12:980-86
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 980-986
    • Zhai, Y.1    Sun, F.2    Li, X.3    Pang, H.4    Xu, X.5
  • 40
    • 34249940286 scopus 로고    scopus 로고
    • Murine hepatitis virus replicase protein nsp10 is a critical regulator of viral RNA synthesis
    • Donaldson EF, Sims AC, Graham RL, Denison MR, Baric RS. 2007. Murine hepatitis virus replicase protein nsp10 is a critical regulator of viral RNA synthesis. J. Virol. 81:6356-68
    • (2007) J. Virol. , vol.81 , pp. 6356-6368
    • Donaldson, E.F.1    Sims, A.C.2    Graham, R.L.3    Denison, M.R.4    Baric, R.S.5
  • 42
    • 84862203582 scopus 로고    scopus 로고
    • RNA 3'-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex
    • Bouvet M, Imbert I, Subissi L, Gluais L, Canard B, Decroly E. 2012. RNA 3'-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex. Proc. Natl. Acad. Sci. USA 109:9372-77
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 9372-9377
    • Bouvet, M.1    Imbert, I.2    Subissi, L.3    Gluais, L.4    Canard, B.5    Decroly, E.6
  • 43
    • 79958067824 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the SARS-coronavirus RNA cap 2'-O-methyltransferase nsp10/nsp16 complex
    • Decroly E, Debarnot C, Ferron F, Bouvet M, Coutard B, et al. 2011. Crystal structure and functional analysis of the SARS-coronavirus RNA cap 2'-O-methyltransferase nsp10/nsp16 complex. PLoS Pathog. 7:e1002059
    • (2011) PLoS Pathog. , vol.7 , pp. e1002059
    • Decroly, E.1    Debarnot, C.2    Ferron, F.3    Bouvet, M.4    Coutard, B.5
  • 44
    • 80055066817 scopus 로고    scopus 로고
    • Biochemical and structural insights into the mechanisms of SARS coronavirus RNA ribose 2'-O-methylation by nsp16/nsp10 protein complex
    • Chen Y, Su C, Ke M, Jin X, Xu L, et al. 2011. Biochemical and structural insights into the mechanisms of SARS coronavirus RNA ribose 2'-O-methylation by nsp16/nsp10 protein complex. PLoS Pathog. 7:e1002294
    • (2011) PLoS Pathog. , vol.7 , pp. e1002294
    • Chen, Y.1    Su, C.2    Ke, M.3    Jin, X.4    Xu, L.5
  • 45
    • 0346888670 scopus 로고    scopus 로고
    • Molecular model of SARS coronavirus polymerase: Implications for biochemical functions and drug design
    • Xu X, Liu Y, Weiss S, Arnold E, Sarafianos SG, Ding J. 2003. Molecular model of SARS coronavirus polymerase: implications for biochemical functions and drug design. Nucleic Acids Res. 31:7117-30
    • (2003) Nucleic Acids Res. , vol.31 , pp. 7117-7130
    • Xu, X.1    Liu, Y.2    Weiss, S.3    Arnold, E.4    Sarafianos, S.G.5    Ding, J.6
  • 46
    • 0036434498 scopus 로고    scopus 로고
    • The palm subdomain-based active site is internally permuted in viral RNA-dependent RNA polymerases of an ancient lineage
    • Gorbalenya AE, Pringle FM, Zeddam JL, Luke BT, Cameron CE, et al. 2002. The palm subdomain-based active site is internally permuted in viral RNA-dependent RNA polymerases of an ancient lineage. J. Mol. Biol. 324:47-62
    • (2002) J. Mol. Biol. , vol.324 , pp. 47-62
    • Gorbalenya, A.E.1    Pringle, F.M.2    Zeddam, J.L.3    Luke, B.T.4    Cameron, C.E.5
  • 47
    • 84866930664 scopus 로고    scopus 로고
    • DNA replication fidelity in Escherichia coli: A multi-DNA polymerase affair
    • Fijalkowska IJ, Schaaper RM, Jonczyk P. 2012. DNA replication fidelity in Escherichia coli: a multi-DNA polymerase affair. FEMS Microbiol. Rev. 36:1105-21
    • (2012) FEMS Microbiol. Rev. , vol.36 , pp. 1105-1121
    • Fijalkowska, I.J.1    Schaaper, R.M.2    Jonczyk, P.3
  • 49
    • 2342419732 scopus 로고    scopus 로고
    • DNA replication fidelity
    • Kunkel TA. 2004. DNA replication fidelity. J. Biol. Chem. 279:16895-98
    • (2004) J. Biol. Chem. , vol.279 , pp. 16895-16898
    • Kunkel, T.A.1
  • 50
    • 0025886466 scopus 로고
    • A constant rate of spontaneous mutation in DNA-based microbes
    • Drake JW. 1991. A constant rate of spontaneous mutation in DNA-based microbes. Proc. Natl. Acad. Sci. USA 88:7160-64
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7160-7164
    • Drake, J.W.1
  • 52
    • 1642588255 scopus 로고    scopus 로고
    • Structures of mismatch replication errors observed in a DNA polymerase
    • Johnson SJ, Beese LS. 2004. Structures of mismatch replication errors observed in a DNA polymerase. Cell 116:803-16
    • (2004) Cell , vol.116 , pp. 803-816
    • Johnson, S.J.1    Beese, L.S.2
  • 53
    • 33746312883 scopus 로고    scopus 로고
    • Remarkable sensitivity to DNA base shape in the DNA polymerase active site
    • Sintim HO, Kool ET. 2006. Remarkable sensitivity to DNA base shape in the DNA polymerase active site. Angew. Chem. Int. Ed. Engl. 45:1974-79
    • (2006) Angew. Chem. Int. Ed. Engl. , vol.45 , pp. 1974-1979
    • Sintim, H.O.1    Kool, E.T.2
  • 54
    • 0035369086 scopus 로고    scopus 로고
    • Structure of the replicating complex of a pol α family DNA polymerase
    • Franklin MC, Wang J, Steitz TA. 2001. Structure of the replicating complex of a pol α family DNA polymerase. Cell 105:657-67
    • (2001) Cell , vol.105 , pp. 657-667
    • Franklin, M.C.1    Wang, J.2    Steitz, T.A.3
  • 55
    • 11844283982 scopus 로고    scopus 로고
    • Incorporation fidelity of the viral RNA-dependent RNA polymerase: A kinetic, thermodynamic and structural perspective
    • Castro C, Arnold JJ, Cameron CE. 2005. Incorporation fidelity of the viral RNA-dependent RNA polymerase: a kinetic, thermodynamic and structural perspective. Virus Res. 107:141-49
    • (2005) Virus Res. , vol.107 , pp. 141-149
    • Castro, C.1    Arnold, J.J.2    Cameron, C.E.3
  • 56
    • 70549114081 scopus 로고    scopus 로고
    • Dynamics: The missing link between structure and function of the viral RNA-dependent RNA polymerase?
    • Cameron CE, Moustafa IM, Arnold JJ. 2009. Dynamics: the missing link between structure and function of the viral RNA-dependent RNA polymerase? Curr. Opin. Struct. Biol. 19:768-74
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 768-774
    • Cameron, C.E.1    Moustafa, I.M.2    Arnold, J.J.3
  • 57
    • 79958744018 scopus 로고    scopus 로고
    • Molecular dynamics simulations of viral RNA polymerases link conserved and correlated motions of functional elements to fidelity
    • Moustafa IM, Shen H, Morton B, Colina CM, Cameron CE. 2011. Molecular dynamics simulations of viral RNA polymerases link conserved and correlated motions of functional elements to fidelity. J. Mol. Biol. 410:159-81
    • (2011) J. Mol. Biol. , vol.410 , pp. 159-181
    • Moustafa, I.M.1    Shen, H.2    Morton, B.3    Colina, C.M.4    Cameron, C.E.5
  • 58
    • 84865768433 scopus 로고    scopus 로고
    • Motif D of viral RNAdependentRNApolymerases determines efficiency and fidelity of nucleotide addition
    • Yang X, Smidansky ED, Maksimchuk KR, Lum D, Welch JL, et al. 2012. Motif D of viral RNAdependentRNApolymerases determines efficiency and fidelity of nucleotide addition. Structure 20:1519-27
    • (2012) Structure , vol.20 , pp. 1519-1527
    • Yang, X.1    Smidansky, E.D.2    Maksimchuk, K.R.3    Lum, D.4    Welch, J.L.5
  • 59
    • 0027064537 scopus 로고
    • Lack of evidence for proofreadingmechanisms associated with an RNA virus polymerase
    • Steinhauer DA, Domingo E,Holland JJ. 1992. Lack of evidence for proofreadingmechanisms associated with an RNA virus polymerase. Gene 122:281-88
    • (1992) Gene , vol.122 , pp. 281-288
    • Steinhauer, D.A.1    Domingo, E.2    Holland, J.J.3
  • 61
    • 0026004621 scopus 로고
    • Eukaryotic DNA polymerase amino acid sequence required for 3'→5' exonuclease activity
    • Morrison A, Bell JB, Kunkel TA, Sugino A. 1991. Eukaryotic DNA polymerase amino acid sequence required for 3'→5' exonuclease activity. Proc. Natl. Acad. Sci. USA 88:9473-77
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9473-9477
    • Morrison, A.1    Bell, J.B.2    Kunkel, T.A.3    Sugino, A.4
  • 62
    • 0024437947 scopus 로고
    • The extreme mutator effect of Escherichia coli mutD5 results from saturation of mismatch repair by excessive DNA replication errors
    • Schaaper RM, Radman M. 1989. The extreme mutator effect of Escherichia coli mutD5 results from saturation of mismatch repair by excessive DNA replication errors. EMBO J. 8:3511-16
    • (1989) EMBO J. , vol.8 , pp. 3511-3516
    • Schaaper, R.M.1    Radman, M.2
  • 63
    • 38049125552 scopus 로고    scopus 로고
    • The fidelity ofDNAsynthesis by eukaryotic replicative and translesion synthesis polymerases
    • McCulloch SD,KunkelTA. 2008. The fidelity ofDNAsynthesis by eukaryotic replicative and translesion synthesis polymerases. Cell Res. 18:148-61
    • (2008) Cell Res. , vol.18 , pp. 148-161
    • McCulloch, S.D.1    Kunkel, T.A.2
  • 64
    • 2442584664 scopus 로고    scopus 로고
    • Poliovirus RNA-dependent RNA polymerase (3Dpol): Pre-steady-state kinetic analysis of ribonucleotide incorporation in the presence of Mg2+
    • Arnold JJ, Cameron CE. 2004. Poliovirus RNA-dependent RNA polymerase (3Dpol): pre-steady-state kinetic analysis of ribonucleotide incorporation in the presence of Mg2+. Biochemistry 43:5126-37
    • (2004) Biochemistry , vol.43 , pp. 5126-5137
    • Arnold, J.J.1    Cameron, C.E.2
  • 66
    • 84883438898 scopus 로고    scopus 로고
    • Coronaviruses lacking exoribonuclease activity are susceptible to lethal mutagenesis: Evidence for proofreading and potential therapeutics
    • Smith EC, Blanc H, Vignuzzi M, Denison MR. 2013. Coronaviruses lacking exoribonuclease activity are susceptible to lethal mutagenesis: evidence for proofreading and potential therapeutics. PLoS Pathog. 9:e1003565
    • (2013) PLoS Pathog. , vol.9 , pp. e1003565
    • Smith, E.C.1    Blanc, H.2    Vignuzzi, M.3    Denison, M.R.4
  • 67
    • 36048969246 scopus 로고    scopus 로고
    • High fidelity of murine hepatitis virus replication is decreased in nsp14 exoribonuclease mutants
    • Eckerle LD, Lu X, Sperry SM, Choi L, Denison MR. 2007. High fidelity of murine hepatitis virus replication is decreased in nsp14 exoribonuclease mutants. J. Virol. 81:12135-44
    • (2007) J. Virol. , vol.81 , pp. 12135-12144
    • Eckerle, L.D.1    Lu, X.2    Sperry, S.M.3    Choi, L.4    Denison, M.R.5
  • 68
    • 77954055072 scopus 로고    scopus 로고
    • Infidelity of SARS-CoV nsp14-exonuclease mutant virus replication is revealed by complete genome sequencing
    • Eckerle LD, Becker MM, Halpin RA, Li K, Venter E, et al. 2010. Infidelity of SARS-CoV nsp14-exonuclease mutant virus replication is revealed by complete genome sequencing. PLoS Pathog. 6:e1000896
    • (2010) PLoS Pathog. , vol.6 , pp. e1000896
    • Eckerle, L.D.1    Becker, M.M.2    Halpin, R.A.3    Li, K.4    Venter, E.5
  • 69
    • 84870946428 scopus 로고    scopus 로고
    • A live, impairedfidelity coronavirus vaccine protects in an aged, immunocompromised mouse model of lethal disease
    • Graham RL, Becker MM, Eckerle LD, BollesM, Denison MR, Baric RS. 2012. A live, impairedfidelity coronavirus vaccine protects in an aged, immunocompromised mouse model of lethal disease. Nat. Med. 18:1820-26
    • (2012) Nat. Med. , vol.18 , pp. 1820-1826
    • Graham, R.L.1    Becker, M.M.2    Eckerle, L.D.3    Bolles, M.4    Denison, M.R.5    Baric, R.S.6
  • 70
    • 84857371051 scopus 로고    scopus 로고
    • Metagenomics and future perspectives in virus discovery
    • Mokili JL, Rohwer F, Dutilh BE. 2012. Metagenomics and future perspectives in virus discovery. Curr. Opin. Virol. 2:63-77
    • (2012) Curr. Opin. Virol. , vol.2 , pp. 63-77
    • Mokili, J.L.1    Rohwer, F.2    Dutilh, B.E.3
  • 71
    • 77957658175 scopus 로고    scopus 로고
    • Quasispecies theory and the behavior of RNA viruses
    • Lauring AS, Andino R. 2010. Quasispecies theory and the behavior of RNA viruses. PLoS Pathog. 6:e1001005
    • (2010) PLoS Pathog. , vol.6 , pp. e1001005
    • Lauring, A.S.1    Andino, R.2
  • 73
    • 81555214151 scopus 로고    scopus 로고
    • Quasispecies as a matter of fact: Viruses and beyond
    • Ojosnegros S, Perales C,Mas A, Domingo E. 2011. Quasispecies as a matter of fact: viruses and beyond. Virus Res. 162:203-15
    • (2011) Virus Res. , vol.162 , pp. 203-215
    • Ojosnegros, S.1    Perales, C.2    Mas, A.3    Domingo, E.4
  • 74
    • 31144465690 scopus 로고    scopus 로고
    • Quasispecies diversity determines pathogenesis through cooperative interactions in a viral population
    • Vignuzzi M, Stone JK, Arnold JJ, Cameron CE, Andino R. 2006. Quasispecies diversity determines pathogenesis through cooperative interactions in a viral population. Nature 439:344-48
    • (2006) Nature , vol.439 , pp. 344-348
    • Vignuzzi, M.1    Stone, J.K.2    Arnold, J.J.3    Cameron, C.E.4    Andino, R.5
  • 75
    • 84876406925 scopus 로고    scopus 로고
    • The role of mutational robustness in RNA virus evolution
    • Lauring AS, Frydman J, Andino R. 2013. The role of mutational robustness in RNA virus evolution. Nat. Rev. Microbiol. 11:327-36
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 327-336
    • Lauring, A.S.1    Frydman, J.2    Andino, R.3
  • 78
    • 24644465004 scopus 로고    scopus 로고
    • Adaptive value of high mutation rates of RNA viruses: Separating causes from consequences
    • Elena SF, Sanjuán R. 2005. Adaptive value of high mutation rates of RNA viruses: separating causes from consequences. J. Virol. 79:11555-58
    • (2005) J. Virol. , vol.79 , pp. 11555-11558
    • Elena, S.F.1    Sanjuán, R.2
  • 79
    • 0030952877 scopus 로고    scopus 로고
    • Negative effects of chemical mutagenesis on the adaptive behavior of vesicular stomatitis virus
    • Lee CH, Gilbertson DL, Novella IS, Huerta R, Domingo E, Holland JJ. 1997. Negative effects of chemical mutagenesis on the adaptive behavior of vesicular stomatitis virus. J. Virol. 71:3636-40
    • (1997) J. Virol. , vol.71 , pp. 3636-3640
    • Lee, C.H.1    Gilbertson, D.L.2    Novella, I.S.3    Huerta, R.4    Domingo, E.5    Holland, J.J.6
  • 80
    • 33745490138 scopus 로고    scopus 로고
    • Increased fidelity reduces poliovirus fitness and virulence under selective pressure in mice
    • Pfeiffer JK, KirkegaardK. 2005. Increased fidelity reduces poliovirus fitness and virulence under selective pressure in mice. PLoS Pathog. 1:e11
    • (2005) PLoS Pathog. , vol.1 , pp. e11
    • Pfeiffer, J.K.1    Kirkegaard, K.2
  • 81
    • 38949184924 scopus 로고    scopus 로고
    • Engineering attenuated virus vaccines by controlling replication fidelity
    • Vignuzzi M, Wendt E, Andino R. 2008. Engineering attenuated virus vaccines by controlling replication fidelity. Nat. Med. 14:154-61
    • (2008) Nat. Med. , vol.14 , pp. 154-161
    • Vignuzzi, M.1    Wendt, E.2    Andino, R.3
  • 82
    • 84869854859 scopus 로고    scopus 로고
    • Viral mutation rates: Modelling the roles of within-host viral dynamics and the trade-off between replication fidelity and speed
    • Regoes RR, Hamblin S, Tanaka MM. 2013. Viral mutation rates: modelling the roles of within-host viral dynamics and the trade-off between replication fidelity and speed. Proc. R. Soc. B 280:20122047
    • (2013) Proc. R. Soc. B , vol.280 , pp. 20122047
    • Regoes, R.R.1    Hamblin, S.2    Tanaka, M.M.3
  • 83
    • 0031894341 scopus 로고    scopus 로고
    • Antimutator mutants in bacteriophage T4 and Escherichia coli
    • Schaaper RM. 1998. Antimutator mutants in bacteriophage T4 and Escherichia coli. Genetics 148:1579-85
    • (1998) Genetics , vol.148 , pp. 1579-1585
    • Schaaper, R.M.1
  • 84
    • 0015524064 scopus 로고
    • Studies on the biochemical basis of spontaneous mutation. I. A comparison of the deoxyribonucleic acid polymerases of mutator, antimutator, and wild type strains of bacteriophage T4
    • MuzyczkaN, Poland RL, BessmanMJ. 1972. Studies on the biochemical basis of spontaneous mutation. I. A comparison of the deoxyribonucleic acid polymerases of mutator, antimutator, and wild type strains of bacteriophage T4. J. Biol. Chem. 247:7116-22
    • (1972) J. Biol. Chem. , vol.247 , pp. 7116-7122
    • Muzyczka, N.1    Poland, R.L.2    Bessman, M.J.3
  • 85
    • 0017137313 scopus 로고
    • Control of mutation frequency by bacteriophage T4 DNA polymerase. I. The CB120 antimutator DNA polymerase is defective in strand displacement
    • Gillin FD, Nossal NG. 1976. Control of mutation frequency by bacteriophage T4 DNA polymerase. I. The CB120 antimutator DNA polymerase is defective in strand displacement. J. Biol. Chem. 251:5219-24
    • (1976) J. Biol. Chem. , vol.251 , pp. 5219-5224
    • Gillin, F.D.1    Nossal, N.G.2
  • 86
    • 0038809107 scopus 로고    scopus 로고
    • A single mutation in poliovirus RNA-dependent RNA polymerase confers resistance to mutagenic nucleotide analogs via increased fidelity
    • Pfeiffer JK, Kirkegaard K. 2003. A single mutation in poliovirus RNA-dependent RNA polymerase confers resistance to mutagenic nucleotide analogs via increased fidelity. Proc. Natl. Acad. Sci. USA 100:7289-94
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7289-7294
    • Pfeiffer, J.K.1    Kirkegaard, K.2
  • 89
    • 21844431621 scopus 로고    scopus 로고
    • Remote site control of an active site fidelity checkpoint in a viral RNA-dependent RNA polymerase
    • Arnold JJ, Vignuzzi M, Stone JK, Andino R, Cameron CE. 2005. Remote site control of an active site fidelity checkpoint in a viral RNA-dependent RNA polymerase. J. Biol. Chem. 280:25706-16
    • (2005) J. Biol. Chem. , vol.280 , pp. 25706-25716
    • Arnold, J.J.1    Vignuzzi, M.2    Stone, J.K.3    Andino, R.4    Cameron, C.E.5
  • 90
    • 84893756804 scopus 로고    scopus 로고
    • Alphavirus mutator variants present host-specific defects and attenuation in mammalian and insect models
    • Rozen-Gagnon K, Stapleford KA, Mongelli V, Blanc H, Failloux AB, et al. 2014. Alphavirus mutator variants present host-specific defects and attenuation in mammalian and insect models. PLoS Pathog. 10:e1003877
    • (2014) PLoS Pathog. , vol.10 , pp. e1003877
    • Rozen-Gagnon, K.1    Stapleford, K.A.2    Mongelli, V.3    Blanc, H.4    Failloux, A.B.5
  • 91
    • 84881162575 scopus 로고    scopus 로고
    • An increased replication fidelity mutant of foot-and-mouth disease virus retains fitness in vitro and virulence in vivo
    • Zeng J, Wang H, Xie X, Yang D, Zhou G, Yu L. 2013. An increased replication fidelity mutant of foot-and-mouth disease virus retains fitness in vitro and virulence in vivo. Antivir. Res. 100:1-7
    • (2013) Antivir. Res. , vol.100 , pp. 1-7
    • Zeng, J.1    Wang, H.2    Xie, X.3    Yang, D.4    Zhou, G.5    Yu, L.6
  • 92
    • 84896904367 scopus 로고    scopus 로고
    • Ribavirin-resistant variants of foot-and-mouth disease virus: The effect of restricted quasispecies diversity on viral virulence
    • Zeng J, Wang H, Xie X, Li C, Zhou G, et al. 2014. Ribavirin-resistant variants of foot-and-mouth disease virus: the effect of restricted quasispecies diversity on viral virulence. J. Virol. 88:4008-20
    • (2014) J. Virol. , vol.88 , pp. 4008-4020
    • Zeng, J.1    Wang, H.2    Xie, X.3    Li, C.4    Zhou, G.5
  • 93
    • 84887467058 scopus 로고    scopus 로고
    • Vaccine-derived mutation in motif D of poliovirus RNA-dependent RNA polymerase lowers nucleotide incorporation fidelity
    • Liu X, Yang X, Lee CA,Moustafa IM, Smidansky ED, et al. 2013. Vaccine-derived mutation in motif D of poliovirus RNA-dependent RNA polymerase lowers nucleotide incorporation fidelity. J. Biol. Chem. 288:32753-65
    • (2013) J. Biol. Chem. , vol.288 , pp. 32753-32765
    • Liu, X.1    Yang, X.2    Lee, C.A.3    Moustafa, I.M.4    Smidansky, E.D.5
  • 94
    • 84881378030 scopus 로고    scopus 로고
    • A study of the virulence in mice of high copying fidelity variants of human enterovirus 71
    • Sadeghipour S, McMinn PC. 2013. A study of the virulence in mice of high copying fidelity variants of human enterovirus 71. Virus Res. 176:265-72
    • (2013) Virus Res. , vol.176 , pp. 265-272
    • Sadeghipour, S.1    McMinn, P.C.2
  • 95
    • 84873023551 scopus 로고    scopus 로고
    • Ribavirin-resistant mutants of human enterovirus 71 express a high replication fidelity phenotype during growth in cell culture
    • Sadeghipour S, Bek EJ, McMinn PC. 2013. Ribavirin-resistant mutants of human enterovirus 71 express a high replication fidelity phenotype during growth in cell culture. J. Virol. 87:1759-69
    • (2013) J. Virol. , vol.87 , pp. 1759-1769
    • Sadeghipour, S.1    Bek, E.J.2    McMinn, P.C.3
  • 96
    • 84866423000 scopus 로고    scopus 로고
    • A polymerase mechanism-based strategy for viral attenuation and vaccine development
    • Weeks SA, Lee CA, Zhao Y, Smidansky ED, August A, et al. 2012. A polymerase mechanism-based strategy for viral attenuation and vaccine development. J. Biol. Chem. 287:31618-22
    • (2012) J. Biol. Chem. , vol.287 , pp. 31618-31622
    • Weeks, S.A.1    Lee, C.A.2    Zhao, Y.3    Smidansky, E.D.4    August, A.5
  • 97
    • 57349131683 scopus 로고    scopus 로고
    • Determinants of RNAdependent RNA polymerase (in)fidelity revealed by kinetic analysis of the polymerase encoded by a foot-and-mouth disease virus mutant with reduced sensitivity to ribavirin
    • Arias A, Arnold JJ, Sierra M, Smidansky ED, Domingo E, Cameron CE. 2008. Determinants of RNAdependent RNA polymerase (in)fidelity revealed by kinetic analysis of the polymerase encoded by a foot-and-mouth disease virus mutant with reduced sensitivity to ribavirin. J. Virol. 82:12346-55
    • (2008) J. Virol. , vol.82 , pp. 12346-12355
    • Arias, A.1    Arnold, J.J.2    Sierra, M.3    Smidansky, E.D.4    Domingo, E.5    Cameron, C.E.6
  • 98
    • 78449244303 scopus 로고    scopus 로고
    • Fidelity variants of RNA dependent RNA polymerases uncover an indirect, mutagenic activity of amiloride compounds
    • Levi LI, Gnädig NF, Beaucourt S, McPherson MJ, Baron B, et al. 2010. Fidelity variants of RNA dependent RNA polymerases uncover an indirect, mutagenic activity of amiloride compounds. PLoS Pathog. 6:e1001163
    • (2010) PLoS Pathog. , vol.6 , pp. e1001163
    • Levi, L.I.1    Gnädig, N.F.2    Beaucourt, S.3    McPherson, M.J.4    Baron, B.5
  • 99
    • 33846813925 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus mutant with decreased sensitivity to ribavirin: Implications for error catastrophe
    • Sierra M, Airaksinen A, González-López C, Agudo R, Arias A, Domingo E. 2007. Foot-and-mouth disease virus mutant with decreased sensitivity to ribavirin: implications for error catastrophe. J. Virol. 81:2012-24
    • (2007) J. Virol. , vol.81 , pp. 2012-2024
    • Sierra, M.1    Airaksinen, A.2    González-López, C.3    Agudo, R.4    Arias, A.5    Domingo, E.6
  • 100
    • 80053447519 scopus 로고    scopus 로고
    • Discovery of the first insect nidovirus, a missing evolutionary link in the emergence of the largest RNA virus genomes
    • Nga PT, Parquet MDC, Lauber C, Parida M, Nabeshima T, et al. 2011. Discovery of the first insect nidovirus, a missing evolutionary link in the emergence of the largest RNA virus genomes. PLoS Pathog. 7:e1002215
    • (2011) PLoS Pathog. , vol.7 , pp. e1002215
    • Nga, P.T.1    Parquet, M.D.C.2    Lauber, C.3    Parida, M.4    Nabeshima, T.5
  • 101
    • 84855197858 scopus 로고    scopus 로고
    • An insect nidovirus emerging from a primary tropical rainforest
    • Zirkel F, Kurth A, Quan PL, Briese T, Ellerbrok H, et al. 2011. An insect nidovirus emerging from a primary tropical rainforest. mBio 2:e00077-11
    • (2011) MBio , vol.2 , pp. e00077-11
    • Zirkel, F.1    Kurth, A.2    Quan, P.L.3    Briese, T.4    Ellerbrok, H.5
  • 102
    • 0035283033 scopus 로고    scopus 로고
    • Exoribonuclease superfamilies: Structural analysis and phylogenetic distribution
    • Zuo Y, DeutscherMP. 2001. Exoribonuclease superfamilies: structural analysis and phylogenetic distribution. Nucleic Acids Res. 29:1017-26
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1017-1026
    • Zuo, Y.1    Deutscher, M.P.2
  • 103
    • 84878197216 scopus 로고    scopus 로고
    • Structure-function analysis of severe acute respiratory syndrome coronavirus RNA cap guanine-N7-methyltransferase
    • Chen Y, Tao J, Sun Y, Wu A, Su C, et al. 2013. Structure-function analysis of severe acute respiratory syndrome coronavirus RNA cap guanine-N7-methyltransferase. J. Virol. 87:6296-305
    • (2013) J. Virol. , vol.87 , pp. 6296-6305
    • Chen, Y.1    Tao, J.2    Sun, Y.3    Wu, A.4    Su, C.5
  • 104
    • 84892882211 scopus 로고    scopus 로고
    • Coronaviruses as DNA wannabes: A new model for the regulation of RNA virus replication fidelity
    • Smith EC, Denison MR. 2013. Coronaviruses as DNA wannabes: a new model for the regulation of RNA virus replication fidelity. PLoS Pathog. 9:e1003760
    • (2013) PLoS Pathog. , vol.9 , pp. e1003760
    • Smith, E.C.1    Denison, M.R.2
  • 105
    • 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 KM, Kimberlin CR, Zandonatti MA, MacRae IJ, Saphire EO. 2011. Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3' to 5' exonuclease activity essential for immune suppression. Proc. Natl. Acad. Sci. USA 108:2396-401
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 2396-2401
    • Hastie, K.M.1    Kimberlin, C.R.2    Zandonatti, M.A.3    Macrae, I.J.4    Saphire, E.O.5
  • 106
    • 84855288589 scopus 로고    scopus 로고
    • SARS coronavirus nsp1 protein induces template-dependent endonucleolytic cleavage ofmRNAs: ViralmRNAsare resistant to nsp1-induced RNA cleavage
    • Huang C, Lokugamage KG, Rozovics JM,Narayanan K, Semler BL,Makino S. 2011. SARS coronavirus nsp1 protein induces template-dependent endonucleolytic cleavage ofmRNAs: viralmRNAsare resistant to nsp1-induced RNA cleavage. PLoS Pathog. 7:e1002433
    • (2011) PLoS Pathog. , vol.7 , pp. e1002433
    • Huang, C.1    Lokugamage, K.G.2    Rozovics, J.M.3    Narayanan, K.4    Semler, B.L.5    Makino, S.6
  • 107
    • 79957805839 scopus 로고    scopus 로고
    • Endoribonuclease activities of porcine reproductive and respiratory syndrome virus nsp11 was essential for nsp11 to inhibit IFN-βinduction
    • Shi X, Wang L, Li X, Zhang G, Guo J, et al. 2011. Endoribonuclease activities of porcine reproductive and respiratory syndrome virus nsp11 was essential for nsp11 to inhibit IFN-βinduction. Mol. Immunol. 48:1568-72
    • (2011) Mol. Immunol. , vol.48 , pp. 1568-1572
    • Shi, X.1    Wang, L.2    Li, X.3    Zhang, G.4    Guo, J.5
  • 108
    • 67449088510 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus papain-like protease ubiquitin-like domain and catalytic domain regulate antagonism of IRF3 and NF-κB signaling
    • Frieman M, Ratia K, Johnston RE, Mesecar AD, Baric RS. 2009. Severe acute respiratory syndrome coronavirus papain-like protease ubiquitin-like domain and catalytic domain regulate antagonism of IRF3 and NF-κB signaling. J. Virol. 83:6689-705
    • (2009) J. Virol. , vol.83 , pp. 6689-6705
    • Frieman, M.1    Ratia, K.2    Johnston, R.E.3    Mesecar, A.D.4    Baric, R.S.5
  • 109
    • 25144450882 scopus 로고    scopus 로고
    • Real ribozymes suggest a relaxed error threshold
    • Kun A, Santos M, Szathmáry E. 2005. Real ribozymes suggest a relaxed error threshold. Nat. Genet. 37:1008-11
    • (2005) Nat. Genet. , vol.37 , pp. 1008-1011
    • Kun, A.1    Santos, M.2    Szathmáry, E.3
  • 110
    • 0018785810 scopus 로고
    • Hypercycles and the origin of life
    • Smith JM. 1979. Hypercycles and the origin of life. Nature 280:445-46
    • (1979) Nature , vol.280 , pp. 445-446
    • Smith, J.M.1
  • 111
    • 84884757034 scopus 로고    scopus 로고
    • The footprint of genome architecture in the largest genome expansion in RNA viruses
    • Lauber C, Goeman JJ, Parquet MDC, Nga PT, Snijder EJ, et al. 2013. The footprint of genome architecture in the largest genome expansion in RNA viruses. PLoS Pathog. 9:e1003500
    • (2013) PLoS Pathog. , vol.9 , pp. e1003500
    • Lauber, C.1    Goeman, J.J.2    Parquet, M.D.C.3    Nga, P.T.4    Snijder, E.J.5
  • 112
    • 35148862429 scopus 로고    scopus 로고
    • Analysis of intraviral proteinprotein interactions of the SARS coronavirus ORFeome
    • von Brunn A, Teepe C, Simpson JC, Pepperkok R, Friedel CC, et al. 2007. Analysis of intraviral proteinprotein interactions of the SARS coronavirus ORFeome. PLoS ONE 2:e459
    • (2007) PLoS ONE , vol.2 , pp. e459
    • Von Brunn, A.1    Teepe, C.2    Simpson, J.C.3    Pepperkok, R.4    Friedel, C.C.5
  • 113
    • 53249097514 scopus 로고    scopus 로고
    • Genome-wide analysis of protein-protein interactions and involvement of viral proteins in SARS-CoV replication
    • Pan J, Peng X, Gao Y, Li Z, Lu X, et al. 2008. Genome-wide analysis of protein-protein interactions and involvement of viral proteins in SARS-CoV replication. PLoS ONE 3:e3299
    • (2008) PLoS ONE , vol.3 , pp. e3299
    • Pan, J.1    Peng, X.2    Gao, Y.3    Li, Z.4    Lu, X.5
  • 114
    • 41249103580 scopus 로고    scopus 로고
    • The SARS-coronavirus PLnc domain of nsp3 as a replication/transcription scaffolding protein
    • Imbert I, Snijder EJ, Dimitrova M, Guillemot JC, Lécine P, Canard B. 2008. The SARS-coronavirus PLnc domain of nsp3 as a replication/transcription scaffolding protein. Virus Res. 133:136-48
    • (2008) Virus Res. , vol.133 , pp. 136-148
    • Imbert, I.1    Snijder, E.J.2    Dimitrova, M.3    Guillemot, J.C.4    Lécine, P.5    Canard, B.6
  • 115
    • 84889954808 scopus 로고    scopus 로고
    • SARS-CoV ORF1b-encoded nonstructural proteins 12-16: Replicative enzymes as antiviral targets
    • Subissi L, Imbert I, Ferron F,ColletA,CoutardB, et al. 2013. SARS-CoV ORF1b-encoded nonstructural proteins 12-16: replicative enzymes as antiviral targets. Antivir. Res. 101:122-30
    • (2013) Antivir. Res. , vol.101 , pp. 122-130
    • Subissi, L.1    Imbert, I.2    Ferron, F.3    Collet, A.4    Coutard, B.5
  • 117
    • 0027158172 scopus 로고
    • DNA polymerase III accessory proteins. V. θ encoded by holE
    • Studwell-Vaughan PS, O'Donnell M. 1993. DNA polymerase III accessory proteins. V. θ encoded by holE. J. Biol. Chem. 268:11785-91
    • (1993) J. Biol. Chem. , vol.268 , pp. 11785-11791
    • Studwell-Vaughan, P.S.1    O'donnell, M.2
  • 118
    • 1942539340 scopus 로고    scopus 로고
    • The θ subunit of Escherichia coli DNA polymerase III: A role in stabilizing the ε proofreading subunit
    • Taft-Benz SA, Schaaper RM. 2004. The θ subunit of Escherichia coli DNA polymerase III: a role in stabilizing the ε proofreading subunit. J. Bacteriol. 186:2774-80
    • (2004) J. Bacteriol. , vol.186 , pp. 2774-2780
    • Taft-Benz, S.A.1    Schaaper, R.M.2
  • 119
    • 0035143741 scopus 로고    scopus 로고
    • The RNA structures engaged in replication and transcription of the A59 strain of mouse hepatitis virus
    • Sawicki D, Wang T, Sawicki S. 2001. The RNA structures engaged in replication and transcription of the A59 strain of mouse hepatitis virus. J. Gen. Virol. 82:385-96
    • (2001) J. Gen. Virol. , vol.82 , pp. 385-396
    • Sawicki, D.1    Wang, T.2    Sawicki, S.3
  • 120
    • 77949570096 scopus 로고    scopus 로고
    • Processivity factor of DNA polymerase and its expanding role in normal and translesion DNA synthesis
    • Zhuang Z, Ai Y. 2010. Processivity factor of DNA polymerase and its expanding role in normal and translesion DNA synthesis. Biochim. Biophys. Acta 1804:1081-93
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1081-1093
    • Zhuang, Z.1    Ai, Y.2
  • 121
    • 78751637122 scopus 로고    scopus 로고
    • Ribose 2'-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5
    • Züst R, Cervantes-Barragan L, HabjanM,Maier R, Neuman BW, et al. 2011. Ribose 2'-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5. Nat. Immunol. 12:137-43
    • (2011) Nat. Immunol. , vol.12 , pp. 137-143
    • Züst, R.1    Cervantes-Barragan, L.2    Habjan, M.3    Maier, R.4    Neuman, B.W.5
  • 122
    • 12144287123 scopus 로고    scopus 로고
    • The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world
    • Egloff MP, Ferron F, Campanacci V, Longhi S, Rancurel C, et al. 2004. The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world. Proc. Natl. Acad. Sci. USA 101:3792-96
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3792-3796
    • Egloff, M.P.1    Ferron, F.2    Campanacci, V.3    Longhi, S.4    Rancurel, C.5


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