메뉴 건너뛰기




Volumn 26, Issue , 2018, Pages

Nucleosides for the treatment of respiratory RNA virus infections

Author keywords

antiviral; coronavirus; influenza; nucleoside analog; picornavirus; Respiratory syncytial virus; rhinovirus; RNA dependent RNA polymerase

Indexed keywords

7 DEAZA 2' C METHYLADENOSINE; ANTIVIRUS AGENT; FAVIPIRAVIR; GENOMIC RNA; LUMICITABINE; MK 0608; NITD 008; NUCLEOSIDE ANALOG; OSELTAMIVIR; PALIVIZUMAB; PERAMIVIR; REMDESIVIR; RIBAVIRIN; RNA POLYMERASE; UNCLASSIFIED DRUG; ZANAMIVIR; NUCLEOSIDE;

EID: 85051395653     PISSN: None     EISSN: 20402066     Source Type: Journal    
DOI: 10.1177/2040206618764483     Document Type: Article
Times cited : (112)

References (170)
  • 1
    • 84898723018 scopus 로고    scopus 로고
    • The global burden of respiratory disease
    • and
    • Ferkol T, andSchraufnagel D., The global burden of respiratory disease. Ann Am Thorac Soc 2014; 11: 404–40-6.
    • (2014) Ann Am Thorac Soc , vol.11 , pp. 404-406
    • Ferkol, T.1    Schraufnagel, D.2
  • 2
    • 34247220809 scopus 로고    scopus 로고
    • Structure and classification of viruses
    • Baron S., (ed), 4th ed, Galveston: University of Texas Medical Branch, In:, (ed
    • Gelderblom HR., Structure and classification of viruses. In: Baron S, (ed) Medical microbiology. 4th ed. Galveston: University of Texas Medical Branch, 1996.
    • (1996) Medical microbiology
    • Gelderblom, H.R.1
  • 3
    • 0038617774 scopus 로고    scopus 로고
    • The classification of viruses infecting the respiratory tract
    • Mackie PL., The classification of viruses infecting the respiratory tract. Paediatr Respir Rev 2003; 4: 84–90.
    • (2003) Paediatr Respir Rev , vol.4 , pp. 84-90
    • Mackie, P.L.1
  • 4
    • 85038231779 scopus 로고    scopus 로고
    • Virus detection in critically ill children with acute respiratory disease: a new profile in view of new technology
    • 107: 504–510
    • Kawaguchi A, Bates A, Lee BE. Virus detection in critically ill children with acute respiratory disease: a new profile in view of new technology. Acta Paediatr 2017; 107: 504–510.
    • (2017) Acta Paediatr
    • Kawaguchi, A.1    Bates, A.2    Lee, B.E.3
  • 5
    • 84978162055 scopus 로고    scopus 로고
    • Influenza virus RNA polymerase: insights into the mechanisms of viral RNA synthesis
    • and
    • Te Velthuis AJ, andFodor E., Influenza virus RNA polymerase: insights into the mechanisms of viral RNA synthesis. Nat Rev Microbiol 2016; 14: 479–493.
    • (2016) Nat Rev Microbiol , vol.14 , pp. 479-493
    • Te Velthuis, A.J.1    Fodor, E.2
  • 6
    • 0023190717 scopus 로고
    • Selective inactivation of influenza C esterase: a probe for detecting 9-O-acetylated sialic acids
    • and
    • Muchmore EA, andVarki A., Selective inactivation of influenza C esterase: a probe for detecting 9-O-acetylated sialic acids. Science 1987; 236: 1293–129-5.
    • (1987) Science , vol.236 , pp. 1293-1295
    • Muchmore, E.A.1    Varki, A.2
  • 7
    • 84956710108 scopus 로고    scopus 로고
    • An open receptor-binding cavity of hemagglutinin-esterase-fusion glycoprotein from newly-identified influenza D virus: Basis for its broad cell tropism
    • Song H, Qi J, Khedri Z. An open receptor-binding cavity of hemagglutinin-esterase-fusion glycoprotein from newly-identified influenza D virus: Basis for its broad cell tropism. PLOS Pathog 2016; 12: e1005411.
    • (2016) PLOS Pathog , vol.12 , pp. e1005411
    • Song, H.1    Qi, J.2    Khedri, Z.3
  • 8
    • 77951636129 scopus 로고    scopus 로고
    • Clinical review: Primary influenza viral pneumonia
    • and
    • Rello J, andPop-Vicas A., Clinical review: Primary influenza viral pneumonia. Crit Care 2009; 13: 235.
    • (2009) Crit Care , vol.13 , pp. 235
    • Rello, J.1    Pop-Vicas, A.2
  • 9
    • 85012110631 scopus 로고    scopus 로고
    • A narrative review of influenza: A seasonal and pandemic disease
    • Moghadami M., A narrative review of influenza: A seasonal and pandemic disease. Iran J Med Sci 2017; 42: 2–13.
    • (2017) Iran J Med Sci , vol.42 , pp. 2-13
    • Moghadami, M.1
  • 10
    • 84941035061 scopus 로고    scopus 로고
    • Incidence of medically attended influenza during pandemic and post-pandemic seasons through the Influenza Incidence Surveillance Project, 2009-2013
    • Fowlkes A, Steffens A, Temte J. Incidence of medically attended influenza during pandemic and post-pandemic seasons through the Influenza Incidence Surveillance Project, 2009-2013. Lancet Respir Med 2015; 3: 709–718.
    • (2015) Lancet Respir Med , vol.3 , pp. 709-718
    • Fowlkes, A.1    Steffens, A.2    Temte, J.3
  • 11
    • 27944442029 scopus 로고    scopus 로고
    • A review of vaccine research and development: Human acute respiratory infections
    • Girard MP, Cherian T, Pervikov Y. A review of vaccine research and development: Human acute respiratory infections. Vaccine 2005; 23: 5708–57-24.
    • (2005) Vaccine , vol.23 , pp. 5708-5724
    • Girard, M.P.1    Cherian, T.2    Pervikov, Y.3
  • 12
    • 84969771887 scopus 로고    scopus 로고
    • Taxonomy of the order Mononegavirales: update 2016
    • Afonso CL, Amarasinghe GK, Banyai K. Taxonomy of the order Mononegavirales: update 2016. Arch Virol 2016; 161: 2351–23-60.
    • (2016) Arch Virol , vol.161 , pp. 2351-2360
    • Afonso, C.L.1    Amarasinghe, G.K.2    Banyai, K.3
  • 13
    • 0035927982 scopus 로고    scopus 로고
    • Respiratory syncytial virus and parainfluenza virus
    • Hall CB., Respiratory syncytial virus and parainfluenza virus. New Engl J Med 2001; 344: 1917–19-28.
    • (2001) New Engl J Med , vol.344 , pp. 1917-1928
    • Hall, C.B.1
  • 14
    • 0030716943 scopus 로고    scopus 로고
    • Pediatric hospitalizations for croup (laryngotracheobronchitis): Biennial increases associated with human parainfluenza virus 1 epidemics
    • Marx A, Török TJ, Holma RC. Pediatric hospitalizations for croup (laryngotracheobronchitis): Biennial increases associated with human parainfluenza virus 1 epidemics. J Infect Dis 1997; 176: 1423–142-7.
    • (1997) J Infect Dis , vol.176 , pp. 1423-1427
    • Marx, A.1    Török, T.J.2    Holma, R.C.3
  • 15
    • 12144289984 scopus 로고    scopus 로고
    • Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy
    • Friesner RA, Banks JL, Murphy RB. Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. J Med Chem 2004; 47: 1739–17-49.
    • (2004) J Med Chem , vol.47 , pp. 1739-1749
    • Friesner, R.A.1    Banks, J.L.2    Murphy, R.B.3
  • 16
    • 84872534732 scopus 로고    scopus 로고
    • Epidemiology and clinical presentation of the four human parainfluenza virus types
    • Liu W-K, Liu Q, Chen D-H. Epidemiology and clinical presentation of the four human parainfluenza virus types. BMC Infect Dis 2013; 13: 28.
    • (2013) BMC Infect Dis , vol.13 , pp. 28
    • Liu, W.-K.1    Liu, Q.2    Chen, D.-H.3
  • 17
    • 1842497566 scopus 로고    scopus 로고
    • Population-based surveillance for hospitalizations associated with respiratory syncytial virus, influenza virus, and parainfluenza viruses among young children
    • Iwane MK, Edwards KM, Szilagyi PG. Population-based surveillance for hospitalizations associated with respiratory syncytial virus, influenza virus, and parainfluenza viruses among young children. Pediatrics 2004; 113: 1758–17-64.
    • (2004) Pediatrics , vol.113 , pp. 1758-1764
    • Iwane, M.K.1    Edwards, K.M.2    Szilagyi, P.G.3
  • 18
    • 77951653074 scopus 로고    scopus 로고
    • Global burden of acute lower respiratory infections due to respiratory syncytial virus in young children: a systematic review and meta-analysis
    • Nair H, Nokes DJ, Gessner BD. Global burden of acute lower respiratory infections due to respiratory syncytial virus in young children: a systematic review and meta-analysis. Lancet 2010; 375: 1545–15-55.
    • (2010) Lancet , vol.375 , pp. 1545-1555
    • Nair, H.1    Nokes, D.J.2    Gessner, B.D.3
  • 19
    • 84930806483 scopus 로고    scopus 로고
    • Respiratory syncytial virus, an ongoing medical dilemma: an expert commentary on respiratory syncytial virus prophylactic and therapeutic pharmaceuticals currently in clinical trials
    • Broadbent L, Groves H, Shields MD. Respiratory syncytial virus, an ongoing medical dilemma: an expert commentary on respiratory syncytial virus prophylactic and therapeutic pharmaceuticals currently in clinical trials. Influenza Other Respir Virus 2015; 9: 169–1-78.
    • (2015) Influenza Other Respir Virus , vol.9 , pp. 169-178
    • Broadbent, L.1    Groves, H.2    Shields, M.D.3
  • 20
    • 0036254559 scopus 로고    scopus 로고
    • The pathogenesis of respiratory syncytial virus disease in childhood
    • and
    • McNamara PS, andSmyth RL., The pathogenesis of respiratory syncytial virus disease in childhood. Br Med Bull 2002; 61: 13–28.
    • (2002) Br Med Bull , vol.61 , pp. 13-28
    • McNamara, P.S.1    Smyth, R.L.2
  • 21
    • 78650656135 scopus 로고    scopus 로고
    • Respiratory syncytial virus disease: update on treatment and prevention
    • Krilov LR., Respiratory syncytial virus disease: update on treatment and prevention. Expert Rev Anti-infect Ther 2011; 9: 27–32.
    • (2011) Expert Rev Anti-infect Ther , vol.9 , pp. 27-32
    • Krilov, L.R.1
  • 22
    • 56149093228 scopus 로고    scopus 로고
    • Human metapneumovirus infection in adults
    • Falsey AR., Human metapneumovirus infection in adults. Pediatr Infect Dis J 2008; 27: S80–S8-3.
    • (2008) Pediatr Infect Dis J , vol.27 , pp. S80-S83
    • Falsey, A.R.1
  • 23
    • 1842509161 scopus 로고    scopus 로고
    • Human metapneumovirus: A new player among respiratory viruses
    • and
    • Hamelin M-È, Abed Y, andBoivin G., Human metapneumovirus: A new player among respiratory viruses. Clin Infect Dis 2004; 38: 983–9-90.
    • (2004) Clin Infect Dis , vol.38 , pp. 983-990
    • Hamelin, M.-È.1    Abed, Y.2    Boivin, G.3
  • 24
    • 0037830656 scopus 로고    scopus 로고
    • Human metapneumovirus associated with respiratory tract infections in a 3-year study of nasal swabs from infants in Italy
    • Maggi F, Pifferi M, Vatteroni M. Human metapneumovirus associated with respiratory tract infections in a 3-year study of nasal swabs from infants in Italy. J Clin Microbiol 2003; 41: 2987–29-91.
    • (2003) J Clin Microbiol , vol.41 , pp. 2987-2991
    • Maggi, F.1    Pifferi, M.2    Vatteroni, M.3
  • 25
    • 0030951318 scopus 로고    scopus 로고
    • Epidemiology, pathogenesis, and treatment of the common cold
    • quiz 9–40
    • Turner RB., Epidemiology, pathogenesis, and treatment of the common cold. Ann Allergy Asthma Immunol 1997; 78: 531–539; quiz 9–40.
    • (1997) Ann Allergy Asthma Immunol , vol.78 , pp. 531-539
    • Turner, R.B.1
  • 26
    • 84873143468 scopus 로고    scopus 로고
    • Picornavirus and enterovirus diversity with associated human diseases
    • Tapparel C, Siegrist F, Petty TJ. Picornavirus and enterovirus diversity with associated human diseases. Infect Genet Evol 2013; 14: 282–2-93.
    • (2013) Infect Genet Evol , vol.14 , pp. 282-293
    • Tapparel, C.1    Siegrist, F.2    Petty, T.J.3
  • 28
    • 84966312325 scopus 로고    scopus 로고
    • de Crom SCM, Rossen JWA, van Furth AM and Obihara CC. Enterovirus and parechovirus infection children: a brief overview., 2016; 175: 1023–1029
    • de Crom SCM, Rossen JWA, van Furth AM and Obihara CC. Enterovirus and parechovirus infection in children: a brief overview. European Journal of Pediatrics 2016; 175: 1023–1029.
  • 29
    • 84899534616 scopus 로고    scopus 로고
    • Recombination in the evolution of enterovirus C species sub-group that contains types CVA-21, CVA-24, EV-C95, EV-C96 and EV-C99
    • Smura T, Blomqvist S, Vuorinen T. Recombination in the evolution of enterovirus C species sub-group that contains types CVA-21, CVA-24, EV-C95, EV-C96 and EV-C99. PloS One 2014; 9: e94579.
    • (2014) PloS One , vol.9 , pp. e94579
    • Smura, T.1    Blomqvist, S.2    Vuorinen, T.3
  • 30
    • 84954457455 scopus 로고    scopus 로고
    • Rhinoviruses and respiratory enteroviruses: Not as simple as ABC
    • and;, : 1–23
    • Royston L, andTapparel C., Rhinoviruses and respiratory enteroviruses: Not as simple as ABC. Viruses 2016; 8: 1–23.
    • (2016) Viruses , vol.8
    • Royston, L.1    Tapparel, C.2
  • 32
    • 84991819367 scopus 로고    scopus 로고
    • Enterovirus 71 infection and neurological complications
    • Lee KY., Enterovirus 71 infection and neurological complications. Korean J Pediatr 2016; 59: 395–401.
    • (2016) Korean J Pediatr , vol.59 , pp. 395-401
    • Lee, K.Y.1
  • 33
    • 85039794011 scopus 로고    scopus 로고
    • Human coronaviruses: A review of virus–host interactions
    • 1–28
    • Lim XY, Ng LY, Tam PJ. Human coronaviruses: A review of virus–host interactions. Diseases 2016; 4: 1–28.
    • (2016) Diseases , vol.4
    • Lim, X.Y.1    Ng, L.Y.2    Tam, P.J.3
  • 34
    • 0142107410 scopus 로고    scopus 로고
    • Coronavirus 229E-related pneumonia in immunocompromised patients
    • Pene F, Merlat A, Vabret A. Coronavirus 229E-related pneumonia in immunocompromised patients. Clin Infect Dis 2003; 37: 929–9-32.
    • (2003) Clin Infect Dis , vol.37 , pp. 929-932
    • Pene, F.1    Merlat, A.2    Vabret, A.3
  • 35
    • 85056037349 scopus 로고    scopus 로고
    • Understanding human coronavirus HCoV-NL63
    • and
    • Abdul-Rasool S, andFielding BC., Understanding human coronavirus HCoV-NL63. Open Virol J 2010; 4: 76–84.
    • (2010) Open Virol J , vol.4 , pp. 76-84
    • Abdul-Rasool, S.1    Fielding, B.C.2
  • 36
    • 33646561863 scopus 로고    scopus 로고
    • Coronavirus HKU1 Infection in the United States
    • Esper F, Weibel C, Ferguson D. Coronavirus HKU1 Infection in the United States. Emerg Infect Dis 2006; 12: 775–77-9.
    • (2006) Emerg Infect Dis , vol.12 , pp. 775-779
    • Esper, F.1    Weibel, C.2    Ferguson, D.3
  • 37
    • 0042354620 scopus 로고    scopus 로고
    • Description and clinical treatment of an early outbreak of severe acute respiratory syndrome (SARS) in Guangzhou, PR China
    • Zhao Z, Zhang F, Xu M. Description and clinical treatment of an early outbreak of severe acute respiratory syndrome (SARS) in Guangzhou, PR China. J Med Microbiol 2003; 52: 715–7-20.
    • (2003) J Med Microbiol , vol.52 , pp. 715-720
    • Zhao, Z.1    Zhang, F.2    Xu, M.3
  • 38
    • 35448985443 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus as an agent of emerging and reemerging infection
    • Cheng VC, Lau SK, Woo PC. Severe acute respiratory syndrome coronavirus as an agent of emerging and reemerging infection. Clin Microbiol Rev 2007; 20: 660–6-94.
    • (2007) Clin Microbiol Rev , vol.20 , pp. 660-694
    • Cheng, V.C.1    Lau, S.K.2    Woo, P.C.3
  • 39
    • 84940313968 scopus 로고    scopus 로고
    • Novel coronavirus infections in Jordan, April 2012: epidemiological findings from a retrospective investigation
    • Hijawi B, Abdallat M, Sayaydeh A. Novel coronavirus infections in Jordan, April 2012: epidemiological findings from a retrospective investigation. East Mediterr Health J 2013; 19 Suppl 1: S12–S18.
    • (2013) East Mediterr Health J , vol.19 , pp. S12-S18
    • Hijawi, B.1    Abdallat, M.2    Sayaydeh, A.3
  • 41
    • 84957818744 scopus 로고    scopus 로고
    • Coronaviruses - drug discovery and therapeutic options
    • Zumla A, Chan JFW, Azhar EI. Coronaviruses - drug discovery and therapeutic options. Nat Rev Drug Discov 2016; 15: 327–3-47.
    • (2016) Nat Rev Drug Discov , vol.15 , pp. 327-347
    • Zumla, A.1    Chan, J.F.W.2    Azhar, E.I.3
  • 42
    • 85044759880 scopus 로고    scopus 로고
    • Infection with Middle East respiratory syndrome coronavirus
    • and
    • Alsolamy S, andArabi YM., Infection with Middle East respiratory syndrome coronavirus. Canad J Respir Ther 2015; 51: 102.
    • (2015) Canad J Respir Ther , vol.51 , pp. 102
    • Alsolamy, S.1    Arabi, Y.M.2
  • 43
    • 60549106419 scopus 로고    scopus 로고
    • Antimicrobial strategies: inhibition of viral polymerases by 3'-hydroxyl nucleosides
    • Deval J., Antimicrobial strategies: inhibition of viral polymerases by 3'-hydroxyl nucleosides. Drugs 2009; 69: 151–1-66.
    • (2009) Drugs , vol.69 , pp. 151-166
    • Deval, J.1
  • 44
    • 79960384534 scopus 로고    scopus 로고
    • Influenza A viruses: new research developments
    • and
    • Medina RA, andGarcía-Sastre A., Influenza A viruses: new research developments. Nat Rev Micro 2011; 9: 590–603.
    • (2011) Nat Rev Micro , vol.9 , pp. 590-603
    • Medina, R.A.1    García-Sastre, A.2
  • 45
    • 84880367286 scopus 로고    scopus 로고
    • The RNA polymerase of influenza a virus: mechanisms of viral transcription and replication
    • Fodor E., The RNA polymerase of influenza a virus: mechanisms of viral transcription and replication. Acta Virol 2013; 57: 113–1-22.
    • (2013) Acta Virol , vol.57 , pp. 113-122
    • Fodor, E.1
  • 46
    • 84922245983 scopus 로고    scopus 로고
    • Structural insight into cap-snatching and RNA synthesis by influenza polymerase
    • Reich S, Guilligay D, Pflug A. Structural insight into cap-snatching and RNA synthesis by influenza polymerase. Nature 2014; 516: 361–36-6.
    • (2014) Nature , vol.516 , pp. 361-366
    • Reich, S.1    Guilligay, D.2    Pflug, A.3
  • 47
    • 0003839687 scopus 로고
    • Role of two of the influenza virus core P proteins in recognizing cap 1 structures (m7GpppNm) on RNAs and in initiating viral RNA transcription
    • and
    • Ulmanen I, Broni BA, andKrug RM., Role of two of the influenza virus core P proteins in recognizing cap 1 structures (m7GpppNm) on RNAs and in initiating viral RNA transcription. Proc Natl Acad Sci 1981; 78: 7355–735-9.
    • (1981) Proc Natl Acad Sci , vol.78 , pp. 7355-7359
    • Ulmanen, I.1    Broni, B.A.2    Krug, R.M.3
  • 48
    • 0020480480 scopus 로고
    • Identification of the cap binding protein of influenza virus
    • and
    • Blass D, Patzelt E, andKuechler E., Identification of the cap binding protein of influenza virus. Nucl Acids Res 1982; 10: 4803–48-12.
    • (1982) Nucl Acids Res , vol.10 , pp. 4803-4812
    • Blass, D.1    Patzelt, E.2    Kuechler, E.3
  • 49
    • 43249128376 scopus 로고    scopus 로고
    • The structural basis for cap binding by influenza virus polymerase subunit PB2
    • Guilligay D, Tarendeau F, Resa-Infante P. The structural basis for cap binding by influenza virus polymerase subunit PB2. Nat Struct Mol Biol 2008; 15: 500–50-6.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 500-506
    • Guilligay, D.1    Tarendeau, F.2    Resa-Infante, P.3
  • 50
    • 67249130012 scopus 로고    scopus 로고
    • The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit
    • Dias A, Bouvier D, Crepin T. The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit. Nature 2009; 458: 914–91-8.
    • (2009) Nature , vol.458 , pp. 914-918
    • Dias, A.1    Bouvier, D.2    Crepin, T.3
  • 51
    • 67249100913 scopus 로고    scopus 로고
    • N reveals an endonuclease active site
    • N reveals an endonuclease active site. Nature 2009; 458: 909.
    • (2009) Nature , vol.458 , pp. 909
    • Yuan, P.1    Bartlam, M.2    Lou, Z.3
  • 52
    • 84922257981 scopus 로고    scopus 로고
    • Structure of influenza A polymerase bound to the viral RNA promoter
    • Pflug A, Guilligay D, Reich S. Structure of influenza A polymerase bound to the viral RNA promoter. Nature 2014; 516: 355–3-60.
    • (2014) Nature , vol.516 , pp. 355-360
    • Pflug, A.1    Guilligay, D.2    Reich, S.3
  • 53
    • 84899859708 scopus 로고    scopus 로고
    • Conserved features of the PB2 627 domain impact influenza virus polymerase function and replication
    • Kirui J, Bucci MD, Poole DS. Conserved features of the PB2 627 domain impact influenza virus polymerase function and replication. J Virol 2014; 88: 5977–59-86.
    • (2014) J Virol , vol.88 , pp. 5977-5986
    • Kirui, J.1    Bucci, M.D.2    Poole, D.S.3
  • 54
    • 85015198109 scopus 로고    scopus 로고
    • Role of the PB2 627 domain in influenza A virus polymerase function
    • and;, : e02467–16
    • Nilsson BE, te Velthuis AJW, andFodor E., Role of the PB2 627 domain in influenza A virus polymerase function. J Virol 2017; 91: e02467–16.
    • (2017) J Virol , vol.91
    • Nilsson, B.E.1    te Velthuis, A.J.W.2    Fodor, E.3
  • 55
    • 85010686232 scopus 로고    scopus 로고
    • The role of the priming loop in influenza A virus RNA synthesis
    • te Velthuis AJW, Robb NC, Kapanidis AN. The role of the priming loop in influenza A virus RNA synthesis. Nat Microbiol 2016; 1: 16029.
    • (2016) Nat Microbiol , vol.1 , pp. 16029
    • te Velthuis, A.J.W.1    Robb, N.C.2    Kapanidis, A.N.3
  • 56
    • 84991769513 scopus 로고    scopus 로고
    • The influenza virus polymerase complex: An update on its structure, functions, and significance for antiviral drug design
    • and
    • Stevaert A, andNaesens L., The influenza virus polymerase complex: An update on its structure, functions, and significance for antiviral drug design. Med Res Rev 2016; 36: 1127–11-73.
    • (2016) Med Res Rev , vol.36 , pp. 1127-1173
    • Stevaert, A.1    Naesens, L.2
  • 57
    • 84937712896 scopus 로고    scopus 로고
    • Initiation and regulation of paramyxovirus transcription and replication
    • and
    • Noton SL, andFearns R., Initiation and regulation of paramyxovirus transcription and replication. Virology 2015; 479–480: 545–554.
    • (2015) Virology , vol.479-480 , pp. 545-554
    • Noton, S.L.1    Fearns, R.2
  • 58
    • 85011536661 scopus 로고    scopus 로고
    • Polymerases of paramyxoviruses and pneumoviruses
    • and
    • Fearns R, andPlemper RK., Polymerases of paramyxoviruses and pneumoviruses. Virus Res 2017; 234: 87–102.
    • (2017) Virus Res , vol.234 , pp. 87-102
    • Fearns, R.1    Plemper, R.K.2
  • 59
    • 84986327392 scopus 로고    scopus 로고
    • New antiviral approaches for respiratory syncytial virus and other mononegaviruses: Inhibiting the RNA polymerase
    • and
    • Fearns R, andDeval J., New antiviral approaches for respiratory syncytial virus and other mononegaviruses: Inhibiting the RNA polymerase. Antiviral Res 2016; 134: 63–76.
    • (2016) Antiviral Res , vol.134 , pp. 63-76
    • Fearns, R.1    Deval, J.2
  • 60
    • 0030028730 scopus 로고    scopus 로고
    • Transcription elongation factor of respiratory syncytial virus, a nonsegmented negative-strand RNA virus
    • Collins PL, Hill MG, Cristina J. Transcription elongation factor of respiratory syncytial virus, a nonsegmented negative-strand RNA virus. Proc Natl Acad Sci 1996; 93: 81–8-5.
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 81-85
    • Collins, P.L.1    Hill, M.G.2    Cristina, J.3
  • 61
    • 0029584042 scopus 로고
    • Production of infectious human respiratory syncytial virus from cloned cDNA confirms an essential role for the transcription elongation factor from the 5' proximal open reading frame of the M2 mRNA in gene expression and provides a capability for vaccine development
    • Collins PL, Hill MG, Camargo E. Production of infectious human respiratory syncytial virus from cloned cDNA confirms an essential role for the transcription elongation factor from the 5' proximal open reading frame of the M2 mRNA in gene expression and provides a capability for vaccine development. Proc Natl Acad Sci 1995; 92: 11563–1156-7.
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 11563-11567
    • Collins, P.L.1    Hill, M.G.2    Camargo, E.3
  • 62
    • 0028135698 scopus 로고
    • Bacterial expression of human respiratory syncytial viral phosphoprotein P and identification of Ser237 as the site of phosphorylation by cellular casein kinase II
    • and
    • Mazumder B, Adhikary G, andBarik S., Bacterial expression of human respiratory syncytial viral phosphoprotein P and identification of Ser237 as the site of phosphorylation by cellular casein kinase II. Virology 1994; 205: 93–103.
    • (1994) Virology , vol.205 , pp. 93-103
    • Mazumder, B.1    Adhikary, G.2    Barik, S.3
  • 63
    • 85012065390 scopus 로고    scopus 로고
    • New insights into structural disorder in human respiratory syncytial virus phosphoprotein and implications for binding of protein partners
    • Pereira N, Cardone C, Lassoued S. New insights into structural disorder in human respiratory syncytial virus phosphoprotein and implications for binding of protein partners. J Biol Chem 2017; 292: 2120–21-31.
    • (2017) J Biol Chem , vol.292 , pp. 2120-2131
    • Pereira, N.1    Cardone, C.2    Lassoued, S.3
  • 64
    • 0141632677 scopus 로고    scopus 로고
    • Interaction between human respiratory syncytial virus (RSV) M2-1 and P proteins is required for reconstitution of M2-1-dependent RSV minigenome activity
    • Mason SW, Aberg E, Lawetz C. Interaction between human respiratory syncytial virus (RSV) M2-1 and P proteins is required for reconstitution of M2-1-dependent RSV minigenome activity. J Virol 2003; 77: 10670–1067-6.
    • (2003) J Virol , vol.77 , pp. 10670-10676
    • Mason, S.W.1    Aberg, E.2    Lawetz, C.3
  • 65
    • 84863658768 scopus 로고    scopus 로고
    • Structure and functional analysis of the RNA-and viral phosphoprotein-binding domain of respiratory syncytial virus M2-1 protein
    • Blondot M-L, Dubosclard V, Fix J. Structure and functional analysis of the RNA-and viral phosphoprotein-binding domain of respiratory syncytial virus M2-1 protein. PLoS Pathog 2012; 8: e1002734.
    • (2012) PLoS Pathog , vol.8 , pp. e1002734
    • Blondot, M.-L.1    Dubosclard, V.2    Fix, J.3
  • 66
    • 84865097975 scopus 로고    scopus 로고
    • Characterization of a viral phosphoprotein binding site on the surface of the respiratory syncytial nucleoprotein
    • Galloux M, Tarus B, Blazevic I. Characterization of a viral phosphoprotein binding site on the surface of the respiratory syncytial nucleoprotein. J Virol 2012; 86: 8375–83-87.
    • (2012) J Virol , vol.86 , pp. 8375-8387
    • Galloux, M.1    Tarus, B.2    Blazevic, I.3
  • 67
    • 33746895769 scopus 로고    scopus 로고
    • Central role of the respiratory syncytial virus matrix protein in infection
    • and
    • Ghildyal R, Ho A, andJans DA., Central role of the respiratory syncytial virus matrix protein in infection. FEMS Microbiol Rev 2006; 30: 692–705.
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 692-705
    • Ghildyal, R.1    Ho, A.2    Jans, D.A.3
  • 68
    • 84937217436 scopus 로고    scopus 로고
    • Structure of the L protein of vesicular stomatitis virus from electron cryomicroscopy
    • Liang B, Li Z, Jenni S. Structure of the L protein of vesicular stomatitis virus from electron cryomicroscopy. Cell 2015; 162: 314–3-27.
    • (2015) Cell , vol.162 , pp. 314-327
    • Liang, B.1    Li, Z.2    Jenni, S.3
  • 69
    • 0025322445 scopus 로고
    • Sequence comparison of five polymerases (L proteins) of unsegmented negative-strand RNA viruses: theoretical assignment of functional domains
    • Poch O, Blumberg BM, Bougueleret L. Sequence comparison of five polymerases (L proteins) of unsegmented negative-strand RNA viruses: theoretical assignment of functional domains. J Gen Virol 1990; 71: 1153–11-62.
    • (1990) J Gen Virol , vol.71 , pp. 1153-1162
    • Poch, O.1    Blumberg, B.M.2    Bougueleret, L.3
  • 70
    • 78650526378 scopus 로고    scopus 로고
    • Molecular architecture of the vesicular stomatitis virus RNA polymerase
    • Rahmeh AA, Schenk AD, Danek EI. Molecular architecture of the vesicular stomatitis virus RNA polymerase. Proc Natl Acad Sci USA 2010; 107: 20075–200-80.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 20075-20080
    • Rahmeh, A.A.1    Schenk, A.D.2    Danek, E.I.3
  • 71
    • 84864448769 scopus 로고    scopus 로고
    • Template-based protein structure modeling using the RaptorX web server
    • Kallberg M, Wang H, Wang S. Template-based protein structure modeling using the RaptorX web server. Nat Protoc 2012; 7: 1511–15-22.
    • (2012) Nat Protoc , vol.7 , pp. 1511-1522
    • Kallberg, M.1    Wang, H.2    Wang, S.3
  • 72
    • 84946771983 scopus 로고    scopus 로고
    • X-ray structure and activities of an essential mononegavirales L-protein domain
    • et al.; 6
    • Paesen GC, Collet A, Sallamand C, et al. X-ray structure and activities of an essential mononegavirales L-protein domain. Nat Commun 2015; 6: 8749.
    • (2015) Nat Commun , pp. 8749
    • Paesen, G.C.1    Collet, A.2    Sallamand, C.3
  • 73
    • 37849014584 scopus 로고    scopus 로고
    • A conserved motif in region v of the large polymerase proteins of nonsegmented negative-sense RNA viruses that is essential for mRNA capping
    • Li J, Rahmeh A, Morelli M. A conserved motif in region v of the large polymerase proteins of nonsegmented negative-sense RNA viruses that is essential for mRNA capping. J Virol 2008; 82: 775–7-84.
    • (2008) J Virol , vol.82 , pp. 775-784
    • Li, J.1    Rahmeh, A.2    Morelli, M.3
  • 74
    • 0036219326 scopus 로고    scopus 로고
    • In silico identification, structure prediction and phylogenetic analysis of the 2′-O-ribose (cap 1) methyltransferase domain in the large structural protein of ssRNA negative-strand viruses
    • and
    • Bujnicki JM, andRychlewski L., In silico identification, structure prediction and phylogenetic analysis of the 2′-O-ribose (cap 1) methyltransferase domain in the large structural protein of ssRNA negative-strand viruses. Prot Eng Des Select 2002; 15: 101–10-8.
    • (2002) Prot Eng Des Select , vol.15 , pp. 101-108
    • Bujnicki, J.M.1    Rychlewski, L.2
  • 75
    • 33845992557 scopus 로고    scopus 로고
    • Unconventional mechanism of mRNA capping by the RNA-dependent RNA polymerase of vesicular stomatitis virus
    • and
    • Ogino T, andBanerjee AK., Unconventional mechanism of mRNA capping by the RNA-dependent RNA polymerase of vesicular stomatitis virus. Mol Cell 2007; 25: 85–97.
    • (2007) Mol Cell , vol.25 , pp. 85-97
    • Ogino, T.1    Banerjee, A.K.2
  • 76
    • 84875258948 scopus 로고    scopus 로고
    • In vitro capping and transcription of rhabdoviruses
    • Ogino T., In vitro capping and transcription of rhabdoviruses. Methods 2013; 59: 188–1-98.
    • (2013) Methods , vol.59 , pp. 188-198
    • Ogino, T.1
  • 77
    • 83855162132 scopus 로고    scopus 로고
    • Conventional and unconventional mechanisms for capping viral mRNA
    • Decroly E, Ferron F, Lescar J. Conventional and unconventional mechanisms for capping viral mRNA. Nat Rev Micro 2012; 10: 51–65.
    • (2012) Nat Rev Micro , vol.10 , pp. 51-65
    • Decroly, E.1    Ferron, F.2    Lescar, J.3
  • 78
    • 84941038188 scopus 로고    scopus 로고
    • RNA-dependent RNA polymerases of picornaviruses: from the structure to regulatory mechanisms
    • and
    • Ferrer-Orta C, Ferrero D, andVerdaguer N., RNA-dependent RNA polymerases of picornaviruses: from the structure to regulatory mechanisms. Viruses 2015; 7: 4438–44-60.
    • (2015) Viruses , vol.7 , pp. 4438-4460
    • Ferrer-Orta, C.1    Ferrero, D.2    Verdaguer, N.3
  • 79
    • 2442677715 scopus 로고    scopus 로고
    • Initiation of viral RNA-dependent RNA polymerization
    • and
    • van Dijk AA, Makeyev EV, andBamford DH., Initiation of viral RNA-dependent RNA polymerization. J Gen Virol 2004; 85: 1077–10-93.
    • (2004) J Gen Virol , vol.85 , pp. 1077-1093
    • van Dijk, A.A.1    Makeyev, E.V.2    Bamford, D.H.3
  • 81
    • 0001856730 scopus 로고    scopus 로고
    • Possible unifying mechanism of picornavirus genome replication
    • Semler B.L., Wimmer E., (eds), Washington, DC, ASM Press, In:, (eds
    • Paul AV., Possible unifying mechanism of picornavirus genome replication. In: Semler BL, andWimmer E, (eds) Molecular biology of picornavirus. Washington, DC: ASM Press, 2002, pp.227–2-46.
    • (2002) Molecular biology of picornavirus , pp. 227-246
    • Paul, A.V.1
  • 82
    • 85011967206 scopus 로고    scopus 로고
    • Picornaviral polymerase structure, function, and fidelity modulation
    • Peersen OB., Picornaviral polymerase structure, function, and fidelity modulation. Virus Res 2017; 234: 4–20.
    • (2017) Virus Res , vol.234 , pp. 4-20
    • Peersen, O.B.1
  • 83
    • 0037223676 scopus 로고    scopus 로고
    • Biochemical and genetic studies of the VPg uridylylation reaction catalyzed by the RNA polymerase of poliovirus
    • Paul AV, Peters J, Mugavero J. Biochemical and genetic studies of the VPg uridylylation reaction catalyzed by the RNA polymerase of poliovirus. J Virol 2003; 77: 891–904.
    • (2003) J Virol , vol.77 , pp. 891-904
    • Paul, A.V.1    Peters, J.2    Mugavero, J.3
  • 84
    • 0242415195 scopus 로고    scopus 로고
    • A “slide-back” mechanism for the initiation of protein-primed RNA synthesis by the RNA polymerase of poliovirus
    • Paul AV, Yin J, Mugavero J. A “slide-back” mechanism for the initiation of protein-primed RNA synthesis by the RNA polymerase of poliovirus. J Biol Chem 2003; 278: 43951–439-60.
    • (2003) J Biol Chem , vol.278 , pp. 43951-43960
    • Paul, A.V.1    Yin, J.2    Mugavero, J.3
  • 85
    • 0033755326 scopus 로고    scopus 로고
    • Genetic and biochemical studies of polioviruscis-acting replication element cre in relation to VPg uridylylation
    • Rieder E, Paul AV, Kim DW. Genetic and biochemical studies of polioviruscis-acting replication element cre in relation to VPg uridylylation. J Virol 2000; 74: 10371–103-80.
    • (2000) J Virol , vol.74 , pp. 10371-10380
    • Rieder, E.1    Paul, A.V.2    Kim, D.W.3
  • 86
    • 10644250663 scopus 로고    scopus 로고
    • Crystal structure of complete rhinovirus RNA polymerase suggests front loading of protein primer
    • Appleby TC, Luecke H, Shim JH. Crystal structure of complete rhinovirus RNA polymerase suggests front loading of protein primer. J Virol 2005; 79: 277–2-88.
    • (2005) J Virol , vol.79 , pp. 277-288
    • Appleby, T.C.1    Luecke, H.2    Shim, J.H.3
  • 87
    • 84877616491 scopus 로고    scopus 로고
    • Crystal structure of enterovirus 71 RNA-dependent RNA polymerase complexed with its protein primer VPg: implication for a trans mechanism of VPg uridylylation
    • Chen C, Wang Y, Shan C. Crystal structure of enterovirus 71 RNA-dependent RNA polymerase complexed with its protein primer VPg: implication for a trans mechanism of VPg uridylylation. J Virol 2013; 87: 5755–57-68.
    • (2013) J Virol , vol.87 , pp. 5755-5768
    • Chen, C.1    Wang, Y.2    Shan, C.3
  • 88
    • 78651097570 scopus 로고    scopus 로고
    • Structural basis for active site closure by the poliovirus RNA-dependent RNA polymerase
    • and
    • Gong P, andPeersen OB., Structural basis for active site closure by the poliovirus RNA-dependent RNA polymerase. Proc Natl Acad Sci 2010; 107: 22505–225-10.
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 22505-22510
    • Gong, P.1    Peersen, O.B.2
  • 89
    • 84901270625 scopus 로고    scopus 로고
    • Evolution of tertiary structure of viral RNA dependent polymerases
    • Černý J, Bolfíková BČ, Valdes JJ. Evolution of tertiary structure of viral RNA dependent polymerases. PloS One 2014; 9: e96070.
    • (2014) PloS One , vol.9 , pp. e96070
    • Černý, J.1    Bolfíková, B.Č.2    Valdes, J.J.3
  • 90
    • 0031571638 scopus 로고    scopus 로고
    • Structure of the RNA-dependent RNA polymerase of poliovirus
    • and
    • Hansen JL, Long AM, andSchultz SC., Structure of the RNA-dependent RNA polymerase of poliovirus. Structure 1997; 5: 1109–11 22.
    • (1997) Structure , vol.5
    • Hansen, J.L.1    Long, A.M.2    Schultz, S.C.3
  • 91
    • 0024784519 scopus 로고
    • Identification of four conserved motifs among the RNA-dependent polymerase encoding elements
    • Poch O, Sauvaget I, Delarue M. Identification of four conserved motifs among the RNA-dependent polymerase encoding elements. EMBO J 1989; 8: 3867–3874.
    • (1989) EMBO J , vol.8 , pp. 3867-3874
    • Poch, O.1    Sauvaget, I.2    Delarue, M.3
  • 92
    • 4644238112 scopus 로고    scopus 로고
    • Structural basis for proteolysis‐dependent activation of the poliovirus RNA‐dependent RNA polymerase
    • and
    • Thompson AA, andPeersen OB., Structural basis for proteolysis‐dependent activation of the poliovirus RNA‐dependent RNA polymerase. EMBO J 2004; 23: 3462–34-71.
    • (2004) EMBO J , vol.23 , pp. 3462-3471
    • Thompson, A.A.1    Peersen, O.B.2
  • 93
    • 0034682792 scopus 로고    scopus 로고
    • Poliovirus RNA-dependent RNA polymerase (3Dpol): Structural, biochemical, and biological analysis of conserved structural motifs A and B
    • Gohara DW, Crotty S, Arnold JJ. Poliovirus RNA-dependent RNA polymerase (3Dpol): Structural, biochemical, and biological analysis of conserved structural motifs A and B. J Biol Chem 2000; 275: 25523–25532.
    • (2000) J Biol Chem , vol.275 , pp. 25523-25532
    • Gohara, D.W.1    Crotty, S.2    Arnold, J.J.3
  • 94
    • 0037150679 scopus 로고    scopus 로고
    • Visualization and functional analysis of RNA-dependent RNA polymerase lattices
    • Lyle JM, Bullitt E, Bienz K. Visualization and functional analysis of RNA-dependent RNA polymerase lattices. Science 2002; 296: 2218–22-22.
    • (2002) Science , vol.296 , pp. 2218-2222
    • Lyle, J.M.1    Bullitt, E.2    Bienz, K.3
  • 95
    • 84879554368 scopus 로고    scopus 로고
    • Surface for catalysis by poliovirus RNA-dependent RNA polymerase
    • and
    • Wang J, Lyle JM, andBullitt E., Surface for catalysis by poliovirus RNA-dependent RNA polymerase. J Mol Biol 2013; 425: 2529–25-40.
    • (2013) J Mol Biol , vol.425 , pp. 2529-2540
    • Wang, J.1    Lyle, J.M.2    Bullitt, E.3
  • 96
    • 0035283140 scopus 로고    scopus 로고
    • Oligomeric structures of poliovirus polymerase are important for function
    • Hobson SD, Rosenblum ES, Richards OC. Oligomeric structures of poliovirus polymerase are important for function. EMBO J 2001; 20: 1153–11-63.
    • (2001) EMBO J , vol.20 , pp. 1153-1163
    • Hobson, S.D.1    Rosenblum, E.S.2    Richards, O.C.3
  • 97
    • 0037200001 scopus 로고    scopus 로고
    • Structure-function relationships of the RNA-dependent RNA polymerase from poliovirus (3Dpol) A surface of the primary oligomerization domain functions in capsid precursor processing and VPg uridylylation
    • Pathak HB, Ghosh SKB, Roberts AW. Structure-function relationships of the RNA-dependent RNA polymerase from poliovirus (3Dpol) A surface of the primary oligomerization domain functions in capsid precursor processing and VPg uridylylation. J Biol Chem 2002; 277: 31551–315-62.
    • (2002) J Biol Chem , vol.277 , pp. 31551-31562
    • Pathak, H.B.1    Ghosh, S.K.B.2    Roberts, A.W.3
  • 98
    • 85014022955 scopus 로고    scopus 로고
    • Nidovirus RNA polymerases: Complex enzymes handling exceptional RNA genomes
    • and
    • Posthuma CC, te Velthuis AJW, andSnijder EJ., Nidovirus RNA polymerases: Complex enzymes handling exceptional RNA genomes. Virus Res 2017; 234: 58–73.
    • (2017) Virus Res , vol.234 , pp. 58-73
    • Posthuma, C.C.1    te Velthuis, A.J.W.2    Snijder, E.J.3
  • 99
    • 67349158649 scopus 로고    scopus 로고
    • Coronaviruses post-SARS: Update on replication and pathogenesis
    • and
    • Perlman S, andNetland J., Coronaviruses post-SARS: Update on replication and pathogenesis. Nat Rev Microbiol 2009; 7: 439–4-50.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 439-450
    • Perlman, S.1    Netland, J.2
  • 100
    • 84907226057 scopus 로고    scopus 로고
    • One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities
    • Subissi L, Posthuma CC, Collet A. One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities. Proc Natl Acad Sci 2014; 111: E3900–E3909.
    • (2014) Proc Natl Acad Sci , vol.111 , pp. E3900-E3909
    • Subissi, L.1    Posthuma, C.C.2    Collet, A.3
  • 101
    • 84945261819 scopus 로고    scopus 로고
    • Discovery of an essential nucleotidylating activity associated with a newly delineated conserved domain in the RNA polymerase-containing protein of all nidoviruses
    • Lehmann KC, Gulyaeva A, Zevenhoven-Dobbe JC. Discovery of an essential nucleotidylating activity associated with a newly delineated conserved domain in the RNA polymerase-containing protein of all nidoviruses. Nucl Acids Res 2015; 43: 8416–84-34.
    • (2015) Nucl Acids Res , vol.43 , pp. 8416-8434
    • Lehmann, K.C.1    Gulyaeva, A.2    Zevenhoven-Dobbe, J.C.3
  • 102
    • 0346888670 scopus 로고    scopus 로고
    • Molecular model of SARS coronavirus polymerase: implications for biochemical functions and drug design
    • Xu X, Liu Y, Weiss S. Molecular model of SARS coronavirus polymerase: implications for biochemical functions and drug design. Nucl Acids Res 2003; 31: 7117–71-30.
    • (2003) Nucl Acids Res , vol.31 , pp. 7117-7130
    • Xu, X.1    Liu, Y.2    Weiss, S.3
  • 103
    • 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 J-L. The palm subdomain-based active site is internally permuted in viral RNA-dependent RNA polymerases of an ancient lineage. J Mol Biol 2002; 324: 47–62.
    • (2002) J Mol Biol , vol.324 , pp. 47-62
    • Gorbalenya, A.E.1    Pringle, F.M.2    Zeddam, J.-L.3
  • 104
    • 17444431570 scopus 로고    scopus 로고
    • Expression, purification, and characterization of SARS coronavirus RNA polymerase
    • Cheng A, Zhang W, Xie Y. Expression, purification, and characterization of SARS coronavirus RNA polymerase. Virology 2005; 335: 165–1-76.
    • (2005) Virology , vol.335 , pp. 165-176
    • Cheng, A.1    Zhang, W.2    Xie, Y.3
  • 105
    • 84938086703 scopus 로고    scopus 로고
    • Structural basis and functional analysis of the SARS coronavirus nsp14–nsp10 complex
    • Ma Y, Wu L, Shaw N. Structural basis and functional analysis of the SARS coronavirus nsp14–nsp10 complex. Proc Natl Acad Sci 2015; 112: 9436–94-41.
    • (2015) Proc Natl Acad Sci , vol.112 , pp. 9436-9441
    • Ma, Y.1    Wu, L.2    Shaw, N.3
  • 106
    • 0015424606 scopus 로고
    • Design, synthesis, and broad spectrum antiviral activity of 1-β-D-ribofuranosyl-1,2,4-triazole-3-carboxamide and related nucleosides
    • Witkowski JT, Robins RK, Sidwell RW. Design, synthesis, and broad spectrum antiviral activity of 1-β-D-ribofuranosyl-1,2,4-triazole-3-carboxamide and related nucleosides. J Med Chem 1972; 15: 1150–115-4.
    • (1972) J Med Chem , vol.15 , pp. 1150-1154
    • Witkowski, J.T.1    Robins, R.K.2    Sidwell, R.W.3
  • 107
    • 0015523596 scopus 로고
    • Broad-spectrum antiviral activity of Virazole: 1-beta-D-ribofuranosyl-1,2,4-triazole-3-carboxamide
    • Sidwell RW, Huffman JH, Khare GP. Broad-spectrum antiviral activity of Virazole: 1-beta-D-ribofuranosyl-1,2,4-triazole-3-carboxamide. Science 1972; 177: 705–70-6.
    • (1972) Science , vol.177 , pp. 705-706
    • Sidwell, R.W.1    Huffman, J.H.2    Khare, G.P.3
  • 108
    • 0018840131 scopus 로고
    • Amantadine and ribavirin aerosol treatment of influenza A and B infection in mice
    • Wilson SZ, Knight V, Wyde PR. Amantadine and ribavirin aerosol treatment of influenza A and B infection in mice. Antimicrob Agents Chemother 1980; 17: 642–64-8.
    • (1980) Antimicrob Agents Chemother , vol.17 , pp. 642-648
    • Wilson, S.Z.1    Knight, V.2    Wyde, P.R.3
  • 109
    • 0023029523 scopus 로고
    • Protection of mice from lethal influenza virus infection with high dose-short duration ribavirin aerosol
    • Wyde PR, Wilson SZ, Gilbert BE. Protection of mice from lethal influenza virus infection with high dose-short duration ribavirin aerosol. Antimicrob Agents Chemother 1986; 30: 942–94-4.
    • (1986) Antimicrob Agents Chemother , vol.30 , pp. 942-944
    • Wyde, P.R.1    Wilson, S.Z.2    Gilbert, B.E.3
  • 110
    • 0034864547 scopus 로고    scopus 로고
    • Ribavirin–current status of a broad spectrum antiviral agent
    • Snell NJ., Ribavirin–current status of a broad spectrum antiviral agent. Expert Opin Pharmacother 2001; 2: 1317–13-24.
    • (2001) Expert Opin Pharmacother , vol.2 , pp. 1317-1324
    • Snell, N.J.1
  • 111
    • 0036240477 scopus 로고    scopus 로고
    • Mechanism of action of ribavirin in the combination treatment of chronic HCV infection
    • Lau JY, Tam RC, Liang TJ. Mechanism of action of ribavirin in the combination treatment of chronic HCV infection. Hepatology 2002; 35: 1002–100-9.
    • (2002) Hepatology , vol.35 , pp. 1002-1009
    • Lau, J.Y.1    Tam, R.C.2    Liang, T.J.3
  • 112
    • 0034532953 scopus 로고    scopus 로고
    • The broad-spectrum antiviral ribonucleoside ribavirin is an RNA virus mutagen
    • Crotty S, Maag D, Arnold JJ. The broad-spectrum antiviral ribonucleoside ribavirin is an RNA virus mutagen. Nat Med 2000; 6: 1375–137-9.
    • (2000) Nat Med , vol.6 , pp. 1375-1379
    • Crotty, S.1    Maag, D.2    Arnold, J.J.3
  • 113
    • 34848918867 scopus 로고    scopus 로고
    • 2'-C-Methyl branched pyrimidine ribonucleoside analogues: potent inhibitors of RNA virus replication
    • Benzaria S, Bardiot D, Bouisset T. 2'-C-Methyl branched pyrimidine ribonucleoside analogues: potent inhibitors of RNA virus replication. Antiviral Chem Chemother 2007; 18: 225–242.
    • (2007) Antiviral Chem Chemother , vol.18 , pp. 225-242
    • Benzaria, S.1    Bardiot, D.2    Bouisset, T.3
  • 114
    • 0037809239 scopus 로고    scopus 로고
    • Inhibition of hepatitis C virus RNA replication by 2'-modified nucleoside analogs
    • Carroll SS, Tomassini JE, Bosserman M. Inhibition of hepatitis C virus RNA replication by 2'-modified nucleoside analogs. J Biol Chem 2003; 278: 11979–119-84.
    • (2003) J Biol Chem , vol.278 , pp. 11979-11984
    • Carroll, S.S.1    Tomassini, J.E.2    Bosserman, M.3
  • 115
    • 4744364179 scopus 로고    scopus 로고
    • Structure-activity relationship of heterobase-modified 2'-C-methyl ribonucleosides as inhibitors of hepatitis C virus RNA replication
    • Eldrup AB, Prhavc M, Brooks J. Structure-activity relationship of heterobase-modified 2'-C-methyl ribonucleosides as inhibitors of hepatitis C virus RNA replication. J Med Chem 2004; 47: 5284–52-97.
    • (2004) J Med Chem , vol.47 , pp. 5284-5297
    • Eldrup, A.B.1    Prhavc, M.2    Brooks, J.3
  • 116
    • 77952669442 scopus 로고    scopus 로고
    • Efficacy of 2'-C-methylcytidine against yellow fever virus in cell culture and in a hamster model
    • Julander JG, Jha AK, Choi JA. Efficacy of 2'-C-methylcytidine against yellow fever virus in cell culture and in a hamster model. Antiviral Res 2010; 86: 261–26-7.
    • (2010) Antiviral Res , vol.86 , pp. 261-267
    • Julander, J.G.1    Jha, A.K.2    Choi, J.A.3
  • 117
    • 4644257970 scopus 로고    scopus 로고
    • A 7-deaza-adenosine analog is a potent and selective inhibitor of hepatitis C virus replication with excellent pharmacokinetic properties
    • Olsen DB, Eldrup AB, Bartholomew L. A 7-deaza-adenosine analog is a potent and selective inhibitor of hepatitis C virus replication with excellent pharmacokinetic properties. Antimicrob Agents Chemother 2004; 48: 3944–39-53.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 3944-3953
    • Olsen, D.B.1    Eldrup, A.B.2    Bartholomew, L.3
  • 118
    • 33847042742 scopus 로고    scopus 로고
    • A dengue fever viremia model in mice shows reduction in viral replication and suppression of the inflammatory response after treatment with antiviral drugs
    • Schul W, Liu W, Xu HY. A dengue fever viremia model in mice shows reduction in viral replication and suppression of the inflammatory response after treatment with antiviral drugs. J Infect Dis 2007; 195: 665–6-74.
    • (2007) J Infect Dis , vol.195 , pp. 665-674
    • Schul, W.1    Liu, W.2    Xu, H.Y.3
  • 119
    • 33750465538 scopus 로고    scopus 로고
    • Synthesis and pharmacokinetics of valopicitabine (NM283), an efficient prodrug of the potent anti-HCV agent 2′-C-methylcytidine
    • Pierra C, Amador A, Benzaria S. Synthesis and pharmacokinetics of valopicitabine (NM283), an efficient prodrug of the potent anti-HCV agent 2′-C-methylcytidine. J Med Chem 2006; 49: 6614–66-20.
    • (2006) J Med Chem , vol.49 , pp. 6614-6620
    • Pierra, C.1    Amador, A.2    Benzaria, S.3
  • 120
    • 62949195680 scopus 로고    scopus 로고
    • Robust antiviral efficacy upon administration of a nucleoside analog to hepatitis C virus-infected chimpanzees
    • Carroll SS, Ludmerer S, Handt L. Robust antiviral efficacy upon administration of a nucleoside analog to hepatitis C virus-infected chimpanzees. Antimicrob Agents Chemother 2009; 53: 926–9-34.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 926-934
    • Carroll, S.S.1    Ludmerer, S.2    Handt, L.3
  • 121
    • 84896823395 scopus 로고    scopus 로고
    • Multiple classes of antiviral agents exhibit in vitro activity against human rhinovirus type C
    • Mello C, Aguayo E, Rodriguez M. Multiple classes of antiviral agents exhibit in vitro activity against human rhinovirus type C. Antimicrob Agents Chemother 2014; 58: 1546–15-55.
    • (2014) Antimicrob Agents Chemother , vol.58 , pp. 1546-1555
    • Mello, C.1    Aguayo, E.2    Rodriguez, M.3
  • 122
    • 73949141554 scopus 로고    scopus 로고
    • An adenosine nucleoside inhibitor of dengue virus
    • Yin Z, Chen YL, Schul W. An adenosine nucleoside inhibitor of dengue virus. Proc Natl Acad Sci USA 2009; 106: 20435–2043-9.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20435-20439
    • Yin, Z.1    Chen, Y.L.2    Schul, W.3
  • 123
    • 77954955357 scopus 로고    scopus 로고
    • Biochemical characterization of the inhibition of the dengue virus RNA polymerase by beta-D-2'-ethynyl-7-deaza-adenosine triphosphate
    • Latour DR, Jekle A, Javanbakht H. Biochemical characterization of the inhibition of the dengue virus RNA polymerase by beta-D-2'-ethynyl-7-deaza-adenosine triphosphate. Antiviral Res 2010; 87: 213–2-22.
    • (2010) Antiviral Res , vol.87 , pp. 213-222
    • Latour, D.R.1    Jekle, A.2    Javanbakht, H.3
  • 124
    • 84908598870 scopus 로고    scopus 로고
    • An adenosine nucleoside analogue NITD008 inhibits EV71 proliferation
    • Shang L, Wang Y, Qing J. An adenosine nucleoside analogue NITD008 inhibits EV71 proliferation. Antiviral Res 2014; 112: 47–58.
    • (2014) Antiviral Res , vol.112 , pp. 47-58
    • Shang, L.1    Wang, Y.2    Qing, J.3
  • 125
    • 84907440604 scopus 로고    scopus 로고
    • Inhibition of enterovirus 71 by adenosine analog NITD008
    • Deng CL, Yeo H, Ye HQ. Inhibition of enterovirus 71 by adenosine analog NITD008. J Virol 2014; 88: 11915–119-23.
    • (2014) J Virol , vol.88 , pp. 11915-11923
    • Deng, C.L.1    Yeo, H.2    Ye, H.Q.3
  • 126
    • 33746613974 scopus 로고    scopus 로고
    • Fluorinated nucleosides as antiviral and antitumor agents
    • and
    • Meng WD, andQing FL., Fluorinated nucleosides as antiviral and antitumor agents. Curr Top Med Chem 2006; 6: 1499–1-528.
    • (2006) Curr Top Med Chem , vol.6 , pp. 1499-1528
    • Meng, W.D.1    Qing, F.L.2
  • 127
    • 0027400040 scopus 로고
    • Purine 2'-deoxy-2'-fluororibosides as antiinfluenza virus agents
    • and
    • Tuttle JV, Tisdale M, andKrenitsky TA., Purine 2'-deoxy-2'-fluororibosides as antiinfluenza virus agents. J Med Chem 1993; 36: 119–1-25.
    • (1993) J Med Chem , vol.36 , pp. 119-125
    • Tuttle, J.V.1    Tisdale, M.2    Krenitsky, T.A.3
  • 128
    • 0028027404 scopus 로고
    • Efficacy of 2'-deoxy-2'-fluororibosides against influenza A and B viruses in ferrets
    • Jakeman KJ, Tisdale M, Russell S. Efficacy of 2'-deoxy-2'-fluororibosides against influenza A and B viruses in ferrets. Antimicrob Agents Chemother 1994; 38: 1864–186-7.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 1864-1867
    • Jakeman, K.J.1    Tisdale, M.2    Russell, S.3
  • 129
    • 0028846207 scopus 로고
    • Inhibition of influenza virus transcription by 2'-deoxy-2'-fluoroguanosine
    • Tisdale M, Ellis M, Klumpp K. Inhibition of influenza virus transcription by 2'-deoxy-2'-fluoroguanosine. Antimicrob Agents Chemother 1995; 39: 2454–245-8.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 2454-2458
    • Tisdale, M.1    Ellis, M.2    Klumpp, K.3
  • 130
    • 80054853586 scopus 로고    scopus 로고
    • In vitro and in vivo efficacy of fluorodeoxycytidine analogs against highly pathogenic avian influenza H5N1, seasonal, and pandemic H1N1 virus infections
    • Kumaki Y, Day CW, Smee DF. In vitro and in vivo efficacy of fluorodeoxycytidine analogs against highly pathogenic avian influenza H5N1, seasonal, and pandemic H1N1 virus infections. Antiviral Res 2011; 92: 329–3-40.
    • (2011) Antiviral Res , vol.92 , pp. 329-340
    • Kumaki, Y.1    Day, C.W.2    Smee, D.F.3
  • 131
    • 19544363065 scopus 로고    scopus 로고
    • Phosphorylation of ribavirin and viramidine by adenosine kinase and cytosolic 5'-nucleotidase II: Implications for ribavirin metabolism in erythrocytes
    • Wu JZ, Larson G, Walker H. Phosphorylation of ribavirin and viramidine by adenosine kinase and cytosolic 5'-nucleotidase II: Implications for ribavirin metabolism in erythrocytes. Antimicrob Agents Chemother 2005; 49: 2164–21-71.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 2164-2171
    • Wu, J.Z.1    Larson, G.2    Walker, H.3
  • 132
    • 13444261067 scopus 로고    scopus 로고
    • Synthesis and anti-viral activity of a series of D- and L-2'-deoxy-2'-fluororibonucleosides in the subgenomic HCV replicon system
    • Shi J, Du J, Ma T. Synthesis and anti-viral activity of a series of D- and L-2'-deoxy-2'-fluororibonucleosides in the subgenomic HCV replicon system. Bioorg Med Chem 2005; 13: 1641–16-52.
    • (2005) Bioorg Med Chem , vol.13 , pp. 1641-1652
    • Shi, J.1    Du, J.2    Ma, T.3
  • 133
    • 9144238660 scopus 로고    scopus 로고
    • Inhibition of the subgenomic hepatitis C virus replicon in huh-7 cells by 2'-deoxy-2'-fluorocytidine
    • Stuyver LJ, McBrayer TR, Whitaker T. Inhibition of the subgenomic hepatitis C virus replicon in huh-7 cells by 2'-deoxy-2'-fluorocytidine. Antimicrob Agents Chemother 2004; 48: 651–65-4.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 651-654
    • Stuyver, L.J.1    McBrayer, T.R.2    Whitaker, T.3
  • 134
    • 84903177093 scopus 로고    scopus 로고
    • Efficiency of incorporation and chain termination determines the inhibition potency of 2'-modified nucleotide analogs against hepatitis C virus polymerase
    • Fung A, Jin Z, Dyatkina N. Efficiency of incorporation and chain termination determines the inhibition potency of 2'-modified nucleotide analogs against hepatitis C virus polymerase. Antimicrob Agents Chemother 2014; 58: 3636–36-45.
    • (2014) Antimicrob Agents Chemother , vol.58 , pp. 3636-3645
    • Fung, A.1    Jin, Z.2    Dyatkina, N.3
  • 135
    • 0022003604 scopus 로고
    • The effect of 2'-fluoro-2'-deoxycytidine on herpes virus growth
    • Wohlrab F, Jamieson AT, Hay J. The effect of 2'-fluoro-2'-deoxycytidine on herpes virus growth. Biochim Biophys Acta 1985; 824: 233–2-42.
    • (1985) Biochim Biophys Acta , vol.824 , pp. 233-242
    • Wohlrab, F.1    Jamieson, A.T.2    Hay, J.3
  • 136
    • 0033954635 scopus 로고    scopus 로고
    • Polymerization of 2'-fluoro- and 2'-O-methyl-dNTPs by human DNA polymerase alpha, polymerase gamma, and primase
    • Richardson FC, Kuchta RD, Mazurkiewicz A. Polymerization of 2'-fluoro- and 2'-O-methyl-dNTPs by human DNA polymerase alpha, polymerase gamma, and primase. Biochem Pharmacol 2000; 59: 1045–10-52.
    • (2000) Biochem Pharmacol , vol.59 , pp. 1045-1052
    • Richardson, F.C.1    Kuchta, R.D.2    Mazurkiewicz, A.3
  • 137
    • 0032701241 scopus 로고    scopus 로고
    • An evaluation of the toxicities of 2'-fluorouridine and 2'-fluorocytidine-HCl in F344 rats and woodchucks (Marmota monax)
    • Richardson FC, Tennant BC, Meyer DJ. An evaluation of the toxicities of 2'-fluorouridine and 2'-fluorocytidine-HCl in F344 rats and woodchucks (Marmota monax). Toxicol Pathol 1999; 27: 607–6-17.
    • (1999) Toxicol Pathol , vol.27 , pp. 607-617
    • Richardson, F.C.1    Tennant, B.C.2    Meyer, D.J.3
  • 138
    • 0036211719 scopus 로고    scopus 로고
    • In vitro and in vivo activities of anti-influenza virus compound T-705
    • Furuta Y, Takahashi K, Fukuda Y. In vitro and in vivo activities of anti-influenza virus compound T-705. Antimicrob Agents Chemother 2002; 46: 977–9-81.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 977-981
    • Furuta, Y.1    Takahashi, K.2    Fukuda, Y.3
  • 139
    • 33847688459 scopus 로고    scopus 로고
    • Efficacy of orally administered T-705 on lethal avian influenza A (H5N1) virus infections in mice
    • Sidwell RW, Barnard DL, Day CW. Efficacy of orally administered T-705 on lethal avian influenza A (H5N1) virus infections in mice. Antimicrob Agents Chemother 2007; 51: 845–8-51.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 845-851
    • Sidwell, R.W.1    Barnard, D.L.2    Day, C.W.3
  • 141
    • 64749093901 scopus 로고    scopus 로고
    • T-705 (favipiravir) and related compounds: Novel broad-spectrum inhibitors of RNA viral infections
    • Furuta Y, Takahashi K, Shiraki K. T-705 (favipiravir) and related compounds: Novel broad-spectrum inhibitors of RNA viral infections. Antiviral Res 2009; 82: 95–102.
    • (2009) Antiviral Res , vol.82 , pp. 95-102
    • Furuta, Y.1    Takahashi, K.2    Shiraki, K.3
  • 142
    • 84875107202 scopus 로고    scopus 로고
    • T-705 (Favipiravir) induces lethal mutagenesis in influenza A H1N1 viruses in vitro
    • et al.; 87: 3741–3751
    • Baranovich T, Wong SS, Armstrong J, et al. T-705 (Favipiravir) induces lethal mutagenesis in influenza A H1N1 viruses in vitro. J Virol 2013; 87: 3741–3751.
    • (2013) J Virol
    • Baranovich, T.1    Wong, S.S.2    Armstrong, J.3
  • 143
    • 84880006467 scopus 로고    scopus 로고
    • The ambiguous base-pairing and high substrate efficiency of T-705 (Favipiravir) Ribofuranosyl 5'-triphosphate towards influenza A virus polymerase
    • Jin Z, Smith LK, Rajwanshi VK. The ambiguous base-pairing and high substrate efficiency of T-705 (Favipiravir) Ribofuranosyl 5'-triphosphate towards influenza A virus polymerase. PLoS One 2013; 8: e68347.
    • (2013) PLoS One , vol.8 , pp. e68347
    • Jin, Z.1    Smith, L.K.2    Rajwanshi, V.K.3
  • 144
    • 84896129506 scopus 로고    scopus 로고
    • Successful treatment of advanced Ebola virus infection with T-705 (favipiravir) in a small animal model
    • Oestereich L, Lüdtke A, Wurr S. Successful treatment of advanced Ebola virus infection with T-705 (favipiravir) in a small animal model. Antiviral Res 2014; 105: 17–21.
    • (2014) Antiviral Res , vol.105 , pp. 17-21
    • Oestereich, L.1    Lüdtke, A.2    Wurr, S.3
  • 145
    • 84896692632 scopus 로고    scopus 로고
    • Post-exposure efficacy of Oral T-705 (Favipiravir) against inhalational Ebola virus infection in a mouse model
    • Smither SJ, Eastaugh LS, Steward JA. Post-exposure efficacy of Oral T-705 (Favipiravir) against inhalational Ebola virus infection in a mouse model. Antiviral Res 2014; 104: 153–15-5.
    • (2014) Antiviral Res , vol.104 , pp. 153-155
    • Smither, S.J.1    Eastaugh, L.S.2    Steward, J.A.3
  • 146
    • 56649102052 scopus 로고    scopus 로고
    • Treatment of late stage disease in a model of arenaviral hemorrhagic fever: T-705 efficacy and reduced toxicity suggests an alternative to ribavirin
    • Gowen BB, Smee DF, Wong MH. Treatment of late stage disease in a model of arenaviral hemorrhagic fever: T-705 efficacy and reduced toxicity suggests an alternative to ribavirin. PLoS One 2008; 3: e3725.
    • (2008) PLoS One , vol.3 , pp. e3725
    • Gowen, B.B.1    Smee, D.F.2    Wong, M.H.3
  • 147
    • 35948957769 scopus 로고    scopus 로고
    • In vitro and in vivo activities of T-705 against arenavirus and bunyavirus infections
    • Gowen BB, Wong MH, Jung KH. In vitro and in vivo activities of T-705 against arenavirus and bunyavirus infections. Antimicrob Agents Chemother 2007; 51: 3168–31-76.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 3168-3176
    • Gowen, B.B.1    Wong, M.H.2    Jung, K.H.3
  • 148
    • 77951297749 scopus 로고    scopus 로고
    • Efficacy of favipiravir (T-705) and T-1106 pyrazine derivatives in phlebovirus disease models
    • Gowen BB, Wong MH, Jung KH. Efficacy of favipiravir (T-705) and T-1106 pyrazine derivatives in phlebovirus disease models. Antiviral Res 2010; 86: 121–12-7.
    • (2010) Antiviral Res , vol.86 , pp. 121-127
    • Gowen, B.B.1    Wong, M.H.2    Jung, K.H.3
  • 149
    • 59749106534 scopus 로고    scopus 로고
    • Activity of T-705 in a hamster model of yellow fever virus infection in comparison with that of a chemically related compound, T-1106
    • Julander JG, Shafer K, Smee DF. Activity of T-705 in a hamster model of yellow fever virus infection in comparison with that of a chemically related compound, T-1106. Antimicrob Agents Chemother 2009; 53: 202–20-9.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 202-209
    • Julander, J.G.1    Shafer, K.2    Smee, D.F.3
  • 150
    • 64749095802 scopus 로고    scopus 로고
    • Effect of T-705 treatment on western equine encephalitis in a mouse model
    • Julander JG, Smee DF, Morrey JD. Effect of T-705 treatment on western equine encephalitis in a mouse model. Antiviral Res 2009; 82: 169–1-71.
    • (2009) Antiviral Res , vol.82 , pp. 169-171
    • Julander, J.G.1    Smee, D.F.2    Morrey, J.D.3
  • 151
    • 78751692774 scopus 로고    scopus 로고
    • T-705 (favipiravir) inhibition of arenavirus replication in cell culture
    • Mendenhall M, Russell A, Juelich T. T-705 (favipiravir) inhibition of arenavirus replication in cell culture. Antimicrob Agents Chemother 2011; 55: 782–78-7.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 782-787
    • Mendenhall, M.1    Russell, A.2    Juelich, T.3
  • 153
    • 84992111855 scopus 로고    scopus 로고
    • Lethal mutagenesis of hepatitis C virus induced by favipiravir
    • de Avila AI, Gallego I, Soria ME. Lethal mutagenesis of hepatitis C virus induced by favipiravir. PLoS One 2016; 11: e0164691.
    • (2016) PLoS One , vol.11 , pp. e0164691
    • de Avila, A.I.1    Gallego, I.2    Soria, M.E.3
  • 154
    • 85018651966 scopus 로고    scopus 로고
    • Structure-activity relationship analysis of mitochondrial toxicity caused by antiviral ribonucleoside analogs
    • Jin Z, Kinkade A, Behera I. Structure-activity relationship analysis of mitochondrial toxicity caused by antiviral ribonucleoside analogs. Antiviral Res 2017; 143: 151–1-61.
    • (2017) Antiviral Res , vol.143 , pp. 151-161
    • Jin, Z.1    Kinkade, A.2    Behera, I.3
  • 155
    • 84954503481 scopus 로고    scopus 로고
    • Biochemical evaluation of the inhibition properties of favipiravir and 2'-C-methyl-cytidine triphosphates against human and mouse norovirus RNA polymerases
    • Jin Z, Tucker K, Lin X. Biochemical evaluation of the inhibition properties of favipiravir and 2'-C-methyl-cytidine triphosphates against human and mouse norovirus RNA polymerases. Antimicrob Agents Chemother 2015; 59: 7504–75-16.
    • (2015) Antimicrob Agents Chemother , vol.59 , pp. 7504-7516
    • Jin, Z.1    Tucker, K.2    Lin, X.3
  • 156
    • 85017331237 scopus 로고    scopus 로고
    • Synthesis of T-705-ribonucleoside and T-705-ribonucleotide and studies of chemical stability
    • Huchting J, Winkler M, Nasser H. Synthesis of T-705-ribonucleoside and T-705-ribonucleotide and studies of chemical stability. ChemMedChem 2017; 12: 652–659.
    • (2017) ChemMedChem , vol.12 , Issue.9 , pp. 652-65
    • Huchting, J.1    Winkler, M.2    Nasser, H.3
  • 157
    • 84994812705 scopus 로고    scopus 로고
    • Distinct effects of T-705 (favipiravir) and ribavirin on influenza virus replication and viral RNA synthesis
    • Vanderlinden E, Vrancken B, Van Houdt J. Distinct effects of T-705 (favipiravir) and ribavirin on influenza virus replication and viral RNA synthesis. Antimicrob Agents Chemother 2016; 60: 6679–66-91.
    • (2016) Antimicrob Agents Chemother , vol.60 , pp. 6679-6691
    • Vanderlinden, E.1    Vrancken, B.2    Van Houdt, J.3
  • 158
    • 84923873501 scopus 로고    scopus 로고
    • Discovery of 4'-chloromethyl-2'-deoxy-3',5'-di-O-isobutyryl-2'-fluorocytidine (ALS-8176), a first-in-class RSV polymerase inhibitor for treatment of human respiratory syncytial virus infection
    • Wang G, Deval J, Hong J. Discovery of 4'-chloromethyl-2'-deoxy-3',5'-di-O-isobutyryl-2'-fluorocytidine (ALS-8176), a first-in-class RSV polymerase inhibitor for treatment of human respiratory syncytial virus infection. J Med Chem 2015; 58: 1862–18-78.
    • (2015) J Med Chem , vol.58 , pp. 1862-1878
    • Wang, G.1    Deval, J.2    Hong, J.3
  • 159
    • 84936741527 scopus 로고    scopus 로고
    • Molecular basis for the selective inhibition of respiratory syncytial virus RNA polymerase by 2'-fluoro-4'-chloromethyl-cytidine triphosphate
    • Deval J, Hong J, Wang G. Molecular basis for the selective inhibition of respiratory syncytial virus RNA polymerase by 2'-fluoro-4'-chloromethyl-cytidine triphosphate. PLoS Pathog 2015; 11: e1004995.
    • (2015) PLoS Pathog , vol.11 , pp. e1004995
    • Deval, J.1    Hong, J.2    Wang, G.3
  • 160
    • 85064212914 scopus 로고    scopus 로고
    • Development of ALS-8112/ALS-8176 as an effective replication inhibitor of human metapneumovirus. In:, Atlanta, 2100–25 May 2017, Abstract 160
    • Meng JDJ, Jekle A, andSymons J., Development of ALS-8112/ALS-8176 as an effective replication inhibitor of human metapneumovirus. In: 30th ICAR - International society for antiviral research, Atlanta, 2100–25 May 2017, Abstract 160.
    • Meng, J.D.J.1    Jekle, A.2    Symons, J.3
  • 161
    • 84947719880 scopus 로고    scopus 로고
    • Activity of oral ALS-008176 in a respiratory syncytial virus challenge study
    • DeVincenzo JP, McClure MW, Symons JA. Activity of oral ALS-008176 in a respiratory syncytial virus challenge study. N Engl J Med 2015; 373: 2048–20-58.
    • (2015) N Engl J Med , vol.373 , pp. 2048-2058
    • DeVincenzo, J.P.1    McClure, M.W.2    Symons, J.A.3
  • 162
    • 84982234143 scopus 로고    scopus 로고
    • Therapeutic efficacy of the small molecule GS-5734 against Ebola virus in rhesus monkeys
    • Warren TK, Jordan R, Lo MK. Therapeutic efficacy of the small molecule GS-5734 against Ebola virus in rhesus monkeys. Nature 2016; 531: 381–38-5.
    • (2016) Nature , vol.531 , pp. 38-45
    • Warren, T.K.1    Jordan, R.2    Lo, M.K.3
  • 163
    • 85014764670 scopus 로고    scopus 로고
    • GS-5734 and its parent nucleoside analog inhibit filo-, pneumo-, and paramyxoviruses
    • Lo MK, Jordan R, Arvey A. GS-5734 and its parent nucleoside analog inhibit filo-, pneumo-, and paramyxoviruses. Sci Reports 2017; 7: 43395.
    • (2017) Sci Reports , vol.7 , pp. 43395
    • Lo, M.K.1    Jordan, R.2    Arvey, A.3
  • 164
    • 85015071018 scopus 로고    scopus 로고
    • Discovery and synthesis of a phosphoramidate prodrug of a pyrrolo[2,1-f][triazin-4-amino] adenine C-nucleoside (GS-5734) for the treatment of Ebola and emerging viruses
    • Siegel D, Hui HC, Doerffler E. Discovery and synthesis of a phosphoramidate prodrug of a pyrrolo[2,1-f][triazin-4-amino] adenine C-nucleoside (GS-5734) for the treatment of Ebola and emerging viruses. J Med Chem 2017; 60: 1648–16-61.
    • (2017) J Med Chem , vol.60 , pp. 1648-1661
    • Siegel, D.1    Hui, H.C.2    Doerffler, E.3
  • 165
    • 84896905217 scopus 로고    scopus 로고
    • Inhibition of hepatitis C virus replication by GS-6620, a potent C-nucleoside monophosphate prodrug
    • Feng JY, Cheng G, Perry J. Inhibition of hepatitis C virus replication by GS-6620, a potent C-nucleoside monophosphate prodrug. Antimicrob Agents Chemother 2014; 58: 1930–19-42.
    • (2014) Antimicrob Agents Chemother , vol.58 , pp. 19-42
    • Feng, J.Y.1    Cheng, G.2    Perry, J.3
  • 166
    • 84896269353 scopus 로고    scopus 로고
    • Discovery of the first C-nucleoside HCV polymerase inhibitor (GS-6620) with demonstrated antiviral response in HCV infected patients
    • Cho A, Zhang L, Xu J. Discovery of the first C-nucleoside HCV polymerase inhibitor (GS-6620) with demonstrated antiviral response in HCV infected patients. J Med Chem 2014; 57: 1812–18-25.
    • (2014) J Med Chem , vol.57 , pp. 1812-1825
    • Cho, A.1    Zhang, L.2    Xu, J.3
  • 167
    • 84979533002 scopus 로고    scopus 로고
    • Late Ebola virus relapse causing meningoencephalitis: a case report
    • Jacobs M, Rodger A, Bell DJ. Late Ebola virus relapse causing meningoencephalitis: a case report. Lancet 2016; 388: 498–503.
    • (2016) Lancet , vol.388 , pp. 498-503
    • Jacobs, M.1    Rodger, A.2    Bell, D.J.3
  • 168
    • 85017391369 scopus 로고    scopus 로고
    • First newborn baby to receive experimental therapies survives Ebola virus disease
    • Dornemann J, Burzio C, Ronsse A, First newborn baby to receive experimental therapies survives Ebola virus disease. J Infect Dis 2017; 215: 171–17-4.
    • (2017) J Infect Dis , vol.215 , pp. 171-174
    • Dornemann, J.1    Burzio, C.2    Ronsse, A.3
  • 169
    • 85021671152 scopus 로고    scopus 로고
    • Broad-spectrum antiviral GS-5734 inhibits both epidemic and zoonotic coronaviruses
    • et al
    • Sheahan TP, Sims AC, Graham RL, et al. Broad-spectrum antiviral GS-5734 inhibits both epidemic and zoonotic coronaviruses. Sci Transl Med 2017; 9: eaal3653.
    • (2017) Sci Transl Med
    • Sheahan, T.P.1    Sims, A.C.2    Graham, R.L.3
  • 170
    • 85064194446 scopus 로고    scopus 로고
    • The nucleoside prodrug GS-5734 inhibits multiple coronaviruses and selects for resistance mutations the RNA-dependent RNA polymerase that are associated with a decrease viral replication fitness. In:, Atlanta, 21–25 May, Abstract 155
    • Agostini MAE, Lu X, Sims A. The nucleoside prodrug GS-5734 inhibits multiple coronaviruses and selects for resistance mutations in the RNA-dependent RNA polymerase that are associated with a decrease in viral replication fitness. In: 30th ICAR - International society for antiviral research, Atlanta, 21–25 May 2017, Abstract 155.
    • (2017)
    • Agostini, M.A.E.1    Lu, X.2    Sims, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.