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Volumn 7, Issue 7, 2015, Pages 3974-3994

Using the hepatitis C virus RNA-dependent RNA polymerase as a model to understand viral polymerase structure, function and dynamics

Author keywords

Conformations; Flaviviridae; Positive strand RNA viruses

Indexed keywords

NONNUCLEOSIDE REVERSE TRANSCRIPTASE INHIBITOR; NONSTRUCTURAL PROTEIN 5B; RNA DIRECTED RNA POLYMERASE; VIRUS ENZYME; VIRUS RNA; NS-5 PROTEIN, HEPATITIS C VIRUS; VIRAL PROTEIN;

EID: 84937422070     PISSN: None     EISSN: 19994915     Source Type: Journal    
DOI: 10.3390/v7072808     Document Type: Article
Times cited : (49)

References (74)
  • 2
    • 33750285215 scopus 로고    scopus 로고
    • Structure and function of RNA replication
    • [CrossRef] [PubMed]
    • Ortin, J.; Parra, F. Structure and function of RNA replication. Annu. Rev. Microbiol. 2006, 60, 305–326. [CrossRef] [PubMed]
    • (2006) Annu. Rev. Microbiol , vol.60 , pp. 305-326
    • Ortin, J.1    Parra, F.2
  • 3
    • 34247113349 scopus 로고    scopus 로고
    • Structure and function of flavivirus ns5 methyltransferase
    • [CrossRef] [PubMed]
    • Zhou, Y.; Ray, D.; Zhao, Y.; Dong, H.; Ren, S.; Li, Z.; Guo, Y.; Bernard, K.A.; Shi, P.-Y.; Li, H.; et al. Structure and function of flavivirus ns5 methyltransferase. J. Virol. 2007, 81, 3891–3903. [CrossRef] [PubMed]
    • (2007) J. Virol , vol.81 , pp. 3891-3903
    • Zhou, Y.1    Ray, D.2    Zhao, Y.3    Dong, H.4    Ren, S.5    Li, Z.6    Guo, Y.7    Bernard, K.A.8    Shi, P.-Y.9    Li, H.10
  • 4
    • 84863394556 scopus 로고    scopus 로고
    • Crystal structures of the reverse transcriptase-associated ribonuclease h domain of xenotropic murine leukemia-virus related virus
    • [CrossRef] [PubMed]
    • Zhou, D.; Chung, S.; Miller, M.; Grice, S.F.J.L.; Wlodawer, A. Crystal structures of the reverse transcriptase-associated ribonuclease h domain of xenotropic murine leukemia-virus related virus. J. Struct. Biol. 2012, 177, 638–645. [CrossRef] [PubMed]
    • (2012) J. Struct. Biol , vol.177 , pp. 638-645
    • Zhou, D.1    Chung, S.2    Miller, M.3    Grice, S.4    Wlodawer, A.5
  • 5
    • 0031904908 scopus 로고    scopus 로고
    • Evolution of viral DNA-dependent DNA polymerases
    • [CrossRef] [PubMed]
    • Knopf, C. Evolution of viral DNA-dependent DNA polymerases. Virus Genes 1998, 16, 47–58. [CrossRef] [PubMed]
    • (1998) Virus Genes , vol.16 , pp. 47-58
    • Knopf, C.1
  • 6
    • 0015114139 scopus 로고
    • Expression of animal virus genomes
    • [PubMed]
    • Baltimore, D. Expression of animal virus genomes. Bacteriol. Rev. 1971, 35, 235–241. [PubMed]
    • (1971) Bacteriol. Rev , vol.35 , pp. 235-241
    • Baltimore, D.1
  • 7
    • 84876101150 scopus 로고    scopus 로고
    • Structural organization of viral RNA-dependent RNA polymerases
    • [CrossRef] [PubMed]
    • Shatskaya, G.S. Structural organization of viral RNA-dependent RNA polymerases. Biochemistry 2013, 78, 231–235. [CrossRef] [PubMed]
    • (2013) Biochemistry , vol.78 , pp. 231-235
    • Shatskaya, G.S.1
  • 8
    • 0021984004 scopus 로고
    • Structure of large fragment of Escherichia coli DNA polymerase i complexed with dtmp
    • [CrossRef] [PubMed]
    • Ollis, D.L.; Brick, P.; Hamlin, R.; Xuong, N.G.; Steitz, T.A. Structure of large fragment of Escherichia coli DNA polymerase i complexed with dtmp. Nature 1985, 313, 762–766. [CrossRef] [PubMed]
    • (1985) Nature , vol.313 , pp. 762-766
    • Ollis, D.L.1    Brick, P.2    Hamlin, R.3    Xuong, N.G.4    Steitz, T.A.5
  • 9
    • 84879176096 scopus 로고    scopus 로고
    • RNA synthetic mechanisms employed by diverse families of RNA viruses
    • [CrossRef] [PubMed]
    • McDonald, S.M. RNA synthetic mechanisms employed by diverse families of RNA viruses. WIREs RNA 2013, 4, 351–367. [CrossRef] [PubMed]
    • (2013) Wires RNA , vol.4 , pp. 351-367
    • McDonald, S.M.1
  • 10
    • 84920109354 scopus 로고    scopus 로고
    • RNA virus polymerases
    • Cameron, C., Gotte, M., Raney, K.D.,, Springer Science: New York, NY, USA
    • Ferrer-Orta, C.; Verdaguer, N. RNA virus polymerases. In Viral Genome Replication; Cameron, C., Gotte, M., Raney, K.D., Eds.; Springer Science: New York, NY, USA, 2009.
    • (2009) Viral Genome Replication
    • Ferrer-Orta, C.1    Verdaguer, N.2
  • 11
    • 0031028380 scopus 로고    scopus 로고
    • Conferring RNA polymerase activity to a DNA polymerase: A single residue in reverse transcriptase controls substrate selection
    • [CrossRef] [PubMed]
    • Gao, G.; Orlova, M.; Georgiadis, M.M.; Hendrickson, W.A.; Goff, S.P. Conferring RNA polymerase activity to a DNA polymerase: A single residue in reverse transcriptase controls substrate selection. Proc. Natl. Acad. Sci. USA 1997, 94, 407–411. [CrossRef] [PubMed]
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 407-411
    • Gao, G.1    Orlova, M.2    Georgiadis, M.M.3    Hendrickson, W.A.4    Goff, S.P.5
  • 12
    • 70549114081 scopus 로고    scopus 로고
    • Dynamics: The missing link between structure and function of the viral RNA-dependent RNA polymerase
    • [CrossRef] [PubMed]
    • Cameron, C.E.; Moustafa, I.M.; Arnold, J.J. Dynamics: The missing link between structure and function of the viral RNA-dependent RNA polymerase? Curr. Opin. Struct. Biol. 2009, 19, 768–774. [CrossRef] [PubMed]
    • (2009) Curr. Opin. Struct. Biol , vol.19 , pp. 768-774
    • Cameron, C.E.1    Moustafa, I.M.2    Arnold, J.J.3
  • 14
    • 84908027496 scopus 로고    scopus 로고
    • Closed-handed affair: Positive-strand RNA virus polymerases
    • [CrossRef]
    • Subissi, L.; Decroly, E.; Selisko, B.; Canard, B.; Imbert1, I. A closed-handed affair: Positive-strand RNA virus polymerases. Future Virol. 2014, 9, 769–784. [CrossRef]
    • (2014) Future Virol , vol.9 , pp. 769-784
    • Subissi, L.1    Decroly, E.2    Selisko, B.3    Canard, B.4    Imbert1, I.A.5
  • 15
    • 79958744018 scopus 로고    scopus 로고
    • Molecular dynamics simulations of viral RNA polymerases link conserved and correlated motions of functional elements to fidelity
    • [CrossRef] [PubMed]
    • Moustafa, I.M.; Shen, H.; Morton, B.; Colina, C.M.; Cameron, C.E. Molecular dynamics simulations of viral RNA polymerases link conserved and correlated motions of functional elements to fidelity. J. Mol. Biol. 2011, 410, 159–181. [CrossRef] [PubMed]
    • (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
  • 16
    • 84871094298 scopus 로고    scopus 로고
    • Thumb inhibitor binding eliminates functionally important dynamics in the hepatitis c virus RNA polymerase
    • [CrossRef] [PubMed]
    • Davis, B.; Thorpe, I.F. Thumb inhibitor binding eliminates functionally important dynamics in the hepatitis c virus RNA polymerase. Proteins Struct. Funct. Bioinform. 2013, 81, 40–52. [CrossRef] [PubMed]
    • (2013) Proteins Struct. Funct. Bioinform , vol.81 , pp. 40-52
    • Davis, B.1    Thorpe, I.F.2
  • 17
    • 84937479210 scopus 로고    scopus 로고
    • International Committee on Taxonomy of Viruses, accessed on February 15,2015
    • International Committee on Taxonomy of Viruses. Available online: http://www.Ictvonline.Org (accessed on February 15,2015).
  • 18
    • 70450211764 scopus 로고    scopus 로고
    • Potential targets and their relevant inhibitors in anti-influenza fields
    • [CrossRef] [PubMed]
    • Gong, J.; Fang, H.; Li, M.; Liu, Y.; Yang, K.; Xu, W. Potential targets and their relevant inhibitors in anti-influenza fields. Curr. Med. Chem. 2009, 16, 3716–3739. [CrossRef] [PubMed]
    • (2009) Curr. Med. Chem , vol.16 , pp. 3716-3739
    • Gong, J.1    Fang, H.2    Li, M.3    Liu, Y.4    Yang, K.5    Xu, W.6
  • 20
    • 64649097038 scopus 로고    scopus 로고
    • Composition and three-dimensional architecture of the dengue virus replication and assembly sites
    • [CrossRef] [PubMed]
    • Welsch, S.; Miller, S.; Romero-Brey, I. Composition and three-dimensional architecture of the dengue virus replication and assembly sites. Cell Host Microbe 2009, 5, 365–375. [CrossRef] [PubMed]
    • (2009) Cell Host Microbe , vol.5 , pp. 365-375
    • Welsch, S.1    Miller, S.2    Romero-Brey, I.3
  • 21
    • 77953280422 scopus 로고    scopus 로고
    • Viral reorganization of the secretory pathway generates distinct organelles for RNA replication
    • [CrossRef] [PubMed]
    • Hsu, N.Y.; Ilnytska, O.; Belov, G. Viral reorganization of the secretory pathway generates distinct organelles for RNA replication. Cell 2010, 141, 799–811. [CrossRef] [PubMed]
    • (2010) Cell , vol.141 , pp. 799-811
    • Hsu, N.Y.1    Ilnytska, O.2    Belov, G.3
  • 22
    • 4444241621 scopus 로고    scopus 로고
    • Hepatitis viruses
    • Baron, S.,, The University of Texas Medical Branch: Galveston, TX, USA
    • Zuckerman, A.J. Hepatitis viruses. In Medical Microbiology; Baron, S., Ed.; The University of Texas Medical Branch: Galveston, TX, USA, 1996.
    • (1996) Medical Microbiology
    • Zuckerman, A.J.1
  • 23
    • 0031571638 scopus 로고    scopus 로고
    • Structure of the RNA-dependent RNA polymerase of poliovirus
    • [CrossRef]
    • Hansen, J.L.; Long, A.M.; Schultz, S.C. Structure of the RNA-dependent RNA polymerase of poliovirus. Structure 1997, 5, 1109–1122. [CrossRef]
    • (1997) Structure , vol.5 , pp. 1109-1122
    • Hansen, J.L.1    Long, A.M.2    Schultz, S.C.3
  • 24
    • 84887197508 scopus 로고    scopus 로고
    • Hepatitis C virus genome replication
    • Cameron, C., Gotte, M., Raney, K.D., Springer Science: New York, NY, USA
    • Lindenbach, B.D.; Tellinghuisen, T.L. Hepatitis C virus genome replication. In Viral Genome Replication; Cameron, C., Gotte, M., Raney, K.D., Eds.; Springer Science: New York, NY, USA, 2009.
    • (2009) Viral Genome Replication
    • Lindenbach, B.D.1    Tellinghuisen, T.L.2
  • 26
    • 7144227111 scopus 로고
    • RNA-dependent RNA polymerase from healthy tomato leaf tissue
    • [CrossRef]
    • Boege, F.; Heinz, L.S. RNA-dependent RNA polymerase from healthy tomato leaf tissue. FEBS Lett. 1980, 121, 91–96. [CrossRef]
    • (1980) FEBS Lett , vol.121 , pp. 91-96
    • Boege, F.1    Heinz, L.S.2
  • 27
    • 0033551328 scopus 로고    scopus 로고
    • Gene silencing in neurospora crassa requires a protein homologous to RNA-dependent RNA polymerase
    • [PubMed]
    • Cogoni. C.; Macino, G. Gene silencing in neurospora crassa requires a protein homologous to RNA-dependent RNA polymerase. Nature 1999, 399, 166–169. [PubMed]
    • (1999) Nature , vol.399 , pp. 166-169
    • Cogoni, C.1    Macino, G.2
  • 28
    • 0034708215 scopus 로고    scopus 로고
    • Ego-1 is related to RNA-directed RNA polymerase and functions in germ-line development and RNA interference in c
    • [CrossRef]
    • Smardon, A.; Spoerke, J.M.; Stacey, S.C.; Klein, M.E.; Mackin, N.; Maine, E.M. Ego-1 is related to RNA-directed RNA polymerase and functions in germ-line development and RNA interference in c. Elegans. Curr. Biol. 2000, 10, 169–178. [CrossRef]
    • (2000) Elegans. Curr. Biol , vol.10 , pp. 169-178
    • Smardon, A.1    Spoerke, J.M.2    Stacey, S.C.3    Klein, M.E.4    Mackin, N.5    Maine, E.M.6
  • 29
    • 79955441522 scopus 로고    scopus 로고
    • RNA-dependent RNA polymerases in RNA silencing
    • [CrossRef] [PubMed]
    • Maida, Y.; Masutomi, K. RNA-dependent RNA polymerases in RNA silencing. Biol. Chem. 2011, 392, 299–304. [CrossRef] [PubMed]
    • (2011) Biol. Chem , vol.392 , pp. 299-304
    • Maida, Y.1    Masutomi, K.2
  • 30
    • 33745768604 scopus 로고    scopus 로고
    • Protein-primed and de novo initiation of RNA synthesis by norovirus 3dpol
    • [CrossRef] [PubMed]
    • Rohayem, J.; Robel, I.; Jager, K.; Scheffler, U.; Rudolph, W. Protein-primed and de novo initiation of RNA synthesis by norovirus 3dpol. J. Virol. 2006, 80, 7060–7069. [CrossRef] [PubMed]
    • (2006) J. Virol , vol.80 , pp. 7060-7069
    • Rohayem, J.1    Robel, I.2    Jager, K.3    Scheffler, U.4    Rudolph, W.5
  • 31
    • 31044446937 scopus 로고    scopus 로고
    • Recombinant viral rdrps can initiate RNA synthesis from circular templates
    • [CrossRef] [PubMed]
    • Ranjith-Kumar, C.T.; Kao, C.C. Recombinant viral rdrps can initiate RNA synthesis from circular templates. RNA 2006, 12, 303–312. [CrossRef] [PubMed]
    • (2006) RNA , vol.12 , pp. 303-312
    • Ranjith-Kumar, C.T.1    Kao, C.C.2
  • 32
    • 0033989278 scopus 로고    scopus 로고
    • De novo initiation of RNA synthesis by the RNA-dependent RNA polymerase (Ns5b) of hepatitis C virus
    • [CrossRef] [PubMed]
    • Luo, G.; Hamatake, R.K.; Mathis, D.M.; Racela, J.; Rigat, K.L.; Lemm, J.; Colonno, R.J. De novo initiation of RNA synthesis by the RNA-dependent RNA polymerase (ns5b) of hepatitis C virus. J. Virol. 2000, 74, 851–863. [CrossRef] [PubMed]
    • (2000) J. Virol , vol.74 , pp. 851-863
    • Luo, G.1    Hamatake, R.K.2    Mathis, D.M.3    Racela, J.4    Rigat, K.L.5    Lemm, J.6    Colonno, R.J.7
  • 33
    • 0033524332 scopus 로고    scopus 로고
    • De novo initiation of RNA synthesis by a recombinant flaviviridae RNA-dependent RNA polymerase
    • [CrossRef] [PubMed]
    • Kao, C.C.; Vecchio, A.M.D.; Zhong, W. De novo initiation of RNA synthesis by a recombinant flaviviridae RNA-dependent RNA polymerase. Virology 1999, 253, 1–7. [CrossRef] [PubMed]
    • (1999) Virology , vol.253 , pp. 1-7
    • Kao, C.C.1    Vecchio, A.2    Zhong, W.3
  • 34
    • 77958464322 scopus 로고    scopus 로고
    • Further insights into the roles of GTP and the C terminus of the hepatitis C virus polymerase in the initiation of RNA synthesis
    • [CrossRef] [PubMed]
    • Harrus, D. Further insights into the roles of GTP and the C terminus of the hepatitis C virus polymerase in the initiation of RNA synthesis. J. Biol. Chem. 2010, 285, 32906–32918. [CrossRef] [PubMed]
    • (2010) J. Biol. Chem , vol.285 , pp. 32906-32918
    • Harrus, D.1
  • 35
    • 33747729605 scopus 로고    scopus 로고
    • Control of template positioning during de novo initiation of RNA synthesis by the bovine viral diarrhea virus NS5B polymerase
    • [CrossRef] [PubMed]
    • D’Abramo, C.M.; Deval, J.; Cameron, C.E.; Cellai, L.; Gotte, M. Control of template positioning during de novo initiation of RNA synthesis by the bovine viral diarrhea virus NS5B polymerase. J. Biol. Chem. 2006, 281, 24991–24998. [CrossRef] [PubMed]
    • (2006) J. Biol. Chem , vol.281 , pp. 24991-24998
    • D’abramo, C.M.1    Deval, J.2    Cameron, C.E.3    Cellai, L.4    Gotte, M.5
  • 36
    • 0036120573 scopus 로고    scopus 로고
    • Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides
    • [CrossRef] [PubMed]
    • Bressanelli, S. Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides. J. Virol. 2002, 76, 3482–3492. [CrossRef] [PubMed]
    • (2002) J. Virol , vol.76 , pp. 3482-3492
    • Bressanelli, S.1
  • 38
    • 2442677715 scopus 로고    scopus 로고
    • Initation of viral RNA-dependent RNA polymerization
    • [CrossRef] [PubMed]
    • Van Dijk, A.A.; Makeyev, E.V.; Bamford, D.H. Initation of viral RNA-dependent RNA polymerization. J. Gen. Virol. 2004, 85, 1077–1093. [CrossRef] [PubMed]
    • (2004) J. Gen. Virol , vol.85 , pp. 1077-1093
    • Van Dijk, A.A.1    Makeyev, E.V.2    Bamford, D.H.3
  • 39
    • 0032518374 scopus 로고    scopus 로고
    • A mechanism for all polymerases
    • [CrossRef] [PubMed]
    • Steitz, T. A mechanism for all polymerases. Nature 1998, 391, 231–232. [CrossRef] [PubMed]
    • (1998) Nature , vol.391 , pp. 231-232
    • Steitz, T.1
  • 41
    • 0025886466 scopus 로고
    • A constant rate of spontaneous mutation in DNA-based microbes
    • [CrossRef] [PubMed]
    • Drake, J.W. A constant rate of spontaneous mutation in DNA-based microbes. Proc. Natl. Acad. Sci. USA 1991, 88, 7160–7164. [CrossRef] [PubMed]
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7160-7164
    • Drake, J.W.1
  • 43
    • 34248365628 scopus 로고    scopus 로고
    • Identification of determinants involved in initatiation of hepatitis c virus RNA synthesis by using intergenotipic chimeras
    • [CrossRef] [PubMed]
    • Binder, M.; Quinckert, D.; Bochkarova, O.; Klein, R.; Kezmic, N.; Bartenschalager, R.; Lohmann, V. Identification of determinants involved in initatiation of hepatitis c virus RNA synthesis by using intergenotipic chimeras. J. Virol. 2007, 81, 5270–5283. [CrossRef] [PubMed]
    • (2007) J. Virol , vol.81 , pp. 5270-5283
    • Binder, M.1    Quinckert, D.2    Bochkarova, O.3    Klein, R.4    Kezmic, N.5    Bartenschalager, R.6    Lohmann, V.7
  • 44
    • 85017672438 scopus 로고    scopus 로고
    • Selection of 31 template bases and initatiting nucleotides by hepatitis c virus RNA by and ago2-miR-122 complex
    • Shim, J.H.; Larson, G.; Hong, J.Z. Selection of 31 template bases and initatiting nucleotides by hepatitis c virus RNA by and ago2-miR-122 complex. Proc. Natl. Acad. Sci. USA 2002, 109, 941–946.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 941-946
    • Shim, J.H.1    Larson, G.2    Hong, J.Z.3
  • 45
    • 23744436747 scopus 로고    scopus 로고
    • Crystal structures of the RNA-dependent RNA polymerase genotype 2A of hepatitis C virus reveal two conformations and suggest mechanisms of inhibition by non-nucleoside inhibitors
    • [CrossRef] [PubMed]
    • Biswal, B.K.; Cherney, M.M.; Wang, M.; Chan, L.; Yannopoulos, C.G.; Bilimoria, D.; Nicolas, O.; Bedard, J.; James, M.N. Crystal structures of the RNA-dependent RNA polymerase genotype 2A of hepatitis C virus reveal two conformations and suggest mechanisms of inhibition by non-nucleoside inhibitors. J. Biol. Chem. 2005, 280, 18202–18210. [CrossRef] [PubMed]
    • (2005) J. Biol. Chem , vol.280 , pp. 18202-18210
    • Biswal, B.K.1    Cherney, M.M.2    Wang, M.3    Chan, L.4    Yannopoulos, C.G.5    Bilimoria, D.6    Nicolas, O.7    Bedard, J.8    James, M.N.9
  • 46
    • 84864011029 scopus 로고    scopus 로고
    • Structure of hepatitis C virus polymerase in complex with primer- template RNA
    • [CrossRef] [PubMed]
    • Mosley, R.T. Structure of hepatitis C virus polymerase in complex with primer- template RNA. J. Virol. 2012, 86, 6503–6511. [CrossRef] [PubMed]
    • (2012) J. Virol , vol.86 , pp. 6503-6511
    • Mosley, R.T.1
  • 47
    • 84926431958 scopus 로고    scopus 로고
    • Allosteric inhibitors have distinct effects, but also common modes of action, in the hcv polymerase
    • [CrossRef] [PubMed]
    • Davis, B.C.; Brown, J.A.; Thorpe, I.F. Allosteric inhibitors have distinct effects, but also common modes of action, in the hcv polymerase. Biophys. J. 2015, 108, 1785–1795. [CrossRef] [PubMed]
    • (2015) Biophys. J , vol.108 , pp. 1785-1795
    • Davis, B.C.1    Brown, J.A.2    Thorpe, I.F.3
  • 48
    • 84895822138 scopus 로고    scopus 로고
    • Polymerases of hepatitis C viruses and flaviviruses: Structural and mechanistic insights and drug development
    • [CrossRef] [PubMed]
    • Caillet-Saguy, C.; Lim, S.P.; Shi, P.-Y.; Lescar, J.; Bressanelli, S. Polymerases of hepatitis C viruses and flaviviruses: Structural and mechanistic insights and drug development. Antivir. Res. 2014, 105, 8–16. [CrossRef] [PubMed]
    • (2014) Antivir. Res , vol.105 , pp. 8-16
    • Caillet-Saguy, C.1    Lim, S.P.2    Shi, P.-Y.3    Lescar, J.4    Bressanelli, S.5
  • 49
    • 1842481188 scopus 로고    scopus 로고
    • The structure of the RNA-dependent RNA polymerase from bovine viral diarrhea virus establishes the role of GTP in de novo initiation
    • [CrossRef] [PubMed]
    • Choi, K.H.; Groarke, J.M.; Young, D.C.; Kuhn, R.J.; Smith, J.L.; Pevear, D.C.; Rossmann, M.G. The structure of the RNA-dependent RNA polymerase from bovine viral diarrhea virus establishes the role of GTP in de novo initiation. Proc. Natl. Acad. Sci. USA 2004, 101, 4425–4430. [CrossRef] [PubMed]
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4425-4430
    • Choi, K.H.1    Groarke, J.M.2    Young, D.C.3    Kuhn, R.J.4    Smith, J.L.5    Pevear, D.C.6    Rossmann, M.G.7
  • 50
    • 26844566830 scopus 로고    scopus 로고
    • Structure and mechanism of DNA polymerases
    • [PubMed]
    • Rothwell, P.J.; Waksman, G. Structure and mechanism of DNA polymerases. Adv. Protein Chem. 2005, 71, 401–440. [PubMed]
    • (2005) Adv. Protein Chem , vol.71 , pp. 401-440
    • Rothwell, P.J.1    Waksman, G.2
  • 51
    • 0033080970 scopus 로고    scopus 로고
    • An open and closed case for all polymerases
    • [CrossRef]
    • Doublie, S.; Sawaya, M.R.; Ellenberger, T. An open and closed case for all polymerases. Structure 1999, 7, R31–R35. [CrossRef]
    • (1999) Structure , vol.7
    • Doublie, S.1    Sawaya, M.R.2    Ellenberger, T.3
  • 53
    • 84862696759 scopus 로고    scopus 로고
    • Rapid and strong antiviral activity of the non-nucleosidic NS5B polymerase inhibitor BI 207127 in combination with peginterferon 2a and ribavirin
    • [CrossRef] [PubMed]
    • Larrey, D.; Lohse, A.W.; de Ledinghen, V.; Trepo, C.; Gerlach, T.; Zarski, J.P.; Tran, A.; Mathurin, P.; Thimme, R.; Arasteh, K.; et al. Rapid and strong antiviral activity of the non-nucleosidic NS5B polymerase inhibitor BI 207127 in combination with peginterferon 2a and ribavirin. J. Hepatol. 2012, 57, 39–46. [CrossRef] [PubMed]
    • (2012) J. Hepatol , vol.57 , pp. 39-46
    • Larrey, D.1    Lohse, A.W.2    De Ledinghen, V.3    Trepo, C.4    Gerlach, T.5    Zarski, J.P.6    Tran, A.7    Mathurin, P.8    Thimme, R.9    Arasteh, K.10
  • 54
    • 78751620008 scopus 로고    scopus 로고
    • Virologic response rates following 4 weeks of filibuvir in combination with pegylated interferon -2a and ribavirin in chronically-infected HCV genotype-1 patients
    • Jacobson, I.; Pockros, P.J.; Lalezari, J.; Lawitz, E.; Rodriguez-Torres, M.; DeJesus, E.; Haas, F.; Martorell, C.; Pruitt, R.; Purohit, V.; et al. Virologic response rates following 4 weeks of filibuvir in combination with pegylated interferon -2a and ribavirin in chronically-infected HCV genotype-1 patients. J. Hepatol. 2010, 52, S465–S465.
    • (2010) J. Hepatol , vol.52
    • Jacobson, I.1    Pockros, P.J.2    Lalezari, J.3    Lawitz, E.4    Rodriguez-Torres, M.5    Dejesus, E.6    Haas, F.7    Martorell, C.8    Pruitt, R.9    Purohit, V.10
  • 55
    • 77954745283 scopus 로고    scopus 로고
    • Safety antiviral activity of the HCV non-nucleoside polymerase inhibitor VX-222 in treatment-naive genotype 1 HCV-infected patients
    • [CrossRef]
    • Rodriguez-Torres, M.; Lawitz, E.; Conway, B.; Kaita, K.; Sheikh, A.M.; Ghalib, R.; Adrover, R.; Cooper, C.; Silva, M.; Rosario, M.; et al. Safety antiviral activity of the HCV non-nucleoside polymerase inhibitor VX-222 in treatment-naive genotype 1 HCV-infected patients. J. Hepatol. 2010, 52, S14–S14. [CrossRef]
    • (2010) J. Hepatol , vol.52
    • Rodriguez-Torres, M.1    Lawitz, E.2    Conway, B.3    Kaita, K.4    Sheikh, A.M.5    Ghalib, R.6    Adrover, R.7    Cooper, C.8    Silva, M.9    Rosario, M.10
  • 56
    • 78751637124 scopus 로고    scopus 로고
    • Safety and antiviral activity of ana 598 in combination with pegylated interferon-2a plus ribavirin in treatment-naive genotype 1 chronic HCV patients
    • [CrossRef]
    • Lawitz, E.; Rodriguez-Torres, M.; Rustgi, V.K. Safety and antiviral activity of ana 598 in combination with pegylated interferon-2a plus ribavirin in treatment-naive genotype 1 chronic HCV patients. J. Hepatol. 2010, 52, 334A–335A. [CrossRef]
    • (2010) J. Hepatol , vol.52
    • Lawitz, E.1    Rodriguez-Torres, M.2    Rustgi, V.K.3
  • 57
    • 79960747322 scopus 로고    scopus 로고
    • A phase 2b trial comparing 24 to 48 weeks treatment with tegobuvir (GS-9190)/PEG/RBV to 48 weeks treatment with PEG/RBV for chronic genotype 1 HCV infection
    • [CrossRef]
    • Lawitz, E.; Jacobson, I.; Godofsky, E.; Foster, G.R.; Flisiak, R.; Bennett, M.; Ryan, M.; Hinkle, J.; Simpson, J.; McHutchison, J.; et al. A phase 2b trial comparing 24 to 48 weeks treatment with tegobuvir (GS-9190)/PEG/RBV to 48 weeks treatment with PEG/RBV for chronic genotype 1 HCV infection. J. Hepatol. 2011, 54, S181–S181. [CrossRef]
    • (2011) J. Hepatol , vol.54
    • Lawitz, E.1    Jacobson, I.2    Godofsky, E.3    Foster, G.R.4    Flisiak, R.5    Bennett, M.6    Ryan, M.7    Hinkle, J.8    Simpson, J.9    McHutchison, J.10
  • 58
    • 84871814966 scopus 로고    scopus 로고
    • Nucleotide polymerase inhibi- tor sofosbuvir plus ribavirin for hepatitis C
    • [CrossRef] [PubMed]
    • Gane, E.J.; Stedman, C.A.; Hyland, R.H. Nucleotide polymerase inhibi- tor sofosbuvir plus ribavirin for hepatitis C. N. Engl. J. Med. 2013, 368, 34–44. [CrossRef] [PubMed]
    • (2013) N. Engl. J. Med , vol.368 , pp. 34-44
    • Gane, E.J.1    Stedman, C.A.2    Hyland, R.H.3
  • 59
    • 84863680448 scopus 로고    scopus 로고
    • Efficacy and safety of mericitabine in combination with PEG-IFN -2a/RBV in G1/4 treatment naive HCV patients: Final analysis from the propel study
    • [CrossRef]
    • Wedemeyer, H.; Jensen, D.; Herring, R., Efficacy and safety of mericitabine in combination with PEG-IFN -2a/RBV in G1/4 treatment naive HCV patients: Final analysis from the propel study. J. Hepatol. 2012, 56, S481–S482. [CrossRef]
    • (2012) J. Hepatol , vol.56
    • Wedemeyer, H.1    Jensen, D.2    Herring, R.3
  • 60
    • 84936818612 scopus 로고    scopus 로고
    • Dual allosteric inhibitors jointly modulate protein structure and dynamics in the hepatitis c virus polymerase
    • [CrossRef] [PubMed]
    • Brown, J.A.; Thorpe, I.F. Dual allosteric inhibitors jointly modulate protein structure and dynamics in the hepatitis c virus polymerase. Biochemistry 2015, 54, 4131–4141. [CrossRef] [PubMed]
    • (2015) Biochemistry , vol.54 , pp. 4131-4141
    • Brown, J.A.1    Thorpe, I.F.2
  • 61
    • 20944431615 scopus 로고    scopus 로고
    • Inhibitors of hcv ns5b polymerase. Part 1: Evaluation of the southern region of (2Z)-2-(benzoylamino)-3-(5-phenyl-2-furyl)acrylic acid
    • [CrossRef] [PubMed]
    • Pfefferkorn, J.A. Inhibitors of hcv ns5b polymerase. Part 1: Evaluation of the southern region of (2Z)-2-(benzoylamino)-3-(5-phenyl-2-furyl)acrylic acid. Bioorg. Med. Chem. Lett. 2005, 15, 2481–2486. [CrossRef] [PubMed]
    • (2005) Bioorg. Med. Chem. Lett , vol.15 , pp. 2481-2486
    • Pfefferkorn, J.A.1
  • 62
    • 0038322074 scopus 로고    scopus 로고
    • Non-nucleoside analogue inhibitors bind to an allosteric site on hcv ns5b polymerase. Crystal structures and mechanism of inhibition
    • [CrossRef] [PubMed]
    • Wang, M. Non-nucleoside analogue inhibitors bind to an allosteric site on hcv ns5b polymerase. Crystal structures and mechanism of inhibition. J. Biol. Chem. 2003, 278, 9489–9495. [CrossRef] [PubMed]
    • (2003) J. Biol. Chem , vol.278 , pp. 9489-9495
    • Wang, M.1
  • 63
    • 69049091942 scopus 로고    scopus 로고
    • Identification and biological evaluation of a series of 1H-benzo[de]isoquinoline-1,3(2H)-diones as hepatitis C virus NS5B polymerase inhibitors
    • [CrossRef] [PubMed]
    • Ontoria, J.M.; Rydberg, E.H.; Carfi, A. Identification and biological evaluation of a series of 1H-benzo[de]isoquinoline-1,3(2H)-diones as hepatitis C virus NS5B polymerase inhibitors. J. Med. Chem. 2009, 52, 5217–5227. [CrossRef] [PubMed]
    • (2009) J. Med. Chem , vol.52 , pp. 5217-5227
    • Ontoria, J.M.1    Rydberg, E.H.2    Carfi, A.3
  • 65
    • 77649106809 scopus 로고    scopus 로고
    • 1a/1bsubtype profiling of nonnucleoside polymerase inhibitors of hepatitis C virus
    • [CrossRef] [PubMed]
    • Nyanguile, O.; Devogelaere, B.; Fanning, G.C. 1a/1bsubtype profiling of nonnucleoside polymerase inhibitors of hepatitis C virus. J. Virol. 2010, 84, 2923–2934. [CrossRef] [PubMed]
    • (2010) J. Virol , vol.84 , pp. 2923-2934
    • Nyanguile, O.1    Devogelaere, B.2    Fanning, G.C.3
  • 66
    • 10744221995 scopus 로고    scopus 로고
    • Mechanism of action and antiviral activity of benzimidazole-based allosteric inhibitors of the hepatitis C virus RNA-dependent RNA polymerase
    • [CrossRef] [PubMed]
    • Tomei, L.; Altamura, S.; Migliaccio, G. Mechanism of action and antiviral activity of benzimidazole-based allosteric inhibitors of the hepatitis C virus RNA-dependent RNA polymerase. J. Virol. 2003, 77, 13225–13231. [CrossRef] [PubMed]
    • (2003) J. Virol , vol.77 , pp. 13225-13231
    • Tomei, L.1    Altamura, S.2    Migliaccio, G.3
  • 67
    • 84897488758 scopus 로고    scopus 로고
    • Structural and regulatory elements of HCV NS5B polymerase—B-Loop and C-terminal tail—Are required for activity of allosteric thumb site II inhibitors
    • [CrossRef] [PubMed]
    • Boyce, S.E.; Tirunagari, N.; Niedziela-Majka, A.; Perry, J.; Wong, M.; Kan, E.; Lagpacan, L.; Barauskas, O.; Hung, M.; Fenaux, M.; et al. Structural and regulatory elements of HCV NS5B polymerase—B-Loop and C-terminal tail—Are required for activity of allosteric thumb site II inhibitors. PLoS ONE 2014, 9, e84808. [CrossRef] [PubMed]
    • (2014) Plos ONE , vol.9
    • Boyce, S.E.1    Tirunagari, N.2    Niedziela-Majka, A.3    Perry, J.4    Wong, M.5    Kan, E.6    Lagpacan, L.7    Barauskas, O.8    Hung, M.9    Fenaux, M.10
  • 68
    • 33845251587 scopus 로고    scopus 로고
    • Molecular mechanism of a thumb domain hepatitis C virus nonnucleoside RNA-dependent RNA polymerase inhibitor
    • [CrossRef] [PubMed]
    • Howe, A.Y.; Cheng, H.; Thompson, I.; Chunduru, S.K.; Herrmann, S. Molecular mechanism of a thumb domain hepatitis C virus nonnucleoside RNA-dependent RNA polymerase inhibitor. Antimicrob. Agents Chemother. 2006, 50, 4103–4113. [CrossRef] [PubMed]
    • (2006) Antimicrob. Agents Chemother , vol.50 , pp. 4103-4113
    • Howe, A.Y.1    Cheng, H.2    Thompson, I.3    Chunduru, S.K.4    Herrmann, S.5
  • 69
    • 84880154850 scopus 로고    scopus 로고
    • Molecular simulations illuminate the role of regulatory components of the RNA polymerase from the hepatitis C virus in influencing protein structure and dynamics
    • [CrossRef] [PubMed]
    • Davis, B.; Thorpe, I.F. Molecular simulations illuminate the role of regulatory components of the RNA polymerase from the hepatitis C virus in influencing protein structure and dynamics. Biochemistry 2013, 52, 4541–4552. [CrossRef] [PubMed]
    • (2013) Biochemistry , vol.52 , pp. 4541-4552
    • Davis, B.1    Thorpe, I.F.2
  • 70
    • 84864378871 scopus 로고    scopus 로고
    • Preclinical characterization of JTK-853, a novel nonnucleoside inhibitor of the hepatitis C virus RNA-dependent RNA polymerase
    • [CrossRef] [PubMed]
    • Ando, I.; Adachi, T.; Ogura, N.; Toyonaga, Y.; Sugimoto, K. Preclinical characterization of JTK-853, a novel nonnucleoside inhibitor of the hepatitis C virus RNA-dependent RNA polymerase. Antimicrob. Agents Chemother. 2012, 56, 4250–4256. [CrossRef] [PubMed]
    • (2012) Antimicrob. Agents Chemother , vol.56 , pp. 4250-4256
    • Ando, I.1    Adachi, T.2    Ogura, N.3    Toyonaga, Y.4    Sugimoto, K.5
  • 71
    • 82555170294 scopus 로고    scopus 로고
    • An objective asessment of conformational variability in complexes of hepatitis C virus polymerase with non-nucleoside inhibitors
    • [CrossRef] [PubMed]
    • Caillet-Saguy, C.; Simister, P.C.; Bressanellli, S. An objective asessment of conformational variability in complexes of hepatitis C virus polymerase with non-nucleoside inhibitors. J. Mol. Biol. 2011, 414, 370–384. [CrossRef] [PubMed]
    • (2011) J. Mol. Biol , vol.414 , pp. 370-384
    • Caillet-Saguy, C.1    Simister, P.C.2    Bressanellli, S.3
  • 72
    • 67649303095 scopus 로고    scopus 로고
    • Recent advances in the development of NS5B polymerase inhibitors for the treatment of hepatitis C virus infection
    • [CrossRef] [PubMed]
    • Beaulieu, P. Recent advances in the development of NS5B polymerase inhibitors for the treatment of hepatitis C virus infection. Expert Opin. Ther. Pat. 2009, 49, 145–164. [CrossRef] [PubMed]
    • (2009) Expert Opin. Ther. Pat , vol.49 , pp. 145-164
    • Beaulieu, P.1
  • 73
    • 84922257981 scopus 로고    scopus 로고
    • Structure of influenza a polymerase bound to the viral RNA promoter
    • [CrossRef] [PubMed]
    • Pflug, A.; Guilligay, D.; Reich, S.; Cusack, S. Structure of influenza a polymerase bound to the viral RNA promoter. Nature 2014, 516, 355–360. [CrossRef] [PubMed]
    • (2014) Nature , vol.516 , pp. 355-360
    • Pflug, A.1    Guilligay, D.2    Reich, S.3    Cusack, S.4


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