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Volumn 234, Issue , 2017, Pages 4-20

Picornaviral polymerase structure, function, and fidelity modulation

Author keywords

Picornavirus; Polymerase; Positive strand RNA virus; RNA dependent RNA polymerase; Structure

Indexed keywords

LIVE VACCINE; POLYPROTEIN; RNA DIRECTED RNA POLYMERASE; TAQ POLYMERASE; VIRUS VACCINE; PROTEIN BINDING; VIRAL PROTEIN; VIRUS RNA;

EID: 85011967206     PISSN: 01681702     EISSN: 18727492     Source Type: Journal    
DOI: 10.1016/j.virusres.2017.01.026     Document Type: Review
Times cited : (67)

References (94)
  • 1
    • 77958122066 scopus 로고    scopus 로고
    • A multi-step process of viral adaptation to a mutagenic nucleoside analogue by modulation of transition types leads to extinction-escape
    • Agudo, R., Ferrer-Orta, C., Arias, A., de la Higuera, I., Perales, C., Perez-Luque, R., Verdaguer, N., Domingo, E., A multi-step process of viral adaptation to a mutagenic nucleoside analogue by modulation of transition types leads to extinction-escape. PLoS Pathog., 6, 2010, e1001072.
    • (2010) PLoS Pathog. , vol.6 , pp. e1001072
    • Agudo, R.1    Ferrer-Orta, C.2    Arias, A.3    de la Higuera, I.4    Perales, C.5    Perez-Luque, R.6    Verdaguer, N.7    Domingo, E.8
  • 2
    • 84937511310 scopus 로고    scopus 로고
    • Viral quasispecies
    • Andino, R., Domingo, E., Viral quasispecies. Virology 479–480 (2015), 46–51.
    • (2015) Virology , vol.479-480 , pp. 46-51
    • Andino, R.1    Domingo, E.2
  • 3
    • 57349131683 scopus 로고    scopus 로고
    • Determinants of RNA-dependent RNA polymerase (in)fidelity revealed by kinetic analysis of the polymerase encoded by a foot-and-mouth disease virus mutant with reduced sensitivity to ribavirin
    • Arias, A., Arnold, J.J., Sierra, M., Smidansky, E.D., Domingo, E., Cameron, C.E., Determinants of RNA-dependent RNA polymerase (in)fidelity revealed by kinetic analysis of the polymerase encoded by a foot-and-mouth disease virus mutant with reduced sensitivity to ribavirin. J. Virol. 82 (2008), 12346–12355.
    • (2008) J. Virol. , vol.82 , pp. 12346-12355
    • Arias, A.1    Arnold, J.J.2    Sierra, M.3    Smidansky, E.D.4    Domingo, E.5    Cameron, C.E.6
  • 4
    • 0034090927 scopus 로고    scopus 로고
    • Poliovirus RNA-dependent RNA polymerase (3D(pol)). Assembly of stable, elongation-competent complexes by using a symmetrical primer-template substrate (sym/sub)
    • Arnold, J.J., Cameron, C.E., Poliovirus RNA-dependent RNA polymerase (3D(pol)). Assembly of stable, elongation-competent complexes by using a symmetrical primer-template substrate (sym/sub). J. Biol. Chem. 275 (2000), 5329–5336.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5329-5336
    • Arnold, J.J.1    Cameron, C.E.2
  • 5
    • 2442584664 scopus 로고    scopus 로고
    • Poliovirus RNA-dependent RNA polymerase (3Dpol): pre-steady-state kinetic analysis of ribonucleotide incorporation in the presence of Mg2+
    • Arnold, J.J., Cameron, C.E., Poliovirus RNA-dependent RNA polymerase (3Dpol): pre-steady-state kinetic analysis of ribonucleotide incorporation in the presence of Mg2+. Biochemistry 43 (2004), 5126–5137.
    • (2004) Biochemistry , vol.43 , pp. 5126-5137
    • Arnold, J.J.1    Cameron, C.E.2
  • 6
    • 21844431621 scopus 로고    scopus 로고
    • Remote site control of an active site fidelity checkpoint in a viral RNA-dependent RNA polymerase
    • Arnold, J.J., Vignuzzi, M., Stone, J.K., Andino, R., Cameron, C.E., Remote site control of an active site fidelity checkpoint in a viral RNA-dependent RNA polymerase. J. Biol. Chem. 280 (2005), 25706–25716.
    • (2005) J. Biol. Chem. , vol.280 , pp. 25706-25716
    • Arnold, J.J.1    Vignuzzi, M.2    Stone, J.K.3    Andino, R.4    Cameron, C.E.5
  • 7
    • 33644674424 scopus 로고    scopus 로고
    • Small ubiquitin-like modifying protein isopeptidase assay based on poliovirus RNA polymerase activity
    • Arnold, J.J., Bernal, A., Uche, U., Sterner, D.E., Butt, T.R., Cameron, C.E., Mattern, M.R., Small ubiquitin-like modifying protein isopeptidase assay based on poliovirus RNA polymerase activity. Anal. Biochem. 350 (2006), 214–221.
    • (2006) Anal. Biochem. , vol.350 , pp. 214-221
    • Arnold, J.J.1    Bernal, A.2    Uche, U.3    Sterner, D.E.4    Butt, T.R.5    Cameron, C.E.6    Mattern, M.R.7
  • 8
    • 84918818959 scopus 로고    scopus 로고
    • Targeting structural dynamics of the RNA-dependent RNA polymerase for anti-viral strategies
    • Boehr, D.D., Liu, X., Yang, X., Targeting structural dynamics of the RNA-dependent RNA polymerase for anti-viral strategies. Curr. Opin. Virol. 9 (2014), 194–200.
    • (2014) Curr. Opin. Virol. , vol.9 , pp. 194-200
    • Boehr, D.D.1    Liu, X.2    Yang, X.3
  • 10
    • 84886942365 scopus 로고    scopus 로고
    • Global RNA structure analysis of poliovirus identifies a conserved RNA structure involved in viral replication and infectivity
    • Burrill, C.P., Westesson, O., Schulte, M.B., Strings, V.R., Segal, M., Andino, R., Global RNA structure analysis of poliovirus identifies a conserved RNA structure involved in viral replication and infectivity. J. Virol. 87 (2013), 11670–11683.
    • (2013) J. Virol. , vol.87 , pp. 11670-11683
    • Burrill, C.P.1    Westesson, O.2    Schulte, M.B.3    Strings, V.R.4    Segal, M.5    Andino, R.6
  • 11
    • 52649143257 scopus 로고    scopus 로고
    • Crystal structure of coxsackievirus B3 3Dpol highlights the functional importance of residue 5 in picornavirus polymerases
    • Campagnola, G., Weygandt, M., Scoggin, K., Peersen, O., Crystal structure of coxsackievirus B3 3Dpol highlights the functional importance of residue 5 in picornavirus polymerases. J. Virol. 82 (2008), 9458–9464.
    • (2008) J. Virol. , vol.82 , pp. 9458-9464
    • Campagnola, G.1    Weygandt, M.2    Scoggin, K.3    Peersen, O.4
  • 12
    • 84919427801 scopus 로고    scopus 로고
    • Structure-function relationships underlying the replication fidelity of viral RNA-dependent RNA polymerases
    • Campagnola, G., McDonald, S., Beaucourt, S., Vignuzzi, M., Peersen, O.B., Structure-function relationships underlying the replication fidelity of viral RNA-dependent RNA polymerases. J. Virol. 89 (2015), 275–286.
    • (2015) J. Virol. , vol.89 , pp. 275-286
    • Campagnola, G.1    McDonald, S.2    Beaucourt, S.3    Vignuzzi, M.4    Peersen, O.B.5
  • 16
    • 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., Sun, Y., Xu, P., Zhou, H., Yang, C., Shi, P.Y., Rao, Z., Zhang, B., Lou, Z., 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. 87 (2013), 5755–5768.
    • (2013) J. Virol. , vol.87 , pp. 5755-5768
    • Chen, C.1    Wang, Y.2    Shan, C.3    Sun, Y.4    Xu, P.5    Zhou, H.6    Yang, C.7    Shi, P.Y.8    Rao, Z.9    Zhang, B.10    Lou, Z.11
  • 17
    • 0027273310 scopus 로고
    • RNA duplex unwinding activity of poliovirus RNA-dependent RNA polymerase 3Dpol
    • Cho, M.W., Richards, O.C., Dmitrieva, T.M., Agol, V., Ehrenfeld, E., RNA duplex unwinding activity of poliovirus RNA-dependent RNA polymerase 3Dpol. J. Virol. 67 (1993), 3010–3018.
    • (1993) J. Virol. , vol.67 , pp. 3010-3018
    • Cho, M.W.1    Richards, O.C.2    Dmitrieva, T.M.3    Agol, V.4    Ehrenfeld, E.5
  • 18
    • 85009792051 scopus 로고    scopus 로고
    • Structure(s), function(s), and inhibition of the RNA-dependent RNA polymerase of noroviruses
    • Deval, J., Jin, Z., Chuang, Y.-C., Kao, C.C., Structure(s), function(s), and inhibition of the RNA-dependent RNA polymerase of noroviruses. Virus Res. 234 (2017), 21–33.
    • (2017) Virus Res. , vol.234 , pp. 21-33
    • Deval, J.1    Jin, Z.2    Chuang, Y.-C.3    Kao, C.C.4
  • 19
    • 8744222695 scopus 로고    scopus 로고
    • Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA
    • Ferrer-Orta, C., Arias, A., Perez-Luque, R., Escarmis, C., Domingo, E., Verdaguer, N., Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA. J. Biol. Chem. 279 (2004), 47212–47221.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47212-47221
    • Ferrer-Orta, C.1    Arias, A.2    Perez-Luque, R.3    Escarmis, C.4    Domingo, E.5    Verdaguer, N.6
  • 20
    • 33644519317 scopus 로고    scopus 로고
    • The structure of a protein primer-polymerase complex in the initiation of genome replication
    • Ferrer-Orta, C., Arias, A., Agudo, R., Perez-Luque, R., Escarmis, C., Domingo, E., Verdaguer, N., The structure of a protein primer-polymerase complex in the initiation of genome replication. EMBO J. 25 (2006), 880–888.
    • (2006) EMBO J. , vol.25 , pp. 880-888
    • Ferrer-Orta, C.1    Arias, A.2    Agudo, R.3    Perez-Luque, R.4    Escarmis, C.5    Domingo, E.6    Verdaguer, N.7
  • 24
    • 71849102316 scopus 로고    scopus 로고
    • Bridging IRES elements in mRNAs to the eukaryotic translation apparatus
    • Fitzgerald, K.D., Semler, B.L., Bridging IRES elements in mRNAs to the eukaryotic translation apparatus. Biochim. Biophys. Acta 1789 (2009), 518–528.
    • (2009) Biochim. Biophys. Acta , vol.1789 , pp. 518-528
    • Fitzgerald, K.D.1    Semler, B.L.2
  • 26
    • 0033212780 scopus 로고    scopus 로고
    • Production of authentic poliovirus RNA-dependent RNA polymerase (3D(pol)) by ubiquitin-protease-mediated cleavage in Escherichia coli
    • Gohara, D.W., Ha, C.S., Kumar, S., Ghosh, B., Arnold, J.J., Wisniewski, T.J., Cameron, C.E., Production of authentic poliovirus RNA-dependent RNA polymerase (3D(pol)) by ubiquitin-protease-mediated cleavage in Escherichia coli. Protein Expr. Purif. 17 (1999), 128–138.
    • (1999) Protein Expr. Purif. , vol.17 , pp. 128-138
    • Gohara, D.W.1    Ha, C.S.2    Kumar, S.3    Ghosh, B.4    Arnold, J.J.5    Wisniewski, T.J.6    Cameron, C.E.7
  • 27
    • 0034682792 scopus 로고    scopus 로고
    • Poliovirus RNA-dependent RNA polymerase (3Dpol): structural, biochemical, and biological analysis of conserved structural motifs A and B
    • Gohara, D.W., Crotty, S., Arnold, J.J., Yoder, J.D., Andino, R., Cameron, C.E., Poliovirus RNA-dependent RNA polymerase (3Dpol): structural, biochemical, and biological analysis of conserved structural motifs A and B. J. Biol. Chem. 275 (2000), 25523–25532.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25523-25532
    • Gohara, D.W.1    Crotty, S.2    Arnold, J.J.3    Yoder, J.D.4    Andino, R.5    Cameron, C.E.6
  • 28
    • 78651097570 scopus 로고    scopus 로고
    • Structural basis for active site closure by the poliovirus RNA-dependent RNA polymerase
    • Gong, P., Peersen, O.B., Structural basis for active site closure by the poliovirus RNA-dependent RNA polymerase. Proc. Natl. Acad. Sci. U. S. A. 107 (2010), 22505–22510.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 22505-22510
    • Gong, P.1    Peersen, O.B.2
  • 29
    • 84877307801 scopus 로고    scopus 로고
    • Structures of coxsackievirus, rhinovirus, and poliovirus polymerase elongation complexes solved by engineering RNA mediated crystal contacts
    • Gong, P., Kortus, M.G., Nix, J.C., Davis, R.E., Peersen, O.B., Structures of coxsackievirus, rhinovirus, and poliovirus polymerase elongation complexes solved by engineering RNA mediated crystal contacts. PLoS One, 8, 2013, e60272.
    • (2013) PLoS One , vol.8 , pp. e60272
    • Gong, P.1    Kortus, M.G.2    Nix, J.C.3    Davis, R.E.4    Peersen, O.B.5
  • 30
    • 78649446462 scopus 로고    scopus 로고
    • Origin and evolution of the picornaviridae proteome
    • E. Ehrenfeld A. Domingo R.P. Roos ASM Press Washington, DC
    • Gorbalenya, A., Lauber, C., Origin and evolution of the picornaviridae proteome. Ehrenfeld, E., Domingo, A., Roos, R.P., (eds.) The Picornaviruses, 2010, ASM Press, Washington, DC, 253–270.
    • (2010) The Picornaviruses , pp. 253-270
    • Gorbalenya, A.1    Lauber, C.2
  • 31
    • 52649173300 scopus 로고    scopus 로고
    • The crystal structure of coxsackievirus B3 RNA-dependent RNA polymerase in complex with its protein primer VPg confirms the existence of a second VPg binding site on Picornaviridae polymerases
    • Gruez, A., Selisko, B., Roberts, M., Bricogne, G., Bussetta, C., Jabafi, I., Coutard, B., De Palma, A.M., Neyts, J., Canard, B., The crystal structure of coxsackievirus B3 RNA-dependent RNA polymerase in complex with its protein primer VPg confirms the existence of a second VPg binding site on Picornaviridae polymerases. J. Virol. 82 (2008), 9577–9590.
    • (2008) J. Virol. , vol.82 , pp. 9577-9590
    • Gruez, A.1    Selisko, B.2    Roberts, M.3    Bricogne, G.4    Bussetta, C.5    Jabafi, I.6    Coutard, B.7    De Palma, A.M.8    Neyts, J.9    Canard, B.10
  • 32
    • 0031571638 scopus 로고    scopus 로고
    • Structure of the RNA-dependent RNA polymerase of poliovirus
    • Hansen, J.L., Long, A.M., Schultz, S.C., Structure of the RNA-dependent RNA polymerase of poliovirus. Structure 5 (1997), 1109–1122.
    • (1997) Structure , vol.5 , pp. 1109-1122
    • Hansen, J.L.1    Long, A.M.2    Schultz, S.C.3
  • 33
    • 0026464666 scopus 로고
    • Purification and characterization of poliovirus polypeptide 3CD, a proteinase and a precursor for RNA polymerase
    • Harris, K.S., Reddigari, S.R., Nicklin, M.J., Hammerle, T., Wimmer, E., Purification and characterization of poliovirus polypeptide 3CD, a proteinase and a precursor for RNA polymerase. J. Virol. 66 (1992), 7481–7489.
    • (1992) J. Virol. , vol.66 , pp. 7481-7489
    • Harris, K.S.1    Reddigari, S.R.2    Nicklin, M.J.3    Hammerle, T.4    Wimmer, E.5
  • 34
    • 77954979735 scopus 로고    scopus 로고
    • Poliovirus polymerase residue 5 plays a critical role in elongation complex stability
    • Hobdey, S.E., Kempf, B.J., Steil, B.P., Barton, D.J., Peersen, O.B., Poliovirus polymerase residue 5 plays a critical role in elongation complex stability. J. Virol. 84 (2010), 8072–8084.
    • (2010) J. Virol. , vol.84 , pp. 8072-8084
    • Hobdey, S.E.1    Kempf, B.J.2    Steil, B.P.3    Barton, D.J.4    Peersen, O.B.5
  • 35
    • 0030732120 scopus 로고    scopus 로고
    • Genetic dissection of interaction between poliovirus 3D polymerase and viral protein 3AB
    • Hope, D.A., Diamond, S.E., Kirkegaard, K., Genetic dissection of interaction between poliovirus 3D polymerase and viral protein 3AB. J. Virol. 71 (1997), 9490–9498.
    • (1997) J. Virol. , vol.71 , pp. 9490-9498
    • Hope, D.A.1    Diamond, S.E.2    Kirkegaard, K.3
  • 36
    • 84858973676 scopus 로고    scopus 로고
    • Assembly, purification and pre-steady-state kinetic analysis of an active RNA-dependent RNA polymerase elongation complex
    • Jin, Z., Leveque, V., Ma, H., Johnson, K.A., Klumpp, K., Assembly, purification and pre-steady-state kinetic analysis of an active RNA-dependent RNA polymerase elongation complex. J. Biol. Chem. 287 (2012), 10674–10683.
    • (2012) J. Biol. Chem. , vol.287 , pp. 10674-10683
    • Jin, Z.1    Leveque, V.2    Ma, H.3    Johnson, K.A.4    Klumpp, K.5
  • 37
    • 84979515428 scopus 로고    scopus 로고
    • ATP is an allosteric inhibitor of coxsackievirus B3 polymerase
    • Karr, J.P., Peersen, O.B., ATP is an allosteric inhibitor of coxsackievirus B3 polymerase. Biochemistry 55 (2016), 3995–4002.
    • (2016) Biochemistry , vol.55 , pp. 3995-4002
    • Karr, J.P.1    Peersen, O.B.2
  • 38
    • 84930074657 scopus 로고    scopus 로고
    • The Phyre2 web portal for protein modeling, prediction and analysis
    • Kelley, L.A., Mezulis, S., Yates, C.M., Wass, M.N., Sternberg, M.J., The Phyre2 web portal for protein modeling, prediction and analysis. Nat. Protoc. 10 (2015), 845–858.
    • (2015) Nat. Protoc. , vol.10 , pp. 845-858
    • Kelley, L.A.1    Mezulis, S.2    Yates, C.M.3    Wass, M.N.4    Sternberg, M.J.5
  • 39
    • 84877358918 scopus 로고    scopus 로고
    • Structural features of a picornavirus polymerase involved in the polyadenylation of viral RNA
    • Kempf, B.J., Kelly, M.M., Springer, C.L., Peersen, O.B., Barton, D.J., Structural features of a picornavirus polymerase involved in the polyadenylation of viral RNA. J. Virol. 87 (2013), 5629–5644.
    • (2013) J. Virol. , vol.87 , pp. 5629-5644
    • Kempf, B.J.1    Kelly, M.M.2    Springer, C.L.3    Peersen, O.B.4    Barton, D.J.5
  • 40
    • 84990248563 scopus 로고    scopus 로고
    • Poliovirus polymerase leu420 facilitates RNA recombination and ribavirin resistance
    • Kempf, B.J., Peersen, O.B., Barton, D.J., Poliovirus polymerase leu420 facilitates RNA recombination and ribavirin resistance. J. Virol. 90 (2016), 8410–8421.
    • (2016) J. Virol. , vol.90 , pp. 8410-8421
    • Kempf, B.J.1    Peersen, O.B.2    Barton, D.J.3
  • 42
    • 84857997971 scopus 로고    scopus 로고
    • A template RNA entry channel in the fingers domain of the poliovirus polymerase
    • Kortus, M.G., Kempf, B.J., Haworth, K.G., Barton, D.J., Peersen, O.B., A template RNA entry channel in the fingers domain of the poliovirus polymerase. J. Mol. Biol. 417 (2012), 263–278.
    • (2012) J. Mol. Biol. , vol.417 , pp. 263-278
    • Kortus, M.G.1    Kempf, B.J.2    Haworth, K.G.3    Barton, D.J.4    Peersen, O.B.5
  • 43
    • 77957658175 scopus 로고    scopus 로고
    • Quasispecies theory and the behavior of RNA viruses
    • Lauring, A.S., Andino, R., Quasispecies theory and the behavior of RNA viruses. PLoS Pathog., 6, 2010, e1001005.
    • (2010) PLoS Pathog. , vol.6 , pp. e1001005
    • Lauring, A.S.1    Andino, R.2
  • 44
    • 77953249856 scopus 로고    scopus 로고
    • Rationalizing the development of live attenuated virus vaccines
    • Lauring, A.S., Jones, J.O., Andino, R., Rationalizing the development of live attenuated virus vaccines. Nat. Biotechnol. 28 (2010), 573–579.
    • (2010) Nat. Biotechnol. , vol.28 , pp. 573-579
    • Lauring, A.S.1    Jones, J.O.2    Andino, R.3
  • 45
    • 84876406925 scopus 로고    scopus 로고
    • The role of mutational robustness in RNA virus evolution
    • Lauring, A.S., Frydman, J., Andino, R., The role of mutational robustness in RNA virus evolution. Nat. Rev. Microbiol. 11 (2013), 327–336.
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 327-336
    • Lauring, A.S.1    Frydman, J.2    Andino, R.3
  • 46
    • 0032876683 scopus 로고    scopus 로고
    • Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site
    • Lesburg, C.A., Cable, M.B., Ferrari, E., Hong, Z., Mannarino, A.F., Weber, P.C., Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site. Nat. Struct. Biol. 6 (1999), 937–943.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 937-943
    • Lesburg, C.A.1    Cable, M.B.2    Ferrari, E.3    Hong, Z.4    Mannarino, A.F.5    Weber, P.C.6
  • 47
    • 84887467058 scopus 로고    scopus 로고
    • Vaccine-derived mutation in motif D of poliovirus RNA-dependent RNA polymerase lowers nucleotide incorporation fidelity
    • Liu, X., Yang, X., Lee, C.A., Moustafa, I.M., Smidansky, E.D., Lum, D., Arnold, J.J., Cameron, C.E., Boehr, D.D., Vaccine-derived mutation in motif D of poliovirus RNA-dependent RNA polymerase lowers nucleotide incorporation fidelity. J. Biol. Chem. 288 (2013), 32753–32765.
    • (2013) J. Biol. Chem. , vol.288 , pp. 32753-32765
    • Liu, X.1    Yang, X.2    Lee, C.A.3    Moustafa, I.M.4    Smidansky, E.D.5    Lum, D.6    Arnold, J.J.7    Cameron, C.E.8    Boehr, D.D.9
  • 48
    • 4143147318 scopus 로고    scopus 로고
    • The crystal structure of the RNA-dependent RNA polymerase from human rhinovirus: a dual function target for common cold antiviral therapy
    • Love, R.A., Maegley, K.A., Yu, X., Ferre, R.A., Lingardo, L.K., Diehl, W., Parge, H.E., Dragovich, P.S., Fuhrman, S.A., The crystal structure of the RNA-dependent RNA polymerase from human rhinovirus: a dual function target for common cold antiviral therapy. Structure 12 (2004), 1533–1544.
    • (2004) Structure , vol.12 , pp. 1533-1544
    • Love, R.A.1    Maegley, K.A.2    Yu, X.3    Ferre, R.A.4    Lingardo, L.K.5    Diehl, W.6    Parge, H.E.7    Dragovich, P.S.8    Fuhrman, S.A.9
  • 49
    • 84903480766 scopus 로고    scopus 로고
    • Recombination in enteroviruses is a biphasic replicative process involving the generation of greater-than genome length ‘imprecise' intermediates
    • Lowry, K., Woodman, A., Cook, J., Evans, D.J., Recombination in enteroviruses is a biphasic replicative process involving the generation of greater-than genome length ‘imprecise' intermediates. PLoS Pathog., 10, 2014, e1004191.
    • (2014) PLoS Pathog. , vol.10 , pp. e1004191
    • Lowry, K.1    Woodman, A.2    Cook, J.3    Evans, D.J.4
  • 50
    • 84883381606 scopus 로고    scopus 로고
    • Crystal structure of the full-Length japanese encephalitis virus NS5 reveals a conserved methyltransferase-polymerase interface
    • Lu, G., Gong, P., Crystal structure of the full-Length japanese encephalitis virus NS5 reveals a conserved methyltransferase-polymerase interface. PLoS Pathog., 9, 2013, e1003549.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003549
    • Lu, G.1    Gong, P.2
  • 51
    • 85011602101 scopus 로고    scopus 로고
    • A structural view of the RNA-dependent RNA polymerases from the Flavivirus genus
    • Lu, G., Gong, P., A structural view of the RNA-dependent RNA polymerases from the Flavivirus genus. Virus Res. 234 (2017), 34–43.
    • (2017) Virus Res. , vol.234 , pp. 34-43
    • Lu, G.1    Gong, P.2
  • 52
    • 33947386595 scopus 로고    scopus 로고
    • Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNA polymerase
    • Marcotte, L.L., Wass, A.B., Gohara, D.W., Pathak, H.B., Arnold, J.J., Filman, D.J., Cameron, C.E., Hogle, J.M., Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNA polymerase. J. Virol. 81 (2007), 3583–3596.
    • (2007) J. Virol. , vol.81 , pp. 3583-3596
    • Marcotte, L.L.1    Wass, A.B.2    Gohara, D.W.3    Pathak, H.B.4    Arnold, J.J.5    Filman, D.J.6    Cameron, C.E.7    Hogle, J.M.8
  • 53
    • 84976648904 scopus 로고    scopus 로고
    • Design of a genetically stable high fidelity coxsackievirus B3 polymerase that attenuates virus growth in vivo
    • McDonald, S., Block, A., Beaucourt, S., Moratorio, G., Vignuzzi, M., Peersen, O.B., Design of a genetically stable high fidelity coxsackievirus B3 polymerase that attenuates virus growth in vivo. J. Biol. Chem. 291 (2016), 13999–14011.
    • (2016) J. Biol. Chem. , vol.291 , pp. 13999-14011
    • McDonald, S.1    Block, A.2    Beaucourt, S.3    Moratorio, G.4    Vignuzzi, M.5    Peersen, O.B.6
  • 54
    • 84879694249 scopus 로고    scopus 로고
    • Recombination in the evolution of human rhinovirus genomes
    • McIntyre, C.L., Savolainen-Kopra, C., Hovi, T., Simmonds, P., Recombination in the evolution of human rhinovirus genomes. Arch. Virol. 158 (2013), 1497–1515.
    • (2013) Arch. Virol. , vol.158 , pp. 1497-1515
    • McIntyre, C.L.1    Savolainen-Kopra, C.2    Hovi, T.3    Simmonds, P.4
  • 55
    • 34247862056 scopus 로고    scopus 로고
    • A fluorescence polarization-based screening assay for nucleic acid polymerase elongation activity
    • Mestas, S.P., Sholders, A.J., Peersen, O.B., A fluorescence polarization-based screening assay for nucleic acid polymerase elongation activity. Anal. Biochem. 365 (2007), 194–200.
    • (2007) Anal. Biochem. , vol.365 , pp. 194-200
    • Mestas, S.P.1    Sholders, A.J.2    Peersen, O.B.3
  • 57
    • 79958744018 scopus 로고    scopus 로고
    • Molecular dynamics simulations of viral RNA polymerases link conserved and correlated motions of functional elements to fidelity
    • Moustafa, 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. 410 (2011), 159–181.
    • (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
  • 59
    • 0037059758 scopus 로고    scopus 로고
    • Crystal structures of active and inactive conformations of a caliciviral RNA-dependent RNA polymerase
    • Ng, K.K., Cherney, M.M., Vazquez, A.L., Machin, A., Alonso, J.M., Parra, F., James, M.N., Crystal structures of active and inactive conformations of a caliciviral RNA-dependent RNA polymerase. J. Biol. Chem. 277 (2002), 1381–1387.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1381-1387
    • Ng, K.K.1    Cherney, M.M.2    Vazquez, A.L.3    Machin, A.4    Alonso, J.M.5    Parra, F.6    James, M.N.7
  • 60
    • 0037470586 scopus 로고    scopus 로고
    • Substrate complexes of hepatitis C virus RNA polymerase (HC-J4): structural evidence for nucleotide import and de-novo initiation
    • O'Farrell, D., Trowbridge, R., Rowlands, D., Jager, J., Substrate complexes of hepatitis C virus RNA polymerase (HC-J4): structural evidence for nucleotide import and de-novo initiation. J. Mol. Biol. 326 (2003), 1025–1035.
    • (2003) J. Mol. Biol. , vol.326 , pp. 1025-1035
    • O'Farrell, D.1    Trowbridge, R.2    Rowlands, D.3    Jager, J.4
  • 61
    • 79952039453 scopus 로고    scopus 로고
    • Genome organization and encoded proteins
    • E. Ehrenfeld A. Domingo R.P. Roos ASM Press Washington, DC
    • Palmenberg, A.C., Neubauer, D., Skern, T., Genome organization and encoded proteins. Ehrenfeld, E., Domingo, A., Roos, R.P., (eds.) The Picornaviruses, 2010, ASM Press, Washington, DC, 3–17.
    • (2010) The Picornaviruses , pp. 3-17
    • Palmenberg, A.C.1    Neubauer, D.2    Skern, T.3
  • 62
    • 0033766003 scopus 로고    scopus 로고
    • Identification of an RNA hairpin in poliovirus RNA that serves as the primary template in the in vitro uridylylation of VPg
    • Paul, A.V., Rieder, E., Kim, D.W., van Boom, J.H., Wimmer, E., Identification of an RNA hairpin in poliovirus RNA that serves as the primary template in the in vitro uridylylation of VPg. J. Virol. 74 (2000), 10359–10370.
    • (2000) J. Virol. , vol.74 , pp. 10359-10370
    • Paul, A.V.1    Rieder, E.2    Kim, D.W.3    van Boom, J.H.4    Wimmer, E.5
  • 63
    • 0242415195 scopus 로고    scopus 로고
    • A slide-back mechanism for the initiation of protein-primed RNA synthesis by the RNA polymerase of poliovirus
    • Paul, A.V., Yin, J., Mugavero, J., Rieder, E., Liu, Y., Wimmer, E., A slide-back mechanism for the initiation of protein-primed RNA synthesis by the RNA polymerase of poliovirus. J. Biol. Chem. 278 (2003), 43951–43960.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43951-43960
    • Paul, A.V.1    Yin, J.2    Mugavero, J.3    Rieder, E.4    Liu, Y.5    Wimmer, E.6
  • 64
    • 0038809107 scopus 로고    scopus 로고
    • A single mutation in poliovirus RNA-dependent RNA polymerase confers resistance to mutagenic nucleotide analogs via increased fidelity
    • Pfeiffer, J.K., Kirkegaard, K., A single mutation in poliovirus RNA-dependent RNA polymerase confers resistance to mutagenic nucleotide analogs via increased fidelity. Proc. Natl. Acad. Sci. U. S. A. 100 (2003), 7289–7294.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7289-7294
    • Pfeiffer, J.K.1    Kirkegaard, K.2
  • 65
    • 33745490138 scopus 로고    scopus 로고
    • Increased fidelity reduces poliovirus fitness and virulence under selective pressure in mice
    • Pfeiffer, J.K., Kirkegaard, K., Increased fidelity reduces poliovirus fitness and virulence under selective pressure in mice. PLoS Pathog., 1, 2005, e11.
    • (2005) PLoS Pathog. , vol.1 , pp. e11
    • Pfeiffer, J.K.1    Kirkegaard, K.2
  • 66
    • 33645758779 scopus 로고    scopus 로고
    • Bottleneck-mediated quasispecies restriction during spread of an RNA virus from inoculation site to brain
    • Pfeiffer, J.K., Kirkegaard, K., Bottleneck-mediated quasispecies restriction during spread of an RNA virus from inoculation site to brain. Proc. Natl. Acad. Sci. U. S. A. 103 (2006), 5520–5525.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 5520-5525
    • Pfeiffer, J.K.1    Kirkegaard, K.2
  • 67
    • 84873023551 scopus 로고    scopus 로고
    • Ribavirin-resistant mutants of human enterovirus 71 express a high replication fidelity phenotype during growth in cell culture
    • Sadeghipour, S., Bek, E.J., McMinn, P.C., Ribavirin-resistant mutants of human enterovirus 71 express a high replication fidelity phenotype during growth in cell culture. J. Virol. 87 (2013), 1759–1769.
    • (2013) J. Virol. , vol.87 , pp. 1759-1769
    • Sadeghipour, S.1    Bek, E.J.2    McMinn, P.C.3
  • 68
    • 84882892620 scopus 로고    scopus 로고
    • Characterization of a nuclear localization signal in the foot-and-mouth disease virus polymerase
    • Sanchez-Aparicio, M.T., Rosas, M.F., Sobrino, F., Characterization of a nuclear localization signal in the foot-and-mouth disease virus polymerase. Virology 444 (2013), 203–210.
    • (2013) Virology , vol.444 , pp. 203-210
    • Sanchez-Aparicio, M.T.1    Rosas, M.F.2    Sobrino, F.3
  • 69
    • 33744984790 scopus 로고    scopus 로고
    • NMR structure of the viral peptide linked to the genome (VPg) of poliovirus
    • Schein, C.H., Oezguen, N., Volk, D.E., Garimella, R., Paul, A., Braun, W., NMR structure of the viral peptide linked to the genome (VPg) of poliovirus. Peptides 27 (2006), 1676–1684.
    • (2006) Peptides , vol.27 , pp. 1676-1684
    • Schein, C.H.1    Oezguen, N.2    Volk, D.E.3    Garimella, R.4    Paul, A.5    Braun, W.6
  • 72
    • 84872021142 scopus 로고    scopus 로고
    • What is the role of motif d in the nucleotide incorporation catalyzed by the RNA-dependent RNA polymerase from poliovirus?
    • Shen, H., Sun, H., Li, G., What is the role of motif d in the nucleotide incorporation catalyzed by the RNA-dependent RNA polymerase from poliovirus?. PLoS Comput. Biol., 8, 2012, e1002851.
    • (2012) PLoS Comput. Biol. , vol.8 , pp. e1002851
    • Shen, H.1    Sun, H.2    Li, G.3
  • 73
    • 84895919460 scopus 로고    scopus 로고
    • Distinct conformations of a putative translocation element in poliovirus polymerase
    • Sholders, A.J., Peersen, O.B., Distinct conformations of a putative translocation element in poliovirus polymerase. J. Mol. Biol. 426 (2014), 1407–1419.
    • (2014) J. Mol. Biol. , vol.426 , pp. 1407-1419
    • Sholders, A.J.1    Peersen, O.B.2
  • 74
    • 84978141666 scopus 로고    scopus 로고
    • Structural basis of viral RNA-dependent RNA polymerase catalysis and translocation
    • Shu, B., Gong, P., Structural basis of viral RNA-dependent RNA polymerase catalysis and translocation. Proc. Natl. Acad. Sci. U. S. A. 113 (2016), E4005–4014.
    • (2016) Proc. Natl. Acad. Sci. U. S. A. , vol.113 , pp. E4005-4014
    • Shu, B.1    Gong, P.2
  • 75
    • 33846813925 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus mutant with decreased sensitivity to ribavirin: implications for error catastrophe
    • Sierra, M., Airaksinen, A., Gonzalez-Lopez, C., Agudo, R., Arias, A., Domingo, E., Foot-and-mouth disease virus mutant with decreased sensitivity to ribavirin: implications for error catastrophe. J. Virol. 81 (2007), 2012–2024.
    • (2007) J. Virol. , vol.81 , pp. 2012-2024
    • Sierra, M.1    Airaksinen, A.2    Gonzalez-Lopez, C.3    Agudo, R.4    Arias, A.5    Domingo, E.6
  • 76
    • 84865994677 scopus 로고    scopus 로고
    • Identification of two functionally redundant RNA elements in the coding sequence of poliovirus using computer-generated design
    • Song, Y., Liu, Y., Ward, C.B., Mueller, S., Futcher, B., Skiena, S., Paul, A.V., Wimmer, E., Identification of two functionally redundant RNA elements in the coding sequence of poliovirus using computer-generated design. Proc. Natl. Acad. Sci. U. S. A. 109 (2012), 14301–14307.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 14301-14307
    • Song, Y.1    Liu, Y.2    Ward, C.B.3    Mueller, S.4    Futcher, B.5    Skiena, S.6    Paul, A.V.7    Wimmer, E.8
  • 77
    • 52649121446 scopus 로고    scopus 로고
    • Poliovirus cis-acting replication element-dependent VPg Uridylylation lowers the Km of the initiating nucleoside triphosphate for viral RNA replication
    • Steil, B.P., Barton, D.J., Poliovirus cis-acting replication element-dependent VPg Uridylylation lowers the Km of the initiating nucleoside triphosphate for viral RNA replication. J. Virol. 82 (2008), 9400–9408.
    • (2008) J. Virol. , vol.82 , pp. 9400-9408
    • Steil, B.P.1    Barton, D.J.2
  • 78
    • 0032518374 scopus 로고    scopus 로고
    • A mechanism for all polymerases
    • Steitz, T.A., A mechanism for all polymerases. Nature 391 (1998), 231–232.
    • (1998) Nature , vol.391 , pp. 231-232
    • Steitz, T.A.1
  • 81
    • 84865149772 scopus 로고    scopus 로고
    • Optimal simultaneous superpositioning of multiple structures with missing data
    • Theobald, D.L., Steindel, P.A., Optimal simultaneous superpositioning of multiple structures with missing data. Bioinformatics (Oxford England) 28 (2012), 1972–1979.
    • (2012) Bioinformatics (Oxford England) , vol.28 , pp. 1972-1979
    • Theobald, D.L.1    Steindel, P.A.2
  • 82
    • 40149086589 scopus 로고    scopus 로고
    • Accurate structural correlations from maximum likelihood superpositions
    • Theobald, D.L., Wuttke, D.S., Accurate structural correlations from maximum likelihood superpositions. PLoS Comput. Biol., 4, 2008, e43.
    • (2008) PLoS Comput. Biol. , vol.4 , pp. e43
    • Theobald, D.L.1    Wuttke, D.S.2
  • 83
    • 4644238112 scopus 로고    scopus 로고
    • Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase
    • Thompson, A.A., Peersen, O.B., Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase. EMBO J. 23 (2004), 3462–3471.
    • (2004) EMBO J. , vol.23 , pp. 3462-3471
    • Thompson, A.A.1    Peersen, O.B.2
  • 84
    • 33846833843 scopus 로고    scopus 로고
    • Stabilization of poliovirus polymerase by NTP binding and fingers-thumb interactions
    • Thompson, A.A., Albertini, R.A., Peersen, O.B., Stabilization of poliovirus polymerase by NTP binding and fingers-thumb interactions. J. Mol. Biol. 366 (2007), 1459–1474.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1459-1474
    • Thompson, A.A.1    Albertini, R.A.2    Peersen, O.B.3
  • 85
    • 31144465690 scopus 로고    scopus 로고
    • Quasispecies diversity determines pathogenesis through cooperative interactions in a viral population
    • Vignuzzi, M., Stone, J.K., Arnold, J.J., Cameron, C.E., Andino, R., Quasispecies diversity determines pathogenesis through cooperative interactions in a viral population. Nature 439 (2006), 344–348.
    • (2006) Nature , vol.439 , pp. 344-348
    • Vignuzzi, M.1    Stone, J.K.2    Arnold, J.J.3    Cameron, C.E.4    Andino, R.5
  • 86
    • 38949184924 scopus 로고    scopus 로고
    • Engineering attenuated virus vaccines by controlling replication fidelity
    • Vignuzzi, M., Wendt, E., Andino, R., Engineering attenuated virus vaccines by controlling replication fidelity. Nat. Med. 14 (2008), 154–161.
    • (2008) Nat. Med. , vol.14 , pp. 154-161
    • Vignuzzi, M.1    Wendt, E.2    Andino, R.3
  • 90
    • 0036314310 scopus 로고    scopus 로고
    • Sequence requirements for viral RNA replication and VPg uridylylation directed by the internal cis-acting replication element (cre) of human rhinovirus type 14
    • Yang, Y., Rijnbrand, R., McKnight, K.L., Wimmer, E., Paul, A., Martin, A., Lemon, S.M., Sequence requirements for viral RNA replication and VPg uridylylation directed by the internal cis-acting replication element (cre) of human rhinovirus type 14. J. Virol. 76 (2002), 7485–7494.
    • (2002) J. Virol. , vol.76 , pp. 7485-7494
    • Yang, Y.1    Rijnbrand, R.2    McKnight, K.L.3    Wimmer, E.4    Paul, A.5    Martin, A.6    Lemon, S.M.7
  • 91
    • 78049295254 scopus 로고    scopus 로고
    • Long-range interaction networks in the function and fidelity of poliovirus RNA-dependent RNA polymerase studied by nuclear magnetic resonance
    • Yang, X., Welch, J.L., Arnold, J.J., Boehr, D.D., Long-range interaction networks in the function and fidelity of poliovirus RNA-dependent RNA polymerase studied by nuclear magnetic resonance. Biochemistry 49 (2010), 9361–9371.
    • (2010) Biochemistry , vol.49 , pp. 9361-9371
    • Yang, X.1    Welch, J.L.2    Arnold, J.J.3    Boehr, D.D.4
  • 92
  • 93
    • 0037405787 scopus 로고    scopus 로고
    • Functional dissection of a poliovirus cis-acting replication element [PV-cre(2C)]: analysis of single- and dual-cre viral genomes and proteins that bind specifically to PV-cre RNA
    • Yin, J., Paul, A.V., Wimmer, E., Rieder, E., Functional dissection of a poliovirus cis-acting replication element [PV-cre(2C)]: analysis of single- and dual-cre viral genomes and proteins that bind specifically to PV-cre RNA. J. Virol. 77 (2003), 5152–5166.
    • (2003) J. Virol. , vol.77 , pp. 5152-5166
    • Yin, J.1    Paul, A.V.2    Wimmer, E.3    Rieder, E.4


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