메뉴 건너뛰기




Volumn 89, Issue 1, 2015, Pages 249-261

Perturbation in the conserved methyltransferase-polymerase interface of flavivirus NS5 differentially affects polymerase initiation and elongation

Author keywords

[No Author keywords available]

Indexed keywords

METHYLTRANSFERASE; NUCLEOTIDE; RNA DIRECTED DNA POLYMERASE; MUTANT PROTEIN; NS5 PROTEIN, FLAVIVIRUS; RNA DIRECTED RNA POLYMERASE; VIRUS PROTEIN;

EID: 84919451239     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02085-14     Document Type: Article
Times cited : (41)

References (55)
  • 1
    • 0018770470 scopus 로고
    • Methylation status of intracellular dengue type 2 40 S RNA
    • Cleaves GR, Dubin DT. 1979. Methylation status of intracellular dengue type 2 40 S RNA. Virology 96:159-165. http://dx.doi.org/10.1016/0042-6822(79)90181-8.
    • (1979) Virology , vol.96 , pp. 159-165
    • Cleaves, G.R.1    Dubin, D.T.2
  • 2
    • 33748669852 scopus 로고    scopus 로고
    • West Nile virus 5'-cap structure is formed by sequential guanine N-7 and ribose 2'-O methylations by nonstructural protein 5
    • Ray D, Shah A, Tilgner M, Guo Y, Zhao Y, Dong H, Deas TS, Zhou Y, Li H, Shi PY. 2006. West Nile virus 5'-cap structure is formed by sequential guanine N-7 and ribose 2'-O methylations by nonstructural protein 5. J Virol 80:8362-8370. http://dx.doi.org/10.1128/JVI.00814-06.
    • (2006) J Virol , vol.80 , pp. 8362-8370
    • Ray, D.1    Shah, A.2    Tilgner, M.3    Guo, Y.4    Zhao, Y.5    Dong, H.6    Deas, T.S.7    Zhou, Y.8    Li, H.9    Shi, P.Y.10
  • 3
    • 73249127604 scopus 로고    scopus 로고
    • The flavivirus NS5 protein is a true RNA guanylyltransferase that catalyzes a two-step reaction to form theRNAcap structure
    • Issur M, Geiss BJ, Bougie I, Picard-Jean F, Despins S, Mayette J, Hobdey SE, Bisaillon M. 2009. The flavivirus NS5 protein is a true RNA guanylyltransferase that catalyzes a two-step reaction to form theRNAcap structure. RNA 15:2340-2350. http://dx.doi.org/10.1261/rna.1609709.
    • (2009) RNA , vol.15 , pp. 2340-2350
    • Issur, M.1    Geiss, B.J.2    Bougie, I.3    Picard-Jean, F.4    Despins, S.5    Mayette, J.6    Hobdey, S.E.7    Bisaillon, M.8
  • 4
    • 0035450225 scopus 로고    scopus 로고
    • De novo initiation of viral RNAdependent RNA synthesis
    • Kao CC, Singh P, Ecker DJ. 2001. De novo initiation of viral RNAdependent RNA synthesis. Virology 287:251-260. http://dx.doi.org/10.1006/viro.2001.1039.
    • (2001) Virology , vol.287 , pp. 251-260
    • Kao, C.C.1    Singh, P.2    Ecker, D.J.3
  • 5
    • 0032876683 scopus 로고    scopus 로고
    • Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site
    • Lesburg CA, Cable MB, Ferrari E, Hong Z, Mannarino AF, Weber PC. 1999. Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site. Nat Struct Biol 6:937-943. http://dx.doi.org/10.1038/13305.
    • (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
  • 6
    • 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. 2013. Crystal structure of the full-length Japanese encephalitis virus NS5 reveals a conserved methyltransferase-polymerase interface. PLoS Pathog 9:e1003549. http://dx.doi.org/10.1371/journal.ppat.1003549.
    • (2013) PLoS Pathog , vol.9
    • Lu, G.1    Gong, P.2
  • 7
    • 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
    • Choi KH, Groarke JM, Young DC, Kuhn RJ, Smith JL, Pevear DC, Rossmann MG. 2004. 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 101:4425-4430. http://dx.doi.org/10.1073/pnas.0400660101.
    • (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
  • 8
    • 0035826258 scopus 로고    scopus 로고
    • A mechanism for initiating RNA-dependent RNA polymerization
    • Butcher SJ, Grimes JM, Makeyev EV, Bamford DH, Stuart DI. 2001. A mechanism for initiating RNA-dependent RNA polymerization. Nature 410:235-240. http://dx.doi.org/10.1038/35065653.
    • (2001) Nature , vol.410 , pp. 235-240
    • Butcher, S.J.1    Grimes, J.M.2    Makeyev, E.V.3    Bamford, D.H.4    Stuart, D.I.5
  • 9
    • 4944262080 scopus 로고    scopus 로고
    • Initial bubble collapse plays a key role in the transition to elongation in T7 RNA polymerase
    • Gong P, Esposito EA, Martin CT. 2004. Initial bubble collapse plays a key role in the transition to elongation in T7 RNA polymerase. J Biol Chem 279:44277-44285. http://dx.doi.org/10.1074/jbc.M409118200.
    • (2004) J Biol Chem , vol.279 , pp. 44277-44285
    • Gong, P.1    Esposito, E.A.2    Martin, C.T.3
  • 10
    • 4444379726 scopus 로고    scopus 로고
    • RNA displacement and resolution of the transcription bubble during transcription by T7 RNA polymerase
    • Jiang M, Ma N, Vassylyev DG, McAllister WT. 2004. RNA displacement and resolution of the transcription bubble during transcription by T7 RNA polymerase. Mol Cell 15:777-788. http://dx.doi.org/10.1016/j.molcel.2004.07.019.
    • (2004) Mol Cell , vol.15 , pp. 777-788
    • Jiang, M.1    Ma, N.2    Vassylyev, D.G.3    McAllister, W.T.4
  • 11
    • 0030758953 scopus 로고    scopus 로고
    • Characterization of RNA products associated with or aborted by a viral RNA-dependent RNA polymerase
    • Sun JH, Kao CC. 1997. Characterization of RNA products associated with or aborted by a viral RNA-dependent RNA polymerase. Virology 236: 348-353. http://dx.doi.org/10.1006/viro.1997.8742.
    • (1997) Virology , vol.236 , pp. 348-353
    • Sun, J.H.1    Kao, C.C.2
  • 12
    • 0037013858 scopus 로고    scopus 로고
    • An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization
    • Egloff MP, Benarroch D, Selisko B, Romette JL, Canard B. 2002. An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization. EMBO J 21:2757-2768. http://dx.doi.org/10.1093/emboj/21.11.2757.
    • (2002) EMBO J , vol.21 , pp. 2757-2768
    • Egloff, M.P.1    Benarroch, D.2    Selisko, B.3    Romette, J.L.4    Canard, B.5
  • 13
    • 77956126053 scopus 로고    scopus 로고
    • FlavivirusRNAcap methyltransferase: structure, function, and inhibition
    • Liu L, Dong H, Chen H, Zhang J, Ling H, Li Z, Shi PY, Li H. 2010. FlavivirusRNAcap methyltransferase: structure, function, and inhibition. Front Biol 5:286-303. http://dx.doi.org/10.1007/s11515-010-0660-y.
    • (2010) Front Biol , vol.5 , pp. 286-303
    • Liu, L.1    Dong, H.2    Chen, H.3    Zhang, J.4    Ling, H.5    Li, Z.6    Shi, P.Y.7    Li, H.8
  • 16
    • 34247610261 scopus 로고    scopus 로고
    • Crystal structure of the dengue virus RNA-dependent RNA polymerase catalytic domain at 1.85-angstrom resolution
    • Yap TL, Xu T, Chen YL, Malet H, Egloff MP, Canard B, Vasudevan SG, Lescar J. 2007. Crystal structure of the dengue virus RNA-dependent RNA polymerase catalytic domain at 1.85-angstrom resolution. J Virol 81: 4753-4765. http://dx.doi.org/10.1128/JVI.02283-06.
    • (2007) J Virol , vol.81 , pp. 4753-4765
    • Yap, T.L.1    Xu, T.2    Chen, Y.L.3    Malet, H.4    Egloff, M.P.5    Canard, B.6    Vasudevan, S.G.7    Lescar, J.8
  • 19
    • 78751508379 scopus 로고    scopus 로고
    • Characterization of the elongation complex of dengue virus RNA polymerase: assembly, kinetics of nucleotide incorporation, and fidelity
    • Jin Z, Deval J, Johnson KA, Swinney DC. 2011. Characterization of the elongation complex of dengue virus RNA polymerase: assembly, kinetics of nucleotide incorporation, and fidelity. J Biol Chem 286:2067-2077. http://dx.doi.org/10.1074/jbc.M110.162685.
    • (2011) J Biol Chem , vol.286 , pp. 2067-2077
    • Jin, Z.1    Deval, J.2    Johnson, K.A.3    Swinney, D.C.4
  • 20
    • 84886647090 scopus 로고    scopus 로고
    • A crystal structure of the dengue virus non-structural protein 5 (NS5) polymerase delineates interdomain amino acid residues that enhance its thermostability and de novo initiation activities
    • Lim SP, Koh JH, Seh CC, Liew CW, Davidson AD, Chua LS, Chandrasekaran R, Cornvik TC, Shi PY, Lescar J. 2013. A crystal structure of the dengue virus non-structural protein 5 (NS5) polymerase delineates interdomain amino acid residues that enhance its thermostability and de novo initiation activities. J Biol Chem 288:31105-31114. http://dx.doi.org/10.1074/jbc.M113.508606.
    • (2013) J Biol Chem , vol.288 , pp. 31105-31114
    • Lim, S.P.1    Koh, J.H.2    Seh, C.C.3    Liew, C.W.4    Davidson, A.D.5    Chua, L.S.6    Chandrasekaran, R.7    Cornvik, T.C.8    Shi, P.Y.9    Lescar, J.10
  • 21
    • 84901767814 scopus 로고    scopus 로고
    • The interface between methyltransferase and polymerase of NS5 is essential for flavivirus replication
    • Li XD, Shan C, Deng CL, Ye HQ, Shi PY, Yuan ZM, Gong P, Zhang B. 2014. The interface between methyltransferase and polymerase of NS5 is essential for flavivirus replication. PLoS Negl Trop Dis 8:e2891. http://dx.doi.org/10.1371/journal.pntd.0002891.
    • (2014) PLoS Negl Trop Dis , vol.8
    • Li, X.D.1    Shan, C.2    Deng, C.L.3    Ye, H.Q.4    Shi, P.Y.5    Yuan, Z.M.6    Gong, P.7    Zhang, B.8
  • 22
    • 0002014756 scopus 로고    scopus 로고
    • Site-directed mutagenesis in one day with >80% efficiency
    • JC
    • Papworth CB, JC, Braman J, Wright DA. 1996. Site-directed mutagenesis in one day with >80% efficiency. Strategies 9:3-4.
    • (1996) Strategies , vol.9 , pp. 3-4
    • Papworth, C.B.1    Braman, J.2    Wright, D.A.3
  • 23
    • 16544395270 scopus 로고    scopus 로고
    • Site-directed, ligaseindependent mutagenesis (SLIM): a single-tube methodology approaching 100% efficiency in 4 h
    • Chiu J, March PE, Lee R, Tillett D. 2004. Site-directed, ligaseindependent mutagenesis (SLIM): a single-tube methodology approaching 100% efficiency in 4 h. Nucleic Acids Res 32:e174. http://dx.doi.org/10.1093/nar/gnh172.
    • (2004) Nucleic Acids Res , vol.32
    • Chiu, J.1    March, P.E.2    Lee, R.3    Tillett, D.4
  • 25
    • 34447527363 scopus 로고    scopus 로고
    • Improved native affinity purification of RNA
    • Batey RT, Kieft JS. 2007. Improved native affinity purification of RNA. RNA 13:1384-1389. http://dx.doi.org/10.1261/rna.528007.
    • (2007) RNA , vol.13 , pp. 1384-1389
    • Batey, R.T.1    Kieft, J.S.2
  • 26
    • 78651097570 scopus 로고    scopus 로고
    • Structural basis for active site closure by the poliovirus RNA-dependent RNA polymerase
    • Gong P, Peersen OB. 2010. Structural basis for active site closure by the poliovirus RNA-dependent RNA polymerase. Proc Natl Acad Sci USA 107:22505-22510. http://dx.doi.org/10.1073/pnas.1007626107.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 22505-22510
    • Gong, P.1    Peersen, O.B.2
  • 27
    • 34548148632 scopus 로고    scopus 로고
    • Structural and functional analysis of methylation and 5'-RNA sequence requirements of short capped RNAs by the methyltransferase domain of dengue virus NS5
    • Egloff MP, Decroly E, Malet H, Selisko B, Benarroch D, Ferron F, Canard B. 2007. Structural and functional analysis of methylation and 5'-RNA sequence requirements of short capped RNAs by the methyltransferase domain of dengue virus NS5. J Mol Biol 372:723-736. http://dx.doi.org/10.1016/j.jmb.2007.07.005.
    • (2007) J Mol Biol , vol.372 , pp. 723-736
    • Egloff, M.P.1    Decroly, E.2    Malet, H.3    Selisko, B.4    Benarroch, D.5    Ferron, F.6    Canard, B.7
  • 28
    • 84859096687 scopus 로고    scopus 로고
    • Effect of the methyltransferase domain of Japanese encephalitis virus NS5 on the polymerase activity
    • Wang Q, Weng L, Tian X, Counor D, Sun J, Mao Y, Deubel V, Okada H, Toyoda T. 2012. Effect of the methyltransferase domain of Japanese encephalitis virus NS5 on the polymerase activity. Biochim Biophys Acta 1819:411-418. http://dx.doi.org/10.1016/j.bbagrm.2012.01.003.
    • (2012) Biochim Biophys Acta , vol.1819 , pp. 411-418
    • Wang, Q.1    Weng, L.2    Tian, X.3    Counor, D.4    Sun, J.5    Mao, Y.6    Deubel, V.7    Okada, H.8    Toyoda, T.9
  • 29
    • 80053317134 scopus 로고    scopus 로고
    • Functional RNA elements in the dengue virus genome
    • Gebhard LG, Filomatori CV, Gamarnik AV. 2011. Functional RNA elements in the dengue virus genome. Viruses 3:1739-1756. http://dx.doi.org/10.3390/v3091739.
    • (2011) Viruses , vol.3 , pp. 1739-1756
    • Gebhard, L.G.1    Filomatori, C.V.2    Gamarnik, A.V.3
  • 30
    • 54049142396 scopus 로고    scopus 로고
    • Terminal structures of West Nile virus genomic RNA and their interactions with viral NS5 protein
    • Dong H, Zhang B, Shi PY. 2008. Terminal structures of West Nile virus genomic RNA and their interactions with viral NS5 protein. Virology 381:123-135. http://dx.doi.org/10.1016/j.virol.2008.07.040.
    • (2008) Virology , vol.381 , pp. 123-135
    • Dong, H.1    Zhang, B.2    Shi, P.Y.3
  • 31
    • 84858973676 scopus 로고    scopus 로고
    • Assembly, purification, and pre-steady-state kinetic analysis of active RNAdependent RNA polymerase elongation complex
    • Jin Z, Leveque V, Ma H, Johnson KA, Klumpp K. 2012. Assembly, purification, and pre-steady-state kinetic analysis of active RNAdependent RNA polymerase elongation complex. J Biol Chem 287: 10674-10683. http://dx.doi.org/10.1074/jbc.M111.325530.
    • (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
  • 32
    • 33747729605 scopus 로고    scopus 로고
    • Control of template positioning during de novo initiation of RNA synthesis by the bovine viral diarrhea virus NS5B polymerase
    • D'Abramo CM, Deval J, Cameron CE, Cellai L, Gotte M. 2006. Control of template positioning during de novo initiation of RNA synthesis by the bovine viral diarrhea virus NS5B polymerase. J Biol Chem 281:24991-24998. http://dx.doi.org/10.1074/jbc.M600474200.
    • (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
  • 33
    • 84872003714 scopus 로고    scopus 로고
    • Residues Arg283, Arg285, and Ile287 in the nucleotide binding pocket of bovine viral diarrhea virus NS5B RNA polymerase affect catalysis and fidelity
    • Curti E, Jaeger J. 2013. Residues Arg283, Arg285, and Ile287 in the nucleotide binding pocket of bovine viral diarrhea virus NS5B RNA polymerase affect catalysis and fidelity. J Virol 87:199-207. http://dx.doi.org/10.1128/JVI.06968-11.
    • (2013) J Virol , vol.87 , pp. 199-207
    • Curti, E.1    Jaeger, J.2
  • 34
    • 84877307801 scopus 로고    scopus 로고
    • Structures of coxsackievirus, rhinovirus, and poliovirus polymerase elongation complexes solved by engineering RNA mediated crystal contacts
    • Gong P, Kortus MG, Nix JC, Davis RE, Peersen OB. 2013. Structures of coxsackievirus, rhinovirus, and poliovirus polymerase elongation complexes solved by engineering RNA mediated crystal contacts. PLoS One 8:e60272. http://dx.doi.org/10.1371/journal.pone.0060272.
    • (2013) PLoS One , vol.8
    • Gong, P.1    Kortus, M.G.2    Nix, J.C.3    Davis, R.E.4    Peersen, O.B.5
  • 35
    • 0023924749 scopus 로고
    • Processivity in early stages of transcription by T7 RNA polymerase
    • Martin CT, Muller DK, Coleman JE. 1988. Processivity in early stages of transcription by T7 RNA polymerase. Biochemistry 27:3966-3974. http://dx.doi.org/10.1021/bi00411a012.
    • (1988) Biochemistry , vol.27 , pp. 3966-3974
    • Martin, C.T.1    Muller, D.K.2    Coleman, J.E.3
  • 36
    • 0034613030 scopus 로고    scopus 로고
    • Characterization of halted T7 RNA polymerase elongation complexes reveals multiple factors that contribute to stability
    • Mentesana PE, Chin-Bow ST, Sousa R, McAllister WT. 2000. Characterization of halted T7 RNA polymerase elongation complexes reveals multiple factors that contribute to stability. J Mol Biol 302:1049-1062. http://dx.doi.org/10.1006/jmbi.2000.4114.
    • (2000) J Mol Biol , vol.302 , pp. 1049-1062
    • Mentesana, P.E.1    Chin-Bow, S.T.2    Sousa, R.3    McAllister, W.T.4
  • 37
    • 67349220414 scopus 로고    scopus 로고
    • A quantitative stopped-flow fluorescence assay for measuring polymerase elongation rates
    • Gong P, Campagnola G, Peersen OB. 2009. A quantitative stopped-flow fluorescence assay for measuring polymerase elongation rates. Anal Biochem 391:45-55. http://dx.doi.org/10.1016/j.ab.2009.04.035.
    • (2009) Anal Biochem , vol.391 , pp. 45-55
    • Gong, P.1    Campagnola, G.2    Peersen, O.B.3
  • 40
    • 0034468107 scopus 로고    scopus 로고
    • Template requirements for RNA synthesis by a recombinant hepatitis C virus RNA-dependent RNA polymerase
    • Kao CC, Yang X, Kline A, Wang QM, Barket D, Heinz BA. 2000. Template requirements for RNA synthesis by a recombinant hepatitis C virus RNA-dependent RNA polymerase. J Virol 74:11121-11128. http://dx.doi.org/10.1128/JVI.74.23.11121-11128.2000.
    • (2000) J Virol , vol.74 , pp. 11121-11128
    • Kao, C.C.1    Yang, X.2    Kline, A.3    Wang, Q.M.4    Barket, D.5    Heinz, B.A.6
  • 41
    • 0034090927 scopus 로고    scopus 로고
    • Poliovirus RNA-dependent RNA polymerase (3Dpol). Assembly of stable, elongation-competent complexes by using a symmetrical primer-template substrate (sym/sub)
    • Arnold JJ, Cameron CE. 2000. Poliovirus RNA-dependent RNA polymerase (3Dpol). Assembly of stable, elongation-competent complexes by using a symmetrical primer-template substrate (sym/sub). J Biol Chem 275:5329-5336. http://dx.doi.org/10.1074/jbc.275.8.5329.
    • (2000) J Biol Chem , vol.275 , pp. 5329-5336
    • Arnold, J.J.1    Cameron, C.E.2
  • 42
    • 0027474037 scopus 로고
    • Computer-assisted identification of a putative methyltransferase domain in NS5 protein of flaviviruses and lambda 2 protein of reovirus
    • Koonin EV. 1993. Computer-assisted identification of a putative methyltransferase domain in NS5 protein of flaviviruses and lambda 2 protein of reovirus. J Gen Virol 74:733-740. http://dx.doi.org/10.1099/0022-1317-74-4-733.
    • (1993) J Gen Virol , vol.74 , pp. 733-740
    • Koonin, E.V.1
  • 43
    • 0024398958 scopus 로고
    • Coronavirus genome: prediction of putative functional domains in the nonstructural polyprotein by comparative amino acid sequence analysis
    • Gorbalenya AE, Koonin EV, Donchenko AP, Blinov VM. 1989. Coronavirus genome: prediction of putative functional domains in the nonstructural polyprotein by comparative amino acid sequence analysis. Nucleic Acids Res 17:4847-4861. http://dx.doi.org/10.1093/nar/17.12.4847.
    • (1989) Nucleic Acids Res , vol.17 , pp. 4847-4861
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 44
    • 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, Tordo N. 1990. Sequence comparison of five polymerases (L proteins) of unsegmented negative-strand RNA viruses: theoretical assignment of functional domains. J Gen Virol 71:1153-1162. http://dx.doi.org/10.1099/0022-1317-71-5-1153.
    • (1990) J Gen Virol , vol.71 , pp. 1153-1162
    • Poch, O.1    Blumberg, B.M.2    Bougueleret, L.3    Tordo, N.4
  • 45
    • 33846833843 scopus 로고    scopus 로고
    • Stabilization of poliovirus polymerase by NTP binding and fingers-thumb interactions
    • Thompson AA, Albertini RA, Peersen OB. 2007. Stabilization of poliovirus polymerase by NTP binding and fingers-thumb interactions. J Mol Biol 366:1459-1474. http://dx.doi.org/10.1016/j.jmb.2006.11.070.
    • (2007) J Mol Biol , vol.366 , pp. 1459-1474
    • Thompson, A.A.1    Albertini, R.A.2    Peersen, O.B.3
  • 46
    • 84857997971 scopus 로고    scopus 로고
    • A template RNA entry channel in the fingers domain of the poliovirus polymerase
    • Kortus MG, Kempf BJ, Haworth KG, Barton DJ, Peersen OB. 2012. A template RNA entry channel in the fingers domain of the poliovirus polymerase. J Mol Biol 417:263-278. http://dx.doi.org/10.1016/j.jmb.2012.01.049.
    • (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
  • 47
    • 4644238112 scopus 로고    scopus 로고
    • Structural basis for proteolysisdependent activation of the poliovirus RNA-dependent RNA polymerase
    • Thompson AA, Peersen OB. 2004. Structural basis for proteolysisdependent activation of the poliovirus RNA-dependent RNA polymerase. EMBO J 23:3462-3471. http://dx.doi.org/10.1038/sj.emboj.7600357.
    • (2004) EMBO J , vol.23 , pp. 3462-3471
    • Thompson, A.A.1    Peersen, O.B.2
  • 48
    • 0037184036 scopus 로고    scopus 로고
    • The interdomain region of dengue NS5 protein that binds to the viral helicase NS3 contains independently functional importin beta 1 and importin alpha/beta-recognized nuclear localization signals
    • Brooks AJ, Johansson M, John AV, Xu Y, Jans DA, Vasudevan SG. 2002. The interdomain region of dengue NS5 protein that binds to the viral helicase NS3 contains independently functional importin beta 1 and importin alpha/beta-recognized nuclear localization signals. J Biol Chem 277:36399-36407. http://dx.doi.org/10.1074/jbc.M204977200.
    • (2002) J Biol Chem , vol.277 , pp. 36399-36407
    • Brooks, A.J.1    Johansson, M.2    John, A.V.3    Xu, Y.4    Jans, D.A.5    Vasudevan, S.G.6
  • 49
    • 0035061425 scopus 로고    scopus 로고
    • A small region of the dengue virus-encoded RNA-dependent RNA polymerase, NS5, confers interaction with both the nuclear transport receptor importinbeta and the viral helicase, NS3
    • Johansson M, Brooks AJ, Jans DA, Vasudevan SG. 2001. A small region of the dengue virus-encoded RNA-dependent RNA polymerase, NS5, confers interaction with both the nuclear transport receptor importinbeta and the viral helicase, NS3. J Gen Virol 82:735-745.
    • (2001) J Gen Virol , vol.82 , pp. 735-745
    • Johansson, M.1    Brooks, A.J.2    Jans, D.A.3    Vasudevan, S.G.4
  • 50
    • 84864436647 scopus 로고    scopus 로고
    • Dengue virus nonstructural protein 5 adopts multiple conformations in solution
    • Bussetta C, Choi KH. 2012. Dengue virus nonstructural protein 5 adopts multiple conformations in solution. Biochemistry 51:5921-5931. http://dx.doi.org/10.1021/bi300406n.
    • (2012) Biochemistry , vol.51 , pp. 5921-5931
    • Bussetta, C.1    Choi, K.H.2
  • 51
    • 0035919073 scopus 로고    scopus 로고
    • A novel mechanism to ensure terminal initiation by hepatitis C virus NS5B polymerase
    • Hong Z, Cameron CE, Walker MP, Castro C, Yao N, Lau JY, Zhong W. 2001. A novel mechanism to ensure terminal initiation by hepatitis C virus NS5B polymerase. Virology 285:6-11. http://dx.doi.org/10.1006/viro.2001.0948.
    • (2001) Virology , vol.285 , pp. 6-11
    • Hong, Z.1    Cameron, C.E.2    Walker, M.P.3    Castro, C.4    Yao, N.5    Lau, J.Y.6    Zhong, W.7
  • 53
    • 2442498536 scopus 로고    scopus 로고
    • Poliovirus RNA-dependent RNA polymerase (3Dpol): pre-steady-state kinetic analysis of ribonucleotide incorporation in the presence of Mn2+
    • Arnold JJ, Gohara DW, Cameron CE. 2004. Poliovirus RNA-dependent RNA polymerase (3Dpol): pre-steady-state kinetic analysis of ribonucleotide incorporation in the presence of Mn2+. Biochemistry 43:5138-5148. http://dx.doi.org/10.1021/bi035213q.
    • (2004) Biochemistry , vol.43 , pp. 5138-5148
    • Arnold, J.J.1    Gohara, D.W.2    Cameron, C.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.