메뉴 건너뛰기




Volumn 4, Issue 4, 2013, Pages 351-367

RNA synthetic mechanisms employed by diverse families of RNA viruses

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED RNA; MESSENGER RNA; POLYPEPTIDE; PROTEIN VP1; RDRP POLYPEPTIDE; RNA POLYMERASE; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS RNA;

EID: 84879176096     PISSN: 17577004     EISSN: 17577012     Source Type: Journal    
DOI: 10.1002/wrna.1164     Document Type: Article
Times cited : (73)

References (108)
  • 1
    • 40649100793 scopus 로고    scopus 로고
    • Structure-function relationships among RNA-dependent RNA polymerases
    • Ng KK, Arnold JJ, Cameron CE. Structure-function relationships among RNA-dependent RNA polymerases. Curr Top Microbiol Immunol 2008, 320: 137-156.
    • (2008) Curr Top Microbiol Immunol , vol.320 , pp. 137-156
    • Ng, K.K.1    Arnold, J.J.2    Cameron, C.E.3
  • 2
    • 70450211764 scopus 로고    scopus 로고
    • Potential targets and their relevant inhibitors in anti-influenza fields
    • 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.
    • (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
  • 5
    • 0037844744 scopus 로고    scopus 로고
    • The genome-linked protein VPg of the Norwalk virus binds eIF3, suggesting its role in translation initiation complex recruitment
    • Daughenbaugh KF, Fraser CS, Hershey JW, Hardy ME. The genome-linked protein VPg of the Norwalk virus binds eIF3, suggesting its role in translation initiation complex recruitment. EMBO J 2003, 22:2852-2859.
    • (2003) EMBO J , vol.22 , pp. 2852-2859
    • Daughenbaugh, K.F.1    Fraser, C.S.2    Hershey, J.W.3    Hardy, M.E.4
  • 8
    • 0018343299 scopus 로고
    • Comparative studies on the genomes of some picornaviruses: denaturation mapping of replicative form RNA and electron microscopy of heteroduplex RNA
    • Cumakov IM, Lipskaya GY, Agol VI. Comparative studies on the genomes of some picornaviruses: denaturation mapping of replicative form RNA and electron microscopy of heteroduplex RNA. Virology 1979, 92:259-270.
    • (1979) Virology , vol.92 , pp. 259-270
    • Cumakov, I.M.1    Lipskaya, G.Y.2    Agol, V.I.3
  • 9
    • 0023062565 scopus 로고
    • Flavivirus replication strategy
    • Westaway EG. Flavivirus replication strategy. Adv Virus Res 1987, 33:45-90.
    • (1987) Adv Virus Res , vol.33 , pp. 45-90
    • Westaway, E.G.1
  • 10
    • 0021893927 scopus 로고
    • Replication strategy of kunjin virus: evidence for recycling role of replicative form RNA as template in semiconservative and asymmetric replication
    • Chu PW, Westaway E. Replication strategy of kunjin virus: evidence for recycling role of replicative form RNA as template in semiconservative and asymmetric replication. Virology 1985, 140:68-79.
    • (1985) Virology , vol.140 , pp. 68-79
    • Chu, P.W.1    Westaway, E.2
  • 11
    • 0014413444 scopus 로고
    • Structure of the poliovirus replicative intermediate RNA
    • Baltimore D. Structure of the poliovirus replicative intermediate RNA. J Mol Biol 1968, 32:359-368.
    • (1968) J Mol Biol , vol.32 , pp. 359-368
    • Baltimore, D.1
  • 12
    • 0015166717 scopus 로고
    • Architecture of the poliovirus replicative intermediate RNA
    • Savage T, Granboulan N, Girard M. Architecture of the poliovirus replicative intermediate RNA. Biochimie 1971, 53:533-543.
    • (1971) Biochimie , vol.53 , pp. 533-543
    • Savage, T.1    Granboulan, N.2    Girard, M.3
  • 13
    • 0019406259 scopus 로고
    • Identification and characterization of type 2 dengue virus replicative intermediate and replicative form RNAs
    • Cleaves GR, Ryan TE, Schlesinger RW. Identification and characterization of type 2 dengue virus replicative intermediate and replicative form RNAs. Virology 1981, 111:73-83.
    • (1981) Virology , vol.111 , pp. 73-83
    • Cleaves, G.R.1    Ryan, T.E.2    Schlesinger, R.W.3
  • 14
    • 33845750075 scopus 로고    scopus 로고
    • A contemporary view of coronavirus transcription
    • Sawicki SG, Sawicki DL, Siddell SG. A contemporary view of coronavirus transcription. J Virol 2007, 81:20-29.
    • (2007) J Virol , vol.81 , pp. 20-29
    • Sawicki, S.G.1    Sawicki, D.L.2    Siddell, S.G.3
  • 15
    • 80051781196 scopus 로고    scopus 로고
    • Nucleoproteins and nucleocapsids of negative-strand RNA viruses
    • Ruigrok RW, Crepin T, Kolakofsky D. Nucleoproteins and nucleocapsids of negative-strand RNA viruses. Curr Opin Microbiol 2011, 14:504-510.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 504-510
    • Ruigrok, R.W.1    Crepin, T.2    Kolakofsky, D.3
  • 16
    • 77749322610 scopus 로고    scopus 로고
    • Towards an atomic resolution understanding of the influenza virus replication machinery
    • Ruigrok RW, Crepin T, Hart DJ, Cusack S. Towards an atomic resolution understanding of the influenza virus replication machinery. Curr Opin Struct Biol 2010, 20:104-113.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 104-113
    • Ruigrok, R.W.1    Crepin, T.2    Hart, D.J.3    Cusack, S.4
  • 17
    • 81555228721 scopus 로고    scopus 로고
    • Structural insights into the rhabdovirus transcription/replication complex
    • Ivanov I, Yabukarski F, Ruigrok RW, Jamin M. Structural insights into the rhabdovirus transcription/replication complex. Virus Res 2011, 162: 126-137.
    • (2011) Virus Res , vol.162 , pp. 126-137
    • Ivanov, I.1    Yabukarski, F.2    Ruigrok, R.W.3    Jamin, M.4
  • 18
    • 84865294044 scopus 로고    scopus 로고
    • Architecture and regulation of negative-strand viral enzymatic machinery
    • Kranzusch PJ, Whelan SP. Architecture and regulation of negative-strand viral enzymatic machinery. RNA Biol 2012, 9:941-948.
    • (2012) RNA Biol , vol.9 , pp. 941-948
    • Kranzusch, P.J.1    Whelan, S.P.2
  • 19
    • 0034948006 scopus 로고    scopus 로고
    • Polymerase slippage at vesicular stomatitis virus gene junctions to generate poly-(A) is regulated by the upstream 3'-AUAC-5' tetranucleotide: implications for the mechanism of transcription termination
    • Barr JN, Wertz GW. Polymerase slippage at vesicular stomatitis virus gene junctions to generate poly-(A) is regulated by the upstream 3'-AUAC-5' tetranucleotide: implications for the mechanism of transcription termination. J Virol 2001, 75:6901-6913.
    • (2001) J Virol , vol.75 , pp. 6901-6913
    • Barr, J.N.1    Wertz, G.W.2
  • 20
    • 77956536783 scopus 로고    scopus 로고
    • Influenza A virus polymerase: structural insights into replication and host adaptation mechanisms
    • Boivin S, Cusack S, Ruigrok RW, Hart DJ. Influenza A virus polymerase: structural insights into replication and host adaptation mechanisms. J Biol Chem 2010, 285:28411-28417.
    • (2010) J Biol Chem , vol.285 , pp. 28411-28417
    • Boivin, S.1    Cusack, S.2    Ruigrok, R.W.3    Hart, D.J.4
  • 21
    • 34447299235 scopus 로고    scopus 로고
    • Orthomyxoviridae: the viruses and their replication
    • In:, and eds. 5th ed. Philadelphia, PA: Lippincott, Williams & Wilkins;
    • Palese P, Shaw ML. Orthomyxoviridae: the viruses and their replication. In: Knipe DM, and Peter Howley eds. Fields Virology. 5th ed. Philadelphia, PA: Lippincott, Williams & Wilkins; 2007, 1917-1974.
    • (2007) Fields Virology , pp. 1917-1974
    • Palese, P.1    Shaw, M.L.2    Knipe, D.M.3    Peter, H.4
  • 22
    • 84856217709 scopus 로고    scopus 로고
    • 2008 estimate of worldwide rotavirus-associated mortality in children younger than 5 years before the introduction of universal rotavirus vaccination programmes: a systematic review and meta-analysis
    • Tate JE, Burton AH, Boschi-Pinto C, Steele AD, Duque J, Parashar UD. 2008 estimate of worldwide rotavirus-associated mortality in children younger than 5 years before the introduction of universal rotavirus vaccination programmes: a systematic review and meta-analysis. Lancet Infect Dis 2012, 12:136-141.
    • (2012) Lancet Infect Dis , vol.12 , pp. 136-141
    • Tate, J.E.1    Burton, A.H.2    Boschi-Pinto, C.3    Steele, A.D.4    Duque, J.5    Parashar, U.D.6
  • 23
    • 77953312059 scopus 로고    scopus 로고
    • Mechanism of intraparticle synthesis of the rotavirus double-stranded RNA genome
    • Guglielmi KM, McDonald SM, Patton JT. Mechanism of intraparticle synthesis of the rotavirus double-stranded RNA genome. J Biol Chem 2010, 285:18123-18128.
    • (2010) J Biol Chem , vol.285 , pp. 18123-18128
    • Guglielmi, K.M.1    McDonald, S.M.2    Patton, J.T.3
  • 25
    • 1542268891 scopus 로고    scopus 로고
    • Nonstructural proteins involved in genome packaging and replication of rotaviruses and other members of the Reoviridae
    • Taraporewala ZF, Patton JT. Nonstructural proteins involved in genome packaging and replication of rotaviruses and other members of the Reoviridae. Virus Res 2004, 101:57-66.
    • (2004) Virus Res , vol.101 , pp. 57-66
    • Taraporewala, Z.F.1    Patton, J.T.2
  • 26
    • 84874420024 scopus 로고    scopus 로고
    • Autophagy hijacked through viroporin-activated calcium/calmodulin-dependent kinase kinase-β signaling is required for rotavirus replication
    • Crawford SE, Hyser JM, Utama B, Estes MK. Autophagy hijacked through viroporin-activated calcium/calmodulin-dependent kinase kinase-β signaling is required for rotavirus replication. Proc Natl Acad Sci U S A 2012, 109:E3405-E3413.
    • (2012) Proc Natl Acad Sci U S A , vol.109
    • Crawford, S.E.1    Hyser, J.M.2    Utama, B.3    Estes, M.K.4
  • 27
    • 77953300336 scopus 로고    scopus 로고
    • Rotaviruses associate with cellular lipid droplet components to replicate in viroplasms, and compounds disrupting or blocking lipid droplets inhibit viroplasm formation and viral replication
    • Cheung W, Gill M, Esposito A, Kaminski CF, Courousse N, Chwetzoff S, Trugnan G, Keshavan N, Lever A, Desselberger U. Rotaviruses associate with cellular lipid droplet components to replicate in viroplasms, and compounds disrupting or blocking lipid droplets inhibit viroplasm formation and viral replication. J Virol 2010, 84:6782-6798.
    • (2010) J Virol , vol.84 , pp. 6782-6798
    • Cheung, W.1    Gill, M.2    Esposito, A.3    Kaminski, C.F.4    Courousse, N.5    Chwetzoff, S.6    Trugnan, G.7    Keshavan, N.8    Lever, A.9    Desselberger, U.10
  • 28
    • 79952101724 scopus 로고    scopus 로고
    • Assortment and packaging of the segmented rotavirus genome
    • McDonald SM, Patton JT. Assortment and packaging of the segmented rotavirus genome. Trends Microbiol 2011, 19:136-144.
    • (2011) Trends Microbiol , vol.19 , pp. 136-144
    • McDonald, S.M.1    Patton, J.T.2
  • 29
    • 0030831560 scopus 로고    scopus 로고
    • Rotavirus RNA polymerase requires the core shell protein to synthesize the double-stranded RNA genome
    • Patton JT, Jones MT, Kalbach AN, He YW, Xiaobo J. Rotavirus RNA polymerase requires the core shell protein to synthesize the double-stranded RNA genome. J Virol 1997, 71:9618-9626.
    • (1997) J Virol , vol.71 , pp. 9618-9626
    • Patton, J.T.1    Jones, M.T.2    Kalbach, A.N.3    He, Y.W.4    Xiaobo, J.5
  • 30
    • 0025281467 scopus 로고
    • Rotavirus RNA replication: single-stranded RNA extends from the replicase particle
    • Patton JT, Gallegos CO. Rotavirus RNA replication: single-stranded RNA extends from the replicase particle. J Gen Virol 1990, 71:1087-1094.
    • (1990) J Gen Virol , vol.71 , pp. 1087-1094
    • Patton, J.T.1    Gallegos, C.O.2
  • 31
    • 50549097204 scopus 로고    scopus 로고
    • Bluetongue virus: dissection of the polymerase complex
    • Roy P. Bluetongue virus: dissection of the polymerase complex. J Gen Virol 2008, 89:1789-1804.
    • (2008) J Gen Virol , vol.89 , pp. 1789-1804
    • Roy, P.1
  • 32
    • 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. Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site. Nat Struct Biol 1999, 6:937-943.
    • (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
  • 33
    • 4644238112 scopus 로고    scopus 로고
    • Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase
    • Thompson AA, Peersen OB. Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase. EMBO J 2004, 23:3462-3471.
    • (2004) EMBO J , vol.23 , pp. 3462-3471
    • Thompson, A.A.1    Peersen, O.B.2
  • 34
    • 1942501581 scopus 로고    scopus 로고
    • Crystal structure of norwalk virus polymerase reveals the carboxyl terminus in the active site cleft
    • Ng KK, Pendas-Franco N, Rojo J, Boga JA, Machin A, Alonso JM, Parra F. Crystal structure of norwalk virus polymerase reveals the carboxyl terminus in the active site cleft. J Biol Chem 2004, 279:16638-16645.
    • (2004) J Biol Chem , vol.279 , pp. 16638-16645
    • Ng, K.K.1    Pendas-Franco, N.2    Rojo, J.3    Boga, J.A.4    Machin, A.5    Alonso, J.M.6    Parra, F.7
  • 36
    • 70549084057 scopus 로고    scopus 로고
    • The ins and outs of four-tunneled reoviridae RNA-dependent RNA polymerases
    • McDonald SM, Tao YJ, Patton JT. The ins and outs of four-tunneled reoviridae RNA-dependent RNA polymerases. Curr Opin Struct Biol 2009, 19:775-782.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 775-782
    • McDonald, S.M.1    Tao, Y.J.2    Patton, J.T.3
  • 38
    • 0032567393 scopus 로고    scopus 로고
    • Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure
    • O'Reilly EK, Kao CC. Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure. Virology 1998, 252:287-303.
    • (1998) Virology , vol.252 , pp. 287-303
    • O'Reilly, E.K.1    Kao, C.C.2
  • 39
    • 0032518374 scopus 로고    scopus 로고
    • A mechanism for all polymerases
    • Steitz TA. A mechanism for all polymerases. Nature 1998, 391:231-232.
    • (1998) Nature , vol.391 , pp. 231-232
    • Steitz, T.A.1
  • 40
    • 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 2012, 8:e1002851.
    • (2012) PLoS Comput Biol , vol.8
    • Shen, H.1    Sun, H.2    Li, G.3
  • 41
    • 2442461170 scopus 로고    scopus 로고
    • Poliovirus RNA-dependent RNA polymerase (3Dpol): kinetic, thermodynamic, and structural analysis of ribonucleotide selection
    • Gohara DW, Arnold JJ, Cameron CE. Poliovirus RNA-dependent RNA polymerase (3Dpol): kinetic, thermodynamic, and structural analysis of ribonucleotide selection. Biochemistry 2004, 43:5149-5158.
    • (2004) Biochemistry , vol.43 , pp. 5149-5158
    • Gohara, D.W.1    Arnold, J.J.2    Cameron, C.E.3
  • 42
    • 84862306547 scopus 로고    scopus 로고
    • Mutational analysis of residues involved in nucleotide and divalent cation stabilization in the rotavirus RNA-dependent RNA polymerase catalytic pocket
    • Ogden KM, Ramanathan HN, Patton JT. Mutational analysis of residues involved in nucleotide and divalent cation stabilization in the rotavirus RNA-dependent RNA polymerase catalytic pocket. Virology 2012, 431:12-20.
    • (2012) Virology , vol.431 , pp. 12-20
    • Ogden, K.M.1    Ramanathan, H.N.2    Patton, J.T.3
  • 44
    • 18744392514 scopus 로고    scopus 로고
    • RNA synthesis in a cage-structural studies of reovirus polymerase lambda3
    • Tao Y, Farsetta DL, Nibert ML, Harrison SC. RNA synthesis in a cage-structural studies of reovirus polymerase lambda3. Cell 2002, 111:733-745.
    • (2002) Cell , vol.111 , pp. 733-745
    • Tao, Y.1    Farsetta, D.L.2    Nibert, M.L.3    Harrison, S.C.4
  • 45
    • 79551694020 scopus 로고    scopus 로고
    • Residues of the rotavirus RNA-dependent RNA polymerase template entry tunnel that mediate RNA recognition and genome replication
    • Ogden KM, Ramanathan HN, Patton JT. Residues of the rotavirus RNA-dependent RNA polymerase template entry tunnel that mediate RNA recognition and genome replication. J Virol 2011, 85:1958-1969.
    • (2011) J Virol , vol.85 , pp. 1958-1969
    • Ogden, K.M.1    Ramanathan, H.N.2    Patton, J.T.3
  • 46
    • 0029278747 scopus 로고
    • DNA replication. A familiar ring to DNA polymerase processivity
    • Wyman C, Botchan M. DNA replication. A familiar ring to DNA polymerase processivity. Curr Biol 1995, 5:334-337.
    • (1995) Curr Biol , vol.5 , pp. 334-337
    • Wyman, C.1    Botchan, M.2
  • 47
    • 0033989278 scopus 로고    scopus 로고
    • De novo initiation of RNA synthesis by the RNA-dependent RNA polymerase (NS5B) of hepatitis C virus
    • Luo G, Hamatake RK, Mathis DM, Racela J, Rigat KL, Lemm J, Colonno RJ. De novo initiation of RNA synthesis by the RNA-dependent RNA polymerase (NS5B) of hepatitis C virus. J Virol 2000, 74:851-863.
    • (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
  • 48
    • 0033524332 scopus 로고    scopus 로고
    • De novo initiation of RNA synthesis by a recombinant flaviviridae RNA-dependent RNA polymerase
    • Kao CC, Del Vecchio AM, Zhong W. De novo initiation of RNA synthesis by a recombinant flaviviridae RNA-dependent RNA polymerase. Virology 1999, 253:1-7.
    • (1999) Virology , vol.253 , pp. 1-7
    • Kao, C.C.1    Del Vecchio, A.M.2    Zhong, W.3
  • 50
    • 0036892593 scopus 로고    scopus 로고
    • Requirements for de novo initiation of RNA synthesis by recombinant flaviviral RNA-dependent RNA polymerases
    • Ranjith-Kumar CT, Gutshall L, Kim MJ, Sarisky RT, Kao CC. Requirements for de novo initiation of RNA synthesis by recombinant flaviviral RNA-dependent RNA polymerases. J Virol 2002, 76:12526-12536.
    • (2002) J Virol , vol.76 , pp. 12526-12536
    • Ranjith-Kumar, C.T.1    Gutshall, L.2    Kim, M.J.3    Sarisky, R.T.4    Kao, C.C.5
  • 51
    • 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. 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 U S A 2004, 101:4425-4430.
    • (2004) Proc Natl Acad Sci U S A , 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
  • 52
    • 0036120573 scopus 로고    scopus 로고
    • Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides
    • Bressanelli S, Tomei L, Rey FA, De Francesco R. Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides. J Virol 2002, 76:3482-3492.
    • (2002) J Virol , vol.76 , pp. 3482-3492
    • Bressanelli, S.1    Tomei, L.2    Rey, F.A.3    De Francesco, R.4
  • 53
    • 81755166311 scopus 로고    scopus 로고
    • The genome-linked protein VPg of vertebrate viruses-a multifaceted protein
    • Goodfellow I. The genome-linked protein VPg of vertebrate viruses-a multifaceted protein. Curr Opin Virol 2011, 1:355-362.
    • (2011) Curr Opin Virol , vol.1 , pp. 355-362
    • Goodfellow, I.1
  • 54
    • 84855826064 scopus 로고    scopus 로고
    • VPg-primed RNA synthesis of norovirus RNA-dependent RNA polymerases by using a novel cell-based assay
    • Subba-Reddy CV, Goodfellow I, Kao CC. VPg-primed RNA synthesis of norovirus RNA-dependent RNA polymerases by using a novel cell-based assay. J Virol 2011, 85:13027-13037.
    • (2011) J Virol , vol.85 , pp. 13027-13037
    • Subba-Reddy, C.V.1    Goodfellow, I.2    Kao, C.C.3
  • 55
    • 77953260284 scopus 로고    scopus 로고
    • Expanding knowledge of P3 proteins in the poliovirus lifecycle
    • Cameron CE, Oh HS, Moustafa IM. Expanding knowledge of P3 proteins in the poliovirus lifecycle. Future Microbiol 2010, 5:867-881.
    • (2010) Future Microbiol , vol.5 , pp. 867-881
    • Cameron, C.E.1    Oh, H.S.2    Moustafa, I.M.3
  • 56
    • 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 2004, 279:47212-47221.
    • (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
  • 58
    • 70549097349 scopus 로고    scopus 로고
    • Structural insights into replication initiation and elongation processes by the FMDV RNA-dependent RNA polymerase
    • Ferrer-Orta C, Agudo R, Domingo E, Verdaguer N. Structural insights into replication initiation and elongation processes by the FMDV RNA-dependent RNA polymerase. Curr Opin Struct Biol 2009, 19:752-758.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 752-758
    • Ferrer-Orta, C.1    Agudo, R.2    Domingo, E.3    Verdaguer, N.4
  • 60
    • 0019394947 scopus 로고
    • A unique cap(m7Gpppxm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription
    • Plotch SJ, Bouloy M, Ulmanen I, Krug RM. A unique cap(m7Gpppxm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription. Cell 1981, 23:847-858.
    • (1981) Cell , vol.23 , pp. 847-858
    • Plotch, S.J.1    Bouloy, M.2    Ulmanen, I.3    Krug, R.M.4
  • 61
    • 0019850995 scopus 로고
    • Selected host cell capped RNA fragments prime influenza A viral transcription in vivo
    • Beaton AR, Krug RM. Selected host cell capped RNA fragments prime influenza A viral transcription in vivo. Nucleic Acids Res 1981, 9:4423-4436.
    • (1981) Nucleic Acids Res , vol.9 , pp. 4423-4436
    • Beaton, A.R.1    Krug, R.M.2
  • 62
    • 33144488409 scopus 로고    scopus 로고
    • Different de novo initiation strategies are used by influenza virus RNA polymerase on its cRNA and viral RNA promoters during viral RNA replication
    • Deng T, Vreede FT, Brownlee GG. Different de novo initiation strategies are used by influenza virus RNA polymerase on its cRNA and viral RNA promoters during viral RNA replication. J Virol 2006, 80:2237-2348.
    • (2006) J Virol , vol.80 , pp. 2237-2348
    • Deng, T.1    Vreede, F.T.2    Brownlee, G.G.3
  • 63
    • 0033169059 scopus 로고    scopus 로고
    • Distinct regions of the influenza virus PB1 polymerase subunit recognize vRNA and cRNA templates
    • Gonzalez S, Ortin J. Distinct regions of the influenza virus PB1 polymerase subunit recognize vRNA and cRNA templates. EMBO J 1999, 18:3767-3775.
    • (1999) EMBO J , vol.18 , pp. 3767-3775
    • Gonzalez, S.1    Ortin, J.2
  • 64
    • 0029998594 scopus 로고    scopus 로고
    • Determinants of membrane association for poliovirus protein 3ab
    • Towner JS, Ho TV, Semler BL. Determinants of membrane association for poliovirus protein 3ab. J Biol Chem 1996, 271:26810-26818.
    • (1996) J Biol Chem , vol.271 , pp. 26810-26818
    • Towner, J.S.1    Ho, T.V.2    Semler, B.L.3
  • 65
    • 0033798416 scopus 로고    scopus 로고
    • Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: an autophagy-like origin for virus-induced vesicles
    • Suhy DA, Giddings TH Jr, Kirkegaard K. Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: an autophagy-like origin for virus-induced vesicles. J Virol 2000, 74:8953-8965.
    • (2000) J Virol , vol.74 , pp. 8953-8965
    • Suhy, D.A.1    Giddings, T.H.2    Kirkegaard, K.3
  • 66
    • 32444439218 scopus 로고    scopus 로고
    • Poliovirus protein 3AB displays nucleic acid chaperone and helix-destabilizing activities
    • DeStefano JJ, Titilope O. Poliovirus protein 3AB displays nucleic acid chaperone and helix-destabilizing activities. J Virol 2006, 80:1662-1671.
    • (2006) J Virol , vol.80 , pp. 1662-1671
    • DeStefano, J.J.1    Titilope, O.2
  • 67
    • 78751674527 scopus 로고    scopus 로고
    • The twenty-nine amino acid C-terminal cytoplasmic domain of poliovirus 3AB is critical for nucleic acid chaperone activity
    • Gangaramani DR, Eden EL, Shah M, Destefano JJ. The twenty-nine amino acid C-terminal cytoplasmic domain of poliovirus 3AB is critical for nucleic acid chaperone activity. RNA Biol 2010, 7:820-829.
    • (2010) RNA Biol , vol.7 , pp. 820-829
    • Gangaramani, D.R.1    Eden, E.L.2    Shah, M.3    Destefano, J.J.4
  • 70
    • 0037223707 scopus 로고    scopus 로고
    • Initiation of poliovirus negative-strand RNA synthesis requires precursor forms of P2 proteins
    • Jurgens C, Flanegan JB. Initiation of poliovirus negative-strand RNA synthesis requires precursor forms of P2 proteins. J Virol 2003, 77:1075-1083.
    • (2003) J Virol , vol.77 , pp. 1075-1083
    • Jurgens, C.1    Flanegan, J.B.2
  • 71
    • 0037013317 scopus 로고    scopus 로고
    • Similar structural basis for membrane localization and protein priming by an RNA-dependent RNA polymerase
    • Lyle JM, Clewell A, Richmond K, Richards OC, Hope DA, Schultz SC, Kirkegaard K. Similar structural basis for membrane localization and protein priming by an RNA-dependent RNA polymerase. J Biol Chem 2002, 277:16324-16331.
    • (2002) J Biol Chem , vol.277 , pp. 16324-16331
    • Lyle, J.M.1    Clewell, A.2    Richmond, K.3    Richards, O.C.4    Hope, D.A.5    Schultz, S.C.6    Kirkegaard, K.7
  • 72
    • 57649219466 scopus 로고    scopus 로고
    • Picornavirus genome replication: roles of precursor proteins and rate-limiting steps in oriI-dependent VPg uridylylation
    • Pathak HB, Oh HS, Goodfellow IG, Arnold JJ, Cameron CE. Picornavirus genome replication: roles of precursor proteins and rate-limiting steps in oriI-dependent VPg uridylylation. J Biol Chem 2008, 283:30677-30688.
    • (2008) J Biol Chem , vol.283 , pp. 30677-30688
    • Pathak, H.B.1    Oh, H.S.2    Goodfellow, I.G.3    Arnold, J.J.4    Cameron, C.E.5
  • 73
    • 84855875985 scopus 로고    scopus 로고
    • The dependence of viral RNA replication on co-opted host factors
    • Nagy PD, Pogany J. The dependence of viral RNA replication on co-opted host factors. Nat Rev Microbiol 2012, 10:137-149.
    • (2012) Nat Rev Microbiol , vol.10 , pp. 137-149
    • Nagy, P.D.1    Pogany, J.2
  • 74
    • 0031571638 scopus 로고    scopus 로고
    • Structure of the RNA-dependent RNA polymerase of poliovirus
    • Hansen JL, Long AM, Schultz SC. Structure of the RNA-dependent RNA polymerase of poliovirus. Structure 1997, 5:1109-1122.
    • (1997) Structure , vol.5 , pp. 1109-1122
    • Hansen, J.L.1    Long, A.M.2    Schultz, S.C.3
  • 75
    • 0037150679 scopus 로고    scopus 로고
    • Visualization and functional analysis of RNA-dependent RNA polymerase lattices
    • Lyle JM, Bullitt E, Bienz K, Kirkegaard K. Visualization and functional analysis of RNA-dependent RNA polymerase lattices. Science 2002, 296:2218-2222.
    • (2002) Science , vol.296 , pp. 2218-2222
    • Lyle, J.M.1    Bullitt, E.2    Bienz, K.3    Kirkegaard, K.4
  • 76
  • 77
    • 0023388295 scopus 로고
    • Location of the binding domains for the RNA polymerase l and the ribonucleocapsid template within different halves of the NS phosphoprotein of vesicular stomatitis virus
    • Emerson SU, Schubert M. Location of the binding domains for the RNA polymerase l and the ribonucleocapsid template within different halves of the NS phosphoprotein of vesicular stomatitis virus. Proc Natl Acad Sci U S A 1987, 84:5655-5659.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 5655-5659
    • Emerson, S.U.1    Schubert, M.2
  • 80
    • 77949393859 scopus 로고    scopus 로고
    • Structure of the dimerization domain of the rabies virus phosphoprotein
    • Ivanov I, Crepin T, Jamin M, Ruigrok RW. Structure of the dimerization domain of the rabies virus phosphoprotein. J Virol 2010, 84:3707-3710.
    • (2010) J Virol , vol.84 , pp. 3707-3710
    • Ivanov, I.1    Crepin, T.2    Jamin, M.3    Ruigrok, R.W.4
  • 81
    • 67650872991 scopus 로고    scopus 로고
    • Structure of the vesicular stomatitis virus nucleocapsid in complex with the nucleocapsid-binding domain of the small polymerase cofactor, P
    • Green TJ, Luo M. Structure of the vesicular stomatitis virus nucleocapsid in complex with the nucleocapsid-binding domain of the small polymerase cofactor, P. Proc Natl Acad Sci U S A 2009, 106:11713-11718.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 11713-11718
    • Green, T.J.1    Luo, M.2
  • 82
    • 5144222412 scopus 로고    scopus 로고
    • Structure and function of the C-terminal domain of the polymerase cofactor of rabies virus
    • Mavrakis M, McCarthy AA, Roche S, Blondel D, Ruigrok RW. Structure and function of the C-terminal domain of the polymerase cofactor of rabies virus. J Mol Biol 2004, 343:819-831.
    • (2004) J Mol Biol , vol.343 , pp. 819-831
    • Mavrakis, M.1    McCarthy, A.A.2    Roche, S.3    Blondel, D.4    Ruigrok, R.W.5
  • 83
    • 37049018431 scopus 로고    scopus 로고
    • 0-P complex formation and encapsidation of viral genome RNA
    • 0-P complex formation and encapsidation of viral genome RNA. J Virol 2007, 81:13478-13485.
    • (2007) J Virol , vol.81 , pp. 13478-13485
    • Chen, M.1    Ogino, T.2    Banerjee, A.K.3
  • 84
    • 1242283916 scopus 로고    scopus 로고
    • Viral DNA polymerase scanning and the gymnastics of sendai virus RNA synthesis
    • Kolakofsky D, Le Mercier P, Iseni F, Garcin D. Viral DNA polymerase scanning and the gymnastics of sendai virus RNA synthesis. Virology 2004, 318:463-473.
    • (2004) Virology , vol.318 , pp. 463-473
    • Kolakofsky, D.1    Le Mercier, P.2    Iseni, F.3    Garcin, D.4
  • 87
    • 67249100913 scopus 로고    scopus 로고
    • Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site
    • Yuan P, Bartlam M, Lou Z, Chen S, Zhou J, He X, Lv Z, Ge R, Li X, Deng T, et al. Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site. Nature 2009, 458:909-913.
    • (2009) Nature , vol.458 , pp. 909-913
    • Yuan, P.1    Bartlam, M.2    Lou, Z.3    Chen, S.4    Zhou, J.5    He, X.6    Lv, Z.7    Ge, R.8    Li, X.9    Deng, T.10
  • 88
    • 33746815630 scopus 로고    scopus 로고
    • Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding
    • Hara K, Schmidt FI, Crow M, Brownlee GG. Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding. J Virol 2006, 80:7789-7798.
    • (2006) J Virol , vol.80 , pp. 7789-7798
    • Hara, K.1    Schmidt, F.I.2    Crow, M.3    Brownlee, G.G.4
  • 89
    • 50649089174 scopus 로고    scopus 로고
    • Crystal structure of the polymerase PA(C)-PB1(N) complex from an avian influenza H5N1 virus
    • He X, Zhou J, Bartlam M, Zhang R, Ma J, Lou Z, Li X, Li J, Joachimiak A, Zeng Z, et al. Crystal structure of the polymerase PA(C)-PB1(N) complex from an avian influenza H5N1 virus. Nature 2008, 454:1123-1126.
    • (2008) Nature , vol.454 , pp. 1123-1126
    • He, X.1    Zhou, J.2    Bartlam, M.3    Zhang, R.4    Ma, J.5    Lou, Z.6    Li, X.7    Li, J.8    Joachimiak, A.9    Zeng, Z.10
  • 94
    • 50849137828 scopus 로고    scopus 로고
    • Host determinant residue lysine 627 lies on the surface of a discrete, folded domain of influenza virus polymerase PB2 subunit
    • Tarendeau F, Crepin T, Guilligay D, Ruigrok RW, Cusack S, Hart DJ. Host determinant residue lysine 627 lies on the surface of a discrete, folded domain of influenza virus polymerase PB2 subunit. PLoS Pathog 2008, 4:e1000136.
    • (2008) PLoS Pathog , vol.4
    • Tarendeau, F.1    Crepin, T.2    Guilligay, D.3    Ruigrok, R.W.4    Cusack, S.5    Hart, D.J.6
  • 96
    • 65449163086 scopus 로고    scopus 로고
    • Structural basis of the influenza a virus RNA polymerase PB2 RNA-binding domain containing the pathogenicity-determinant lysine 627 residue
    • Kuzuhara T, Kise D, Yoshida H, Horita T, Murazaki Y, Nishimura A, Echigo N, Utsunomiya H, Tsuge H. Structural basis of the influenza a virus RNA polymerase PB2 RNA-binding domain containing the pathogenicity-determinant lysine 627 residue. J Biol Chem 2009, 284:6855-6860.
    • (2009) J Biol Chem , vol.284 , pp. 6855-6860
    • Kuzuhara, T.1    Kise, D.2    Yoshida, H.3    Horita, T.4    Murazaki, Y.5    Nishimura, A.6    Echigo, N.7    Utsunomiya, H.8    Tsuge, H.9
  • 97
    • 67649552964 scopus 로고    scopus 로고
    • Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase
    • Sugiyama K, Obayashi E, Kawaguchi A, Suzuki Y, Tame JR, Nagata K, Park SY. Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase. EMBO J 2009, 28:1803-1811.
    • (2009) EMBO J , vol.28 , pp. 1803-1811
    • Sugiyama, K.1    Obayashi, E.2    Kawaguchi, A.3    Suzuki, Y.4    Tame, J.R.5    Nagata, K.6    Park, S.Y.7
  • 98
    • 0029843594 scopus 로고    scopus 로고
    • Rotavirus VP1 alone specifically binds to the 3' end of viral mRNA, but the interaction is not sufficient to initiate minus-strand synthesis
    • Patton JT. Rotavirus VP1 alone specifically binds to the 3' end of viral mRNA, but the interaction is not sufficient to initiate minus-strand synthesis. J Virol 1996, 70:7940-7947.
    • (1996) J Virol , vol.70 , pp. 7940-7947
    • Patton, J.T.1
  • 99
  • 100
    • 77349116567 scopus 로고    scopus 로고
    • X-ray crystal structure of the rotavirus inner capsid particle at 3.8 Åresolution
    • McClain B, Settembre E, Temple BR, Bellamy AR, Harrison SC. X-ray crystal structure of the rotavirus inner capsid particle at 3.8 Åresolution. J Mol Biol 2010, 397:587-599.
    • (2010) J Mol Biol , vol.397 , pp. 587-599
    • McClain, B.1    Settembre, E.2    Temple, B.R.3    Bellamy, A.R.4    Harrison, S.C.5
  • 103
    • 79952579269 scopus 로고    scopus 로고
    • Rotavirus VP2 core shell regions critical for viral polymerase activation
    • McDonald SM, Patton JT. Rotavirus VP2 core shell regions critical for viral polymerase activation. J Virol 2011, 85:3095-3105.
    • (2011) J Virol , vol.85 , pp. 3095-3105
    • McDonald, S.M.1    Patton, J.T.2
  • 104
    • 84866181977 scopus 로고    scopus 로고
    • Norovirus RNA synthesis is modulated by an interaction between the viral RNA-dependent RNA polymerase and the major capsid protein, VP1
    • Subba-Reddy CV, Yunus MA, Goodfellow IG, Kao CC. Norovirus RNA synthesis is modulated by an interaction between the viral RNA-dependent RNA polymerase and the major capsid protein, VP1. J Virol 2012, 86:10138-10149.
    • (2012) J Virol , vol.86 , pp. 10138-10149
    • Subba-Reddy, C.V.1    Yunus, M.A.2    Goodfellow, I.G.3    Kao, C.C.4
  • 107
    • 84879153876 scopus 로고    scopus 로고
    • Unraveling the structure of viral replication complexes at super-resolution
    • Linnik O, Liesche J, Tilsner J, Oparka KJ. Unraveling the structure of viral replication complexes at super-resolution. Front Plant Sci 2013, 4:6.
    • (2013) Front Plant Sci , vol.4 , pp. 6
    • Linnik, O.1    Liesche, J.2    Tilsner, J.3    Oparka, K.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.