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Volumn 9, Issue , 2014, Pages 74-83

Regulation of Flavivirus RNA synthesis and replication

Author keywords

[No Author keywords available]

Indexed keywords

CIS ACTING ELEMENT; GENOMIC RNA; METHYLTRANSFERASE; NONSTRUCTURAL PROTEIN 5; RNA DIRECTED RNA POLYMERASE; VIRUS RNA;

EID: 84908177059     PISSN: 18796257     EISSN: 18796265     Source Type: Journal    
DOI: 10.1016/j.coviro.2014.09.011     Document Type: Review
Times cited : (70)

References (101)
  • 2
    • 84893270975 scopus 로고    scopus 로고
    • Noncoding subgenomic flavivirus RNA: Multiple functions in West Nile virus pathogenesis and modulation of host responses
    • J.A. Roby, G.P. Pijlman, J. Wilusz, and A.A. Khromykh Noncoding subgenomic flavivirus RNA: multiple functions in West Nile virus pathogenesis and modulation of host responses Viruses 6 2014 404 427
    • (2014) Viruses , vol.6 , pp. 404-427
    • Roby, J.A.1    Pijlman, G.P.2    Wilusz, J.3    Khromykh, A.A.4
  • 3
    • 84891441339 scopus 로고    scopus 로고
    • Replication cycle and molecular biology of the West Nile virus
    • M.A. Brinton Replication cycle and molecular biology of the West Nile virus Viruses 6 2014 13 53
    • (2014) Viruses , vol.6 , pp. 13-53
    • Brinton, M.A.1
  • 5
    • 84885763719 scopus 로고    scopus 로고
    • Regulation of flavivirus RNA synthesis and capping
    • B.J. Saeedi, and B.J. Geiss Regulation of flavivirus RNA synthesis and capping Wiley Interdiscip Rev RNA 4 2013 723 735
    • (2013) Wiley Interdiscip Rev RNA , vol.4 , pp. 723-735
    • Saeedi, B.J.1    Geiss, B.J.2
  • 6
    • 83855162132 scopus 로고    scopus 로고
    • Conventional and unconventional mechanisms for capping viral mRNA
    • E. Decroly, F. Ferron, J. Lescar, and B. Canard Conventional and unconventional mechanisms for capping viral mRNA Nat Rev Microbiol 10 2012 51 65
    • (2012) Nat Rev Microbiol , vol.10 , pp. 51-65
    • Decroly, E.1    Ferron, F.2    Lescar, J.3    Canard, B.4
  • 7
    • 84899845392 scopus 로고    scopus 로고
    • Dengue virus- and hepatitis C virus-induced replication and assembly compartments: The enemy inside-caught in the web
    • L. Chatel-Chaix, and R. Bartenschlager Dengue virus- and hepatitis C virus-induced replication and assembly compartments: the enemy inside-caught in the web J Virol 88 2014 5907 5911
    • (2014) J Virol , vol.88 , pp. 5907-5911
    • Chatel-Chaix, L.1    Bartenschlager, R.2
  • 11
    • 79851492362 scopus 로고    scopus 로고
    • RIG-I, MDA5 and TLR3 synergistically play an important role in restriction of dengue virus infection
    • A.M.A. Nasirudeen, H.H. Wong, P. Thien, S. Xu, K.-P. Lam, and D.X. Liu RIG-I, MDA5 and TLR3 synergistically play an important role in restriction of dengue virus infection PLoS Negl Trop Dis 5 2011 e926
    • (2011) PLoS Negl Trop Dis , vol.5 , pp. 926
    • Nasirudeen, A.M.A.1    Wong, H.H.2    Thien, P.3    Xu, S.4    Lam, K.-P.5    Liu, D.X.6
  • 12
    • 84867669809 scopus 로고    scopus 로고
    • A noncoding RNA produced by arthropod-borne flaviviruses inhibits the cellular exoribonuclease XRN1 and alters host mRNA stability
    • S.L. Moon, J.R. Anderson, Y. Kumagai, C.J. Wilusz, S. Akira, A.A. Khromykh, and J. Wilusz A noncoding RNA produced by arthropod-borne flaviviruses inhibits the cellular exoribonuclease XRN1 and alters host mRNA stability RNA 18 2012 2029 2040
    • (2012) RNA , vol.18 , pp. 2029-2040
    • Moon, S.L.1    Anderson, J.R.2    Kumagai, Y.3    Wilusz, C.J.4    Akira, S.5    Khromykh, A.A.6    Wilusz, J.7
  • 13
    • 84908163314 scopus 로고    scopus 로고
    • STAT2 signaling and dengue virus infection
    • J. Morrison, and A. García-Sastre STAT2 signaling and dengue virus infection JAK-STAT 3 2014 e27715
    • (2014) JAK-STAT , vol.3 , pp. 27715
    • Morrison, J.1    García-Sastre, A.2
  • 14
    • 66149146738 scopus 로고    scopus 로고
    • NS5 of dengue virus mediates STAT2 binding and degradation
    • J. Ashour, M. Laurent-Rolle, P.-Y. Shi, and A. García-Sastre NS5 of dengue virus mediates STAT2 binding and degradation J Virol 83 2009 5408 5418
    • (2009) J Virol , vol.83 , pp. 5408-5418
    • Ashour, J.1    Laurent-Rolle, M.2    Shi, P.-Y.3    García-Sastre, A.4
  • 15
    • 70349432365 scopus 로고    scopus 로고
    • Dengue virus NS5 inhibits interferon-alpha signaling by blocking signal transducer and activator of transcription 2 phosphorylation
    • M. Mazzon, M. Jones, A. Davidson, B. Chain, and M. Jacobs Dengue virus NS5 inhibits interferon-alpha signaling by blocking signal transducer and activator of transcription 2 phosphorylation J Infect Dis 200 2009 1261 1270
    • (2009) J Infect Dis , vol.200 , pp. 1261-1270
    • Mazzon, M.1    Jones, M.2    Davidson, A.3    Chain, B.4    Jacobs, M.5
  • 16
    • 0029027850 scopus 로고
    • Association between NS3 and NS5 proteins of dengue virus type 2 in the putative RNA replicase is linked to differential phosphorylation of NS5
    • M. Kapoor, L. Zhang, M. Ramachandra, J. Kusukawa, K.E. Ebner, and R. Padmanabhan Association between NS3 and NS5 proteins of dengue virus type 2 in the putative RNA replicase is linked to differential phosphorylation of NS5 J Biol Chem 270 1995 19100 19106
    • (1995) J Biol Chem , vol.270 , pp. 19100-19106
    • Kapoor, M.1    Zhang, L.2    Ramachandra, M.3    Kusukawa, J.4    Ebner, K.E.5    Padmanabhan, R.6
  • 17
    • 0026511204 scopus 로고
    • Monoclonal antibodies identify the NS5 yellow fever virus non-structural protein in the nuclei of infected cells
    • A. Buckley, S. Gaidamovich, A. Turchinskaya, and E.A. Gould Monoclonal antibodies identify the NS5 yellow fever virus non-structural protein in the nuclei of infected cells J Gen Virol 73 Pt 5 1992 1125 1130
    • (1992) J Gen Virol , vol.73 , Issue.PART 5 , pp. 1125-1130
    • Buckley, A.1    Gaidamovich, S.2    Turchinskaya, A.3    Gould, E.A.4
  • 18
    • 33845322955 scopus 로고    scopus 로고
    • Dengue virus RNA polymerase NS5: A potential therapeutic target?
    • S.M. Rawlinson, M.J. Pryor, P.J. Wright, and D.A. Jans Dengue virus RNA polymerase NS5: a potential therapeutic target? Curr Drug Targets 7 2006 1623 1638
    • (2006) Curr Drug Targets , vol.7 , pp. 1623-1638
    • Rawlinson, S.M.1    Pryor, M.J.2    Wright, P.J.3    Jans, D.A.4
  • 20
    • 84881238516 scopus 로고    scopus 로고
    • Serotype-specific differences in dengue virus non-structural protein 5 nuclear localization
    • H. Hannemann, P.-Y. Sung, H.-C. Chiu, A. Yousuf, J. Bird, S.P. Lim, and A.D. Davidson Serotype-specific differences in dengue virus non-structural protein 5 nuclear localization J Biol Chem 288 2013 22621 22635
    • (2013) J Biol Chem , vol.288 , pp. 22621-22635
    • Hannemann, H.1    Sung, P.-Y.2    Chiu, H.-C.3    Yousuf, A.4    Bird, J.5    Lim, S.P.6    Davidson, A.D.7
  • 21
    • 67650106549 scopus 로고    scopus 로고
    • CRM1-mediated nuclear export of dengue virus RNA polymerase NS5 modulates interleukin-8 induction and virus production
    • S.M. Rawlinson, M.J. Pryor, P.J. Wright, and D.A. Jans CRM1-mediated nuclear export of dengue virus RNA polymerase NS5 modulates interleukin-8 induction and virus production J Biol Chem 284 2009 15589 15597
    • (2009) J Biol Chem , vol.284 , pp. 15589-15597
    • Rawlinson, S.M.1    Pryor, M.J.2    Wright, P.J.3    Jans, D.A.4
  • 22
    • 84875802186 scopus 로고    scopus 로고
    • Nuclear localization of dengue virus nonstructural protein 5 does not strictly correlate with efficient viral RNA replication and inhibition of type i interferon signaling
    • A. Kumar, S. Bühler, B. Selisko, A. Davidson, K. Mulder, B. Canard, S. Miller, and R. Bartenschlager Nuclear localization of dengue virus nonstructural protein 5 does not strictly correlate with efficient viral RNA replication and inhibition of type I interferon signaling J Virol 87 2013 4545 4557
    • (2013) J Virol , vol.87 , pp. 4545-4557
    • Kumar, A.1    Bühler, S.2    Selisko, B.3    Davidson, A.4    Mulder, K.5    Canard, B.6    Miller, S.7    Bartenschlager, R.8
  • 23
    • 84895824915 scopus 로고    scopus 로고
    • RNA-dependent RNA polymerase of Japanese encephalitis virus binds the initiator nucleotide GTP to form a mechanistically important pre-initiation state
    • P. Surana, V. Satchidanandam, and D.T. Nair RNA-dependent RNA polymerase of Japanese encephalitis virus binds the initiator nucleotide GTP to form a mechanistically important pre-initiation state Nucleic Acids Res 42 2014 2758 2773
    • (2014) Nucleic Acids Res , vol.42 , pp. 2758-2773
    • Surana, P.1    Satchidanandam, V.2    Nair, D.T.3
  • 24
    • 77954955357 scopus 로고    scopus 로고
    • Biochemical characterization of the inhibition of the dengue virus RNA polymerase by beta-d-2′-ethynyl-7-deaza-adenosine triphosphate
    • D.R. Latour, A. Jekle, H. Javanbakht, R. Henningsen, P. Gee, I. Lee, P. Tran, S. Ren, A.K. Kutach, and S.F. Harris Biochemical characterization of the inhibition of the dengue virus RNA polymerase by beta-d-2′-ethynyl-7-deaza-adenosine triphosphate Antiviral Res 87 2010 213 222
    • (2010) Antiviral Res , vol.87 , pp. 213-222
    • Latour, D.R.1    Jekle, A.2    Javanbakht, H.3    Henningsen, R.4    Gee, P.5    Lee, I.6    Tran, P.7    Ren, S.8    Kutach, A.K.9    Harris, S.F.10
  • 25
    • 79958098689 scopus 로고    scopus 로고
    • The F1 motif of dengue virus polymerase NS5 is involved in promoter-dependent RNA synthesis
    • N.G. Iglesias, C.V. Filomatori, and A.V. Gamarnik The F1 motif of dengue virus polymerase NS5 is involved in promoter-dependent RNA synthesis J Virol 85 2011 5745 5756
    • (2011) J Virol , vol.85 , pp. 5745-5756
    • Iglesias, N.G.1    Filomatori, C.V.2    Gamarnik, A.V.3
  • 26
    • 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
    • S.P. Lim, J.H.K. Koh, C.C. Seh, C.W. Liew, A.D. Davidson, L.S. Chua, R. Chandrasekaran, T.C. Cornvik, P.-Y. Shi, and J. Lescar 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 2013 31105 31114
    • (2013) J Biol Chem , vol.288 , pp. 31105-31114
    • Lim, S.P.1    Koh, J.H.K.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
  • 27
    • 0035955628 scopus 로고    scopus 로고
    • De novo synthesis of RNA by the dengue virus RNA-dependent RNA polymerase exhibits temperature dependence at the initiation but not elongation phase
    • M. Ackermann, and R. Padmanabhan De novo synthesis of RNA by the dengue virus RNA-dependent RNA polymerase exhibits temperature dependence at the initiation but not elongation phase J Biol Chem 276 2001 39926 39937
    • (2001) J Biol Chem , vol.276 , pp. 39926-39937
    • Ackermann, M.1    Padmanabhan, R.2
  • 28
    • 84895822138 scopus 로고    scopus 로고
    • Polymerases of hepatitis C viruses and flaviviruses: Structural and mechanistic insights and drug development
    • C. Caillet-Saguy, S.P. Lim, P.-Y. Shi, J. Lescar, and S. Bressanelli Polymerases of hepatitis C viruses and flaviviruses: structural and mechanistic insights and drug development Antiviral Res 105 2014 8 16
    • (2014) Antiviral Res , vol.105 , pp. 8-16
    • Caillet-Saguy, C.1    Lim, S.P.2    Shi, P.-Y.3    Lescar, J.4    Bressanelli, S.5
  • 29
    • 84883381606 scopus 로고    scopus 로고
    • Crystal structure of the full-length Japanese encephalitis virus NS5 reveals a conserved methyltransferase-polymerase interface
    • G. Lu, and P. Gong 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. 1003549
    • Lu, G.1    Gong, P.2
  • 30
    • 34247610261 scopus 로고    scopus 로고
    • Crystal structure of the dengue virus RNA-dependent RNA polymerase catalytic domain at 1.85-angstrom resolution
    • T.L. Yap, T. Xu, Y.-L. Chen, H. Malet, M.-P. Egloff, B. Canard, S.G. Vasudevan, and J. Lescar Crystal structure of the dengue virus RNA-dependent RNA polymerase catalytic domain at 1.85-angstrom resolution J Virol 81 2007 4753 4765
    • (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
  • 31
    • 84876340250 scopus 로고    scopus 로고
    • Conformational flexibility of the dengue virus RNA-dependent RNA polymerase revealed by a complex with an inhibitor
    • C.G. Noble, S.P. Lim, Y.-L. Chen, C.W. Liew, L. Yap, J. Lescar, and P.-Y. Shi Conformational flexibility of the dengue virus RNA-dependent RNA polymerase revealed by a complex with an inhibitor J Virol 87 2013 5291 5295
    • (2013) J Virol , vol.87 , pp. 5291-5295
    • Noble, C.G.1    Lim, S.P.2    Chen, Y.-L.3    Liew, C.W.4    Yap, L.5    Lescar, J.6    Shi, P.-Y.7
  • 32
    • 84893864367 scopus 로고    scopus 로고
    • Comparison of dengue virus and HCV: From impact on global health to their RNA-dependent RNA polymerase
    • S. Potisopon, S. Priet, B. Selisko, and B. Canard Comparison of dengue virus and HCV: from impact on global health to their RNA-dependent RNA polymerase Future Virol 9 2014 53 67
    • (2014) Future Virol , vol.9 , pp. 53-67
    • Potisopon, S.1    Priet, S.2    Selisko, B.3    Canard, B.4
  • 33
    • 84879074185 scopus 로고    scopus 로고
    • Role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity
    • D. Garriga, C. Ferrer-Orta, J. Querol-Audí, B. Oliva, and N. Verdaguer Role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity J Mol Biol 425 2013 2279 2287
    • (2013) J Mol Biol , vol.425 , pp. 2279-2287
    • Garriga, D.1    Ferrer-Orta, C.2    Querol-Audí, J.3    Oliva, B.4    Verdaguer, N.5
  • 35
    • 84865734775 scopus 로고    scopus 로고
    • Conformational changes in motif D of RdRPs as fidelity determinant
    • N. Verdaguer, and C. Ferrer-Orta Conformational changes in motif D of RdRPs as fidelity determinant Structure 20 2012 1448 1450
    • (2012) Structure , vol.20 , pp. 1448-1450
    • Verdaguer, N.1    Ferrer-Orta, C.2
  • 37
    • 84873669740 scopus 로고    scopus 로고
    • Highly similar structural frames link the template tunnel and NTP entry tunnel to the exterior surface in RNA-dependent RNA polymerases
    • D.M. Lang, A.T. Zemla, and C.L.E. Zhou Highly similar structural frames link the template tunnel and NTP entry tunnel to the exterior surface in RNA-dependent RNA polymerases Nucleic Acids Res 41 2013 1464 1482
    • (2013) Nucleic Acids Res , vol.41 , pp. 1464-1482
    • Lang, D.M.1    Zemla, A.T.2    Zhou, C.L.E.3
  • 39
    • 84908163313 scopus 로고    scopus 로고
    • The methytransferase domain of the dengue virus protein NS5 ensures efficient RNA synthesis initiation and elongation by the polymerase domain
    • pii:gku666 [Epub ahead of print]
    • S. Potisopon, S. Priet, A. Collet, E. Decroly, B. Canard, and B. Selisko The methytransferase domain of the dengue virus protein NS5 ensures efficient RNA synthesis initiation and elongation by the polymerase domain Nucleic Acids Res 2014 pii:gku666 [Epub ahead of print]
    • (2014) Nucleic Acids Res
    • Potisopon, S.1    Priet, S.2    Collet, A.3    Decroly, E.4    Canard, B.5    Selisko, B.6
  • 40
    • 84864436647 scopus 로고    scopus 로고
    • Dengue virus nonstructural protein 5 adopts multiple conformations in solution
    • C. Bussetta, and K.H. Choi Dengue virus nonstructural protein 5 adopts multiple conformations in solution Biochemistry (Mosc.) 51 2012 5921 5931
    • (2012) Biochemistry (Mosc.) , vol.51 , pp. 5921-5931
    • Bussetta, C.1    Choi, K.H.2
  • 41
    • 84884539994 scopus 로고    scopus 로고
    • Protein-protein interactions among West Nile non-structural proteins and transmembrane complex formation in mammalian cells
    • L. Yu, K. Takeda, and L. Markoff Protein-protein interactions among West Nile non-structural proteins and transmembrane complex formation in mammalian cells Virology 446 2013 365 377
    • (2013) Virology , vol.446 , pp. 365-377
    • Yu, L.1    Takeda, K.2    Markoff, L.3
  • 42
    • 84875969405 scopus 로고    scopus 로고
    • The flavivirus NS1 protein: Molecular and structural biology, immunology, role in pathogenesis and application as a diagnostic biomarker
    • D.A. Muller, and P.R. Young The flavivirus NS1 protein: molecular and structural biology, immunology, role in pathogenesis and application as a diagnostic biomarker Antiviral Res 98 2013 192 208
    • (2013) Antiviral Res , vol.98 , pp. 192-208
    • Muller, D.A.1    Young, P.R.2
  • 43
    • 84875777404 scopus 로고    scopus 로고
    • Membrane topology and function of dengue virus NS2A protein
    • X. Xie, S. Gayen, C. Kang, Z. Yuan, and P.-Y. Shi Membrane topology and function of dengue virus NS2A protein J Virol 87 2013 4609 4622
    • (2013) J Virol , vol.87 , pp. 4609-4622
    • Xie, X.1    Gayen, S.2    Kang, C.3    Yuan, Z.4    Shi, P.-Y.5
  • 44
    • 84864188513 scopus 로고    scopus 로고
    • NS4A and NS4B proteins from dengue virus: Membranotropic regions
    • H. Nemésio, F. Palomares-Jerez, and J. Villalaín NS4A and NS4B proteins from dengue virus: membranotropic regions Biochim Biophys Acta 1818 2012 2818 2830
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 2818-2830
    • Nemésio, H.1    Palomares-Jerez, F.2    Villalaín, J.3
  • 45
    • 0034011620 scopus 로고    scopus 로고
    • Cis- and trans-acting elements in flavivirus RNA replication
    • A.A. Khromykh, P.L. Sedlak, and E.G. Westaway cis- and trans-acting elements in flavivirus RNA replication J Virol 74 2000 3253 3263
    • (2000) J Virol , vol.74 , pp. 3253-3263
    • Khromykh, A.A.1    Sedlak, P.L.2    Westaway, E.G.3
  • 46
    • 34247848008 scopus 로고    scopus 로고
    • The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner
    • S. Miller, S. Kastner, J. Krijnse-Locker, S. Bühler, and R. Bartenschlager The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner J Biol Chem 282 2007 8873 8882
    • (2007) J Biol Chem , vol.282 , pp. 8873-8882
    • Miller, S.1    Kastner, S.2    Krijnse-Locker, J.3    Bühler, S.4    Bartenschlager, R.5
  • 47
    • 70349337005 scopus 로고    scopus 로고
    • NS4A regulates the ATPase activity of the NS3 helicase: A novel cofactor role of the non-structural protein NS4A from West Nile virus
    • S.A. Shiryaev, A.V. Chernov, A.E. Aleshin, T.N. Shiryaeva, and A.Y. Strongin NS4A regulates the ATPase activity of the NS3 helicase: a novel cofactor role of the non-structural protein NS4A from West Nile virus J Gen Virol 90 2009 2081 2085
    • (2009) J Gen Virol , vol.90 , pp. 2081-2085
    • Shiryaev, S.A.1    Chernov, A.V.2    Aleshin, A.E.3    Shiryaeva, T.N.4    Strongin, A.Y.5
  • 48
    • 33747338217 scopus 로고    scopus 로고
    • Dengue virus NS4B interacts with NS3 and dissociates it from single-stranded RNA
    • I. Umareddy, A. Chao, A. Sampath, F. Gu, and S.G. Vasudevan Dengue virus NS4B interacts with NS3 and dissociates it from single-stranded RNA J Gen Virol 87 2006 2605 2614
    • (2006) J Gen Virol , vol.87 , pp. 2605-2614
    • Umareddy, I.1    Chao, A.2    Sampath, A.3    Gu, F.4    Vasudevan, S.G.5
  • 49
    • 84900338393 scopus 로고    scopus 로고
    • Functional interplay among the flavivirus NS3 protease, helicase, and cofactors
    • K. Li, W.W. Phoo, and D. Luo Functional interplay among the flavivirus NS3 protease, helicase, and cofactors Virol Sin 29 2014 74 85
    • (2014) Virol Sin , vol.29 , pp. 74-85
    • Li, K.1    Phoo, W.W.2    Luo, D.3
  • 50
    • 53249121029 scopus 로고    scopus 로고
    • Towards the design of antiviral inhibitors against flaviviruses: The case for the multifunctional NS3 protein from Dengue virus as a target
    • J. Lescar, D. Luo, T. Xu, A. Sampath, S.P. Lim, B. Canard, and S.G. Vasudevan Towards the design of antiviral inhibitors against flaviviruses: the case for the multifunctional NS3 protein from Dengue virus as a target Antiviral Res 80 2008 94 101
    • (2008) Antiviral Res , vol.80 , pp. 94-101
    • Lescar, J.1    Luo, D.2    Xu, T.3    Sampath, A.4    Lim, S.P.5    Canard, B.6    Vasudevan, S.G.7
  • 51
    • 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 importin-beta and the viral helicase, NS3
    • M. Johansson, A.J. Brooks, D.A. Jans, and S.G. Vasudevan A small region of the dengue virus-encoded RNA-dependent RNA polymerase, NS5, confers interaction with both the nuclear transport receptor importin-beta and the viral helicase, NS3 J Gen Virol 82 2001 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
  • 55
    • 0032486596 scopus 로고    scopus 로고
    • Recombinant dengue virus type 1 NS3 protein exhibits specific viral RNA binding and NTPase activity regulated by the NS5 protein
    • T. Cui, R.J. Sugrue, Q. Xu, A.K. Lee, Y.C. Chan, and J. Fu Recombinant dengue virus type 1 NS3 protein exhibits specific viral RNA binding and NTPase activity regulated by the NS5 protein Virology 246 1998 409 417
    • (1998) Virology , vol.246 , pp. 409-417
    • Cui, T.1    Sugrue, R.J.2    Xu, Q.3    Lee, A.K.4    Chan, Y.C.5    Fu, J.6
  • 56
    • 22844443626 scopus 로고    scopus 로고
    • Modulation of the nucleoside triphosphatase/RNA helicase and 5′-RNA triphosphatase activities of Dengue virus type 2 nonstructural protein 3 (NS3) by interaction with NS5, the RNA-dependent RNA polymerase
    • C. Yon, T. Teramoto, N. Mueller, J. Phelan, V.K. Ganesh, K.H.M. Murthy, and R. Padmanabhan Modulation of the nucleoside triphosphatase/RNA helicase and 5′-RNA triphosphatase activities of Dengue virus type 2 nonstructural protein 3 (NS3) by interaction with NS5, the RNA-dependent RNA polymerase J Biol Chem 280 2005 27412 27419
    • (2005) J Biol Chem , vol.280 , pp. 27412-27419
    • Yon, C.1    Teramoto, T.2    Mueller, N.3    Phelan, J.4    Ganesh, V.K.5    Murthy, K.H.M.6    Padmanabhan, R.7
  • 57
    • 84910613036 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of host-virus interactions reveals a role for GBF1 in dengue infection
    • L.N. Carpp, R.S. Rogers, R.L. Moritz, and J.D. Aitchison Quantitative proteomic analysis of host-virus interactions reveals a role for GBF1 in dengue infection Mol Cell Proteomics 2014 10.1074/mcp.M114. 038984
    • (2014) Mol Cell Proteomics
    • Carpp, L.N.1    Rogers, R.S.2    Moritz, R.L.3    Aitchison, J.D.4
  • 58
    • 67749119973 scopus 로고    scopus 로고
    • Cyclosporine inhibits flavivirus replication through blocking the interaction between host cyclophilins and viral NS5 protein
    • M. Qing, F. Yang, B. Zhang, G. Zou, J.M. Robida, Z. Yuan, H. Tang, and P.-Y. Shi Cyclosporine inhibits flavivirus replication through blocking the interaction between host cyclophilins and viral NS5 protein Antimicrob Agents Chemother 53 2009 3226 3235
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 3226-3235
    • Qing, M.1    Yang, F.2    Zhang, B.3    Zou, G.4    Robida, J.M.5    Yuan, Z.6    Tang, H.7    Shi, P.-Y.8
  • 61
    • 84884521148 scopus 로고    scopus 로고
    • Heat shock protein 70 is associated with replicase complex of Japanese encephalitis virus and positively regulates viral genome replication
    • J. Ye, Z. Chen, B. Zhang, H. Miao, A. Zohaib, Q. Xu, H. Chen, and S. Cao Heat shock protein 70 is associated with replicase complex of Japanese encephalitis virus and positively regulates viral genome replication PLOS ONE 8 2013 e75188
    • (2013) PLOS ONE , vol.8 , pp. 75188
    • Ye, J.1    Chen, Z.2    Zhang, B.3    Miao, H.4    Zohaib, A.5    Xu, Q.6    Chen, H.7    Cao, S.8
  • 62
    • 77958100661 scopus 로고    scopus 로고
    • Dengue virus nonstructural protein 3 redistributes fatty acid synthase to sites of viral replication and increases cellular fatty acid synthesis
    • N.S. Heaton, R. Perera, K.L. Berger, S. Khadka, D.J. Lacount, R.J. Kuhn, and G. Randall Dengue virus nonstructural protein 3 redistributes fatty acid synthase to sites of viral replication and increases cellular fatty acid synthesis Proc Natl Acad Sci U S A 107 2010 17345 17350
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 17345-17350
    • Heaton, N.S.1    Perera, R.2    Berger, K.L.3    Khadka, S.4    Lacount, D.J.5    Kuhn, R.J.6    Randall, G.7
  • 64
    • 0030761459 scopus 로고    scopus 로고
    • Translation elongation factor-1 alpha interacts with the 3′ stem-loop region of West Nile virus genomic RNA
    • J.L. Blackwell, and M.A. Brinton Translation elongation factor-1 alpha interacts with the 3′ stem-loop region of West Nile virus genomic RNA J Virol 71 1997 6433 6444
    • (1997) J Virol , vol.71 , pp. 6433-6444
    • Blackwell, J.L.1    Brinton, M.A.2
  • 65
    • 35348822495 scopus 로고    scopus 로고
    • Interaction between the cellular protein eEF1A and the 3′-terminal stem-loop of West Nile virus genomic RNA facilitates viral minus-strand RNA synthesis
    • W.G. Davis, J.L. Blackwell, P.-Y. Shi, and M.A. Brinton Interaction between the cellular protein eEF1A and the 3′-terminal stem-loop of West Nile virus genomic RNA facilitates viral minus-strand RNA synthesis J Virol 81 2007 10172 10187
    • (2007) J Virol , vol.81 , pp. 10172-10187
    • Davis, W.G.1    Blackwell, J.L.2    Shi, P.-Y.3    Brinton, M.A.4
  • 66
    • 70849127442 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein is relocated to the cytoplasm and is required during dengue virus infection in Vero cells
    • R.A. Agis-Juárez, I. Galván, F. Medina, T. Daikoku, R. Padmanabhan, J.E. Ludert, and R.M. del Angel Polypyrimidine tract-binding protein is relocated to the cytoplasm and is required during dengue virus infection in Vero cells J Gen Virol 90 2009 2893 2901
    • (2009) J Gen Virol , vol.90 , pp. 2893-2901
    • Agis-Juárez, R.A.1    Galván, I.2    Medina, F.3    Daikoku, T.4    Padmanabhan, R.5    Ludert, J.E.6    Del Angel, R.M.7
  • 67
    • 0036061536 scopus 로고    scopus 로고
    • Translation elongation factor-1alpha. La, and PTB interact with the 3′ untranslated region of dengue 4 virus RNA
    • M. De Nova-Ocampo, N. Villegas-Sepúlveda, and R.M. del Angel Translation elongation factor-1alpha. La, and PTB interact with the 3′ untranslated region of dengue 4 virus RNA Virology 295 2002 337 347
    • (2002) Virology , vol.295 , pp. 337-347
    • De Nova-Ocampo, M.1    Villegas-Sepúlveda, N.2    Del Angel, R.M.3
  • 68
    • 67349133117 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein influences negative strand RNA synthesis of dengue virus
    • L. Jiang, H. Yao, X. Duan, X. Lu, and Y. Liu Polypyrimidine tract-binding protein influences negative strand RNA synthesis of dengue virus Biochem Biophys Res Commun 385 2009 187 192
    • (2009) Biochem Biophys Res Commun , vol.385 , pp. 187-192
    • Jiang, L.1    Yao, H.2    Duan, X.3    Lu, X.4    Liu, Y.5
  • 69
    • 79952223157 scopus 로고    scopus 로고
    • NF90 binds the dengue virus RNA 3′ terminus and is a positive regulator of dengue virus replication
    • R.C. Gomila, G.W. Martin, and L. Gehrke NF90 binds the dengue virus RNA 3′ terminus and is a positive regulator of dengue virus replication PLoS ONE 6 2011 e16687
    • (2011) PLoS ONE , vol.6 , pp. 16687
    • Gomila, R.C.1    Martin, G.W.2    Gehrke, L.3
  • 70
    • 81255210913 scopus 로고    scopus 로고
    • Quantitative mass spectrometry of DENV-2 RNA-interacting proteins reveals that the DEAD-box RNA helicase DDX6 binds the DB1 and DB2 3′ UTR structures
    • A.M. Ward, K. Bidet, A. Yinglin, S.G. Ler, K. Hogue, W. Blackstock, J. Gunaratne, and M.A. Garcia-Blanco Quantitative mass spectrometry of DENV-2 RNA-interacting proteins reveals that the DEAD-box RNA helicase DDX6 binds the DB1 and DB2 3′ UTR structures RNA Biol 8 2011 1173 1186
    • (2011) RNA Biol , vol.8 , pp. 1173-1186
    • Ward, A.M.1    Bidet, K.2    Yinglin, A.3    Ler, S.G.4    Hogue, K.5    Blackstock, W.6    Gunaratne, J.7    Garcia-Blanco, M.A.8
  • 71
    • 79955780170 scopus 로고    scopus 로고
    • Functional interaction between cellular p100 and the dengue virus 3′ UTR
    • Y. Lei, Y. Huang, H. Zhang, L. Yu, M. Zhang, and A. Dayton Functional interaction between cellular p100 and the dengue virus 3′ UTR J Gen Virol 92 2011 796 806
    • (2011) J Gen Virol , vol.92 , pp. 796-806
    • Lei, Y.1    Huang, Y.2    Zhang, H.3    Yu, L.4    Zhang, M.5    Dayton, A.6
  • 72
    • 35648946315 scopus 로고    scopus 로고
    • Y box-binding protein-1 binds to the dengue virus 3′-untranslated region and mediates antiviral effects
    • S.M. Paranjape, and E. Harris Y box-binding protein-1 binds to the dengue virus 3′-untranslated region and mediates antiviral effects J Biol Chem 282 2007 30497 30508
    • (2007) J Biol Chem , vol.282 , pp. 30497-30508
    • Paranjape, S.M.1    Harris, E.2
  • 73
    • 63449118113 scopus 로고    scopus 로고
    • Poly(A)-binding protein binds to the non-polyadenylated 3′ untranslated region of dengue virus and modulates translation efficiency
    • C. Polacek, P. Friebe, and E. Harris Poly(A)-binding protein binds to the non-polyadenylated 3′ untranslated region of dengue virus and modulates translation efficiency J Gen Virol 90 2009 687 692
    • (2009) J Gen Virol , vol.90 , pp. 687-692
    • Polacek, C.1    Friebe, P.2    Harris, E.3
  • 74
    • 74049150019 scopus 로고    scopus 로고
    • Control of dengue virus translation and replication
    • S.M. Paranjape, and E. Harris Control of dengue virus translation and replication Curr Top Microbiol Immunol 338 2010 15 34
    • (2010) Curr Top Microbiol Immunol , vol.338 , pp. 15-34
    • Paranjape, S.M.1    Harris, E.2
  • 76
    • 79953200163 scopus 로고    scopus 로고
    • RNA sequences and structures required for the recruitment and activity of the dengue virus polymerase
    • C.V. Filomatori, N.G. Iglesias, S.M. Villordo, D.E. Alvarez, and A.V. Gamarnik RNA sequences and structures required for the recruitment and activity of the dengue virus polymerase J Biol Chem 286 2011 6929 6939
    • (2011) J Biol Chem , vol.286 , pp. 6929-6939
    • Filomatori, C.V.1    Iglesias, N.G.2    Villordo, S.M.3    Alvarez, D.E.4    Gamarnik, A.V.5
  • 79
    • 42749084987 scopus 로고    scopus 로고
    • Functional analysis of dengue virus cyclization sequences located at the 5′ and 3′UTRs
    • D.E. Alvarez, C.V. Filomatori, and A.V. Gamarnik Functional analysis of dengue virus cyclization sequences located at the 5′ and 3′UTRs Virology 375 2008 223 235
    • (2008) Virology , vol.375 , pp. 223-235
    • Alvarez, D.E.1    Filomatori, C.V.2    Gamarnik, A.V.3
  • 80
    • 58149526753 scopus 로고    scopus 로고
    • Conformational changes in the solution structure of the dengue virus 5′ end in the presence and absence of the 3′ untranslated region
    • C. Polacek, J.E. Foley, and E. Harris Conformational changes in the solution structure of the dengue virus 5′ end in the presence and absence of the 3′ untranslated region J Virol 83 2009 1161 1166
    • (2009) J Virol , vol.83 , pp. 1161-1166
    • Polacek, C.1    Foley, J.E.2    Harris, E.3
  • 81
    • 78951475155 scopus 로고    scopus 로고
    • The 5′ and 3′ downstream AUG region elements are required for mosquito-borne flavivirus RNA replication
    • P. Friebe, P.-Y. Shi, and E. Harris The 5′ and 3′ downstream AUG region elements are required for mosquito-borne flavivirus RNA replication J Virol 85 2011 1900 1905
    • (2011) J Virol , vol.85 , pp. 1900-1905
    • Friebe, P.1    Shi, P.-Y.2    Harris, E.3
  • 82
    • 77952736780 scopus 로고    scopus 로고
    • Interplay of RNA elements in the dengue virus 5′ and 3′ ends required for viral RNA replication
    • P. Friebe, and E. Harris Interplay of RNA elements in the dengue virus 5′ and 3′ ends required for viral RNA replication J Virol 84 2010 6103 6118
    • (2010) J Virol , vol.84 , pp. 6103-6118
    • Friebe, P.1    Harris, E.2
  • 83
    • 84855203268 scopus 로고    scopus 로고
    • Composition of the sequence downstream of the dengue virus 5′ cyclization sequence (dCS) affects viral RNA replication
    • P. Friebe, J. Peña, M.O.F. Pohl, and E. Harris Composition of the sequence downstream of the dengue virus 5′ cyclization sequence (dCS) affects viral RNA replication Virology 422 2012 346 356
    • (2012) Virology , vol.422 , pp. 346-356
    • Friebe, P.1    Peña, J.2    Pohl, M.O.F.3    Harris, E.4
  • 84
    • 50349101877 scopus 로고    scopus 로고
    • The capsid-coding region hairpin element (cHP) is a critical determinant of dengue virus and West Nile virus RNA synthesis
    • K. Clyde, J. Barrera, and E. Harris The capsid-coding region hairpin element (cHP) is a critical determinant of dengue virus and West Nile virus RNA synthesis Virology 379 2008 314 323
    • (2008) Virology , vol.379 , pp. 314-323
    • Clyde, K.1    Barrera, J.2    Harris, E.3
  • 85
    • 33144458778 scopus 로고    scopus 로고
    • RNA secondary structure in the coding region of dengue virus type 2 directs translation start codon selection and is required for viral replication
    • K. Clyde, and E. Harris RNA secondary structure in the coding region of dengue virus type 2 directs translation start codon selection and is required for viral replication J Virol 80 2006 2170 2182
    • (2006) J Virol , vol.80 , pp. 2170-2182
    • Clyde, K.1    Harris, E.2
  • 86
    • 84865305540 scopus 로고    scopus 로고
    • A novel coding-region RNA element modulates infectious dengue virus particle production in both mammalian and mosquito cells and regulates viral replication in Aedes aegypti mosquitoes
    • A.M. Groat-Carmona, S. Orozco, P. Friebe, A. Payne, L. Kramer, and E. Harris A novel coding-region RNA element modulates infectious dengue virus particle production in both mammalian and mosquito cells and regulates viral replication in Aedes aegypti mosquitoes Virology 432 2012 511 526
    • (2012) Virology , vol.432 , pp. 511-526
    • Groat-Carmona, A.M.1    Orozco, S.2    Friebe, P.3    Payne, A.4    Kramer, L.5    Harris, E.6
  • 87
    • 80053317134 scopus 로고    scopus 로고
    • Functional RNA elements in the dengue virus genome
    • L.G. Gebhard, C.V. Filomatori, and A.V. Gamarnik Functional RNA elements in the dengue virus genome Viruses 3 2011 1739 1756
    • (2011) Viruses , vol.3 , pp. 1739-1756
    • Gebhard, L.G.1    Filomatori, C.V.2    Gamarnik, A.V.3
  • 88
    • 34547570863 scopus 로고    scopus 로고
    • Characterization of the variable region in the 3′ non-translated region of dengue type 1 virus
    • S. Tajima, Y. Nukui, T. Takasaki, and I. Kurane Characterization of the variable region in the 3′ non-translated region of dengue type 1 virus J Gen Virol 88 2007 2214 2222
    • (2007) J Gen Virol , vol.88 , pp. 2214-2222
    • Tajima, S.1    Nukui, Y.2    Takasaki, T.3    Kurane, I.4
  • 92
    • 23844507858 scopus 로고    scopus 로고
    • Role of RNA structures present at the 3′UTR of dengue virus on translation, RNA synthesis, and viral replication
    • D.E. Alvarez, A.L. De Lella Ezcurra, S. Fucito, and A.V. Gamarnik Role of RNA structures present at the 3′UTR of dengue virus on translation, RNA synthesis, and viral replication Virology 339 2005 200 212
    • (2005) Virology , vol.339 , pp. 200-212
    • Alvarez, D.E.1    De Lella Ezcurra, A.L.2    Fucito, S.3    Gamarnik, A.V.4
  • 93
    • 79959343157 scopus 로고    scopus 로고
    • Identification of cis-acting elements in the 3′-untranslated region of the dengue virus type 2 RNA that modulate translation and replication
    • M. Manzano, E.D. Reichert, S. Polo, B. Falgout, W. Kasprzak, B.A. Shapiro, and R. Padmanabhan Identification of cis-acting elements in the 3′-untranslated region of the dengue virus type 2 RNA that modulate translation and replication J Biol Chem 286 2011 22521 22534
    • (2011) J Biol Chem , vol.286 , pp. 22521-22534
    • Manzano, M.1    Reichert, E.D.2    Polo, S.3    Falgout, B.4    Kasprzak, W.5    Shapiro, B.A.6    Padmanabhan, R.7
  • 94
    • 84877267759 scopus 로고    scopus 로고
    • Structural complexity of Dengue virus untranslated regions: Cis-acting RNA motifs and pseudoknot interactions modulating functionality of the viral genome
    • J. Sztuba-Solinska, T. Teramoto, J.W. Rausch, B.A. Shapiro, R. Padmanabhan, and S.F.J. Le Grice Structural complexity of Dengue virus untranslated regions: cis-acting RNA motifs and pseudoknot interactions modulating functionality of the viral genome Nucleic Acids Res 41 2013 5075 5089
    • (2013) Nucleic Acids Res , vol.41 , pp. 5075-5089
    • Sztuba-Solinska, J.1    Teramoto, T.2    Rausch, J.W.3    Shapiro, B.A.4    Padmanabhan, R.5    Le Grice, S.F.J.6
  • 95
    • 1542781698 scopus 로고    scopus 로고
    • 5′- and 3′-noncoding regions in flavivirus RNA
    • L. Markoff 5′- and 3′-noncoding regions in flavivirus RNA Adv Virus Res 59 2003 177 228
    • (2003) Adv Virus Res , vol.59 , pp. 177-228
    • Markoff, L.1
  • 96
    • 0031849664 scopus 로고    scopus 로고
    • Identification of specific nucleotide sequences within the conserved 3′-SL in the dengue type 2 virus genome required for replication
    • L. Zeng, B. Falgout, and L. Markoff Identification of specific nucleotide sequences within the conserved 3′-SL in the dengue type 2 virus genome required for replication J Virol 72 1998 7510 7522
    • (1998) J Virol , vol.72 , pp. 7510-7522
    • Zeng, L.1    Falgout, B.2    Markoff, L.3
  • 97
    • 30044452235 scopus 로고    scopus 로고
    • Inhibition of dengue virus translation and RNA synthesis by a morpholino oligomer targeted to the top of the terminal 3′ stem-loop structure
    • K.L. Holden, D.A. Stein, T.C. Pierson, A.A. Ahmed, K. Clyde, P.L. Iversen, and E. Harris Inhibition of dengue virus translation and RNA synthesis by a morpholino oligomer targeted to the top of the terminal 3′ stem-loop structure Virology 344 2006 439 452
    • (2006) Virology , vol.344 , pp. 439-452
    • Holden, K.L.1    Stein, D.A.2    Pierson, T.C.3    Ahmed, A.A.4    Clyde, K.5    Iversen, P.L.6    Harris, E.7
  • 98
    • 11344282039 scopus 로고    scopus 로고
    • The flavivirus-conserved penta-nucleotide in the 3′ stem-loop of the West Nile virus genome requires a specific sequence and structure for RNA synthesis, but not for viral translation
    • M. Tilgner, T.S. Deas, and P.-Y. Shi The flavivirus-conserved penta-nucleotide in the 3′ stem-loop of the West Nile virus genome requires a specific sequence and structure for RNA synthesis, but not for viral translation Virology 331 2005 375 386
    • (2005) Virology , vol.331 , pp. 375-386
    • Tilgner, M.1    Deas, T.S.2    Shi, P.-Y.3
  • 99
    • 84881225571 scopus 로고    scopus 로고
    • Differential RNA sequence requirement for dengue virus replication in mosquito and mammalian cells
    • S.M. Villordo, and A.V. Gamarnik Differential RNA sequence requirement for dengue virus replication in mosquito and mammalian cells J Virol 87 2013 9365 9372
    • (2013) J Virol , vol.87 , pp. 9365-9372
    • Villordo, S.M.1    Gamarnik, A.V.2
  • 100
    • 78649681550 scopus 로고    scopus 로고
    • A balance between circular and linear forms of the dengue virus genome is crucial for viral replication
    • S.M. Villordo, D.E. Alvarez, and A.V. Gamarnik A balance between circular and linear forms of the dengue virus genome is crucial for viral replication RNA 16 2010 2325 2335
    • (2010) RNA , vol.16 , pp. 2325-2335
    • Villordo, S.M.1    Alvarez, D.E.2    Gamarnik, A.V.3
  • 101
    • 84895919460 scopus 로고    scopus 로고
    • Distinct conformations of a putative translocation element in poliovirus polymerase
    • A. Sholders, and O. Peersen 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.1    Peersen, O.2


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