메뉴 건너뛰기




Volumn 85, Issue 3, 2010, Pages 450-462

Strategies for development of dengue virus inhibitors

Author keywords

Antiviral; Cell based assay; Dengue virus; Drug discovery; Enzyme assay; Flavivirus; High throughput screening

Indexed keywords

1 DEOXYNOJIRIMYCIN; ADEFOVIR DIPIVOXIL; ADENOSINE DERIVATIVE; ALPHA GLUCOSIDASE; AMPRENAVIR; ANTIVIRUS AGENT; APROTININ; CAPSID PROTEIN; CASTANOSPERMINE; CELL SURFACE RECEPTOR; ENFUVIRTIDE; FC RECEPTOR; INTERLEUKIN 8 ANTIBODY; MARAVIROC; NITD 008; NONSTRUCTURAL PROTEIN 2; NONSTRUCTURAL PROTEIN 3; NUCLEOSIDE ANALOG; PALIVIZUMAB; PROTEINASE INHIBITOR; RNA DIRECTED DNA POLYMERASE INHIBITOR; RNA DIRECTED RNA POLYMERASE; RNA HELICASE; RNA METHYLTRANSFERASE; SERINE PROTEINASE INHIBITOR; TENOFOVIR DISOPROXIL; TUMOR NECROSIS FACTOR ANTIBODY; UNCLASSIFIED DRUG; UNINDEXED DRUG; VIRUS ENVELOPE PROTEIN; VIRUS PROTEIN;

EID: 76949091459     PISSN: 01663542     EISSN: 18729096     Source Type: Journal    
DOI: 10.1016/j.antiviral.2009.12.011     Document Type: Review
Times cited : (234)

References (154)
  • 1
    • 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
    • Ackermann M., and Padmanabhan R. 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 43 (2001) 39926-39937
    • (2001) J. Biol. Chem. , vol.276 , Issue.43 , pp. 39926-39937
    • Ackermann, M.1    Padmanabhan, R.2
  • 2
    • 63549108516 scopus 로고    scopus 로고
    • Antiviral activity of carbohydrate-binding agents and the role of DC-SIGN in dengue virus infection
    • Alen M.M., Kaptein S.J., De Burghgraeve T., Balzarini J., Neyts J., and Schols D. Antiviral activity of carbohydrate-binding agents and the role of DC-SIGN in dengue virus infection. Virology 387 1 (2009) 67-75
    • (2009) Virology , vol.387 , Issue.1 , pp. 67-75
    • Alen, M.M.1    Kaptein, S.J.2    De Burghgraeve, T.3    Balzarini, J.4    Neyts, J.5    Schols, D.6
  • 3
    • 34247625945 scopus 로고    scopus 로고
    • Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold
    • Aleshin A., Shiryaev S., Strongin A., and Liddington R. Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold. Protein Sci. 16 5 (2007) 795-806
    • (2007) Protein Sci. , vol.16 , Issue.5 , pp. 795-806
    • Aleshin, A.1    Shiryaev, S.2    Strongin, A.3    Liddington, R.4
  • 7
    • 0024372153 scopus 로고
    • Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses
    • Bazan J.F., and Fletterick R.J. Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses. Virology 171 2 (1989) 637-639
    • (1989) Virology , vol.171 , Issue.2 , pp. 637-639
    • Bazan, J.F.1    Fletterick, R.J.2
  • 9
  • 10
    • 0021880733 scopus 로고
    • Use of an enzyme-linked immunosorbent assay performed directly on fixed infected cell monolayers for evaluating drugs against varicella-zoster virus
    • Berkowitz F.E., and Levin M.J. Use of an enzyme-linked immunosorbent assay performed directly on fixed infected cell monolayers for evaluating drugs against varicella-zoster virus. Antimicrob. Agents Chemother. 28 2 (1985) 207-210
    • (1985) Antimicrob. Agents Chemother. , vol.28 , Issue.2 , pp. 207-210
    • Berkowitz, F.E.1    Levin, M.J.2
  • 11
    • 0036093580 scopus 로고    scopus 로고
    • Potent in vivo antiviral activity of the herpes simplex virus primase-helicase inhibitor BAY 57-1293
    • Betz U.A., Fischer R., Kleymann G., Hendrix M., and Rubsamen-Waigmann H. Potent in vivo antiviral activity of the herpes simplex virus primase-helicase inhibitor BAY 57-1293. Antimicrob. Agents Chemother. 46 6 (2002) 1766-1772
    • (2002) Antimicrob. Agents Chemother. , vol.46 , Issue.6 , pp. 1766-1772
    • Betz, U.A.1    Fischer, R.2    Kleymann, G.3    Hendrix, M.4    Rubsamen-Waigmann, H.5
  • 12
    • 33947241644 scopus 로고    scopus 로고
    • The helicase primase inhibitor, BAY 57-1293 shows potent therapeutic antiviral activity superior to famciclovir in BALB/c mice infected with herpes simplex virus type 1
    • Biswas S., Jennens L., and Field H.J. The helicase primase inhibitor, BAY 57-1293 shows potent therapeutic antiviral activity superior to famciclovir in BALB/c mice infected with herpes simplex virus type 1. Antiviral Res. 75 1 (2007) 30-35
    • (2007) Antiviral Res. , vol.75 , Issue.1 , pp. 30-35
    • Biswas, S.1    Jennens, L.2    Field, H.J.3
  • 15
    • 33744477373 scopus 로고    scopus 로고
    • Nucleoside analog inhibitors of hepatitis C virus replication
    • Carroll S.S., and Olsen D.B. Nucleoside analog inhibitors of hepatitis C virus replication. Infect. Disord. Drug Targets 6 1 (2006) 17-29
    • (2006) Infect. Disord. Drug Targets , vol.6 , Issue.1 , pp. 17-29
    • Carroll, S.S.1    Olsen, D.B.2
  • 16
    • 0026039916 scopus 로고
    • Processing of the yellow fever virus nonstructural polyprotein: a catalytically active NS3 proteinase domain and NS2B are required for cleavages at dibasic sites
    • Chambers T.J., Grakoui A., and Rice C.M. Processing of the yellow fever virus nonstructural polyprotein: a catalytically active NS3 proteinase domain and NS2B are required for cleavages at dibasic sites. J. Virol. 65 11 (1991) 6042-6050
    • (1991) J. Virol. , vol.65 , Issue.11 , pp. 6042-6050
    • Chambers, T.J.1    Grakoui, A.2    Rice, C.M.3
  • 17
    • 0025201350 scopus 로고
    • Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein
    • Chambers T.J., Weir R.C., Grakoui A., McCourt D.W., Bazan J.F., Fletterick R.J., and Rice C.M. Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein. Proc. Nat. Acad. Sci. U.S.A. 87 22 (1990) 8898-8902
    • (1990) Proc. Nat. Acad. Sci. U.S.A. , vol.87 , Issue.22 , pp. 8898-8902
    • Chambers, T.J.1    Weir, R.C.2    Grakoui, A.3    McCourt, D.W.4    Bazan, J.F.5    Fletterick, R.J.6    Rice, C.M.7
  • 19
    • 13644262812 scopus 로고    scopus 로고
    • Inhibition of West Nile virus entry by using a recombinant domain III from the envelope glycoprotein
    • Chu J., Rajamanonmani R., Li J., Bhuvanakantham R., Lescar J., and Ng M. Inhibition of West Nile virus entry by using a recombinant domain III from the envelope glycoprotein. J. Gen. Virol. 86 Pt 2 (2005) 405-412
    • (2005) J. Gen. Virol. , vol.86 , Issue.PART 2 , pp. 405-412
    • Chu, J.1    Rajamanonmani, R.2    Li, J.3    Bhuvanakantham, R.4    Lescar, J.5    Ng, M.6
  • 20
    • 33847671789 scopus 로고    scopus 로고
    • c-Src protein kinase inhibitors block assembly and maturation of dengue virus
    • Chu J.J., and Yang P.L. c-Src protein kinase inhibitors block assembly and maturation of dengue virus. Proc. Natl. Acad. Sci. U.S.A. 104 9 (2007) 3520-3525
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , Issue.9 , pp. 3520-3525
    • Chu, J.J.1    Yang, P.L.2
  • 21
    • 0018770470 scopus 로고
    • Methylation status of intracellular Dengue type 2 40S RNA
    • Cleaves G.R., and Dubin D.T. Methylation status of intracellular Dengue type 2 40S RNA. Virology 96 (1979) 159-165
    • (1979) Virology , vol.96 , pp. 159-165
    • Cleaves, G.R.1    Dubin, D.T.2
  • 22
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • Cordin O., Banroques J., Tanner N.K., and Linder P. The DEAD-box protein family of RNA helicases. Gene 367 (2006) 17-37
    • (2006) Gene , vol.367 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 24
    • 0033988280 scopus 로고    scopus 로고
    • Alpha-glucosidase inhibitors reduce dengue virus production by affecting the initial steps of virion morphogenesis in the endoplasmic reticulum
    • Courageot M.P., Frenkiel M.P., Dos Santos C.D., Deubel V., and Despres P. Alpha-glucosidase inhibitors reduce dengue virus production by affecting the initial steps of virion morphogenesis in the endoplasmic reticulum. J. Virol. 74 1 (2000) 564-572
    • (2000) J. Virol. , vol.74 , Issue.1 , pp. 564-572
    • Courageot, M.P.1    Frenkiel, M.P.2    Dos Santos, C.D.3    Deubel, V.4    Despres, P.5
  • 25
    • 0034899311 scopus 로고    scopus 로고
    • Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells
    • Crill W.D., and Roehrig J.T. Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells. J. Virol. 75 16 (2001) 7769-7773
    • (2001) J. Virol. , vol.75 , Issue.16 , pp. 7769-7773
    • Crill, W.D.1    Roehrig, J.T.2
  • 26
    • 34247564968 scopus 로고    scopus 로고
    • Distinct RNA elements confer specificity to flavivirus RNA cap methylation events
    • Dong H., Ray D., Ren S., Zhang B., Puig-Basagoiti F., Takagi Y., Ho C., Li H., and Shi P. Distinct RNA elements confer specificity to flavivirus RNA cap methylation events. J. Virol. 81 9 (2007) 4412-4421
    • (2007) J. Virol. , vol.81 , Issue.9 , pp. 4412-4421
    • Dong, H.1    Ray, D.2    Ren, S.3    Zhang, B.4    Puig-Basagoiti, F.5    Takagi, Y.6    Ho, C.7    Li, H.8    Shi, P.9
  • 27
    • 50049109958 scopus 로고    scopus 로고
    • Flavivirus methyltransferase: a novel antiviral target
    • Dong H., Zhang B., and Shi P.Y. Flavivirus methyltransferase: a novel antiviral target. Antiviral Res. 80 1 (2008) 1-10
    • (2008) Antiviral Res. , vol.80 , Issue.1 , pp. 1-10
    • Dong, H.1    Zhang, B.2    Shi, P.Y.3
  • 29
    • 0037013858 scopus 로고    scopus 로고
    • An RNA cap (nucleoside-2′-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization
    • Egloff M.P., Benarroch D., Selisko B., Romette J.L., and Canard B. An RNA cap (nucleoside-2′-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization. EMBO J. 21 11 (2002) 2757-2768
    • (2002) EMBO J. , vol.21 , Issue.11 , pp. 2757-2768
    • Egloff, M.P.1    Benarroch, D.2    Selisko, B.3    Romette, J.L.4    Canard, B.5
  • 30
    • 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 M.P., Decroly E., Malet H., Selisko B., Benarroch D., Ferron F., and Canard B. 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 3 (2007) 723-736
    • (2007) J. Mol. Biol. , vol.372 , Issue.3 , 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
  • 32
    • 0037236396 scopus 로고    scopus 로고
    • Cleavage of protein prM is necessary for infection of BHK-21 cells by tick-borne encephalitis virus
    • Elshuber S., Allison S.L., Heinz F.X., and Mandl C.W. Cleavage of protein prM is necessary for infection of BHK-21 cells by tick-borne encephalitis virus. J. Gen. Virol. 84 Pt 1 (2003) 183-191
    • (2003) J. Gen. Virol. , vol.84 , Issue.PART 1 , pp. 183-191
    • Elshuber, S.1    Allison, S.L.2    Heinz, F.X.3    Mandl, C.W.4
  • 34
    • 0027499688 scopus 로고
    • Deletion analysis of dengue virus type 4 nonstructural protein NS2B: identification of a domain required for NS2B-NS3 protease activity
    • Falgout B., Miller R.H., and Lai C.J. Deletion analysis of dengue virus type 4 nonstructural protein NS2B: identification of a domain required for NS2B-NS3 protease activity. J. Virol. 67 4 (1993) 2034-2042
    • (1993) J. Virol. , vol.67 , Issue.4 , pp. 2034-2042
    • Falgout, B.1    Miller, R.H.2    Lai, C.J.3
  • 35
    • 0025735688 scopus 로고
    • Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein
    • Fenouillet E., and Gluckman J.C. Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein. J. Gen. Virol. 72 Pt 8 (1991) 1919-1926
    • (1991) J. Gen. Virol. , vol.72 , Issue.PART 8 , pp. 1919-1926
    • Fenouillet, E.1    Gluckman, J.C.2
  • 36
    • 0034567861 scopus 로고    scopus 로고
    • Viral and cellular mRNA capping: past and prospects
    • Furuichi Y., and Shatkin A.J. Viral and cellular mRNA capping: past and prospects. Adv. Virus Res. 55 (2000) 135-184
    • (2000) Adv. Virus Res. , vol.55 , pp. 135-184
    • Furuichi, Y.1    Shatkin, A.J.2
  • 37
    • 34547141259 scopus 로고    scopus 로고
    • Monoclonal antibody-mediated enhancement of dengue virus infection in vitro and in vivo and strategies for prevention
    • Goncalvez A.P., Engle R.E., St Claire M., Purcell R.H., and Lai C.J. Monoclonal antibody-mediated enhancement of dengue virus infection in vitro and in vivo and strategies for prevention. Proc. Natl. Acad. Sci. U.S.A. 104 22 (2007) 9422-9427
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , Issue.22 , pp. 9422-9427
    • Goncalvez, A.P.1    Engle, R.E.2    St Claire, M.3    Purcell, R.H.4    Lai, C.J.5
  • 39
    • 45949089393 scopus 로고    scopus 로고
    • Cell-based assays to identify inhibitors of viral disease
    • Green N., Ott R., Isaacs R., and Fang H. Cell-based assays to identify inhibitors of viral disease. Expert Opin. Drug Discov. 3 (2008) 671-676
    • (2008) Expert Opin. Drug Discov. , vol.3 , pp. 671-676
    • Green, N.1    Ott, R.2    Isaacs, R.3    Fang, H.4
  • 40
    • 50149096815 scopus 로고    scopus 로고
    • Characterization of dengue virus complex-specific neutralizing epitopes on envelope protein domain III of dengue 2 virus
    • Gromowski G.D., Barrett N.D., and Barrett A.D. Characterization of dengue virus complex-specific neutralizing epitopes on envelope protein domain III of dengue 2 virus. J. Virol. 82 17 (2008) 8828-8837
    • (2008) J. Virol. , vol.82 , Issue.17 , pp. 8828-8837
    • Gromowski, G.D.1    Barrett, N.D.2    Barrett, A.D.3
  • 41
    • 33947216518 scopus 로고    scopus 로고
    • Antiviral profiles of novel iminocyclitol compounds against bovine viral diarrhea virus, West Nile virus, dengue virus and hepatitis B virus
    • Gu B., Mason P., Wang L., Norton P., Bourne N., Moriarty R., Mehta A., Despande M., Shah R., and Block T. Antiviral profiles of novel iminocyclitol compounds against bovine viral diarrhea virus, West Nile virus, dengue virus and hepatitis B virus. Antivir. Chem. Chemother. 18 1 (2007) 49-59
    • (2007) Antivir. Chem. Chemother. , vol.18 , Issue.1 , pp. 49-59
    • Gu, B.1    Mason, P.2    Wang, L.3    Norton, P.4    Bourne, N.5    Moriarty, R.6    Mehta, A.7    Despande, M.8    Shah, R.9    Block, T.10
  • 42
    • 35348925573 scopus 로고    scopus 로고
    • Flaviviruses
    • Knipe D.M., and Howley P.M. (Eds), Lippincott William & Wilkins, Philadelphia, PA
    • Gubler D., Kuno G., and Markoff L. Flaviviruses. In: Knipe D.M., and Howley P.M. (Eds). Fields Virology. 5th ed. vol. 1 (2007), Lippincott William & Wilkins, Philadelphia, PA 1153-1253
    • (2007) Fields Virology. 5th ed. , vol.1 , pp. 1153-1253
    • Gubler, D.1    Kuno, G.2    Markoff, L.3
  • 43
    • 0019614627 scopus 로고
    • Epidemic dengue 3 in central Java, associated with low viremia in man
    • Gubler D.J., Suharyono W., Lubis I., Eram S., and Gunarso S. Epidemic dengue 3 in central Java, associated with low viremia in man. Am. J. Trop. Med. Hyg. 30 5 (1981) 1094-1099
    • (1981) Am. J. Trop. Med. Hyg. , vol.30 , Issue.5 , pp. 1094-1099
    • Gubler, D.J.1    Suharyono, W.2    Lubis, I.3    Eram, S.4    Gunarso, S.5
  • 44
    • 13744259524 scopus 로고    scopus 로고
    • West nile virus inhibits the signal transduction pathway of alpha interferon
    • Guo J., Hayashi J., and Seeger C. West nile virus inhibits the signal transduction pathway of alpha interferon. J. Virol. 79 3 (2005) 1343-1350
    • (2005) J. Virol. , vol.79 , Issue.3 , pp. 1343-1350
    • Guo, J.1    Hayashi, J.2    Seeger, C.3
  • 45
    • 0642287817 scopus 로고    scopus 로고
    • Neutralization and antibody-dependent enhancement of dengue viruses
    • Halstead S.B. Neutralization and antibody-dependent enhancement of dengue viruses. Adv. Virus Res. 60 (2003) 421-467
    • (2003) Adv. Virus Res. , vol.60 , pp. 421-467
    • Halstead, S.B.1
  • 46
    • 0031662109 scopus 로고    scopus 로고
    • 5′-Amino acid esters of antiviral nucleosides, acyclovir, and AZT are absorbed by the intestinal PEPT1 peptide transporter
    • Han H., de Vrueh R.L., Rhie J.K., Covitz K.M., Smith P.L., Lee C.P., Oh D.M., Sadee W., and Amidon G.L. 5′-Amino acid esters of antiviral nucleosides, acyclovir, and AZT are absorbed by the intestinal PEPT1 peptide transporter. Pharm. Res. 15 8 (1998) 1154-1159
    • (1998) Pharm. Res. , vol.15 , Issue.8 , pp. 1154-1159
    • Han, H.1    de Vrueh, R.L.2    Rhie, J.K.3    Covitz, K.M.4    Smith, P.L.5    Lee, C.P.6    Oh, D.M.7    Sadee, W.8    Amidon, G.L.9
  • 47
    • 26944466459 scopus 로고    scopus 로고
    • Mechanism of membrane fusion by viral envelope proteins
    • Harrison S.C. Mechanism of membrane fusion by viral envelope proteins. Adv. Virus Res. 64 (2005) 231-261
    • (2005) Adv. Virus Res. , vol.64 , pp. 231-261
    • Harrison, S.C.1
  • 48
    • 44949211332 scopus 로고    scopus 로고
    • Fragment-based activity space: smaller is better
    • Hesterkamp T., and Whittaker M. Fragment-based activity space: smaller is better. Curr. Opin. Chem. Biol. 12 3 (2008) 260-268
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , Issue.3 , pp. 260-268
    • Hesterkamp, T.1    Whittaker, M.2
  • 49
    • 0035194285 scopus 로고    scopus 로고
    • Effector function activities of a panel of mutants of a broadly neutralizing antibody against human immunodeficiency virus type 1
    • Hezareh M., Hessell A.J., Jensen R.C., van de Winkel J.G., and Parren P.W. Effector function activities of a panel of mutants of a broadly neutralizing antibody against human immunodeficiency virus type 1. J. Virol. 75 24 (2001) 12161-12168
    • (2001) J. Virol. , vol.75 , Issue.24 , pp. 12161-12168
    • Hezareh, M.1    Hessell, A.J.2    Jensen, R.C.3    van de Winkel, J.G.4    Parren, P.W.5
  • 51
    • 23744446349 scopus 로고    scopus 로고
    • Peptide inhibitors of dengue virus and West Nile virus infectivity
    • Hrobowski Y., Garry R., and Michael S. Peptide inhibitors of dengue virus and West Nile virus infectivity. Virol. J. 2 (2005) 49
    • (2005) Virol. J. , vol.2 , pp. 49
    • Hrobowski, Y.1    Garry, R.2    Michael, S.3
  • 52
    • 44649160013 scopus 로고    scopus 로고
    • A comparative biochemical analysis of the NS2B(H)-NS3pro protease complex from four dengue virus serotypes
    • Iempridee T., Thongphung R., Angsuthanasombat C., and Katzenmeier G. A comparative biochemical analysis of the NS2B(H)-NS3pro protease complex from four dengue virus serotypes. Biochim. Biophys. Acta 1780 7-8 (2008) 989-994
    • (2008) Biochim. Biophys. Acta , vol.1780 , Issue.7-8 , pp. 989-994
    • Iempridee, T.1    Thongphung, R.2    Angsuthanasombat, C.3    Katzenmeier, G.4
  • 53
    • 35348922285 scopus 로고    scopus 로고
    • Fragment-based screening using X-ray crystallography and NMR spectroscopy
    • Jhoti H., Cleasby A., Verdonk M., and Williams G. Fragment-based screening using X-ray crystallography and NMR spectroscopy. Curr. Opin. Chem. Biol. 11 5 (2007) 485-493
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , Issue.5 , pp. 485-493
    • Jhoti, H.1    Cleasby, A.2    Verdonk, M.3    Williams, G.4
  • 54
    • 2442457815 scopus 로고    scopus 로고
    • Identification of GRP 78 (BiP) as a liver cell expressed receptor element for dengue virus serotype 2
    • Jindadamrongwech S., Thepparit C., and Smith D.R. Identification of GRP 78 (BiP) as a liver cell expressed receptor element for dengue virus serotype 2. Arch. Virol. 149 5 (2004) 915-927
    • (2004) Arch. Virol. , vol.149 , Issue.5 , pp. 915-927
    • Jindadamrongwech, S.1    Thepparit, C.2    Smith, D.R.3
  • 56
    • 0031798576 scopus 로고    scopus 로고
    • Encapsidation of the flavivirus Kunjin replicon RNA by using a complementation system providing Kunjin virus structural proteins in trans
    • Khromykh A.A., Varnavski A.N., and Westaway E.G. Encapsidation of the flavivirus Kunjin replicon RNA by using a complementation system providing Kunjin virus structural proteins in trans. J. Virol. 72 (1998) 5967-5977
    • (1998) J. Virol. , vol.72 , pp. 5967-5977
    • Khromykh, A.A.1    Varnavski, A.N.2    Westaway, E.G.3
  • 58
    • 0036232747 scopus 로고    scopus 로고
    • Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles
    • Kummerer B.M., and Rice C.M. Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles. J. Virol. 76 10 (2002) 4773-4784
    • (2002) J. Virol. , vol.76 , Issue.10 , pp. 4773-4784
    • Kummerer, B.M.1    Rice, C.M.2
  • 59
    • 65549140728 scopus 로고    scopus 로고
    • HIV-1 entry inhibitors: an overview
    • Kuritzkes D.R. HIV-1 entry inhibitors: an overview. Curr. Opin. HIV AIDS 4 2 (2009) 82-87
    • (2009) Curr. Opin. HIV AIDS , vol.4 , Issue.2 , pp. 82-87
    • Kuritzkes, D.R.1
  • 60
    • 0032520794 scopus 로고    scopus 로고
    • Detection of hepatitis C virus helicase activity using the scintillation proximity assay system
    • Kyono K., Miyashiro M., and Taguchi I. Detection of hepatitis C virus helicase activity using the scintillation proximity assay system. Anal. Biochem. 257 2 (1998) 120-126
    • (1998) Anal. Biochem. , vol.257 , Issue.2 , pp. 120-126
    • Kyono, K.1    Miyashiro, M.2    Taguchi, I.3
  • 61
    • 44449142885 scopus 로고    scopus 로고
    • Existence of hepatitis C virus NS5B variants naturally resistant to non-nucleoside, but not to nucleoside, polymerase inhibitors among untreated patients
    • Le Pogam S., Seshaadri A., Kosaka A., Chiu S., Kang H., Hu S., Rajyaguru S., Symons J., Cammack N., and Najera I. Existence of hepatitis C virus NS5B variants naturally resistant to non-nucleoside, but not to nucleoside, polymerase inhibitors among untreated patients. J. Antimicrob. Chemother. 61 6 (2008) 1205-1216
    • (2008) J. Antimicrob. Chemother. , vol.61 , Issue.6 , pp. 1205-1216
    • Le Pogam, S.1    Seshaadri, A.2    Kosaka, A.3    Chiu, S.4    Kang, H.5    Hu, S.6    Rajyaguru, S.7    Symons, J.8    Cammack, N.9    Najera, I.10
  • 62
    • 0036173445 scopus 로고    scopus 로고
    • Susceptibilities of herpes simplex viruses to penciclovir and acyclovir in eight cell lines
    • Leary J.J., Wittrock R., Sarisky R.T., Weinberg A., and Levin M.J. Susceptibilities of herpes simplex viruses to penciclovir and acyclovir in eight cell lines. Antimicrob. Agents Chemother. 46 3 (2002) 762-768
    • (2002) Antimicrob. Agents Chemother. , vol.46 , Issue.3 , pp. 762-768
    • Leary, J.J.1    Wittrock, R.2    Sarisky, R.T.3    Weinberg, A.4    Levin, M.J.5
  • 63
    • 45749091387 scopus 로고    scopus 로고
    • Cholesterol effectively blocks entry of flavivirus
    • Lee C.J., Lin H.R., Liao C.L., and Lin Y.L. Cholesterol effectively blocks entry of flavivirus. J. Virol. 82 13 (2008) 6470-6480
    • (2008) J. Virol. , vol.82 , Issue.13 , pp. 6470-6480
    • Lee, C.J.1    Lin, H.R.2    Liao, C.L.3    Lin, Y.L.4
  • 64
    • 0035824539 scopus 로고    scopus 로고
    • Activity of recombinant dengue 2 virus NS3 protease in the presence of a truncated NS2B co-factor, small peptide substrates, and inhibitors
    • Leung D., Schroder K., White H., Fang N.-X., Stoermer M., Abbenante G., Martin J., PR Y., and Fairlie D. Activity of recombinant dengue 2 virus NS3 protease in the presence of a truncated NS2B co-factor, small peptide substrates, and inhibitors. J. Biol. Chem. 276 (2001) 45762-45771
    • (2001) J. Biol. Chem. , vol.276 , pp. 45762-45771
    • Leung, D.1    Schroder, K.2    White, H.3    Fang, N.-X.4    Stoermer, M.5    Abbenante, G.6    Martin, J.7    PR, Y.8    Fairlie, D.9
  • 66
    • 26444506252 scopus 로고    scopus 로고
    • Domain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusion
    • Liao M., and Kielian M. Domain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusion. J. Cell Biol. 171 1 (2005) 111-120
    • (2005) J. Cell Biol. , vol.171 , Issue.1 , pp. 111-120
    • Liao, M.1    Kielian, M.2
  • 67
    • 0037108657 scopus 로고    scopus 로고
    • High circulating levels of the dengue virus nonstructural protein NS1 early in dengue illness correlate with the development of dengue hemorrhagic fever
    • Libraty D.H., Young P.R., Pickering D., Endy T.P., Kalayanarooj S., Green S., Vaughn D.W., Nisalak A., Ennis F.A., and Rothman A.L. High circulating levels of the dengue virus nonstructural protein NS1 early in dengue illness correlate with the development of dengue hemorrhagic fever. J. Infect. Dis. 186 8 (2002) 1165-1168
    • (2002) J. Infect. Dis. , vol.186 , Issue.8 , pp. 1165-1168
    • Libraty, D.H.1    Young, P.R.2    Pickering, D.3    Endy, T.P.4    Kalayanarooj, S.5    Green, S.6    Vaughn, D.W.7    Nisalak, A.8    Ennis, F.A.9    Rothman, A.L.10
  • 68
    • 0030774240 scopus 로고    scopus 로고
    • Trans-complementation of yellow fever virus NS1 reveals a role in early RNA replication
    • Lindenbach B., and Rice C. Trans-complementation of yellow fever virus NS1 reveals a role in early RNA replication. J. Virol. 71 (1997) 9608-9617
    • (1997) J. Virol. , vol.71 , pp. 9608-9617
    • Lindenbach, B.1    Rice, C.2
  • 69
    • 34548278532 scopus 로고    scopus 로고
    • Mapping to completeness and transplantation of a group-specific, discontinuous, neutralizing epitope in the envelope protein of dengue virus
    • Lisova O., Hardy F., Petit V., and Bedouelle H. Mapping to completeness and transplantation of a group-specific, discontinuous, neutralizing epitope in the envelope protein of dengue virus. J. Gen. Virol. 88 Pt 9 (2007) 2387-2397
    • (2007) J. Gen. Virol. , vol.88 , Issue.PART 9 , pp. 2387-2397
    • Lisova, O.1    Hardy, F.2    Petit, V.3    Bedouelle, H.4
  • 70
    • 13744254078 scopus 로고    scopus 로고
    • Inhibition of interferon signaling by the New York 99 strain and Kunjin subtype of West Nile virus involves blockage of STAT1 and STAT2 activation by nonstructural proteins
    • Liu W., Wang X., Mokhonov V., Shi P., Randall R., and Khromykh A. Inhibition of interferon signaling by the New York 99 strain and Kunjin subtype of West Nile virus involves blockage of STAT1 and STAT2 activation by nonstructural proteins. J. Virol. 79 3 (2005) 1934-1942
    • (2005) J. Virol. , vol.79 , Issue.3 , pp. 1934-1942
    • Liu, W.1    Wang, X.2    Mokhonov, V.3    Shi, P.4    Randall, R.5    Khromykh, A.6
  • 71
    • 0038421087 scopus 로고    scopus 로고
    • Molecular and functional analyses of Kunjin virus infectious cDNA clones demonstrate the essential roles for NS2A in virus assembly and for a nonconservative residue in NS3 in RNA replication
    • Liu W.J., Chen H.B., and Khromykh A.A. Molecular and functional analyses of Kunjin virus infectious cDNA clones demonstrate the essential roles for NS2A in virus assembly and for a nonconservative residue in NS3 in RNA replication. J. Virol. 77 14 (2003) 7804-7813
    • (2003) J. Virol. , vol.77 , Issue.14 , pp. 7804-7813
    • Liu, W.J.1    Chen, H.B.2    Khromykh, A.A.3
  • 73
    • 0018865387 scopus 로고
    • Antigenic variants of influenza viruses: marked differences in the frequencies of variants selected with different monoclonal antibodies
    • Lubeck M.D., Schulman J.L., and Palese P. Antigenic variants of influenza viruses: marked differences in the frequencies of variants selected with different monoclonal antibodies. Virology 102 2 (1980) 458-462
    • (1980) Virology , vol.102 , Issue.2 , pp. 458-462
    • Lubeck, M.D.1    Schulman, J.L.2    Palese, P.3
  • 74
    • 76949101007 scopus 로고    scopus 로고
    • Crystal structure of the NS3 protease-helicase from Dengue virus
    • (Epub ahead of print)
    • Luo D., Xu T., Hunke C., Gruber G., Vasudevan S., and Lescar J. Crystal structure of the NS3 protease-helicase from Dengue virus. J. Virol. (2007) (Epub ahead of print)
    • (2007) J. Virol.
    • Luo, D.1    Xu, T.2    Hunke, C.3    Gruber, G.4    Vasudevan, S.5    Lescar, J.6
  • 76
    • 33750499753 scopus 로고    scopus 로고
    • Dengue-virus-infected dendritic cells trigger vascular leakage through metalloproteinase overproduction
    • Luplertlop N., Misse D., Bray D., Deleuze V., Gonzalez J.P., Leardkamolkarn V., Yssel H., and Veas F. Dengue-virus-infected dendritic cells trigger vascular leakage through metalloproteinase overproduction. EMBO Rep. 7 11 (2006) 1176-1181
    • (2006) EMBO Rep. , vol.7 , Issue.11 , pp. 1176-1181
    • Luplertlop, N.1    Misse, D.2    Bray, D.3    Deleuze, V.4    Gonzalez, J.P.5    Leardkamolkarn, V.6    Yssel, H.7    Veas, F.8
  • 77
  • 81
    • 34748876762 scopus 로고    scopus 로고
    • Structure of the Murray Valley encephalitis virus RNA helicase at 1.9 Angstrom resolution
    • Mancini E., Assenberg R., Verma A., Walter T., Tuma R., Grimes J., Owens R., and Stuart D. Structure of the Murray Valley encephalitis virus RNA helicase at 1.9 Angstrom resolution. Protein Sci. 16 10 (2007) 2294-2300
    • (2007) Protein Sci. , vol.16 , Issue.10 , pp. 2294-2300
    • Mancini, E.1    Assenberg, R.2    Verma, A.3    Walter, T.4    Tuma, R.5    Grimes, J.6    Owens, R.7    Stuart, D.8
  • 82
    • 41449108064 scopus 로고    scopus 로고
    • A dual-purpose synthetic colloidal platform for protease mapping: substrate profiling for Dengue and West Nile virus proteases
    • Marcon L., Kozak D., Battersby B.J., Chappell K.J., Fairlie D.P., Young P., and Trau M. A dual-purpose synthetic colloidal platform for protease mapping: substrate profiling for Dengue and West Nile virus proteases. Anal. Biochem. 376 1 (2008) 151-153
    • (2008) Anal. Biochem. , vol.376 , Issue.1 , pp. 151-153
    • Marcon, L.1    Kozak, D.2    Battersby, B.J.3    Chappell, K.J.4    Fairlie, D.P.5    Young, P.6    Trau, M.7
  • 83
    • 0034102651 scopus 로고    scopus 로고
    • Broad-spectrum antiviral activity of the IMP dehydrogenase inhibitor VX-497: a comparison with ribavirin and demonstration of antiviral additivity with alpha interferon
    • Markland W., McQuaid T.J., Jain J., and Kwong A.D. Broad-spectrum antiviral activity of the IMP dehydrogenase inhibitor VX-497: a comparison with ribavirin and demonstration of antiviral additivity with alpha interferon. Antimicrob. Agent. Chemother. 44 4 (2000) 859-866
    • (2000) Antimicrob. Agent. Chemother. , vol.44 , Issue.4 , pp. 859-866
    • Markland, W.1    McQuaid, T.J.2    Jain, J.3    Kwong, A.D.4
  • 84
    • 48949117560 scopus 로고    scopus 로고
    • The current status of the NNRTI family of antiretrovirals used in the HAART regime against HIV infection
    • Martins S., Ramos M.J., and Fernandes P.A. The current status of the NNRTI family of antiretrovirals used in the HAART regime against HIV infection. Curr. Med. Chem. 15 11 (2008) 1083-1095
    • (2008) Curr. Med. Chem. , vol.15 , Issue.11 , pp. 1083-1095
    • Martins, S.1    Ramos, M.J.2    Fernandes, P.A.3
  • 85
    • 0041920922 scopus 로고    scopus 로고
    • The utility of siRNA transcripts produced by RNA polymerase i in down regulating viral gene expression and replication of negative- and positive-strand RNA viruses
    • McCown M., Diamond M.S., and Pekosz A. The utility of siRNA transcripts produced by RNA polymerase i in down regulating viral gene expression and replication of negative- and positive-strand RNA viruses. Virology 313 2 (2003) 514-524
    • (2003) Virology , vol.313 , Issue.2 , pp. 514-524
    • McCown, M.1    Diamond, M.S.2    Pekosz, A.3
  • 86
    • 73549088708 scopus 로고    scopus 로고
    • Menéndez-Arias, L., 2010. Molecular basis of human immunodeficiency virus drug resistance: an update. Antiviral Res., doi:10.1016/j.antiviral.2009.07.006.
    • Menéndez-Arias, L., 2010. Molecular basis of human immunodeficiency virus drug resistance: an update. Antiviral Res., doi:10.1016/j.antiviral.2009.07.006.
  • 89
    • 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
    • Miller S., Kastner S., Krijnse-Locker J., Buhler S., and Bartenschlager R. 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 12 (2007) 8873-8882
    • (2007) J. Biol. Chem. , vol.282 , Issue.12 , pp. 8873-8882
    • Miller, S.1    Kastner, S.2    Krijnse-Locker, J.3    Buhler, S.4    Bartenschlager, R.5
  • 90
    • 33646851580 scopus 로고    scopus 로고
    • Subcellular localization and membrane topology of the dengue virus type 2 non-structural protein 4B
    • Miller S., Sparacio S., and Bartenschlager R. Subcellular localization and membrane topology of the dengue virus type 2 non-structural protein 4B. J. Biol. Chem. 281 13 (2006) 8854-8863
    • (2006) J. Biol. Chem. , vol.281 , Issue.13 , pp. 8854-8863
    • Miller, S.1    Sparacio, S.2    Bartenschlager, R.3
  • 91
    • 0037495036 scopus 로고    scopus 로고
    • A ligand-binding pocket in the dengue virus envelope glycoprotein
    • Modis Y., Ogata S., Clements D., and Harrison S.C. A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc. Natl. Acad. Sci. U.S.A. 100 12 (2003) 6986-6991
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , Issue.12 , pp. 6986-6991
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 92
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis Y., Ogata S., Clements D., and Harrison S.C. Structure of the dengue virus envelope protein after membrane fusion. Nature 427 6972 (2004) 313-319
    • (2004) Nature , vol.427 , Issue.6972 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 94
    • 69249209851 scopus 로고    scopus 로고
    • Humanized mice show clinical signs of dengue fever according to infecting virus genotype
    • Mota J., and Rico-Hesse R. Humanized mice show clinical signs of dengue fever according to infecting virus genotype. J. Virol. 83 17 (2009) 8638-8645
    • (2009) J. Virol. , vol.83 , Issue.17 , pp. 8638-8645
    • Mota, J.1    Rico-Hesse, R.2
  • 95
    • 0034537548 scopus 로고    scopus 로고
    • Toxicity of antiretroviral nucleoside and nucleotide analogues: is mitochondrial toxicity the only mechanism?
    • Moyle G. Toxicity of antiretroviral nucleoside and nucleotide analogues: is mitochondrial toxicity the only mechanism?. Drug Saf. 23 6 (2000) 467-481
    • (2000) Drug Saf. , vol.23 , Issue.6 , pp. 467-481
    • Moyle, G.1
  • 96
    • 50949084334 scopus 로고    scopus 로고
    • Identification and biochemical characterization of small-molecule inhibitors of west nile virus serine protease by a high-throughput screen
    • Mueller N.H., Pattabiraman N., Ansarah-Sobrinho C., Viswanathan P., Pierson T.C., and Padmanabhan R. Identification and biochemical characterization of small-molecule inhibitors of west nile virus serine protease by a high-throughput screen. Antimicrob. Agents Chemother. 52 9 (2008) 3385-3393
    • (2008) Antimicrob. Agents Chemother. , vol.52 , Issue.9 , pp. 3385-3393
    • Mueller, N.H.1    Pattabiraman, N.2    Ansarah-Sobrinho, C.3    Viswanathan, P.4    Pierson, T.C.5    Padmanabhan, R.6
  • 97
    • 33846246837 scopus 로고    scopus 로고
    • Characterization of the West Nile virus protease substrate specificity and inhibitors
    • Mueller N.H., Yon C., Ganesh V.K., and Padmanabhan R. Characterization of the West Nile virus protease substrate specificity and inhibitors. Int. J. Biochem. Cell Biol. 39 3 (2007) 606-614
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , Issue.3 , pp. 606-614
    • Mueller, N.H.1    Yon, C.2    Ganesh, V.K.3    Padmanabhan, R.4
  • 100
    • 0041563793 scopus 로고    scopus 로고
    • Dendritic-cell-specific ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses
    • Navarro-Sanchez E., Altmeyer R., Amara A., Schwartz O., Fieschi F., Virelizier J.L., Arenzana-Seisdedos F., and Despres P. Dendritic-cell-specific ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses. EMBO Rep. 4 7 (2003) 723-728
    • (2003) EMBO Rep. , vol.4 , Issue.7 , pp. 723-728
    • Navarro-Sanchez, E.1    Altmeyer, R.2    Amara, A.3    Schwartz, O.4    Fieschi, F.5    Virelizier, J.L.6    Arenzana-Seisdedos, F.7    Despres, P.8
  • 101
    • 35349023246 scopus 로고    scopus 로고
    • Construction and characterization of a stable subgenomic dengue virus type 2 replicon system for antiviral compound and siRNA testing
    • Ng C.Y., Gu F., Phong W.Y., Chen Y.L., Lim S.P., Davidson A., and Vasudevan S.G. Construction and characterization of a stable subgenomic dengue virus type 2 replicon system for antiviral compound and siRNA testing. Antiviral Res. 76 3 (2007) 222-231
    • (2007) Antiviral Res. , vol.76 , Issue.3 , pp. 222-231
    • Ng, C.Y.1    Gu, F.2    Phong, W.Y.3    Chen, Y.L.4    Lim, S.P.5    Davidson, A.6    Vasudevan, S.G.7
  • 102
    • 33745516142 scopus 로고    scopus 로고
    • Probing the substrate specificity of the dengue virus type 2 NS3 serine protease by using internally quenched fluorescent peptides
    • Niyomrattanakit P., Yahorava S., Mutule I., Mutulis F., Petrovska R., Prusis P., Katzenmeier G., and Wikberg J.E. Probing the substrate specificity of the dengue virus type 2 NS3 serine protease by using internally quenched fluorescent peptides. Biochem. J. 397 1 (2006) 203-211
    • (2006) Biochem. J. , vol.397 , Issue.1 , pp. 203-211
    • Niyomrattanakit, P.1    Yahorava, S.2    Mutule, I.3    Mutulis, F.4    Petrovska, R.5    Prusis, P.6    Katzenmeier, G.7    Wikberg, J.E.8
  • 104
    • 19044373919 scopus 로고    scopus 로고
    • Development of Dengue virus type 2 replicons capable of prolonged expression in host cells
    • Pang X., Zhang M., and Dayton A.I. Development of Dengue virus type 2 replicons capable of prolonged expression in host cells. BMC Microbiol. 1 (2001) 18
    • (2001) BMC Microbiol. , vol.1 , pp. 18
    • Pang, X.1    Zhang, M.2    Dayton, A.I.3
  • 108
    • 50049120491 scopus 로고    scopus 로고
    • Closing the door on flaviviruses: entry as a target for antiviral drug design
    • Perera R., Khaliq M., and Kuhn R.J. Closing the door on flaviviruses: entry as a target for antiviral drug design. Antiviral Res. 80 1 (2008) 11-22
    • (2008) Antiviral Res. , vol.80 , Issue.1 , pp. 11-22
    • Perera, R.1    Khaliq, M.2    Kuhn, R.J.3
  • 109
    • 35848930168 scopus 로고    scopus 로고
    • First example of phosphoramidate approach applied to a 4′-substituted purine nucleoside (4′-azidoadenosine): conversion of an inactive nucleoside to a submicromolar compound versus hepatitis C virus
    • Perrone P., Daverio F., Valente R., Rajyaguru S., Martin J.A., Leveque V., Le Pogam S., Najera I., Klumpp K., Smith D.B., and McGuigan C. First example of phosphoramidate approach applied to a 4′-substituted purine nucleoside (4′-azidoadenosine): conversion of an inactive nucleoside to a submicromolar compound versus hepatitis C virus. J. Med. Chem. 50 22 (2007) 5463-5470
    • (2007) J. Med. Chem. , vol.50 , Issue.22 , pp. 5463-5470
    • Perrone, P.1    Daverio, F.2    Valente, R.3    Rajyaguru, S.4    Martin, J.A.5    Leveque, V.6    Le Pogam, S.7    Najera, I.8    Klumpp, K.9    Smith, D.B.10    McGuigan, C.11
  • 112
    • 0025033393 scopus 로고
    • In vitro processing of dengue virus type 2 nonstructural proteins NS2A, NS2B, and NS3
    • Preugschat F., Yao C.W., and Strauss J.H. In vitro processing of dengue virus type 2 nonstructural proteins NS2A, NS2B, and NS3. J. Virol. 64 9 (1990) 4364-4374
    • (1990) J. Virol. , vol.64 , Issue.9 , pp. 4364-4374
    • Preugschat, F.1    Yao, C.W.2    Strauss, J.H.3
  • 116
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • Pyle A.M. Translocation and unwinding mechanisms of RNA and DNA helicases. Annu. Rev. Biophys. 37 (2008) 317-336
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 117
    • 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 T., Zhou Y., Li H., and Shi P. 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 17 (2006) 8362-8370
    • (2006) J. Virol. , vol.80 , Issue.17 , pp. 8362-8370
    • Ray, D.1    Shah, A.2    Tilgner, M.3    Guo, Y.4    Zhao, Y.5    Dong, H.6    Deas, T.7    Zhou, Y.8    Li, H.9    Shi, P.10
  • 118
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution
    • Rey F.A., Heinz F.X., Mandl C., Kunz C., and Harrison S.C. The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature 375 6529 (1995) 291-298
    • (1995) Nature , vol.375 , Issue.6529 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 121
    • 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
    • Shiryaev S.A., Chernov A.V., Aleshin A.E., Shiryaeva T.N., and Strongin A.Y. 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 Pt 9 (2009) 2081-2085
    • (2009) J. Gen. Virol. , vol.90 , Issue.PART 9 , pp. 2081-2085
    • Shiryaev, S.A.1    Chernov, A.V.2    Aleshin, A.E.3    Shiryaeva, T.N.4    Strongin, A.Y.5
  • 122
    • 33749467342 scopus 로고    scopus 로고
    • Murine model for dengue virus-induced lethal disease with increased vascular permeability
    • Shresta S., Sharar K.L., Prigozhin D.M., Beatty P.R., and Harris E. Murine model for dengue virus-induced lethal disease with increased vascular permeability. J. Virol. 80 20 (2006) 10208-10217
    • (2006) J. Virol. , vol.80 , Issue.20 , pp. 10208-10217
    • Shresta, S.1    Sharar, K.L.2    Prigozhin, D.M.3    Beatty, P.R.4    Harris, E.5
  • 123
    • 0032403125 scopus 로고    scopus 로고
    • High-throughput screening assay for helicase enzymes
    • Sivaraja M., Giordano H., and Peterson M.G. High-throughput screening assay for helicase enzymes. Anal. Biochem. 265 1 (1998) 22-27
    • (1998) Anal. Biochem. , vol.265 , Issue.1 , pp. 22-27
    • Sivaraja, M.1    Giordano, H.2    Peterson, M.G.3
  • 127
    • 33846830063 scopus 로고    scopus 로고
    • Virus-induced decline in soluble vascular endothelial growth receptor 2 is associated with plasma leakage in dengue hemorrhagic fever
    • Srikiatkhachorn A., Ajariyakhajorn C., Endy T.P., Kalayanarooj S., Libraty D.H., Green S., Ennis F.A., and Rothman A.L. Virus-induced decline in soluble vascular endothelial growth receptor 2 is associated with plasma leakage in dengue hemorrhagic fever. J. Virol. 81 4 (2007) 1592-1600
    • (2007) J. Virol. , vol.81 , Issue.4 , pp. 1592-1600
    • Srikiatkhachorn, A.1    Ajariyakhajorn, C.2    Endy, T.P.3    Kalayanarooj, S.4    Libraty, D.H.5    Green, S.6    Ennis, F.A.7    Rothman, A.L.8
  • 128
    • 0030764780 scopus 로고    scopus 로고
    • Proteolytic activation of tick-borne encephalitis virus by furin
    • Stadler K., Allison S.L., Schalich J., and Heinz F.X. Proteolytic activation of tick-borne encephalitis virus by furin. J. Virol. 71 11 (1997) 8475-8481
    • (1997) J. Virol. , vol.71 , Issue.11 , pp. 8475-8481
    • Stadler, K.1    Allison, S.L.2    Schalich, J.3    Heinz, F.X.4
  • 129
    • 3343021140 scopus 로고    scopus 로고
    • IL8 release, tight junction and cytoskeleton dynamic reorganization conducive to permeability increase are induced by dengue virus infection of microvascular endothelial monolayers
    • Talavera D., Castillo A.M., Dominguez M.C., Gutierrez A.E., and Meza I. IL8 release, tight junction and cytoskeleton dynamic reorganization conducive to permeability increase are induced by dengue virus infection of microvascular endothelial monolayers. J. Gen. Virol. 85 Pt 7 (2004) 1801-1813
    • (2004) J. Gen. Virol. , vol.85 , Issue.PART 7 , pp. 1801-1813
    • Talavera, D.1    Castillo, A.M.2    Dominguez, M.C.3    Gutierrez, A.E.4    Meza, I.5
  • 130
    • 0029863798 scopus 로고    scopus 로고
    • Recombinant dengue type 1 virus NS5 protein expressed in Escherichia coli exhibits RNA-dependent RNA polymerase activity
    • Tan B.H., Fu J., Sugrue R.J., Yap E.H., Chan Y.C., and Tan Y.H. Recombinant dengue type 1 virus NS5 protein expressed in Escherichia coli exhibits RNA-dependent RNA polymerase activity. Virology 216 2 (1996) 317-325
    • (1996) Virology , vol.216 , Issue.2 , pp. 317-325
    • Tan, B.H.1    Fu, J.2    Sugrue, R.J.3    Yap, E.H.4    Chan, Y.C.5    Tan, Y.H.6
  • 132
    • 0026043319 scopus 로고
    • In situ ELISA for the evaluation of antiviral compounds effective against human cytomegalovirus
    • Tatarowicz W.A., Lurain N.S., and Thompson K.D. In situ ELISA for the evaluation of antiviral compounds effective against human cytomegalovirus. J. Virol. Methods 35 2 (1991) 207-215
    • (1991) J. Virol. Methods , vol.35 , Issue.2 , pp. 207-215
    • Tatarowicz, W.A.1    Lurain, N.S.2    Thompson, K.D.3
  • 133
    • 7644219512 scopus 로고    scopus 로고
    • Serotype-specific entry of dengue virus into liver cells: identification of the 37-kilodalton/67-kilodalton high-affinity laminin receptor as a dengue virus serotype 1 receptor
    • Thepparit C., and Smith D.R. Serotype-specific entry of dengue virus into liver cells: identification of the 37-kilodalton/67-kilodalton high-affinity laminin receptor as a dengue virus serotype 1 receptor. J. Virol. 78 22 (2004) 12647-12656
    • (2004) J. Virol. , vol.78 , Issue.22 , pp. 12647-12656
    • Thepparit, C.1    Smith, D.R.2
  • 134
    • 0031975823 scopus 로고    scopus 로고
    • Mutagenesis of the NS3 protease of dengue virus type 2
    • Valle R.P., and Falgout B. Mutagenesis of the NS3 protease of dengue virus type 2. J. Virol. 72 1 (1998) 624-632
    • (1998) J. Virol. , vol.72 , Issue.1 , pp. 624-632
    • Valle, R.P.1    Falgout, B.2
  • 136
    • 62049084648 scopus 로고    scopus 로고
    • The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner
    • von Moeller H., Basquin C., and Conti E. The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner. Nat. Struct. Mol. Biol. 16 3 (2009) 247-254
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , Issue.3 , pp. 247-254
    • von Moeller, H.1    Basquin, C.2    Conti, E.3
  • 138
    • 0019418822 scopus 로고
    • Terminal sequences of the genome and replicative-form RNA of the flavivirus West Nile virus: absence of poly(A) and possible role in RNA replication
    • Wengler G. Terminal sequences of the genome and replicative-form RNA of the flavivirus West Nile virus: absence of poly(A) and possible role in RNA replication. Virology 113 2 (1981) 544-555
    • (1981) Virology , vol.113 , Issue.2 , pp. 544-555
    • Wengler, G.1
  • 139
    • 0025945616 scopus 로고
    • The carboxy-terminal part of the NS 3 protein of the West Nile flavivirus can be isolated as a soluble protein after proteolytic cleavage and represents an RNA-stimulated NTPase
    • Wengler G., and Wengler G. The carboxy-terminal part of the NS 3 protein of the West Nile flavivirus can be isolated as a soluble protein after proteolytic cleavage and represents an RNA-stimulated NTPase. Virology 184 2 (1991) 707-715
    • (1991) Virology , vol.184 , Issue.2 , pp. 707-715
    • Wengler, G.1    Wengler, G.2
  • 140
    • 0027366948 scopus 로고
    • The NS3 nonstructural protein of flaviviruses contains an RNA triphosphatase activity
    • Wengler G., and Wengler G. The NS3 nonstructural protein of flaviviruses contains an RNA triphosphatase activity. Virology 197 (1993) 265-273
    • (1993) Virology , vol.197 , pp. 265-273
    • Wengler, G.1    Wengler, G.2
  • 141
    • 21644477919 scopus 로고    scopus 로고
    • Castanospermine, a potent inhibitor of dengue virus infection in vitro and in vivo
    • Whitby K., Pierson T., Geiss B., Lane K., Engle M., Zhou Y., Doms R., and Diamond M. Castanospermine, a potent inhibitor of dengue virus infection in vitro and in vivo. J. Virol. 79 14 (2005) 8698-8706
    • (2005) J. Virol. , vol.79 , Issue.14 , pp. 8698-8706
    • Whitby, K.1    Pierson, T.2    Geiss, B.3    Lane, K.4    Engle, M.5    Zhou, Y.6    Doms, R.7    Diamond, M.8
  • 142
    • 23244450531 scopus 로고    scopus 로고
    • Structure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing
    • Wu J., Bera A., Kuhn R., and Smith J. Structure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing. J. Virol. 79 16 (2005) 10268-10277
    • (2005) J. Virol. , vol.79 , Issue.16 , pp. 10268-10277
    • Wu, J.1    Bera, A.2    Kuhn, R.3    Smith, J.4
  • 143
    • 28444499425 scopus 로고    scopus 로고
    • Recent advances in discovery and development of promising therapeutics against hepatitis C virus NS5B RNA-dependent RNA polymerase
    • Wu J.Z., Yao N., Walker M., and Hong Z. Recent advances in discovery and development of promising therapeutics against hepatitis C virus NS5B RNA-dependent RNA polymerase. Mini Rev. Med. Chem. 5 12 (2005) 1103-1112
    • (2005) Mini Rev. Med. Chem. , vol.5 , Issue.12 , pp. 1103-1112
    • Wu, J.Z.1    Yao, N.2    Walker, M.3    Hong, Z.4
  • 144
    • 0036196402 scopus 로고    scopus 로고
    • Antiviral effects of an iminosugar derivative on flavivirus infections
    • Wu S.-F., Lee C.-J., Liao C.-L., Dwek R., Zitzmann N., and Lin Y.-L. Antiviral effects of an iminosugar derivative on flavivirus infections. J. Virol. 76 8 (2002) 3596-3604
    • (2002) J. Virol. , vol.76 , Issue.8 , pp. 3596-3604
    • Wu, S.-F.1    Lee, C.-J.2    Liao, C.-L.3    Dwek, R.4    Zitzmann, N.5    Lin, Y.-L.6
  • 145
    • 23244464646 scopus 로고    scopus 로고
    • Structure of the Dengue virus helicase/nucleoside triphosphatase catalytic domain at a resolution of 2.4 A
    • Xu T., Sampath A., Chao A., Wen D., Nanao M., Chene P., Vasudevan S., and Lescar J. Structure of the Dengue virus helicase/nucleoside triphosphatase catalytic domain at a resolution of 2.4 A. J. Virol. 79 16 (2005) 10278-10288
    • (2005) J. Virol. , vol.79 , Issue.16 , pp. 10278-10288
    • Xu, T.1    Sampath, A.2    Chao, A.3    Wen, D.4    Nanao, M.5    Chene, P.6    Vasudevan, S.7    Lescar, J.8
  • 146
    • 40849130890 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of Japanese encephalitis virus NS3 helicase/nucleoside triphosphatase at a resolution of 1.8 A
    • Yamashita T., Unno H., Mori Y., Tani H., Moriishi K., Takamizawa A., Agoh M., Tsukihara T., and Matsuura Y. Crystal structure of the catalytic domain of Japanese encephalitis virus NS3 helicase/nucleoside triphosphatase at a resolution of 1.8 A. Virology 373 2 (2008) 426-436
    • (2008) Virology , vol.373 , Issue.2 , pp. 426-436
    • Yamashita, T.1    Unno, H.2    Mori, Y.3    Tani, H.4    Moriishi, K.5    Takamizawa, A.6    Agoh, M.7    Tsukihara, T.8    Matsuura, Y.9
  • 147
    • 34247610261 scopus 로고    scopus 로고
    • Crystal structure of the dengue virus RNA-dependent RNA polymerase catalytic domain at 1.85-angstrom resolution
    • Yap T., Xu T., Chen Y., Malet H., Egloff M., Canard B., Vasudevan S., and Lescar J. Crystal structure of the dengue virus RNA-dependent RNA polymerase catalytic domain at 1.85-angstrom resolution. J. Virol. 81 9 (2007) 4753-4765
    • (2007) J. Virol. , vol.81 , Issue.9 , pp. 4753-4765
    • Yap, T.1    Xu, T.2    Chen, Y.3    Malet, H.4    Egloff, M.5    Canard, B.6    Vasudevan, S.7    Lescar, J.8
  • 148
    • 7044253474 scopus 로고    scopus 로고
    • Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function
    • Yedavalli V.S., Neuveut C., Chi Y.H., Kleiman L., and Jeang K.T. Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function. Cell 119 3 (2004) 381-392
    • (2004) Cell , vol.119 , Issue.3 , pp. 381-392
    • Yedavalli, V.S.1    Neuveut, C.2    Chi, Y.H.3    Kleiman, L.4    Jeang, K.T.5
  • 149
    • 50249144556 scopus 로고    scopus 로고
    • Ring expanded nucleoside analogues inhibit RNA helicase and intracellular human immunodeficiency virus type 1 replication
    • Yedavalli V.S., Zhang N., Cai H., Zhang P., Starost M.F., Hosmane R.S., and Jeang K.T. Ring expanded nucleoside analogues inhibit RNA helicase and intracellular human immunodeficiency virus type 1 replication. J. Med. Chem. 51 16 (2008) 5043-5051
    • (2008) J. Med. Chem. , vol.51 , Issue.16 , pp. 5043-5051
    • Yedavalli, V.S.1    Zhang, N.2    Cai, H.3    Zhang, P.4    Starost, M.F.5    Hosmane, R.S.6    Jeang, K.T.7
  • 151
    • 0034616194 scopus 로고    scopus 로고
    • Purified NS2B/NS3 serine protease of dengue virus type 2 exhibits cofactor NS2B dependence for cleavage of substrates with dibasic amino acids in vitro
    • Yusof R., Clum S., Wetzel M., Murthy H.M., and Padmanabhan R. Purified NS2B/NS3 serine protease of dengue virus type 2 exhibits cofactor NS2B dependence for cleavage of substrates with dibasic amino acids in vitro. J. Biol. Chem. 275 14 (2000) 9963-9969
    • (2000) J. Biol. Chem. , vol.275 , Issue.14 , pp. 9963-9969
    • Yusof, R.1    Clum, S.2    Wetzel, M.3    Murthy, H.M.4    Padmanabhan, R.5
  • 152
    • 67650697066 scopus 로고    scopus 로고
    • Development of resistance to passive therapy with a potently neutralizing humanized monoclonal antibody against West Nile virus
    • Zhang S., Vogt M.R., Oliphant T., Engle M., Bovshik E.I., Diamond M.S., and Beasley D.W. Development of resistance to passive therapy with a potently neutralizing humanized monoclonal antibody against West Nile virus. J. Infect. Dis. 200 2 (2009) 202-205
    • (2009) J. Infect. Dis. , vol.200 , Issue.2 , pp. 202-205
    • Zhang, S.1    Vogt, M.R.2    Oliphant, T.3    Engle, M.4    Bovshik, E.I.5    Diamond, M.S.6    Beasley, D.W.7
  • 154
    • 58149487623 scopus 로고    scopus 로고
    • Mechanism of NS2B-mediated activation of NS3pro in dengue virus: molecular dynamics simulations and bioassays
    • Zuo Z., Liew O.W., Chen G., Chong P.C., Lee S.H., Chen K., Jiang H., Puah C.M., and Zhu W. Mechanism of NS2B-mediated activation of NS3pro in dengue virus: molecular dynamics simulations and bioassays. J. Virol. 83 2 (2009) 1060-1070
    • (2009) J. Virol. , vol.83 , Issue.2 , pp. 1060-1070
    • Zuo, Z.1    Liew, O.W.2    Chen, G.3    Chong, P.C.4    Lee, S.H.5    Chen, K.6    Jiang, H.7    Puah, C.M.8    Zhu, W.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.