메뉴 건너뛰기




Volumn 11, Issue 5, 2016, Pages 433-445

New developments in flavivirus drug discovery

Author keywords

Antiviral; dengue; flavivirus; inhibitor; nucleoside; peptide; small molecule

Indexed keywords

ANTIVIRUS AGENT; NONSTRUCTURAL PROTEIN 3; NONSTRUCTURAL PROTEIN 5; VIRUS PROTEIN; VIRAL PROTEIN;

EID: 84961390432     PISSN: 17460441     EISSN: 1746045X     Source Type: Journal    
DOI: 10.1517/17460441.2016.1160887     Document Type: Review
Times cited : (40)

References (128)
  • 2
    • 84876804736 scopus 로고    scopus 로고
    • The global distribution and burden of dengue
    • Bhatt S, Gething PW, Brady OJ, et al. The global distribution and burden of dengue. Nature. 2013;496(7446):504-507. doi:10.1038/ nature12060.
    • (2013) Nature , vol.496 , Issue.7446 , pp. 504-507
    • Bhatt, S.1    Gething, P.W.2    Brady, O.J.3
  • 3
    • 84872423665 scopus 로고    scopus 로고
    • WHO Factscheet No117. May 2015 [cited 2015 Sep 29];
    • Dengue and severe dengue. WHO Factscheet No117. May 2015 [cited 2015 Sep 29]; Available from: http://www.who.int/mediacen tre/factsheets/fs117/en/
    • Dengue and Severe Dengue
  • 4
    • 79955602230 scopus 로고    scopus 로고
    • Dengue: A continuing global threat
    • Guzman MG, Halstead SB, Artsob H, et al. Dengue: a continuing global threat. Nat Rev Micro. 2010;8(12 Suppl):S7-S16.
    • (2010) Nat Rev Micro , vol.8 , Issue.12 , pp. S7-S16
    • Guzman, M.G.1    Halstead, S.B.2    Artsob, H.3
  • 5
    • 0036468861 scopus 로고    scopus 로고
    • Epidemic dengue/dengue hemorrhagic fever as a public health social and economic problem in the 21st century
    • Gubler DJ. Epidemic dengue/dengue hemorrhagic fever as a public health, social and economic problem in the 21st century. Trends in Microbiology. 2002;10(2):100-103.
    • (2002) Trends in Microbiology , vol.10 , Issue.2 , pp. 100-103
    • Gubler, D.J.1
  • 6
    • 84896984783 scopus 로고    scopus 로고
    • Japanese encephalitis: The virus and vaccines
    • Yun S-I, Lee Y-M. Japanese encephalitis: the virus and vaccines. Hum Vaccin Immunother. 2014;10(2):263-279. doi:10.4161/ hv.26902.
    • (2014) Hum Vaccin Immunother , vol.10 , Issue.2 , pp. 263-279
    • Yun, S.-I.1    Lee, Y.-M.2
  • 7
    • 84896704524 scopus 로고    scopus 로고
    • Yellow fever vaccine: An effective vaccine for travelers
    • Verma R, Khanna P, Chawla S. Yellow fever vaccine: An effective vaccine for travelers. Hum Vaccin Immunother. 2014;10(1):126-128. doi:10.4161/hv.26549.
    • (2014) Hum Vaccin Immunother , vol.10 , Issue.1 , pp. 126-128
    • Verma, R.1    Khanna, P.2    Chawla, S.3
  • 8
    • 45849098301 scopus 로고    scopus 로고
    • Advances in vaccination against tick-borne encephalitis
    • Rendi-Wagner P. Advances in vaccination against tick-borne encephalitis. Expert Rev Vaccines. 2008;7(5):589-596. doi:10.1586/ 14760584.7.5.589.
    • (2008) Expert Rev Vaccines , vol.7 , Issue.5 , pp. 589-596
    • Rendi-Wagner, P.1
  • 9
    • 0004214516 scopus 로고    scopus 로고
    • WHO Factsheet No100. Mar 2014 [cited 2015 Sep 30];
    • Yellow fever. WHO Factsheet No100. Mar 2014 [cited 2015 Sep 30]; Available from: http://www.who.int/mediacentre/factsheets/fs100/en/
    • Yellow Fever
  • 10
    • 84860710019 scopus 로고    scopus 로고
    • WHO Factsheet No386, Mar 2014 [cited 2015 Sep 30];
    • Japanese encephalitis. WHO Factsheet No386 2015. Mar 2014 [cited 2015 Sep 30]; Available from: http://www.who.int/mediacen tre/factsheets/fs386/en/
    • (2015) Japanese Encephalitis
  • 11
    • 84861978036 scopus 로고    scopus 로고
    • Flaviviruses and flavivirus vaccines
    • Heinz FX, Stiasny K. Flaviviruses and flavivirus vaccines. Vaccine. 2012;30(29):4301-4306. doi:10.1016/j.vaccine.2011.09.114.
    • (2012) Vaccine , vol.30 , Issue.29 , pp. 4301-4306
    • Heinz, F.X.1    Stiasny, K.2
  • 12
    • 77950448257 scopus 로고    scopus 로고
    • Natural strain variation and antibody neutralization of dengue serotype 3 viruses
    • Wahala WMPB, Donaldson EF, de Alwis R, et al. Natural strain variation and antibody neutralization of dengue serotype 3 viruses. PLoS Pathog. 2010;6(3):e1000821. doi:10.1371/journal. ppat.1000975.
    • (2010) PLoS Pathog , vol.6 , Issue.3
    • Wahala, W.M.P.B.1    Donaldson, E.F.2    De Alwis, R.3
  • 13
    • 84952639313 scopus 로고    scopus 로고
    • Development of the Sanofi Pasteur tetravalent dengue vaccine: One more step forward
    • Guy B, Briand O, Lang J, et al. Development of the Sanofi Pasteur tetravalent dengue vaccine: one more step forward. Vaccine. 2015;33. doi:10.1016/j.vaccine.2015.09.108.
    • (2015) Vaccine , pp. 33
    • Guy, B.1    Briand, O.2    Lang, J.3
  • 14
    • 84893952668 scopus 로고    scopus 로고
    • Targeting host factors to treat west nile and dengue viral infections
    • 683
    • Krishnan M, Garcia-Blanco M. Targeting host factors to treat west nile and dengue viral infections. Viruses. 2014;6(2):683. doi:10.3390/ v6020683.
    • (2014) Viruses , vol.6 , Issue.2
    • Krishnan, M.1    Garcia-Blanco, M.2
  • 15
    • 77955842615 scopus 로고    scopus 로고
    • Role of host cell factors in flavivirus infection: Implications for pathogenesis and development of antiviral drugs
    • Pastorino B, Nougairède A, Wurtz N, et al. Role of host cell factors in flavivirus infection: implications for pathogenesis and development of antiviral drugs. Antiviral Res. 2010;87(3):281-94. doi:10.1016/j. antiviral.2010.04.014.
    • (2010) Antiviral Res , vol.87 , Issue.3 , pp. 281-294
    • Pastorino, B.1    Nougairède, A.2    Wurtz, N.3
  • 16
    • 84935710644 scopus 로고    scopus 로고
    • Flaviviral NS4b, chameleon and jack-in-the-box roles in viral replication and pathogenesis, and a molecular target for antiviral intervention
    • Zmurko J, Neyts J, Dallmeier K. Flaviviral NS4b, chameleon and jack-in-the-box roles in viral replication and pathogenesis, and a molecular target for antiviral intervention. Rev Med Virol. 2015;25 (4):205-23. doi:10.1002/rmv.1835.
    • (2015) Rev Med Virol , vol.25 , Issue.4 , pp. 205-223
    • Zmurko, J.1    Neyts, J.2    Dallmeier, K.3
  • 17
    • 84938152526 scopus 로고    scopus 로고
    • Discovery of dengue virus NS4B inhibitors
    • Wang Q-Y, Dong H, Zou B, et al. Discovery of dengue virus NS4B inhibitors. J Virol. 2015. doi:10.1128/JVI.00855-15.
    • (2015) J Virol
    • Wang, Q.-Y.1    Dong, H.2    Zou, B.3
  • 18
    • 84925855875 scopus 로고    scopus 로고
    • Targeting dengue virus NS4B protein for drug discovery
    • Xie X, Zou J, Wang Q-Y, et al. Targeting dengue virus NS4B protein for drug discovery. Antiviral Res. 2015;118:39-45. doi:10.1016/j. antiviral.2015.03.007.
    • (2015) Antiviral Res , vol.118 , pp. 39-45
    • Xie, X.1    Zou, J.2    Wang, Q.-Y.3
  • 19
    • 11144348130 scopus 로고    scopus 로고
    • A structural perspective of the flavivirus life cycle
    • Mukhopadhyay S, Kuhn RJ, Rossmann MG. A structural perspective of the flavivirus life cycle. Nat Rev Micro. 2005;3(1):13-22. doi:10.1038/nrmicro1067.
    • (2005) Nat Rev Micro , vol.3 , Issue.1 , pp. 13-22
    • Mukhopadhyay, S.1    Kuhn, R.J.2    Rossmann, M.G.3
  • 20
    • 84875777404 scopus 로고    scopus 로고
    • Membrane topology and function of dengue virus NS2A Protein
    • Xie X, Gayen S, Kang C, et al. Membrane topology and function of dengue virus NS2A Protein. J Virol. 2013;87(8):4609-4622. doi:10.1128/JVI.02424-12.
    • (2013) J Virol , vol.87 , Issue.8 , pp. 4609-4622
    • Xie, X.1    Gayen, S.2    Kang, C.3
  • 21
    • 84944257957 scopus 로고
    • Secondary structure and membrane topology of dengue virus NS4B N-terminal 125 amino acids
    • Li Y, Kim YM, Zou J, et al. Secondary structure and membrane topology of dengue virus NS4B N-terminal 125 amino acids. Biochim Biophys Acta - Biomembr. 2015;1848(12):3150-3157. doi:10.1016/j.bbamem.2015.09.016.
    • (1848) Biochim Biophys Acta - Biomembr , Issue.12 , pp. 3150-3157
    • Li, Y.1    Kim, Y.M.2    Zou, J.3
  • 22
    • 26944495290 scopus 로고    scopus 로고
    • Wrapping things up about virus RNA replication
    • Mackenzie J. Wrapping things up about virus RNA replication. Traffic. 2005;6(11):967-977. doi:10.1111/j.1600-0854.2005.00339.x.
    • (2005) Traffic , vol.6 , Issue.11 , pp. 967-977
    • Mackenzie, J.1
  • 23
    • 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 TJ, Weir RC, Grakoui A, et al. 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 Natl Acad Sci U S A. 1990;87 (22):8898-8902.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , Issue.22 , pp. 8898-8902
    • Chambers, T.J.1    Weir, R.C.2    Grakoui, A.3
  • 24
    • 77954956665 scopus 로고    scopus 로고
    • Structure and functionality in flavivirus NS-proteins: Perspectives for drug design
    • Bollati M, Alvarez K, Assenberg R, et al. Structure and functionality in flavivirus NS-proteins: Perspectives for drug design. Antiviral Res. 2010;87(2):125-148. doi:10.1016/j.antiviral.2009.11.009.
    • (2010) Antiviral Res , vol.87 , Issue.2 , pp. 125-148
    • Bollati, M.1    Alvarez, K.2    Assenberg, R.3
  • 25
    • 0037495036 scopus 로고    scopus 로고
    • A ligand-binding pocket in the dengue virus envelope glycoprotein
    • Modis Y, Ogata S, Clements D, et al. A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc Natl Acad Sci U S A. 2003;100(12):6986-6991. doi:10.1073/pnas.0832193100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.12 , pp. 6986-6991
    • Modis, Y.1    Ogata, S.2    Clements, D.3
  • 26
    • 0037013858 scopus 로고    scopus 로고
    • An RNA cap (nucleoside-2'- O-)-methyltransferase in the flavivirus RNA polymerase NS5: Crystal structure and functional characterization
    • Egloff MP, Benarroch D, Selisko B, et al. An RNA cap (nucleoside-2'- O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization. Embo J. 2002;21 (11):2757-2768. doi:10.1093/emboj/21.11.2757.
    • (2002) Embo J , vol.21 , Issue.11 , pp. 2757-2768
    • Egloff, M.P.1    Benarroch, D.2    Selisko, B.3
  • 27
    • 34247610261 scopus 로고    scopus 로고
    • Crystal structure of the dengue virus RNA-dependent RNA polymerase catalytic domain at 1.85-angstrom resolution
    • Yap TL, Xu T, Chen YL, et al. Crystal structure of the dengue virus RNA-dependent RNA polymerase catalytic domain at 1.85-angstrom resolution. J Virol. 2007;81(9):4753-4765. doi:10.1128/ JVI.02283-06.
    • (2007) J Virol , vol.81 , Issue.9 , pp. 4753-4765
    • Yap, T.L.1    Xu, T.2    Chen, Y.L.3
  • 28
    • 33745025763 scopus 로고    scopus 로고
    • Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus
    • Erbel P, Schiering N, D'Arcy A, et al. Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus. Nat Struct Mol Biol. 2006;13(4):372-373. doi:10.1038/nsmb1073.
    • (2006) Nat Struct Mol Biol , vol.13 , Issue.4 , pp. 372-373
    • Erbel, P.1    Schiering, N.2    D'Arcy, A.3
  • 29
    • 37349023165 scopus 로고    scopus 로고
    • Crystal structure of the NS3 proteasehelicase from dengue virus
    • Luo D, Xu T, Hunke C, et al. Crystal structure of the NS3 proteasehelicase from dengue virus. J Virol. 2008;82(1):173-183. doi:10.1128/JVI.01788-07.
    • (2008) J Virol , vol.82 , Issue.1 , pp. 173-183
    • Luo, D.1    Xu, T.2    Hunke, C.3
  • 30
    • 57149091105 scopus 로고    scopus 로고
    • Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein
    • Luo D, Xu T, Watson RP, et al. Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein. EMBO Journal. 2008;27 (23):3209-3219. doi:10.1038/emboj.2008.232.
    • (2008) EMBO Journal , vol.27 , Issue.23 , pp. 3209-3219
    • Luo, D.1    Xu, T.2    Watson, R.P.3
  • 31
    • 77955710423 scopus 로고    scopus 로고
    • Dengue virus life cycle: Viral and host factors modulating infectivity
    • Rodenhuis-Zybert I, Wilschut J, Smit J. Dengue virus life cycle: viral and host factors modulating infectivity. Cell Mol Life Sci. 2010;67 (16):2773-2786. doi:10.1007/s00018-010-0357-z.
    • (2010) Cell Mol Life Sci , vol.67 , Issue.16 , pp. 2773-2786
    • Rodenhuis-Zybert, I.1    Wilschut, J.2    Smit, J.3
  • 32
    • 58149265437 scopus 로고    scopus 로고
    • Dissecting the cell entry pathway of dengue virus by single-particle tracking in living cells
    • can der Schaar HM, Rust MJ, Chen C, et al. Dissecting the cell entry pathway of dengue virus by single-particle tracking in living cells. PLoS Pathog. 2008;4(12):e1000244. doi:10.1371/journal. ppat.1000244.
    • (2008) PLoS Pathog , vol.4 , Issue.12
    • Can Der Schaar, H.M.1    Rust, M.J.2    Chen, C.3
  • 33
    • 0031729823 scopus 로고    scopus 로고
    • Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41- mediated virus entry
    • Kilby JM, Hopkins S, Venetta TM, et al. Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41- mediated virus entry. Nat Med. 1998;4(11):1302-1307. doi:10.1038/3293.
    • (1998) Nat Med , vol.4 , Issue.11 , pp. 1302-1307
    • Kilby, J.M.1    Hopkins, S.2    Venetta, T.M.3
  • 34
    • 84941114795 scopus 로고    scopus 로고
    • Interaction of flaviviruses with reproduction inhibitors binding in β-OG pocket: Insights from molecular dynamics simulations
    • Dueva EV, Osolodkin DI, Kozlovskaya LI, et al. Interaction of flaviviruses with reproduction inhibitors binding in β-OG pocket: insights from molecular dynamics simulations. Mol Inform. 2014;33(10):695-708. doi:10.1002/minf.201300185.
    • (2014) Mol Inform , vol.33 , Issue.10 , pp. 695-708
    • Dueva, E.V.1    Osolodkin, D.I.2    Kozlovskaya, L.I.3
  • 35
    • 84940003248 scopus 로고    scopus 로고
    • Design syn thesis, optimization and antiviral activity of a class of hybrid dengue virus e protein inhibitors
    • Jadav SS, Kaptein S, Timiri A, et al. Design, synthesis, optimization and antiviral activity of a class of hybrid dengue virus E protein inhibitors. Bioorg Med Chem Lett. 2015;25(8):1747-1752. doi:10.1016/j.bmcl.2015.02.059.
    • (2015) Bioorg Med Chem Lett , vol.25 , Issue.8 , pp. 1747-1752
    • Jadav, S.S.1    Kaptein, S.2    Timiri, A.3
  • 36
    • 84924322763 scopus 로고    scopus 로고
    • Synthesis and assessment of 4-aminotetrahydroquinazoline derivatives as tick-borne encephalitis virus reproduction inhibitors
    • Sedenkova KN, Dueva EV, Averina EB, et al. Synthesis and assessment of 4-aminotetrahydroquinazoline derivatives as tick-borne encephalitis virus reproduction inhibitors. Org Biomol Chem. 2015;13(11):3406-3415. doi:10.1039/C4OB02649G.
    • (2015) Org Biomol Chem , vol.13 , Issue.11 , pp. 3406-3415
    • Sedenkova, K.N.1    Dueva, E.V.2    Averina, E.B.3
  • 37
    • 84883701961 scopus 로고    scopus 로고
    • Antibodydependent enhancement of dengue virus infection is inhibited by SA-17, a doxorubicin derivative
    • Ayala-Nuñez NV, Jarupathirun P, Kaptein SJF, et al. Antibodydependent enhancement of dengue virus infection is inhibited by SA-17, a doxorubicin derivative. Antiviral Res. 2013;100(1):238-45. doi:10.1016/j.antiviral.2013.08.013.
    • (2013) Antiviral Res , vol.100 , Issue.1 , pp. 238-245
    • Ayala-Nuñez, N.V.1    Jarupathirun, P.2    Kaptein, S.J.F.3
  • 38
    • 84862094841 scopus 로고    scopus 로고
    • An analogue of the antibiotic teicoplanin prevents flavivirus entry in vitro
    • De Burghgraeve T, Kaptein SJF, Ayala-Nunez NV, et al. An analogue of the antibiotic teicoplanin prevents flavivirus entry in vitro. PLoS ONE. 2012;7(5):e37244. doi:10.1371/journal.pone.0037244.
    • (2012) PLoS ONE , vol.7 , Issue.5
    • De Burghgraeve, T.1    Kaptein, S.J.F.2    Ayala-Nunez, N.V.3
  • 39
    • 77957192264 scopus 로고    scopus 로고
    • Genotype-specific neutralization and protection by antibodies against dengue virus type 3
    • Brien JD, Austin SK, Sukupolvi-Petty S, et al. Genotype-specific neutralization and protection by antibodies against dengue virus type 3. J Virol. 2010;84(20):10630-10643. doi:10.1128/JVI.01190-10.
    • (2010) J Virol , vol.84 , Issue.20 , pp. 10630-10643
    • Brien, J.D.1    Austin, S.K.2    Sukupolvi-Petty, S.3
  • 40
    • 84935097021 scopus 로고    scopus 로고
    • Dengue Virus. Cryo-EM structure of an antibody that neutralizes dengue virus type 2 by locking e protein dimers
    • Fibriansah G, Ibarra KD, Ng TS, et al. Dengue Virus. Cryo-EM structure of an antibody that neutralizes dengue virus type 2 by locking E protein dimers. Science. 2015;349(6243):88-91. doi:10.1126/ science.aaa8651.
    • (2015) Science , vol.349 , Issue.6243 , pp. 88-91
    • Fibriansah, G.1    Ibarra, K.D.2    Ng, T.S.3
  • 41
    • 84938422733 scopus 로고    scopus 로고
    • Structureguided design of an anti-dengue antibody directed to a nonimmunodominant epitope
    • Robinson Luke N, Tharakaraman K, Rowley Kirk J, et al. Structureguided design of an anti-dengue antibody directed to a nonimmunodominant epitope. Cell. 2015;162(3):493-504. doi:10.1016/ j.cell.2015.06.057.
    • (2015) Cell , vol.162 , Issue.3 , pp. 493-504
    • Robinson Luke, N.1    Tharakaraman, K.2    Rowley Kirk, J.3
  • 42
    • 84860826712 scopus 로고    scopus 로고
    • Identification of human neutralizing antibodies that bind to complex epitopes on dengue virions
    • de Alwis R, Smith SA, Olivarez NP, et al. Identification of human neutralizing antibodies that bind to complex epitopes on dengue virions. Proc Natl Acad Sci U S A. 2012;109(19):7439-7444. doi:10.1073/pnas.1200566109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.19 , pp. 7439-7444
    • De Alwis, R.1    Smith, S.A.2    Olivarez, N.P.3
  • 43
    • 0030764559 scopus 로고    scopus 로고
    • Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate
    • Chen Y, Maguire T, Hileman RE, et al. Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate. Nat Med. 1997;3(8):866-871.
    • (1997) Nat Med , vol.3 , Issue.8 , pp. 866-871
    • Chen, Y.1    Maguire, T.2    Hileman, R.E.3
  • 44
    • 84876821169 scopus 로고    scopus 로고
    • Sulfated polysaccharide, curdlan sulfate, efficiently prevents entry/fusion and restricts antibody-dependent enhancement of dengue virus infection in vitro: A possible candidate for clinical application
    • Ichiyama K, Gopala Reddy SB, Zhang LF, et al. Sulfated polysaccharide, curdlan sulfate, efficiently prevents entry/fusion and restricts antibody-dependent enhancement of dengue virus infection in vitro: a possible candidate for clinical application. PLoS Negl Trop Dis. 2013;7(4):e2188. doi:10.1371/journal.pntd.0002188.
    • (2013) PLoS Negl Trop Dis , vol.7 , Issue.4
    • Ichiyama, K.1    Gopala Reddy, S.B.2    Zhang, L.F.3
  • 45
    • 84883415457 scopus 로고    scopus 로고
    • Sulfated Escherichia coli K5 Polysaccharide derivatives inhibit dengue virus infection of human microvascular endothelial cells by interacting with the viral envelope protein e domain III
    • Vervaeke P, Alen M, Noppen S, et al. Sulfated Escherichia coli K5 Polysaccharide derivatives inhibit dengue virus infection of human microvascular endothelial cells by interacting with the viral envelope protein E domain III. PLoS ONE. 2013;8(8):e74035. doi:10.1371/ journal.pone.0074035.
    • (2013) PLoS ONE , vol.8 , Issue.8 , pp. e74035
    • Vervaeke, P.1    Alen, M.2    Noppen, S.3
  • 46
    • 84865574164 scopus 로고    scopus 로고
    • Antiviral activity against dengue virus of diverse classes of algal sulfated polysaccharides
    • Pujol CA, Ray S, Ray B, et al. Antiviral activity against dengue virus of diverse classes of algal sulfated polysaccharides. Int J Biol Macromol. 2012;51(4):412-416. doi:10.1016/j.ijbiomac.2012.05.028.
    • (2012) Int J Biol Macromol , vol.51 , Issue.4 , pp. 412-416
    • Pujol, C.A.1    Ray, S.2    Ray, B.3
  • 47
    • 84898664227 scopus 로고    scopus 로고
    • Changes in antiviral susceptibility to entry inhibitors and endocytic uptake of dengue-2 virus serially passaged in Vero or C6/36 cells
    • Acosta EG, Piccini LE, Talarico LB, et al. Changes in antiviral susceptibility to entry inhibitors and endocytic uptake of dengue-2 virus serially passaged in Vero or C6/36 cells. Virus Res. 2014;184:39-43. doi:10.1016/j.virusres.2014.02.011.
    • (2014) Virus Res , vol.184 , pp. 39-43
    • Acosta, E.G.1    Piccini, L.E.2    Talarico, L.B.3
  • 48
    • 84878992111 scopus 로고    scopus 로고
    • Exploiting herpes simplex virus entry for novel therapeutics
    • Hadigal S, Shukla D. Exploiting herpes simplex virus entry for novel therapeutics. Viruses. 2013;5(6):1447-1465. doi:10.3390/v5061447.
    • (2013) Viruses , vol.5 , Issue.6 , pp. 1447-1465
    • Hadigal, S.1    Shukla, D.2
  • 49
    • 55949108725 scopus 로고    scopus 로고
    • Identification of specific histidines as pH sensors in flavivirus membrane fusion
    • Fritz R, Stiasny K, Heinz FX. Identification of specific histidines as pH sensors in flavivirus membrane fusion. J Cell Biol. 2008;183(2):353-361. doi:10.1083/jcb.200806081.
    • (2008) J Cell Biol , vol.183 , Issue.2 , pp. 353-361
    • Fritz, R.1    Stiasny, K.2    Heinz, F.X.3
  • 50
    • 23744446349 scopus 로고    scopus 로고
    • Peptide inhibitors of dengue virus and West Nile virus infectivity
    • Hrobowski YM, Garry RF, Michael SF. Peptide inhibitors of dengue virus and West Nile virus infectivity. Virol J. 2005;2:49-49. doi:10.1186/1743-422X-2-49.
    • (2005) Virol J , vol.2 , pp. 49
    • Hrobowski, Y.M.1    Garry, R.F.2    Michael, S.F.3
  • 51
    • 84870626791 scopus 로고    scopus 로고
    • Release of dengue virus genome induced by a peptide inhibitor
    • Lok S-M, Costin JM, Hrobowski YM, et al. Release of dengue virus genome induced by a peptide inhibitor. PLoS ONE. 2012;7(11): e50995. doi:10.1371/journal.pone.0050995.
    • (2012) PLoS ONE , vol.7 , Issue.11
    • Lok, S.-M.1    Costin, J.M.2    Hrobowski, Y.M.3
  • 52
    • 77956998861 scopus 로고    scopus 로고
    • Structural optimization and de novo design of dengue virus entry inhibitory peptides
    • Costin JM, Jenwitheesuk E, Lok S-M, et al. Structural optimization and de novo design of dengue virus entry inhibitory peptides. PLoS Negl Trop Dis. 2010;4(6):e721. doi:10.1371/journal.pntd.0000721.
    • (2010) PLoS Negl Trop Dis , vol.4 , Issue.6
    • Costin, J.M.1    Jenwitheesuk, E.2    Lok, S.-M.3
  • 53
    • 84894210072 scopus 로고    scopus 로고
    • Peptide inhibitor of Japanese encephalitis virus infection targeting envelope protein domain III
    • Zu X, Liu Y, Wang S, et al. Peptide inhibitor of Japanese encephalitis virus infection targeting envelope protein domain III. Antiviral Res. 2014;104:7-14. doi:10.1016/j.antiviral.2014.01.011.
    • (2014) Antiviral Res , vol.104 , pp. 7-14
    • Zu, X.1    Liu, Y.2    Wang, S.3
  • 54
    • 84861211842 scopus 로고    scopus 로고
    • Small-molecule inhibitors of dengue-virus entry
    • Schmidt AG, Lee K, Yang PL, et al. Small-molecule inhibitors of dengue-virus entry. PLoS Pathog. 2012;8(4):e1002627. doi:10.1371/journal.ppat.1002627.
    • (2012) PLoS Pathog , vol.8 , Issue.4
    • Schmidt, A.G.1    Lee, K.2    Yang, P.L.3
  • 55
    • 73549088708 scopus 로고    scopus 로고
    • Molecular basis of human immunodeficiency virus drug resistance: An update
    • Menéndez-Arias L. Molecular basis of human immunodeficiency virus drug resistance: an update. Antiviral Res. 2010;85(1):210-231. doi:10.1016/j.antiviral.2009.07.006.
    • (2010) Antiviral Res , vol.85 , Issue.1 , pp. 210-231
    • Menéndez-Arias, L.1
  • 56
    • 0034628448 scopus 로고    scopus 로고
    • Protease Inhibitors: Current status and future prospects
    • Leung D, Abbenante G, Fairlie DP. Protease Inhibitors: Current status and future prospects. J Med Chem. 2000;43(3):305-341.
    • (2000) J Med Chem , vol.43 , Issue.3 , pp. 305-341
    • Leung, D.1    Abbenante, G.2    Fairlie, D.P.3
  • 57
    • 84892151143 scopus 로고    scopus 로고
    • Chronic hepatitis C: Future treatment
    • Wendt A, Adhoute X, Castellani P, et al. Chronic hepatitis C: future treatment. Clin Pharmacol. 2014;6:1-17. doi:10.2147/CPAA.S30338.
    • (2014) Clin Pharmacol , vol.6 , pp. 1-17
    • Wendt, A.1    Adhoute, X.2    Castellani, P.3
  • 58
    • 0025864149 scopus 로고
    • Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins
    • Falgout B, Pethel M, Zhang YM, et al. Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins. J Virol. 1991;65(5):2467-2475.
    • (1991) J Virol , vol.65 , Issue.5 , pp. 2467-2475
    • Falgout, B.1    Pethel, M.2    Zhang, Y.M.3
  • 59
    • 33846106926 scopus 로고    scopus 로고
    • Substrate specificity of recombinant dengue 2 virus NS2B-NS3 protease: Influence of natural and unnatural basic amino acids on hydrolysis of synthetic fluorescent substrates
    • Gouvea IE, Izidoro MA, Judice WAS, et al. Substrate specificity of recombinant dengue 2 virus NS2B-NS3 protease: Influence of natural and unnatural basic amino acids on hydrolysis of synthetic fluorescent substrates. Arch Biochem Biophys. 2007;457(2):187-196. doi:10.1016/j.abb.2006.11.005.
    • (2007) Arch Biochem Biophys , vol.457 , Issue.2 , pp. 187-196
    • Gouvea, I.E.1    Izidoro, M.A.2    Judice, W.A.S.3
  • 60
    • 23344446921 scopus 로고    scopus 로고
    • Functional profiling of recombinant NS3 proteases from all four serotypes of dengue virus using tetrapeptide and octapeptide substrate libraries
    • Li J, Lim SP, Beer D, et al. Functional profiling of recombinant NS3 proteases from all four serotypes of dengue virus using tetrapeptide and octapeptide substrate libraries. J Biol Chem. 2005;280 (31):28766-28774. doi:10.1074/jbc.M500588200.
    • (2005) J Biol Chem , vol.280 , Issue.31 , pp. 28766-28774
    • Li, J.1    Lim, S.P.2    Beer, D.3
  • 61
    • 33846883704 scopus 로고    scopus 로고
    • Cleavage preference distinguishes the two-component NS2B-NS3 serine proteinases of dengue and West Nile viruses
    • Shiryaev Sergey A, Kozlov Igor A, Ratnikov Boris I, et al. Cleavage preference distinguishes the two-component NS2B-NS3 serine proteinases of dengue and West Nile viruses. Biochem J. 2007;401 (Pt 3):743-752. doi:10.1042/BJ20061136.
    • (2007) Biochem J , vol.401 , pp. 743-752
    • Shiryaev Sergey, A.1    Kozlov Igor, A.2    Ratnikov Boris, I.3
  • 62
    • 67650663433 scopus 로고    scopus 로고
    • New approaches to structure-based discovery of dengue protease inhibitors
    • Tomlinson SM, Malmstrom RD, Watowich SJ. New approaches to structure-based discovery of dengue protease inhibitors. Infect Disorders Drug Targets. 2009;9(3):17. doi:10.2174/ 1871526510909030327.
    • (2009) Infect Disorders Drug Targets , vol.9 , Issue.3 , pp. 17
    • Tomlinson, S.M.1    Malmstrom, R.D.2    Watowich, S.J.3
  • 63
    • 52449113528 scopus 로고    scopus 로고
    • Potent cationic inhibitors of West Nile virus NS2B/NS3 protease with serum stability, cell permeability and antiviral activity
    • Stoermer MJ, Chappell KJ, Liebscher S, et al. Potent cationic inhibitors of West Nile virus NS2B/NS3 protease with serum stability, cell permeability and antiviral activity. J Med Chem. 2008;51 (18):5714-5721. doi:10.1021/jm800503y.
    • (2008) J Med Chem , vol.51 , Issue.18 , pp. 5714-5721
    • Stoermer, M.J.1    Chappell, K.J.2    Liebscher, S.3
  • 64
    • 27744520272 scopus 로고    scopus 로고
    • Peptide inhibitors of dengue virus NS3 protease. Part 2: SAR study of tetrapeptide aldehyde inhibitors
    • Yin Z, Patel SJ, Wang W-L, et al. Peptide inhibitors of dengue virus NS3 protease. Part 2: SAR study of tetrapeptide aldehyde inhibitors. Bioorg Med Chem Lett. 2006;16(1):40-43. doi:10.1016/j. bmcl.2005.09.049.
    • (2006) Bioorg Med Chem Lett , vol.16 , Issue.1 , pp. 40-43
    • Yin, Z.1    Patel, S.J.2    Wang, W.-L.3
  • 65
    • 80052859422 scopus 로고    scopus 로고
    • Tripeptide inhibitors of dengue and West Nile virus NS2B-NS3 protease
    • Schüller A, Yin Z, Brian Chia CS, et al. Tripeptide inhibitors of dengue and West Nile virus NS2B-NS3 protease. Antiviral Res. 2011;92(1):96-101. doi:10.1016/j.antiviral.2011.07.002.
    • (2011) Antiviral Res , vol.92 , Issue.1 , pp. 96-101
    • Schüller, A.1    Yin, Z.2    Brian Chia, C.S.3
  • 66
    • 84858145412 scopus 로고    scopus 로고
    • Retro peptide-hybrids as selective inhibitors of the dengue virus NS2B-NS3 protease
    • Nitsche C, Behnam MAM, Steuer C, et al. Retro peptide-hybrids as selective inhibitors of the dengue virus NS2B-NS3 protease. Antiviral Res. 2012;94(1):72-79. doi:10.1016/j.antiviral.2012.02.008.
    • (2012) Antiviral Res , vol.94 , Issue.1 , pp. 72-79
    • Nitsche, C.1    Behnam, M.A.M.2    Steuer, C.3
  • 67
    • 84946496771 scopus 로고    scopus 로고
    • Dual inhibitors of the dengue and West Nile virus NS2B-NS3 proteases: Syn thesis, biological evaluation and docking studies of novel peptide-hybrids
    • Bastos Lima A, Behnam MAM, El Sherif Y, et al. Dual inhibitors of the dengue and West Nile virus NS2B-NS3 proteases: synthesis, biological evaluation and docking studies of novel peptide-hybrids. Bioorg Med Chem. 2015;23(17):5748-5755. doi:10.1016/j. bmc.2015.07.012.
    • (2015) Bioorg Med Chem , vol.23 , Issue.17 , pp. 5748-5755
    • Bastos Lima, A.1    Behnam, M.A.M.2    El Sherif, Y.3
  • 68
    • 84949907949 scopus 로고    scopus 로고
    • Discovery of nanomolar dengue and West Nile virus protease inhibitors containing a 4-benzyloxyphenylglycine residue
    • Behnam MAM, Graf D, Bartenschlager R, et al. Discovery of nanomolar dengue and West Nile virus protease inhibitors containing a 4-benzyloxyphenylglycine residue. J Med Chem. 2015. doi:10.1021/ acs.jmedchem.5b01441.
    • (2015) J Med Chem
    • Behnam, M.A.M.1    Graf, D.2    Bartenschlager, R.3
  • 69
    • 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, et al. Probing the substrate specificity of the dengue virus type 2 NS3 serine protease by using internally quenched fluorescent peptides. Biochem J. 2006;397(1):203-211. doi:10.1042/BJ20051767.
    • (2006) Biochem J , vol.397 , Issue.1 , pp. 203-211
    • Niyomrattanakit, P.1    Yahorava, S.2    Mutule, I.3
  • 70
    • 84873816287 scopus 로고    scopus 로고
    • Development and characterization of new peptidomimetic inhibitors of the West Nile virus NS2B-NS3 protease
    • Hammamy MZ, Haase C, Hammami M, et al. Development and characterization of new peptidomimetic inhibitors of the West Nile virus NS2B-NS3 protease. ChemMedChem. 2013;8(2):231-241. doi:10.1002/cmdc.201200497.
    • (2013) ChemMedChem , vol.8 , Issue.2 , pp. 231-241
    • Hammamy, M.Z.1    Haase, C.2    Hammami, M.3
  • 71
    • 84943749258 scopus 로고    scopus 로고
    • Phenylalanine and phenylglycine analogues as arginine mimetics in dengue protease inhibitors
    • Weigel LF, Nitsche C, Graf D, et al. Phenylalanine and phenylglycine analogues as arginine mimetics in dengue protease inhibitors. J Med Chem. 2015;58(19):7719-7733. doi:10.1021/acs. jmedchem.5b00612.
    • (2015) J Med Chem , vol.58 , Issue.19 , pp. 7719-7733
    • Weigel, L.F.1    Nitsche, C.2    Graf, D.3
  • 72
    • 84864957319 scopus 로고    scopus 로고
    • Critical effect of peptide cyclization on the potency of peptide inhibitors against dengue virus NS2B-NS3 protease
    • Xu S, Li H, Shao X, et al. Critical effect of peptide cyclization on the potency of peptide inhibitors against dengue virus NS2B-NS3 protease. J Med Chem. 2012;55(15):6881-6887. doi:10.1021/jm300655h.
    • (2012) J Med Chem , vol.55 , Issue.15 , pp. 6881-6887
    • Xu, S.1    Li, H.2    Shao, X.3
  • 73
    • 84873604286 scopus 로고    scopus 로고
    • Antiviral resistance and the future landscape of hepatitis C virus infection therapy
    • Wyles DL. Antiviral resistance and the future landscape of hepatitis C virus infection therapy. J Infect Dis. 2013;207(Suppl 1):S33-9. doi:10.1093/infdis/jis761.
    • (2013) J Infect Dis , vol.207 , pp. S33-S39
    • Wyles, D.L.1
  • 74
    • 84878175594 scopus 로고    scopus 로고
    • Design and evaluation of substrate-based octapeptide and non substrate-based tetrapeptide inhibitors of dengue virus NS2B-NS3 proteases
    • Prusis P, Junaid M, Petrovska R, et al. Design and evaluation of substrate-based octapeptide and non substrate-based tetrapeptide inhibitors of dengue virus NS2B-NS3 proteases. Biochem Biophys Res Commun. 2013;434(4):767-772. doi:10.1016/j. bbrc.2013.03.139.
    • (2013) Biochem Biophys Res Commun , vol.434 , Issue.4 , pp. 767-772
    • Prusis, P.1    Junaid, M.2    Petrovska, R.3
  • 75
    • 84890813052 scopus 로고    scopus 로고
    • Allosteric inhibition of the NS2BNS3 protease from dengue virus
    • Yildiz M, Ghosh S, Bell JA, et al. Allosteric inhibition of the NS2BNS3 protease from dengue virus. ACS Chem Biol. 2013;8(12):2744-2752. doi:10.1021/cb400612h.
    • (2013) ACS Chem Biol , vol.8 , Issue.12 , pp. 2744-2752
    • Yildiz, M.1    Ghosh, S.2    Bell, J.A.3
  • 76
    • 84878367059 scopus 로고    scopus 로고
    • Synthesis and in vitro evaluation of West Nile virus protease inhibitors based on the 2-{6-[2-(5-Phenyl-4H- {1,2,4]triazol-3-ylsulfanyl)acetylamino]benzothiazol-2-ylsulfanyl} acetamide scaffold
    • Samanta S, Lim TL, Lam Y. Synthesis and in vitro evaluation of West Nile virus protease inhibitors based on the 2-{6-[2-(5-Phenyl-4H- {1,2,4]triazol-3-ylsulfanyl)acetylamino]benzothiazol-2-ylsulfanyl} acetamide scaffold. ChemMedChem. 2013;8(6):994-1001. doi:10.1002/cmdc.201300114.
    • (2013) Chem Med Chem , vol.8 , Issue.6 , pp. 994-1001
    • Samanta, S.1    Lim, T.L.2    Lam, Y.3
  • 77
    • 84924156322 scopus 로고    scopus 로고
    • A small molecule inhibitor of dengue virus type 2 protease inhibits the replication of all four dengue virus serotypes in cell culture
    • Raut R, Beesetti H, Tyagi P, et al. A small molecule inhibitor of dengue virus type 2 protease inhibits the replication of all four dengue virus serotypes in cell culture. Virol J. 2015;12:16. doi:10.1186/s12985-015-0248-x.
    • (2015) Virol J , vol.12 , pp. 16
    • Raut, R.1    Beesetti, H.2    Tyagi, P.3
  • 78
    • 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
    • Lescar J, Luo D, Xu T, et al. Towards the design of antiviral inhibitors against flaviviruses: the case for the multifunctional NS3 protein from dengue virus as a target. Antiviral Res. 2008;80(2):94-101. doi:10.1016/j.antiviral.2008.07.001.
    • (2008) Antiviral Res , vol.80 , Issue.2 , pp. 94-101
    • Lescar, J.1    Luo, D.2    Xu, T.3
  • 79
    • 23244450531 scopus 로고    scopus 로고
    • Structure of the flavivirus helicase: Implications for catalytic activity, protein interactions, and proteolytic processing
    • Wu J, Bera AK, Kuhn RJ, et al. Structure of the flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing. J Virol. 2005;79(16):10268-10277. doi:10.1128/ JVI.79.16.10268-10277.2005.
    • (2005) J Virol , vol.79 , Issue.16 , pp. 10268-10277
    • Wu, J.1    Bera, A.K.2    Kuhn, R.J.3
  • 80
    • 0027366948 scopus 로고
    • The NS 3 nonstructural protein of flaviviruses contains an RNA triphosphatase activity
    • Wengler G, Wengler G. The NS 3 nonstructural protein of flaviviruses contains an RNA triphosphatase activity. Virology. 1993;197 (1):265-273. doi:10.1006/viro.1993.1587.
    • (1993) Virology , vol.197 , Issue.1 , pp. 265-273
    • Wengler, G.1    Wengler, G.2
  • 81
    • 0034802008 scopus 로고    scopus 로고
    • Mutagenesis of the dengue virus type 2 NS3 protein within and outside helicase motifs: Effects on enzyme activity and virus replication
    • Matusan AE, Pryor MJ, Davidson AD, et al. Mutagenesis of the dengue virus type 2 NS3 protein within and outside helicase motifs: effects on enzyme activity and virus replication. J Virol. 2001;75(20):9633-9643. doi:10.1128/JVI.75.20.9633-9643.2001.
    • (2001) J Virol , vol.75 , Issue.20 , pp. 9633-9643
    • Matusan, A.E.1    Pryor, M.J.2    Davidson, A.D.3
  • 82
    • 84880836962 scopus 로고    scopus 로고
    • Discovering new medicines targeting helicases: Challenges and recent progress
    • Shadrick WR, Ndjomou J, Kolli R, et al. Discovering new medicines targeting helicases: challenges and recent progress. J Biomol Screen. 2013;18(7):761-781. doi:10.1177/1087057113482586.
    • (2013) J Biomol Screen , vol.18 , Issue.7 , pp. 761-781
    • Shadrick, W.R.1    Ndjomou, J.2    Kolli, R.3
  • 83
    • 84864523421 scopus 로고    scopus 로고
    • Ivermectin is a potent inhibitor of flavivirus replication specifically targeting NS3 helicase activity: New prospects for an old drug
    • Mastrangelo E, Pezzullo M, De Burghgraeve T, et al. Ivermectin is a potent inhibitor of flavivirus replication specifically targeting NS3 helicase activity: new prospects for an old drug. J Antimicrob Chemother. 2012;67(8):1884-1894. doi:10.1093/jac/dks147.
    • (2012) J Antimicrob Chemother , vol.67 , Issue.8 , pp. 1884-1894
    • Mastrangelo, E.1    Pezzullo, M.2    De Burghgraeve, T.3
  • 84
    • 84856093723 scopus 로고    scopus 로고
    • Use of parallel validation highthroughput screens to reduce false positives and identify novel dengue NS2B-NS3 protease inhibitors
    • Tomlinson SM, Watowich SJ. Use of parallel validation highthroughput screens to reduce false positives and identify novel dengue NS2B-NS3 protease inhibitors. Antiviral Res. 2012;93 (2):245-252. doi:10.1016/j.antiviral.2011.12.003.
    • (2012) Antiviral Res , vol.93 , Issue.2 , pp. 245-252
    • Tomlinson, S.M.1    Watowich, S.J.2
  • 85
    • 84875173228 scopus 로고    scopus 로고
    • Novel benzoxazole inhibitor of dengue virus replication that targets the NS3 helicase
    • Byrd CM, Grosenbach DW, Berhanu A, et al. Novel benzoxazole inhibitor of dengue virus replication that targets the NS3 helicase. Antimicrob Agents Chemother. 2013;57(4):1902-1912. doi:10.1128/ AAC.02251-12.
    • (2013) Antimicrob Agents Chemother , vol.57 , Issue.4 , pp. 1902-1912
    • Byrd, C.M.1    Grosenbach, D.W.2    Berhanu, A.3
  • 86
    • 77958487269 scopus 로고    scopus 로고
    • Update on new antivirals under development for the treatment of double-stranded DNA virus infections
    • Dropulic LK, Cohen JI. Update on new antivirals under development for the treatment of double-stranded DNA virus infections. Clin Pharmacol Ther. 2010;88(5):610-619. doi:10.1038/ clpt.2010.178.
    • (2010) Clin Pharmacol Ther , vol.88 , Issue.5 , pp. 610-619
    • Dropulic, L.K.1    Cohen, J.I.2
  • 87
    • 84918509852 scopus 로고    scopus 로고
    • Suramin inhibits helicase activity of NS3 protein of dengue virus in a fluorescence-based high throughput assay format
    • Basavannacharya C, Vasudevan SG. Suramin inhibits helicase activity of NS3 protein of dengue virus in a fluorescence-based high throughput assay format. Biochem Biophys Res Commun. 2014;453 (3):539-544. doi:10.1016/j.bbrc.2014.09.113.
    • (2014) Biochem Biophys Res Commun , vol.453 , Issue.3 , pp. 539-544
    • Basavannacharya, C.1    Vasudevan, S.G.2
  • 88
    • 84969213558 scopus 로고    scopus 로고
    • Benzothiazole and pyrrolone flavivirus inhibitors targeting the viral helicase
    • Sweeney NL, Hanson AM, Mukherjee S, et al. Benzothiazole and pyrrolone flavivirus inhibitors targeting the viral helicase. ACS Infect Dis. 2015;1(3):140-148. doi:10.1021/id5000458.
    • (2015) ACS Infect Dis , vol.1 , Issue.3 , pp. 140-148
    • Sweeney, N.L.1    Hanson, A.M.2    Mukherjee, S.3
  • 89
    • 0025743809 scopus 로고
    • The phylogeny of RNA-dependent RNA polymerases of positive-strand RNA viruses
    • Koonin EV. The phylogeny of RNA-dependent RNA polymerases of positive-strand RNA viruses. J Gen Virol. 1991;72(9):2197-2206. doi:10.1099/0022-1317-72-9-2197.
    • (1991) J Gen Virol , vol.72 , Issue.9 , pp. 2197-2206
    • Koonin, E.V.1
  • 90
    • 0027474037 scopus 로고
    • Computer-assisted identification of a putative methyltransferase domain in NS5 protein of flaviviruses and λ2 protein of reovirus
    • Koonin EV. Computer-assisted identification of a putative methyltransferase domain in NS5 protein of flaviviruses and λ2 protein of reovirus. J Gen Virol. 1993;74(4):733-740. doi:10.1099/0022-1317- 74-4-733.
    • (1993) J Gen Virol , vol.74 , Issue.4 , pp. 733-740
    • Koonin, E.V.1
  • 91
    • 77955657482 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of dengue virus methyltransferase
    • Dong H, Chang DC, Xie X, et al. Biochemical and genetic characterization of dengue virus methyltransferase. Virology. 2010;405 (2):568-578. doi:10.1016/j.virol.2010.06.039.
    • (2010) Virology , vol.405 , Issue.2 , pp. 568-578
    • Dong, H.1    Chang, D.C.2    Xie, X.3
  • 92
    • 84883398813 scopus 로고    scopus 로고
    • Rational design of a live attenuated dengue vaccine: 2'-O-methyltransferase mutants are highly attenuated and immunogenic in mice and macaques
    • Züst R, Dong H, Li X-F, et al. Rational design of a live attenuated dengue vaccine: 2'-O-methyltransferase mutants are highly attenuated and immunogenic in mice and macaques. PLoS Pathog. 2013;9(8):e1003521. doi:10.1371/journal.ppat.1003521.
    • (2013) PLoS Pathog , vol.9 , Issue.8
    • Züst, R.1    Dong, H.2    Li, X.-F.3
  • 93
    • 79953188722 scopus 로고    scopus 로고
    • Small molecule inhibitors that selectively block dengue virus methyltransferase
    • Lim SP, Sonntag LS, Noble C, et al. Small molecule inhibitors that selectively block dengue virus methyltransferase. J Biol Chem. 2011;286(8):6233-6240. doi:10.1074/jbc.M110.179184.
    • (2011) J Biol Chem , vol.286 , Issue.8 , pp. 6233-6240
    • Lim, S.P.1    Sonntag, L.S.2    Noble, C.3
  • 94
    • 84907485267 scopus 로고    scopus 로고
    • Crystal structure of dengue virus methyltransferase without S-adenosyl-L-methionine
    • Noble CG, Li S-H, Dong H, et al. Crystal structure of dengue virus methyltransferase without S-adenosyl-L-methionine. Antiviral Res. 2014;111:78-81. doi:10.1016/j.antiviral.2014.09.003.
    • (2014) Antiviral Res , vol.111 , pp. 78-81
    • Noble, C.G.1    Li, S.-H.2    Dong, H.3
  • 95
    • 84928894975 scopus 로고    scopus 로고
    • Refolding of a fully functional flavivirus methyltransferase revealed that S-adenosyl methionine but not S-adenosyl homocysteine is copurified with flavivirus methyltransferase
    • Brecher MB, Li Z, Zhang J, et al. Refolding of a fully functional flavivirus methyltransferase revealed that S-adenosyl methionine but not S-adenosyl homocysteine is copurified with flavivirus methyltransferase. Protein Sci. 2015;24(1):117-128. doi:10.1002/ pro.2594.
    • (2015) Protein Sci , vol.24 , Issue.1 , pp. 117-128
    • Brecher, M.B.1    Li, Z.2    Zhang, J.3
  • 96
    • 84969271146 scopus 로고    scopus 로고
    • Identification and characterization of novel broad-spectrum inhibitors of the flavivirus methyltransferase
    • Brecher M, Chen H, Li Z, et al. Identification and characterization of novel broad-spectrum inhibitors of the flavivirus methyltransferase. ACS Infect Dis. 2015;1(8):340-349. doi:10.1021/acsinfecdis.5b00070.
    • (2015) ACS Infect Dis , vol.1 , Issue.8 , pp. 340-349
    • Brecher, M.1    Chen, H.2    Li, Z.3
  • 97
    • 84926429155 scopus 로고    scopus 로고
    • A crystal structure of the dengue virus NS5 protein reveals a novel inter-domain interface essential for protein flexibility and virus replication
    • Zhao Y, Soh TS, Zheng J, et al. A crystal structure of the dengue virus NS5 protein reveals a novel inter-domain interface essential for protein flexibility and virus replication. PLoS Pathog. 2015;11(3): e1004682. doi:10.1371/journal.ppat.1004682.
    • (2015) PLoS Pathog , vol.11 , Issue.3
    • Zhao, Y.1    Soh, T.S.2    Zheng, J.3
  • 98
    • 77957764872 scopus 로고    scopus 로고
    • Structural and functional analyses of a conserved hydrophobic pocket of flavivirus methyltransferase
    • Dong H, Liu L, Zou G, et al. Structural and functional analyses of a conserved hydrophobic pocket of flavivirus methyltransferase. J Biol Chem. 2010;285(42):32586-32595. doi:10.1074/jbc.M110.129197.
    • (2010) J Biol Chem , vol.285 , Issue.42 , pp. 32586-32595
    • Dong, H.1    Liu, L.2    Zou, G.3
  • 99
    • 85040379681 scopus 로고    scopus 로고
    • Active site specific pharmacophore-based screening for methyltransferase inhibitors
    • Tamilvanan T, Hopper W. Active site specific pharmacophore-based screening for methyltransferase inhibitors. J Pharm Res. 2013;7 (1):121-126. doi:10.1016/j.jopr.2013.01.016.
    • (2013) J Pharm Res , vol.7 , Issue.1 , pp. 121-126
    • Tamilvanan, T.1    Hopper, W.2
  • 100
    • 84901012308 scopus 로고    scopus 로고
    • Assessment of dengue virus helicase and methyltransferase as targets for fragment-based drug discovery
    • Coutard B, Decroly E, Li C, et al. Assessment of dengue virus helicase and methyltransferase as targets for fragment-based drug discovery. Antiviral Res. 2014;106:61-70. doi:10.1016/j. antiviral.2014.03.013.
    • (2014) Antiviral Res , vol.106 , pp. 61-70
    • Coutard, B.1    Decroly, E.2    Li, C.3
  • 101
    • 84948670351 scopus 로고    scopus 로고
    • Molecular basis for specific viral RNA recognition and 2'-O-ribose methylation by the dengue virus nonstructural protein 5 (NS5)
    • Zhao Y, Soh TS, Lim SP, et al. Molecular basis for specific viral RNA recognition and 2'-O-ribose methylation by the dengue virus nonstructural protein 5 (NS5). Proc Natl Acad Sci U S A. 2015;112 (48):14834-14839. doi:10.1073/pnas.1514978112.
    • (2015) Proc Natl Acad Sci U S A , vol.112 , Issue.48 , pp. 14834-14839
    • Zhao, Y.1    Soh, T.S.2    Lim, S.P.3
  • 102
    • 80054773940 scopus 로고    scopus 로고
    • A high-throughput screening assay for the identification of flavivirus NS5 capping enzyme GTPbinding inhibitors: Implications for antiviral drug development
    • Geiss BJ, Stahla-Beek HJ, Hannah AM, et al. A high-throughput screening assay for the identification of flavivirus NS5 capping enzyme GTPbinding inhibitors: implications for antiviral drug development. J Biomol Screen. 2011;16(8):852-861. doi:10.1177/1087057111412183.
    • (2011) J Biomol Screen , vol.16 , Issue.8 , pp. 852-861
    • Geiss, B.J.1    Stahla-Beek, H.J.2    Hannah, A.M.3
  • 103
    • 56349149403 scopus 로고    scopus 로고
    • A scintillation proximity assay for dengue virus NS5 2'-O-methyltransferase-kinetic and inhibition analyses
    • Lim SP, Wen D, Yap TL, et al. A scintillation proximity assay for dengue virus NS5 2'-O-methyltransferase-kinetic and inhibition analyses. Antiviral Res. 2008;80(3):360-369. doi:10.1016/j. antiviral.2008.08.005.
    • (2008) Antiviral Res , vol.80 , Issue.3 , pp. 360-369
    • Lim, S.P.1    Wen, D.2    Yap, T.L.3
  • 104
    • 84884537505 scopus 로고    scopus 로고
    • Development of specific dengue virus 2'-O- and N7-methyltransferase assays for antiviral drug screening
    • Barral K, Sallamand C, Petzold C, et al. Development of specific dengue virus 2'-O- and N7-methyltransferase assays for antiviral drug screening. Antiviral Res. 2013;99(3):292-300. doi:10.1016/j. antiviral.2013.06.001.
    • (2013) Antiviral Res , vol.99 , Issue.3 , pp. 292-300
    • Barral, K.1    Sallamand, C.2    Petzold, C.3
  • 105
    • 84905584515 scopus 로고    scopus 로고
    • Aptamer displacement screen for flaviviral RNA methyltransferase inhibitors
    • Falk SP, Weisblum B. Aptamer displacement screen for flaviviral RNA methyltransferase inhibitors. J Biomol Screen. 2014;19 (8):1147-1153. doi:10.1177/1087057114533147.
    • (2014) J Biomol Screen , vol.19 , Issue.8 , pp. 1147-1153
    • Falk, S.P.1    Weisblum, B.2
  • 106
    • 84901767814 scopus 로고    scopus 로고
    • The interface between methyltransferase and polymerase of NS5 is essential for flavivirus replication
    • Li X-D, Shan C, Deng C-L, et al. The interface between methyltransferase and polymerase of NS5 is essential for flavivirus replication. PLoS Negl Trop Dis. 2014;8(5):e2891. doi:10.1371/journal. pntd.0002891.
    • (2014) PLoS Negl Trop Dis , vol.8 , Issue.5
    • Li, X.-D.1    Shan, C.2    Deng, C.-L.3
  • 107
    • 84883381606 scopus 로고    scopus 로고
    • Crystal structure of the full-length Japanese encephalitis virus NS5 reveals a conserved methyltransferase-polymerase interface
    • Lu G, Gong P. Crystal structure of the full-length japanese encephalitis virus NS5 reveals a conserved methyltransferase-polymerase interface. PLoS Pathog. 2013;9(8):e1003549. doi:10.1371/ journal.ppat.1003549.
    • (2013) PLoS Pathog , vol.9 , Issue.8
    • Lu, G.1    Gong, P.2
  • 108
    • 84919451239 scopus 로고    scopus 로고
    • Perturbation in the conserved methyltransferase- polymerase interface of flavivirus NS5 differentially affects polymerase initiation and elongation
    • Wu J, Lu G, Zhang B, et al. Perturbation in the conserved methyltransferase- polymerase interface of flavivirus NS5 differentially affects polymerase initiation and elongation. J Virol. 2015;89 (1):249-261. doi:10.1128/JVI.02085-14.
    • (2015) J Virol , vol.89 , Issue.1 , pp. 249-261
    • Wu, J.1    Lu, G.2    Zhang, B.3
  • 109
    • 84877315512 scopus 로고    scopus 로고
    • Rational design of a flavivirus vaccine by abolishing viral RNA 2'-O methylation
    • Li S-H, Dong H, Li X-F, et al. Rational design of a flavivirus vaccine by abolishing viral RNA 2'-O methylation. J Virol. 2013;87(10):5812-5819. doi:10.1128/JVI.02806-12.
    • (2013) J Virol , vol.87 , Issue.10 , pp. 5812-5819
    • Li, S.-H.1    Dong, H.2    Li, X.-F.3
  • 110
    • 61549128714 scopus 로고    scopus 로고
    • Antiviral agents acting as DNA or RNA chain terminators
    • In: Kräusslich H-G, Bartenschlager R, editors., Berlin: Springer;
    • De Clercq E, Neyts J. Antiviral agents acting as DNA or RNA chain terminators. In: Kräusslich H-G, Bartenschlager R, editors. Antiviral strategies. Berlin: Springer; 2009. p. 53-84.
    • (2009) Antiviral Strategies , pp. 53-84
    • De Clercq, E.1    Neyts, J.2
  • 111
    • 84963654655 scopus 로고    scopus 로고
    • Hepatitis C Online 2015 [cited 2015 Dec 14];
    • Sofosbuvir (Sovaldi). Hepatitis C Online 2015 [cited 2015 Dec 14]; Available from: http://www.hepatitisc.uw.edu/page/treatment/ drugs/sofosbuvir-drug
    • Sofosbuvir (Sovaldi)
  • 112
    • 84878233812 scopus 로고    scopus 로고
    • In search of flavivirus inhibitors: Evaluation of different tritylated nucleoside analogues
    • Chatelain G, Debing Y, De Burghgraeve T, et al. In search of flavivirus inhibitors: Evaluation of different tritylated nucleoside analogues. Eur J Med Chem. 2013;65:249-255. doi:10.1016/j. ejmech.2013.04.034.
    • (2013) Eur J Med Chem , vol.65 , pp. 249-255
    • Chatelain, G.1    Debing, Y.2    De Burghgraeve, T.3
  • 113
    • 84896874457 scopus 로고    scopus 로고
    • In search of Flavivirus inhibitors part 2: Tritylated, diphenylmethylated and other alkylated nucleoside analogues
    • Saudi M, Zmurko J, Kaptein S, et al. In search of Flavivirus inhibitors part 2: tritylated, diphenylmethylated and other alkylated nucleoside analogues. Eur J Med Chem. 2014;76:98-109. doi:10.1016/j. ejmech.2014.02.011.
    • (2014) Eur J Med Chem , vol.76 , pp. 98-109
    • Saudi, M.1    Zmurko, J.2    Kaptein, S.3
  • 114
    • 84875981242 scopus 로고    scopus 로고
    • 3',5'Di-O-trityluridine inhibits in vitro flavivirus replication
    • De Burghgraeve T, Selisko B, Kaptein S, et al. 3',5'Di-O-trityluridine inhibits in vitro flavivirus replication. Antiviral Res. 2013;98(2):242-247. doi:10.1016/j.antiviral.2013.01.011.
    • (2013) Antiviral Res , vol.98 , Issue.2 , pp. 242-247
    • De Burghgraeve, T.1    Selisko, B.2    Kaptein, S.3
  • 115
    • 84940952926 scopus 로고    scopus 로고
    • Nucleoside inhibitors of tick-borne encephalitis virus
    • Eyer L, Valdés JJ, Gil VA, et al. Nucleoside inhibitors of tick-borne encephalitis virus. Antimicrob Agents Chemother. 2015;59(9):5483-5493. doi:10.1128/AAC.00807-15.
    • (2015) Antimicrob Agents Chemother , vol.59 , Issue.9 , pp. 5483-5493
    • Eyer, L.1    Valdés, J.J.2    Gil, V.A.3
  • 116
    • 73949141554 scopus 로고    scopus 로고
    • An adenosine nucleoside inhibitor of dengue virus
    • Yin Z, Chen Y-L, Schul W, et al. An adenosine nucleoside inhibitor of dengue virus. Proc Natl Acad Sci U S A. 2009;106(48):20435-20439. doi:10.1073/pnas.0907010106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.48 , pp. 20435-20439
    • Yin, Z.1    Chen, Y.-L.2    Schul, W.3
  • 117
    • 11844257006 scopus 로고    scopus 로고
    • Cell entry and export of nucleoside analogues
    • Pastor-Anglada M, Cano-Soldado P, Molina-Arcas M, et al. Cell entry and export of nucleoside analogues. Virus Res. 2005;107(2):151-164. doi:10.1016/j.virusres.2004.11.005.
    • (2005) Virus Res , vol.107 , Issue.2 , pp. 151-164
    • Pastor-Anglada, M.1    Cano-Soldado, P.2    Molina-Arcas, M.3
  • 118
    • 77955363550 scopus 로고    scopus 로고
    • Inhibition of dengue virus by an ester prodrug of an adenosine analog
    • Chen Y-L, Yin Z, Lakshminarayana SB, et al. Inhibition of dengue virus by an ester prodrug of an adenosine analog. Antimicrob Agents Chemother. 2010;54(8):3255-3261. doi:10.1128/AAC.00397-10.
    • (2010) Antimicrob Agents Chemother , vol.54 , Issue.8 , pp. 3255-3261
    • Chen, Y.-L.1    Yin, Z.2    Lakshminarayana, S.B.3
  • 119
    • 33645232568 scopus 로고    scopus 로고
    • The novel nucleoside analog R1479 (4'-Azidocytidine) is a potent inhibitor of NS5Bdependent RNA synthesis and hepatitis C virus replication in cell culture
    • Klumpp K, Lévêque V, Le Pogam S, et al. The novel nucleoside analog R1479 (4'-Azidocytidine) is a potent inhibitor of NS5Bdependent RNA synthesis and hepatitis C virus replication in cell culture. J Biol Chem. 2006;281(7):3793-3799. doi:10.1074/jbc. M510195200.
    • (2006) J Biol Chem , vol.281 , Issue.7 , pp. 3793-3799
    • Klumpp, K.1    Lévêque, V.2    Le Pogam, S.3
  • 120
    • 84875997317 scopus 로고    scopus 로고
    • A randomized, double-blind placebo controlled trial of balapiravir, a polymerase inhibitor, in adult dengue patients
    • Nguyen NM, Tran CNB, Phung LK, et al. A randomized, double-blind placebo controlled trial of balapiravir, a polymerase inhibitor, in adult dengue patients. J Infect Dis. 2013;207(9):1442-1450. doi:10.1093/infdis/jis470.
    • (2013) J Infect Dis , vol.207 , Issue.9 , pp. 1442-1450
    • Nguyen, N.M.1    Tran, C.N.B.2    Phung, L.K.3
  • 121
    • 0032585237 scopus 로고    scopus 로고
    • Randomised trial of interferon α2b plus ribavirin for 48 weeks or for 24 weeks versus interferon α2b plus placebo for 48 weeks for treatment of chronic infection with hepatitis C virus
    • Poynard T, Marcellin P, Lee SS, et al. Randomised trial of interferon α2b plus ribavirin for 48 weeks or for 24 weeks versus interferon α2b plus placebo for 48 weeks for treatment of chronic infection with hepatitis C virus. The Lancet. 1998;352(9138):1426-1432. doi:10.1016/S0140-6736(98)07124-4.
    • (1998) The Lancet , vol.352 , Issue.9138 , pp. 1426-1432
    • Poynard, T.1    Marcellin, P.2    Lee, S.S.3
  • 122
    • 27644499521 scopus 로고    scopus 로고
    • Broad-spectrum inhibitor of viruses in the flaviviridae family
    • Ojwang JO, Ali S, Smee DF, et al. Broad-spectrum inhibitor of viruses in the flaviviridae family. Antiviral Res. 2005;68(2):49-55. doi:10.1016/j.antiviral.2005.06.002.
    • (2005) Antiviral Res , vol.68 , Issue.2 , pp. 49-55
    • Ojwang, J.O.1    Ali, S.2    Smee, D.F.3
  • 123
    • 84938910333 scopus 로고    scopus 로고
    • Combined treatment of adenosine nucleoside inhibitor NITD008 and histone deacetylase inhibitor vorinostat represents an immunotherapy strategy to ameliorate West Nile virus infection
    • Nelson J, Roe K, Orillo B, et al. Combined treatment of adenosine nucleoside inhibitor NITD008 and histone deacetylase inhibitor vorinostat represents an immunotherapy strategy to ameliorate West Nile virus infection. Antiviral Res. 2015;122:39-45. doi:10.1016/j.antiviral.2015.07.008.
    • (2015) Antiviral Res , vol.122 , pp. 39-45
    • Nelson, J.1    Roe, K.2    Orillo, B.3
  • 124
    • 77954706293 scopus 로고    scopus 로고
    • Small molecule drug discovery for Dengue and West Nile viruses: Applying experience from hepatitis C virus
    • Parkinson T. Small molecule drug discovery for Dengue and West Nile viruses: applying experience from hepatitis C virus. Future Med Chem. 2010;2(7):1181-1203. doi:10.4155/fmc.10.195.
    • (2010) Future Med Chem , vol.2 , Issue.7 , pp. 1181-1203
    • Parkinson, T.1
  • 125
    • 10344248922 scopus 로고    scopus 로고
    • Enzymatic characterization and homology model of a catalytically active recombinant West Nile virus NS3 protease
    • Nall TA, Chappell KJ, Stoermer MJ, et al. Enzymatic characterization and homology model of a catalytically active recombinant West Nile virus NS3 protease. J Biol Chem. 2004;279(47):48535-48542. doi:10.1074/jbc.M406810200.
    • (2004) J Biol Chem , vol.279 , Issue.47 , pp. 48535-48542
    • Nall, T.A.1    Chappell, K.J.2    Stoermer, M.J.3
  • 126
    • 84951335929 scopus 로고    scopus 로고
    • Mouse models of dengue virus infection for vaccine testing
    • Sarathy VV, Milligan GN, Bourne N, et al. Mouse models of dengue virus infection for vaccine testing. Vaccine. 2015;33(50):7051-7060. doi:10.1016/j.vaccine.2015.09.112.
    • (2015) Vaccine , vol.33 , Issue.50 , pp. 7051-7060
    • Sarathy, V.V.1    Milligan, G.N.2    Bourne, N.3
  • 127
    • 84940396925 scopus 로고    scopus 로고
    • Animal models for studying dengue pathogenesis and therapy
    • Chan KWK, Watanabe S, Kavishna R, et al. Animal models for studying dengue pathogenesis and therapy. Antiviral Res. 2015;123:5-14. doi:10.1016/j.antiviral.2015.08.013.
    • (2015) Antiviral Res , vol.123 , pp. 5-14
    • Chan, K.W.K.1    Watanabe, S.2    Kavishna, R.3
  • 128
    • 84885567750 scopus 로고    scopus 로고
    • Ten years of dengue drug discovery: Progress and prospects
    • Lim SP, Wang Q-Y, Noble CG, et al. Ten years of dengue drug discovery: progress and prospects. Antiviral Res. 2013;100(2):500-519. doi:10.1016/j.antiviral.2013.09.013.
    • (2013) Antiviral Res , vol.100 , Issue.2 , pp. 500-519
    • Lim, S.P.1    Wang, Q.-Y.2    Noble, C.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.