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Volumn 82, Issue 1, 2013, Pages 1-11

Rational discovery of dengue type 2 non-competitive inhibitors

Author keywords

AutoDock virtual screening; DEN 2; Dengue virus type 2; NS2B NS3; Protease assay; Rational drug discovery; Small compounds

Indexed keywords

2 (2,3 DIHYDRO 1,4 BENZODIOXIN 6 YL) 3,4 DIHYDRO 2H 1 BENZOPYRAN 4 ONE; 2 [4 (DIMETHYLAMINO)PHENYL] 5,7 DIMETHYYL 3,4 DIHYDRO 2H 1 BENZOPYRAN 4 ONE; 2 PHENYL 6 (1H 1,2,3,4 TETRAZZOL 5 YL) 4H CHROMEN 4 ONE; 6 PHENYL 6A,12A DIHYDRO 6H,7H CHROMENO [4,3 B]CHROMENE; ANTIVIRUS AGENT; CARDAMONIN; FLAVANONE; NONSTRUCTURAL PROTEIN 2B NONSTRUCTURAL PROTEIN 3 PROTEASE; NONSTRUCTURAL PROTEIN 2B NONSTRUCTURAL PROTEIN 3 PROTEASE INHIBITOR; PINOSTROBIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84879541677     PISSN: 17470277     EISSN: 17470285     Source Type: Journal    
DOI: 10.1111/cbdd.12122     Document Type: Article
Times cited : (45)

References (51)
  • 1
    • 0031823546 scopus 로고    scopus 로고
    • Dengue and dengue hemorrhagic fever
    • Gubler D.J. (1998) Dengue and dengue hemorrhagic fever. Clin Microbiol Rev;11:480-496.
    • (1998) Clin Microbiol Rev , vol.11 , pp. 480-496
    • Gubler, D.J.1
  • 2
    • 18044367101 scopus 로고    scopus 로고
    • Dengue fever: new paradigms for a changing epidemiology
    • Guha-Sapir D., Schimmer B. (2005) Dengue fever: new paradigms for a changing epidemiology. Emerg Themes Epidemiol;2:1.
    • (2005) Emerg Themes Epidemiol , vol.2 , pp. 1
    • Guha-Sapir, D.1    Schimmer, B.2
  • 3
    • 77954942481 scopus 로고    scopus 로고
    • Design, structure-based focusing and in silico screening of combinatorial library of peptidomimetic inhibitors of dengue virus NS2B-NS3 protease
    • Frecer V., Miertus S. (2010) Design, structure-based focusing and in silico screening of combinatorial library of peptidomimetic inhibitors of dengue virus NS2B-NS3 protease. J Comput Aided Mol Des;24:195-212.
    • (2010) J Comput Aided Mol Des , vol.24 , pp. 195-212
    • Frecer, V.1    Miertus, S.2
  • 4
    • 79952268132 scopus 로고    scopus 로고
    • Design of new competitive dengue ns2b/ns3 protease inhibitors-a computational approach
    • Frimayanti N., Chee C.F., Zain S.M., Rahman N.A. (2011) Design of new competitive dengue ns2b/ns3 protease inhibitors-a computational approach. Int J Mol Sci;12:1089-1100.
    • (2011) Int J Mol Sci , vol.12 , pp. 1089-1100
    • Frimayanti, N.1    Chee, C.F.2    Zain, S.M.3    Rahman, N.A.4
  • 5
    • 23744446349 scopus 로고    scopus 로고
    • Peptide inhibitors of dengue virus and West Nile virus infectivity
    • Hrobowski Y.M., Garry R.F., Michael S.F. (2005) Peptide inhibitors of dengue virus and West Nile virus infectivity. Virol J;2:49.
    • (2005) Virol J , vol.2 , pp. 49
    • Hrobowski, Y.M.1    Garry, R.F.2    Michael, S.F.3
  • 6
    • 33646177244 scopus 로고    scopus 로고
    • Inhibitory activity of cyclohexenyl chalcone derivatives and flavonoids of fingerroot, Boesenbergia rotunda (L.), towards dengue-2 virus NS3 protease
    • Kiat T.S., Pippen R., Yusof R., Ibrahim H., Khalid N., Rahman N.A. (2006) Inhibitory activity of cyclohexenyl chalcone derivatives and flavonoids of fingerroot, Boesenbergia rotunda (L.), towards dengue-2 virus NS3 protease. Bioorg Med Chem Lett;16:3337-3340.
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 3337-3340
    • Kiat, T.S.1    Pippen, R.2    Yusof, R.3    Ibrahim, H.4    Khalid, N.5    Rahman, N.A.6
  • 7
    • 65449140627 scopus 로고    scopus 로고
    • Nonsubstrate based inhibitors of dengue virus serine protease: a molecular docking approach to study binding interactions between protease and inhibitors
    • Lee Y.K., Tan S.K., Habibah A.W., Rohana Y., Noorsaadah A.R. (2007) Nonsubstrate based inhibitors of dengue virus serine protease: a molecular docking approach to study binding interactions between protease and inhibitors. Asia Pac J Mol Biol Biotechnol;15:53-59.
    • (2007) Asia Pac J Mol Biol Biotechnol , vol.15 , pp. 53-59
    • Lee, Y.K.1    Tan, S.K.2    Habibah, A.W.3    Rohana, Y.4    Noorsaadah, A.R.5
  • 8
    • 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., Sampath A., Lim S.P., Canard B., Vasudevan S.G. (2008) Towards the design of antiviral inhibitors against flaviviruses: the case for the multifunctional NS3 protein from dengue virus as a target. Antiviral Res;80:94-101.
    • (2008) Antiviral Res , vol.80 , pp. 94-101
    • Lescar, J.1    Luo, D.2    Xu, T.3    Sampath, A.4    Lim, S.P.5    Canard, B.6    Vasudevan, S.G.7
  • 9
    • 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.J., Abbenante G., Martin J.L., Young P.R., Fairlie D.P. (2001) 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;276:45762-45771.
    • (2001) J Biol Chem , vol.276 , pp. 45762-45771
    • Leung, D.1    Schroder, K.2    White, H.3    Fang, N.X.4    Stoermer, M.J.5    Abbenante, G.6    Martin, J.L.7    Young, P.R.8    Fairlie, D.P.9
  • 10
    • 52049104700 scopus 로고    scopus 로고
    • Docking of noncompetitive inhibitors into dengue virus type 2 protease: understanding the interactions with allosteric binding sites
    • Othman R., Kiat T.S., Khalid N., Yusof R., Newhouse E.I., Newhouse J.S., Alam M., Rahman N.A. (2008) Docking of noncompetitive inhibitors into dengue virus type 2 protease: understanding the interactions with allosteric binding sites. J Chem Inf Model;48:1582-1591.
    • (2008) J Chem Inf Model , vol.48 , pp. 1582-1591
    • Othman, R.1    Kiat, T.S.2    Khalid, N.3    Yusof, R.4    Newhouse, E.I.5    Newhouse, J.S.6    Alam, M.7    Rahman, N.A.8
  • 14
    • 77953308454 scopus 로고    scopus 로고
    • Antiviral actions of flavanoid-derived compounds on dengue virus type-2
    • Muhamad M., Kee L.Y., Rahman N.A., Yusof R. (2010) Antiviral actions of flavanoid-derived compounds on dengue virus type-2. Int J Biol Sci;6:294-302.
    • (2010) Int J Biol Sci , vol.6 , pp. 294-302
    • Muhamad, M.1    Kee, L.Y.2    Rahman, N.A.3    Yusof, R.4
  • 16
    • 13944278364 scopus 로고    scopus 로고
    • rDEN4delta30, a live attenuated dengue virus type 4 vaccine candidate, is safe, immunogenic, and highly infectious in healthy adult volunteers
    • Durbin A.P., Whitehead S.S., McArthur J., Perreault J.R., Blaney J.E. Jr, Thumar B., Murphy B.R., Karron R.A. (2005) rDEN4delta30, a live attenuated dengue virus type 4 vaccine candidate, is safe, immunogenic, and highly infectious in healthy adult volunteers. J Infect Dis;191:710-718.
    • (2005) J Infect Dis , vol.191 , pp. 710-718
    • Durbin, A.P.1    Whitehead, S.S.2    McArthur, J.3    Perreault, J.R.4    Blaney Jr., J.E.5    Thumar, B.6    Murphy, B.R.7    Karron, R.A.8
  • 17
    • 34447134784 scopus 로고    scopus 로고
    • Dengue vaccines approach the finish line
    • Edelman R. (2007) Dengue vaccines approach the finish line. Clin Infect Dis;45(Suppl 1):S56-S60.
    • (2007) Clin Infect Dis , vol.45 , Issue.SUPPL. 1
    • Edelman, R.1
  • 18
    • 4043141495 scopus 로고    scopus 로고
    • Introduction of mutations into the non-structural genes or 3′ untranslated region of an attenuated dengue virus type 4 vaccine candidate further decreases replication in rhesus monkeys while retaining protective immunity
    • Hanley K.A., Manlucu L.R., Manipon G.G., Hanson C.T., Whitehead S.S., Murphy B.R., Blaney J.E. Jr. (2004) Introduction of mutations into the non-structural genes or 3′ untranslated region of an attenuated dengue virus type 4 vaccine candidate further decreases replication in rhesus monkeys while retaining protective immunity. Vaccines;22:3440-3448.
    • (2004) Vaccines , vol.22 , pp. 3440-3448
    • Hanley, K.A.1    Manlucu, L.R.2    Manipon, G.G.3    Hanson, C.T.4    Whitehead, S.S.5    Murphy, B.R.6    Blaney Jr., J.E.7
  • 20
    • 22244477049 scopus 로고    scopus 로고
    • An evaluation of dengue type-2 inactivated, recombinant subunit, and live-attenuated vaccine candidates in the rhesus macaque model
    • Robert Putnak J., Coller B.A., Voss G., Vaughn D.W., Clements D., Peters I., Bignami G. et al. (2005) An evaluation of dengue type-2 inactivated, recombinant subunit, and live-attenuated vaccine candidates in the rhesus macaque model. Vaccines;23:4442-4452.
    • (2005) Vaccines , vol.23 , pp. 4442-4452
    • Robert Putnak, J.1    Coller, B.A.2    Voss, G.3    Vaughn, D.W.4    Clements, D.5    Peters, I.6    Bignami, G.7
  • 21
    • 0037223896 scopus 로고    scopus 로고
    • A live, attenuated dengue virus type 1 vaccine candidate with a 30-nucleotide deletion in the 3′ untranslated region is highly attenuated and immunogenic in monkeys
    • Whitehead S.S., Falgout B., Hanley K.A., Blaney J.E. Jr, Markoff L., Murphy B.R. (2003) A live, attenuated dengue virus type 1 vaccine candidate with a 30-nucleotide deletion in the 3′ untranslated region is highly attenuated and immunogenic in monkeys. J Virol;77:1653-1657.
    • (2003) J Virol , vol.77 , pp. 1653-1657
    • Whitehead, S.S.1    Falgout, B.2    Hanley, K.A.3    Blaney Jr., J.E.4    Markoff, L.5    Murphy, B.R.6
  • 22
    • 0014311222 scopus 로고
    • An insular outbreak of dengue hemorrhagic fever. 3. Identification of vectors and observations on vector ecology
    • Gould D.J., Yuill T.M., Moussa M.A., Simasathien P., Rutledge L.C. (1968) An insular outbreak of dengue hemorrhagic fever. 3. Identification of vectors and observations on vector ecology. Am J Trop Med Hyg;17:609-618.
    • (1968) Am J Trop Med Hyg , vol.17 , pp. 609-618
    • Gould, D.J.1    Yuill, T.M.2    Moussa, M.A.3    Simasathien, P.4    Rutledge, L.C.5
  • 23
    • 0001401744 scopus 로고
    • Viruses associated with epidemic hemorrhagic fevers of the Philippines and Thailand
    • Hammon W.M., Rudnick A., Sather G.E. (1960) Viruses associated with epidemic hemorrhagic fevers of the Philippines and Thailand. Science;131:1102-1103.
    • (1960) Science , vol.131 , pp. 1102-1103
    • Hammon, W.M.1    Rudnick, A.2    Sather, G.E.3
  • 26
    • 0024603620 scopus 로고
    • Sequence analysis of cloned dengue virus type 2 genome (New Guinea-C strain)
    • Irie K., Mohan P.M., Sasaguri Y., Putnak R., Padmanabhan R. (1989) Sequence analysis of cloned dengue virus type 2 genome (New Guinea-C strain). Gene;75:197-211.
    • (1989) Gene , vol.75 , pp. 197-211
    • Irie, K.1    Mohan, P.M.2    Sasaguri, Y.3    Putnak, R.4    Padmanabhan, R.5
  • 27
    • 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 Y.M., Lai C.J. (1991) Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins. J Virol;65:2467-2475.
    • (1991) J Virol , vol.65 , pp. 2467-2475
    • Falgout, B.1    Pethel, M.2    Zhang, Y.M.3    Lai, C.J.4
  • 29
    • 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., Padmanabhan R. (2000) 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;275:9963-9969.
    • (2000) J Biol Chem , vol.275 , pp. 9963-9969
    • Yusof, R.1    Clum, S.2    Wetzel, M.3    Murthy, H.M.4    Padmanabhan, R.5
  • 30
    • 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., Rice C.M. (1990) 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 USA;87:8898-8902.
    • (1990) Proc Natl Acad Sci USA , vol.87 , 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
  • 31
    • 0027248585 scopus 로고
    • Role of protein conformation in the processing of dengue virus type 2 nonstructural polyprotein precursor
    • Zhang L., Padmanabhan R. (1993) Role of protein conformation in the processing of dengue virus type 2 nonstructural polyprotein precursor. Gene;129:197-205.
    • (1993) Gene , vol.129 , pp. 197-205
    • Zhang, L.1    Padmanabhan, R.2
  • 32
    • 34748873170 scopus 로고    scopus 로고
    • Flaviviridae: the viruses and their replication
    • Knipe D.M., Howley P.M., editors., 5th edn. Philadelphia: Lippincott-Raven Publishers
    • Lindenbach B.D., Thiel H.J., Rice C.M. (2007) Flaviviridae: the viruses and their replication. In: Knipe D.M., Howley P.M., editors. Fields Virology, 5th edn. Philadelphia: Lippincott-Raven Publishers; p. 1101-1152.
    • (2007) Fields Virology , pp. 1101-1152
    • Lindenbach, B.D.1    Thiel, H.J.2    Rice, C.M.3
  • 34
    • 34247625945 scopus 로고    scopus 로고
    • Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold
    • Aleshin A.E., Shiryaev S.A., Strongin A.Y., Liddington R.C. (2007) Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold. Protein Sci;16:795-806.
    • (2007) Protein Sci , vol.16 , pp. 795-806
    • Aleshin, A.E.1    Shiryaev, S.A.2    Strongin, A.Y.3    Liddington, R.C.4
  • 35
    • 58649113845 scopus 로고    scopus 로고
    • Structure of West Nile virus NS3 protease: ligand stabilization of the catalytic conformation
    • Robin G., Chappell K., Stoermer M.J., Hu S.H., Young P.R., Fairlie D.P., Martin J.L. (2009) Structure of West Nile virus NS3 protease: ligand stabilization of the catalytic conformation. J Mol Biol;385:1568-1577.
    • (2009) J Mol Biol , vol.385 , pp. 1568-1577
    • Robin, G.1    Chappell, K.2    Stoermer, M.J.3    Hu, S.H.4    Young, P.R.5    Fairlie, D.P.6    Martin, J.L.7
  • 36
    • 77649114480 scopus 로고    scopus 로고
    • Serotype-specific structural differences in the protease-cofactor complexes of the dengue virus family
    • Chandramouli S., Joseph J.S., Daudenarde S., Gatchalian J., Cornillez-Ty C., Kuhn P. (2010) Serotype-specific structural differences in the protease-cofactor complexes of the dengue virus family. J Virol;84:3059-3067.
    • (2010) J Virol , vol.84 , pp. 3059-3067
    • Chandramouli, S.1    Joseph, J.S.2    Daudenarde, S.3    Gatchalian, J.4    Cornillez-Ty, C.5    Kuhn, P.6
  • 37
    • 84855921187 scopus 로고    scopus 로고
    • Ligand-bound structures of the dengue virus protease reveal the active conformation
    • Noble C.G., Seh C.C., Chao A.T., Shi P.Y. (2012) Ligand-bound structures of the dengue virus protease reveal the active conformation. J Virol;86:438-446.
    • (2012) J Virol , vol.86 , pp. 438-446
    • Noble, C.G.1    Seh, C.C.2    Chao, A.T.3    Shi, P.Y.4
  • 39
    • 34247522323 scopus 로고    scopus 로고
    • A revisit into the DEN2 NS2B/NS3 Virus Protease Homology Model: structural verification and comparison with crystal structure of HCV NS3/4A and DEN2 NS3
    • Lee Y.K., Rozana O., Habibah A.W., Rohana Y., Noorsaadah A.R. (2006) A revisit into the DEN2 NS2B/NS3 Virus Protease Homology Model: structural verification and comparison with crystal structure of HCV NS3/4A and DEN2 NS3. Malays J Sci;25:15-22.
    • (2006) Malays J Sci , vol.25 , pp. 15-22
    • Lee, Y.K.1    Rozana, O.2    Habibah, A.W.3    Rohana, Y.4    Noorsaadah, A.R.5
  • 40
    • 77950675654 scopus 로고    scopus 로고
    • Homology modeling and molecular dynamics simulations of dengue virus NS2B/NS3 protease: insight into molecular interaction
    • Wichapong K., Pianwanit S., Sippl W., Kokpol S. (2010) Homology modeling and molecular dynamics simulations of dengue virus NS2B/NS3 protease: insight into molecular interaction. J Mol Recognit;23:283-300.
    • (2010) J Mol Recognit , vol.23 , pp. 283-300
    • Wichapong, K.1    Pianwanit, S.2    Sippl, W.3    Kokpol, S.4
  • 41
    • 33947716119 scopus 로고    scopus 로고
    • A semiempirical free energy force field with charge-based desolvation
    • Huey R., Morris G.M., Olson A.J., Goodsell D.S. (2007) A semiempirical free energy force field with charge-based desolvation. J Comput Chem;28:1145-1152.
    • (2007) J Comput Chem , vol.28 , pp. 1145-1152
    • Huey, R.1    Morris, G.M.2    Olson, A.J.3    Goodsell, D.S.4
  • 42
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris G.M., Goodsell D.S., Halliday R.S., Huey R., Hart W.E., Belew R.K., Olson A.J. (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J Comput Chem;19:1639-1662.
    • (1998) J Comput Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 44
    • 13844312649 scopus 로고    scopus 로고
    • ZINC-a free database of commercially available compounds for virtual screening
    • Irwin J.J., Shoichet B.K. (2005) ZINC-a free database of commercially available compounds for virtual screening. J Chem Inf Model;45:177-182.
    • (2005) J Chem Inf Model , vol.45 , pp. 177-182
    • Irwin, J.J.1    Shoichet, B.K.2
  • 45
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol;234:779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 46
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., Thornton J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr;26:283-291.
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 47
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy R., Bowie J.U., Eisenberg D. (1992) Assessment of protein models with three-dimensional profiles. Nature;356:83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 48
    • 0028922586 scopus 로고
    • LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
    • Wallace A.C., Laskowski R.A., Thornton J.M. (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng;8:127-134.
    • (1995) Protein Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 49
    • 55849123292 scopus 로고    scopus 로고
    • Substrate inhibition kinetic model for West Nile virus NS2B-NS3 protease
    • Tomlinson S.M., Watowich S.J. (2008) Substrate inhibition kinetic model for West Nile virus NS2B-NS3 protease. Biochemistry;47:11763-11770.
    • (2008) Biochemistry , vol.47 , pp. 11763-11770
    • Tomlinson, S.M.1    Watowich, S.J.2


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