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Volumn 56, Issue 21, 2013, Pages 8389-8403

Thiazolidinone-peptide hybrids as dengue virus protease inhibitors with antiviral activity in cell culture

Author keywords

[No Author keywords available]

Indexed keywords

2,4 THIAZOLIDINEDIONE DERIVATIVE; ANTIVIRUS AGENT; OXYGEN; PEPTIDE; PROTEINASE INHIBITOR; RHODANINE; SULFUR; THIOHYDANTOIN DERIVATIVE;

EID: 84887869847     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm400828u     Document Type: Article
Times cited : (130)

References (68)
  • 4
    • 84867236960 scopus 로고    scopus 로고
    • Structural biology of dengue virus enzymes: Towards rational design of therapeutics
    • Noble, C. G.; Shi, P.-Y. Structural biology of dengue virus enzymes: towards rational design of therapeutics Antiviral Res. 2012, 96, 115-126
    • (2012) Antiviral Res. , vol.96 , pp. 115-126
    • Noble, C.G.1    Shi, P.-Y.2
  • 5
    • 84880810570 scopus 로고    scopus 로고
    • Viral proteases as targets for drug design
    • Skoreński, M.; Sieńczyk, M. Viral proteases as targets for drug design Curr. Pharm. Des. 2013, 19, 1126-1153
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 1126-1153
    • Skoreński, M.1    Sieńczyk, M.2
  • 6
    • 84879420038 scopus 로고    scopus 로고
    • The molecular and structural basis of advanced antiviral therapy for hepatitis C virus infection
    • Bartenschlager, R.; Lohmann, V.; Penin, F. The molecular and structural basis of advanced antiviral therapy for hepatitis C virus infection Nature Rev. Microbiol. 2013, 11, 482-496
    • (2013) Nature Rev. Microbiol. , vol.11 , pp. 482-496
    • Bartenschlager, R.1    Lohmann, V.2    Penin, F.3
  • 7
    • 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. H.; Xu, T.; Sampath, A.; Lim, S. P.; Canard, B.; Vasudevan, S. G. 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, 94-101
    • (2008) Antiviral Res. , vol.80 , pp. 94-101
    • Lescar, J.1    Luo, D.H.2    Xu, T.3    Sampath, A.4    Lim, S.P.5    Canard, B.6    Vasudevan, S.G.7
  • 8
    • 0031975823 scopus 로고    scopus 로고
    • Mutagenesis of the NS3 protease of dengue virus type 2
    • Valle, R. P.; Falgout, B. Mutagenesis of the NS3 protease of dengue virus type 2 J. Virol. 1998, 72, 624-32
    • (1998) J. Virol. , vol.72 , pp. 624-632
    • Valle, R.P.1    Falgout, B.2
  • 9
    • 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. Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins J. Virol. 1991, 65, 2467-75
    • (1991) J. Virol. , vol.65 , pp. 2467-2475
    • Falgout, B.1    Pethel, M.2    Zhang, Y.M.3    Lai, C.J.4
  • 11
    • 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. Serotype-Specific Structural Differences in the Protease-Cofactor Complexes of the Dengue Virus Family J. Virol. 2010, 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
  • 12
    • 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. Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold Protein Sci. 2007, 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
  • 13
    • 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. Structure of West Nile Virus NS3 Protease: Ligand Stabilization of the Catalytic Conformation J. Mol. Biol. 2009, 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
  • 14
    • 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. Ligand-Bound Structures of the Dengue Virus Protease Reveal the Active Conformation J. Virol. 2012, 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
  • 15
    • 81855172065 scopus 로고    scopus 로고
    • Binding of Low Molecular Weight Inhibitors Promotes Large Conformational Changes in the Dengue Virus NS2B-NS3 Protease: Fold Analysis by Pseudocontact Shifts
    • de la Cruz, L.; Thi, H. D. N.; Ozawa, K.; Shin, J.; Graham, B.; Huber, T.; Otting, G. Binding of Low Molecular Weight Inhibitors Promotes Large Conformational Changes in the Dengue Virus NS2B-NS3 Protease: Fold Analysis by Pseudocontact Shifts J. Am. Chem. Soc. 2011, 133, 19205-19215
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 19205-19215
    • De La Cruz, L.1    Thi, H.D.N.2    Ozawa, K.3    Shin, J.4    Graham, B.5    Huber, T.6    Otting, G.7
  • 16
    • 84887934372 scopus 로고    scopus 로고
    • Backbone 1H, 13C and 15N resonance assignments of dengue virus NS2B-NS3p in complex with aprotinin
    • Bi, Y.; Zhu, L.; Li, H.; Wu, B.; Liu, J.; Wang, J. Backbone 1H, 13C and 15N resonance assignments of dengue virus NS2B-NS3p in complex with aprotinin Biomol. NMR Assignments 2012, 1-3
    • (2012) Biomol. NMR Assignments , pp. 1-3
    • Bi, Y.1    Zhu, L.2    Li, H.3    Wu, B.4    Liu, J.5    Wang, J.6
  • 17
    • 74549156902 scopus 로고    scopus 로고
    • NMR Analysis of the Dynamic Exchange of the NS2B Cofactor between Open and Closed Conformations of the West Nile Virus NS2B-NS3 Protease
    • Su, X.-C.; Ozawa, K.; Qi, R.; Vasudevan, S. G.; Lim, S. P.; Otting, G. NMR Analysis of the Dynamic Exchange of the NS2B Cofactor between Open and Closed Conformations of the West Nile Virus NS2B-NS3 Protease PLoS Neglected Trop. Dis. 2009, 3, e561
    • (2009) PLoS Neglected Trop. Dis. , vol.3 , pp. 561
    • Su, X.-C.1    Ozawa, K.2    Qi, R.3    Vasudevan, S.G.4    Lim, S.P.5    Otting, G.6
  • 20
    • 82255192015 scopus 로고    scopus 로고
    • Arylcyanoacrylamides as inhibitors of the Dengue and West Nile virus proteases
    • Nitsche, C.; Steuer, C.; Klein, C. D. Arylcyanoacrylamides as inhibitors of the Dengue and West Nile virus proteases Bioorg. Med. Chem. 2011, 19, 7318-7337
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 7318-7337
    • Nitsche, C.1    Steuer, C.2    Klein, C.D.3
  • 21
    • 79959530775 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of alpha-ketoamides as inhibitors of the Dengue virus protease with antiviral activity in cell culture
    • Steuer, C.; Gege, C.; Fischl, W.; Heinonen, K. H.; Bartenschlager, R.; Klein, C. D. Synthesis and biological evaluation of alpha-ketoamides as inhibitors of the Dengue virus protease with antiviral activity in cell culture Bioorg. Med. Chem. 2011, 19, 4067-4074
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 4067-4074
    • Steuer, C.1    Gege, C.2    Fischl, W.3    Heinonen, K.H.4    Bartenschlager, R.5    Klein, C.D.6
  • 22
    • 84856383832 scopus 로고    scopus 로고
    • Privileged Scaffolds or Promiscuous Binders: A Comparative Study on Rhodanines and Related Heterocycles in Medicinal Chemistry
    • Mendgen, T.; Steuer, C.; Klein, C. D. Privileged Scaffolds or Promiscuous Binders: A Comparative Study on Rhodanines and Related Heterocycles in Medicinal Chemistry J. Med. Chem. 2012, 55, 743-753
    • (2012) J. Med. Chem. , vol.55 , pp. 743-753
    • Mendgen, T.1    Steuer, C.2    Klein, C.D.3
  • 23
    • 78751620005 scopus 로고    scopus 로고
    • Anthracene-based inhibitors of dengue virus NS2B-NS3 protease
    • Tomlinson, S. M.; Watowich, S. J. Anthracene-based inhibitors of dengue virus NS2B-NS3 protease Antiviral Res. 2011, 89, 127-35
    • (2011) Antiviral Res. , vol.89 , pp. 127-135
    • Tomlinson, S.M.1    Watowich, S.J.2
  • 25
    • 84871380932 scopus 로고    scopus 로고
    • Characterization of 8-hydroxyquinoline derivatives containing aminobenzothiazole as inhibitors of dengue virus type 2 protease in vitro
    • Lai, H.; Sridhar Prasad, G.; Padmanabhan, R. Characterization of 8-hydroxyquinoline derivatives containing aminobenzothiazole as inhibitors of dengue virus type 2 protease in vitro Antiviral Res. 2013, 97, 74-80
    • (2013) Antiviral Res. , vol.97 , pp. 74-80
    • Lai, H.1    Sridhar Prasad, G.2    Padmanabhan, R.3
  • 27
    • 84856213045 scopus 로고    scopus 로고
    • Inhibition of Dengue virus and West Nile virus proteases by click chemistry-derived benz[ d ]isothiazol-3(2 H)-one derivatives
    • Tiew, K.-C.; Dou, D.; Teramoto, T.; Lai, H.; Alliston, K. R.; Lushington, G. H.; Padmanabhan, R.; Groutas, W. C. Inhibition of Dengue virus and West Nile virus proteases by click chemistry-derived benz[ d ]isothiazol-3(2 H)-one derivatives Bioorg. Med. Chem. 2012, 20, 1213-1221
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 1213-1221
    • Tiew, K.-C.1    Dou, D.2    Teramoto, T.3    Lai, H.4    Alliston, K.R.5    Lushington, G.H.6    Padmanabhan, R.7    Groutas, W.C.8
  • 31
    • 75149168873 scopus 로고    scopus 로고
    • Synthesis and disulfide bond connectivity-activity studies of a kalata B1-inspired cyclopeptide against dengue NS2B-NS3 protease
    • Gao, Y.; Cui, T.; Lam, Y. Synthesis and disulfide bond connectivity-activity studies of a kalata B1-inspired cyclopeptide against dengue NS2B-NS3 protease Bioorg. Med. Chem. 2010, 18, 1331-1336
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 1331-1336
    • Gao, Y.1    Cui, T.2    Lam, Y.3
  • 32
    • 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.; Fan, C.; Ericksen, B.; Liu, J.; Chi, C.; Wang, C. Critical Effect of Peptide Cyclization on the Potency of Peptide Inhibitors against Dengue Virus NS2B-NS3 Protease J. Med. Chem. 2012, 55, 6881-6887
    • (2012) J. Med. Chem. , vol.55 , pp. 6881-6887
    • Xu, S.1    Li, H.2    Shao, X.3    Fan, C.4    Ericksen, B.5    Liu, J.6    Chi, C.7    Wang, C.8
  • 33
    • 84871836593 scopus 로고    scopus 로고
    • Protegrin-1 Inhibits Dengue NS2B-NS3 Serine Protease and Viral Replication in MK2 Cells
    • Article ID 251482, 6 pp, DOI 10.1155/2012/251482.
    • Rothan, H. A.; Abdulrahman, A. Y.; Sasikumer, P. G.; Othman, S.; Abd Rahman, N.; Yusof, R. Protegrin-1 Inhibits Dengue NS2B-NS3 Serine Protease and Viral Replication in MK2 Cells. J. Biomed. Biotechnol. 2012, Article ID 251482, 6 pp, DOI 10.1155/2012/251482.
    • (2012) J. Biomed. Biotechnol.
    • Rothan, H.A.1    Abdulrahman, A.Y.2    Sasikumer, P.G.3    Othman, S.4    Abd Rahman, N.5    Yusof, R.6
  • 34
    • 84869218137 scopus 로고    scopus 로고
    • Inhibition of dengue NS2B-NS3 protease and viral replication in Vero cells by recombinant retrocyclin-1
    • Rothan, H.; Han, H. C.; Ramasamy, T. S.; Othman, S.; Rahman, N. A.; Yusof, R. Inhibition of dengue NS2B-NS3 protease and viral replication in Vero cells by recombinant retrocyclin-1 BMC Infect. Dis. 2012, 12, 314
    • (2012) BMC Infect. Dis. , vol.12 , pp. 314
    • Rothan, H.1    Han, H.C.2    Ramasamy, T.S.3    Othman, S.4    Rahman, N.A.5    Yusof, R.6
  • 36
    • 84860526352 scopus 로고    scopus 로고
    • Discovery of boceprevir, a direct-acting NS3/4A protease inhibitor for treatment of chronic hepatitis C infections
    • Venkatraman, S. Discovery of boceprevir, a direct-acting NS3/4A protease inhibitor for treatment of chronic hepatitis C infections Trends Pharmacol. Sci. 2012, 33, 289-294
    • (2012) Trends Pharmacol. Sci. , vol.33 , pp. 289-294
    • Venkatraman, S.1
  • 37
    • 84858145412 scopus 로고    scopus 로고
    • Retro peptide-hybrids as selective inhibitors of the Dengue virus NS2B-NS3 protease
    • Nitsche, C.; Behnam, M. A. M.; Steuer, C.; Klein, C. D. Retro peptide-hybrids as selective inhibitors of the Dengue virus NS2B-NS3 protease Antiviral Res. 2012, 94, 72-79
    • (2012) Antiviral Res. , vol.94 , pp. 72-79
    • Nitsche, C.1    Behnam, M.A.M.2    Steuer, C.3    Klein, C.D.4
  • 38
    • 0019408388 scopus 로고
    • Chemistry and biological activity of thiazolidinones
    • Singh, S. P.; Parmar, S. S.; Raman, K.; Stenberg, V. I. Chemistry and biological activity of thiazolidinones Chem. Rev. 1981, 81, 175-203
    • (1981) Chem. Rev. , vol.81 , pp. 175-203
    • Singh, S.P.1    Parmar, S.S.2    Raman, K.3    Stenberg, V.I.4
  • 39
    • 33947479100 scopus 로고
    • 4-Thiazolidinones
    • Brown, F. C. 4-Thiazolidinones Chem. Rev. 1961, 61, 463-521
    • (1961) Chem. Rev. , vol.61 , pp. 463-521
    • Brown, F.C.1
  • 40
    • 6044256350 scopus 로고    scopus 로고
    • 4-Thiazolidones: Centenarian history, current status and perspectives for modern organic and medicinal chemistry
    • Lesyk, R. B.; Zimenkovsky, B. S. 4-Thiazolidones: centenarian history, current status and perspectives for modern organic and medicinal chemistry Curr. Org. Chem. 2004, 8, 1547-1577
    • (2004) Curr. Org. Chem. , vol.8 , pp. 1547-1577
    • Lesyk, R.B.1    Zimenkovsky, B.S.2
  • 41
    • 67650261319 scopus 로고    scopus 로고
    • Rhodanine as a Privileged Scaffold in Drug Discovery
    • Tomasic, T.; Masic, L. P. Rhodanine as a Privileged Scaffold in Drug Discovery Curr. Med. Chem. 2009, 16, 1596-1629
    • (2009) Curr. Med. Chem. , vol.16 , pp. 1596-1629
    • Tomasic, T.1    Masic, L.P.2
  • 44
    • 34250081066 scopus 로고
    • The crystal structure of 5-(2-nitrophenylmethylene)-2-thioxothiazolidin- 4-one-3-(α-benzyl)ethanoic acid: Preference for the Z-configuration
    • Nyburg, S.; Parkins, A.; Smith, B. The crystal structure of 5-(2-nitrophenylmethylene)-2-thioxothiazolidin-4-one-3-(α-benzyl)ethanoic acid: preference for the Z-configuration J. Cryst. Spectrosc. 1993, 23, 459-463
    • (1993) J. Cryst. Spectrosc. , vol.23 , pp. 459-463
    • Nyburg, S.1    Parkins, A.2    Smith, B.3
  • 45
    • 84865449477 scopus 로고    scopus 로고
    • Aqueous microwave-assisted one-pot synthesis of N-substituted rhodanines
    • Nitsche, C.; Klein, C. D. Aqueous microwave-assisted one-pot synthesis of N-substituted rhodanines Tetrahedron Lett. 2012, 53, 5197-5201
    • (2012) Tetrahedron Lett. , vol.53 , pp. 5197-5201
    • Nitsche, C.1    Klein, C.D.2
  • 46
    • 2942729106 scopus 로고
    • Notes - Alkylation of 2,4-Thiazolidinedione
    • Lo, C.-P.; Shropshire, E. Notes-Alkylation of 2,4-Thiazolidinedione J. Org. Chem. 1957, 22, 999-1001
    • (1957) J. Org. Chem. , vol.22 , pp. 999-1001
    • Lo, C.-P.1    Shropshire, E.2
  • 47
    • 0027981411 scopus 로고
    • Oxidationen an Thiourethanen, 12. Mitt.: Oxidative Desulfurierung von Cyclischen Dithiocarbamaten und -carbazaten mittels Wasserstoffperoxid oder Wasserstoffperoxid/Natriumwolframat im Zweiphasen-System
    • Hanefeld, W.; Schlitzer, M. Oxidationen an Thiourethanen, 12. Mitt.: Oxidative Desulfurierung von Cyclischen Dithiocarbamaten und -carbazaten mittels Wasserstoffperoxid oder Wasserstoffperoxid/Natriumwolframat im Zweiphasen-System Arch. Pharm. 1994, 327, 413-415
    • (1994) Arch. Pharm. , vol.327 , pp. 413-415
    • Hanefeld, W.1    Schlitzer, M.2
  • 48
    • 0037029812 scopus 로고    scopus 로고
    • Microwave-mediated solventless synthesis of new derivatives of marine alkaloid Leucettamine B
    • Chérouvrier, J.-R.; Carreaux, F.; Bazureau, J. P. Microwave-mediated solventless synthesis of new derivatives of marine alkaloid Leucettamine B Tetrahedron Lett. 2002, 43, 3581-3584
    • (2002) Tetrahedron Lett. , vol.43 , pp. 3581-3584
    • Chérouvrier, J.-R.1    Carreaux, F.2    Bazureau, J.P.3
  • 49
    • 68949163953 scopus 로고    scopus 로고
    • A Novel Multicomponent Method for the Synthesis of 2-Thioxo-1,3- thiazolidin-4-ones
    • Alizadeh, A.; Zohreh, N. A Novel Multicomponent Method for the Synthesis of 2-Thioxo-1,3-thiazolidin-4-ones Synlett 2009, 2146-2148
    • (2009) Synlett , pp. 2146-2148
    • Alizadeh, A.1    Zohreh, N.2
  • 50
    • 60349129901 scopus 로고    scopus 로고
    • A simple and effective approach to the synthesis of rhodanine derivatives via three-component reactions in water
    • Alizadeh, A.; Rostamnia, S.; Zohreh, N.; Hosseinpour, R. A simple and effective approach to the synthesis of rhodanine derivatives via three-component reactions in water Tetrahedron Lett. 2009, 50, 1533-1535
    • (2009) Tetrahedron Lett. , vol.50 , pp. 1533-1535
    • Alizadeh, A.1    Rostamnia, S.2    Zohreh, N.3    Hosseinpour, R.4
  • 51
    • 84880122957 scopus 로고    scopus 로고
    • Fluorimetric and HPLC-Based Dengue Virus Protease Assays Using a FRET Substrate
    • Gong, E. Y. Humana Press: Totowa, NJ; Vol. (Methods in Molecular Biology)
    • Nitsche, C.; Klein, C. D. Fluorimetric and HPLC-Based Dengue Virus Protease Assays Using a FRET Substrate. In Antiviral Methods and Protocols, Gong, E. Y., Ed.; Humana Press: Totowa, NJ, 2013; Vol. 1030 (Methods in Molecular Biology), pp 221-236.
    • (2013) Antiviral Methods and Protocols , vol.1030 , pp. 221-236
    • Nitsche, C.1    Klein, C.D.2
  • 52
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • Dixon, M. The determination of enzyme inhibitor constants Biochem. J. 1953, 55, 170-171
    • (1953) Biochem. J. , vol.55 , pp. 170-171
    • Dixon, M.1
  • 53
    • 0015972948 scopus 로고
    • A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors
    • Cornish-Bowden, A. A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors Biochem. J. 1974, 137, 143-144
    • (1974) Biochem. J. , vol.137 , pp. 143-144
    • Cornish-Bowden, A.1
  • 56
  • 57
    • 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. 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. 2000, 275, 9963-9
    • (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
  • 58
    • 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. 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. 2001, 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
  • 60
    • 0032568397 scopus 로고    scopus 로고
    • Physicochemical High Throughput Screening: Parallel Artificial Membrane Permeation Assay in the Description of Passive Absorption Processes
    • Kansy, M.; Senner, F.; Gubernator, K. Physicochemical High Throughput Screening: Parallel Artificial Membrane Permeation Assay in the Description of Passive Absorption Processes J. Med. Chem. 1998, 41, 1007-1010
    • (1998) J. Med. Chem. , vol.41 , pp. 1007-1010
    • Kansy, M.1    Senner, F.2    Gubernator, K.3
  • 61
    • 44749090398 scopus 로고    scopus 로고
    • A Novel Design of Artificial Membrane for Improving the PAMPA Model
    • Chen, X.; Murawski, A.; Patel, K.; Crespi, C.; Balimane, P. A Novel Design of Artificial Membrane for Improving the PAMPA Model Pharm. Res. 2008, 25, 1511-1520
    • (2008) Pharm. Res. , vol.25 , pp. 1511-1520
    • Chen, X.1    Murawski, A.2    Patel, K.3    Crespi, C.4    Balimane, P.5
  • 62
    • 10344248922 scopus 로고    scopus 로고
    • Enzymatic characterization and homology model of a catalytically active recombinant West Nile virus NS3 protease
    • Nall, T. A.; Chappell, K. J.; Stoermer, M. J.; Fang, N. X.; Tyndall, J. D. A.; Young, P. R.; Fairlie, D. P. Enzymatic characterization and homology model of a catalytically active recombinant West Nile virus NS3 protease J. Biol. Chem. 2004, 279, 48535-48542
    • (2004) J. Biol. Chem. , vol.279 , pp. 48535-48542
    • Nall, T.A.1    Chappell, K.J.2    Stoermer, M.J.3    Fang, N.X.4    Tyndall, J.D.A.5    Young, P.R.6    Fairlie, D.P.7
  • 63
    • 74049147097 scopus 로고    scopus 로고
    • Optimization of Assay Conditions for Dengue Virus Protease: Effect of Various Polyols and Nonionic Detergents
    • Steuer, C.; Heinonen, K. H.; Kattner, L.; Klein, C. D. Optimization of Assay Conditions for Dengue Virus Protease: Effect of Various Polyols and Nonionic Detergents J. Biomol. Screening 2009, 14, 1102-1108
    • (2009) J. Biomol. Screening , vol.14 , pp. 1102-1108
    • Steuer, C.1    Heinonen, K.H.2    Kattner, L.3    Klein, C.D.4
  • 64
    • 84887931576 scopus 로고    scopus 로고
    • National Center for Biotechnology Informaion: Bethesda, MD, March 15, Assay ID.
    • Diamond, S. L. Thrombin 1536 HTS. National Center for Biotechnology Informaion: Bethesda, MD, March 15, 2013; Assay ID 1046, http://pubchem.ncbi. nlm.nih.gov/assay/assay.cgi?aid=1046&loc=ea-ras.
    • (2013) Thrombin 1536 HTS , pp. 1046
    • Diamond, S.L.1
  • 65
    • 0033557480 scopus 로고    scopus 로고
    • Use of a fluorescence plate reader for measuring kinetic parameters with inner filter effect correction
    • Liu, Y. Y.; Kati, W.; Chen, C. M.; Tripathi, R.; Molla, A.; Kohlbrenner, W. Use of a fluorescence plate reader for measuring kinetic parameters with inner filter effect correction Anal. Biochem. 1999, 267, 331-335
    • (1999) Anal. Biochem. , vol.267 , pp. 331-335
    • Liu, Y.Y.1    Kati, W.2    Chen, C.M.3    Tripathi, R.4    Molla, A.5    Kohlbrenner, W.6
  • 66
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones, G.; Willett, P.; Glen, R. C.; Leach, A. R.; Taylor, R. Development and validation of a genetic algorithm for flexible docking J. Mol. Biol. 1997, 267, 727-48
    • (1997) J. Mol. Biol. , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 68
    • 84880113515 scopus 로고    scopus 로고
    • High-Throughput Screening Using Dengue Virus Reporter Genomes
    • Gong, E. Y. Humana Press: Totowa, NJ, Vol. (Methods in Molecular Biology)
    • Fischl, W.; Bartenschlager, R. High-Throughput Screening Using Dengue Virus Reporter Genomes. In Antiviral Methods and Protocols; Gong, E. Y., Ed.; Humana Press: Totowa, NJ, 2013; Vol. 1030 (Methods in Molecular Biology), pp 205-219.
    • (2013) Antiviral Methods and Protocols , vol.1030 , pp. 205-219
    • Fischl, W.1    Bartenschlager, R.2


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