메뉴 건너뛰기




Volumn 48, Issue 1, 2005, Pages 1-20

Control of hepatitis C: A medicinal chemistry perspective

Author keywords

[No Author keywords available]

Indexed keywords

2 [(2,4 DICHLOROBENZOYL)(3 TRIFLUOROMETHYLBENZYL)AMINO] 3 PHENYLPROPIONIC ACID; 2 [(5 BENZOFURAN 2 YLTHIOPHEN 2 YLMETHYL)(2,4 DICHLOROBENZOYL)AMINO] 3 PHENYLPROPIONIC ACID; 4,5,6,7 TETRABROMOBENZOTRIAZOLE; 5,6 DICHLORO 1 (BETA DEXTRO RIBOFURANOSYL)BENZOTRIAZOLE; ALPHA INTERFERON; ANTIVIRUS AGENT; BENZAMIDE DERIVATIVE; BENZIMIDAZOLE DERIVATIVE; BENZOTHIADIAZINE DERIVATIVE; BENZOXAZOLE DERIVATIVE; BETA DEXTRO 2' METHYLRIBOFURANOSYLGUANOSINE; CARBAZOLE DERIVATIVE; CARBOXYLIC ACID DERIVATIVE; EPIRUBICIN; MURAYAQUINONE; NOGALAMYCIN; PACLITAXEL; PHENAZINE; RIBAVIRIN; RIBAVIRIN DIPHOSPHATE; RIBAVIRIN TRIPHOSPHATE; SCH 351633; SCH 68631; THIAZOLIDINE DERIVATIVE; THIOMORPHOLINE; TRIFLUOPERAZINE; UNCLASSIFIED DRUG; VIRUS ENZYME;

EID: 12144260229     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm0400101     Document Type: Review
Times cited : (117)

References (166)
  • 1
    • 0034695289 scopus 로고    scopus 로고
    • Hepatitis C-Global prevalence (update)
    • Hepatitis C-Global prevalence (update). Weekly Epidemiol. Rec. 2000, 75, 18-19.
    • (2000) Weekly Epidemiol. Rec. , vol.75 , pp. 18-19
  • 2
    • 0024509701 scopus 로고
    • Isolation of a cDNA clone derived from a bloodborne non-A, non-B viral hepatitis genome
    • Choo, Q. L.; Kuo, G.; Weiner, A. J.; Overby, L. R.; Bradley, D. W.; Houghton, M. Isolation of a cDNA clone derived from a bloodborne non-A, non-B viral hepatitis genome. Science 1989, 244, 359-362.
    • (1989) Science , vol.244 , pp. 359-362
    • Choo, Q.L.1    Kuo, G.2    Weiner, A.J.3    Overby, L.R.4    Bradley, D.W.5    Houghton, M.6
  • 3
    • 0030928695 scopus 로고    scopus 로고
    • Hepatitis C: The clinical spectrum of disease
    • Hoofnagle, J. H. Hepatitis C: the clinical spectrum of disease. Hepatology 1997, 26, 15S-20S.
    • (1997) Hepatology , vol.26
    • Hoofnagle, J.H.1
  • 4
    • 0034877411 scopus 로고    scopus 로고
    • Novel cell culture systems for the hepatitis C virus
    • Bartenschlager, R.; Lohmann, V. Novel cell culture systems for the hepatitis C virus. Antiviral Res. 2001, 52, 1-17.
    • (2001) Antiviral Res. , vol.52 , pp. 1-17
    • Bartenschlager, R.1    Lohmann, V.2
  • 5
    • 0141456064 scopus 로고    scopus 로고
    • Bovine viral diarrhea virus as a surrogate model of hepatitis C virus for the evaluation of antiviral agents
    • Buckwold, V. E.; Beer, B. E.; Donis, R. O. Bovine viral diarrhea virus as a surrogate model of hepatitis C virus for the evaluation of antiviral agents. Antiviral Res. 2003, 60, 1-15.
    • (2003) Antiviral Res. , vol.60 , pp. 1-15
    • Buckwold, V.E.1    Beer, B.E.2    Donis, R.O.3
  • 6
    • 0036815957 scopus 로고    scopus 로고
    • Advances in therapy for hepatitis C infection
    • Zein, C. O.; Zein, N. N. Advances in therapy for hepatitis C infection. Microbes Infect. 2002, 4, 1237-1246.
    • (2002) Microbes Infect. , vol.4 , pp. 1237-1246
    • Zein, C.O.1    Zein, N.N.2
  • 7
    • 3042703977 scopus 로고    scopus 로고
    • Current and emerging therapeutic approaches to hepatitis C infection
    • Durantel, D.; Escuret, V.; Zoulim, F. Current and emerging therapeutic approaches to hepatitis C infection. Expert Rev. Anti-Infect. Ther. 2003, 1, 441-454.
    • (2003) Expert Rev. Anti-Infect. Ther. , vol.1 , pp. 441-454
    • Durantel, D.1    Escuret, V.2    Zoulim, F.3
  • 8
    • 0033230584 scopus 로고    scopus 로고
    • Hepatitis C virus: An overview of current approaches and progress
    • Walker, M. A. Hepatitis C virus: an overview of current approaches and progress. Drug Discovery Today 1999, 4, 518-529.
    • (1999) Drug Discovery Today , vol.4 , pp. 518-529
    • Walker, M.A.1
  • 10
    • 0038076230 scopus 로고    scopus 로고
    • Molecular mechanisms of hepatitis C virus, potential therapeutic targets
    • Rivas-Estilla, A. M.; Panduro, A. Molecular mechanisms of hepatitis C virus, potential therapeutic targets. Rev. Invest. Clin. 2003, 55, 51-64.
    • (2003) Rev. Invest. Clin. , vol.55 , pp. 51-64
    • Rivas-Estilla, A.M.1    Panduro, A.2
  • 11
    • 0037367315 scopus 로고    scopus 로고
    • Approaching a new era for hepatitis C virus therapy, inhibitors of the NS3-4A serine protease and the NS5B RNA-dependent RNA polymerase
    • De Francesco, R.; Tomei, L.; Altamura, S.; Summa, V.; Migliaccio, G. Approaching a new era for hepatitis C virus therapy, inhibitors of the NS3-4A serine protease and the NS5B RNA-dependent RNA polymerase. Antiviral Res. 2003, 58, 1-16.
    • (2003) Antiviral Res. , vol.58 , pp. 1-16
    • De Francesco, R.1    Tomei, L.2    Altamura, S.3    Summa, V.4    Migliaccio, G.5
  • 12
    • 0036835590 scopus 로고    scopus 로고
    • Hepatitis C therapeutics: Current status and emerging strategies
    • Tan, S.-L.; Pause, A.; Shi, Y.; Sonenberg, N. Hepatitis C therapeutics: current status and emerging strategies. Nat. Rev. Drug Discovery 2002, 1, 867-881.
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 867-881
    • Tan, S.-L.1    Pause, A.2    Shi, Y.3    Sonenberg, N.4
  • 14
    • 0041822106 scopus 로고    scopus 로고
    • Early virologic response to treatment with peginterferon α-2b plus ribavirin in patients with chronic hepatitis C
    • Davis, G. L.; Wong, J. B.; McHutchison, J. G.; Manns, M. P.; Harvey, J.; Albrecht, J. Early virologic response to treatment with peginterferon α-2b plus ribavirin in patients with chronic hepatitis C. Hepatology 2003, 38, 645-652.
    • (2003) Hepatology , vol.38 , pp. 645-652
    • Davis, G.L.1    Wong, J.B.2    McHutchison, J.G.3    Manns, M.P.4    Harvey, J.5    Albrecht, J.6
  • 15
    • 0037379437 scopus 로고    scopus 로고
    • Alpha interferon induces distinct translational control programs to suppress hepatitis C virus RNA replication
    • Wang, C.; Pflugheber, J.; Sumpter, R., Jr.; Sodora, D. L.; Hui, D.; Sen, G. C.; Gale, M., Jr. Alpha interferon induces distinct translational control programs to suppress hepatitis C virus RNA replication. J. Virol. 2003, 77, 3898-3912.
    • (2003) J. Virol. , vol.77 , pp. 3898-3912
    • Wang, C.1    Pflugheber, J.2    Sumpter Jr., R.3    Sodora, D.L.4    Hui, D.5    Sen, G.C.6    Gale Jr., M.7
  • 16
    • 0030726545 scopus 로고    scopus 로고
    • Interferon (IFN)-a activation of human blood mononuclear cells in vitro and in vivo for nitric oxide synthase (NOS) type 2 mRNA and protein expression: Possible relationship of induced NOS2 to the anti-hepatitis C effects of IFN-α in vivo
    • Sharara, A. I.; Perkins, D. J.; Misukonis, M. A.; Chan, S. U.; Dominitz, J. A.; Weinberg, J. B. Interferon (IFN)-a activation of human blood mononuclear cells in vitro and in vivo for nitric oxide synthase (NOS) type 2 mRNA and protein expression: possible relationship of induced NOS2 to the anti-hepatitis C effects of IFN-α in vivo. J. Exp. Med. 1997, 186, 1495-1502.
    • (1997) J. Exp. Med. , vol.186 , pp. 1495-1502
    • Sharara, A.I.1    Perkins, D.J.2    Misukonis, M.A.3    Chan, S.U.4    Dominitz, J.A.5    Weinberg, J.B.6
  • 17
    • 0036190222 scopus 로고    scopus 로고
    • Interferon-α-2b plus ribavirin: A review of its use in the management of chronic hepatitis C
    • Scott, L. J.; Perry, C. M. Interferon-α-2b plus ribavirin: A review of its use in the management of chronic hepatitis C. Drugs 2002, 62, 507-556.
    • (2002) Drugs , vol.62 , pp. 507-556
    • Scott, L.J.1    Perry, C.M.2
  • 20
    • 0036830454 scopus 로고    scopus 로고
    • Side effects of therapy of hepatitis C and their management
    • Fried Michael, W. Side effects of therapy of hepatitis C and their management. Hepatology 2002, 36, S237-S244.
    • (2002) Hepatology , vol.36
    • Fried Michael, W.1
  • 21
    • 0029432861 scopus 로고
    • Expression and characterization of hepatitis C virus (HCV) proteins
    • Matsuura, Y. Expression and characterization of hepatitis C virus (HCV) proteins. Uirusu 1995, 45, 105-115.
    • (1995) Uirusu , vol.45 , pp. 105-115
    • Matsuura, Y.1
  • 22
    • 0026334457 scopus 로고
    • Nucleotide sequence and mutation rate of the H strain of hepatitis C virus
    • Ogata, N.; Alter, H. J.; Miller, R. H.; Purcell, R. H. Nucleotide sequence and mutation rate of the H strain of hepatitis C virus. Proc. Nat. Acad. Sci. U.S.A. 1991, 88, 3392-3396.
    • (1991) Proc. Nat. Acad. Sci. U.S.A. , vol.88 , pp. 3392-3396
    • Ogata, N.1    Alter, H.J.2    Miller, R.H.3    Purcell, R.H.4
  • 23
    • 12144267646 scopus 로고    scopus 로고
    • Expression and characterization of the HCV NS2 protease
    • Reed, K. E.; Rice, C. M. Expression and characterization of the HCV NS2 protease. Metod Mol. Med. 1998, 19, 331-342.
    • (1998) Metod Mol. Med. , vol.19 , pp. 331-342
    • Reed, K.E.1    Rice, C.M.2
  • 25
    • 0035185968 scopus 로고    scopus 로고
    • Hepatitis C virus: Prospects for future therapies
    • Wilkinson, T. Hepatitis C virus: Prospects for future therapies. Curr. Opin. Invest. Drugs 2001, 2, 1516-1522.
    • (2001) Curr. Opin. Invest. Drugs , vol.2 , pp. 1516-1522
    • Wilkinson, T.1
  • 26
    • 0038382863 scopus 로고    scopus 로고
    • The dynamic nature of the four-way junction of the hepatitis C virus IRES
    • Melcher, S. E.; Wilson, T. J.; Lilley, D. M. J. The dynamic nature of the four-way junction of the hepatitis C virus IRES. RNA 2003, 9, 809-820.
    • (2003) RNA , vol.9 , pp. 809-820
    • Melcher, S.E.1    Wilson, T.J.2    Lilley, D.M.J.3
  • 30
    • 0034663698 scopus 로고    scopus 로고
    • In vivo determination of substrate specificity of hepatitis C virus NS3 protease: Genetic assay for site-specific proteolysis
    • Kim, S. Y.; Park, K. W.; Lee, Y. J.; Back, S. H.; Goo, J. H.; Park, O. K.; Jang, S. K.; Park, W. J. In vivo determination of substrate specificity of hepatitis C virus NS3 protease: genetic assay for site-specific proteolysis. Anal. Biochem. 2000, 284, 42-48.
    • (2000) Anal. Biochem. , vol.284 , pp. 42-48
    • Kim, S.Y.1    Park, K.W.2    Lee, Y.J.3    Back, S.H.4    Goo, J.H.5    Park, O.K.6    Jang, S.K.7    Park, W.J.8
  • 31
    • 0027999994 scopus 로고
    • Specificity of the hepatitis C virus NS3 serine protease: Effects of substitutions at the 3/4A, 4A/4B, 4B/5A, and 5A/5B cleavage sites on polyprotein processing
    • Kolykhalov, A. A.; Agapov, E. V.; Rice, C. M. Specificity of the hepatitis C virus NS3 serine protease: effects of substitutions at the 3/4A, 4A/4B, 4B/5A, and 5A/5B cleavage sites on polyprotein processing. J. Virol. 1994, 68, 7525-7533.
    • (1994) J. Virol. , vol.68 , pp. 7525-7533
    • Kolykhalov, A.A.1    Agapov, E.V.2    Rice, C.M.3
  • 32
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schlechter, I.; Berger, A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 1987, 27, 157-162.
    • (1987) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schlechter, I.1    Berger, A.2
  • 33
    • 0027414062 scopus 로고
    • Characterization of the hepatitis C virus-encoded serine proteinase: Determination of proteinase-dependent polyprotein cleavage sites
    • Grakoui, A.; McCourt, D. W.; Wychowski, C.; Feinstone, S. M.; Rice, C. M. Characterization of the hepatitis C virus-encoded serine proteinase: Determination of proteinase-dependent polyprotein cleavage sites. J. Virol. 1993, 67, 2832-2843.
    • (1993) J. Virol. , vol.67 , pp. 2832-2843
    • Grakoui, A.1    McCourt, D.W.2    Wychowski, C.3    Feinstone, S.M.4    Rice, C.M.5
  • 40
    • 0033992657 scopus 로고    scopus 로고
    • Structure and function of the hepatitis C virus NS3-NS4A serine proteinase
    • De Francesco, R.; Steinkuhler, C. Structure and function of the hepatitis C virus NS3-NS4A serine proteinase. Curr. Top. Microbiol. Immunol. 2000, 242, 149-169.
    • (2000) Curr. Top. Microbiol. Immunol. , vol.242 , pp. 149-169
    • De Francesco, R.1    Steinkuhler, C.2
  • 41
    • 0034940307 scopus 로고    scopus 로고
    • Hepatitis C virus serine protease inhibitors: Current progress and future challenges
    • Steinkuhler, C.; Koch, U.; Narjes, F.; Matassa, V. G. Hepatitis C virus serine protease inhibitors: current progress and future challenges. Curr. Med. Chem. 2001, 8, 919-932.
    • (2001) Curr. Med. Chem. , vol.8 , pp. 919-932
    • Steinkuhler, C.1    Koch, U.2    Narjes, F.3    Matassa, V.G.4
  • 45
    • 0003072207 scopus 로고    scopus 로고
    • Therapies for hepatitis C infection: Targeting the non-structural proteins of HCV
    • Beaulieu, P. L.; Llinas-Brunet, M. Therapies for hepatitis C infection: targeting the non-structural proteins of HCV. Curr. Med. Chem. 2002, 1, 163-176.
    • (2002) Curr. Med. Chem. , vol.1 , pp. 163-176
    • Beaulieu, P.L.1    Llinas-Brunet, M.2
  • 47
    • 16044364658 scopus 로고    scopus 로고
    • Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide
    • Kim, J. L.; Morgenstern, K. A.; Lin, C.; Fox, T.; Dwyer, M. D.; Landro, J. A.; Chambers, S. P.; Markland, W.; Lepre, C. A. Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide. Cell 1996, 87, 343-355.
    • (1996) Cell , vol.87 , pp. 343-355
    • Kim, J.L.1    Morgenstern, K.A.2    Lin, C.3    Fox, T.4    Dwyer, M.D.5    Landro, J.A.6    Chambers, S.P.7    Markland, W.8    Lepre, C.A.9
  • 49
    • 0035936581 scopus 로고    scopus 로고
    • Role of charged residues in the catalytic mechanism of hepatitis C virus NS3 protease: Electrostatic precollision guidance and transition-state stabilization
    • Koch, U.; Biasiol, G.; Brunetti, M.; Fattori, D.; Pallaoro, M.; Steinkuhler, C. Role of charged residues in the catalytic mechanism of hepatitis C virus NS3 protease: electrostatic precollision guidance and transition-state stabilization. Biochemistry 2001, 40, 631-640.
    • (2001) Biochemistry , vol.40 , pp. 631-640
    • Koch, U.1    Biasiol, G.2    Brunetti, M.3    Fattori, D.4    Pallaoro, M.5    Steinkuhler, C.6
  • 50
    • 12144272227 scopus 로고    scopus 로고
    • Modification of NSAIDs by sulfur-containing functional groups. U.S. 6,429,223, 2002
    • Lai, C.-S.; Wang, T. Modification of NSAIDs by sulfur-containing functional groups. U.S. 6,429,223, 2002.
    • Lai, C.-S.1    Wang, T.2
  • 51
    • 0026509189 scopus 로고
    • Increased prevalence of poor sulphoxidation in patients with rheumatoid arthritis: Effect of changes in the acute phase response and second line drug treatment
    • Emery, P.; Bradley, H.; Gough, A.; Arthur, V.; Jubb, R.; Waring, R. Increased prevalence of poor sulphoxidation in patients with rheumatoid arthritis: effect of changes in the acute phase response and second line drug treatment. Ann. Rheum. Dis. 1992, 51, 318-320.
    • (1992) Ann. Rheum. Dis. , vol.51 , pp. 318-320
    • Emery, P.1    Bradley, H.2    Gough, A.3    Arthur, V.4    Jubb, R.5    Waring, R.6
  • 55
    • 84962396688 scopus 로고    scopus 로고
    • Structure-based design of inhibitors of NS3 serine protease of hepatitis C virus
    • Frecer, V.; Kabelac, M.; De Nardi, P.; Pricl, S.; Miertus, S. Structure-based design of inhibitors of NS3 serine protease of hepatitis C virus. J. Mol. Graphics Modell. 2003, 22, 209-220.
    • (2003) J. Mol. Graphics Modell. , vol.22 , pp. 209-220
    • Frecer, V.1    Kabelac, M.2    De Nardi, P.3    Pricl, S.4    Miertus, S.5
  • 56
    • 0347991962 scopus 로고    scopus 로고
    • NMR Structural Characterization of Peptide Inhibitors Bound to the Hepatitis C Virus NS3 Protease: Design of a New P2 Substituent
    • Goudreau, N.; Cameron, D. R.; Bonneau, P.; Gorys, V.; Plouffe, C.; Poirier, M.; Lamarre, D.; Llinas-Brunet, M. NMR Structural Characterization of Peptide Inhibitors Bound to the Hepatitis C Virus NS3 Protease: Design of a New P2 Substituent. J. Med. Chem. 2004, 47, 123-132.
    • (2004) J. Med. Chem. , vol.47 , pp. 123-132
    • Goudreau, N.1    Cameron, D.R.2    Bonneau, P.3    Gorys, V.4    Plouffe, C.5    Poirier, M.6    Lamarre, D.7    Llinas-Brunet, M.8
  • 57
    • 0033522886 scopus 로고    scopus 로고
    • The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism
    • Barbato, G.; Cicero, D. O.; Nardi, M. C.; Steinkuehler, C.; Cortese, R.; De Franscesco, R.; Bazzo, R. The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism. J. Mol. Biol. 1999, 289, 371-384.
    • (1999) J. Mol. Biol. , vol.289 , pp. 371-384
    • Barbato, G.1    Cicero, D.O.2    Nardi, M.C.3    Steinkuehler, C.4    Cortese, R.5    De Franscesco, R.6    Bazzo, R.7
  • 59
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski, C. A.; Lombardo, F.; Dominy, B. W.; Feeney, P. J. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Delivery Rev. 2001, 46, 3-26.
    • (2001) Adv. Drug Delivery Rev. , vol.46 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 65
    • 12144270047 scopus 로고    scopus 로고
    • Synthetic inhibitors of hepatitis C virus NS3 protease (Schering Corporation). Application WO9743310, 1997; 59 pp.
    • Zhang, R.; Mui, P. W.; Weber, P. C. Synthetic inhibitors of hepatitis C virus NS3 protease (Schering Corporation). Application WO9743310, 1997; 59 pp.
    • Zhang, R.1    Mui, P.W.2    Weber, P.C.3
  • 66
    • 0030871616 scopus 로고    scopus 로고
    • Mechanistic Role of an NS4A Peptide Cofactor with the Truncated NS3 Protease of Hepatitis C Virus: Elucidation of the NS4A Stimulatory Effect via Kinetic Analysis and Inhibitor Mapping
    • Landro, J. A.; Raybuck, S. A.; Luong, Y. P. C.; O'Malley, E. T.; Harbeson, S. L.; Morgenstern, K. A.; Rao, G.; Livingston, D. J. Mechanistic Role of an NS4A Peptide Cofactor with the Truncated NS3 Protease of Hepatitis C Virus: Elucidation of the NS4A Stimulatory Effect via Kinetic Analysis and Inhibitor Mapping. Biochemistry 1997, 36, 9340-9348.
    • (1997) Biochemistry , vol.36 , pp. 9340-9348
    • Landro, J.A.1    Raybuck, S.A.2    Luong, Y.P.C.3    O'Malley, E.T.4    Harbeson, S.L.5    Morgenstern, K.A.6    Rao, G.7    Livingston, D.J.8
  • 68
    • 0037472688 scopus 로고    scopus 로고
    • Phenethyl Amides as Novel Noncovalent Inhibitors of Hepatitis C Virus NS3/4A Protease: Discovery, Initial SAR, and Molecular Modeling
    • Colarusso, S.; Koch, U.; Gerlach, B.; Steinkuehler, C.; De Francesco, R.; Altamura, S.; Matassa, V. G.; Narjes, F. Phenethyl Amides as Novel Noncovalent Inhibitors of Hepatitis C Virus NS3/4A Protease: Discovery, Initial SAR, and Molecular Modeling. J. Med. Chem. 2003, 46, 345-348.
    • (2003) J. Med. Chem. , vol.46 , pp. 345-348
    • Colarusso, S.1    Koch, U.2    Gerlach, B.3    Steinkuehler, C.4    De Francesco, R.5    Altamura, S.6    Matassa, V.G.7    Narjes, F.8
  • 69
    • 0030589011 scopus 로고    scopus 로고
    • Enhancement of hepatitis C virus NS3 proteinase activity by association with NS4A-specific synthetic peptides: Identification of sequence and critical residues of NS4A for the cofactor activity
    • Butkiewicz, N. J.; Wendel, M.; Zhang, R.; Jubin, R.; Pichardo, J.; Smith, E. B.; Hart, A. M.; Ingram, R.; Durkin, J.; et al. Enhancement of hepatitis C virus NS3 proteinase activity by association with NS4A-specific synthetic peptides: identification of sequence and critical residues of NS4A for the cofactor activity. Virology 1996, 225, 328-338.
    • (1996) Virology , vol.225 , pp. 328-338
    • Butkiewicz, N.J.1    Wendel, M.2    Zhang, R.3    Jubin, R.4    Pichardo, J.5    Smith, E.B.6    Hart, A.M.7    Ingram, R.8    Durkin, J.9
  • 71
    • 0033584192 scopus 로고    scopus 로고
    • Isolation and structure of SCH 351633: A novel hepatitis C virus (HCV) NS3 protease inhibitor from the fungus Penicillium griseofulvum
    • Chu, M.; Mierzwa, R.; He, L.; King, A.; Patel, M.; Pichardo, J.; Hart, A.; Butkiewicz, N.; Puar, M. S. Isolation and structure of SCH 351633: a novel hepatitis C virus (HCV) NS3 protease inhibitor from the fungus Penicillium griseofulvum. Bioorg. Med. Chem. Lett. 1999, 9, 1949-1952.
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 1949-1952
    • Chu, M.1    Mierzwa, R.2    He, L.3    King, A.4    Patel, M.5    Pichardo, J.6    Hart, A.7    Butkiewicz, N.8    Puar, M.S.9
  • 75
    • 0030708525 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins
    • Hajduk, P. J.; Meadows, R. P.; Fesik, S. W. Discovering high-affinity ligands for proteins. Science 1997, 278, 497-499.
    • (1997) Science , vol.278 , pp. 497-499
    • Hajduk, P.J.1    Meadows, R.P.2    Fesik, S.W.3
  • 76
    • 0036175914 scopus 로고    scopus 로고
    • NMR-based structural characterization of large protein-ligand interactions
    • Pellecchia, M.; Meininger, D.; Dong, Q.; Chang, E.; Jack, R.; Sem, D. S. NMR-based structural characterization of large protein-ligand interactions. J. Biomol. NMR 2002, 22, 165-173.
    • (2002) J. Biomol. NMR , vol.22 , pp. 165-173
    • Pellecchia, M.1    Meininger, D.2    Dong, Q.3    Chang, E.4    Jack, R.5    Sem, D.S.6
  • 78
    • 0037009985 scopus 로고    scopus 로고
    • Spatial localization of ligand binding sites from electron current density surfaces calculated from NMR chemical shift perturbations
    • McCoy, M. A.; Wyss, D. F. Spatial localization of ligand binding sites from electron current density surfaces calculated from NMR chemical shift perturbations. J. Am. Chem. Soc. 2002, 124, 11758-11763.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11758-11763
    • McCoy, M.A.1    Wyss, D.F.2
  • 79
    • 0033636878 scopus 로고    scopus 로고
    • Alignment of weakly interacting molecules to protein surfaces using simulations of chemical shift perturbations
    • McCoy, M. A.; Wyss, D. F. Alignment of weakly interacting molecules to protein surfaces using simulations of chemical shift perturbations. J. Biomol. NMR 2000, 18, 189-198.
    • (2000) J. Biomol. NMR , vol.18 , pp. 189-198
    • McCoy, M.A.1    Wyss, D.F.2
  • 80
    • 2342652311 scopus 로고    scopus 로고
    • Non-Peptidic Small-Molecule Inhibitors of the Single-Chain Hepatitis C Virus NS3 Protease/NS4A Cofactor Complex Discovered by Structure-Based NMR Screening
    • Wyss, D. F.; Arasappan, A.; Senior, M. M.; Wang, Y.-S.; Beyer, B. M.; Njoroge, F. G.; McCoy, M. A. Non-Peptidic Small-Molecule Inhibitors of the Single-Chain Hepatitis C Virus NS3 Protease/NS4A Cofactor Complex Discovered by Structure-Based NMR Screening. J. Med. Chem. 2004, 47, 2486-2498.
    • (2004) J. Med. Chem. , vol.47 , pp. 2486-2498
    • Wyss, D.F.1    Arasappan, A.2    Senior, M.M.3    Wang, Y.-S.4    Beyer, B.M.5    Njoroge, F.G.6    McCoy, M.A.7
  • 83
    • 0036200412 scopus 로고    scopus 로고
    • Selection of RNA aptamers that are specific and high-affinity ligands of the hepatitis C virus RNA-dependent RNA polymerase
    • Biroccio, A.; Hamm, J.; Incitti, I.; De Francesco, R.; Tomei, L. Selection of RNA aptamers that are specific and high-affinity ligands of the hepatitis C virus RNA-dependent RNA polymerase. J. Virol. 2002, 76, 3688-3696.
    • (2002) J. Virol. , vol.76 , pp. 3688-3696
    • Biroccio, A.1    Hamm, J.2    Incitti, I.3    De Francesco, R.4    Tomei, L.5
  • 86
    • 0347457077 scopus 로고    scopus 로고
    • Modulation of the Hepatitis C Virus RNA-Dependent RNA Polymerase Activity by the Non-Structural NS3 Helicase and the NS4B Membrane Protein
    • Piccininni, S.; Varaklioti, A.; Nardelli, M.; Dave, B.; Raney, K. D.; McCarthy, J. E. G. Modulation of the Hepatitis C Virus RNA-Dependent RNA Polymerase Activity by the Non-Structural NS3 Helicase and the NS4B Membrane Protein. J. Biol. Chem. 2002, 277, 45670-45679.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45670-45679
    • Piccininni, S.1    Varaklioti, A.2    Nardelli, M.3    Dave, B.4    Raney, K.D.5    McCarthy, J.E.G.6
  • 91
    • 0032902564 scopus 로고    scopus 로고
    • Characterization of soluble hepatitis C virus RNA-dependent RNA polymerase expressed in Escherichia coli
    • Ferrari, E.; Wright-Minogue, J.; Fang, J. W. S.; Baroudy, B. M.; Lau, J. Y. N.; Hong, Z. Characterization of soluble hepatitis C virus RNA-dependent RNA polymerase expressed in Escherichia coli. J. Virol. 1999, 73, 1649-1654.
    • (1999) J. Virol. , vol.73 , pp. 1649-1654
    • Ferrari, E.1    Wright-Minogue, J.2    Fang, J.W.S.3    Baroudy, B.M.4    Lau, J.Y.N.5    Hong, Z.6
  • 92
    • 0032876683 scopus 로고    scopus 로고
    • Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site
    • Lesburg, C. A.; Cable, M. B.; Ferrari, E.; Hong, Z.; Mannarino, A. F.; Weber, P. C. Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site. Nat. Struct. Biol. 1999, 6, 937-943.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 937-943
    • Lesburg, C.A.1    Cable, M.B.2    Ferrari, E.3    Hong, Z.4    Mannarino, A.F.5    Weber, P.C.6
  • 93
    • 0031571638 scopus 로고    scopus 로고
    • Structure of the RNA-dependent RNA polymerase of poliovirus
    • Hansen, J. L.; Long, A. M.; Schultz, S. C. Structure of the RNA-dependent RNA polymerase of poliovirus. Structure 1997, 5, 1109-1122.
    • (1997) Structure , vol.5 , pp. 1109-1122
    • Hansen, J.L.1    Long, A.M.2    Schultz, S.C.3
  • 95
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: Structural diversity and common mechanisms
    • Steitz, T. A. DNA polymerases: structural diversity and common mechanisms. J. Biol. Chem. 1999, 274, 17395-17398.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 96
    • 0037470586 scopus 로고    scopus 로고
    • Substrate complexes of hepatitis C virus RNA polymerase (HC-J4): Structural evidence for nucleotide import and de-novo initiation
    • O'Farrell, D.; Trowbridge, R.; Rowlands, D.; Jager, J. Substrate complexes of hepatitis C virus RNA polymerase (HC-J4): structural evidence for nucleotide import and de-novo initiation. J. Mol. Biol. 2003, 326, 1025-1035.
    • (2003) J. Mol. Biol. , vol.326 , pp. 1025-1035
    • O'Farrell, D.1    Trowbridge, R.2    Rowlands, D.3    Jager, J.4
  • 97
    • 0036240477 scopus 로고    scopus 로고
    • Mechanism of action of ribavirin in the combination treatment of chronic HCV infection
    • Lau, J. Y. N.; Tam, R. C.; Liang, T. J.; Hong, Z. Mechanism of action of ribavirin in the combination treatment of chronic HCV infection. Hepatology 2002, 35, 1002-1009.
    • (2002) Hepatology , vol.35 , pp. 1002-1009
    • Lau, J.Y.N.1    Tam, R.C.2    Liang, T.J.3    Hong, Z.4
  • 99
    • 0035824671 scopus 로고    scopus 로고
    • Hepatitis C virus RNA-dependent RNA polymerase (NS5B) as a mediator of the antiviral activity of ribavirin
    • Maag, D.; Castro, C.; Hong, Z.; Cameron, C. E. Hepatitis C virus RNA-dependent RNA polymerase (NS5B) as a mediator of the antiviral activity of ribavirin. J. Biol. Chem. 2001, 276, 46094-46098.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46094-46098
    • Maag, D.1    Castro, C.2    Hong, Z.3    Cameron, C.E.4
  • 101
    • 0035934568 scopus 로고    scopus 로고
    • Peginterferon α-2b plus ribavirin compared with interferon α-2b plus ribavirin for initial treatment of chronic hepatitis C: A randomized trial
    • Manns, M. P.; McHutchison, J. G.; Gordon, S. C.; Rustgi, V. K.; Shiffman, M.; Reindollar, R.; Goodman, Z. D.; Koury, K.; Ling, M. H.; Albrecht, J. K. Peginterferon α-2b plus ribavirin compared with interferon α-2b plus ribavirin for initial treatment of chronic hepatitis C: a randomized trial. Lancet 2001, 358, 958-965.
    • (2001) Lancet , vol.358 , pp. 958-965
    • Manns, M.P.1    McHutchison, J.G.2    Gordon, S.C.3    Rustgi, V.K.4    Shiffman, M.5    Reindollar, R.6    Goodman, Z.D.7    Koury, K.8    Ling, M.H.9    Albrecht, J.K.10
  • 102
    • 12144250748 scopus 로고    scopus 로고
    • Method for the treatment or prevention of flavivirus infections using nucleoside analogues. WO 2001060315, 2001
    • Ismaili, H. M. A.; Cheng, Y.-X.; Lavallee, J.-F.; Siddiqui, A.; Storer, R. Method for the treatment or prevention of flavivirus infections using nucleoside analogues. WO 2001060315, 2001.
    • Ismaili, H.M.A.1    Cheng, Y.-X.2    Lavallee, J.-F.3    Siddiqui, A.4    Storer, R.5
  • 103
    • 12144256377 scopus 로고    scopus 로고
    • Method for the treatment or prevention of Flaviviridae viral infection using nucleoside analogs. WO 2001032153, 2001
    • Storer, R. Method for the treatment or prevention of Flaviviridae viral infection using nucleoside analogs. WO 2001032153, 2001.
    • Storer, R.1
  • 104
    • 12144273640 scopus 로고    scopus 로고
    • Preparation of benzimidazolecarboxylates and related compounds as viral polymerase inhibitors. WO 2002004425, 2002
    • Beaulieu, P. L.; Fazal, G.; Gillard, J.; Kukolj, G.; Austel, V. Preparation of benzimidazolecarboxylates and related compounds as viral polymerase inhibitors. WO 2002004425, 2002.
    • Beaulieu, P.L.1    Fazal, G.2    Gillard, J.3    Kukolj, G.4    Austel, V.5
  • 105
    • 12144254166 scopus 로고    scopus 로고
    • Preparation of heterocyclic compounds as remedies for hepatitis C. WO 2001047883, 2001
    • Hashimoto, H.; Mizutani, K.; Yoshida, A. Preparation of heterocyclic compounds as remedies for hepatitis C. WO 2001047883, 2001.
    • Hashimoto, H.1    Mizutani, K.2    Yoshida, A.3
  • 106
    • 12144253800 scopus 로고    scopus 로고
    • Preparation of 3-(1,1-dioxo-2H-benzo-1,2,4-thiadiazin-3-yl)-2-quinolones as novel anti-infectives. WO 2001085172, 2001
    • Dhanak, D.; Kaura, A. C.; Shaw, A. Preparation of 3-(1,1-dioxo-2H-benzo- 1,2,4-thiadiazin-3-yl)-2-quinolones as novel anti-infectives. WO 2001085172, 2001.
    • Dhanak, D.1    Kaura, A.C.2    Shaw, A.3
  • 107
    • 12144253801 scopus 로고    scopus 로고
    • Preparation of pyrrolidine-2,4-dicarboxylic acid derivatives as novel anti-infectives. WO 2001085720, 2001
    • Dhanak, D.; Carr, T. Preparation of pyrrolidine-2,4-dicarboxylic acid derivatives as novel anti-infectives. WO 2001085720, 2001.
    • Dhanak, D.1    Carr, T.2
  • 108
    • 12144250352 scopus 로고    scopus 로고
    • Self-replicating RNA molecule from hepatitis C virus having adaptive mutations, and its uses in screening assay for HCV replication inhibitors. WO 2002052015, 2002
    • Kukolj, G.; Pause, A. Self-replicating RNA molecule from hepatitis C virus having adaptive mutations, and its uses in screening assay for HCV replication inhibitors. WO 2002052015, 2002.
    • Kukolj, G.1    Pause, A.2
  • 110
    • 12144260214 scopus 로고    scopus 로고
    • Preparation of substituted 1-cyclohexyl-2-phenylbenzimidazole-5- carboxylic acids as remedies for hepatitis C. WO 2003050320, 2003
    • Hashimoto, H.; Mizutani, K.; Yoshida, A. Preparation of substituted 1-cyclohexyl-2-phenylbenzimidazole-5-carboxylic acids as remedies for hepatitis C. WO 2003050320, 2003.
    • Hashimoto, H.1    Mizutani, K.2    Yoshida, A.3
  • 111
    • 12144278821 scopus 로고    scopus 로고
    • Diketoacid derivatives as inhibitors of viral polymerases. WO 2000006529, 2000
    • Altamura, S.; Tomei, L.; Koch, U.; Neuner, P. J. S.; Summa, V. Diketoacid derivatives as inhibitors of viral polymerases. WO 2000006529, 2000.
    • Altamura, S.1    Tomei, L.2    Koch, U.3    Neuner, P.J.S.4    Summa, V.5
  • 113
    • 0347361643 scopus 로고    scopus 로고
    • Discovery of α,γ-Diketo Acids as Potent Selective and Reversible Inhibitors of Hepatitis C Virus NS5b RNA-Dependent RNA Polymerase
    • Summa, V.; Petrocchi, A.; Pace, P.; Matassa, V. G.; De Francesco, R.; Altamura, S.; Tomei, L.; Koch, U.; Neuner, P. Discovery of α,γ- Diketo Acids as Potent Selective and Reversible Inhibitors of Hepatitis C Virus NS5b RNA-Dependent RNA Polymerase J. Med. Chem. 2004, 47 (1), 14-17.
    • (2004) J. Med. Chem. , vol.47 , Issue.1 , pp. 14-17
    • Summa, V.1    Petrocchi, A.2    Pace, P.3    Matassa, V.G.4    De Francesco, R.5    Altamura, S.6    Tomei, L.7    Koch, U.8    Neuner, P.9
  • 114
    • 0035976707 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of an engineered arginine-rich subdomain 2 of the hepatitis C virus NS3 RNA helicase
    • Liu, D.; Wang, Y. S.; Gesell, J. J.; Wyss, D. F. Solution structure and backbone dynamics of an engineered arginine-rich subdomain 2 of the hepatitis C virus NS3 RNA helicase. J. Mol. Biol. 2001, 314, 543-561.
    • (2001) J. Mol. Biol. , vol.314 , pp. 543-561
    • Liu, D.1    Wang, Y.S.2    Gesell, J.J.3    Wyss, D.F.4
  • 115
    • 0036752091 scopus 로고    scopus 로고
    • Nucleotide triphosphatase/helicase of hepatitis C virus as a target for antiviral therapy
    • Borowski, P.; Schalinski, S.; Schmitz, H. Nucleotide triphosphatase/ helicase of hepatitis C virus as a target for antiviral therapy. Antiviral Res. 2002, 55, 397-412.
    • (2002) Antiviral Res. , vol.55 , pp. 397-412
    • Borowski, P.1    Schalinski, S.2    Schmitz, H.3
  • 116
    • 0033947171 scopus 로고    scopus 로고
    • The RNA helicase and nucleotide triphosphatase activities of the bovine viral diarrhea virus NS3 protein are essential for viral replication
    • Gu, B.; Liu, C.; Lin-Goerke, J.; Maley, D. R.; Gutshall L. L.; Fletenberger, C. A.; Del Vecchio, A. The RNA helicase and nucleotide triphosphatase activities of the bovine viral diarrhea virus NS3 protein are essential for viral replication. J. Virol. 2000, 74, 1794-1800.
    • (2000) J. Virol. , vol.74 , pp. 1794-1800
    • Gu, B.1    Liu, C.2    Lin-Goerke, J.3    Maley, D.R.4    Gutshall, L.L.5    Fletenberger, C.A.6    Del Vecchio, A.7
  • 117
    • 0034802008 scopus 로고    scopus 로고
    • Mutagenesis of the Dengue Virus Type 2 NS3 Protein within and outside Helicase Motifs: Effectson Enzyme Activity and Virus Replication
    • Matusan, A. E.; Pryor, M. J.; Davidson, A. D.; Wright, P. J. Mutagenesis of the Dengue Virus Type 2 NS3 Protein within and outside Helicase Motifs: Effectson Enzyme Activity and Virus Replication. J. Virol. 2001, 75, 9633-9643.
    • (2001) J. Virol. , vol.75 , pp. 9633-9643
    • Matusan, A.E.1    Pryor, M.J.2    Davidson, A.D.3    Wright, P.J.4
  • 118
    • 0030897821 scopus 로고    scopus 로고
    • Virus-encoded RNA helicases
    • Kadare, G.; Haenni, A.-L. Virus-encoded RNA helicases. J. Virol. 1997, 71, 2583-2590.
    • (1997) J. Virol. , vol.71 , pp. 2583-2590
    • Kadare, G.1    Haenni, A.-L.2
  • 119
    • 0024462161 scopus 로고
    • Viral proteins containing the purine NTP-binding sequence pattern
    • Gorbalenya, A. E.; Koonin, E. V. Viral proteins containing the purine NTP-binding sequence pattern. Nucleic Acids Res. 1989, 17, 8413-8440.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8413-8440
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 120
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E.; Saraste, M.; Runswick, M. J.; Gay, N. J. Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1982, 1, 945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 121
    • 0034870450 scopus 로고    scopus 로고
    • Structure-based mutational analysis of the hepatitis C virus NS3 helicase
    • Tai, C. L.; Pan, W. C.; Liaw, S. H.; Yang, U. C.; Hwang, L. H.; Chen, D. S. Structure-based mutational analysis of the hepatitis C virus NS3 helicase. J. Virol. 2001, 75, 8289-8297.
    • (2001) J. Virol. , vol.75 , pp. 8289-8297
    • Tai, C.L.1    Pan, W.C.2    Liaw, S.H.3    Yang, U.C.4    Hwang, L.H.5    Chen, D.S.6
  • 123
    • 0032518490 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: The crystal structure provides insights into the mode of unwinding
    • Kim, J. L.; Morgenstern, K. A.; Griffith, J. P.; Dwyer, M. D.; Thomson, J. A.; Murcko, M. A.; Lin, C.; Caron, P. R. Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding. Structure 1998, 6, 89-100.
    • (1998) Structure , vol.6 , pp. 89-100
    • Kim, J.L.1    Morgenstern, K.A.2    Griffith, J.P.3    Dwyer, M.D.4    Thomson, J.A.5    Murcko, M.A.6    Lin, C.7    Caron, P.R.8
  • 125
    • 0032510963 scopus 로고    scopus 로고
    • Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanism of unwind-ing duplex RNA
    • Cho, H. S.; Ha, N. C.; Kang, L. W.; Chung, K. M.; Bac, S. H.; Jang, S. K.; Oh, B. H. Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanism of unwind-ing duplex RNA. J. Biol. Chem. 1998, 273, 15045-15052.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15045-15052
    • Cho, H.S.1    Ha, N.C.2    Kang, L.W.3    Chung, K.M.4    Bac, S.H.5    Jang, S.K.6    Oh, B.H.7
  • 126
    • 0033573066 scopus 로고    scopus 로고
    • Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair
    • Theis, K.; Chen, P. J.; Skorvaga, M.; Van Houten, B.; Kisker, C. Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair. EMBO J. 1999, 18, 6899-6907.
    • (1999) EMBO J. , vol.18 , pp. 6899-6907
    • Theis, K.1    Chen, P.J.2    Skorvaga, M.3    Van Houten, B.4    Kisker, C.5
  • 127
    • 0030897821 scopus 로고    scopus 로고
    • Virus-encoded RNA helicases
    • Kadare, G.; Haenni, A.-L. Virus-encoded RNA helicases. J. Virol. 1997, 71, 2583-2590.
    • (1997) J. Virol. , vol.71 , pp. 2583-2590
    • Kadare, G.1    Haenni, A.-L.2
  • 128
    • 0024462161 scopus 로고
    • Viral proteins containing the purine NTP-binding sequence pattern
    • Gorbalenya, A. E.; Kunin, E. V. Viral proteins containing the purine NTP-binding sequence pattern. Nucleic Acids Res. 1989, 17, 8413-8440.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8413-8440
    • Gorbalenya, A.E.1    Kunin, E.V.2
  • 129
    • 0029970903 scopus 로고    scopus 로고
    • The helicase activity associated with hepatitis C virus nonstructural protein 3 (NS3)
    • Tai, C. L.; Chi, W. K.; Chen, D. S.; Hwang, L. H. The helicase activity associated with hepatitis C virus nonstructural protein 3 (NS3). J. Virol. 1996, 70, 8477-8484.
    • (1996) J. Virol. , vol.70 , pp. 8477-8484
    • Tai, C.L.1    Chi, W.K.2    Chen, D.S.3    Hwang, L.H.4
  • 130
    • 0141758201 scopus 로고    scopus 로고
    • Helicases as antiviral drug targets
    • Frick, D. N. Helicases as antiviral drug targets. Drug News Perspect. 2003, 16, 355-362.
    • (2003) Drug News Perspect. , vol.16 , pp. 355-362
    • Frick, D.N.1
  • 132
    • 0038747996 scopus 로고    scopus 로고
    • Halogenated benzimidazoles and benzotriazoles as inhibitors of the NTPase/helicase activities of hepatitis C and related viruses
    • Borowski, P.; Deinert, J.; Schalinski, S.; Bretner, M.; Ginalski, K.; Kulikowski, T.; Shugar, D. Halogenated benzimidazoles and benzotriazoles as inhibitors of the NTPase/helicase activities of hepatitis C and related viruses. Eur. J. Biochem. 2003, 270, 1645-1653.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1645-1653
    • Borowski, P.1    Deinert, J.2    Schalinski, S.3    Bretner, M.4    Ginalski, K.5    Kulikowski, T.6    Shugar, D.7
  • 133
    • 0141567430 scopus 로고    scopus 로고
    • Ring-expanded ("fat") nucleoside and nucleotide analogues exhibit potent in vitro activity against flaviviridae NTPases/helicases, including those of the West Nile virus, hepatitis C virus, and Japanese encephalitis virus
    • Zhang, N.; Chen, H.-M.; Koch, V.; Schmitz, H.; Liao, C.-L.; Bretner, M.; Bhadti, V. S.; Fattom, A. I.; Naso, R. B.; Hosmane, R. S.; Borowski, P. Ring-expanded ("fat") nucleoside and nucleotide analogues exhibit potent in vitro activity against flaviviridae NTPases/helicases, including those of the West Nile virus, hepatitis C virus, and Japanese encephalitis virus. J. Med. Chem. 2003, 46, 4149-4164.
    • (2003) J. Med. Chem. , vol.46 , pp. 4149-4164
    • Zhang, N.1    Chen, H.-M.2    Koch, V.3    Schmitz, H.4    Liao, C.-L.5    Bretner, M.6    Bhadti, V.S.7    Fattom, A.I.8    Naso, R.B.9    Hosmane, R.S.10    Borowski, P.11
  • 135
  • 137
    • 0033590119 scopus 로고    scopus 로고
    • Adriamycin inhibits human RH II/Gu RNA helicase activity by binding to its substrate
    • Zhu, K.; Henning, D.; Iwakuma, T.; Valdez, B. C.; Busch, H. Adriamycin inhibits human RH II/Gu RNA helicase activity by binding to its substrate. Biochem. Biophys. Res. Commun. 1999, 266, 361-365.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 361-365
    • Zhu, K.1    Henning, D.2    Iwakuma, T.3    Valdez, B.C.4    Busch, H.5
  • 139
    • 0031658923 scopus 로고    scopus 로고
    • The 3′-untranslated region of hepatitis C virus RNA enhances translation from an internal ribosomal entry site
    • Ito, T.; Tahara, S. M.; Lai, M. M. The 3′-untranslated region of hepatitis C virus RNA enhances translation from an internal ribosomal entry site. J. Virol. 1998, 72, 8789-8796.
    • (1998) J. Virol. , vol.72 , pp. 8789-8796
    • Ito, T.1    Tahara, S.M.2    Lai, M.M.3
  • 140
    • 0030790922 scopus 로고    scopus 로고
    • Genetic analysis of internal ribosomal entry site on hepatitis C virus RNA: Implication for involvement of the highly ordered structure and cell type-specific transacting factors
    • Kamoshita, N.; Tsukiyama-Kohara, K.; Kohara, M.; Nomoto, A. Genetic analysis of internal ribosomal entry site on hepatitis C virus RNA: implication for involvement of the highly ordered structure and cell type-specific transacting factors. Virology 1997, 233, 9-18.
    • (1997) Virology , vol.233 , pp. 9-18
    • Kamoshita, N.1    Tsukiyama-Kohara, K.2    Kohara, M.3    Nomoto, A.4
  • 142
    • 0033744387 scopus 로고    scopus 로고
    • A potential RNA drug target in the hepatitis C virus internal ribosomal entry site
    • Klinck, R.; Westhof, E.; Walker, S.; Afshar, M.; Collier, A.; Aboul-Ela, F. A potential RNA drug target in the hepatitis C virus internal ribosomal entry site. RNA 2000, 6, 1423-1431.
    • (2000) RNA , vol.6 , pp. 1423-1431
    • Klinck, R.1    Westhof, E.2    Walker, S.3    Afshar, M.4    Collier, A.5    Aboul-Ela, F.6
  • 143
    • 12144255989 scopus 로고    scopus 로고
    • Methods for identifying small molecules that bind specific RNA structural motifs and uses high-throughput screening of combinatorial librarys. WO 2002083953, 2002
    • Rando, R.; Welch, E. Methods for identifying small molecules that bind specific RNA structural motifs and uses high-throughput screening of combinatorial librarys. WO 2002083953, 2002.
    • Rando, R.1    Welch, E.2
  • 144
    • 0037102582 scopus 로고    scopus 로고
    • RNA molecules with structure dependent functions are uniquely folded
    • Le, S.-Y.; Zhang, K.; Maizel, J. V., Jr. RNA molecules with structure dependent functions are uniquely folded. Nucleic Acids Res. 2002, 30, 3574-3582.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3574-3582
    • Le, S.-Y.1    Zhang, K.2    Maizel Jr., J.V.3
  • 147
    • 0942289830 scopus 로고    scopus 로고
    • Identification of the most accessible sites to ribozymes on the hepatitis C virus internal ribosome entry site
    • Ryu, K.-J.; Lee, S.-W. Identification of the most accessible sites to ribozymes on the hepatitis C virus internal ribosome entry site. J. Biochem. Mol. Biol. 2003, 36, 538-544.
    • (2003) J. Biochem. Mol. Biol. , vol.36 , pp. 538-544
    • Ryu, K.-J.1    Lee, S.-W.2
  • 150
    • 0037368588 scopus 로고    scopus 로고
    • RNA aptamers targeted to domain II of hepatitis C virus IRES that bind to its apical loop region
    • Kikuchi, K.; Umehara, T.; Fukuda, K.; Hwang, J.; Kuno, A.; Hasegawa, T.; Nishikawa, S. RNA aptamers targeted to domain II of hepatitis C virus IRES that bind to its apical loop region. J. Biochem. 2003, 133, 263-270.
    • (2003) J. Biochem. , vol.133 , pp. 263-270
    • Kikuchi, K.1    Umehara, T.2    Fukuda, K.3    Hwang, J.4    Kuno, A.5    Hasegawa, T.6    Nishikawa, S.7
  • 151
    • 0035182631 scopus 로고    scopus 로고
    • ISIS-14803 Isis Pharmaceuticals
    • Witherell, G. W. ISIS-14803 Isis Pharmaceuticals. Curr. Opin. Invest. Drugs 2001, 2, 1523-1529.
    • (2001) Curr. Opin. Invest. Drugs , vol.2 , pp. 1523-1529
    • Witherell, G.W.1
  • 152
    • 12144281374 scopus 로고    scopus 로고
    • Heptazyme
    • Heptazyme. Drug News Perspect. 2000, 13, 112.
    • (2000) Drug News Perspect. , vol.13 , pp. 112
  • 154
    • 0030700403 scopus 로고    scopus 로고
    • Hepatitis C virus NS2-3 proteinase
    • Wilkinson, C. S. Hepatitis C virus NS2-3 proteinase. Biochem. Soc. Trans. 1997, 25, S611.
    • (1997) Biochem. Soc. Trans. , vol.25
    • Wilkinson, C.S.1
  • 155
    • 0028832632 scopus 로고
    • The NS2 protein of hepatitis C virus is a transmembrane polypeptide
    • Santolini, E.; Pacini, L.; Fipaldini, C.; Migliaceio, G.; Monica, N. The NS2 protein of hepatitis C virus is a transmembrane polypeptide. J. Virol. 1995, 69, 7461-7471.
    • (1995) J. Virol. , vol.69 , pp. 7461-7471
    • Santolini, E.1    Pacini, L.2    Fipaldini, C.3    Migliaceio, G.4    Monica, N.5
  • 156
    • 0033521138 scopus 로고    scopus 로고
    • Inhibition of hepatitis C virus NS2/3 processing by NS4A peptides. Implications for control of viral processing
    • Darke, P. L.; Jacobs, A. R.; Waxman, L.; Kuo, L. C. Inhibition of hepatitis C virus NS2/3 processing by NS4A peptides. Implications for control of viral processing. J. Biol. Chem. 1999, 274, 34511-34514.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34511-34514
    • Darke, P.L.1    Jacobs, A.R.2    Waxman, L.3    Kuo, L.C.4
  • 161
    • 0033781909 scopus 로고    scopus 로고
    • Characterization of hepatitis C virus (HCV) and HCV E2 interactions with CD81 and the low-density lipoprotein receptor
    • Wunschmann, S.; Medh, J. D.; Klinzmann, D.; Schmidt, W. N.; Stapleton, J. T. Characterization of hepatitis C virus (HCV) and HCV E2 interactions with CD81 and the low-density lipoprotein receptor. J. Virol. 2000, 74, 10055-10062.
    • (2000) J. Virol. , vol.74 , pp. 10055-10062
    • Wunschmann, S.1    Medh, J.D.2    Klinzmann, D.3    Schmidt, W.N.4    Stapleton, J.T.5
  • 164
    • 0037033363 scopus 로고    scopus 로고
    • Binding of the hepatitis C virus envelope protein E2 to CD81 inhibits natural killer cell functions
    • Tseng, C.-T. K.; Klimpel, G. R. Binding of the hepatitis C virus envelope protein E2 to CD81 inhibits natural killer cell functions. J. Exp. Med. 2002, 195, 43-49.
    • (2002) J. Exp. Med. , vol.195 , pp. 43-49
    • Tseng, C.-T.K.1    Klimpel, G.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.