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Volumn 80, Issue 1, 2006, Pages 149-160

A novel, highly selective inhibitor of pestivirus replication that targets the viral RNA-dependent RNA polymerase

(21)  Paeshuyse, Jan a   Leyssen, Pieter a   Mabery, Eric b   Boddeker, Nina b   Vrancken, Robert c   Froeyen, Matheus a   Ansari, Israrul H d   Dutartre, Hélène e   Rozenski, Jef a   Gil, Laura H V G d   Letellier, Carine c   Lanford, Robert f   Canard, Bruno e   Koenen, Frank c   Kerkhofs, Pierre c   Donis, Ruben O d   Herdewijn, Piet a   Watson, Julia b   De Clercq, Erik a   Puerstinger, Gerhard g   more..


Author keywords

[No Author keywords available]

Indexed keywords

5 [(4 BROMOPHENYL)METHYL] 2 PHENYL 5H IMIDAZO[4,5 C]PYRIDINE; ANTIVIRUS AGENT; N PROPYL N [2 (2H 1,2,4 TRIAZINO[5,6 B]INDOL 3 YLTHIO)ETHYL] 1 PROPANAMINE; PROPIONAMIDE DERIVATIVE; PYRIDINE DERIVATIVE; RNA DIRECTED RNA POLYMERASE; UNCLASSIFIED DRUG; VIRUS PROTEIN; VP 32947;

EID: 33645966527     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.80.1.149-160.2006     Document Type: Article
Times cited : (74)

References (58)
  • 3
    • 0034877411 scopus 로고    scopus 로고
    • Novel cell culture systems for the hepatitis C virus
    • Bartenschlager, R., and V. Lohmann. 2001. Novel cell culture systems for the hepatitis C virus. Antivir. Res. 52:1-17.
    • (2001) Antivir. Res. , vol.52 , pp. 1-17
    • Bartenschlager, R.1    Lohmann, V.2
  • 4
    • 0035079046 scopus 로고    scopus 로고
    • Antiviral effect of N-butyldeoxynojirimycin against bovine viral diarrhea virus correlates with misfolding of E2 envelope proteins and impairment of their association into E1-E2 heterodimers
    • Branza-Nichita, N., D. Durantel, S. Carrouée-Durantel, R. A. Dwek, and N. Zitzmann. 2001. Antiviral effect of N-butyldeoxynojirimycin against bovine viral diarrhea virus correlates with misfolding of E2 envelope proteins and impairment of their association into E1-E2 heterodimers. J. Virol. 75:3527-3536.
    • (2001) J. Virol. , vol.75 , pp. 3527-3536
    • Branza-Nichita, N.1    Durantel, D.2    Carrouée-Durantel, S.3    Dwek, R.A.4    Zitzmann, N.5
  • 5
    • 0036120573 scopus 로고    scopus 로고
    • Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides
    • Bressanelli, S., L. Tomei, F. A. Rey, and R. De Francesco. 2002. Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides. J. Virol. 76:3482-3492.
    • (2002) J. Virol. , vol.76 , pp. 3482-3492
    • Bressanelli, S.1    Tomei, L.2    Rey, F.A.3    De Francesco, R.4
  • 6
    • 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., B. E. Beer, and R. O. Donis. 2004. Bovine viral diarrhea virus as a surrogate model of hepatitis C virus for the evaluation of antiviral agents. Antivir. Res. 60:1-15.
    • (2004) Antivir. Res. , vol.60 , pp. 1-15
    • Buckwold, V.E.1    Beer, B.E.2    Donis, R.O.3
  • 7
    • 0035738231 scopus 로고    scopus 로고
    • Inhibition of the bovine viral diarrhoea virus NS3 serine protease by a boron-modified peptidyl mimetic of its natural substrate
    • Bukhtiyarova, M., C. J. Rizzo, C. A. Kettner, B. D. Korant, H. T. Scarnati, and R. W. King. 2001. Inhibition of the bovine viral diarrhoea virus NS3 serine protease by a boron-modified peptidyl mimetic of its natural substrate. Antivir. Chem. Chemother. 12:367-373.
    • (2001) Antivir. Chem. Chemother. , vol.12 , pp. 367-373
    • Bukhtiyarova, M.1    Rizzo, C.J.2    Kettner, C.A.3    Korant, B.D.4    Scarnati, H.T.5    King, R.W.6
  • 9
    • 1842481188 scopus 로고    scopus 로고
    • The structure of the RNA-dependent RNA polymerase from bovine viral diarrhea virus establishes the role of GTP in de novo initiation
    • Choi, K. H., J. M. Groarke, D. C. Young, R. J. Kuhn, J. L. Smith, D. C. Pevear, and M. G. Rossmann. 2004. The structure of the RNA-dependent RNA polymerase from bovine viral diarrhea virus establishes the role of GTP in de novo initiation. Proc. Natl. Acad. Sci. USA 101:4425-4430.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4425-4430
    • Choi, K.H.1    Groarke, J.M.2    Young, D.C.3    Kuhn, R.J.4    Smith, J.L.5    Pevear, D.C.6    Rossmann, M.G.7
  • 10
    • 0037404536 scopus 로고    scopus 로고
    • Protein-protein interactions between hepatitis C virus nonstructural proteins
    • Dimitrova, M., I. Imbert, M. P. Kieny, and C. Schuster. 2003. Protein-protein interactions between hepatitis C virus nonstructural proteins. J. Virol. 77:5401-5414.
    • (2003) J. Virol. , vol.77 , pp. 5401-5414
    • Dimitrova, M.1    Imbert, I.2    Kieny, M.P.3    Schuster, C.4
  • 12
    • 0034849492 scopus 로고    scopus 로고
    • Study of the mechanism of antiviral action of iminosugar derivatives against bovine viral diarrhea virus
    • Durantel, D., N. Branza-Nichita, S. Carrouée-Durantel, T. D. Butters, R. A. Dwek, and N. Zitzmann. 2001. Study of the mechanism of antiviral action of iminosugar derivatives against bovine viral diarrhea virus. J. Virol. 75:8987-8998.
    • (2001) J. Virol. , vol.75 , pp. 8987-8998
    • Durantel, D.1    Branza-Nichita, N.2    Carrouée-Durantel, S.3    Butters, T.D.4    Dwek, R.A.5    Zitzmann, N.6
  • 13
    • 0942290557 scopus 로고    scopus 로고
    • Effects of interferon, ribavirin, and iminosugar derivatives on cells persistently infected with noncytopathic bovine viral diarrhea virus
    • Durantel, D., S. Carrouée-Durantel, N. Branza-Nichita, R. A. Dwek, and N. Zitzmann. 2004. Effects of interferon, ribavirin, and iminosugar derivatives on cells persistently infected with noncytopathic bovine viral diarrhea virus. Antimicrob. Agents Chemother. 48:497-504.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 497-504
    • Durantel, D.1    Carrouée-Durantel, S.2    Branza-Nichita, N.3    Dwek, R.A.4    Zitzmann, N.5
  • 16
    • 33645963536 scopus 로고    scopus 로고
    • Further additions to Molscript 1.4. including reading and contouring of electron-density maps
    • Esnouf, R. 1999. Further additions to Molscript 1.4. including reading and contouring of electron-density maps. Acta Crystallogr. 277:505-524.
    • (1999) Acta Crystallogr. , vol.277 , pp. 505-524
    • Esnouf, R.1
  • 17
    • 0032924734 scopus 로고    scopus 로고
    • Selection of RNA replicons capable of persistent noncytopathic replication in mammalian cells
    • Frolov, I., E. Agapov, T.-A. J. Hoffman, B. M. Pragai, M. Lippa, S. Schlesinger, and C. M. Rice. 1999. Selection of RNA replicons capable of persistent noncytopathic replication in mammalian cells. J. Virol. 73:3854-3865.
    • (1999) J. Virol. , vol.73 , pp. 3854-3865
    • Frolov, I.1    Agapov, E.2    Hoffman, T.-A.J.3    Pragai, B.M.4    Lippa, M.5    Schlesinger, S.6    Rice, C.M.7
  • 20
    • 0038289071 scopus 로고    scopus 로고
    • Bovine viral diarrhoea eradication and control programmes in Europe
    • Greiser-Wilke, I., B. Grummer, and V. Moennig. 2003. Bovine viral diarrhoea eradication and control programmes in Europe. Biologicals 31:113-118.
    • (2003) Biologicals , vol.31 , pp. 113-118
    • Greiser-Wilke, I.1    Grummer, B.2    Moennig, V.3
  • 21
    • 0038627860 scopus 로고    scopus 로고
    • Economic impact of BVDV infection in dairies
    • Houe, H. 2003. Economic impact of BVDV infection in dairies. Biologicals 31:137-143.
    • (2003) Biologicals , vol.31 , pp. 137-143
    • Houe, H.1
  • 22
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • Jones, G., P. Willet, and R. Glen. 1995. Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation. J. Mol. Biol. 245:43-53.
    • (1995) J. Mol. Biol. , vol.245 , pp. 43-53
    • Jones, G.1    Willet, P.2    Glen, R.3
  • 23
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones, G., P. Willet, R. Glen, A. Leach, and R. Taylor. 1997. Development and validation of a genetic algorithm for flexible docking. J. Mol. Biol. 267:727-748.
    • (1997) J. Mol. Biol. , vol.267 , pp. 727-748
    • Jones, G.1    Willet, P.2    Glen, R.3    Leach, A.4    Taylor, R.5
  • 24
    • 0038007927 scopus 로고    scopus 로고
    • Selection of a thiazole urea-resistant variant of bovine viral diarrhoea virus that maps to the RNA-dependent RNA polymerase
    • King, R. W., H. T. Scarnati, E. S. Priestley, I. De Lucca, A. Bansal, and J. K. Williams. 2002. Selection of a thiazole urea-resistant variant of bovine viral diarrhoea virus that maps to the RNA-dependent RNA polymerase. Antivir. Chem. Chemother. 13:315-323.
    • (2002) Antivir. Chem. Chemother. , vol.13 , pp. 315-323
    • King, R.W.1    Scarnati, H.T.2    Priestley, E.S.3    De Lucca, I.4    Bansal, A.5    Williams, J.K.6
  • 25
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 27
    • 0034864550 scopus 로고    scopus 로고
    • Ribavirin induces error-prone replication of GB virus B in primary tamarin hepatocytes
    • Lanford, R. E., D. Chavez, B. Guerra, J. Y. Lau, Z. Hong, K. M. Brasky, and B. Beames. 2001. Ribavirin induces error-prone replication of GB virus B in primary tamarin hepatocytes. J. Virol. 75:8074-8081.
    • (2001) J. Virol. , vol.75 , pp. 8074-8081
    • Lanford, R.E.1    Chavez, D.2    Guerra, B.3    Lau, J.Y.4    Hong, Z.5    Brasky, K.M.6    Beames, B.7
  • 28
    • 0035811625 scopus 로고    scopus 로고
    • Hepatitis C virus infection
    • Lauer, G. M., and B. D. Walker. 2001. Hepatitis C virus infection. N. Engl. J. Med. 345:41-52.
    • (2001) N. Engl. J. Med. , vol.345 , pp. 41-52
    • Lauer, G.M.1    Walker, B.D.2
  • 29
    • 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., M. B. Cable, E. Ferrari, Z. Hong, A. F. Mannarino, and P. C. Weber. 1999. Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site. Nat. Struct. Biol. 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
  • 30
    • 0033046398 scopus 로고    scopus 로고
    • Detection and genotyping of bovine diarrhea virus by reverse transcription-polymerase chain amplification of the 5′ untranslated region
    • Letellier, C., P. Kerkhofs, G. Wellemans, and E. Vanopdenbosch. 1999. Detection and genotyping of bovine diarrhea virus by reverse transcription-polymerase chain amplification of the 5′ untranslated region. Vet. Microbiol. 64:155-167.
    • (1999) Vet. Microbiol. , vol.64 , pp. 155-167
    • Letellier, C.1    Kerkhofs, P.2    Wellemans, G.3    Vanopdenbosch, E.4
  • 31
    • 0000163169 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • D. M. Knipe, P. M. Howley, D. E. Griffin, M. A. Martin, R. A. Lamb, B. Roizman, and S. E. Straus (ed.). Lippincott Williams & Wilkins, Philadelphia, Pa.
    • Lindenbach, B. D., and C. M. Rice. 2001. Flaviviridae: the viruses and their replication, p. 991-1041. In D. M. Knipe, P. M. Howley, D. E. Griffin, M. A. Martin, R. A. Lamb, B. Roizman, and S. E. Straus (ed.), Fields virology. Lippincott Williams & Wilkins, Philadelphia, Pa.
    • (2001) Fields Virology , pp. 991-1041
    • Lindenbach, B.D.1    Rice, C.M.2
  • 34
    • 0028304962 scopus 로고
    • Satisfying Hydrogen bonding potential in proteins
    • McDonald, I., and J. Thornston. 1994. Satisfying Hydrogen bonding potential in proteins. J. Mol. Biol. 238:777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.1    Thornston, J.2
  • 35
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D photorealistic molecular graphics
    • Merritt, E. 1997. Raster3D photorealistic molecular graphics. Methods Enzymol. 277:505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.1
  • 37
    • 0029633186 scopus 로고
    • AMBER, a computer program for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to elucidate the structures and energies of molecules
    • Pearlman, D., D. Case, J. Caldwell, W. Ross, T. Cheatham, S. DeBolt, D. Ferguson, G. Seibel, and P. Kollman. 1995. AMBER, a computer program for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to elucidate the structures and energies of molecules. Comp. Phys. Commun. 91:1-41.
    • (1995) Comp. Phys. Commun. , vol.91 , pp. 1-41
    • Pearlman, D.1    Case, D.2    Caldwell, J.3    Ross, W.4    Cheatham, T.5    Debolt, S.6    Ferguson, D.7    Seibel, G.8    Kollman, P.9
  • 38
    • 0347457077 scopus 로고    scopus 로고
    • Modulation of the hepatitis C virus RNA-dependent RNA polymerase activity by the non-structural (NS) 3 helicase and the NS4B membrane protein
    • Piccininni, S., A. Varaklioti, M. Nardelli, B. Dave, K. D. Raney, and J. E. McCarthy. 2002. Modulation of the hepatitis C virus RNA-dependent RNA polymerase activity by the non-structural (NS) 3 helicase and the NS4B membrane protein. J. Biol. Chem. 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.6
  • 39
    • 0034812103 scopus 로고    scopus 로고
    • The hepatitis C virus replicon system and its application to molecular studies
    • Pietschmann, T., and R. Bartenschlager. 2001. The hepatitis C virus replicon system and its application to molecular studies. Curr. Opin. Drug Discov. Dev. 4:657-664.
    • (2001) Curr. Opin. Drug Discov. Dev. , vol.4 , pp. 657-664
    • Pietschmann, T.1    Bartenschlager, R.2
  • 40
    • 33646016356 scopus 로고    scopus 로고
    • note
    • Reference deleted.
  • 41
    • 33745158157 scopus 로고
    • A simple method of estimating fifty percent endpoints
    • Reed, L. J., and A. H. Muench. 1938. A simple method of estimating fifty percent endpoints. Am. J. Hyg. 27:493-497.
    • (1938) Am. J. Hyg. , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, A.H.2
  • 43
    • 33646010717 scopus 로고    scopus 로고
    • note
    • Reference deleted.
  • 49
    • 0042591335 scopus 로고    scopus 로고
    • Architecture of the flaviviral replication complex. Protease, nuclease, and detergents reveal encasement within double-layered membrane compartments
    • Uchil, P. D., and V. Satchidanandam. 2003. Architecture of the flaviviral replication complex. Protease, nuclease, and detergents reveal encasement within double-layered membrane compartments. J. Biol. Chem. 278:24388-24398.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24388-24398
    • Uchil, P.D.1    Satchidanandam, V.2
  • 50
    • 0034715307 scopus 로고    scopus 로고
    • Bovine viral diarrhea virus induced apoptosis correlates with increased intracellular viral RNA accumulation
    • Vassilev, V. B., and R. O. Donis. 2000. Bovine viral diarrhea virus induced apoptosis correlates with increased intracellular viral RNA accumulation. Virus Res. 69:95-107.
    • (2000) Virus Res. , vol.69 , pp. 95-107
    • Vassilev, V.B.1    Donis, R.O.2
  • 52
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A., R. Laskowski, and J. Thornton. 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.1    Laskowski, R.2    Thornton, J.3
  • 53
  • 54
    • 84988053694 scopus 로고
    • An all atom force field for simulations of proteins and nucleic acids
    • Weiner, P., P. Kollman, D. Nguyen, and D. Case. 1986. An all atom force field for simulations of proteins and nucleic acids J. Comput. Chem. 7:230-252.
    • (1986) J. Comput. Chem. , vol.7 , pp. 230-252
    • Weiner, P.1    Kollman, P.2    Nguyen, D.3    Case, D.4
  • 55
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: Using hydrogen atom contacts in the choice of sidechain amide orientation
    • Word, M., S. Lovell, J. Richardson, and D. Richardson. 1999. Asparagine and glutamine: using hydrogen atom contacts in the choice of sidechain amide orientation. J. Mol. Biol. 285:1733-1745.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1733-1745
    • Word, M.1    Lovell, S.2    Richardson, J.3    Richardson, D.4
  • 57
    • 0031686765 scopus 로고    scopus 로고
    • Identification and characterization of an RNA-dependent RNA polymerase activity within the nonstructural protein 5B region of bovine viral diarrhea virus
    • Zhong, W., L. L. Gutshall, and A. M. Del-Vecchio. 1998. Identification and characterization of an RNA-dependent RNA polymerase activity within the nonstructural protein 5B region of bovine viral diarrhea virus. J. Virol. 72:9365-9369.
    • (1998) J. Virol. , vol.72 , pp. 9365-9369
    • Zhong, W.1    Gutshall, L.L.2    Del-Vecchio, A.M.3
  • 58
    • 0032694353 scopus 로고    scopus 로고
    • Imino sugars inhibit the formation and secretion of bovine viral diarrhea virus, a pestivirus model of hepatitis C virus: Implications for the development of broad spectrum anti-hepatitis virus agents
    • Zitzmann, N., A. S. Mehta, S. Carrouee, T. D. Butters, F. M. Platt, J. McCauley, B. S. Blumberg, R. A. Dwek, and T. M. Block. 1999. Imino sugars inhibit the formation and secretion of bovine viral diarrhea virus, a pestivirus model of hepatitis C virus: implications for the development of broad spectrum anti-hepatitis virus agents. Proc. Natl. Acad. Sci. USA 96:11878-11882.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11878-11882
    • Zitzmann, N.1    Mehta, A.S.2    Carrouee, S.3    Butters, T.D.4    Platt, F.M.5    McCauley, J.6    Blumberg, B.S.7    Dwek, R.A.8    Block, T.M.9


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