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Volumn 1820, Issue 10, 2012, Pages 1526-1534

Understanding the drug resistance mechanism of hepatitis C virus NS3/4A to ITMN-191 due to R155K, A156V, D168A/E mutations: A computational study

Author keywords

Drug resistance; Hepatitis C virus; ITMN 191; Molecular dynamics simulation; NS3 4A protease

Indexed keywords

DANOPREVIR; NONSTRUCTURAL PROTEIN 3; NONSTRUCTURAL PROTEIN 4A;

EID: 84863438978     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2012.06.001     Document Type: Article
Times cited : (34)

References (45)
  • 1
    • 84875380538 scopus 로고    scopus 로고
    • World Health Organization
    • World Health Organization Media centre Hepatitis C Fact sheet N°164 http://www.who.int/mediacentre/factsheets/fs164/en/ 2011
    • (2011) Media Centre Hepatitis C Fact Sheet N°164
  • 3
    • 0024509701 scopus 로고
    • Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome
    • Q.L. Choo, G. Kuo, A.J. Weiner, L.R. Overby, D.W. Bradley, and M. Houghton Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome Science 244 1989 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
  • 4
  • 8
    • 77952060993 scopus 로고    scopus 로고
    • Hepatitis C: An unsuspected drug target
    • C.L. Murray, and C.M. Rice Hepatitis C: an unsuspected drug target Nature 465 2010 42 44
    • (2010) Nature , vol.465 , pp. 42-44
    • Murray, C.L.1    Rice, C.M.2
  • 9
    • 0033920304 scopus 로고    scopus 로고
    • Hepatitis C virus-encoded enzymatic activities and conserved RNA elements in the 3′ nontranslated region are essential for virus replication in vivo
    • A.A. Kolykhalov, K. Mihalik, S.M. Feinstone, and C.M. Rice Hepatitis C virus-encoded enzymatic activities and conserved RNA elements in the 3′ nontranslated region are essential for virus replication in vivo J. Virol. 74 2000 2046 2051
    • (2000) J. Virol. , vol.74 , pp. 2046-2051
    • Kolykhalov, A.A.1    Mihalik, K.2    Feinstone, S.M.3    Rice, C.M.4
  • 10
    • 33745788149 scopus 로고    scopus 로고
    • Future therapies for hepatitis C
    • J.M. Pawlotsky, and R.G. Gish Future therapies for hepatitis C Antivir. Ther. 11 2006 397 408
    • (2006) Antivir. Ther. , vol.11 , pp. 397-408
    • Pawlotsky, J.M.1    Gish, R.G.2
  • 11
    • 0242456017 scopus 로고    scopus 로고
    • Subcellular localization, stability, and trans-cleavage competence of he hepatitis C virus NS3-NS4A complex expressed in tetracycline-regulated cell lines
    • B. Wolk, D. Sansonno, H.G. Krausslich, F. Dammacco, C.M. Rice, H.E. Blum, and D. Moradpour Subcellular localization, stability, and trans-cleavage competence of he hepatitis C virus NS3-NS4A complex expressed in tetracycline-regulated cell lines J. Virol. 74 2000 2293 2304
    • (2000) J. Virol. , vol.74 , pp. 2293-2304
    • Wolk, B.1    Sansonno, D.2    Krausslich, H.G.3    Dammacco, F.4    Rice, C.M.5    Blum, H.E.6    Moradpour, D.7
  • 12
    • 0031780867 scopus 로고    scopus 로고
    • The NS5A/NS5 proteins of viruses from three genera of the family flaviviridae are phosphorylated by associated serine/threonine kinases
    • K.E. Reed, A.E. Gorbalenya, and C.M. Rice The NS5A/NS5 proteins of viruses from three genera of the family flaviviridae are phosphorylated by associated serine/threonine kinases J. Virol. 72 1998 6199 6206
    • (1998) J. Virol. , vol.72 , pp. 6199-6206
    • Reed, K.E.1    Gorbalenya, A.E.2    Rice, C.M.3
  • 13
    • 0037150679 scopus 로고    scopus 로고
    • Visualization and functional analysis of RNA-dependent RNA polymerase lattices
    • J.M. Lyle, E. Bullitt, K. Bienz, and K. Kirkegaard Visualization and functional analysis of RNA-dependent RNA polymerase lattices Science 296 2002 2218 2222
    • (2002) Science , vol.296 , pp. 2218-2222
    • Lyle, J.M.1    Bullitt, E.2    Bienz, K.3    Kirkegaard, K.4
  • 14
    • 0033571623 scopus 로고    scopus 로고
    • Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase
    • N. Yao, P. Reichert, S.S. Taremi, W.W. Prosise, and P.C. Weber Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase Structure 7 1999 1353 1363
    • (1999) Structure , vol.7 , pp. 1353-1363
    • Yao, N.1    Reichert, P.2    Taremi, S.S.3    Prosise, W.W.4    Weber, P.C.5
  • 16
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • E. Meylan, J. Curran, K. Hofmann, D. Moradpour, M. Binder, R. Bartenschlager, and J. Tschopp Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus Nature 437 2005 1167 1172
    • (2005) Nature , vol.437 , pp. 1167-1172
    • Meylan, E.1    Curran, J.2    Hofmann, K.3    Moradpour, D.4    Binder, M.5    Bartenschlager, R.6    Tschopp, J.7
  • 19
    • 77954974327 scopus 로고    scopus 로고
    • Danoprevir, a small-molecule NS3/4A protease inhibitor for the potential oral treatment of HCV infection
    • M. Deutsch, and G.V. Papatheodoridis Danoprevir, a small-molecule NS3/4A protease inhibitor for the potential oral treatment of HCV infection Curr. Opin. Invest. Drugs 11 2010 951 963
    • (2010) Curr. Opin. Invest. Drugs , vol.11 , pp. 951-963
    • Deutsch, M.1    Papatheodoridis, G.V.2
  • 23
    • 34249884397 scopus 로고    scopus 로고
    • In vitro synergistic antiviral activity of ITMN-191, an orally active inhibitor of the hepatitis C virus (HCV) NS3/4A protease, in combination with Peg-Interferon alfa-2a
    • H. Tan, S. Seiwert, and L. Blatt In vitro synergistic antiviral activity of ITMN-191, an orally active inhibitor of the hepatitis C virus (HCV) NS3/4A protease, in combination with Peg-Interferon alfa-2a Hepatology 44 2006 534A
    • (2006) Hepatology , vol.44
    • Tan, H.1    Seiwert, S.2    Blatt, L.3
  • 24
    • 57049180607 scopus 로고    scopus 로고
    • Generation and characterization of HCV replicons with reduced sensitivity to ITMN 191, a macrocyclic inhibitor of NS3/4A
    • S. Seiwert, S. Andrews, H. Tan, K. Condroski, J. Ballard, B. Bernat, J. Josey, and L. Blatt Generation and characterization of HCV replicons with reduced sensitivity to ITMN 191, a macrocyclic inhibitor of NS3/4A Gastroenterology 130 2006
    • (2006) Gastroenterology , vol.130
    • Seiwert, S.1    Andrews, S.2    Tan, H.3    Condroski, K.4    Ballard, J.5    Bernat, B.6    Josey, J.7    Blatt, L.8
  • 25
    • 78650481557 scopus 로고    scopus 로고
    • Drug resistance against HCV NS3/4A inhibitors is defined by the balance of substrate recognition versus inhibitor binding
    • K.P. Romano, A. Ali, W.E. Royer, and C.A. Schiffer Drug resistance against HCV NS3/4A inhibitors is defined by the balance of substrate recognition versus inhibitor binding Proc. Natl. Acad. Sci. U. S. A. 107 2010 20986
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 20986
    • Romano, K.P.1    Ali, A.2    Royer, W.E.3    Schiffer, C.A.4
  • 28
    • 77953267929 scopus 로고    scopus 로고
    • In silico identification of the potential drug resistance sites over 2009 influenza A (H1N1) virus neuraminidase
    • H. Liu, X. Yao, C. Wang, and J. Han In silico identification of the potential drug resistance sites over 2009 influenza A (H1N1) virus neuraminidase Mol. Pharm. 7 2010 894 904
    • (2010) Mol. Pharm. , vol.7 , pp. 894-904
    • Liu, H.1    Yao, X.2    Wang, C.3    Han, J.4
  • 29
    • 79952588669 scopus 로고    scopus 로고
    • Assessing the performance of the MM/PBSA and MM/GBSA methods. 1. The accuracy of binding free energy calculations based on molecular dynamics simulations
    • T. Hou, J. Wang, Y. Li, and W. Wang Assessing the performance of the MM/PBSA and MM/GBSA methods. 1. The accuracy of binding free energy calculations based on molecular dynamics simulations J. Chem. Inf. Model. 51 2011 69 82
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 69-82
    • Hou, T.1    Wang, J.2    Li, Y.3    Wang, W.4
  • 30
    • 33947644064 scopus 로고    scopus 로고
    • Molecular dynamics and free energy studies on the wild-type and double mutant HIV-1 protease complexed with amprenavir and two amprenavir-related inhibitors: Mechanism for binding and drug resistance
    • T. Hou, and R. Yu Molecular dynamics and free energy studies on the wild-type and double mutant HIV-1 protease complexed with amprenavir and two amprenavir-related inhibitors: mechanism for binding and drug resistance J. Med. Chem. 50 2007 1177 1188
    • (2007) J. Med. Chem. , vol.50 , pp. 1177-1188
    • Hou, T.1    Yu, R.2
  • 31
    • 69949105160 scopus 로고    scopus 로고
    • Characterization of temperature dependent and substrate-binding cleft movements in Bacillus circulans family 11 xylanase: A molecular dynamics investigation
    • D.S. Vieira, L. Degreve, and R.J. Ward Characterization of temperature dependent and substrate-binding cleft movements in Bacillus circulans family 11 xylanase: a molecular dynamics investigation Biochim. Biophys. Acta 1790 2009 1301 1306
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 1301-1306
    • Vieira, D.S.1    Degreve, L.2    Ward, R.J.3
  • 32
  • 36
    • 2442480826 scopus 로고    scopus 로고
    • Distinguish protein decoys by using a scoring function based on a new AMBER force field, short molecular dynamics simulations, and the generalized born solvent model
    • M.C. Lee, and Y. Duan Distinguish protein decoys by using a scoring function based on a new AMBER force field, short molecular dynamics simulations, and the generalized born solvent model Proteins 55 2004 620 634
    • (2004) Proteins , vol.55 , pp. 620-634
    • Lee, M.C.1    Duan, Y.2
  • 40
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • J.-P. Ryckaert, G. Ciccotti, and H.J.C. Berendsen Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes J. Comput. Phys. 23 1977 327 341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 42
    • 0032560959 scopus 로고    scopus 로고
    • Continuum solvent studies of the stability of DNA, RNA, and phosphoramidate-DNA helices
    • J. Srinivasan, T.E. Cheatham, P. Cieplak, P.A. Kollman, and D.A. Case Continuum solvent studies of the stability of DNA, RNA, and phosphoramidate-DNA helices J. Am. Chem. Soc. 120 1998 9401 9409
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9401-9409
    • Srinivasan, J.1    Cheatham, T.E.2    Cieplak, P.3    Kollman, P.A.4    Case, D.A.5
  • 43
    • 32844457567 scopus 로고
    • Accurate calculation of hydration free energies using macroscopic solvent models
    • D. Sitkoff, K.A. Sharp, and B. Honig Accurate calculation of hydration free energies using macroscopic solvent models J. Phys. Chem. 98 1994 1978 1988
    • (1994) J. Phys. Chem. , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 44
    • 76249112547 scopus 로고    scopus 로고
    • Fast and accurate predictions of binding free energies using MM-PBSA and MM-GBSA
    • G. Rastelli, A. Del Rio, G. Degliesposti, and M. Sgobba Fast and accurate predictions of binding free energies using MM-PBSA and MM-GBSA J. Comput. Chem. 31 2010 797 810
    • (2010) J. Comput. Chem. , vol.31 , pp. 797-810
    • Rastelli, G.1    Del Rio, A.2    Degliesposti, G.3    Sgobba, M.4


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