메뉴 건너뛰기




Volumn 11, Issue 7, 2006, Pages 847-855

Resistance of hepatitis C virus to NS3-4A protease inhibitors: Mechanisms of drug resistance induced by R155Q, A156T, D168A and D168V mutations

Author keywords

[No Author keywords available]

Indexed keywords

CILUPREVIR; MONTIRELIN; PROTEINASE INHIBITOR;

EID: 33750947650     PISSN: 13596535     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (49)

References (49)
  • 1
    • 0035934568 scopus 로고    scopus 로고
    • Peginterferon alfa-2b plus ribavirin compared with interferon alfa-2b plus ribavirin for initial treatment of chronic hepatitis C: A randomised trial
    • Manns MP, McHutchison JG, Gordon SC, et al. Peginterferon alfa-2b plus ribavirin compared with interferon alfa-2b plus ribavirin for initial treatment of chronic hepatitis C: a randomised 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
  • 2
    • 0037179698 scopus 로고    scopus 로고
    • Peginterferon alfa-2a plus ribavirin for chronic hepatitis C virus infection
    • Fried MW, Shiffman ML, Reddy KR, et al. Peginterferon alfa-2a plus ribavirin for chronic hepatitis C virus infection. N Engl J Med 2002; 347:975-982.
    • (2002) N Engl J Med , vol.347 , pp. 975-982
    • Fried, M.W.1    Shiffman, M.L.2    Reddy, K.R.3
  • 3
    • 1542378867 scopus 로고    scopus 로고
    • Peginterferon-alpha2a and ribavirin combination therapy in chronic hepatitis C: A randomized study of treatment duration and ribavirin dose
    • Hadziyannis SJ, Sette H, Jr, Morgan TR, et al. Peginterferon-alpha2a and ribavirin combination therapy in chronic hepatitis C: a randomized study of treatment duration and ribavirin dose. Ann Intern Med 2004; 140:346-355.
    • (2004) Ann Intern Med , vol.140 , pp. 346-355
    • Hadziyannis, S.J.1    Sette Jr., H.2    Morgan, T.R.3
  • 4
    • 0036250277 scopus 로고    scopus 로고
    • Incidence of side effects during therapy with different types of alpha interferon: A randomised controlled trial comparing recombinant alpha 2b versus leukocyte interferon in the therapy of naive patients with chronic hepatitis C
    • Ascione A, De Luca M, Di Costanzo GG, et al. Incidence of side effects during therapy with different types of alpha interferon: a randomised controlled trial comparing recombinant alpha 2b versus leukocyte interferon in the therapy of naive patients with chronic hepatitis C. Curr Pharm Des 2002; 8:977-980.
    • (2002) Curr Pharm Des , vol.8 , pp. 977-980
    • Ascione, A.1    De Luca, M.2    Di Costanzo, G.G.3
  • 5
    • 0037308288 scopus 로고    scopus 로고
    • Adherence and mental side effects during hepatitis C treatment with interferon alfa and ribavirin in psychiatric risk groups
    • Schaefer M, Schmidt F, Folwaczny C, et al. Adherence and mental side effects during hepatitis C treatment with interferon alfa and ribavirin in psychiatric risk groups. Hepatology 2003; 37:443-451.
    • (2003) Hepatology , vol.37 , pp. 443-451
    • Schaefer, M.1    Schmidt, F.2    Folwaczny, C.3
  • 6
    • 19944386924 scopus 로고    scopus 로고
    • Pegylated versus standard interferon-alpha in antiviral regimens for post-transplant recurrent hepatitis C: Comparison of tolerability and efficacy
    • Toniutto P, Fabris C, Fumo E, et al. Pegylated versus standard interferon-alpha in antiviral regimens for post-transplant recurrent hepatitis C: Comparison of tolerability and efficacy. J Gastroenterol Hepatol 2005; 20:577-582.
    • (2005) J Gastroenterol Hepatol , vol.20 , pp. 577-582
    • Toniutto, P.1    Fabris, C.2    Fumo, E.3
  • 7
    • 25444466243 scopus 로고    scopus 로고
    • The impact of haematopoietic growth factors on the management and efficacy of antiviral treatment in patients with hepatitis C virus
    • Lebray P, Nalpas B, Vallet-Pichard A, et al. The impact of haematopoietic growth factors on the management and efficacy of antiviral treatment in patients with hepatitis C virus. Antivir Ther 2005; 10:769-776.
    • (2005) Antivir Ther , vol.10 , pp. 769-776
    • Lebray, P.1    Nalpas, B.2    Vallet-Pichard, A.3
  • 8
    • 0028820118 scopus 로고
    • Complex formation between the NS3 serine-type proteinase of the hepatitis C virus and NS4A and its importance for polyprotein maturation
    • Bartenschlager R, Lohmann V, Wilkinson T, Koch JO. Complex formation between the NS3 serine-type proteinase of the hepatitis C virus and NS4A and its importance for polyprotein maturation. J Virol 1995; 69:7519-7528.
    • (1995) J Virol , vol.69 , pp. 7519-7528
    • Bartenschlager, R.1    Lohmann, V.2    Wilkinson, T.3    Koch, J.O.4
  • 9
    • 0033571623 scopus 로고    scopus 로고
    • Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase
    • Yao N, Reichert P, Taremi SS, Prosise WW, Weber PC. Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase. Structure 1999; 7:1353-1363.
    • (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
  • 10
    • 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
  • 11
    • 23944485662 scopus 로고    scopus 로고
    • Evasion of intracellular host defence by hepatitis C virus
    • Gale M, Jr., Foy EM. Evasion of intracellular host defence by hepatitis C virus. Nature 2005; 436:939-945.
    • (2005) Nature , vol.436 , pp. 939-945
    • Gale Jr., M.1    Foy, E.M.2
  • 12
    • 14544280209 scopus 로고    scopus 로고
    • Immune evasion by hepatitis C virus NS3/4A protease-mediated cleavage of the Toll-like receptor 3 adaptor protein TRIF
    • Li K, Foy E, Ferreon JC, et al. Immune evasion by hepatitis C virus NS3/4A protease-mediated cleavage of the Toll-like receptor 3 adaptor protein TRIF. Proc Natl Acad Sci USA 2005; 102:2992-2997.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 2992-2997
    • Li, K.1    Foy, E.2    Ferreon, J.C.3
  • 13
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • Meylan E, Curran J, Hofmann K, et al. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature 2005; 437:1167-1172.
    • (2005) Nature , vol.437 , pp. 1167-1172
    • Meylan, E.1    Curran, J.2    Hofmann, K.3
  • 14
    • 0037687422 scopus 로고    scopus 로고
    • Regulation of interferon regulatory factor-3 by the hepatitis C virus serine protease
    • Foy E, Li K, Wang C, et al. Regulation of interferon regulatory factor-3 by the hepatitis C virus serine protease. Science 2003; 300:1145-1148.
    • (2003) Science , vol.300 , pp. 1145-1148
    • Foy, E.1    Li, K.2    Wang, C.3
  • 15
    • 0344201903 scopus 로고    scopus 로고
    • An NS3 protease inhibitor with antiviral effects in humans infected with hepatitis C virus
    • Lamarre D, Anderson PC, Bailey M, et al. An NS3 protease inhibitor with antiviral effects in humans infected with hepatitis C virus. Nature 2003; 426:186-189.
    • (2003) Nature , vol.426 , pp. 186-189
    • Lamarre, D.1    Anderson, P.C.2    Bailey, M.3
  • 16
    • 27744529265 scopus 로고    scopus 로고
    • In vitro studies of cross-resistance mutations against two hepatitis C virus serine protease inhibitors, VX-950 and BILN 2061
    • Lin C, Gates CA, Rao BG, et al. In vitro studies of cross-resistance mutations against two hepatitis C virus serine protease inhibitors, VX-950 and BILN 2061. J Biol Chem 2005; 280:36784-36791.
    • (2005) J Biol Chem , vol.280 , pp. 36784-36791
    • Lin, C.1    Gates, C.A.2    Rao, B.G.3
  • 17
    • 2342420348 scopus 로고    scopus 로고
    • In vitro resistance studies of hepatitis C virus serine protease inhibitors, VX-950 and BILN 2061: Structural analysis indicates different resistance mechanisms
    • Lin C, Lin K, Luong YP, et al. In vitro resistance studies of hepatitis C virus serine protease inhibitors, VX-950 and BILN 2061: structural analysis indicates different resistance mechanisms. J Biol Chem 2004; 279:17508-17514.
    • (2004) J Biol Chem , vol.279 , pp. 17508-17514
    • Lin, C.1    Lin, K.2    Luong, Y.P.3
  • 18
    • 33646369669 scopus 로고    scopus 로고
    • Mutations conferring resistance to SCH6, a novel hepatitis C virus NS3/4A protease inhibitor: Reduced RNA replication fitness and partial rescue by second-site mutations
    • Yi M, Tong X, Skelton A, et al. Mutations conferring resistance to SCH6, a novel hepatitis C virus NS3/4A protease inhibitor: Reduced RNA replication fitness and partial rescue by second-site mutations. J Biol Chem 2006 281:8205-8215.
    • (2006) J Biol Chem , vol.281 , pp. 8205-8215
    • Yi, M.1    Tong, X.2    Skelton, A.3
  • 19
    • 20444376886 scopus 로고    scopus 로고
    • Confronting the emergence of drug-resistant HIV type 1: Impact of antiretroviral therapy on individual and population resistance
    • Daar ES, Richman DD. Confronting the emergence of drug-resistant HIV type 1: impact of antiretroviral therapy on individual and population resistance. AIDS Res Hum Retroviruses 2005; 21:343-357.
    • (2005) AIDS Res Hum Retroviruses , vol.21 , pp. 343-357
    • Daar, E.S.1    Richman, D.D.2
  • 20
    • 3242879168 scopus 로고    scopus 로고
    • Structural determinants and molecular mechanisms for the resistance of HIV-1 RT to nucleoside analogues
    • Deval J, Courcambeck J, Selmi B, Boretto J, Canard B. Structural determinants and molecular mechanisms for the resistance of HIV-1 RT to nucleoside analogues. Curr Drug Metab 2004; 5:305-316.
    • (2004) Curr Drug Metab , vol.5 , pp. 305-316
    • Deval, J.1    Courcambeck, J.2    Selmi, B.3    Boretto, J.4    Canard, B.5
  • 21
    • 3042855671 scopus 로고    scopus 로고
    • The influence of protease inhibitor resistance profiles on selection of HIV therapy in treatment-naive patients
    • Turner D, Schapiro JM, Brenner BG, Wainberg MA. The influence of protease inhibitor resistance profiles on selection of HIV therapy in treatment-naive patients. Antivir Ther 2004; 9:301-314.
    • (2004) Antivir Ther , vol.9 , pp. 301-314
    • Turner, D.1    Schapiro, J.M.2    Brenner, B.G.3    Wainberg, M.A.4
  • 22
    • 2342433984 scopus 로고    scopus 로고
    • Comparisons of the HBV and HIV polymerase, and antiviral resistance mutations
    • Bartholomeusz A, Tehan BG, Chalmers DK. Comparisons of the HBV and HIV polymerase, and antiviral resistance mutations. Antivir Ther 2004; 9:149-160.
    • (2004) Antivir Ther , vol.9 , pp. 149-160
    • Bartholomeusz, A.1    Tehan, B.G.2    Chalmers, D.K.3
  • 23
    • 30344458192 scopus 로고    scopus 로고
    • Cellular and virological mechanisms of HBV drug resistance
    • Locarnini S, Mason WS. Cellular and virological mechanisms of HBV drug resistance. J Hepatol 2006; 44:422-431.
    • (2006) J Hepatol , vol.44 , pp. 422-431
    • Locarnini, S.1    Mason, W.S.2
  • 24
    • 24044526915 scopus 로고    scopus 로고
    • Cross-resistance testing of next-generation nucleoside and nucleotide analogues against lamivudine-resistant HBV
    • Yang H, Qi X, Sabogal A, et al. Cross-resistance testing of next-generation nucleoside and nucleotide analogues against lamivudine-resistant HBV. Antivir Ther 2005; 10:625-633.
    • (2005) Antivir Ther , vol.10 , pp. 625-633
    • Yang, H.1    Qi, X.2    Sabogal, A.3
  • 25
    • 0037264227 scopus 로고    scopus 로고
    • Herpes simplex virus resistance to antiviral drugs
    • Morfin F, Thouvenot D. Herpes simplex virus resistance to antiviral drugs. J Clin Virol 2003; 26:29-37.
    • (2003) J Clin Virol , vol.26 , pp. 29-37
    • Morfin, F.1    Thouvenot, D.2
  • 26
    • 1542349069 scopus 로고    scopus 로고
    • Sequential switching of DNA polymerase and thymidine kinase-mediated HSV-1 drug resistance in an immunocompromised child
    • Stranska R, van Loon AM, Bredius RG, et al. Sequential switching of DNA polymerase and thymidine kinase-mediated HSV-1 drug resistance in an immunocompromised child. Antivir Ther 2004; 9:97-104.
    • (2004) Antivir Ther , vol.9 , pp. 97-104
    • Stranska, R.1    Van Loon, A.M.2    Bredius, R.G.3
  • 27
    • 0037303608 scopus 로고    scopus 로고
    • Amino acid changes within conserved region III of the herpes simplex virus and human cytomegalovirus DNA polymerases confer resistance to 4-oxo-dihydroquinolines, a novel class of herpesvirus antiviral agents
    • Thomsen DR, Oien NL, Hopkins TA, et al. Amino acid changes within conserved region III of the herpes simplex virus and human cytomegalovirus DNA polymerases confer resistance to 4-oxo-dihydroquinolines, a novel class of herpesvirus antiviral agents. J Virol 2003; 77:1868-1876.
    • (2003) J Virol , vol.77 , pp. 1868-1876
    • Thomsen, D.R.1    Oien, N.L.2    Hopkins, T.A.3
  • 28
    • 23944482649 scopus 로고    scopus 로고
    • Challenges and successes in developing new therapies for hepatitis C
    • De Francesco R, Migliaccio G. Challenges and successes in developing new therapies for hepatitis C. Nature 2005; 436:953-960.
    • (2005) Nature , vol.436 , pp. 953-960
    • De Francesco, R.1    Migliaccio, G.2
  • 29
    • 27844600612 scopus 로고    scopus 로고
    • Opinion paper. Resistance to new anti-HIV agents: Problems in the pathway of drug registration
    • Dalmau D, Klimkait T, Telenti A. Opinion paper. Resistance to new anti-HIV agents: problems in the pathway of drug registration. Antivir Ther 2005; 10:867-872.
    • (2005) Antivir Ther , vol.10 , pp. 867-872
    • Dalmau, D.1    Klimkait, T.2    Telenti, A.3
  • 30
    • 0037333918 scopus 로고    scopus 로고
    • In vitro selection and characterization of hepatitis C virus serine protease variants resistant to an active-site peptide inhibitor
    • Trozzi C, Bartholomew L, Ceccacci A, et al. In vitro selection and characterization of hepatitis C virus serine protease variants resistant to an active-site peptide inhibitor. J Virol 2003; 77:3669-3679.
    • (2003) J Virol , vol.77 , pp. 3669-3679
    • Trozzi, C.1    Bartholomew, L.2    Ceccacci, A.3
  • 31
    • 1542677267 scopus 로고    scopus 로고
    • Characterization of resistance to non-obligate chain-terminating ribonucleoside analogs that inhibit hepatitis C virus replication in vitro
    • Migliaccio G, Tomassini JE, Carroll SS, et al. Characterization of resistance to non-obligate chain-terminating ribonucleoside analogs that inhibit hepatitis C virus replication in vitro. J Biol Chem 2003; 278:49164-49170.
    • (2003) J Biol Chem , vol.278 , pp. 49164-49170
    • Migliaccio, G.1    Tomassini, J.E.2    Carroll, S.S.3
  • 32
    • 0242290994 scopus 로고    scopus 로고
    • Resistance profile of a hepatitis C virus RNA-dependent RNA polymerase benzothiadiazine inhibitor
    • Nguyen TT, Gates AT, Gutshall LL, et al. Resistance profile of a hepatitis C virus RNA-dependent RNA polymerase benzothiadiazine inhibitor. Antimicrob Agents Chemother 2003; 47:3525-3530.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 3525-3530
    • Nguyen, T.T.1    Gates, A.T.2    Gutshall, L.L.3
  • 33
    • 2542467813 scopus 로고    scopus 로고
    • Mutations conferring resistance to a potent hepatitis C virus serine protease inhibitor in vitro
    • Lu L, Pilot-Matias TJ, Stewart KD, et al. Mutations conferring resistance to a potent hepatitis C virus serine protease inhibitor in vitro. Antimicrob Agents Chemother 2004; 48:2260-2266.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 2260-2266
    • Lu, L.1    Pilot-Matias, T.J.2    Stewart, K.D.3
  • 34
    • 33750940852 scopus 로고    scopus 로고
    • Molecular mechanism susceptibility profile of BILN-2061 to various hepatitis C virus genotypes and NS3-NS4A protease mutations: D168A and D168V
    • 29 October-2 November. Abstract 513
    • Courcambeck J, Perbost R, Chabaud P, et al. Molecular mechanism susceptibility profile of BILN-2061 to various hepatitis C virus genotypes and NS3-NS4A protease mutations: D168A and D168V. 55th Annual Meeting of the American Association for the Study of Liver Diseases. 29 October-2 November 2004. Abstract 513.
    • (2004) 55th Annual Meeting of the American Association for the Study of Liver Diseases
    • Courcambeck, J.1    Perbost, R.2    Chabaud, P.3
  • 35
    • 0034629363 scopus 로고    scopus 로고
    • Inhibition of the hepatitis C virus NS3/4A protease. The crystal structures of two protease-inhibitor complexes
    • Di Marco S, Rizzi M, Volpari C, et al. Inhibition of the hepatitis C virus NS3/4A protease. The crystal structures of two protease-inhibitor complexes. J Biol Chem 2000; 275:7152-7157.
    • (2000) J Biol Chem , vol.275 , pp. 7152-7157
    • Di Marco, S.1    Rizzi, M.2    Volpari, C.3
  • 36
    • 3142700044 scopus 로고    scopus 로고
    • Sensitivity of NS3 serine proteases from hepatitis C virus genotypes 2 and 3 to the inhibitor BILN 2061
    • Thibeault D, Bousquet C, Gingras R, et al. Sensitivity of NS3 serine proteases from hepatitis C virus genotypes 2 and 3 to the inhibitor BILN 2061. J Virol 2004; 78:7352-7359.
    • (2004) J Virol , vol.78 , pp. 7352-7359
    • Thibeault, D.1    Bousquet, C.2    Gingras, R.3
  • 37
    • 0037210253 scopus 로고    scopus 로고
    • Hydration free energy a fragmental model and drug design
    • Pepe G, Guiliani G, Loustalet S, Halfon P. Hydration free energy a fragmental model and drug design. Eur J Med Chem 2002; 37:865-872.
    • (2002) Eur J Med Chem , vol.37 , pp. 865-872
    • Pepe, G.1    Guiliani, G.2    Loustalet, S.3    Halfon, P.4
  • 38
    • 0347052875 scopus 로고    scopus 로고
    • Mechanistic basis for reduced viral and enzymatic fitness of HIV-1 reverse transcriptase containing both K65R and M184V mutations
    • Deval J, White KL, Miller MD, et al. Mechanistic basis for reduced viral and enzymatic fitness of HIV-1 reverse transcriptase containing both K65R and M184V mutations. J Biol Chem 2004; 279:509-516.
    • (2004) J Biol Chem , vol.279 , pp. 509-516
    • Deval, J.1    White, K.L.2    Miller, M.D.3
  • 39
    • 0011907937 scopus 로고
    • Surface electrostatic potentials on macromolecules in a monopole approximation: A computer program and an application to cytochromes
    • Pepe G, Seres B, Laporte D, Del Re C. Surface electrostatic potentials on macromolecules in a monopole approximation: A computer program and an application to cytochromes. J Theor Biol 1985; 115:571-593.
    • (1985) J Theor Biol , vol.115 , pp. 571-593
    • Pepe, G.1    Seres, B.2    Laporte, D.3    Del Re, C.4
  • 40
    • 0343285634 scopus 로고
    • GENMOL. A fast program for molecular modeling. Application to the determination of the psychotonic or sedative effect of tricyclic antidepressant drugs
    • Pepe G, Siri D. GENMOL. A fast program for molecular modeling. Application to the determination of the psychotonic or sedative effect of tricyclic antidepressant drugs. Stud Phys Theor Chem 1990; 71:93-101.
    • (1990) Stud Phys Theor Chem , vol.71 , pp. 93-101
    • Pepe, G.1    Siri, D.2
  • 41
    • 2642590958 scopus 로고    scopus 로고
    • Complex of NS3 protease and NS4A peptide of BK strain hepatitis C virus: A 2.2 A resolution structure in a hexagonal crystal form
    • Yan Y, Li Y, Munshi S, et al. Complex of NS3 protease and NS4A peptide of BK strain hepatitis C virus: a 2.2 A resolution structure in a hexagonal crystal form. Protein Sci 1998; 7:837-847.
    • (1998) Protein Sci , vol.7 , pp. 837-847
    • Yan, Y.1    Li, Y.2    Munshi, S.3
  • 42
    • 0037471233 scopus 로고    scopus 로고
    • Macrocyclic inhibitors of the NS3 protease as potential therapeutic agents of hepatitis C virus infection
    • Tsantrizos YS, Bolger G, Bonneau P, et al. Macrocyclic inhibitors of the NS3 protease as potential therapeutic agents of hepatitis C virus infection. Angew Chem Int Ed Engl 2003; 42:1356-1360.
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 1356-1360
    • Tsantrizos, Y.S.1    Bolger, G.2    Bonneau, P.3
  • 43
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 1993; 26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 44
    • 0034616958 scopus 로고    scopus 로고
    • The role of steric hindrance in 3TC resistance of human immunodeficiency virus type-1 reverse transcriptase
    • Gao HQ, Boyer PL, Sarafianos SG, Arnold E, Hughes SH. The role of steric hindrance in 3TC resistance of human immunodeficiency virus type-1 reverse transcriptase. J Mol Biol 2000; 300:403-418.
    • (2000) J Mol Biol , vol.300 , pp. 403-418
    • Gao, H.Q.1    Boyer, P.L.2    Sarafianos, S.G.3    Arnold, E.4    Hughes, S.H.5
  • 45
    • 0033621167 scopus 로고    scopus 로고
    • Lamivudine (3TC) resistance in HIV-1 reverse transcriptase involves steric hindrance with beta-branched amino acids
    • Sarafianos SG, Das K, Clark AD, Jr, et al. Lamivudine (3TC) resistance in HIV-1 reverse transcriptase involves steric hindrance with beta-branched amino acids. Proc Natl Acad Sci USA 1999; 96:10027-10032.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10027-10032
    • Sarafianos, S.G.1    Das, K.2    Clark Jr., A.D.3
  • 46
    • 33750930732 scopus 로고    scopus 로고
    • Molecular susceptibility profil of BILN-2061 for common HCV genotypes and NS3-NS4A protease resistance mutations: D168A and D168V
    • Courcambeck J, Perbost R, Chabaud P, et al. Molecular susceptibility profil of BILN-2061 for common HCV genotypes and NS3-NS4A protease resistance mutations: D168A and D168V. Gastroenterol Clin Biol 2004; 28:768.
    • (2004) Gastroenterol Clin Biol , vol.28 , pp. 768
    • Courcambeck, J.1    Perbost, R.2    Chabaud, P.3
  • 47
    • 2942616457 scopus 로고    scopus 로고
    • A loss of viral replicative capacity correlates with altered DNA polymerization kinetics by the human immunodeficiency virus reverse transcriptase bearing the K65R and L74V dideoxynucleoside resistance substitutions
    • Deval J, Navarro JM, Selmi B, et al. A loss of viral replicative capacity correlates with altered DNA polymerization kinetics by the human immunodeficiency virus reverse transcriptase bearing the K65R and L74V dideoxynucleoside resistance substitutions. J Biol Chem 2004; 279:25489-25496.
    • (2004) J Biol Chem , vol.279 , pp. 25489-25496
    • Deval, J.1    Navarro, J.M.2    Selmi, B.3
  • 48
    • 33646036163 scopus 로고    scopus 로고
    • Identification and analysis of fitness of resistance mutations against the HCV protease inhibitor SCH 503034
    • Tong X, Chase R, Skelton A, et al. Identification and analysis of fitness of resistance mutations against the HCV protease inhibitor SCH 503034. Antiviral Res 2006.
    • (2006) Antiviral Res
    • Tong, X.1    Chase, R.2    Skelton, A.3
  • 49
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997; 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.