메뉴 건너뛰기




Volumn 11, Issue 4, 1998, Pages 614-627

Protease inhibitors as antiviral agents

Author keywords

[No Author keywords available]

Indexed keywords

ACICLOVIR; AG 6084; ANALGESIC AGENT; ANTIARRHYTHMIC AGENT; ANTIBIOTIC AGENT; ANTICOAGULANT AGENT; ANTICONVULSIVE AGENT; ANTIEMETIC AGENT; ANTIFUNGAL AGENT; ANTIVIRUS AGENT; BENZOXAZINONE DERIVATIVE; BETA LACTAM; GANCICLOVIR; INTERCELLULAR ADHESION MOLECULE 1; LAMIVUDINE; NUCLEOSIDE ANALOG; PHENANTHRENE DERIVATIVE; PLECONARIL; PROTEINASE INHIBITOR; RNA DIRECTED DNA POLYMERASE INHIBITOR; THIAZOLIDINE DERIVATIVE; TRIPEPTIDE DERIVATIVE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VIRUS DNA; VIRUS ENZYME; ZIDOVUDINE;

EID: 0031736007     PISSN: 08938512     EISSN: None     Source Type: Journal    
DOI: 10.1128/cmr.11.4.614     Document Type: Review
Times cited : (202)

References (170)
  • 1
    • 3643122635 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 3
    • 0028328469 scopus 로고
    • Picornaviral 3C cycteine proteinases have a fold similar to chymotrypsin-like serine proteinases
    • Allaire, M., M. M. Chernaia, B. A. Malcom, and M. N. James. 1994. Picornaviral 3C cycteine proteinases have a fold similar to chymotrypsin-like serine proteinases. Nature 369:72-76.
    • (1994) Nature , vol.369 , pp. 72-76
    • Allaire, M.1    Chernaia, M.M.2    Malcom, B.A.3    James, M.N.4
  • 4
    • 0028898609 scopus 로고
    • Epidemiology of hepatitis C in the west
    • Alter, M. J. 1995. Epidemiology of hepatitis C in the west. Semin. Liver Dis. 15:5-14.
    • (1995) Semin. Liver Dis. , vol.15 , pp. 5-14
    • Alter, M.J.1
  • 5
    • 0344746430 scopus 로고    scopus 로고
    • Inhibitors of HIV-1 protease
    • P. Veerapandian (ed.), Marcel Dekker, Inc., New York, N.Y.
    • Appelt, K. 1997. Inhibitors of HIV-1 protease, p. 1-39. In P. Veerapandian (ed.), Structure-based drug design. Marcel Dekker, Inc., New York, N.Y.
    • (1997) Structure-based Drug Design , pp. 1-39
    • Appelt, K.1
  • 6
    • 0001900367 scopus 로고
    • Clinical studies of antiviral agents for picornaviral infections
    • D. J. Jeffries and E. De Clerq (ed.), John Wiley & Sons, Ltd., Chichester, United Kingdom
    • Arruda, E., and F. G. Hayden. 1995. Clinical studies of antiviral agents for picornaviral infections, p. 321-355. In D. J. Jeffries and E. De Clerq (ed.), Antiviral chemotherapy. John Wiley & Sons, Ltd., Chichester, United Kingdom.
    • (1995) Antiviral Chemotherapy , pp. 321-355
    • Arruda, E.1    Hayden, F.G.2
  • 7
    • 0027287798 scopus 로고
    • Nonstructural protein 3 of the hepatitis C virus encodes a serine-type proteinase required for cleavage at the NS3/4 and NS4/5 junctions
    • Bartenschlager, R., L. Ahlborn-Laake, J. Mous, and H. Jacobsen. 1993. Nonstructural protein 3 of the hepatitis C virus encodes a serine-type proteinase required for cleavage at the NS3/4 and NS4/5 junctions. J. Virol. 67:3835-3844.
    • (1993) J. Virol. , vol.67 , pp. 3835-3844
    • Bartenschlager, R.1    Ahlborn-Laake, L.2    Mous, J.3    Jacobsen, H.4
  • 8
    • 0028241489 scopus 로고
    • Kinetic and structural analyses of hepatitis C virus polyprotein processing
    • Bartenschlager, R., L. Ahlborn-Laake, J. Mous, and H. Jacobsen. 1994. Kinetic and structural analyses of hepatitis C virus polyprotein processing. J. Virol. 68:5045-5055.
    • (1994) J. Virol. , vol.68 , pp. 5045-5055
    • Bartenschlager, R.1    Ahlborn-Laake, L.2    Mous, J.3    Jacobsen, H.4
  • 9
    • 84960989167 scopus 로고
    • The antiviral and synergic actions of isatin ithiosemicarbazone and certain phenoxypyrimidines in vaccinia infection in mice
    • Bauer, D. J. 1955. The antiviral and synergic actions of isatin ithiosemicarbazone and certain phenoxypyrimidines in vaccinia infection in mice. Br. J. Exp. Pathol. 36:105-114.
    • (1955) Br. J. Exp. Pathol. , vol.36 , pp. 105-114
    • Bauer, D.J.1
  • 10
    • 0027402613 scopus 로고
    • Expression and analysis of the human cytomegalovirus UL80-encoded protease: Identification of autoproteolytic sites
    • Baum, E. Z., G. A. Bebernitz, J. D. Hulmes, V. P. Muzithras, T. R. Jones, and Y. Gluzman. 1993. Expression and analysis of the human cytomegalovirus UL80-encoded protease: identification of autoproteolytic sites. J. Virol. 67:497-506.
    • (1993) J. Virol. , vol.67 , pp. 497-506
    • Baum, E.Z.1    Bebernitz, G.A.2    Hulmes, J.D.3    Muzithras, V.P.4    Jones, T.R.5    Gluzman, Y.6
  • 14
    • 0030051777 scopus 로고    scopus 로고
    • Identification and properties of the RNA-dependcnt RNA polymerase of hepatitis C virus
    • Behrens, S.-E., L. Tomei, and R. DeFrancesco. 1996. Identification and properties of the RNA-dependcnt RNA polymerase of hepatitis C virus. EMBO J. 15:12-22.
    • (1996) EMBO J. , vol.15 , pp. 12-22
    • Behrens, S.-E.1    Tomei, L.2    DeFrancesco, R.3
  • 16
    • 0028300385 scopus 로고
    • Human cytomegalovirus maturational proteinase: Expression in Escherichia coli, purification, and enzymatic characterization by using peptide substrate mimics of natural cleavage sites
    • Burck, P. J., D. H. Berg, T. P. Luk, L. M. Sassmannshausen, M. Wakulchik, D. P. Smith, H. M. Hsiung, G. W. Becker, W. Gibson, and E. C. Villareal. 1994. Human cytomegalovirus maturational proteinase: expression in Escherichia coli, purification, and enzymatic characterization by using peptide substrate mimics of natural cleavage sites. J. Virol. 68:2937-2946.
    • (1994) J. Virol. , vol.68 , pp. 2937-2946
    • Burck, P.J.1    Berg, D.H.2    Luk, T.P.3    Sassmannshausen, L.M.4    Wakulchik, M.5    Smith, D.P.6    Hsiung, H.M.7    Becker, G.W.8    Gibson, W.9    Villareal, E.C.10
  • 19
    • 0344036978 scopus 로고    scopus 로고
    • HIV protease inhibitors
    • Carr, A., and D. A. Cooper. 1996. HIV protease inhibitors. AIDS 10:S151-S157.
    • (1996) AIDS , vol.10
    • Carr, A.1    Cooper, D.A.2
  • 20
    • 0028151652 scopus 로고
    • Picornavirus inhibitors
    • Carrasco, L. 1994. Picornavirus inhibitors. Pharmacol. Ther. 64:119-128.
    • (1994) Pharmacol. Ther. , vol.64 , pp. 119-128
    • Carrasco, L.1
  • 21
    • 0031059174 scopus 로고    scopus 로고
    • New therapeutic approaches to the alphaherpesvirus infections
    • Cassady, K. A., and R. J. Whitley. 1997. New therapeutic approaches to the alphaherpesvirus infections. J. Antimicrob. Chemother. 39:119-128.
    • (1997) J. Antimicrob. Chemother. , vol.39 , pp. 119-128
    • Cassady, K.A.1    Whitley, R.J.2
  • 22
    • 0025201350 scopus 로고
    • Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein
    • Chambers, T. J., R. C. Weir, A. Grakoui, D. W. Court, J. F. Bazan, R. J. Fletterick, and C. M. Rice. 1990. Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein. Proc. Natl. Acad. Sci. USA 87:8898-8902.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8898-8902
    • Chambers, T.J.1    Weir, R.C.2    Grakoui, A.3    Court, D.W.4    Bazan, J.F.5    Fletterick, R.J.6    Rice, C.M.7
  • 24
    • 0029131607 scopus 로고
    • Three-dimensional structure of a mutant HIV-1 protease displaying cross-resistance to all protease inhibitors in clinical trials
    • Chen, Z., H. B. Schock, D. Hall, E. Chen, and L. C. Kuo. 1995. Three-dimensional structure of a mutant HIV-1 protease displaying cross-resistance to all protease inhibitors in clinical trials. J. Biol. Chem. 270:21433-21436.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21433-21436
    • Chen, Z.1    Schock, H.B.2    Hall, D.3    Chen, E.4    Kuo, L.C.5
  • 25
    • 0031004331 scopus 로고    scopus 로고
    • Construction of hepatitis C-SIN virus recombinants with replicative dependency on hepatitis C virus serine protease activity
    • Cho, Y.-G., H.-S. Moon, and Y.-C. Sung. 1997. Construction of hepatitis C-SIN virus recombinants with replicative dependency on hepatitis C virus serine protease activity. J. Virol. Methods 65:201-207.
    • (1997) J. Virol. Methods , vol.65 , pp. 201-207
    • Cho, Y.-G.1    Moon, H.-S.2    Sung, Y.-C.3
  • 29
    • 0342323915 scopus 로고    scopus 로고
    • A randomized phase II dose range-finding study of the HIV protease inhibitor VIRACEPT® as monotherapy in HIV positive patients
    • abstr. 2129
    • Conant, M., M. Markowitz, A. Hurley, D. Ho, J. Peterkin, and S. Chapman. 1996. A randomized phase II dose range-finding study of the HIV protease inhibitor VIRACEPT® as monotherapy in HIV positive patients, abstr. 2129, p. 286. In Abstracts of the XI International Conference on AIDS.
    • (1996) Abstracts of the XI International Conference on AIDS , pp. 286
    • Conant, M.1    Markowitz, M.2    Hurley, A.3    Ho, D.4    Peterkin, J.5    Chapman, S.6
  • 32
    • 0000824034 scopus 로고
    • Rhinoviruses
    • B. N. Fields and D. M. Knipe (ed.), Raven Press, New York, N.Y.
    • Couch, R. B. 1990. Rhinoviruses, p. 607-629. In B. N. Fields and D. M. Knipe (ed.), Virology. Raven Press, New York, N.Y.
    • (1990) Virology , pp. 607-629
    • Couch, R.B.1
  • 38
    • 0030796292 scopus 로고    scopus 로고
    • Characterization of engineered hepatitis C virus NS3 protease inhibitors affinity selected from human pancreatic secretory trypsin inhibitor and minibody repertoires
    • Dimasi, N., F. Martin, C. Volpari, M. Brunetti, G. Biasiol, S. Altamura, R. Cortese, R. de Francesco, C. Steinkühler, and M. Sollazzo. 1997. Characterization of engineered hepatitis C virus NS3 protease inhibitors affinity selected from human pancreatic secretory trypsin inhibitor and minibody repertoires. J. Virol. 71:7461-7469.
    • (1997) J. Virol. , vol.71 , pp. 7461-7469
    • Dimasi, N.1    Martin, F.2    Volpari, C.3    Brunetti, M.4    Biasiol, G.5    Altamura, S.6    Cortese, R.7    De Francesco, R.8    Steinkühler, C.9    Sollazzo, M.10
  • 40
    • 0027138172 scopus 로고
    • Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes
    • Dougherty, W. G., and B. L. Semler. 1993. Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes. Microbiol. Rev. 57:781-822.
    • (1993) Microbiol. Rev. , vol.57 , pp. 781-822
    • Dougherty, W.G.1    Semler, B.L.2
  • 43
    • 0027170423 scopus 로고
    • The hepatitis C virus encodes a serine proteinase involved in processing of the putative nonstructural proteins from the viral polyprotein precursor
    • Eckart M. R., M. Selby, F. Masiarz, C. Lee, K. Berger, C. Crawford, C. Kuo, G. Kuo, M. Houghton, and Q.-L. Choo. 1993. The hepatitis C virus encodes a serine proteinase involved in processing of the putative nonstructural proteins from the viral polyprotein precursor. Biochem. Biophys. Res. Commun. 192:399-406.
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 399-406
    • Eckart, M.R.1    Selby, M.2    Masiarz, F.3    Lee, C.4    Berger, K.5    Crawford, C.6    Kuo, C.7    Kuo, G.8    Houghton, M.9    Choo, Q.-L.10
  • 45
    • 0028290579 scopus 로고
    • Both NS3 and NS4A are required for proteolytic processing of hepatitis C virus nonstructural proteins
    • Failla, C., L. Tomei, and R. DeFrancesco. 1994. Both NS3 and NS4A are required for proteolytic processing of hepatitis C virus nonstructural proteins. J. Virol. 68:3753-3760.
    • (1994) J. Virol. , vol.68 , pp. 3753-3760
    • Failla, C.1    Tomei, L.2    DeFrancesco, R.3
  • 46
    • 0031036325 scopus 로고    scopus 로고
    • Chimeric Sindbis viruses dependent on the NS3 protease of hepatitis C virus
    • Filocamo, G., L. Pacini, and G. Migliaccio. 1997. Chimeric Sindbis viruses dependent on the NS3 protease of hepatitis C virus. J. Virol. 71:1417-1427.
    • (1997) J. Virol. , vol.71 , pp. 1417-1427
    • Filocamo, G.1    Pacini, L.2    Migliaccio, G.3
  • 49
    • 1842293317 scopus 로고    scopus 로고
    • VP-63843 Pleconaril WIN-63843
    • Fromtling, R. A., and J. Castañer. 1997. VP-63843 Pleconaril WIN-63843. Drugs Future 22:40-44.
    • (1997) Drugs Future , vol.22 , pp. 40-44
    • Fromtling, R.A.1    Castañer, J.2
  • 52
    • 0030426255 scopus 로고    scopus 로고
    • Structure and assembly of the virion
    • Gibson, W. 1996. Structure and assembly of the virion. Intervirology 39: 389-400.
    • (1996) Intervirology , vol.39 , pp. 389-400
    • Gibson, W.1
  • 53
    • 0022570578 scopus 로고
    • Poliovirus-encoded proteinase 3C: A possible evolutionary link between cellular senne and cysteine proteinase families
    • Gorbalenya, A. E., V. M. Blinov, and A. P. Donchenko. 1986. Poliovirus-encoded proteinase 3C: a possible evolutionary link between cellular senne and cysteine proteinase families. FEBS Lett. 194:253-259.
    • (1986) FEBS Lett. , vol.194 , pp. 253-259
    • Gorbalenya, A.E.1    Blinov, V.M.2    Donchenko, A.P.3
  • 55
    • 0027414062 scopus 로고
    • Characterization of the hepatitis C virus-encoded serine proteinase: Determination of proteinase-dependent polyprotein cleavage site
    • Grakoui, A., D. W. McCourt, C. Wychowski, S. M. Feinstone, and C. M. Rice. 1993 Characterization of the hepatitis C virus-encoded serine proteinase: determination of proteinase-dependent polyprotein cleavage site. J. Virol. 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
  • 56
    • 0030589469 scopus 로고    scopus 로고
    • Generation of a novel poliovirus with a requirement of hepatitis C virus protease NS3 activity
    • Hahm, B., S. H. Back, T. G. Lee, E. Wimmer, and S. K. Jang. 1996. Generation of a novel poliovirus with a requirement of hepatitis C virus protease NS3 activity. Virology 226:318-326.
    • (1996) Virology , vol.226 , pp. 318-326
    • Hahm, B.1    Back, S.H.2    Lee, T.G.3    Wimmer, E.4    Jang, S.K.5
  • 59
    • 84964127683 scopus 로고
    • Activity of p-ammobenzaldehyde, 3-thiosemicarbazone in the chick embryo and in the mouse
    • Hamre, D., J. Bernstein, and R. Donovick. 1950. Activity of p-ammobenzaldehyde, 3-thiosemicarbazone in the chick embryo and in the mouse. Proc. Soc. Exp. Biol. Med. 73:275-278.
    • (1950) Proc. Soc. Exp. Biol. Med. , vol.73 , pp. 275-278
    • Hamre, D.1    Bernstein, J.2    Donovick, R.3
  • 61
    • 0345629011 scopus 로고    scopus 로고
    • Experience with a ritonavir/saquinavir based regimen for the treatment of HIV-infection in subjects developing increased viral loads while receiving nelfinavir
    • abstr. I-204, American Society for Microbiology, Washington, D.C.
    • Henry, K., E. Kane, H. Melroe, J. Simpson, A. Patick, and D. Winslow. 1997. Experience with a ritonavir/saquinavir based regimen for the treatment of HIV-infection in subjects developing increased viral loads while receiving nelfinavir, abstr. I-204, p. 282. In Program and Abstracts of the 37th Interscience Conference on Antimicrobial Agents and Chemotherapy. American Society for Microbiology, Washington, D.C.
    • (1997) Program and Abstracts of the 37th Interscience Conference on Antimicrobial Agents and Chemotherapy , pp. 282
    • Henry, K.1    Kane, E.2    Melroe, H.3    Simpson, J.4    Patick, A.5    Winslow, D.6
  • 64
    • 0027163740 scopus 로고
    • Two distinct proteinase activities required for the processing of a putative nonstructural precursor protein of the hepatitis C virus
    • Hijikata, M., H. Mizushima, T. Akagi, S. Mori, N. Kakiuchi, N. Kato, T. Tanaka, K. Kimura, and K. Shimotohno. 1993. Two distinct proteinase activities required for the processing of a putative nonstructural precursor protein of the hepatitis C virus. J. Virol. 67:4665-4675.
    • (1993) J. Virol. , vol.67 , pp. 4665-4675
    • Hijikata, M.1    Mizushima, H.2    Akagi, T.3    Mori, S.4    Kakiuchi, N.5    Kato, N.6    Tanaka, T.7    Kimura, K.8    Shimotohno, K.9
  • 65
    • 0028838013 scopus 로고
    • A novel method for analysis of viral proteinase activity encoded by hepatitis C virus in cultured cells
    • Hirowatari, Y., M. Hijikata, and K. Shimotohno. 1995. A novel method for analysis of viral proteinase activity encoded by hepatitis C virus in cultured cells. Anal. Biochem. 225:113-120.
    • (1995) Anal. Biochem. , vol.225 , pp. 113-120
    • Hirowatari, Y.1    Hijikata, M.2    Shimotohno, K.3
  • 66
    • 0028874048 scopus 로고
    • Rapid turnover of plasma virions and CD4 lymphocytes in HIV-1 infection
    • Ho, D. D., A. U. Neuman, A. S. Perelson, W. Chen, J. M. Leonard, and M. Markowitz. 1995. Rapid turnover of plasma virions and CD4 lymphocytes in HIV-1 infection. Nature 373:123-126.
    • (1995) Nature , vol.373 , pp. 123-126
    • Ho, D.D.1    Neuman, A.U.2    Perelson, A.S.3    Chen, W.4    Leonard, J.M.5    Markowitz, M.6
  • 67
  • 69
  • 72
    • 0029824426 scopus 로고    scopus 로고
    • In vivo resistance to a human immunodeficiency virus type 1 proteinase inhibitor: Mutations, kinetics and frequencies
    • Jacobsen, H., M. Hänggi, M. Ott, I. B. Duncan, S. Owen, M. Andreoni, S. Vella, and J. Mous. 1996. In vivo resistance to a human immunodeficiency virus type 1 proteinase inhibitor: mutations, kinetics and frequencies. J. Infect. Dis. 173:1379-1387.
    • (1996) J. Infect. Dis. , vol.173 , pp. 1379-1387
    • Jacobsen, H.1    Hänggi, M.2    Ott, M.3    Duncan, I.B.4    Owen, S.5    Andreoni, M.6    Vella, S.7    Mous, J.8
  • 73
    • 0028843163 scopus 로고
    • Characterization of human immunodeficiency virus type 1 mutants with decreased sensitivity to proteinase inhibitor Ro 31-8959
    • Jacobsen, H., K. Yasargil, D. L. Winslow, J. C. Craig, A. Krohn, I. B. Duncan, and J. Mous. 1995. Characterization of human immunodeficiency virus type 1 mutants with decreased sensitivity to proteinase inhibitor Ro 31-8959. Virology 206:527-534.
    • (1995) Virology , vol.206 , pp. 527-534
    • Jacobsen, H.1    Yasargil, K.2    Winslow, D.L.3    Craig, J.C.4    Krohn, A.5    Duncan, I.B.6    Mous, J.7
  • 77
    • 0027158754 scopus 로고
    • Partial inhibition of the human immunodeficiency virus type 1 protease results in aberrant virus assembly and the formation of noninfectious particles
    • Kaplan, A. H., J. A. Zack, M. Knigge, D. A. Paul, D. J. Kempf, D. W. Norbeck, and R. Swanstrom. 1993. Partial inhibition of the human immunodeficiency virus type 1 protease results in aberrant virus assembly and the formation of noninfectious particles. J. Virol. 67:4050-4055.
    • (1993) J. Virol. , vol.67 , pp. 4050-4055
    • Kaplan, A.H.1    Zack, J.A.2    Knigge, M.3    Paul, D.A.4    Kempf, D.J.5    Norbeck, D.W.6    Swanstrom, R.7
  • 78
    • 0025017237 scopus 로고
    • Viral proteinases: Weakness in strength
    • Kay, J., and B. M. Dunn. 1990. Viral proteinases: weakness in strength. Biochim. Biophys. Acta 1048:1-18.
    • (1990) Biochim. Biophys. Acta , vol.1048 , pp. 1-18
    • Kay, J.1    Dunn, B.M.2
  • 79
    • 0027291014 scopus 로고
    • Substitution mutations at the putative catalytic triad of the poliovirus 3C protease have differential effects on cleavage at different sites
    • Kean, K. M., M. T. Howell, S. Grünert, M. Girard, and R. J. Jackson. 1993. Substitution mutations at the putative catalytic triad of the poliovirus 3C protease have differential effects on cleavage at different sites. Virology 194:360-364.
    • (1993) Virology , vol.194 , pp. 360-364
    • Kean, K.M.1    Howell, M.T.2    Grünert, S.3    Girard, M.4    Jackson, R.J.5
  • 83
    • 0030699529 scopus 로고    scopus 로고
    • Determinants of substrate specificity in the NS3 serine proteinase of the hepatitis C virus
    • Koch, J. O., and R. Bartenschlager. 1997. Determinants of substrate specificity in the NS3 serine proteinase of the hepatitis C virus. Virology 237: 78-88.
    • (1997) Virology , vol.237 , pp. 78-88
    • Koch, J.O.1    Bartenschlager, R.2
  • 91
    • 0025335389 scopus 로고
    • Picornavirus protein processing -enzymes, substrates, and genetic regulation
    • Lawson, M. A., and B. L. Semler. 1990. Picornavirus protein processing -enzymes, substrates, and genetic regulation. Curr. Top. Microbiol. Immunol. 161:49-80.
    • (1990) Curr. Top. Microbiol. Immunol. , vol.161 , pp. 49-80
    • Lawson, M.A.1    Semler, B.L.2
  • 92
    • 0030610689 scopus 로고    scopus 로고
    • In vitro effect of alpha-acid glycoprotein on the anti-human immunodeficiency virus (HIV) activity of the protease inhibitor CGP 61755: A comparative study with other relevant HIV protease inhibitors
    • Lazdins, J. K., J. Mestan, G. Goutte, M. R. Walker, G. Bold, H. G. Capraro, and T. Klimkait. 1997. In vitro effect of alpha-acid glycoprotein on the anti-human immunodeficiency virus (HIV) activity of the protease inhibitor CGP 61755: a comparative study with other relevant HIV protease inhibitors. J. Infect. Dis. 175:1063-1070.
    • (1997) J. Infect. Dis. , vol.175 , pp. 1063-1070
    • Lazdins, J.K.1    Mestan, J.2    Goutte, G.3    Walker, M.R.4    Bold, G.5    Capraro, H.G.6    Klimkait, T.7
  • 93
    • 0029094449 scopus 로고
    • The hepatitis C virus NS3 serine proteinase and NS4A cofactor: Establishment of a cell-free trans-processing assay
    • Lin, C., and C. M. Rice. 1995. The hepatitis C virus NS3 serine proteinase and NS4A cofactor: establishment of a cell-free trans-processing assay. Proc. Natl. Acad. Sci. USA 92:7622-7626.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7622-7626
    • Lin, C.1    Rice, C.M.2
  • 95
    • 0030592514 scopus 로고    scopus 로고
    • The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site
    • Love, R. A., H. E. Parge, J. A. Wickersham, Z. Hostomsky, N. Habuka, E. W. Moomaw, T. Adachi, and Z. Hostomska. 1996. The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site. Cell 87:331-342.
    • (1996) Cell , vol.87 , pp. 331-342
    • Love, R.A.1    Parge, H.E.2    Wickersham, J.A.3    Hostomsky, Z.4    Habuka, N.5    Moomaw, E.W.6    Adachi, T.7    Hostomska, Z.8
  • 97
    • 0029969303 scopus 로고    scopus 로고
    • Dimerization of the human cytomegalovirus protease: Kinetic and biochemical characterization of the catalytic homodimer
    • Margosiak, S. A., D. L. Vanderpool, W. Sisson, C. Pinko, and C.-C. Ran. 1996. Dimerization of the human cytomegalovirus protease: kinetic and biochemical characterization of the catalytic homodimer. Biochemistry 35: 5300-5307.
    • (1996) Biochemistry , vol.35 , pp. 5300-5307
    • Margosiak, S.A.1    Vanderpool, D.L.2    Sisson, W.3    Pinko, C.4    Ran, C.-C.5
  • 99
    • 0028854676 scopus 로고
    • Selection and analysis of human immunodeficiency virus type 1 variants with increased resistance to ABT-538, a novel protease inhibitor
    • Markowitz, M., H. Mo, D. J. Kempf, D. W. Norbeck, T. Narayana Bhat, J. W. Erickson, and D. D. Ho. 1995. Selection and analysis of human immunodeficiency virus type 1 variants with increased resistance to ABT-538, a novel protease inhibitor. J. Virol. 69:701-706.
    • (1995) J. Virol. , vol.69 , pp. 701-706
    • Markowitz, M.1    Mo, H.2    Kempf, D.J.3    Norbeck, D.W.4    Narayana Bhat, T.5    Erickson, J.W.6    Ho, D.D.7
  • 101
    • 0026538287 scopus 로고
    • Hepatitis C virus (HCV) circulates as a population of different but closely related genomes: Quasispecies nature of HCV genome distribution
    • Martell, M., J. I. Esteban, J. Quer, J. Genesca, A. Weiner, R. Esteban, J. Guardia, and J. Gomez. 1992. Hepatitis C virus (HCV) circulates as a population of different but closely related genomes: quasispecies nature of HCV genome distribution. J. Virol. 66:3225-3229.
    • (1992) J. Virol. , vol.66 , pp. 3225-3229
    • Martell, M.1    Esteban, J.I.2    Quer, J.3    Genesca, J.4    Weiner, A.5    Esteban, R.6    Guardia, J.7    Gomez, J.8
  • 102
    • 0026561407 scopus 로고
    • Recent advances in the design of HIV proteinase inhibitors
    • Martin, J. A. 1992. Recent advances in the design of HIV proteinase inhibitors. Antiviral Res. 17:265-278.
    • (1992) Antiviral Res. , vol.17 , pp. 265-278
    • Martin, J.A.1
  • 104
    • 0030993833 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 protease inhibitors
    • McDonald, C. K., and D. R. Kuritzkes. 1997. Human immunodeficiency virus type 1 protease inhibitors. Arch. Intern. Med. 157:951-959.
    • (1997) Arch. Intern. Med. , vol.157 , pp. 951-959
    • McDonald, C.K.1    Kuritzkes, D.R.2
  • 105
    • 0026803235 scopus 로고
    • Treatment of the picornavirus common cold by inhibitors of viral uncoating and attachment
    • McKinlay, M. A., D. C. Pevear, and M. G. Rossmann. 1992. Treatment of the picornavirus common cold by inhibitors of viral uncoating and attachment. Annu. Rev. Microbiol. 46:635-654.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 635-654
    • McKinlay, M.A.1    Pevear, D.C.2    Rossmann, M.G.3
  • 106
    • 0001109983 scopus 로고
    • Enteroviruses: Polioviruses, coxsackieviruses, echoviruses, and newer enteroviruses
    • B. N. Fields and D. M. Knipe (ed.), Raven Press, New York, N.Y.
    • Melnick, J. L. 1990. Enteroviruses: polioviruses, coxsackieviruses, echoviruses, and newer enteroviruses, p. 549-605. In B. N. Fields and D. M. Knipe (ed.), Virology. Raven Press, New York, N.Y.
    • (1990) Virology , pp. 549-605
    • Melnick, J.L.1
  • 108
    • 0001331114 scopus 로고    scopus 로고
    • Cytomegaloviruses and their replication
    • B. N. Fields and D. M. Knipe (ed.), Lippincott-Raven, Philadelphia, Pa.
    • Mocarski, E. S., Jr. 1996. Cytomegaloviruses and their replication, p. 2447-2492. In B. N. Fields and D. M. Knipe (ed.), Virology, 3rd ed. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Virology, 3rd Ed. , pp. 2447-2492
    • Mocarski Jr., E.S.1
  • 111
    • 0030928281 scopus 로고    scopus 로고
    • Antiviral chemotherapy
    • Mueller, B. U. 1997. Antiviral chemotherapy. Curr. Opin. Pediatr. 9:178-183.
    • (1997) Curr. Opin. Pediatr. , vol.9 , pp. 178-183
    • Mueller, B.U.1
  • 114
    • 0028942788 scopus 로고
    • The effect of internal autocleavage on kinetic properties of the human cytomegalovirus protease catalytic domain
    • O'Boyle, D. R. I., K. Wager-Smith, J. T. Stevens, and S. P. Weinheimer. 1995. The effect of internal autocleavage on kinetic properties of the human cytomegalovirus protease catalytic domain. J. Biol. Chem. 270:4753-1758.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4753-11758
    • O'Boyle, D.R.I.1    Wager-Smith, K.2    Stevens, J.T.3    Weinheimer, S.P.4
  • 116
  • 118
    • 0030812875 scopus 로고    scopus 로고
    • Activities of the human immunodeficiency virus type 1 (HIV-1) protease inhibitor nelfinavir mesylate in combination with reverse transcriptase and protease inhibitors against acute HIV-1 infection in vitro
    • Patick, A. K., T. J. Boritzki, and L. A. Bloom. 1997. Activities of the human immunodeficiency virus type 1 (HIV-1) protease inhibitor nelfinavir mesylate in combination with reverse transcriptase and protease inhibitors against acute HIV-1 infection in vitro. Antimicrob. Agents Chemother. 41:2159-2164.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 2159-2164
    • Patick, A.K.1    Boritzki, T.J.2    Bloom, L.A.3
  • 124
    • 0024334170 scopus 로고
    • Role of human immunodeficiency virus type 1-specific protease in core protein maturation and viral infectivity
    • Peng, C., B. K. Ho, T. W. Chang, and N. T. Chang. 1989. Role of human immunodeficiency virus type 1-specific protease in core protein maturation and viral infectivity. J. Virol. 63:2550-2556.
    • (1989) J. Virol. , vol.63 , pp. 2550-2556
    • Peng, C.1    Ho, B.K.2    Chang, T.W.3    Chang, N.T.4
  • 125
    • 0029967721 scopus 로고    scopus 로고
    • HIV-1 dynamics in vivo: Virion clearance rate, infected cell life-span and viral generation time
    • Perelson, A. S., A. U. Neuman, M. Markowitz, J. M. Leonard, and D. D. Ho. 1996. HIV-1 dynamics in vivo: virion clearance rate, infected cell life-span and viral generation time. Science 271:1582-1586.
    • (1996) Science , vol.271 , pp. 1582-1586
    • Perelson, A.S.1    Neuman, A.U.2    Markowitz, M.3    Leonard, J.M.4    Ho, D.D.5
  • 130
    • 0001424128 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • B. N. Fields and D. M. Knipe (ed.). Lippincott-Raven. Philadelphia, Pa.
    • Rice, C. M. 1996 Flaviviridae: the viruses and their replication, p. 931-959. In B. N. Fields and D. M. Knipe (ed.). Virology, 3rd ed. Lippincott-Raven. Philadelphia, Pa.
    • (1996) Virology, 3rd Ed. , pp. 931-959
    • Rice, C.M.1
  • 133
    • 0001952393 scopus 로고
    • Picornaviridae and their replication
    • B. N. Fields and D. M. Knipe (ed.), Raven Press, New York, N.Y.
    • Rueckert, R. R. 1990. Picornaviridae and their replication, p. 507-548. In B. N. Fields and D. M. Knipe (ed.), Virology. Raven Press, New York, N.Y.
    • (1990) Virology , pp. 507-548
    • Rueckert, R.R.1
  • 136
    • 0028233530 scopus 로고
    • Biosynthesis and biochemical properties of the hepatitis C virus core protein
    • Santolini, E., G. Migliaccio, and N. LaMonica. 1994. Biosynthesis and biochemical properties of the hepatitis C virus core protein. J. Virol. 68: 3631-3641.
    • (1994) J. Virol. , vol.68 , pp. 3631-3641
    • Santolini, E.1    Migliaccio, G.2    LaMonica, N.3
  • 137
    • 0028839782 scopus 로고
    • The long-term efficacy of Interferon alpha in chronic hepatitis C patients: A critical review
    • Saracco, G., and M. Rizzetto. 1995. The long-term efficacy of Interferon alpha in chronic hepatitis C patients: a critical review. J. Gastroenterol. Hepatol. 10:668-673.
    • (1995) J. Gastroenterol. Hepatol. , vol.10 , pp. 668-673
    • Saracco, G.1    Rizzetto, M.2
  • 138
    • 0030317870 scopus 로고    scopus 로고
    • The effect of high-dose saquinavir on viral load and CD4+ T-cell counts in HIV-counts in HIV-infected patients
    • Schapiro, J. M., M. A. Winters, F. Stewart, B. Efron, J. Norris, M. J. Kozal, and T. C. Merigan. 1996. The effect of high-dose saquinavir on viral load and CD4+ T-cell counts in HIV-counts in HIV-infected patients. Ann. Intern. Med. 124:1039-1050.
    • (1996) Ann. Intern. Med. , vol.124 , pp. 1039-1050
    • Schapiro, J.M.1    Winters, M.A.2    Stewart, F.3    Efron, B.4    Norris, J.5    Kozal, M.J.6    Merigan, T.C.7
  • 139
    • 0026081042 scopus 로고
    • The 45-kilodalton protein of cytomegalovirus (Colburn) B-capsids is an amino-terminal extension form of the assembly protein
    • Schenk, P., A. S. Woods, and W. Gibson. 1991. The 45-kilodalton protein of cytomegalovirus (Colburn) B-capsids is an amino-terminal extension form of the assembly protein. J. Virol. 65:1525-1529.
    • (1991) J. Virol. , vol.65 , pp. 1525-1529
    • Schenk, P.1    Woods, A.S.2    Gibson, W.3
  • 141
    • 0030012398 scopus 로고    scopus 로고
    • Resistance-related mutations in the HIV-1 protease gene of patients treated for one year with the protease inhibitor ritonavir (ABT-538)
    • Schmit, J.-C., L. Ruiz, B. Clotet, A. Raventos, J. Tor, J. Leonard, J. Desmyter E. De Clercq, and A.-M. Vandamme. 1996. Resistance-related mutations in the HIV-1 protease gene of patients treated for one year with the protease inhibitor ritonavir (ABT-538). AIDS 10:995-999.
    • (1996) AIDS , vol.10 , pp. 995-999
    • Schmit, J.-C.1    Ruiz, L.2    Clotet, B.3    Raventos, A.4    Tor, J.5    Leonard, J.6    Desmyter, J.7    De Clercq, E.8    Vandamme, A.-M.9
  • 145
    • 8044260834 scopus 로고    scopus 로고
    • Clinical efficacy of monotherapy with stavudine compared with zidovudine in HIV-infected zidovudine-experienced patients. A randomized, double-blind, controlled trial
    • Bristol-Myers Squibb Stavudine/019 Study Group.
    • Spruance, S. L., A. T. Pavia, J. W. Mellors, R. Murphy, J. Gathe, Jr., E. Stool, J. G. Jemsek, P. Dellamonica, A. Cross, and L. Dunkle. 1997. Clinical efficacy of monotherapy with stavudine compared with zidovudine in HIV-infected zidovudine-experienced patients. A randomized, double-blind, controlled trial. Bristol-Myers Squibb Stavudine/019 Study Group. Ann. Intern. Med. 126:355-363.
    • (1997) Ann. Intern. Med. , vol.126 , pp. 355-363
    • Spruance, S.L.1    Pavia, A.T.2    Mellors, J.W.3    Murphy, R.4    Gathe Jr., J.5    Stool, E.6    Jemsek, J.G.7    Dellamonica, P.8    Cross, A.9    Dunkle, L.10
  • 149
    • 3643053708 scopus 로고    scopus 로고
    • Facts and comparisons: Loose leaf drug infor-mation service
    • St. Louis, Mo.
    • Threlkeld, D. S. (ed.). 1997. Facts and comparisons: loose leaf drug infor-mation service, p. 402A-407Z. Facts and Comparisons, St. Louis, Mo.
    • (1997) Facts and Comparisons
    • Threlkeld, D.S.1
  • 150
    • 0029133978 scopus 로고
    • Cross-resistance analysis of human immunodeficiency virus type 1 variants individually selected for resistance to five different protease inhibitors
    • Tisdale, M., R. E. Myers, B. Maschera, N. R. Parry, N. M. Oliver, and E. D. Blair 1995 Cross-resistance analysis of human immunodeficiency virus type 1 variants individually selected for resistance to five different protease inhibitors. Antimicrob. Agents Chemother. 39:1704-1710.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1704-1710
    • Tisdale, M.1    Myers, R.E.2    Maschera, B.3    Parry, N.R.4    Oliver, N.M.5    Blair, E.D.6
  • 151
    • 0027176287 scopus 로고
    • NS3 is a serine protease required for processing of hepatitis C virus polyprotein
    • Tomei, L., C. Failla, E. Santolini, R. De Francesco, and N. LaMonica. 1993. NS3 is a serine protease required for processing of hepatitis C virus polyprotein. J. Virol. 67:4017-4026.
    • (1993) J. Virol. , vol.67 , pp. 4017-4026
    • Tomei, L.1    Failla, C.2    Santolini, E.3    De Francesco, R.4    LaMonica, N.5
  • 152
    • 0029793554 scopus 로고    scopus 로고
    • A new serine-protease fold revealed by the crystal structure of human cytomegalovirus protease
    • Tong, L., C. Qian, M.-J. Massariol, P. R. Bonneau, M. G. Cordingley, and L. Lagacé. 1996. A new serine-protease fold revealed by the crystal structure of human cytomegalovirus protease. Nature 383:272-275.
    • (1996) Nature , vol.383 , pp. 272-275
    • Tong, L.1    Qian, C.2    Massariol, M.-J.3    Bonneau, P.R.4    Cordingley, M.G.5    Lagacé, L.6
  • 157
    • 0030818159 scopus 로고    scopus 로고
    • Update on protease inhibitors
    • Vella, S., and L. Palmisano. 1997. Update on protease inhibitors. Antiviral Ther. 2:29-37.
    • (1997) Antiviral Ther. , vol.2 , pp. 29-37
    • Vella, S.1    Palmisano, L.2
  • 158
    • 0030444391 scopus 로고    scopus 로고
    • Retroviral proteases: Structure, function and inhibition from a non-anticipated viral enzyme to the target of a most promising HIV therapy
    • Von der Helm, K. 1996. Retroviral proteases: structure, function and inhibition from a non-anticipated viral enzyme to the target of a most promising HIV therapy. Biol. Chem. 377:765-774.
    • (1996) Biol. Chem. , vol.377 , pp. 765-774
    • Von Der Helm, K.1
  • 163
    • 0025721850 scopus 로고
    • A herpesvirus maturational proteinase, assemblin: Identification of its gene, putative active site domain, and cleavage site
    • Welch, A. R., A. S. Woods, L. M. McNally, R. J. Cotter, and W. Gibson. 1991. A herpesvirus maturational proteinase, assemblin: identification of its gene, putative active site domain, and cleavage site. Proc. Natl. Acad. Sci. USA 88:10792-10796.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10792-10796
    • Welch, A.R.1    Woods, A.S.2    McNally, L.M.3    Cotter, R.J.4    Gibson, W.5
  • 164
    • 0344243836 scopus 로고
    • HIV protease inhibitors
    • Winslow, D. L., and M. J. Otto. 1995. HIV protease inhibitors. AIDS 9:S183-S192.
    • (1995) AIDS , vol.9
    • Winslow, D.L.1    Otto, M.J.2
  • 165
    • 0027218692 scopus 로고
    • Structure-based inhibitors of HIV-1 protease
    • Wlodawer, A., and J. W. Erickson. 1993. Structure-based inhibitors of HIV-1 protease. Annu. Rev. Biochem. 62:543-585.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 543-585
    • Wlodawer, A.1    Erickson, J.W.2
  • 167
    • 0031010133 scopus 로고    scopus 로고
    • Bovine viral diarrhea virus NS3 serine proteinase: Polyprotein cleavage sites, cofactor requirements, and molecular model of an enzyme essential for pestivirus replication
    • Xu, J., E. Mendez, P. R. Caron, C. Lin, M. A. Murcko, M. S. Collett, and C. M. Rice. 1997. Bovine viral diarrhea virus NS3 serine proteinase: polyprotein cleavage sites, cofactor requirements, and molecular model of an enzyme essential for pestivirus replication. J. Virol. 71:5312-5322.
    • (1997) J. Virol. , vol.71 , pp. 5312-5322
    • Xu, J.1    Mendez, E.2    Caron, P.R.3    Lin, C.4    Murcko, M.A.5    Collett, M.S.6    Rice, C.M.7
  • 168
    • 0030740520 scopus 로고    scopus 로고
    • Transcripts from a single full-length cDNA clone of hepatitis C virus are infectious when directly transfected into the liver of a chimpanzee
    • Yanagi, M., R. H. Purcell, S. U. Emerson, and J. Bukh. 1997. Transcripts from a single full-length cDNA clone of hepatitis C virus are infectious when directly transfected into the liver of a chimpanzee. Proc. Natl. Acad. Sci. USA 94:8738-8743.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8738-8743
    • Yanagi, M.1    Purcell, R.H.2    Emerson, S.U.3    Bukh, J.4
  • 169
    • 3643049553 scopus 로고    scopus 로고
    • A novel anti-rhinoviral compound directed at 3C protease can diminish IL-6 and IL-8 production in a transformed bronchial epithelial cell line
    • abstr. 172
    • Zalman, L. S., M. A. Brothers, K. Okano, and S. E. Webber. 1997. A novel anti-rhinoviral compound directed at 3C protease can diminish IL-6 and IL-8 production in a transformed bronchial epithelial cell line, abstr. 172, p. A89. In Abstracts of the 10th International Conference on Antiviral Research.
    • (1997) Abstracts of the 10th International Conference on Antiviral Research
    • Zalman, L.S.1    Brothers, M.A.2    Okano, K.3    Webber, S.E.4
  • 170
    • 0030844455 scopus 로고    scopus 로고
    • Probing the substrate specificity of hepatitis C virus NS3 serine protease by using synthetic peptides
    • Zhang, R., J. Durkin, W. T. Windsor, C. McNemar, L. Ramanathan, and H. V. Le. 1997. Probing the substrate specificity of hepatitis C virus NS3 serine protease by using synthetic peptides. J. Virol. 71:6208-6213.
    • (1997) J. Virol. , vol.71 , pp. 6208-6213
    • Zhang, R.1    Durkin, J.2    Windsor, W.T.3    McNemar, C.4    Ramanathan, L.5    Le, H.V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.