메뉴 건너뛰기




Volumn 42, Issue 11, 1998, Pages 2775-2783

Resistance to human immunodeficiency virus type 1 protease inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

AMPRENAVIR; INDINAVIR; LAMIVUDINE; LOPINAVIR; NELFINAVIR; PROTEINASE INHIBITOR; RITONAVIR; RNA DIRECTED DNA POLYMERASE; SAQUINAVIR; TIPRANAVIR; UNCLASSIFIED DRUG; VIRUS RNA; ZIDOVUDINE;

EID: 0031724008     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.42.11.2775     Document Type: Review
Times cited : (188)

References (97)
  • 3
    • 0029131607 scopus 로고
    • Three-dimensional structure of a mutant HIV-1 protease displaying cross-resistance to all protease inhibitors in clinical trials
    • Chen, Z., Y. Li, 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    Li, Y.2    Hall, D.3    Chen, E.4    Kuo, L.C.5
  • 4
    • 0030671536 scopus 로고    scopus 로고
    • In vitro combination of PNU-140690, a human immunodeficiency virus protease inhibitor, with ritonavir against ritonavir-sensitive and -resistant clinical isolates
    • Chong, K.-T., and P. J. Pagano. 1997. In vitro combination of PNU-140690, a human immunodeficiency virus protease inhibitor, with ritonavir against ritonavir-sensitive and -resistant clinical isolates. Antimicrob. Agents Chemother. 41:2367-2373.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 2367-2373
    • Chong, K.-T.1    Pagano, P.J.2
  • 5
    • 0028952146 scopus 로고
    • HIV population in vivo: Implications for genetic variation, pathogenesis, and therapy
    • Coffin, J. M. 1995. HIV population in vivo: implications for genetic variation, pathogenesis, and therapy. Science 267:483-489.
    • (1995) Science , vol.267 , pp. 483-489
    • Coffin, J.M.1
  • 7
    • 0028958868 scopus 로고
    • Flap opening in HIV-1 protease simulated by activated molecular dynamics
    • Collins, J. R., S. K. Burt, and J. W. Erickson. 1995. Flap opening in HIV-1 protease simulated by activated molecular dynamics. Nat. Struct. Biol. 2:334-338.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 334-338
    • Collins, J.R.1    Burt, S.K.2    Erickson, J.W.3
  • 8
    • 0029102730 scopus 로고
    • Activated dynamics of flap opening in HIV-1 protease
    • Collins, J. R., S. K. Burt, and J. W. Erickson. 1995. Activated dynamics of flap opening in HIV-1 protease. Adv. Exp. Med. Biol. 362:455-460.
    • (1995) Adv. Exp. Med. Biol. , vol.362 , pp. 455-460
    • Collins, J.R.1    Burt, S.K.2    Erickson, J.W.3
  • 12
    • 0029795283 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 subtypes defined by env show high frequency of recombinant gag genes
    • Cornelissen, M., G. Kampinga, F. Zorgdrager, J. Goudsmit, and the UNAIDS Network for HIV Isolation and Characterization. 1996. Human immunodeficiency virus type 1 subtypes defined by env show high frequency of recombinant gag genes. J. Virol. 70:8209-8212.
    • (1996) J. Virol. , vol.70 , pp. 8209-8212
    • Cornelissen, M.1    Kampinga, G.2    Zorgdrager, F.3    Goudsmit, J.4
  • 13
    • 0030858617 scopus 로고    scopus 로고
    • pol gene diversity of five human immunodeficiency virus type 1 subtypes: Evidence for naturally occurring mutations that contribute to drug resistance, limited recombination patterns, and common ancestry for subtypes B and D
    • Cornelissen, M., R. van den Burg, F. Zorgdrager, V. Lukashov, and J. Goudsmit. 1997. pol gene diversity of five human immunodeficiency virus type 1 subtypes: evidence for naturally occurring mutations that contribute to drug resistance, limited recombination patterns, and common ancestry for subtypes B and D. J. Virol. 71:6348-6358.
    • (1997) J. Virol. , vol.71 , pp. 6348-6358
    • Cornelissen, M.1    Van Den Burg, R.2    Zorgdrager, F.3    Lukashov, V.4    Goudsmit, J.5
  • 14
    • 0345659615 scopus 로고
    • Ro 31-8959, an inhibitor of HIV proteinase, appears relatively refractory to the generation of virus mutants with reduced sensitivity
    • abstr. PO-A26-0694, Berlin, Germany
    • Craig, I. C., I. B. Duncan, N. A. Roberts, and L. Whittaker. 1993. Ro 31-8959, an inhibitor of HIV proteinase, appears relatively refractory to the generation of virus mutants with reduced sensitivity, abstr. PO-A26-0694, p. 243. In Abstracts of the 9th International Conference on AIDS, Berlin, Germany.
    • (1993) 9th International Conference on AIDS , pp. 243
    • Craig, I.C.1    Duncan, I.B.2    Roberts, N.A.3    Whittaker, L.4
  • 15
    • 0021931766 scopus 로고
    • A deletion mutation in the 5′ part of the pol gene of Moloney murine leukemia virus blocks proteolytic processing of the gag and pol polyproteins
    • Crawford, S., and S. P. Goff. 1985. A deletion mutation in the 5′ part of the pol gene of Moloney murine leukemia virus blocks proteolytic processing of the gag and pol polyproteins. J. Virol. 53:899-907.
    • (1985) J. Virol. , vol.53 , pp. 899-907
    • Crawford, S.1    Goff, S.P.2
  • 19
    • 0026523623 scopus 로고
    • HIV inhibitors targeted at the reverse transcriptase
    • De Clerq, E. 1992. HIV inhibitors targeted at the reverse transcriptase. AIDS Res. Hum. Retroviruses 8:119-134.
    • (1992) AIDS Res. Hum. Retroviruses , vol.8 , pp. 119-134
    • De Clerq, E.1
  • 20
    • 0029069857 scopus 로고
    • Dual human immunodeficiency virus type 1 infection and recombination in a dually exposed transfusion recipient
    • Diaz, R. S., E. C. Sabino, A. Mayer, J. W. Mosley, M. P. Bush, and The Transfusion Safety Study Group. 1995. Dual human immunodeficiency virus type 1 infection and recombination in a dually exposed transfusion recipient. J. Virol. 69:3273-3281.
    • (1995) J. Virol. , vol.69 , pp. 3273-3281
    • Diaz, R.S.1    Sabino, E.C.2    Mayer, A.3    Mosley, J.W.4    Bush, M.P.5
  • 21
    • 0029899093 scopus 로고    scopus 로고
    • Second locus involved in human immunodeficiency virus type 1 resistance to protease inhibitors
    • Doyon, L., G. Croteau, D. Thibeault, F. Poulin, L. Pilote, and D. Lamarre. 1996. Second locus involved in human immunodeficiency virus type 1 resistance to protease inhibitors. J. Virol. 70:3763-3769.
    • (1996) J. Virol. , vol.70 , pp. 3763-3769
    • Doyon, L.1    Croteau, G.2    Thibeault, D.3    Poulin, F.4    Pilote, L.5    Lamarre, D.6
  • 22
    • 0026663760 scopus 로고
    • Hydroxyethylene isostere inhibitors of human immunodeficiency virus-1 protease: Structure-activity analysis using enzyme kinetics, X-ray crystallography, and infected T-cell assays
    • Dreyer, G. B., D. M. Lambert, T. D. Meek, T. J. Carr, T. A. Tomaszek, Jr., A. V. Fernandez, H. Bartus, E. Cacciavillani, A. M. Hassell, and M. Minnich. 1992. Hydroxyethylene isostere inhibitors of human immunodeficiency virus-1 protease: structure-activity analysis using enzyme kinetics, X-ray crystallography, and infected T-cell assays. Biochemistry 31:6646-6659.
    • (1992) Biochemistry , vol.31 , pp. 6646-6659
    • Dreyer, G.B.1    Lambert, D.M.2    Meek, T.D.3    Carr, T.J.4    Tomaszek T.A., Jr.5    Fernandez, A.V.6    Bartus, H.7    Cacciavillani, E.8    Hassell, A.M.9    Minnich, M.10
  • 26
    • 0345659613 scopus 로고    scopus 로고
    • Acquisition of genotypic mutations associated with reduced susceptibility to protease inhibitors during saquinavir monotherapy
    • abstr. 30, St. Petersburg, Fla.
    • Eastman, P. S., I. B. Duncan, C. Gee, and E. Race. 1997. Acquisition of genotypic mutations associated with reduced susceptibility to protease inhibitors during saquinavir monotherapy, abstr. 30, p. 19. In Abstracts of the International Workshop on HIV Drug Resistance, Treatment Strategies and Eradication, St. Petersburg, Fla.
    • (1997) International Workshop on HIV Drug Resistance, Treatment Strategies and Eradication , pp. 19
    • Eastman, P.S.1    Duncan, I.B.2    Gee, C.3    Race, E.4
  • 28
    • 0344796785 scopus 로고    scopus 로고
    • In vivo resistance of HIV-1 variants with reduced susceptibility to the protease inhibitor L-735,524 and related compounds
    • Emini, E. A., W. A. Schleif, P. Deutsch, and J. H. Condra. 1996. In vivo resistance of HIV-1 variants with reduced susceptibility to the protease inhibitor L-735,524 and related compounds. Antiviral Chemother. 4:327-331.
    • (1996) Antiviral Chemother. , vol.4 , pp. 327-331
    • Emini, E.A.1    Schleif, W.A.2    Deutsch, P.3    Condra, J.H.4
  • 30
    • 0342394457 scopus 로고
    • Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of the human immunodeficiency virus type 1
    • Gottlinger, H. G., J. G. Sodroski, and W. A. Haseltine. 1989. Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of the human immunodeficiency virus type 1. Proc. Natl. Acad. Sci. USA 86: 5781-5785.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5781-5785
    • Gottlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 31
    • 0029151345 scopus 로고
    • Kinetic characterization and cross-resistance patterns of HIV-1 protease mutants selected under drug pressure
    • Gulnik, S. V., L. I. Suvorov, B. Liu, B. Yu, B. Anderson, H. Mitsuya, and J. W. Erickson. 1995. Kinetic characterization and cross-resistance patterns of HIV-1 protease mutants selected under drug pressure. Biochemistry 34: 9282-9287.
    • (1995) Biochemistry , vol.34 , pp. 9282-9287
    • Gulnik, S.V.1    Suvorov, L.I.2    Liu, B.3    Yu, B.4    Anderson, B.5    Mitsuya, H.6    Erickson, J.W.7
  • 33
    • 0028874048 scopus 로고
    • Rapid turnover of plasma virions and CD4 lymphocytes in HIV-1 infection
    • Ho, D. D., A. U. Neumann, 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    Neumann, A.U.2    Perelson, A.S.3    Chen, W.4    Leonard, J.M.5    Markowitz, M.6
  • 37
    • 0025952925 scopus 로고
    • HIV protease: A novel chemotherapeutic target for AIDS
    • Huff, J. R. 1991. HIV protease: a novel chemotherapeutic target for AIDS. J. Med. Chem. 34:2305-2314.
    • (1991) J. Med. Chem. , vol.34 , pp. 2305-2314
    • Huff, J.R.1
  • 39
    • 0023870815 scopus 로고    scopus 로고
    • Characterization of ribosomal frameshifting in HIV-1 gag-pol expression
    • Jacks, T., M. D. Power, F. R. Masiarz, P. A. Luciw, P. J. Barr, and H. E. Varmus. 1998. Characterization of ribosomal frameshifting in HIV-1 gag-pol expression. Nature 331:280-283.
    • (1998) Nature , vol.331 , pp. 280-283
    • Jacks, T.1    Power, M.D.2    Masiarz, F.R.3    Luciw, P.A.4    Barr, P.J.5    Varmus, H.E.6
  • 41
    • 0028843163 scopus 로고
    • Characterization of human immunodeficiency virus type 1 mutant with decreased sensitivity to proteinase inhibitor Ro 31-8959
    • Jacobsen, H., K. Yasargil, D. L. Winslow, J. C. Craig, A. Kroehn, I. B. Duncan, and J. Mous. 1995. Characterization of human immunodeficiency virus type 1 mutant 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    Kroehn, A.5    Duncan, I.B.6    Mous, J.7
  • 42
    • 0029824426 scopus 로고    scopus 로고
    • In vivo resistance to a human immunodeficiency virus type 1 proteinase inhibitor: Mutations, kinetics, frequencies
    • Jacobsen, H., M. Hangi, 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, frequencies. J. Infect. Dis. 173:1379-1387.
    • (1996) J. Infect. Dis. , vol.173 , pp. 1379-1387
    • Jacobsen, H.1    Hangi, M.2    Ott, M.3    Duncan, I.B.4    Owen, S.5    Andreoni, M.6    Vella, S.7    Mous, J.8
  • 44
    • 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
  • 45
    • 0021846499 scopus 로고
    • Murine leukemia virus maturation: Protease region required for conversion from "immature" to "mature" core form and for virus infectivity
    • Katoh, I., Y. Yoshinaka, A. Rein, M. Shibuya, T. Odaka, and S. Oroszlan. 1985. Murine leukemia virus maturation: protease region required for conversion from "immature" to "mature" core form and for virus infectivity. Virology 145:280-292.
    • (1985) Virology , vol.145 , pp. 280-292
    • Katoh, I.1    Yoshinaka, Y.2    Rein, A.3    Shibuya, M.4    Odaka, T.5    Oroszlan, S.6
  • 46
    • 0028846226 scopus 로고
    • Crystal structure of HIV-1 protease in complex with VX-478, a potent and orally bioavailable inhibitor of the enzyme
    • Kim, E. E., C. T. Baker, M. D. Dwyer, M. A. Murcko, B. G. Rao, R. D. Tung, and M. A. Navia. 1995. Crystal structure of HIV-1 protease in complex with VX-478, a potent and orally bioavailable inhibitor of the enzyme. J. Am. Chem. Soc. 117:1181-1182.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 1181-1182
    • Kim, E.E.1    Baker, C.T.2    Dwyer, M.D.3    Murcko, M.A.4    Rao, B.G.5    Tung, R.D.6    Navia, M.A.7
  • 47
    • 0026051925 scopus 로고
    • Expression of active human immunodeficiency virus type 1 protease by noninfectious chimeric virus particles
    • Kohl, N. E., R. E. Diehl, E. Rands, L. J. Davis, M. G. Hanobik, B. Wolanski, and R. A. Dixon. 1991. Expression of active human immunodeficiency virus type 1 protease by noninfectious chimeric virus particles. J. Virol. 65:3007-3014.
    • (1991) J. Virol. , vol.65 , pp. 3007-3014
    • Kohl, N.E.1    Diehl, R.E.2    Rands, E.3    Davis, L.J.4    Hanobik, M.G.5    Wolanski, B.6    Dixon, R.A.7
  • 49
    • 0010351096 scopus 로고
    • Synthetic peptides as substrates and inhibitors of a retroviral protease
    • Kotler, M., R. A. Katz, W. Danho, J. Leis, and A. M. Skalka. 1988. Synthetic peptides as substrates and inhibitors of a retroviral protease. Proc. Natl. Acad. Sci. USA 85:4185-4189.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4185-4189
    • Kotler, M.1    Katz, R.A.2    Danho, W.3    Leis, J.4    Skalka, A.M.5
  • 51
    • 0029006027 scopus 로고
    • Impaired infectivity of HIV-1 after a single point mutation in the pol gene to escape the effect of a protease inhibitor in vitro
    • Kuroda, M. J., M. A. El-Farrash, S. Cloudhury, and S. Harada. 1995. Impaired infectivity of HIV-1 after a single point mutation in the pol gene to escape the effect of a protease inhibitor in vitro. Virology 210:212-216.
    • (1995) Virology , vol.210 , pp. 212-216
    • Kuroda, M.J.1    El-Farrash, M.A.2    Cloudhury, S.3    Harada, S.4
  • 54
    • 0023687861 scopus 로고
    • Purification and structural characterization of the putative gag-pol protease of human immunodeficiency virus
    • Lillehoj, E. P., F. H. R. Salazar, R. J. Mervis, M. G. Raum, H. W. Chan, N. Ahmad, and S. Venkatesan. 1988. Purification and structural characterization of the putative gag-pol protease of human immunodeficiency virus. J. Virol. 62:3053-3058.
    • (1988) J. Virol. , vol.62 , pp. 3053-3058
    • Lillehoj, E.P.1    Salazar, F.H.R.2    Mervis, R.J.3    Raum, M.G.4    Chan, H.W.5    Ahmad, N.6    Venkatesan, S.7
  • 56
    • 0029075130 scopus 로고    scopus 로고
    • Lower in vivo mutation rate of human immunodeficiency virus type 1 than that predicted from the fidelity of purified reverse transcriptase
    • Mansky, L. M., and H. M. Temin. 1996. Lower in vivo mutation rate of human immunodeficiency virus type 1 than that predicted from the fidelity of purified reverse transcriptase. J. Virol. 69:5087-5094.
    • (1996) J. Virol. , vol.69 , pp. 5087-5094
    • Mansky, L.M.1    Temin, H.M.2
  • 58
    • 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. N. 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    Bhat, T.N.5    Erickson, J.W.6    Ho, D.D.7
  • 59
    • 0030468331 scopus 로고    scopus 로고
    • Human immunodeficiency virus. Mutations in the viral protease that confers resistance to saquinavir increase the dissociation rate constant of the protease-saquinavir complex
    • Maschera, B., G. Darby, G. Palú, L. L. Wright, M. Tisdale, R. Meyers, E. D. Blair, and E. S. Furfine. 1996. Human immunodeficiency virus. Mutations in the viral protease that confers resistance to saquinavir increase the dissociation rate constant of the protease-saquinavir complex. J. Biol. Chem. 271: 33231-33235.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33231-33235
    • Maschera, B.1    Darby, G.2    Palú, G.3    Wright, L.L.4    Tisdale, M.5    Meyers, R.6    Blair, E.D.7    Furfine, E.S.8
  • 64
    • 0344796778 scopus 로고    scopus 로고
    • Personal communication
    • Molla, A. Personal communication.
    • Molla, A.1
  • 65
    • 1842277019 scopus 로고
    • Characterization of in vivo selected HIV-1 variants with reduced sensitivity to proteinase inhibitor saquinavir
    • abstr. 515B, Yokohama, Japan
    • Mous, J., F. Brun-Vezinet, I. B. Duncan, M. Haenggi, H. Jacobsen, and S. Vella. 1994. Characterization of in vivo selected HIV-1 variants with reduced sensitivity to proteinase inhibitor saquinavir, abstr. 515B, p. 90. In Abstracts of the 10th International Conference on AIDS, Yokohama, Japan.
    • (1994) 10th International Conference on AIDS , pp. 90
    • Mous, J.1    Brun-Vezinet, F.2    Duncan, I.B.3    Haenggi, M.4    Jacobsen, H.5    Vella, S.6
  • 68
    • 0344364937 scopus 로고    scopus 로고
    • The use of a rapid phenotypic HIV-1 drug resistance and susceptibility assay in analyzing the emergence of drug-resistant virus during triple combination therapy
    • abstr. LB-1, American Society for Microbiology, Toronto, Canada
    • Parkin, N., J. Whitcomb, D. Smith, T. Tian, K. Limoli, Y. S. Lie, G. Winslow, T. Wrin, D. Capon, and C. J. Petropoulos. 1997. The use of a rapid phenotypic HIV-1 drug resistance and susceptibility assay in analyzing the emergence of drug-resistant virus during triple combination therapy, abstr. LB-1, p. 7. In Program addendum of the 37th Interscience Conference on Antimicrobial Agents and Chemotherapy. American Society for Microbiology, Toronto, Canada.
    • (1997) 37th Interscience Conference on Antimicrobial Agents and Chemotherapy , pp. 7
    • Parkin, N.1    Whitcomb, J.2    Smith, D.3    Tian, T.4    Limoli, K.5    Lie, Y.S.6    Winslow, G.7    Wrin, T.8    Capon, D.9    Petropoulos, C.J.10
  • 70
    • 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
  • 73
    • 0029896360 scopus 로고    scopus 로고
    • Kinetic characterization of human immunodeficiency virus type 1 protease resistant variants
    • Pazhanisamy, S., C. M. Stuver, A. B. Cullinan, N. Margolin, and B. G. Rao. 1996. Kinetic characterization of human immunodeficiency virus type 1 protease resistant variants. J. Biol. Chem. 271:17979-17985.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17979-17985
    • Pazhanisamy, S.1    Stuver, C.M.2    Cullinan, A.B.3    Margolin, N.4    Rao, B.G.5
  • 74
    • 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
  • 77
    • 0024558304 scopus 로고
    • Effective blocking of HIV-1 proteinase activity by characteristic inhibitors of aspartic proteinases
    • Richards, A. D., R. Roberts, B. M. Dunn, M. C. Graves, and J. Kay. 1989. Effective blocking of HIV-1 proteinase activity by characteristic inhibitors of aspartic proteinases. FEBS Lett. 247:113.
    • (1989) FEBS Lett. , vol.247 , pp. 113
    • Richards, A.D.1    Roberts, R.2    Dunn, B.M.3    Graves, M.C.4    Kay, J.5
  • 82
    • 0030012398 scopus 로고    scopus 로고
    • Resistance-related mutations in the HIV-1 protease gene of patients treated for 1 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 Clerq, and A. M. Vandamme. 1996. Resistance-related mutations in the HIV-1 protease gene of patients treated for 1 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 Clerq, E.8    Vandamme, A.M.9
  • 83
    • 0029731556 scopus 로고    scopus 로고
    • Mutational anatomy of an HIV-1 protease variant conferring cross-resistance to protease inhibitors in clinical trials
    • Schock, H. B., V. M. Garsky, and L. C. Kuo. 1996. Mutational anatomy of an HIV-1 protease variant conferring cross-resistance to protease inhibitors in clinical trials. J. Biol. Chem. 271:31957-31963.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31957-31963
    • Schock, H.B.1    Garsky, V.M.2    Kuo, L.C.3
  • 84
    • 0030032764 scopus 로고    scopus 로고
    • Preclinical pharmacokinetics and distribution to tissue of AG1343, an inhibitor of human immunodeficiency virus type 1 protease
    • Shetty, B. V., M. B. Kosa, D. A. Khalil, and S. Webber. 1996. Preclinical pharmacokinetics and distribution to tissue of AG1343, an inhibitor of human immunodeficiency virus type 1 protease. Antimicrob. Agents Chemother. 40:110-114.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 110-114
    • Shetty, B.V.1    Kosa, M.B.2    Khalil, D.A.3    Webber, S.4
  • 86
    • 0025000261 scopus 로고
    • Properties of avian retrovirus particles defective in viral protease
    • Stewart, L., G. Schatz, and V. M. Vogt. 1990. Properties of avian retrovirus particles defective in viral protease. J. Virol. 64:5076-5092.
    • (1990) J. Virol. , vol.64 , pp. 5076-5092
    • Stewart, L.1    Schatz, G.2    Vogt, V.M.3
  • 87
    • 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
  • 88
    • 36849159719 scopus 로고
    • Retroviral protease-like sequence in the yeast transposon Ty 1
    • Toh, H., M. Ono, K. Saigo, and T. Miyata. 1985. Retroviral protease-like sequence in the yeast transposon Ty 1. Nature 315:691.
    • (1985) Nature , vol.315 , pp. 691
    • Toh, H.1    Ono, M.2    Saigo, K.3    Miyata, T.4
  • 90
    • 0028525039 scopus 로고
    • Identification of an amino acid substitution involved in the reduction of sensitivity of HIV-1 to an inhibitor of viral proteinase
    • Turriziani, O., G. Antonelli, H. Jacobsen, J. Mous, E. Riva, M. Pistello, and F. Dianzani. 1994. Identification of an amino acid substitution involved in the reduction of sensitivity of HIV-1 to an inhibitor of viral proteinase. Acta Virol. 38:297-298.
    • (1994) Acta Virol. , vol.38 , pp. 297-298
    • Turriziani, O.1    Antonelli, G.2    Jacobsen, H.3    Mous, J.4    Riva, E.5    Pistello, M.6    Dianzani, F.7
  • 92
    • 0029927979 scopus 로고    scopus 로고
    • Saquinavir/zidovudine combination in patients with advanced HIV infection and no prior antiretroviral therapy: CD4+ lymphocyte/plasma RNA changes, and emergence of HIV strains with reduced phenotypic sensitivity
    • Vella, S., C. Galluzzo, G. Giannini, M. F. Pirillo, I. Duncan, H. Jacobsen, M. Andreoni, L. Sarmati, and L. Ercoli. 1996. Saquinavir/zidovudine combination in patients with advanced HIV infection and no prior antiretroviral therapy: CD4+ lymphocyte/plasma RNA changes, and emergence of HIV strains with reduced phenotypic sensitivity. Antiviral Res. 29:91-93.
    • (1996) Antiviral Res. , vol.29 , pp. 91-93
    • Vella, S.1    Galluzzo, C.2    Giannini, G.3    Pirillo, M.F.4    Duncan, I.5    Jacobsen, H.6    Andreoni, M.7    Sarmati, L.8    Ercoli, L.9
  • 94
    • 14444287982 scopus 로고    scopus 로고
    • Genotypic and phenotypic analysis of the protease gene in HIV-1 infected patients that failed long-term saquinavir therapy and switched to other protease inhibitors
    • abstr. 17, St. Petersburg, Fla.
    • Winters, M. A., J. M. Schapiro, J. Lawrence, and T. C. Merigan. 1997. Genotypic and phenotypic analysis of the protease gene in HIV-1 infected patients that failed long-term saquinavir therapy and switched to other protease inhibitors, abstr. 17, p. 11. In Abstracts of the International Workshop on HIV Drug Resistance, Treatment Strategies and Eradication, St. Petersburg, Fla.
    • (1997) International Workshop on HIV Drug Resistance, Treatment Strategies and Eradication , pp. 11
    • Winters, M.A.1    Schapiro, J.M.2    Lawrence, J.3    Merigan, T.C.4
  • 95
    • 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. 62:543-580.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 543-580
    • Wlodawer, A.1    Erickson, J.W.2
  • 97
    • 0030769354 scopus 로고    scopus 로고
    • Drug resistance during indinavir therapy is caused by mutations in the protease gene and in its gag substrate cleavage sites
    • Zhang, Y.-M., H. Imamichi, T. Imamichi, H. C. Lane, J. Falloon, M. B. Vasudevachari, and N. P. Salzman. 1997. Drug resistance during indinavir therapy is caused by mutations in the protease gene and in its gag substrate cleavage sites. J. Virol. 71:6662-6670.
    • (1997) J. Virol. , vol.71 , pp. 6662-6670
    • Zhang, Y.-M.1    Imamichi, H.2    Imamichi, T.3    Lane, H.C.4    Falloon, J.5    Vasudevachari, M.B.6    Salzman, N.P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.