메뉴 건너뛰기




Volumn 44, Issue 5, 2005, Pages 1595-1606

Dissecting the effects of DNA polymerase and ribonuclease H inhibitor combinations on HIV-1 reverse-transcriptase activities

Author keywords

[No Author keywords available]

Indexed keywords

BIOASSAY; CRYSTAL STRUCTURE; ENZYME KINETICS; ENZYMES; GELS; ORGANIC ACIDS; RNA;

EID: 13444257639     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0486740     Document Type: Article
Times cited : (78)

References (34)
  • 1
    • 0023608993 scopus 로고
    • Phosphonoformate (foscarnet): A pilot study in AIDS and AIDS related complex
    • Farthing, C. F., Dalgleish, A. G., Clark, A., McClure, M., Chanas, A., and Gazzard, B. G. (1987) Phosphonoformate (foscarnet): A pilot study in AIDS and AIDS related complex, AIDS 1, 21-25.
    • (1987) AIDS , vol.1 , pp. 21-25
    • Farthing, C.F.1    Dalgleish, A.G.2    Clark, A.3    McClure, M.4    Chanas, A.5    Gazzard, B.G.6
  • 2
    • 0029044698 scopus 로고
    • Novel mutations in reverse transcriptase of human immunodeficiency virus type 1 reduce susceptibility to foscarnet in laboratory and clinical isolates
    • Mellors, J. W., Bazmi, H. Z., Schinazi, R. F., Roy, B. M., Hsiou, Y., Arnold, E., Weir, J., and Mayers, D. L. (1995) Novel mutations in reverse transcriptase of human immunodeficiency virus type 1 reduce susceptibility to foscarnet in laboratory and clinical isolates, Antimicrob. Agents Chemother. 39, 1087-1092.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1087-1092
    • Mellors, J.W.1    Bazmi, H.Z.2    Schinazi, R.F.3    Roy, B.M.4    Hsiou, Y.5    Arnold, E.6    Weir, J.7    Mayers, D.L.8
  • 3
    • 0030966369 scopus 로고    scopus 로고
    • Mutations within the primer grip region of HIV-1 reverse transcriptase result in loss of RNasè H function
    • Palaniappan, C., Wisniewski, M., Jacques, P. S., Le Grice, S. F., Fay, P. J., and Bambara, R. A. (1997) Mutations within the primer grip region of HIV-1 reverse transcriptase result in loss of RNasè H function, J. Biol. Chem. 272, 11157-11164.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11157-11164
    • Palaniappan, C.1    Wisniewski, M.2    Jacques, P.S.3    Le Grice, S.F.4    Fay, P.J.5    Bambara, R.A.6
  • 4
    • 0037117744 scopus 로고    scopus 로고
    • Altering the RNase H primer grip of human immunodeficiency virus reverse transcriptase modifies cleavage specificity
    • Rausch, J. W., Lener, D., Miller, J. T., Julias, J. G., Hughes, S. H., and Le Grice, S. F. (2002) Altering the RNase H primer grip of human immunodeficiency virus reverse transcriptase modifies cleavage specificity, Biochemistry 41, 4856-4865.
    • (2002) Biochemistry , vol.41 , pp. 4856-4865
    • Rausch, J.W.1    Lener, D.2    Miller, J.T.3    Julias, J.G.4    Hughes, S.H.5    Le Grice, S.F.6
  • 5
    • 0037047073 scopus 로고    scopus 로고
    • Mutations in the RNase H domain of HIV-1 reverse transcriptase affect the initiation of DNA synthesis and the specificity of RNase H cleavage in vivo
    • Julias, J. G., McWilliams, M. J., Sarafianos, S. G., Arnold, E., and Hughes, S. H. (2002) Mutations in the RNase H domain of HIV-1 reverse transcriptase affect the initiation of DNA synthesis and the specificity of RNase H cleavage in vivo, Proc. Natl. Acad. Sci. U.S.A. 99, 9515-9520.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 9515-9520
    • Julias, J.G.1    McWilliams, M.J.2    Sarafianos, S.G.3    Arnold, E.4    Hughes, S.H.5
  • 6
    • 0038107748 scopus 로고    scopus 로고
    • Mutation of amino acids in the connection domain of human immunodeficiency virus type 1 reverse transcriptase that contact the template-primer affects RNase H activity
    • Julias, J. G., McWilliams, M. J., Sarafianos, S. G., Alvord, W. G., Arnold, E., and Hughes, S. H. (2003) Mutation of amino acids in the connection domain of human immunodeficiency virus type 1 reverse transcriptase that contact the template-primer affects RNase H activity, J. Virol. 77, 8548-8554.
    • (2003) J. Virol. , vol.77 , pp. 8548-8554
    • Julias, J.G.1    McWilliams, M.J.2    Sarafianos, S.G.3    Alvord, W.G.4    Arnold, E.5    Hughes, S.H.6
  • 7
    • 0028926938 scopus 로고
    • Nevirapine alters the cleavage specificity of ribonuclease H of human immunodeficiency virus 1 reverse transcriptase
    • Palaniappan, C., Fay, P. J., and Bambara, R. A. (1995) Nevirapine alters the cleavage specificity of ribonuclease H of human immunodeficiency virus 1 reverse transcriptase, J. Biol. Chem. 270, 4861-4869.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4861-4869
    • Palaniappan, C.1    Fay, P.J.2    Bambara, R.A.3
  • 8
    • 0028023808 scopus 로고
    • Effect of a thiobenzimidazolone derivative on DNA strand transfer catalyzed by HIV-1 reverse transcriptase
    • Gopalakrishnan, V., and Benkovic, S. (1994) Effect of a thiobenzimidazolone derivative on DNA strand transfer catalyzed by HIV-1 reverse transcriptase, J. Biol. Chem. 269, 4110-4115.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4110-4115
    • Gopalakrishnan, V.1    Benkovic, S.2
  • 9
    • 0033863784 scopus 로고    scopus 로고
    • Mutants of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase resistant to nonnucleoside reverse transcriptase inhibitors demonstrate altered rates of RNase H cleavage that correlate with HIV-1 replication fitness in cell culture
    • Archer, R. H., Dykes, C., Gerondelis, P., Lloyd, A., Fay, P., Reichman, R. C., Bambara, R. A., and Demeter, L. M. (2000) Mutants of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase resistant to nonnucleoside reverse transcriptase inhibitors demonstrate altered rates of RNase H cleavage that correlate with HIV-1 replication fitness in cell culture, J. Virol. 74, 8390-8401.
    • (2000) J. Virol. , vol.74 , pp. 8390-8401
    • Archer, R.H.1    Dykes, C.2    Gerondelis, P.3    Lloyd, A.4    Fay, P.5    Reichman, R.C.6    Bambara, R.A.7    Demeter, L.M.8
  • 10
    • 0035799358 scopus 로고    scopus 로고
    • The Y181C mutant of HIV-1 reverse transcriptase resistant to nonnucleoside reverse transcriptase inhibitors alters the size distribution of RNase H cleavages
    • Archer, R. H., Wisniewski, M., Bambara, R. A., and Demeter, L. M. (2001) The Y181C mutant of HIV-1 reverse transcriptase resistant to nonnucleoside reverse transcriptase inhibitors alters the size distribution of RNase H cleavages, Biochemistry 40, 4087-4095.
    • (2001) Biochemistry , vol.40 , pp. 4087-4095
    • Archer, R.H.1    Wisniewski, M.2    Bambara, R.A.3    Demeter, L.M.4
  • 11
    • 0032993043 scopus 로고    scopus 로고
    • The P236L delavirdine-resistant human immunodeficiency virus type 1 mutant is replication defective and demonstrates alterations in both RNA 5′-end- and DNA 3′-end-directed RNase H activities
    • Gerondelis, P., Archer, R. H., Palaniappan, C., Reichman, R. C., Fay, P. J., Bambara, R. A., and Demeter, L. M. (1999) The P236L delavirdine-resistant human immunodeficiency virus type 1 mutant is replication defective and demonstrates alterations in both RNA 5′-end- and DNA 3′-end-directed RNase H activities, J. Virol. 73, 5803-5813.
    • (1999) J. Virol. , vol.73 , pp. 5803-5813
    • Gerondelis, P.1    Archer, R.H.2    Palaniappan, C.3    Reichman, R.C.4    Fay, P.J.5    Bambara, R.A.6    Demeter, L.M.7
  • 12
    • 0141758137 scopus 로고    scopus 로고
    • A fluorescence-based high-throughput screening assay for inhibitors of human immunodeficiency virus-1 reverse transcriptase-associated ribonuclease H activity
    • Parniak, M. A., Min, K. L., Budihas, S. R., Le Grice, S. F., and Beutler, J. A. (2003) A fluorescence-based high-throughput screening assay for inhibitors of human immunodeficiency virus-1 reverse transcriptase-associated ribonuclease H activity, Anal. Biochem. 322, 33-39.
    • (2003) Anal. Biochem. , vol.322 , pp. 33-39
    • Parniak, M.A.1    Min, K.L.2    Budihas, S.R.3    Le Grice, S.F.4    Beutler, J.A.5
  • 15
    • 0032847978 scopus 로고    scopus 로고
    • Inhibitors of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase
    • Gabbara, S., Davis, W. R., Hupe, L., Hupe, D., and Peliska, J. A. (1999) Inhibitors of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase, Biochemistry 38, 13070-13076.
    • (1999) Biochemistry , vol.38 , pp. 13070-13076
    • Gabbara, S.1    Davis, W.R.2    Hupe, L.3    Hupe, D.4    Peliska, J.A.5
  • 16
    • 13444276992 scopus 로고    scopus 로고
    • Segel, I. H. (1975) pp 474-488, John Wiley and Sons, Inc., New York
    • Segel, I. H. (1975) pp 474-488, John Wiley and Sons, Inc., New York.
  • 17
    • 0021118703 scopus 로고
    • Quantitative analysis of dose-effect relationships: The combined effects of multiple drugs or enzyme inhibitors
    • Chou, T. C., and Talalay, P. (1984) Quantitative analysis of dose-effect relationships: The combined effects of multiple drugs or enzyme inhibitors, Adv. Enzyme Regul. 22, 27-55.
    • (1984) Adv. Enzyme Regul. , vol.22 , pp. 27-55
    • Chou, T.C.1    Talalay, P.2
  • 18
    • 0034700290 scopus 로고    scopus 로고
    • Inhibition of HIV-1 reverse transcriptase-catalyzed DNA strand transfer reactions by 4-chlorophenylhydrazone of mesoxalic acid
    • Davis, W. R., Tomsho, J., Nikam, S., Cook, E. M., Somand, D., and Peliska, J. A. (2000) Inhibition of HIV-1 reverse transcriptase-catalyzed DNA strand transfer reactions by 4-chlorophenylhydrazone of mesoxalic acid, Biochemistry 39, 14279-14291.
    • (2000) Biochemistry , vol.39 , pp. 14279-14291
    • Davis, W.R.1    Tomsho, J.2    Nikam, S.3    Cook, E.M.4    Somand, D.5    Peliska, J.A.6
  • 20
    • 0036090544 scopus 로고    scopus 로고
    • Potency of nonnucleoside reverse transcriptase inhibitors (NNRTIs) used in combination with other human immunodeficiency virus NNRTIs, NRTIs, or protease inhibitors
    • King, R. W., Klabe, R. M., Reid, C. D., and Erickson-Viitanen, S. K. (2002) Potency of nonnucleoside reverse transcriptase inhibitors (NNRTIs) used in combination with other human immunodeficiency virus NNRTIs, NRTIs, or protease inhibitors, Antimicrob. Agents Chemother. 46, 1640-1646.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 1640-1646
    • King, R.W.1    Klabe, R.M.2    Reid, C.D.3    Erickson-Viitanen, S.K.4
  • 21
    • 0028569182 scopus 로고
    • Inhibition of HIV-1 reverse transcriptase by a quinazolinone and comparison with inhibition by pyridinones. Differences in the rates of inhibitor binding and in synergistic inhibition with nucleoside analogs
    • Carroll, S. S., Stahlhut, M., Geib, J., and Olsen, D. B. (1994) Inhibition of HIV-1 reverse transcriptase by a quinazolinone and comparison with inhibition by pyridinones. Differences in the rates of inhibitor binding and in synergistic inhibition with nucleoside analogs, J. Biol. Chem. 269, 32351-32357.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32351-32357
    • Carroll, S.S.1    Stahlhut, M.2    Geib, J.3    Olsen, D.B.4
  • 22
    • 0026010601 scopus 로고
    • Synergistic inhibition of human immunodeficiency virus type 1 replication in vitro by two-drug and three-drug combinations of 3′-azido-3′- deoxythymidine, phosphonoformate, and 2′,3′-dideoxythymidine
    • Kong, X. B., Zhu, Q. Y., Ruprecht, R. M., Watanabe, K. A., Zeidler, J. M., Gold, J. W., Polsky, B., Armstrong, D., and Chou, T. C. (1991) Synergistic inhibition of human immunodeficiency virus type 1 replication in vitro by two-drug and three-drug combinations of 3′-azido-3′-deoxythymidine, phosphonoformate, and 2′,3′-dideoxythymidine, Antimicrob. Agents Chemother. 35, 2003-2011.
    • (1991) Antimicrob. Agents Chemother. , vol.35 , pp. 2003-2011
    • Kong, X.B.1    Zhu, Q.Y.2    Ruprecht, R.M.3    Watanabe, K.A.4    Zeidler, J.M.5    Gold, J.W.6    Polsky, B.7    Armstrong, D.8    Chou, T.C.9
  • 23
    • 0030586090 scopus 로고    scopus 로고
    • Structure of unliganded HIV-1 reverse transcriptase at 2.7 Å resolution: Implications of conformational changes for polymerization and inhibition mechanisms
    • Hsiou, Y., Ding, J., Das, K., Clark, A. D., Jr., Hughes, S. H., and Arnold, E. (1996) Structure of unliganded HIV-1 reverse transcriptase at 2.7 Å resolution: Implications of conformational changes for polymerization and inhibition mechanisms, Structure 4, 853-860.
    • (1996) Structure , vol.4 , pp. 853-860
    • Hsiou, Y.1    Ding, J.2    Das, K.3    Clark Jr., A.D.4    Hughes, S.H.5    Arnold, E.6
  • 26
    • 0036782103 scopus 로고    scopus 로고
    • Inhibitor binding alters the directions of domain motions in HIV-1 reverse transcriptase
    • Temiz, N. A., and Bahar, I. (2002) Inhibitor binding alters the directions of domain motions in HIV-1 reverse transcriptase, Proteins 49, 61-70.
    • (2002) Proteins , vol.49 , pp. 61-70
    • Temiz, N.A.1    Bahar, I.2
  • 27
    • 0029075207 scopus 로고
    • Structure of HIV-1 RT/TIBO R 86183 complex reveals similarity in the binding of diverse nonnucleoside inhibitors
    • Ding, J., Das, K., Moereels, H., Koymans, L., Andries, K., Janssen, P. A., Hughes, S. H., and Arnold, E. (1995) Structure of HIV-1 RT/TIBO R 86183 complex reveals similarity in the binding of diverse nonnucleoside inhibitors, Nat. Struct. Biol. 2, 407-415.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 407-415
    • Ding, J.1    Das, K.2    Moereels, H.3    Koymans, L.4    Andries, K.5    Janssen, P.A.6    Hughes, S.H.7    Arnold, E.8
  • 31
    • 0035889686 scopus 로고    scopus 로고
    • Molecular dynamics of HIV-1 reverse transcriptase indicates increased flexibility upon DNA binding
    • Madrid, M., Lukin, J. A., Madura, J. D., Ding, J., and Arnold, E. (2001) Molecular dynamics of HIV-1 reverse transcriptase indicates increased flexibility upon DNA binding, Proteins 45, 176-182.
    • (2001) Proteins , vol.45 , pp. 176-182
    • Madrid, M.1    Lukin, J.A.2    Madura, J.D.3    Ding, J.4    Arnold, E.5
  • 32
    • 0027382852 scopus 로고
    • Two defective forms of reverse transcriptase can complement to restore retroviral infectivity
    • Telesnitsky, A., and Goff, S. P. (1993) Two defective forms of reverse transcriptase can complement to restore retroviral infectivity, EMBO J. 12, 4433-4438.
    • (1993) EMBO J. , vol.12 , pp. 4433-4438
    • Telesnitsky, A.1    Goff, S.P.2
  • 33
    • 0034990535 scopus 로고    scopus 로고
    • Replication of phenotypically mixed human immunodeficiency virus type 1 virions containing catalytically active and catalytically inactive reverse transcriptase
    • Julias, J. G., Ferris, A. L., Boyer, P. L., and Hughes, S. H. (2001) Replication of phenotypically mixed human immunodeficiency virus type 1 virions containing catalytically active and catalytically inactive reverse transcriptase, J. Virol. 75, 6537-6546.
    • (2001) J. Virol. , vol.75 , pp. 6537-6546
    • Julias, J.G.1    Ferris, A.L.2    Boyer, P.L.3    Hughes, S.H.4
  • 34
    • 0035834131 scopus 로고    scopus 로고
    • Dynamic copy choice: Steady state between murine leukemia virus polymerase and polymerase-dependent RNase H activity determines frequency of in vivo template switching
    • Hwang, C. K., Svarovskaia, E. S., and Pathak, V. K. (2001) Dynamic copy choice: Steady state between murine leukemia virus polymerase and polymerase-dependent RNase H activity determines frequency of in vivo template switching, Proc. Natl. Acad. Sci. U.S.A. 98, 12209-12214.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 12209-12214
    • Hwang, C.K.1    Svarovskaia, E.S.2    Pathak, V.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.