메뉴 건너뛰기




Volumn 50, Issue 5, 1996, Pages 1057-1064

Differences in the inhibition of human immunodeficiency virus type 1 reverse transcriptase DNA polymerase activity by analogs of nevirapine and [2',5'-bis-O-(tert-butyldimethylsilyl)3'-spiro-5''-(4''-amino-1'', 2''- oxathiole-2'',2''-dioxide] (TSAO)

Author keywords

[No Author keywords available]

Indexed keywords

1 [2',5' BIS O (TERT BUTYLDIMETHYLSILYL) BETA RIBOFURANOSYL] 3' SPIRO 5'' (4'' AMINO 1'', 2'' OXATHIOLE 2'',2'' DIOXIDE) 3 ETHYLTHYMINE; 9 AMINONEVIRAPINE; DNA POLYMERASE; NEVIRAPINE DERIVATIVE; RNA DIRECTED DNA POLYMERASE; RNA DIRECTED DNA POLYMERASE INHIBITOR; UNCLASSIFIED DRUG; ZIDOVUDINE;

EID: 0029804757     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (15)

References (40)
  • 1
    • 0001707601 scopus 로고
    • 3′-Azido-3′deoxythymidine (BWA509U): An antiviral agent that inhibits the infectivity and cytopathic effect of human T-lymphotropic virus type III/lymphadenopathy-associated virus in vitro
    • Mitsuya, H., K. J. Weinhold, P. A. Furman, M. H. St. Clair, S. N. Lehrman, R. C. Gallo, D. Bolognesi, D. W. Barry, and S. Broder. 3′-Azido-3′deoxythymidine (BWA509U): an antiviral agent that inhibits the infectivity and cytopathic effect of human T-lymphotropic virus type III/lymphadenopathy-associated virus in vitro. Proc. Natl. Acad. Sci. USA 82:7096-7100 (1985).
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7096-7100
    • Mitsuya, H.1    Weinhold, K.J.2    Furman, P.A.3    St. Clair, M.H.4    Lehrman, S.N.5    Gallo, R.C.6    Bolognesi, D.7    Barry, D.W.8    Broder, S.9
  • 3
    • 0025339708 scopus 로고
    • Selective action of 3′-azido-3′-dideoxythymidine 5′-triphosphate on viral reverse transcriptase and human DNA polymerases
    • Huang, P., D. Farquhar, and W. Plunkett. Selective action of 3′-azido-3′-dideoxythymidine 5′-triphosphate on viral reverse transcriptase and human DNA polymerases. J. Biol. Chem. 265:11914-11918 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 11914-11918
    • Huang, P.1    Farquhar, D.2    Plunkett, W.3
  • 4
    • 0025866982 scopus 로고
    • Anti-human immunodeficiency virus type 1 activity and in vitro toxicity of 2′-deoxy-3′-thiacytidine (BCH-189), a novel heterocyclic nucleoside analog
    • Soudeyns, H., X-J. Yao, Q. Gao, B. Belleau, J-L. Kraus, N. Nguyen-Ba, B. Spira, and M. A. Wainberg. Anti-human immunodeficiency virus type 1 activity and in vitro toxicity of 2′-deoxy-3′-thiacytidine (BCH-189), a novel heterocyclic nucleoside analog. Antimicrob. Agents Chemother. 35:1386-1390 (1991).
    • (1991) Antimicrob. Agents Chemother. , vol.35 , pp. 1386-1390
    • Soudeyns, H.1    Yao, X.-J.2    Gao, Q.3    Belleau, B.4    Kraus, J.-L.5    Nguyen-Ba, N.6    Spira, B.7    Wainberg, M.A.8
  • 7
    • 0028034266 scopus 로고
    • The K65R mutant reverse transcriptase of HIV-1 cross resistant to 2′,3′-dideoxycytidine, 2′,3′-dideoxy-3′-thiacytidine, and 2′,3′-dideoxyinosine shows reduced sensitivity to specific dideoxynucleoside triphosphate inhibitors in vitro
    • Gu, Z., R. S. Fletcher, E. J. Arts, M. A. Wainberg, and M. A. Parniak. The K65R mutant reverse transcriptase of HIV-1 cross resistant to 2′,3′-dideoxycytidine, 2′,3′-dideoxy-3′-thiacytidine, and 2′,3′-dideoxyinosine shows reduced sensitivity to specific dideoxynucleoside triphosphate inhibitors in vitro. J. Biol. Chem. 269:28118-28122 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 28118-28122
    • Gu, Z.1    Fletcher, R.S.2    Arts, E.J.3    Wainberg, M.A.4    Parniak, M.A.5
  • 8
    • 0028940368 scopus 로고
    • Mutated K65R recombinant reverse transcriptase of human immunodeficiency virus type 1 shows diminished chain termination in the presence of 2′,3′-dideoxycytidine 5′-triphosphate and other drugs
    • Gu, Z., E. J. Arts, M. A. Parniak, and M. A. Wainberg. Mutated K65R recombinant reverse transcriptase of human immunodeficiency virus type 1 shows diminished chain termination in the presence of 2′,3′-dideoxycytidine 5′-triphosphate and other drugs. Proc. Natl. Acad. Sci. USA 92:2760-2764 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2760-2764
    • Gu, Z.1    Arts, E.J.2    Parniak, M.A.3    Wainberg, M.A.4
  • 10
    • 0025822033 scopus 로고
    • Steady state kinetics and inhibition of HIV-1 reverse transcriptase by a non-nucleoside dipyridodiazepinone, BI-RG-587, using a heteropolymeric template
    • Kopp, E. B., J. J. Miglietta, A. G. Shrutkowski, C-K. Shih, P. M. Grob, and M. T. Skoog. Steady state kinetics and inhibition of HIV-1 reverse transcriptase by a non-nucleoside dipyridodiazepinone, BI-RG-587, using a heteropolymeric template. Nucleic Acids Res. 19:3035-3039 (1991).
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3035-3039
    • Kopp, E.B.1    Miglietta, J.J.2    Shrutkowski, A.G.3    Shih, C.-K.4    Grob, P.M.5    Skoog, M.T.6
  • 14
    • 0028922944 scopus 로고
    • Carboxanilide derivative non-nucleoside inhibitors of HIV-1 reverse transcriptase interact with different mechanistic forms of the enzyme
    • Fletcher, R. S., K. Syed, S. Mithani, G. I. Dmitrienko, and M. A. Parniak. Carboxanilide derivative non-nucleoside inhibitors of HIV-1 reverse transcriptase interact with different mechanistic forms of the enzyme. Biochemistry 34:4346-4353 (1995).
    • (1995) Biochemistry , vol.34 , pp. 4346-4353
    • Fletcher, R.S.1    Syed, K.2    Mithani, S.3    Dmitrienko, G.I.4    Parniak, M.A.5
  • 15
    • 0029153101 scopus 로고
    • Synergistic inhibition of HIV-1 reverse transcriptase DNA polymerase activity and virus replication in vitro by combinations of carboxanilide nonnucleoside compounds
    • Fletcher, R. S., D. Arion, G. Borkow, M. A. Wainberg, G. I. Dmitrienko, and M. A. Parniak. Synergistic inhibition of HIV-1 reverse transcriptase DNA polymerase activity and virus replication in vitro by combinations of carboxanilide nonnucleoside compounds. Biochemistry 34:10106-10112 (1995).
    • (1995) Biochemistry , vol.34 , pp. 10106-10112
    • Fletcher, R.S.1    Arion, D.2    Borkow, G.3    Wainberg, M.A.4    Dmitrienko, G.I.5    Parniak, M.A.6
  • 17
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 a resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt, L. A., J. Wang, J. M. Friedman, P. A. Rice, and T. A. Steitz. Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science (Washington D. C.) 256:1783-1790 (1992).
    • (1992) Science (Washington D. C.) , vol.256 , pp. 1783-1790
    • Kohlstaedt, L.A.1    Wang, J.2    Friedman, J.M.3    Rice, P.A.4    Steitz, T.A.5
  • 18
    • 0028271687 scopus 로고
    • Structure of the binding site for nonnucleoside inhibitors of the reverse transcriptase of human immunodeficiency virus type 1
    • Smerdon, S. J., J. Jäger, L. A. Kohlstaedt, A. J. Chirino, J. M. Friedman, P. A. Rice, and T. A. Steitz. Structure of the binding site for nonnucleoside inhibitors of the reverse transcriptase of human immunodeficiency virus type 1. Proc. Natl. Acad. Sci. USA 91:3911-3915 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3911-3915
    • Smerdon, S.J.1    Jäger, J.2    Kohlstaedt, L.A.3    Chirino, A.J.4    Friedman, J.M.5    Rice, P.A.6    Steitz, T.A.7
  • 19
  • 21
    • 0026724892 scopus 로고
    • Kinetics of inhibition of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase by the novel HIV-1-specific nucleoside analogue [2′,5′-bis-o-(terf-butyldimethylsilyl)-b-D-ribofuranosyl]-3′- spiro-5″-(4″-amino-1″, 2″-oxathiole-2″, 2″-dioxide)thymine (TSAO-T)
    • Balzarini, J., M-J. Pérez-Pérez, A. San-Félix, M-J. Camarasa, I. C. Bathurst, P. J. Barr, and E. De Clercq. Kinetics of inhibition of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase by the novel HIV-1-specific nucleoside analogue [2′,5′-bis-o-(terf-butyldimethylsilyl)-b-D-ribofuranosyl]-3′- spiro-5″-(4″-amino-1″, 2″-oxathiole-2″, 2″-dioxide)thymine (TSAO-T). J. Biol. Chem. 267:11831-11838 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 11831-11838
    • Balzarini, J.1    Pérez-Pérez, M.-J.2    San-Félix, A.3    Camarasa, M.-J.4    Bathurst, I.C.5    Barr, P.J.6    De Clercq, E.7
  • 22
    • 0026606044 scopus 로고
    • 2′,5′-bis-o-(tertbutyldimethylsilyl)-3′-spiro-5″ - (4″-amino-1″, 2″-oxathiole-2″, 2″-dioxide) pyrimidine (TSAO) nucleoside analogues: Highly selective inhibitors of human immunodeficiency virus type 1 that are targeted at the viral reverse transcriptase
    • Balzarini, J., M-J. Pérez-Pérez, A. San-Félix, D. Schols, C-F. Perno, A-M. Vandamme, M-J. Camarasa, and E. De Clercq. 2′,5′-bis-o-(tertbutyldimethylsilyl)-3′-spiro-5″- (4″-amino-1″, 2″-oxathiole-2″, 2″-dioxide) pyrimidine (TSAO) nucleoside analogues: highly selective inhibitors of human immunodeficiency virus type 1 that are targeted at the viral reverse transcriptase. Proc. Natl. Acad. Sci. USA 89:4392-4396 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4392-4396
    • Balzarini, J.1    Pérez-Pérez, M.-J.2    San-Félix, A.3    Schols, D.4    Perno, C.-F.5    Vandamme, A.-M.6    Camarasa, M.-J.7    De Clercq, E.8
  • 23
    • 0027202617 scopus 로고
    • Human immunodeficiency virus type 1 (HIV-1) strains selected for resistance against the HIV-1-specific [2′,5′-bis-o-(tert- butyldimethylsilyl)ribofuranosyl]-3′-spiro-5″-(4″- Amino-1 ″, 2″-oxathiole-2″, 2″-dioxide)-b-D- pentofuranosyl (TSAO) nucleoside analogues retain sensitivity to HIV-1-specific nonnucleoside inhibitors
    • Balzarini, J., A. Karlsson, A-M. Vandamme, M-J. Pérez-Pérez, H. Zhang, L. Vrang, B. Oberg, K. Backbro, T. Unge, A. San-Felix, S. Velázquez, M-J. Camarasa, and E. De Clercq. Human immunodeficiency virus type 1 (HIV-1) strains selected for resistance against the HIV-1-specific [2′,5′-bis-o-(tert-butyldimethylsilyl)ribofuranosyl]-3′-spiro- 5″-(4″- amino-1″, 2″-oxathiole-2″, 2″-dioxide)]-b-D- pentofuranosyl (TSAO) nucleoside analogues retain sensitivity to HIV-1-specific nonnucleoside inhibitors. Proc. Natl. Acad. Sci. USA 90:6952-6956 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6952-6956
    • Balzarini, J.1    Karlsson, A.2    Vandamme, A.-M.3    Pérez-Pérez, M.-J.4    Zhang, H.5    Vrang, L.6    Oberg, B.7    Backbro, K.8    Unge, T.9    San-Felix, A.10    Velázquez, S.11    Camarasa, M.-J.12    De Clercq, E.13
  • 24
    • 0028024028 scopus 로고
    • Subunit specificity of mutations that confer resistance to nonnucleoside inhibitors in human immunodeficiency virus type 1 reverse transcriptase
    • Boyer, P. L., J. Ding. E. Arnold, and S. H. Hughes. Subunit specificity of mutations that confer resistance to nonnucleoside inhibitors in human immunodeficiency virus type 1 reverse transcriptase. Antimicrob. Agents Chemother. 38:1909-1914 (1994).
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1909-1914
    • Boyer, P.L.1    Ding, J.2    Arnold, E.3    Hughes, S.H.4
  • 25
    • 0028099251 scopus 로고
    • Resistance of HIV-1 reverse transcriptase against [2′,5′-bis-o-(tert-butyldimethylsilyl)-3′-spiro-5″- (4″-amino-1″, 2″-oxathiole-2″, 2″-dioxide)] (TSAO)
    • Jonckheere, H., J-M. Taymans, J. Balzarini, S. Velázquez, M-J. Camarasa, J. Desmyter, E. De Clercq, and J. Anné. Resistance of HIV-1 reverse transcriptase against [2′,5′-bis-o-(tert-butyldimethylsilyl)-3′-spiro-5″- (4″-amino-1″, 2″-oxathiole-2″, 2″-dioxide)] (TSAO). J. Biol. Chem. 269:25255-25258 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 25255-25258
    • Jonckheere, H.1    Taymans, J.-M.2    Balzarini, J.3    Velázquez, S.4    Camarasa, M.-J.5    Desmyter, J.6    De Clercq, E.7    Anné, J.8
  • 28
    • 0026737678 scopus 로고
    • TSAO analogues. Stereospecific synthesis and anti-HIV-1 activity of 1-[2′,5′-bis-o-(tert-butyldimethylsilyl)-b-D-ribofuranosyl]- 3′-spiro-5″-(4″-amino-1″, 2″-oxathiole-2″, 2″-dioxide) pyrimidine and pyrimidine-modified nucleosides
    • Pérez-Pérez, M-J., A. San-Félix, J. Balzarini, E. De Clercq, and M-J. Camarasa. TSAO analogues. Stereospecific synthesis and anti-HIV-1 activity of [1-[2′,5′-bis-o-(tert-butyldimethylsilyl)-b-D-ribofuranosyl]- 3′-spiro-5″-(4″-amino-1″, 2″-oxathiole-2″, 2″-dioxide) pyrimidine and pyrimidine-modified nucleosides. J. Med. Chem. 35:2988-2995 (1992).
    • (1992) J. Med. Chem. , vol.35 , pp. 2988-2995
    • Pérez-Pérez, M.-J.1    San-Félix, A.2    Balzarini, J.3    De Clercq, E.4    Camarasa, M.-J.5
  • 29
    • 0028176053 scopus 로고
    • Lys-3 as primers in an endogenous human immunodeficiency virus-1 in vitro reverse transcription/template switching reaction
    • Lys-3 as primers in an endogenous human immunodeficiency virus-1 in vitro reverse transcription/template switching reaction. J. Biol. Chem. 269:14672-14680 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 14672-14680
    • Arts, E.J.1    Li, X.2    Gu, Z.3    Kleiman, L.4    Parniak, M.A.5    Wainberg, M.A.6
  • 31
    • 0021118703 scopus 로고
    • Quantitative analysis of dose-effect relationships: The combined effects of multiple drugs or enzyme inhibitors
    • Chou, T.-C., and P. Talalay. Quantitative analysis of dose-effect relationships: the combined effects of multiple drugs or enzyme inhibitors. Adv. Enzyme Regul. 22:27-55 (1984).
    • (1984) Adv. Enzyme Regul. , vol.22 , pp. 27-55
    • Chou, T.-C.1    Talalay, P.2
  • 32
    • 0027424779 scopus 로고
    • Kinetic analysis of template-primer interactions with recombinant forms of HIV-1 reverse transcriptase
    • Beard, W. A., and S. H. Wilson. Kinetic analysis of template-primer interactions with recombinant forms of HIV-1 reverse transcriptase. Biochemistry 32:9745-9753 (1993).
    • (1993) Biochemistry , vol.32 , pp. 9745-9753
    • Beard, W.A.1    Wilson, S.H.2
  • 33
    • 0028172345 scopus 로고
    • Locations of anti-AIDS drug binding sites and resistance mutations in the three-dimensional structure of HTV-1 reverse transcriptase. Implications for mechanism of drug inhibition and resistance
    • Tantillo, C., J. Ding, A. Jacobo-Molina, R. G. Nanni, P. L. Boyer, S. H. Hughes, R. Pauwels, K. Andries, P. A. J. Janssen, and E. Arnold. Locations of anti-AIDS drug binding sites and resistance mutations in the three-dimensional structure of HTV-1 reverse transcriptase. Implications for mechanism of drug inhibition and resistance. J. Mol. Biol. 243:369-387 (1994).
    • (1994) J. Mol. Biol. , vol.243 , pp. 369-387
    • Tantillo, C.1    Ding, J.2    Jacobo-Molina, A.3    Nanni, R.G.4    Boyer, P.L.5    Hughes, S.H.6    Pauwels, R.7    Andries, K.8    Janssen, P.A.J.9    Arnold, E.10
  • 34
    • 0024519430 scopus 로고
    • Human immunodeficiency virus 1 reverse transcriptase. Template binding, processivity, strand displacement synthesis, and template switching
    • Huber, E. H., J. M. McCoy, J. S. Seerah, and C. C. Richardson. Human immunodeficiency virus 1 reverse transcriptase. Template binding, processivity, strand displacement synthesis, and template switching. J. Biol. Chem. 264:4669-4678 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 4669-4678
    • Huber, E.H.1    McCoy, J.M.2    Seerah, J.S.3    Richardson, C.C.4
  • 35
    • 0025054298 scopus 로고
    • Synthesis of DNA by human immunodeficiency virus reverse transcriptase is preferentially blocked at template oligo(deoxyadenosine) tracts
    • Williams, K. J., L. A. Loeb, and M. Fry. Synthesis of DNA by human immunodeficiency virus reverse transcriptase is preferentially blocked at template oligo(deoxyadenosine) tracts. J. Biol. Chem. 265:18682-18689 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 18682-18689
    • Williams, K.J.1    Loeb, L.A.2    Fry, M.3
  • 36
    • 0027215749 scopus 로고
    • Mechanism of HIV-1 reverse transcriptase. Termination of processive synthesis on a natural DNA template is influenced by the sequence of the template-primer stem
    • Abbotts, J., K. Bebenek, T. A Kunkel, and S. H. Wilson. Mechanism of HIV-1 reverse transcriptase. Termination of processive synthesis on a natural DNA template is influenced by the sequence of the template-primer stem. J. Biol. Chem. 268:10312-10323 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 10312-10323
    • Abbotts, J.1    Bebenek, K.2    Kunkel, T.A.3    Wilson, S.H.4
  • 37
    • 0027238697 scopus 로고
    • Template-directed pausing of DNA synthesis by HIV-1 reverse transcriptase during polymerzation of HIV-1 sequences in vitro
    • Klarmann, G. J., C. A. Schauber, and B. D. Preston. Template-directed pausing of DNA synthesis by HIV-1 reverse transcriptase during polymerzation of HIV-1 sequences in vitro. J. Biol. Chem. 268:9793-9802 (1993)
    • (1993) J. Biol. Chem. , vol.268 , pp. 9793-9802
    • Klarmann, G.J.1    Schauber, C.A.2    Preston, B.D.3
  • 38
    • 0025785370 scopus 로고
    • Human immunodeficiency virus reverse transcriptase. Effect of primer length on template-primer binding
    • Reardon, J. E., E. S. Furfine, and N. Cheng. Human immunodeficiency virus reverse transcriptase. Effect of primer length on template-primer binding. J. Biol. Chem. 266:14128-14134 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 14128-14134
    • Reardon, J.E.1    Furfine, E.S.2    Cheng, N.3
  • 39
    • 0027092323 scopus 로고
    • Mechanism and fidelity of HIV reverse transcriptase
    • Kati, W. M., K. A. Johnson, L. F. Jerva, and K. S. Anderson. Mechanism and fidelity of HIV reverse transcriptase. J. Biol. Chem. 267:25988-25997 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 25988-25997
    • Kati, W.M.1    Johnson, K.A.2    Jerva, L.F.3    Anderson, K.S.4
  • 40
    • 0028304576 scopus 로고
    • Effect of template secondary structure on the inhibition of HIV-1 reverse transcriptase by a pyridinone non-nucleoside inhibitor
    • Olsen, D. B., S. S. Carroll, J. C. Culberson, J. A. Shafer, and L. C. Kuo. Effect of template secondary structure on the inhibition of HIV-1 reverse transcriptase by a pyridinone non-nucleoside inhibitor. Nucleic Acids Res. 22:1437-1443 (1994).
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1437-1443
    • Olsen, D.B.1    Carroll, S.S.2    Culberson, J.C.3    Shafer, J.A.4    Kuo, L.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.