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Volumn 54, Issue 11, 2010, Pages 4799-4811

Mechanisms involved in the selection of HIV-1 reverse transcriptase thumb subdomain polymorphisms associated with nucleoside analogue therapy failure

Author keywords

[No Author keywords available]

Indexed keywords

ABACAVIR; CARBOVIR; DIDANOSINE; DNA; LAMIVUDINE; PHOSPHATE; RIBONUCLEASE H; RNA; RNA DIRECTED DNA POLYMERASE; RNA DIRECTED DNA POLYMERASE INHIBITOR; STAVUDINE; TENOFOVIR; ZIDOVUDINE;

EID: 78049269916     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00716-10     Document Type: Article
Times cited : (28)

References (75)
  • 1
    • 69749111210 scopus 로고    scopus 로고
    • Increased thermostability and fidelity of DNA synthesis of wild-type and mutant HIV-1 group O reverse transcriptases
    • Álvarez, M., T. Matamoros, and L. Menéndez-Arias. 2009. Increased thermostability and fidelity of DNA synthesis of wild-type and mutant HIV-1 group O reverse transcriptases. J. Mol. Biol. 392:872-884.
    • (2009) J. Mol. Biol. , vol.392 , pp. 872-884
    • Álvarez, M.1    Matamoros, T.2    Menéndez-Arias, L.3
  • 2
    • 0032506055 scopus 로고    scopus 로고
    • Phenotypic mechanism of HIV-1 resistance to 3′-azido-3′- deoxythymidine (AZT): Increased polymerization processivity and enhanced sensitivity to pyrophosphate of the mutant viral reverse transcriptase
    • Arion, D., N. Kaushik, S. McCormick, G. Borkow, and M. A. Parniak. 1998. Phenotypic mechanism of HIV-1 resistance to 3′-azido-3′- deoxythymidine (AZT): increased polymerization processivity and enhanced sensitivity to pyrophosphate of the mutant viral reverse transcriptase. Biochemistry 37: 15908-15917.
    • (1998) Biochemistry , vol.37 , pp. 15908-15917
    • Arion, D.1    Kaushik, N.2    McCormick, S.3    Borkow, G.4    Parniak, M.A.5
  • 3
    • 36849078038 scopus 로고    scopus 로고
    • Reverse transcription of the HIV-1 pandemic
    • Basavapathruni, A., and K. S. Anderson. 2007. Reverse transcription of the HIV-1 pandemic. FASEB J. 21:3795-3808.
    • (2007) FASEB J. , vol.21 , pp. 3795-3808
    • Basavapathruni, A.1    Anderson, K.S.2
  • 4
    • 0029144027 scopus 로고
    • Reduced frameshift fidelity and processivity of HIV-1 reverse transcriptase mutants containing alanine substitutions in helix H of the thumb subdomain
    • Bebenek, K., W. A. Beard, J. R. Casas-Finet, H.-R. Kim, T. A. Darden, S. H. Wilson, and T. A. Kunkel. 1995. Reduced frameshift fidelity and processivity of HIV-1 reverse transcriptase mutants containing alanine substitutions in helix H of the thumb subdomain. J. Biol. Chem. 270:19516-19523.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19516-19523
    • Bebenek, K.1    Beard, W.A.2    Casas-Finet, J.R.3    Kim, H.-R.4    Darden, T.A.5    Wilson, S.H.6    Kunkel, T.A.7
  • 6
    • 78049294469 scopus 로고    scopus 로고
    • Mechanisms of nucleoside analogue resistance associated with the selection of HIV-1 reverse transcriptase thumb subdomain polymorphisms
    • Betancour, G., M. C. Puertas, M. Nevot, C. Garriga, M. A. Martínez, J. Martinez-Picado, and L. Menéndez-Arias. 2010. Mechanisms of nucleoside analogue resistance associated with the selection of HIV-1 reverse transcriptase thumb subdomain polymorphisms. Antivir. Ther. 15(Suppl. 2):A80.
    • (2010) Antivir. Ther. , vol.15 , Issue.SUPPL. 2
    • Betancour, G.1    Puertas, M.C.2    Nevot, M.3    Garriga, C.4    Martínez, M.A.5    Martinez-Picado, J.6    Menéndez-Arias, L.7
  • 7
    • 0035337271 scopus 로고    scopus 로고
    • An integrated system to study multiply substituted human immunodeficiency virus type 1 reverse transcriptase
    • Boretto, J., S. Longhi, J.-M. Navarro, B. Selmi, J. Sire, and B. Canard. 2001. An integrated system to study multiply substituted human immunodeficiency virus type 1 reverse transcriptase. Anal. Biochem. 292:139-147.
    • (2001) Anal. Biochem. , vol.292 , pp. 139-147
    • Boretto, J.1    Longhi, S.2    Navarro, J.-M.3    Selmi, B.4    Sire, J.5    Canard, B.6
  • 8
    • 0035031936 scopus 로고    scopus 로고
    • Selective excision of AZTMP by drug-resistant human immunodeficiency virus reverse transcriptase
    • Boyer, P. L., S. G. Sarafianos, E. Arnold, and S. H. Hughes. 2001. Selective excision of AZTMP by drug-resistant human immunodeficiency virus reverse transcriptase. J. Virol. 75:4832-4842.
    • (2001) J. Virol. , vol.75 , pp. 4832-4842
    • Boyer, P.L.1    Sarafianos, S.G.2    Arnold, E.3    Hughes, S.H.4
  • 9
    • 58849109055 scopus 로고    scopus 로고
    • Mechanism by which a glutamine to leucine substitution at residue 509 in the ribonuclease H domain of HIV-1 reverse transcriptase confers zidovudine resistance
    • Brehm, J. H., J. W. Mellors, and N. Sluis-Cremer. 2008. Mechanism by which a glutamine to leucine substitution at residue 509 in the ribonuclease H domain of HIV-1 reverse transcriptase confers zidovudine resistance. Biochemistry 47:14020-14027.
    • (2008) Biochemistry , vol.47 , pp. 14020-14027
    • Brehm, J.H.1    Mellors, J.W.2    Sluis-Cremer, N.3
  • 10
    • 33847018853 scopus 로고    scopus 로고
    • Identification of accessory mutations associated with high-level resistance in HIV-1 reverse transcriptase
    • on behalf of the UK Collaborative Group on HIV Drug Resistance
    • Cane, P. A., H. Green, E. Fearnhill, and D. Dunn, on behalf of the UK Collaborative Group on HIV Drug Resistance. 2007. Identification of accessory mutations associated with high-level resistance in HIV-1 reverse transcriptase. AIDS 21:447-455.
    • (2007) AIDS , vol.21 , pp. 447-455
    • Cane, P.A.1    Green, H.2    Fearnhill, E.3    Dunn, D.4
  • 11
    • 33751552155 scopus 로고    scopus 로고
    • Mutational patterns associated with the 69 insertion complex in multidrug-resistant HIV-1 reverse transcriptase that confer increased excision activity and high-level resistance to zidovudine
    • Cases-González, C. E., S. Franco, M. A. Martínez, and L. Menéndez-Arias. 2007. Mutational patterns associated with the 69 insertion complex in multidrug-resistant HIV-1 reverse transcriptase that confer increased excision activity and high-level resistance to zidovudine. J. Mol. Biol. 365:298-309.
    • (2007) J. Mol. Biol. , vol.365 , pp. 298-309
    • Cases-González, C.E.1    Franco, S.2    Martínez, M.A.3    Menéndez-Arias, L.4
  • 13
    • 61549128714 scopus 로고    scopus 로고
    • Antiviral agents acting as DNA or RNA chain terminators
    • De Clercq, E., and J. Neyts. 2009. Antiviral agents acting as DNA or RNA chain terminators. Handb. Exp. Pharmacol. 189:53-84.
    • (2009) Handb. Exp. Pharmacol. , vol.189 , pp. 53-84
    • De Clercq, E.1    Neyts, J.2
  • 14
    • 34250811908 scopus 로고    scopus 로고
    • Mutations in human immunodeficiency virus type 1 RNase H primer grip enhance 3′-azido-3′-deoxythymidine resistance
    • Delviks-Frankenberry, K. A., G. N. Nikolenko, R. Barr, and V. K. Pathak. 2007. Mutations in human immunodeficiency virus type 1 RNase H primer grip enhance 3′-azido-3′-deoxythymidine resistance. J. Virol. 81:6837-6845.
    • (2007) J. Virol. , vol.81 , pp. 6837-6845
    • Delviks-Frankenberry, K.A.1    Nikolenko, G.N.2    Barr, R.3    Pathak, V.K.4
  • 16
    • 2942616457 scopus 로고    scopus 로고
    • A loss of viral replicative capacity correlates with altered DNA polymerization kinetics by the human immunodeficiency virus reverse transcriptase bearing the K65R and L74V dideoxynucleoside resistance substitutions
    • Deval, J., J.-M. Navarro, B. Selmi, J. Courcambeck, J. Boretto, P. Halfon, S. Garrido-Urbani, J. Sire, and B. Canard. 2004. A loss of viral replicative capacity correlates with altered DNA polymerization kinetics by the human immunodeficiency virus reverse transcriptase bearing the K65R and L74V dideoxynucleoside resistance substitutions. J. Biol. Chem. 279:25489-25496.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25489-25496
    • Deval, J.1    Navarro, J.-M.2    Selmi, B.3    Courcambeck, J.4    Boretto, J.5    Halfon, P.6    Garrido-Urbani, S.7    Sire, J.8    Canard, B.9
  • 17
    • 0032509101 scopus 로고    scopus 로고
    • Structural and functional implications of the polymerase active site region in a complex of HIV-1 RT with a double-stranded DNA template-primer and an antibody Fab fragment at 2.8 å resolution
    • Ding, J., K. Das, Y. Hsiou, S. G. Sarafianos, A. D. Clark, Jr., A. Jacobo-Molina, C. Tantillo, S. H. Hughes, and E. Arnold. 1998. Structural and functional implications of the polymerase active site region in a complex of HIV-1 RT with a double-stranded DNA template-primer and an antibody Fab fragment at 2.8 Å resolution. J. Mol. Biol. 284:1095-1111.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1095-1111
    • Ding, J.1    Das, K.2    Hsiou, Y.3    Sarafianos, S.G.4    Clark Jr., A.D.5    Jacobo-Molina, A.6    Tantillo, C.7    Hughes, S.H.8    Arnold, E.9
  • 18
    • 70450193040 scopus 로고    scopus 로고
    • Mutations in the thumb allow human immunodeficiency virus type 1 reverse transcriptase to be cleaved by protease in virions
    • Dunn, L. L., M. J. McWilliams, K. Das, E. Arnold, and S. H. Hughes. 2009. Mutations in the thumb allow human immunodeficiency virus type 1 reverse transcriptase to be cleaved by protease in virions. J. Virol. 83:12336-12344.
    • (2009) J. Virol. , vol.83 , pp. 12336-12344
    • Dunn, L.L.1    McWilliams, M.J.2    Das, K.3    Arnold, E.4    Hughes, S.H.5
  • 19
    • 52049107430 scopus 로고    scopus 로고
    • Connection domain mutations N348I and A360V in HIV-1 reverse transcriptase enhance resistance to 3′-azido-3′-deoxythymidine through both RNase H-dependent and -independent mechanisms
    • Ehteshami, M., G. L. Beilhartz, B. J. Scarth, E. P. Tchesnokov, S. McCormick, B. Wynhoven, P. R. Harrigan, and M. Götte. 2008. Connection domain mutations N348I and A360V in HIV-1 reverse transcriptase enhance resistance to 3′-azido-3′-deoxythymidine through both RNase H-dependent and -independent mechanisms. J. Biol. Chem. 283:22222-22232.
    • (2008) J. Biol. Chem. , vol.283 , pp. 22222-22232
    • Ehteshami, M.1    Beilhartz, G.L.2    Scarth, B.J.3    Tchesnokov, E.P.4    McCormick, S.5    Wynhoven, B.6    Harrigan, P.R.7    Götte, M.8
  • 20
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • Felsenstein, J. 1985. Confidence limits on phylogenies: an approach using the bootstrap. Evolution 39:783-791.
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 21
    • 67650979706 scopus 로고    scopus 로고
    • HIV-1 reverse transcriptase thumb subdomain polymorphisms associated with virological failure to nucleoside drug combinations
    • on behalf of the Spanish Group for the Study of Antiretroviral Drug Resistance
    • Garriga, C., M. J. Pérez-Elías, R. Delgado, L. Ruiz, L. Pérez-Álvarez, T. Pumarola, A. López-Lirola, J. González-García, and L. Menéndez-Arias, on behalf of the Spanish Group for the Study of Antiretroviral Drug Resistance. 2009. HIV-1 reverse transcriptase thumb subdomain polymorphisms associated with virological failure to nucleoside drug combinations. J. Antimicrob. Chemother. 64:251-258.
    • (2009) J. Antimicrob. Chemother. , vol.64 , pp. 251-258
    • Garriga, C.1    Pérez-Elías, M.J.2    Delgado, R.3    Ruiz, L.4    Pérez-Álvarez, L.5    Pumarola, T.6    López-Lirola, A.7    González-García, J.8    Menéndez-Arias, L.9
  • 22
    • 41149145592 scopus 로고    scopus 로고
    • Amino acid mutation N348I in the connection subdomain of human immunodeficiency virus type 1 reverse transcriptase confers multiclass resistance to nucleoside and nonnucleoside reverse transcriptase inhibitors
    • Hachiya, A., E. N. Kodama, S. G. Sarafianos, M. M. Schuckmann, Y. Sakagami, M. Matsuoka, M. Takiguchi, H. Gatanaga, and S. Oka. 2008. Amino acid mutation N348I in the connection subdomain of human immunodeficiency virus type 1 reverse transcriptase confers multiclass resistance to nucleoside and nonnucleoside reverse transcriptase inhibitors. J. Virol. 82:3261-3270.
    • (2008) J. Virol. , vol.82 , pp. 3261-3270
    • Hachiya, A.1    Kodama, E.N.2    Sarafianos, S.G.3    Schuckmann, M.M.4    Sakagami, Y.5    Matsuoka, M.6    Takiguchi, M.7    Gatanaga, H.8    Oka, S.9
  • 23
    • 0028090098 scopus 로고
    • The 'helix clamp' in HIV-1 reverse transcriptase: A new nucleic acid binding motif common in nucleic acid polymerases
    • Hermann, T., T. Meier, M. Götte, and H. Heumann. 1994. The 'helix clamp' in HIV-1 reverse transcriptase: a new nucleic acid binding motif common in nucleic acid polymerases. Nucleic Acids Res. 22:4625-4633.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4625-4633
    • Hermann, T.1    Meier, T.2    Götte, M.3    Heumann, H.4
  • 24
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: Implications for drug resistance
    • Huang, H., R. Chopra, G. L. Verdine, and S. C. Harrison. 1998. Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance. Science 282:1669-1675.
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 25
    • 41549097303 scopus 로고    scopus 로고
    • Identification of a novel resistance (E40F) and compensatory (K43E) substitution in HIV-1 reverse transcriptase
    • Huigen, M. C., P. M. van Ham, L. de Graaf, R. M. Kagan, C. A. Boucher, and M. Nijhuis. 2008. Identification of a novel resistance (E40F) and compensatory (K43E) substitution in HIV-1 reverse transcriptase. Retrovirology 5:20.
    • (2008) Retrovirology , vol.5 , pp. 20
    • Huigen, M.C.1    Van Ham, P.M.2    De Graaf, L.3    Kagan, R.M.4    Boucher, C.A.5    Nijhuis, M.6
  • 26
    • 0035966048 scopus 로고    scopus 로고
    • The emergence of different resistance mechanisms toward nucleoside inhibitors is explained by the properties of the wild type HIV-1 reverse transcriptase
    • Isel, C., C. Ehresmann, P. Walter, B. Ehresmann, and R. Marquet. 2001. The emergence of different resistance mechanisms toward nucleoside inhibitors is explained by the properties of the wild type HIV-1 reverse transcriptase. J. Biol. Chem. 276:48725-48732.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48725-48732
    • Isel, C.1    Ehresmann, C.2    Walter, P.3    Ehresmann, B.4    Marquet, R.5
  • 28
    • 0027092323 scopus 로고
    • Mechanism and fidelity of HIV reverse transcriptase
    • Kati, W. M., K. A. Johnson, L. F. Jerva, and K. S. Anderson. 1992. Mechanism and fidelity of HIV reverse transcriptase. J. Biol. Chem. 267:25988-25997.
    • (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
  • 29
    • 0028085161 scopus 로고
    • Recombinant virus assay: A rapid, phenotypic assay for assessment of drug susceptibility of human immunodeficiency virus type 1 isolates
    • Kellam, P., and B. A. Larder. 1994. Recombinant virus assay: a rapid, phenotypic assay for assessment of drug susceptibility of human immunodeficiency virus type 1 isolates. Antimicrob. Agents Chemother. 38:23-30.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 23-30
    • Kellam, P.1    Larder, B.A.2
  • 30
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 Å 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. 1992. Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science 256:1783-1790.
    • (1992) Science , vol.256 , pp. 1783-1790
    • Kohlstaedt, L.A.1    Wang, J.2    Friedman, J.M.3    Rice, P.A.4    Steitz, T.A.5
  • 31
    • 24144463796 scopus 로고    scopus 로고
    • Effect of the Q207D mutation in HIV type 1 reverse transcriptase on zidovudine susceptibility and replicative fitness
    • Lu, L., J. Whitcomb, and D. R. Kuritzkes. 2005. Effect of the Q207D mutation in HIV type 1 reverse transcriptase on zidovudine susceptibility and replicative fitness. J. Acquir. Immune Defic. Syndr. 40:20-23.
    • (2005) J. Acquir. Immune Defic. Syndr. , vol.40 , pp. 20-23
    • Lu, L.1    Whitcomb, J.2    Kuritzkes, D.R.3
  • 32
    • 34547641773 scopus 로고    scopus 로고
    • Effects of the translocation status of human immunodeficiency virus type 1 reverse transcriptase on the efficiency of excision of tenofovir
    • Marchand, B., K. L. White, J. K. Ly, N. A. Margot, R. Wang, M. McDermott, M. D. Miller, and M. Götte. 2007. Effects of the translocation status of human immunodeficiency virus type 1 reverse transcriptase on the efficiency of excision of tenofovir. Antimicrob. Agents Chemother. 51:2911-2919.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 2911-2919
    • Marchand, B.1    White, K.L.2    Ly, J.K.3    Margot, N.A.4    Wang, R.5    McDermott, M.6    Miller, M.D.7    Götte, M.8
  • 33
    • 0034329473 scopus 로고    scopus 로고
    • Role of a dipeptide insertion between codons 69 and 70 of HIV-1 reverse transcriptase in the mechanism of AZT resistance
    • Mas, A., M. Parera, C. Briones, V. Soriano, M. A. Martínez, E. Domingo, and L. Menéndez-Arias. 2000. Role of a dipeptide insertion between codons 69 and 70 of HIV-1 reverse transcriptase in the mechanism of AZT resistance. EMBO J. 19:5752-5761.
    • (2000) EMBO J. , vol.19 , pp. 5752-5761
    • Mas, A.1    Parera, M.2    Briones, C.3    Soriano, V.4    Martínez, M.A.5    Domingo, E.6    Menéndez-Arias, L.7
  • 34
    • 0036406111 scopus 로고    scopus 로고
    • Multidrug-resistant HIV-1 reverse transcriptase: Involvement of ribonucleotide-dependent phosphorolysis in cross-resistance to nucleoside analogue inhibitors
    • Mas, A., B. M. Vázquez-Álvarez, E. Domingo, and L. Menéndez-Arias. 2002. Multidrug-resistant HIV-1 reverse transcriptase: involvement of ribonucleotide-dependent phosphorolysis in cross-resistance to nucleoside analogue inhibitors. J. Mol. Biol. 323:181-197.
    • (2002) J. Mol. Biol. , vol.323 , pp. 181-197
    • Mas, A.1    Vázquez-Álvarez, B.M.2    Domingo, E.3    Menéndez- Arias, L.4
  • 35
    • 19444382473 scopus 로고    scopus 로고
    • Suppression of multidrug-resistant HIV-1 reverse transcriptase primer unblocking activity by α-phosphate-modified thymidine analogues
    • Matamoros, T., J. Deval, C. Guerreiro, L. Mulard, B. Canard, and L. Menéndez-Arias. 2005. Suppression of multidrug-resistant HIV-1 reverse transcriptase primer unblocking activity by α-phosphate-modified thymidine analogues. J. Mol. Biol. 349:451-463.
    • (2005) J. Mol. Biol. , vol.349 , pp. 451-463
    • Matamoros, T.1    Deval, J.2    Guerreiro, C.3    Mulard, L.4    Canard, B.5    Menéndez-Arias, L.6
  • 36
    • 2642518791 scopus 로고    scopus 로고
    • Molecular determinants of multi-nucleoside analogue resistance in HIV-1 reverse transcriptases containing a dipeptide insertion in the fingers subdomain: Effect of mutations D67N and T215Y on removal of thymidine nucleotide analogues from blocked DNA primers
    • Matamoros, T., S. Franco, B. M. Vázquez-Álvarez, A. Mas, M. A. Martínez, and L. Menéndez-Arias. 2004. Molecular determinants of multi-nucleoside analogue resistance in HIV-1 reverse transcriptases containing a dipeptide insertion in the fingers subdomain: effect of mutations D67N and T215Y on removal of thymidine nucleotide analogues from blocked DNA primers. J. Biol. Chem. 279:24569-24577.
    • (2004) J. Biol. Chem. , vol.279 , pp. 24569-24577
    • Matamoros, T.1    Franco, S.2    Vázquez-Álvarez, B.M.3    Mas, A.4    Martínez, M.A.5    Menéndez-Arias, L.6
  • 37
    • 70450228474 scopus 로고    scopus 로고
    • Thymidine analogue resistance suppression by V75I of HIV-1 reverse transcriptase. Effects of substituting valine 75 on stavudine excision and discrimination
    • Matamoros, T., M. Nevot, M. A. Martínez, and L. Menéndez-Arias. 2009. Thymidine analogue resistance suppression by V75I of HIV-1 reverse transcriptase. Effects of substituting valine 75 on stavudine excision and discrimination. J. Biol. Chem. 284:32792-32802.
    • (2009) J. Biol. Chem. , vol.284 , pp. 32792-32802
    • Matamoros, T.1    Nevot, M.2    Martínez, M.A.3    Menéndez-Arias, L.4
  • 38
    • 0039393614 scopus 로고    scopus 로고
    • Studies on the effects of truncating α-helix E′ of p66 human immunodeficiency virus type 1 reverse transcriptase on templateprimer binding and fidelity of DNA synthesis
    • Menéndez-Arias, L. 1998. Studies on the effects of truncating α-helix E′ of p66 human immunodeficiency virus type 1 reverse transcriptase on templateprimer binding and fidelity of DNA synthesis. Biochemistry 37:16636-16644.
    • (1998) Biochemistry , vol.37 , pp. 16636-16644
    • Menéndez-Arias, L.1
  • 39
    • 43049105858 scopus 로고    scopus 로고
    • Mechanisms of resistance to nucleoside analogue inhibitors of HIV-1 reverse transcriptase
    • Menéndez-Arias, L. 2008. Mechanisms of resistance to nucleoside analogue inhibitors of HIV-1 reverse transcriptase. Virus Res. 134:124-146.
    • (2008) Virus Res. , vol.134 , pp. 124-146
    • Menéndez-Arias, L.1
  • 40
    • 73549088708 scopus 로고    scopus 로고
    • Molecular basis of human immunodeficiency drug resistance: An update
    • Menéndez-Arias, L. 2010. Molecular basis of human immunodeficiency drug resistance: an update. Antiviral Res. 85:210-231.
    • (2010) Antiviral Res. , vol.85 , pp. 210-231
    • Menéndez-Arias, L.1
  • 41
    • 0035920168 scopus 로고    scopus 로고
    • Functional characterization of chimeric reverse transcriptases with polypeptide subunits of highly divergent HIV-1 group M and O strains
    • Menéndez-Arias, L., A. Abraha, M. E. Quiñones-Mateu, A. Mas, M.-J. Camarasa, and E. J. Arts. 2001. Functional characterization of chimeric reverse transcriptases with polypeptide subunits of highly divergent HIV-1 group M and O strains. J. Biol. Chem. 276:27470-27479.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27470-27479
    • Menéndez-Arias, L.1    Abraha, A.2    Quiñones-Mateu, M.E.3    Mas, A.4    Camarasa, M.-J.5    Arts, E.J.6
  • 42
    • 0033165851 scopus 로고    scopus 로고
    • A mechanism of AZT resistance: An increase in nucleotide-dependent primer unblocking by mutant HIV-1 reverse transcriptase
    • Meyer, P. R., S. E. Matsuura, A. M. Mian, A. G. So, and W. A. Scott. 1999. A mechanism of AZT resistance: an increase in nucleotide-dependent primer unblocking by mutant HIV-1 reverse transcriptase. Mol. Cell 4:35-43.
    • (1999) Mol. Cell , vol.4 , pp. 35-43
    • Meyer, P.R.1    Matsuura, S.E.2    Mian, A.M.3    So, A.G.4    Scott, W.A.5
  • 43
    • 0034425841 scopus 로고    scopus 로고
    • Differential removal of thymidine nucleotide analogues from blocked DNA chains by human immunodeficiency virus reverse transcriptase in the presence of physiological concentrations of 2′-deoxynucleoside triphosphates
    • Meyer, P. R., S. E. Matsuura, R. F. Schinazi, A. G. So, and W. A. Scott. 2000. Differential removal of thymidine nucleotide analogues from blocked DNA chains by human immunodeficiency virus reverse transcriptase in the presence of physiological concentrations of 2′-deoxynucleoside triphosphates. Antimicrob. Agents Chemother. 44:3465-3472.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 3465-3472
    • Meyer, P.R.1    Matsuura, S.E.2    Schinazi, R.F.3    So, A.G.4    Scott, W.A.5
  • 44
    • 0036233261 scopus 로고    scopus 로고
    • Effects of specific zidovudine resistance mutations and substrate structure on nucleotide-dependent primer unblocking by human immunodeficiency virus type 1 reverse transcriptase
    • Meyer, P. R., S. E. Matsuura, A. A. Tolun, I. Pfeifer, A. G. So, J. W. Mellors, and W. A. Scott. 2002. Effects of specific zidovudine resistance mutations and substrate structure on nucleotide-dependent primer unblocking by human immunodeficiency virus type 1 reverse transcriptase. Antimicrob. Agents Chemother. 46:1540-1545.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 1540-1545
    • Meyer, P.R.1    Matsuura, S.E.2    Tolun, A.A.3    Pfeifer, I.4    So, A.G.5    Mellors, J.W.6    Scott, W.A.7
  • 45
    • 8544267978 scopus 로고    scopus 로고
    • Effects of primer-template sequence on ATP-dependent removal of chain-terminating nucleotide analogues by HIV-1 reverse transcriptase
    • Meyer, P. R., A. J. Smith, S. E. Matsuura, and W. A. Scott. 2004. Effects of primer-template sequence on ATP-dependent removal of chain-terminating nucleotide analogues by HIV-1 reverse transcriptase. J. Biol. Chem. 279: 45389-45398.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45389-45398
    • Meyer, P.R.1    Smith, A.J.2    Matsuura, S.E.3    Scott, W.A.4
  • 46
    • 0033576276 scopus 로고    scopus 로고
    • The thumb domain of the p51-subunit is essential for activation of HIV reverse transcriptase
    • Morris, M. C., C. Berducou, J. Mery, F. Heitz, and G. Divita. 1999. The thumb domain of the p51-subunit is essential for activation of HIV reverse transcriptase. Biochemistry 38:15097-15103.
    • (1999) Biochemistry , vol.38 , pp. 15097-15103
    • Morris, M.C.1    Berducou, C.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 47
    • 0035984790 scopus 로고    scopus 로고
    • ATP-dependent removal of nucleoside reverse transcriptase inhibitors by human immunodeficiency virus type 1 reverse transcriptase
    • Naeger, L. K., N. A. Margot, and M. D. Miller. 2002. ATP-dependent removal of nucleoside reverse transcriptase inhibitors by human immunodeficiency virus type 1 reverse transcriptase. Antimicrob. Agents Chemother. 46:2179-2184.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 2179-2184
    • Naeger, L.K.1    Margot, N.A.2    Miller, M.D.3
  • 49
    • 13844312476 scopus 로고    scopus 로고
    • Mechanism for nucleoside analog-mediated abrogation of HIV-1 replication: Balance between RNase H activity and nucleotide excision
    • Nikolenko, G. N., S. Palmer, F. Maldarelli, J. W. Mellors, J. M. Coffin, and V. K. Pathak. 2005. Mechanism for nucleoside analog-mediated abrogation of HIV-1 replication: balance between RNase H activity and nucleotide excision. Proc. Natl. Acad. Sci. U. S. A. 102:2093-2098.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 2093-2098
    • Nikolenko, G.N.1    Palmer, S.2    Maldarelli, F.3    Mellors, J.W.4    Coffin, J.M.5    Pathak, V.K.6
  • 50
    • 34547954123 scopus 로고    scopus 로고
    • HIV-1 protease dimer interface mutations that compensate for viral reverse transcriptase instability in infectious virions
    • Olivares, I., A. Mulky, P. I. Boross, J. Tözsér, J. C. Kappes, C. López-Galíndez, and L. Menéndez-Arias. 2007. HIV-1 protease dimer interface mutations that compensate for viral reverse transcriptase instability in infectious virions. J. Mol. Biol. 372:369-381.
    • (2007) J. Mol. Biol. , vol.372 , pp. 369-381
    • Olivares, I.1    Mulky, A.2    Boross, P.I.3    Tözsér, J.4    Kappes, J.C.5    López-Galíndez, C.6    Menéndez-Arias, L.7
  • 52
    • 0033538339 scopus 로고    scopus 로고
    • Residues in the αH and αI helices of the HIV-1 reverse transcriptase thumb subdomain required for the specificity of RNase H-catalyzed removal of the polypurine tract primer
    • Powell, M. D., W. A. Beard, K. Bebenek, K. J. Howard, S. F. J. Le Grice, T. A. Darden, T. A. Kunkel, S. H. Wilson, and J. G. Levin. 1999. Residues in the αH and αI helices of the HIV-1 reverse transcriptase thumb subdomain required for the specificity of RNase H-catalyzed removal of the polypurine tract primer. J. Biol. Chem. 274:19885-19893.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19885-19893
    • Powell, M.D.1    Beard, W.A.2    Bebenek, K.3    Howard, K.J.4    Le Grice, S.F.J.5    Darden, T.A.6    Kunkel, T.A.7    Wilson, S.H.8    Levin, J.G.9
  • 54
    • 77949362812 scopus 로고    scopus 로고
    • N348I in reverse transcriptase provides a genetic pathway for HIV-1 to select thymidine analogue mutations and mutations antagonistic to thymidine analogue mutations
    • Radzio, J., S.-H. Yap, G. Tachedjian, and N. Sluis-Cremer. 2010. N348I in reverse transcriptase provides a genetic pathway for HIV-1 to select thymidine analogue mutations and mutations antagonistic to thymidine analogue mutations. AIDS 24:659-667.
    • (2010) AIDS , vol.24 , pp. 659-667
    • Radzio, J.1    Yap, S.-H.2    Tachedjian, G.3    Sluis-Cremer, N.4
  • 55
    • 0037175023 scopus 로고    scopus 로고
    • Mechanistic studies to understand the progressive development of resistance in human immunodeficiency virus type 1 reverse transcriptase to abacavir
    • Ray, A. S., A. Basavapathruni, and K. S. Anderson. 2002. Mechanistic studies to understand the progressive development of resistance in human immunodeficiency virus type 1 reverse transcriptase to abacavir. J. Biol. Chem. 277:40479-40490.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40479-40490
    • Ray, A.S.1    Basavapathruni, A.2    Anderson, K.S.3
  • 56
    • 0042347690 scopus 로고    scopus 로고
    • Probing the molecular mechanisms of AZT drug resistance mediated by HIV-1 reverse transcriptase using a transient kinetic analysis
    • Ray, A. S., E. Murakami, A. Basavapathruni, J. A. Vaccaro, D. Ulrich, C. K. Chu, R. F. Schinazi, and K. S. Anderson. 2003. Probing the molecular mechanisms of AZT drug resistance mediated by HIV-1 reverse transcriptase using a transient kinetic analysis. Biochemistry 42:8831-8841.
    • (2003) Biochemistry , vol.42 , pp. 8831-8841
    • Ray, A.S.1    Murakami, E.2    Basavapathruni, A.3    Vaccaro, J.A.4    Ulrich, D.5    Chu, C.K.6    Schinazi, R.F.7    Anderson, K.S.8
  • 57
    • 0036888501 scopus 로고    scopus 로고
    • Interactions of enantiomers of 2′,3′-didehydro-2′, 3′-dideoxy-fluorocytidine with wild type and M184V mutant HIV-1 reverse transcriptase
    • Ray, A. S., E. Murakami, C. N. Peterson, J. Shi, R. F. Schinazi, and K. S. Anderson. 2002. Interactions of enantiomers of 2′,3′-didehydro- 2′,3′-dideoxy-fluorocytidine with wild type and M184V mutant HIV-1 reverse transcriptase. Antiviral Res. 56:189-205.
    • (2002) Antiviral Res. , vol.56 , pp. 189-205
    • Ray, A.S.1    Murakami, E.2    Peterson, C.N.3    Shi, J.4    Schinazi, R.F.5    Anderson, K.S.6
  • 58
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N., and M. Nei. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 62
    • 58149133507 scopus 로고    scopus 로고
    • Structure and function of HIV-1 reverse transcriptase: Molecular mechanisms of polymerization and inhibition
    • Sarafianos, S. G., B. Marchand, K. Das, D. M. Himmel, M. A. Parniak, S. H. Hughes, and E. Arnold. 2009. Structure and function of HIV-1 reverse transcriptase: molecular mechanisms of polymerization and inhibition. J. Mol. Biol. 385:693-713.
    • (2009) J. Mol. Biol. , vol.385 , pp. 693-713
    • Sarafianos, S.G.1    Marchand, B.2    Das, K.3    Himmel, D.M.4    Parniak, M.A.5    Hughes, S.H.6    Arnold, E.7
  • 63
    • 33747100570 scopus 로고    scopus 로고
    • Pharmacology of current and promising nucleosides for the treatment of human immunodeficiency viruses
    • Schinazi, R. F., B. Hernandez-Santiago, and S. J. Hurwitz. 2006. Pharmacology of current and promising nucleosides for the treatment of human immunodeficiency viruses. Antiviral Res. 71:322-334.
    • (2006) Antiviral Res. , vol.71 , pp. 322-334
    • Schinazi, R.F.1    Hernandez-Santiago, B.2    Hurwitz, S.J.3
  • 64
    • 33845997466 scopus 로고    scopus 로고
    • Molecular mechanism by which the K70E mutation in human immunodeficiency virus type 1 reverse transcriptase confers resistance to nucleoside reverse transcriptase inhibitors
    • Sluis-Cremer, N., C.-W. Sheen, S. Zelina, P. S. A. Torres, U. M. Parikh, and J. W. Mellors. 2007. Molecular mechanism by which the K70E mutation in human immunodeficiency virus type 1 reverse transcriptase confers resistance to nucleoside reverse transcriptase inhibitors. Antimicrob. Agents Chemother. 51:48-53.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 48-53
    • Sluis-Cremer, N.1    Sheen, C.-W.2    Zelina, S.3    Torres, P.S.A.4    Parikh, U.M.5    Mellors, J.W.6
  • 65
    • 33646519924 scopus 로고    scopus 로고
    • The influence of natural substrates and inhibitors on the nucleotide-dependent excision activity of HIV-1 reverse transcriptase in the infected cell
    • Smith, A. J., and W. A. Scott. 2006. The influence of natural substrates and inhibitors on the nucleotide-dependent excision activity of HIV-1 reverse transcriptase in the infected cell. Curr. Pharm. Des. 12:1827-1841.
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 1827-1841
    • Smith, A.J.1    Scott, W.A.2
  • 67
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetic Analysis (MEGA) software
    • version 4.0
    • Tamura, K., J. Dudley, M. Nei, and S. Kumar. 2007. MEGA4: Molecular Evolutionary Genetic Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24:1596-1599.
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 68
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • Traut, T. W. 1994. Physiological concentrations of purines and pyrimidines. Mol. Cell. Biochem. 140:1-22.
    • (1994) Mol. Cell. Biochem. , vol.140 , pp. 1-22
    • Traut, T.W.1
  • 71
    • 56049097627 scopus 로고    scopus 로고
    • Mutational analysis of the "turn" of helix clamp motif of HIV-1 reverse transcriptase
    • Wang, Y.-X., H.-J. Zhang, J. Xu, B.-J. Zheng, and Y.-M. Wen. 2008. Mutational analysis of the "turn" of helix clamp motif of HIV-1 reverse transcriptase. Biochem. Biophys. Res. Commun. 377:915-920.
    • (2008) Biochem. Biophys. Res. Commun. , vol.377 , pp. 915-920
    • Wang, Y.-X.1    Zhang, H.-J.2    Xu, J.3    Zheng, B.-J.4    Wen, Y.-M.5
  • 75
    • 37849050932 scopus 로고    scopus 로고
    • Mechanisms by which the G333D mutation in human immunodeficiency virus type 1 reverse transcriptase facilitates dual resistance to zidovudine and lamivudine
    • Zelina, S., C.-W. Sheen, J. Radzio, J. W. Mellors, and N. Sluis-Cremer. 2008. Mechanisms by which the G333D mutation in human immunodeficiency virus type 1 reverse transcriptase facilitates dual resistance to zidovudine and lamivudine. Antimicrob. Agents Chemother. 52:157-163.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 157-163
    • Zelina, S.1    Sheen, C.-W.2    Radzio, J.3    Mellors, J.W.4    Sluis-Cremer, N.5


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