메뉴 건너뛰기




Volumn 11, Issue 2, 2006, Pages 155-163

The K65R reverse transcriptase mutation in HIV-1 reverses the excision phenotype of zidovudine resistance mutations

Author keywords

[No Author keywords available]

Indexed keywords

RNA DIRECTED DNA POLYMERASE; TENOFOVIR; TENOFOVIR DISOPROXIL; THYMIDINE DERIVATIVE; ZIDOVUDINE;

EID: 33645500469     PISSN: 13596535     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (70)

References (52)
  • 1
    • 0024310253 scopus 로고
    • Multiple mutations in HIV-1 reverse transcriptase confer high-level resistance to zidovudine (AZT)
    • Larder BA, Kemp SD. Multiple mutations in HIV-1 reverse transcriptase confer high-level resistance to zidovudine (AZT). Science 1989; 246:1155-1158.
    • (1989) Science , vol.246 , pp. 1155-1158
    • Larder, B.A.1    Kemp, S.D.2
  • 2
    • 0027988547 scopus 로고
    • Genotypic and phenotypic analysis of human immunodeficiency virus type 1 isolates from patients on prolonged stavudine therapy
    • Lin P-F, Samanta H, Rose RE, et al. Genotypic and phenotypic analysis of human immunodeficiency virus type 1 isolates from patients on prolonged stavudine therapy. J Infect Dis 1994; 170:1157-1164.
    • (1994) J Infect Dis , vol.170 , pp. 1157-1164
    • Lin, P.-F.1    Samanta, H.2    Rose, R.E.3
  • 3
    • 0030945276 scopus 로고    scopus 로고
    • Combination of mutations in human immunodeficiency virus type 1 reverse transcriptase required for resistance to the carbocyclic nucleoside 1592U89
    • Tisdale M, Alnadaf T, Cousens D. Combination of mutations in human immunodeficiency virus type 1 reverse transcriptase required for resistance to the carbocyclic nucleoside 1592U89. Antimicrob Agents Chemother 1997; 41:1094-1098.
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 1094-1098
    • Tisdale, M.1    Alnadaf, T.2    Cousens, D.3
  • 4
    • 20644436472 scopus 로고    scopus 로고
    • In vitro selection and characterization of HIV-1 with reduced susceptibility to PMPA
    • Wainberg MA, Miller MD, Quan Y, et al. In vitro selection and characterization of HIV-1 with reduced susceptibility to PMPA. Antivir Ther 1999; 4:87-94.
    • (1999) Antivir Ther , vol.4 , pp. 87-94
    • Wainberg, M.A.1    Miller, M.D.2    Quan, Y.3
  • 5
    • 0038033098 scopus 로고    scopus 로고
    • A novel genetic pathway of human immunodeficiency virus type 1 resistance to stavudine mediated by the K65R mutation
    • Garcia-Lerma JG, MacInnes H, Bennett D, et al. A novel genetic pathway of human immunodeficiency virus type 1 resistance to stavudine mediated by the K65R mutation. J Virol 2003; 77:5685-5693.
    • (2003) J Virol , vol.77 , pp. 5685-5693
    • Garcia-Lerma, J.G.1    MacInnes, H.2    Bennett, D.3
  • 6
    • 0030892246 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 reverse transcriptase genotype and drug susceptibility changes in infected individuals receiving dideoxyinosine monotherapy for 1 to 2 years
    • Winters MA, Shafer RW, Jellinger RA, et al. Human immunodeficiency virus type 1 reverse transcriptase genotype and drug susceptibility changes in infected individuals receiving dideoxyinosine monotherapy for 1 to 2 years. Antimicrob Agents Chemother 1997; 41:757-762.
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 757-762
    • Winters, M.A.1    Shafer, R.W.2    Jellinger, R.A.3
  • 7
    • 0028057581 scopus 로고
    • Identification of a mutation of codon 65 in the IKKK motif of reverse transcriptase that encodes human immunodeficiency virus resistance to 2′,3′-dideoxycytidine and 2′,3′-dideoxy-3′- thiacytidine
    • Gu Z, Gao Q, Fang H, et al. Identification of a mutation of codon 65 in the IKKK motif of reverse transcriptase that encodes human immunodeficiency virus resistance to 2′,3′-dideoxycytidine and 2′,3′- dideoxy-3′-thiacytidine. Antimicrob Agents Chemother 1994; 38:275-281.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 275-281
    • Gu, Z.1    Gao, Q.2    Fang, H.3
  • 8
    • 0036839746 scopus 로고    scopus 로고
    • Molecular mechanisms of resistance to human immunodeficiency virus type 1 with reverse transcriptase mutations K65R and K65R+M184V and their effects on enzyme function and viral replication capacity
    • White KL, Margot NA, Wrin T, et al. Molecular mechanisms of resistance to human immunodeficiency virus type 1 with reverse transcriptase mutations K65R and K65R+M184V and their effects on enzyme function and viral replication capacity. Antimicrob Agents Chemother 2002; 46:3437-3446.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 3437-3446
    • White, K.L.1    Margot, N.A.2    Wrin, T.3
  • 9
    • 1542327561 scopus 로고    scopus 로고
    • Genotypic and phenotypic predictors of the magnitude of response to tenofovir disoproxil fumarate in antiretroviral-experienced patients
    • Miller MD, Margot N, Lu B, et al. Genotypic and phenotypic predictors of the magnitude of response to tenofovir disoproxil fumarate in antiretroviral-experienced patients. J Infect Dis 2004; 189:837-846.
    • (2004) J Infect Dis , vol.189 , pp. 837-846
    • Miller, M.D.1    Margot, N.2    Lu, B.3
  • 11
    • 11844254885 scopus 로고    scopus 로고
    • K65R: A multi-nucleoside resistance mutation of increasing prevalence exhibits bi-directional phenotypic antagonism with TAM
    • February 8-11 San Francisco, Calif, USA. Abstract 54
    • Parikh U, Koontz D, Sluis-Cremer N, et al. K65R: A multi-nucleoside resistance mutation of increasing prevalence exhibits bi-directional phenotypic antagonism with TAM. 11th Conference on Retroviruses and Opportunistic Infections. February 8-11 San Francisco, Calif, USA. Abstract 54.
    • 11th Conference on Retroviruses and Opportunistic Infections
    • Parikh, U.1    Koontz, D.2    Sluis-Cremer, N.3
  • 12
    • 0033921632 scopus 로고    scopus 로고
    • In vitro selection of mutations in the human immunodeficiency virus type 1 reverse transcriptase that decrease susceptibility to (-)-beta-D-dioxolane- guanosine and suppress resistance to 3′-azido-3′-deoxythymidine
    • Bazmi HZ, Hammond JL, Cavalcanti SCH, Chu CK, Schinazi R, Mellors JW. In vitro selection of mutations in the human immunodeficiency virus type 1 reverse transcriptase that decrease susceptibility to (-)-beta-D-dioxolane-guanosine and suppress resistance to 3′-azido-3′-deoxythymidine. Antimicrob Agents Chemother 2000; 44:1783-1788.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 1783-1788
    • Bazmi, H.Z.1    Hammond, J.L.2    Cavalcanti, S.C.H.3    Chu, C.K.4    Schinazi, R.5    Mellors, J.W.6
  • 13
    • 9244234943 scopus 로고    scopus 로고
    • Effect of concurrent zidovudine use on the resistance pathway selected by abacavir-containing regimens
    • Lanier ER, Givens N, Stone C, et al. Effect of concurrent zidovudine use on the resistance pathway selected by abacavir-containing regimens. HIV Med 2004; 5:394-399.
    • (2004) HIV Med , vol.5 , pp. 394-399
    • Lanier, E.R.1    Givens, N.2    Stone, C.3
  • 14
    • 3042588297 scopus 로고    scopus 로고
    • COL40263: Resistance and efficacy of once-daily trizivir and tenofovir DF in anti-retroviral naïve subjects
    • February 8-11 San Francisco, Calif, USA. Abstract 53
    • Elion R, Cohen C, DeJesus E, et al. COL40263: Resistance and efficacy of once-daily trizivir and tenofovir DF in anti-retroviral naïve subjects. 11th Conference on Retroviruses and Opportunistic Infections. February 8-11 San Francisco, Calif, USA. Abstract 53.
    • 11th Conference on Retroviruses and Opportunistic Infections
    • Elion, R.1    Cohen, C.2    Dejesus, E.3
  • 15
    • 0035061595 scopus 로고    scopus 로고
    • Mechanisms of HIV-1 nucleoside reverse transcriptase inhibitor resistance: Is it all figured out?
    • Naeger LK, Miller MD. Mechanisms of HIV-1 nucleoside reverse transcriptase inhibitor resistance: is it all figured out? Curr Opin Investig Drugs 2001; 2:335-339.
    • (2001) Curr Opin Investig Drugs , vol.2 , pp. 335-339
    • Naeger, L.K.1    Miller, M.D.2
  • 16
    • 2942560771 scopus 로고    scopus 로고
    • Primer unblocking by HIV-1 reverse transcriptase and resistance to nucleoside RT inhibitors (NRTIs)
    • Goldschmidt V, Marquet R. Primer unblocking by HIV-1 reverse transcriptase and resistance to nucleoside RT inhibitors (NRTIs). Int J Biochem Cell Biol 2004; 36:1687-1705.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 1687-1705
    • Goldschmidt, V.1    Marquet, R.2
  • 17
    • 27544431950 scopus 로고    scopus 로고
    • A combination of decreased NRTI incorporation and decreased excision determines the resistance profile of HIV-1 K65R RT
    • White KL, Margot NA, Ly JK, et al. A combination of decreased NRTI incorporation and decreased excision determines the resistance profile of HIV-1 K65R RT. AIDS 2005; 19:1751-1760.
    • (2005) AIDS , vol.19 , pp. 1751-1760
    • White, K.L.1    Margot, N.A.2    Ly, J.K.3
  • 18
    • 0032937011 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 expressing the lamivudine-associated M184V mutation in reverse transcriptase shows increased susceptibility to adefovir and decreased replication capability in vitro
    • Miller MD, Anton KE, Mulato AS, Lamy PD, Cherrington JM. Human immunodeficiency virus type 1 expressing the lamivudine-associated M184V mutation in reverse transcriptase shows increased susceptibility to adefovir and decreased replication capability in vitro. J Infect Dis 1999; 179:92-100.
    • (1999) J Infect Dis , vol.179 , pp. 92-100
    • Miller, M.D.1    Anton, K.E.2    Mulato, A.S.3    Lamy, P.D.4    Cherrington, J.M.5
  • 19
    • 0029816733 scopus 로고    scopus 로고
    • HIV-1 drug susceptibility determination by using recombinant viruses generated from patient sera tested in a cell-killing assay
    • Boucher CAB, Keulen W, van Bommel T, et al. HIV-1 drug susceptibility determination by using recombinant viruses generated from patient sera tested in a cell-killing assay. Antimicrob Agents Chemother 1996; 40:2404-2409.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 2404-2409
    • Boucher, C.A.B.1    Keulen, W.2    Van Bommel, T.3
  • 20
    • 15844392150 scopus 로고    scopus 로고
    • Comparative kinetic analysis of interation of inhibitors with Rauscher murine leukemia virus and human immunodeficiency virus reverse transcriptases
    • Cherrington JM, Fuller MD, Mulato AS, et al. Comparative kinetic analysis of interation of inhibitors with Rauscher murine leukemia virus and human immunodeficiency virus reverse transcriptases. Antimicrob Agents Chemother 1996; 40:1270-1273.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 1270-1273
    • Cherrington, J.M.1    Fuller, M.D.2    Mulato, A.S.3
  • 22
    • 1442349112 scopus 로고    scopus 로고
    • Molecular mechanisms of tenofovir resistance conferred by human immunodeficiency virus type 1 reverse transcriptase containing a diserine insertion after residue 69 and multiple thymidine analog-associated mutations
    • White KL, Chen JM, Margot NA, et al. Molecular mechanisms of tenofovir resistance conferred by human immunodeficiency virus type 1 reverse transcriptase containing a diserine insertion after residue 69 and multiple thymidine analog-associated mutations. Antimicrob Agents Chemother 2004; 48:992-1003.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 992-1003
    • White, K.L.1    Chen, J.M.2    Margot, N.A.3
  • 23
    • 0032506228 scopus 로고    scopus 로고
    • Unblocking of chain-terminated primer by HIV-1 reverse transcriptase through a nucleotide-dependent mechanism
    • Meyer PR, Matsuura SE, So AG, Scott WA. Unblocking of chain-terminated primer by HIV-1 reverse transcriptase through a nucleotide-dependent mechanism. Proc Natl Acad Sci U S A 1998; 95:13471-13476.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 13471-13476
    • Meyer, P.R.1    Matsuura, S.E.2    So, A.G.3    Scott, W.A.4
  • 24
    • 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 PR, Matsuura SE, Schinazi RF, So AG, Scott WA. 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 2000; 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
  • 25
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • Traut T. Physiological concentrations of purines and pyrimidines. Mol Cell Biochem 1994; 140:1-22.
    • (1994) Mol Cell Biochem , vol.140 , pp. 1-22
    • Traut, T.1
  • 26
    • 0027377963 scopus 로고
    • Low levels of deoxynucleotides in peripheral blood lymphocytes: A strategy to inhibit human immunodeficiency virus type 1 replication
    • Gao W-Y, Cara A, Gallo RC & Lori F. Low levels of deoxynucleotides in peripheral blood lymphocytes: a strategy to inhibit human immunodeficiency virus type 1 replication. Proc Natl Acad Sci U S A 1993; 90:8925-8928.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 8925-8928
    • Gao, W.-Y.1    Cara, A.2    Gallo, R.C.3    Lori, F.4
  • 27
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: Implications for drug resistance
    • Huang H, Chopra R, Verdine GL, Harrison SC. Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance. Science 1998; 282:1669-1675.
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 28
    • 2342453265 scopus 로고    scopus 로고
    • Structures of HIV-1 RT-DNA complexes before and after incorporation of the anti-AIDS drug tenofovir
    • Tuske S, Sarafianos SG, Clark AD, et al. Structures of HIV-1 RT-DNA complexes before and after incorporation of the anti-AIDS drug tenofovir. Nat Struct Mol Biol 2004; 11:469-474.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 469-474
    • Tuske, S.1    Sarafianos, S.G.2    Clark, A.D.3
  • 29
    • 0037156343 scopus 로고    scopus 로고
    • Anthranilate sulfonamide hydroxamate TACE inhibitors. Part 1: Structure-based design of novel acetylenic P1′ groups
    • Chen JM, Jin G, Sung A, Levin JI. Anthranilate sulfonamide hydroxamate TACE inhibitors. Part 1: Structure-based design of novel acetylenic P1′ groups. Bioorg Med Chem Lett 2002; 12:1195-1198.
    • (2002) Bioorg Med Chem Lett , vol.12 , pp. 1195-1198
    • Chen, J.M.1    Jin, G.2    Sung, A.3    Levin, J.I.4
  • 30
    • 0021905444 scopus 로고
    • Dynamics and conformational energetics of a peptide ormone: Vasopressin
    • Hagler AT, Osguthorpe DJ, Dauber-Osguthorpe P, Hempel JC. Dynamics and conformational energetics of a peptide ormone: vasopressin. Science 1985; 227:1309-1315.
    • (1985) Science , vol.227 , pp. 1309-1315
    • Hagler, A.T.1    Osguthorpe, D.J.2    Dauber-Osguthorpe, P.3    Hempel, J.C.4
  • 31
    • 0027716827 scopus 로고
    • Molecular dynamics of the H-ras gene-encoded p21 protein; identification of flexible regions and possible effector domains
    • Dykes DC, Friedman FK, Dykes SL, Murphy RB, Brandt-Rauf PW, Pincus MR. Molecular dynamics of the H-ras gene-encoded p21 protein; identification of flexible regions and possible effector domains. J Biomol Struct Dyn 1993; 11:443-58.
    • (1993) J Biomol Struct Dyn , vol.11 , pp. 443-458
    • Dykes, D.C.1    Friedman, F.K.2    Dykes, S.L.3    Murphy, R.B.4    Brandt-Rauf, P.W.5    Pincus, M.R.6
  • 32
    • 0029833963 scopus 로고    scopus 로고
    • Inhibition of viral polymerases by chain-terminating substrates: A kinetic analysis
    • Edited by Kuo LC, Olsen DB and Carroll SS. San Diego: Academic Press, Inc.
    • Wilson JE, Porter DJT, Reardon JE. Inhibition of viral polymerases by chain-terminating substrates: a kinetic analysis. In Methods of Enzymology, vol. 275; pp. 398-424. Edited by Kuo LC, Olsen DB and Carroll SS. San Diego: Academic Press, Inc.
    • Methods of Enzymology , vol.275 , pp. 398-424
    • Wilson, J.E.1    Porter, D.J.T.2    Reardon, J.E.3
  • 33
    • 0347052875 scopus 로고    scopus 로고
    • Mechanistic basis for reduced viral and enzymatic fitness of HIV-1 reverse transcriptase containing both K65R and M184V mutations
    • Deval J, White KL, Miller MD, et al. Mechanistic basis for reduced viral and enzymatic fitness of HIV-1 reverse transcriptase containing both K65R and M184V mutations. J Biol Chem 2004; 279:509-516.
    • (2004) J Biol Chem , vol.279 , pp. 509-516
    • Deval, J.1    White, K.L.2    Miller, M.D.3
  • 34
    • 0033165851 scopus 로고    scopus 로고
    • A mechanism of AZT resistance: An increase in nucleotide-dependent primer unblocking by mutant HIV-1 reverse transcriptase
    • Meyer PR, Matsuura SE, Mian AM, So AG, Scott WA. A mechanism of AZT resistance: an increase in nucleotide-dependent primer unblocking by mutant HIV-1 reverse transcriptase. Mol Cell 1999; 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
  • 35
    • 0030987309 scopus 로고    scopus 로고
    • Nucleotide-induced stable complex formation by HIV-1 reverse transcriptase
    • Tong W, Lu C-D, Sharma SK, Matsuura S, So AG & Scott WA. Nucleotide-induced stable complex formation by HIV-1 reverse transcriptase. Biochemistry 1997; 36:5749-5757.
    • (1997) Biochemistry , vol.36 , pp. 5749-5757
    • Tong, W.1    Lu, C.-D.2    Sharma, S.K.3    Matsuura, S.4    So, A.G.5    Scott, W.A.6
  • 36
    • 0015718863 scopus 로고
    • Analysis of nucleotide pools in animal cells
    • Hauschka PV. Analysis of nucleotide pools in animal cells. Methods Cell Biol 1973; 7:361-462.
    • (1973) Methods Cell Biol , vol.7 , pp. 361-462
    • Hauschka, P.V.1
  • 37
    • 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 AS, Murakami E, Basavapathruni A, et al. Probing the molecular mechanisms of AZT drug resistance mediated by HIV-1 reverse transcriptase using a transient kinetic analysis. Biochemistry 2003; 42:8831-8841.
    • (2003) Biochemistry , vol.42 , pp. 8831-8841
    • Ray, A.S.1    Murakami, E.2    Basavapathruni, A.3
  • 38
    • 0035031936 scopus 로고    scopus 로고
    • Selective excision of AZTMP by drug-resistant human immunodeficiency virus reverse transcriptase
    • Boyer PL, Sarafianos SG, Arnold E, Hughes SH. Selective excision of AZTMP by drug-resistant human immunodeficiency virus reverse transcriptase. J Virol 2001; 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
  • 39
    • 0031046557 scopus 로고    scopus 로고
    • Comparative enzymatic study of HIV-1 reverse transcriptase resistant to 2′,3-dideoxynucleotide analogs using the single-nucleotide incorporation assay
    • Ueno T, Mitsuya H. Comparative enzymatic study of HIV-1 reverse transcriptase resistant to 2′,3-dideoxynucleotide analogs using the single-nucleotide incorporation assay. Biochemistry 1997; 36:1092-1099.
    • (1997) Biochemistry , vol.36 , pp. 1092-1099
    • Ueno, T.1    Mitsuya, H.2
  • 40
    • 0028034266 scopus 로고
    • The K65R mutant reverse transcriptase of HTV-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, Fletcher RS, Arts EJ, Wainberg MA, Parniak MA. The K65R mutant reverse transcriptase of HTV-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 1994; 269:28118-28122.
    • (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
  • 41
    • 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, Kaushik N, McCormick S, Borkow G, Parniak MA. 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 1998; 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
  • 42
    • 0035984790 scopus 로고    scopus 로고
    • ATP-dependent removal of nucleoside reverse transcriptase inhibitors by human immunodeficiency virus type 1 reverse transcriptase
    • Naeger LK, Margot NA, Miller MD. ATP-dependent removal of nucleoside reverse transcriptase inhibitors by human immunodeficiency virus type 1 reverse transcriptase. Antimicrob Agents Chemother 2002; 46:2179-2184.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 2179-2184
    • Naeger, L.K.1    Margot, N.A.2    Miller, M.D.3
  • 43
    • 0034948070 scopus 로고    scopus 로고
    • Correlation between viral resistance to zidovudine and resistance at the reverse transcriptase level for a panel of human immunodeficiency virus type 1 mutants
    • Lennerstrand J, Hertogs K, Stammers DK, Larder BA. Correlation between viral resistance to zidovudine and resistance at the reverse transcriptase level for a panel of human immunodeficiency virus type 1 mutants. J Virol 2001; 75:7202-7205.
    • (2001) J Virol , vol.75 , pp. 7202-7205
    • Lennerstrand, J.1    Hertogs, K.2    Stammers, D.K.3    Larder, B.A.4
  • 44
    • 23844479950 scopus 로고    scopus 로고
    • The 3′-azido group is not the primary determinant of AZT responsible for the excision phenotype of AZT-resistant HIV-1
    • Sluis-Cremer N, Arion D, Parikh U, et al. The 3′-azido group is not the primary determinant of AZT responsible for the excision phenotype of AZT-resistant HIV-1. J Biol Chem 2005; 280:29047-29052
    • (2005) J Biol Chem , vol.280 , pp. 29047-29052
    • Sluis-Cremer, N.1    Arion, D.2    Parikh, U.3
  • 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 PR, Smith AJ, Matsuura SE, Scott WA. Effects of primer-template sequence on ATP-dependent removal of chain-terminating nucleotide analogues by HIV-1 reverse transcriptase. J Biol Chem 2004; 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
    • 4444355318 scopus 로고    scopus 로고
    • Effects of the Delta67 complex of mutations in human immunodeficiency virus type 1 reverse transcriptase on nucleoside analog excision
    • Boyer PL, Imamichi T, Sarafianos SG, Arnold E, Hughes SH. Effects of the Delta67 complex of mutations in human immunodeficiency virus type 1 reverse transcriptase on nucleoside analog excision. J Virol 2004; 78:9987-9997.
    • (2004) J Virol , vol.78 , pp. 9987-9997
    • Boyer, P.L.1    Imamichi, T.2    Sarafianos, S.G.3    Arnold, E.4    Hughes, S.H.5
  • 47
    • 0034947293 scopus 로고    scopus 로고
    • Increased drug susceptibility of HIV-1 reverse transcriptase mutants containing M184V and zidovudine-associated mutations: Analysis of enzyme processivity, chain-terminator removal and viral replication
    • Naeger LK, Margot NA, Miller MD. Increased drug susceptibility of HIV-1 reverse transcriptase mutants containing M184V and zidovudine-associated mutations: analysis of enzyme processivity, chain-terminator removal and viral replication. Antivir Ther 2001; 6:115-126.
    • (2001) Antivir Ther , vol.6 , pp. 115-126
    • Naeger, L.K.1    Margot, N.A.2    Miller, M.D.3
  • 48
    • 0037689445 scopus 로고    scopus 로고
    • Relationship between 3′-azido-3′-deoxythymidine resistance and primer unblocking activity in foscarnet-resistant mutants or human immunodeficiency virus type 1 reverse transcriptase
    • Meyer PR, Matsuura SE, Zonarich D, et al. Relationship between 3′-azido-3′-deoxythymidine resistance and primer unblocking activity in foscarnet-resistant mutants or human immunodeficiency virus type 1 reverse transcriptase. J Virol 2003; 77:6127-6137.
    • (2003) J Virol , vol.77 , pp. 6127-6137
    • Meyer, P.R.1    Matsuura, S.E.2    Zonarich, D.3
  • 49
    • 0027365750 scopus 로고
    • Kinetic mechanism of the DNA-dependent DNA polymerase activity of human immunodeficiency virus reverse transcriptase
    • Hsieh JC, Zinnen S, Modrich P. Kinetic mechanism of the DNA-dependent DNA polymerase activity of human immunodeficiency virus reverse transcriptase. J Biol Chem 1993; 268:24607-24613.
    • (1993) J Biol Chem , vol.268 , pp. 24607-24613
    • Hsieh, J.C.1    Zinnen, S.2    Modrich, P.3
  • 50
    • 0025799903 scopus 로고
    • Kinetic mechanism of DNA polymerase I (Klenow fragment): Identification of a second conformational change and evaluation of the internal equilibrium constant
    • Dahlberg ME, Benkovic SJ. Kinetic mechanism of DNA polymerase I (Klenow fragment): identification of a second conformational change and evaluation of the internal equilibrium constant. Biochemistry 1991; 30:4835-4843.
    • (1991) Biochemistry , vol.30 , pp. 4835-4843
    • Dahlberg, M.E.1    Benkovic, S.J.2
  • 52
    • 0034282409 scopus 로고    scopus 로고
    • Differential influence of nucleoside analog-resistance mutations K65R and L74V on the overall mutation rate and error specificity of human immunodeficiency virus type 1 reverse transcriptase
    • Shah FS, Curr KA, Hamburgh ME, et al. Differential influence of nucleoside analog-resistance mutations K65R and L74V on the overall mutation rate and error specificity of human immunodeficiency virus type 1 reverse transcriptase. J Biol Chem 2000; 275:27037-27044.
    • (2000) J Biol Chem , vol.275 , pp. 27037-27044
    • Shah, F.S.1    Curr, K.A.2    Hamburgh, M.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.