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Volumn 13, Issue 2, 2002, Pages 115-128

Molecular mechanism of DAPD/DXG against zidovudine- and lamivudine- drug resistant mutants: A molecular modelling approach

Author keywords

3TC; AZT; DAPD; Drug resistance; DXG; HIV 1 RT; Molecular modelling

Indexed keywords

1,3 DIOXOLANE DERIVATIVE; 2,6 DIAMINOPURINE DIOXOLANE; ARGININE; BETA DEXTRO DIOXOLANE GUANINE; LAMIVUDINE; LYSINE; RNA DIRECTED DNA POLYMERASE INHIBITOR; TYROSINE; UNCLASSIFIED DRUG; ZIDOVUDINE;

EID: 0038240528     PISSN: 09563202     EISSN: None     Source Type: Journal    
DOI: 10.1177/095632020201300205     Document Type: Article
Times cited : (28)

References (71)
  • 1
    • 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 (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
  • 2
    • 0033014502 scopus 로고    scopus 로고
    • HIV resistance to zidovudine: The role of pyrophosphorolysis
    • Arion D & Parniak MA (1999) HIV resistance to zidovudine: the role of pyrophosphorolysis. Drug Resisitance Updates 2:91-95.
    • (1999) Drug Resisitance Updates , vol.2 , pp. 91-95
    • Arion, D.1    Parniak, M.A.2
  • 3
    • 0029912274 scopus 로고    scopus 로고
    • Mechanisms of nucleoside analog antiviral activity and resistance during human immunodeficiency virus reverse transcription
    • Arts EJ & Wainberg MA (1996) Mechanisms of nucleoside analog antiviral activity and resistance during human immunodeficiency virus reverse transcription. Antimicrobial Agents & Chemotherapy 40:527-540.
    • (1996) Antimicrobial Agents & Chemotherapy , vol.40 , pp. 527-540
    • Arts, E.J.1    Wainberg, M.A.2
  • 5
    • 0029035638 scopus 로고
    • Analysis of mutations at position-184 in reverse transcriptase of human immunodeficiency virus type 1
    • Boyer PL & Hughes SH (1995) Analysis of mutations at position-184 in reverse transcriptase of human immunodeficiency virus type 1. Antimicrobial Agents and Chemotherapy 39:1624-1628.
    • (1995) Antimicrobial Agents and Chemotherapy , vol.39 , pp. 1624-1628
    • Boyer, P.L.1    Hughes, S.H.2
  • 7
    • 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 (2001) Selective excision of AZTMP by drug-resistant human immunodeficiency virus reverse transcriptase. Journal of Virology 75:4832-4842.
    • (2001) Journal of Virology , vol.75 , pp. 4832-4842
    • Boyer, P.L.1    Sarafianos, S.G.2    Arnold, E.3    Hughes, S.H.4
  • 8
    • 0028341306 scopus 로고
    • Sensitivity of wild-type human immunodeficiency virus type 1 reverse transcriptase to dideoxynucleotides depends on template length-the sensitivity of drug-resistant mutants does not
    • Boyer PL, Tantillo C, Jacobo-Molina A, Nanni RG, Ding J, Arnold E & Hughes SH (1994) Sensitivity of wild-type human immunodeficiency virus type 1 reverse transcriptase to dideoxynucleotides depends on template length-the sensitivity of drug-resistant mutants does not. Proceedings of the National Academy of Sciences USA 91:4882-4886.
    • (1994) Proceedings of the National Academy of Sciences USA , vol.91 , pp. 4882-4886
    • Boyer, P.L.1    Tantillo, C.2    Jacobo-Molina, A.3    Nanni, R.G.4    Ding, J.5    Arnold, E.6    Hughes, S.H.7
  • 11
    • 0028221001 scopus 로고
    • Sensitivity of HIV-1 reverse transcriptase and its mutants to inhibition by azidothymidine triphosphate
    • Carroll SS, Geib J, Olsen DB, Stahlhut M, Shafer JA & Kuo LC (1994) Sensitivity of HIV-1 reverse transcriptase and its mutants to inhibition by azidothymidine triphosphate. Biochemistry 332:113-2120.
    • (1994) Biochemistry , vol.332 , pp. 113-2120
    • Carroll, S.S.1    Geib, J.2    Olsen, D.B.3    Stahlhut, M.4    Shafer, J.A.5    Kuo, L.C.6
  • 12
    • 0028921384 scopus 로고
    • The nucleoside deaminases for cytidine and adenosine-structure, transition-state stabilization, mechanism, and evolution
    • Carter C W (1995) The nucleoside deaminases for cytidine and adenosine-structure, transition-state stabilization, mechanism, and evolution. Biohemie 77:92-98.
    • (1995) Biohemie , vol.77 , pp. 92-98
    • Carter, C.W.1
  • 13
    • 0026697262 scopus 로고
    • Deoxycytidine deaminase-resistant stereoisomer is the active form of (±)-2′,3′-dideoxy-3′-thiacytidine in the inhibition of hepatitis B virus replication
    • Chang CN, Doong SL, Zhou JH, Beach JW, Jeong LS, Chu CK, Tsai CH & Cheng YC (1992) Deoxycytidine deaminase-resistant stereoisomer is the active form of (±)-2′,3′-dideoxy-3′-thiacytidine in the inhibition of hepatitis B virus replication. Journal of Biological Chemistry 267:13938-13942.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 13938-13942
    • Chang, C.N.1    Doong, S.L.2    Zhou, J.H.3    Beach, J.W.4    Jeong, L.S.5    Chu, C.K.6    Tsai, C.H.7    Cheng, Y.C.8
  • 14
    • 0026563976 scopus 로고
    • Biochemical pharmacology of (+)-2′,3′-dideoxy-3′-thiacytidine and (-)-2′,3′-dideoxy-3′-thiacytidine as antihepatitis B-virus agents
    • Chang CN, Skalski V, Zhou J & Cheng YC (1992) Biochemical pharmacology of (+)-2′,3′-dideoxy-3′-thiacytidine and (-)-2′,3′-dideoxy-3′-thiacytidine as antihepatitis B-virus agents. Journal of Biological Chemistry 267:22414-22420.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 22414-22420
    • Chang, C.N.1    Skalski, V.2    Zhou, J.3    Cheng, Y.C.4
  • 15
    • 0032509101 scopus 로고    scopus 로고
    • Structure 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 JP, Das K, Hsiou Y, Sarafianos SG, Clark Jr AD, Jacobo-Molina A, Tantillo C, Hughes SH & Arnold E (1998) Structure 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. Journal of Molecular Biology 284:1095-1111.
    • (1998) Journal of Molecular Biology , vol.284 , pp. 1095-1111
    • Ding, J.P.1    Das, K.2    Hsiou, Y.3    Sarafianos, S.G.4    Clark A.D., Jr.5    Jacobo-Molina, A.6    Tantillo, C.7    Hughes, S.H.8    Arnold, E.9
  • 16
    • 0038210853 scopus 로고
    • Inhibition of HIV-1 and simian immunodeficiency virus (SIV) reverse transcriptases by the 5′-triphosphates of 3′-azido-2′,3′-dideoxyuridine (CS-87), 3′azido-3′-deoxyuthymidine (AZT), and 3′-azido-2′,3′-dideoxy-5-ethyluridine (CS-85)
    • Eriksson BFH, Schinazi RF & Chu CK (1988) Inhibition of HIV-1 and simian immunodeficiency virus (SIV) reverse transcriptases by the 5′-triphosphates of 3′-azido-2′,3′-dideoxyuridine (CS-87), 3′azido-3′-deoxyuthymidine (AZT), and 3′-azido-2′,3′-dideoxy-5-ethyluridine (CS-85). Antiviral Research 9:84-84.
    • (1988) Antiviral Research , vol.9 , pp. 84
    • Eriksson, B.F.H.1    Schinazi, R.F.2    Chu, C.K.3
  • 17
    • 0033524447 scopus 로고    scopus 로고
    • Mechanistic studies comparing the incorporation of (+) and (-) isomers of 3TCTP by HIV-1 reverse transcriptase
    • Feng JY & Anderson KS (1999) Mechanistic studies comparing the incorporation of (+) and (-) isomers of 3TCTP by HIV-1 reverse transcriptase. Biochemistry 38:55-63.
    • (1999) Biochemistry , vol.38 , pp. 55-63
    • Feng, J.Y.1    Anderson, K.S.2
  • 18
    • 0033773435 scopus 로고    scopus 로고
    • Cellular factors for resistance against antiretroviral agents
    • Fridland A, Connelly MC & Robbins BL (2000) Cellular factors for resistance against antiretroviral agents. Antiviral Therapy 5:181-185.
    • (2000) Antiviral Therapy , vol.5 , pp. 181-185
    • Fridland, A.1    Connelly, M.C.2    Robbins, B.L.3
  • 22
    • 0026542755 scopus 로고
    • In vitro selection of variants of human immunodeficiency virus type 1 resistant to 3′-azido-3′-deoxythymidine and 2′,3′-dideoxyinosine
    • Gao Q, Gu Z, Parniak MA, Li X & Wainberg MA (1992) In vitro selection of variants of human immunodeficiency virus type 1 resistant to 3′-azido-3′-deoxythymidine and 2′,3′-dideoxyinosine. Journal of Virology 66:12-19.
    • (1992) Journal of Virology , vol.66 , pp. 12-19
    • Gao, Q.1    Gu, Z.2    Parniak, M.A.3    Li, X.4    Wainberg, M.A.5
  • 23
    • 49149147973 scopus 로고
    • Iterative partial equalization of orbital electronegativity - A rapid access to atomic charges
    • Gästalger J & Marsili M (1980) Iterative partial equalization of orbital electronegativity - A rapid access to atomic charges. Tetrahedron. 36:3219-3228.
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gästalger, J.1    Marsili, M.2
  • 24
    • 0028865886 scopus 로고
    • The intracallular phosphorylation of (-)-2′-deoxy-3′-thiacytidine (3TC) and the incorporation of 3TC 5′-monophosphate into DNA by HIV-1 reverse transcriptase and human DNA-polymerase γ
    • Gray NM, Marr CL, Penn CR, Cameron JL & Bethell RC (1995) The intracallular phosphorylation of (-)-2′-deoxy-3′-thiacytidine (3TC) and the incorporation of 3TC 5′-monophosphate into DNA by HIV-1 reverse transcriptase and human DNA-polymerase γ. Biochemical Pharmacology 50:1043-1051.
    • (1995) Biochemical Pharmacology , vol.50 , pp. 1043-1051
    • Gray, N.M.1    Marr, C.L.2    Penn, C.R.3    Cameron, J.L.4    Bethell, R.C.5
  • 25
    • 0032823357 scopus 로고    scopus 로고
    • Mechanism of action and in vitro activity of 1′,3′-dioxolanylpurine nucleoside analogues against sensitive and drug-resistant human immunodeficiency virus type 1 variants
    • Gu Z, Wainberg MA, Nguyen-Ba N, L'Heureux L, De Muys JM, Bowlin TL & Rando RF (1999) Mechanism of action and in vitro activity of 1′,3′-dioxolanylpurine nucleoside analogues against sensitive and drug-resistant human immunodeficiency virus type 1 variants. Antimicrobial Agents and Chemotherapy 43:2376-2382.
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , pp. 2376-2382
    • Gu, Z.1    Wainberg, M.A.2    Nguyen-Ba, N.3    L'Heureux, L.4    De Muys, J.M.5    Bowlin, T.L.6    Rando, R.F.7
  • 27
    • 0029843986 scopus 로고    scopus 로고
    • Significance of amino acid variation at human immunodeficiency virus type 1 reverse transcriptase residue 210 for zidovudine susceptibility
    • Harrigan PR, Kinghorn I, Bloor S, Kemp SD, Najera I, Kohli A & Larder BA (1996) Significance of amino acid variation at human immunodeficiency virus type 1 reverse transcriptase residue 210 for zidovudine susceptibility. Journal of Virology 70:5930-5934.
    • (1996) Journal of Virology , vol.70 , pp. 5930-5934
    • Harrigan, P.R.1    Kinghorn, I.2    Bloor, S.3    Kemp, S.D.4    Najera, I.5    Kohli, A.6    Larder, B.A.7
  • 28
    • 0017314888 scopus 로고
    • Electrostatic potentials of proteins. 2. Role of electrostatics in a possible catalytic mechanism for carboxypeptidase-A
    • Hayes DM, Kollman PA (1976) Electrostatic potentials of proteins. 2. Role of electrostatics in a possible catalytic mechanism for carboxypeptidase-A. Journal of the American Chemical Society 98:3335-3345.
    • (1976) Journal of the American Chemical Society , vol.98 , pp. 3335-3345
    • Hayes, D.M.1    Kollman, P.A.2
  • 29
    • 10244227943 scopus 로고    scopus 로고
    • An in vivo mutation from leucine to tryptophan at position 210 in human immunodeficiency virus type 1 reverse transcriptase contributes to high-level resistance to 3′-azido-3′-deoxythymidine
    • Hooker DJ, Tachedjian G, Solomon AE, Gurusinghe AD, Land S, Birch C, Anderson JL, Roy BM, Aronld E & Deacon NJ (1996) An in vivo mutation from leucine to tryptophan at position 210 in human immunodeficiency virus type 1 reverse transcriptase contributes to high-level resistance to 3′-azido-3′-deoxythymidine. Journal of Virology 70:8010-8018.
    • (1996) Journal of Virology , vol.70 , pp. 8010-8018
    • Hooker, D.J.1    Tachedjian, G.2    Solomon, A.E.3    Gurusinghe, A.D.4    Land, S.5    Birch, C.6    Anderson, J.L.7    Roy, B.M.8    Aronld, E.9    Deacon, N.J.10
  • 30
    • 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 G & Harrison S (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.3    Harrison, S.4
  • 31
    • 0024519430 scopus 로고
    • Human immunodeficiency virus-1 reverse transcriptase-template binding, processivity, strand displacement synthesis, and template switching
    • Huber HE, McCoy JM, Seehra JS & Richardson CC (1989) Human immunodeficiency virus-1 reverse transcriptase-template binding, processivity, strand displacement synthesis, and template switching. Journal of Biological Chemistry 264:4669-4678.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 4669-4678
    • Huber, H.E.1    McCoy, J.M.2    Seehra, J.S.3    Richardson, C.C.4
  • 34
    • 0030331806 scopus 로고    scopus 로고
    • Modeling of purine nucleoside metabolism during mouse embryonic development. Relative routes of adenosine, deoxyadenosine and deoxyguanosine metabolism
    • Jenuth JP, Mably ER & Snyder FF (1996) Modeling of purine nucleoside metabolism during mouse embryonic development. Relative routes of adenosine, deoxyadenosine and deoxyguanosine metabolism. Biochemistry and Cell Biology 74:219-225.
    • (1996) Biochemistry and Cell Biology , vol.74 , pp. 219-225
    • Jenuth, J.P.1    Mably, E.R.2    Snyder, F.F.3
  • 36
    • 0026565278 scopus 로고
    • Fifth mutation in human immunodeficiency virus type 1 reverse transcriptase contributes to the development of high-level resistance to zidovudine
    • Kellam P, Boucher CA & Larder BA (1992) Fifth mutation in human immunodeficiency virus type 1 reverse transcriptase contributes to the development of high-level resistance to zidovudine. Proceedings of the National Academy of Sciences USA 89:1934-1938.
    • (1992) Proceedings of the National Academy of Sciences USA , vol.89 , pp. 1934-1938
    • Kellam, P.1    Boucher, C.A.2    Larder, B.A.3
  • 37
    • 0030703245 scopus 로고    scopus 로고
    • Pre-steady-state kinetic characterization of wild-type and 3′-azido-3′-deoxythymidine (AZT) resistant human immunodeficiency virus type 1 reverse transcriptase: Implication of RNA directed DNA polymerization in the mechanism of AZT resistance
    • Kerr SG & Anderson KS (1997) Pre-steady-state kinetic characterization of wild-type and 3′-azido-3′-deoxythymidine (AZT) resistant human immunodeficiency virus type 1 reverse transcriptase: implication of RNA directed DNA polymerization in the mechanism of AZT resistance. Biochemistry 36:14064-14070.
    • (1997) Biochemistry , vol.36 , pp. 14064-14070
    • Kerr, S.G.1    Anderson, K.S.2
  • 41
    • 0343811737 scopus 로고    scopus 로고
    • Single-step kinetics of HIV-1 reverse transcriptase mutants responsible for virus resistance to nucleoside inhibitors zidovudine and 3TC
    • Krebs R, Immendörfer U, Thrall SH, Wohrl BM & Goody RS (1997) Single-step kinetics of HIV-1 reverse transcriptase mutants responsible for virus resistance to nucleoside inhibitors zidovudine and 3TC. Biochemistry 36:10292-10300.
    • (1997) Biochemistry , vol.36 , pp. 10292-10300
    • Krebs, R.1    Immendörfer, U.2    Thrall, S.H.3    Wohrl, B.M.4    Goody, R.S.5
  • 42
    • 0026755210 scopus 로고
    • Biochemical studies on the reverse transcriptase and RNAse H activities from human immunodeficiency virus strains resistant to 3′-azido-3′-deoxythymidine
    • Lacey SF, Reardon JE, Furfine ES, Kunkel TA, Bebenek K, Eckert KA, Kemp SD & Larder BA (1992) Biochemical studies on the reverse transcriptase and RNAse H activities from human immunodeficiency virus strains resistant to 3′-azido-3′-deoxythymidine. Journal of Biological Chemistry 267:15789-15794.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 15789-15794
    • Lacey, S.F.1    Reardon, J.E.2    Furfine, E.S.3    Kunkel, T.A.4    Bebenek, K.5    Eckert, K.A.6    Kemp, S.D.7    Larder, B.A.8
  • 43
    • 0024310253 scopus 로고
    • Multiple mutations in HIV-1 reverse transcriptase confer high-level resistance to Zidovudine (AZT)
    • Larder BA & Kemp SD (1989) Multiple mutations in HIV-1 reverse transcriptase confer high-level resistance to Zidovudine (AZT). Science 246:1155-1158.
    • (1989) Science , vol.246 , pp. 1155-1158
    • Larder, B.A.1    Kemp, S.D.2
  • 45
    • 0009653840 scopus 로고
    • AZT resistance suppressed by a mutation conferring HIV-1 resistance to non-nucleoside reverse transcriptase inhibitors
    • Larder BA (1992) AZT resistance suppressed by a mutation conferring HIV-1 resistance to non-nucleoside reverse transcriptase inhibitors. Antimicrobial Agents and Chemotherapy 36:1171-1174.
    • (1992) Antimicrobial Agents and Chemotherapy , vol.36 , pp. 1171-1174
    • Larder, B.A.1
  • 46
    • 0035173806 scopus 로고    scopus 로고
    • Molecular modeling approach to understanding the mode of action of L-nucleosides as antiviral agents
    • Lee K & Chu CK (2001) Molecular modeling approach to understanding the mode of action of L-nucleosides as antiviral agents. Antimicrobial Agents and Chamotherapy 45:138-144.
    • (2001) Antimicrobial Agents and Chamotherapy , vol.45 , pp. 138-144
    • Lee, K.1    Chu, C.K.2
  • 49
    • 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 (1999) A mechanism of AZT resistance: an increase in nucleotide-dependent primer unblocking by mutant HIV-1 reverse transcriptase. Molecular Cell 4:35-43.
    • (1999) Molecular 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
  • 50
    • 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 (1998) Unblocking of chain-terminated primer by HIV-1 reverse transcriptase through a nucleotide dependent mechanism. Proceedings of the National Academy of Sciences USA 95:13471-13476.
    • (1998) Proceedings of the National Academy of Sciences USA , vol.95 , pp. 13471-13476
    • Meyer, P.R.1    Matsuura, S.E.2    So, A.G.3    Scott, W.A.4
  • 51
    • 0000568705 scopus 로고
    • Resistance to antiretroviral compounds: Implications for the clinical management of HIV infection
    • Moyle GJ (1995) Resistance to antiretroviral compounds: implications for the clinical management of HIV infection. Immunology Infectious Diseases 5:170-182.
    • (1995) Immunology Infectious Diseases , vol.5 , pp. 170-182
    • Moyle, G.J.1
  • 52
    • 0027295759 scopus 로고
    • A comparison of the conformations of the 5′-triphosphates of zidovudine (AZT) and thymidine bound to HIV-1 reverse transcriptase
    • Painter GR, Aulabaugh AE & Andrew CW (1993) A comparison of the conformations of the 5′-triphosphates of zidovudine (AZT) and thymidine bound to HIV-1 reverse transcriptase. Biochemical and Biophysical Research Communications 191:1166-1171.
    • (1993) Biochemical and Biophysical Research Communications , vol.191 , pp. 1166-1171
    • Painter, G.R.1    Aulabaugh, A.E.2    Andrew, C.W.3
  • 53
    • 0025998147 scopus 로고
    • Initial binding of 2′-deoxynucleoside 5′-triphosphates to hyman immunodeficiency virus type 1 reverse transcriptase
    • Painter GR, Wright LL, Hopkins S & Furman PA (1991) Initial binding of 2′-deoxynucleoside 5′-triphosphates to hyman immunodeficiency virus type 1 reverse transcriptase. Journal of Biological Chemistry 266:19362-19368.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 19362-19368
    • Painter, G.R.1    Wright, L.L.2    Hopkins, S.3    Furman, P.A.4
  • 54
    • 0024267430 scopus 로고
    • Fidelity of HIV-1 reverse transcriptase
    • Preston BD, Poiesz BJ & Loeb LA (1988) Fidelity of HIV-1 reverse transcriptase. Science 242:1168-1171.
    • (1988) Science , vol.242 , pp. 1168-1171
    • Preston, B.D.1    Poiesz, B.J.2    Loeb, L.A.3
  • 55
    • 33751578897 scopus 로고
    • A brief review and table of semiempirical parameters used in Hückel molecular orbital method
    • Purcell WP & Singer JA (1967) A brief review and table of semiempirical parameters used in Hückel molecular orbital method. Journal of Chemical & Engineering Data 12:235-246.
    • (1967) Journal of Chemical & Engineering Data , vol.12 , pp. 235-246
    • Purcell, W.P.1    Singer, J.A.2
  • 56
    • 0024273119 scopus 로고
    • The accuracy of reverse transcriptase from HIV-1
    • Roberts JD, Bebenek K & Kunkel TA (1988) The accuracy of reverse transcriptase from HIV-1. Science 242:1171-1173.
    • (1988) Science , vol.242 , pp. 1171-1173
    • Roberts, J.D.1    Bebenek, K.2    Kunkel, T.A.3
  • 62
    • 0027431843 scopus 로고
    • The biochemical basis for the differential anti-human-immunodeficiency-virus activity of 2 cis enantiomers of 2′,3′-dideoxy-3′-thiacytidine
    • Skalski V, Chang CN, Dutschman G & Cheng YC (1993) The biochemical basis for the differential anti-human-immunodeficiency-virus activity of 2 cis enantiomers of 2′,3′-dideoxy-3′-thiacytidine. Journal of Biological Chemistry 168:23234-23238.
    • (1993) Journal of Biological Chemistry , vol.168 , pp. 23234-23238
    • Skalski, V.1    Chang, C.N.2    Dutschman, G.3    Cheng, Y.C.4
  • 63
    • 0033770149 scopus 로고    scopus 로고
    • Molecular mechanisms of HIV-1 resistance to nucleoside reverse transcriptase inhibitors (NRTIs)
    • Sluis-Cremer N, Arion D & Parniak MA (2000) Molecular mechanisms of HIV-1 resistance to nucleoside reverse transcriptase inhibitors (NRTIs). Cellular and Molecular Life Science 57:1408-1422.
    • (2000) Cellular and Molecular Life Science , vol.57 , pp. 1408-1422
    • Sluis-Cremer, N.1    Arion, D.2    Parniak, M.A.3
  • 65
    • 0028172345 scopus 로고
    • Locations of anti-AIDS drug binding sites and resistance mutations in the 3-dimensional structure of HIV-1 reverse transcriptase-implications for mechanisms of drug-inhibition and resistance
    • Tantillo C, Ding J, Jacobo-Molina A, Nanni RG, Boyer PL, Hughes SH, Pauwels R, Andries K, Janssen PAJ & Arnold E (1994) Locations of anti-AIDS drug binding sites and resistance mutations in the 3-dimensional structure of HIV-1 reverse transcriptase-implications for mechanisms of drug-inhibition and resistance. Journal of Molecular Biology 243:369-387.
    • (1994) Journal of Molecular Biology , 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
  • 66
    • 0023926840 scopus 로고
    • Solid-state conformation of anti-human immunodeficiency virus type-1 agents-Crystal structure of 3′-azido-3′deoxythymidine analogs
    • Van Roey P, Salerno JM, Duax WL, Chu CK, Anh MK & Schinazi RF (1988) Solid-state conformation of anti-human immunodeficiency virus type-1 agents-Crystal structure of 3′-azido-3′deoxythymidine analogs. Journal of the American Chemical Society 110:2277-2282.
    • (1988) Journal of the American Chemical Society , vol.110 , pp. 2277-2282
    • Van Roey, P.1    Salerno, J.M.2    Duax, W.L.3    Chu, C.K.4    Anh, M.K.5    Schinazi, R.F.6
  • 69
    • 0001154313 scopus 로고
    • Molecular mechanics studies of enzyme-substrate interactions-The interaction of L-N-acetylryptophanamide and D-N-acetyltryptophanamide with α-chymotrypsin
    • Wipff G, Dearing A, Weiner PK, Blaney JM, Kollman PA (1983) Molecular mechanics studies of enzyme-substrate interactions-The interaction of L-N-acetylryptophanamide and D-N-acetyltryptophanamide with α-chymotrypsin. Journal of the American Chemical Society 105:997-1005.
    • (1983) Journal of the American Chemical Society , vol.105 , pp. 997-1005
    • Wipff, G.1    Dearing, A.2    Weiner, P.K.3    Blaney, J.M.4    Kollman, P.A.5
  • 70
    • 0029812857 scopus 로고    scopus 로고
    • Transport of the antiviral nucleoside analogs 3′-azido-3′-deoxythymidine and 2′,3′-dideoxycytidine by a recombinant nucleoside transporter (rCNT) expressed in Xenopus laevis
    • Yao SYM, Cass C. E & Young JD (1996) Transport of the antiviral nucleoside analogs 3′-azido-3′-deoxythymidine and 2′,3′-dideoxycytidine by a recombinant nucleoside transporter (rCNT) expressed in Xenopus laevis. Molecular Pharmacology 50:388-393.
    • (1996) Molecular Pharmacology , vol.50 , pp. 388-393
    • Yao, S.Y.M.1    Cass, C.E.2    Young, J.D.3
  • 71
    • 0026760911 scopus 로고
    • Comparison of HIV-1 and avian myeloblastosis virus reverse transcriptase fidelity on RNA and DNA templates
    • Yu H & Goodman MF (1992) Comparison of HIV-1 and avian myeloblastosis virus reverse transcriptase fidelity on RNA and DNA templates. Journal of Biological Chemistry 267:10888-10896.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 10888-10896
    • Yu, H.1    Goodman, M.F.2


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