메뉴 건너뛰기




Volumn 11, Issue 3, 2000, Pages 165-189

The enantioselectivity of enzymes involved in current antiviral therapy using nucleoside analogues: A new strategy?

Author keywords

Enantioselectivity; L nucleosides; Nucleoside metabolizing enzymes; Viral enzymes; Virus inhibitors

Indexed keywords

ABACAVIR; ADENOSINE DEAMINASE; ANTIVIRUS AGENT; CYTIDINE DEAMINASE; DEOXYCYTIDINE KINASE; DEOXYGUANOSINE DERIVATIVE; DEOXYGUANOSINE KINASE; DEOXYURIDINE DERIVATIVE; DIDANOSINE; DNA POLYMERASE; EDOXUDINE; IDOXURIDINE; LAMIVUDINE; NUCLEOSIDE; NUCLEOSIDE ANALOG; NUCLEOTIDE; PENCICLOVIR; PHOSPHOTRANSFERASE; RNA DIRECTED DNA POLYMERASE; STAVUDINE; THYMIDINE KINASE; TRIFLURIDINE; VIDARABINE; VIRUS DNA; VIRUS ENZYME; ZALCITABINE; ZIDOVUDINE;

EID: 0033934998     PISSN: 09563202     EISSN: None     Source Type: Journal    
DOI: 10.1177/095632020001100301     Document Type: Review
Times cited : (40)

References (151)
  • 3
    • 0031463610 scopus 로고    scopus 로고
    • Pyrimidine nucleotidases from human erythrocytes possess phosphotransferase activities specific for pyrimidine nucleotides
    • Amici A, Emanuelli M, Magni G, Rafaelli N & Ruggieri S (1997) Pyrimidine nucleotidases from human erythrocytes possess phosphotransferase activities specific for pyrimidine nucleotides. FEBS Letters 419:263-267.
    • (1997) FEBS Letters , vol.419 , pp. 263-267
    • Amici, A.1    Emanuelli, M.2    Magni, G.3    Rafaelli, N.4    Ruggieri, S.5
  • 5
    • 0025219482 scopus 로고
    • Carbocyclic 5-iodo-2′-deoxyuridine (C-IdU) and carbocyclic (E)-5-(2-bromovinyl)-2′-deoxyuridine (C-BVdU) as unique examples of chiral molecules where the two enantiomers forms are biologically active: Interaction of the (+)- and (-)-enantiomers of C-IdU and C-BVdU with the thymidine kinase of Herpes simplex virus type 1
    • Balzarini J, De Clercq E, Baumgartner H, Bodenteich M & Griengl H (1990) Carbocyclic 5-iodo-2′-deoxyuridine (C-IdU) and carbocyclic (E)-5-(2-bromovinyl)-2′-deoxyuridine (C-BVdU) as unique examples of chiral molecules where the two enantiomers forms are biologically active: interaction of the (+)- and (-)-enantiomers of C-IdU and C-BVdU with the thymidine kinase of Herpes simplex virus type 1. Molecular Pharmacology 37:395-401.
    • (1990) Molecular Pharmacology , vol.37 , pp. 395-401
    • Balzarini, J.1    De Clercq, E.2    Baumgartner, H.3    Bodenteich, M.4    Griengl, H.5
  • 6
    • 0024592935 scopus 로고
    • Differential patterns of intracellular metabolism of 2′,3′-didehydro-2′,3′-dideoxythymidine and 3′-azidothymidine, two potent anti-human immunodeficiency virus compounds
    • Balzarini J, Herdewiijn P & De Clercq E (1989) Differential patterns of intracellular metabolism of 2′,3′-didehydro-2′,3′-dideoxythymidine and 3′-azidothymidine, two potent anti-human immunodeficiency virus compounds. Journal of Biological Chemistry 264:6127-6133.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 6127-6133
    • Balzarini, J.1    Herdewiijn, P.2    De Clercq, E.3
  • 9
    • 0344878893 scopus 로고    scopus 로고
    • Metabolism in human cells of the D and L enantiomers of the carbocyclic analog of 2′-deoxyguanosine: Substrate activity with deoxycytidine kinase, mitochondrial deoxyguanosine kinase and 5′-nucleotidase
    • Bennett LL, Allan PW, Arnett G, Shealy YF, Shewach DS, Mason WS, Fourel I & Parker WB (1998) Metabolism in human cells of the D and L enantiomers of the carbocyclic analog of 2′-deoxyguanosine: substrate activity with deoxycytidine kinase, mitochondrial deoxyguanosine kinase and 5′-nucleotidase. Antimicrobial Agents and Chemotherapy 42:1045-1051.
    • (1998) Antimicrobial Agents and Chemotherapy , vol.42 , pp. 1045-1051
    • Bennett, L.L.1    Allan, P.W.2    Arnett, G.3    Shealy, Y.F.4    Shewach, D.S.5    Mason, W.S.6    Fourel, I.7    Parker, W.B.8
  • 10
    • 0027755282 scopus 로고
    • Phosphorylation of the enandomers of the carbocyclic analog of 2′-deoxyguanosine in cells infected with Herpes simplex virus type 1 and in uninfected cells. Lack of enantiomeric selectivity with the viral thymidine kinase
    • Bennett LL, Parker WB, Allan LW, Rose LM, Shealy YF, Secrist III JA, Montgomery JA, Arnett G, Kirkman RL & Shannon WM (1993) Phosphorylation of the enandomers of the carbocyclic analog of 2′-deoxyguanosine in cells infected with Herpes simplex virus type 1 and in uninfected cells. Lack of enantiomeric selectivity with the viral thymidine kinase. Molecular Pharmacology 44:1258-1266.
    • (1993) Molecular Pharmacology , vol.44 , pp. 1258-1266
    • Bennett, L.L.1    Parker, W.B.2    Allan, L.W.3    Rose, L.M.4    Shealy, Y.F.5    Secrist J.A. III6    Montgomery, J.A.7    Arnett, G.8    Kirkman, R.L.9    Shannon, W.M.10
  • 17
    • 0028921384 scopus 로고
    • The nucleoside deaminases for cytidine and adenosine: Structure, transition state stabilization, mechanism, and evolution
    • Carter CW (1995) The nucleoside deaminases for cytidine and adenosine: Structure, transition state stabilization, mechanism, and evolution. Biochimie 77:92-98.
    • (1995) Biochimie , vol.77 , pp. 92-98
    • Carter, C.W.1
  • 19
    • 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 C & Cheng Y-C (1992a) 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.7    Cheng, Y.-C.8
  • 20
    • 0026563976 scopus 로고
    • Biochemical pharmacology of (+)- and (-)-2′,3′-dideoxy-3′-thiacytidine as anti-hepatitis B virus agents
    • Chang C-N, Skalski V, Zhou JH & Cheng Y-C (1992b) Biochemical pharmacology of (+)- and (-)-2′,3′-dideoxy-3′-thiacytidine as anti-hepatitis 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.H.3    Cheng, Y.-C.4
  • 23
    • 1842293414 scopus 로고    scopus 로고
    • Inhibitory effect of penciclovir-triphosphate on duck hepatitis B virus reverse transcription
    • Dannaoui E, Trepo C & Zoulim F (1997) Inhibitory effect of penciclovir-triphosphate on duck hepatitis B virus reverse transcription. Antiviral Chemistry and Chemotherapy 8:38-46.
    • (1997) Antiviral Chemistry and Chemotherapy , vol.8 , pp. 38-46
    • Dannaoui, E.1    Trepo, C.2    Zoulim, F.3
  • 25
    • 0030458758 scopus 로고    scopus 로고
    • Phosphorylation of nucleoside diphosphate kinase at the active site studied by steady-state and time-resolved fluorescence
    • Deville-Bonne D, Sellam O, Merola F, Lascu I, Desmadril M & Veron M (1996) Phosphorylation of nucleoside diphosphate kinase at the active site studied by steady-state and time-resolved fluorescence. Biochemistry 35:14643-14650.
    • (1996) Biochemistry , vol.35 , pp. 14643-14650
    • Deville-Bonne, D.1    Sellam, O.2    Merola, F.3    Lascu, I.4    Desmadril, M.5    Veron, M.6
  • 27
    • 0031836316 scopus 로고    scopus 로고
    • 2′,3′-Dideoxy-2′,3′-didehydro-ß-L(-)-5- fluorocytidine and its activity in combination with clinically approved anti-human immunodeficiency virus β-D(+)nucleoside analogs in vitro
    • Dutschman GE, Bridges EG, Liu SH, Gullen E, Guo X, Kukhanova M & Cheng Y-C (1998) 2′,3′-Dideoxy-2′,3′-didehydro-ß-L(-)-5- fluorocytidine and its activity in combination with clinically approved anti-human immunodeficiency virus β-D(+)nucleoside analogs in vitro. Antimicrobial Agents and Chemotherapy 42:1799-1804.
    • (1998) Antimicrobial Agents and Chemotherapy , vol.42 , pp. 1799-1804
    • Dutschman, G.E.1    Bridges, E.G.2    Liu, S.H.3    Gullen, E.4    Guo, X.5    Kukhanova, M.6    Cheng, Y.-C.7
  • 29
    • 0030855683 scopus 로고    scopus 로고
    • Substrate specificities, expression and primary sequences of deoxynucleoside kinases; implications for chemotherapy
    • Eriksson S & Wang L (1997) Substrate specificities, expression and primary sequences of deoxynucleoside kinases; implications for chemotherapy. Nucleosides and Nucleotides 16:653-659.
    • (1997) Nucleosides and Nucleotides , vol.16 , pp. 653-659
    • Eriksson, S.1    Wang, L.2
  • 32
    • 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 38 , pp. 55-63
    • Feng, J.Y.1    Anderson, K.S.2
  • 33
    • 0029094279 scopus 로고
    • Stereospecificity of human DNA polymerases α, β, γ, δ, and ε, HIV-reverse transcriptase, HSV-1 DNA polymerase, calf thymus terminal transferase and Escherichia coli DNA polymerase I in recognising D- and L-thymidine 5′-triphosphate as substrate
    • Focher F, Maga G, Bendiscioli A, Capobianco M, Colonna F, Garbesi A, Spadari S (1995) Stereospecificity of human DNA polymerases α, β, γ, δ, and ε, HIV-reverse transcriptase, HSV-1 DNA polymerase, calf thymus terminal transferase and Escherichia coli DNA polymerase I in recognising D- and L-thymidine 5′-triphosphate as substrate. Nucleic Acids Research 23:2840-2847.
    • (1995) Nucleic Acids Research , vol.23 , pp. 2840-2847
    • Focher, F.1    Maga, G.2    Bendiscioli, A.3    Capobianco, M.4    Colonna, F.5    Garbesi, A.6    Spadari, S.7
  • 37
    • 15444378688 scopus 로고
    • Deamination of carbocyclic adenosine analogs with adenosine deaminase and its synthetic utility
    • Gala D & Schumacher DP (1992) Deamination of carbocyclic adenosine analogs with adenosine deaminase and its synthetic utility. Synlett 61-63.
    • (1992) Synlett , pp. 61-63
    • Gala, D.1    Schumacher, D.P.2
  • 38
    • 0024431197 scopus 로고
    • Enantiomeric selectivity of adenosine transport systems in mouse erythrocytes and L1210 cells
    • Gati WP, Dagnino L & Paterson ARP (1989) Enantiomeric selectivity of adenosine transport systems in mouse erythrocytes and L1210 cells. Biochemical Journal 263:957-960.
    • (1989) Biochemical Journal , vol.263 , pp. 957-960
    • Gati, W.P.1    Dagnino, L.2    Paterson, A.R.P.3
  • 41
    • 0026464790 scopus 로고
    • Viral thymidine kinases and their relatives
    • Gentry GA (1992) Viral thymidine kinases and their relatives. Pharmacology and Therapeutics 54:319-355.
    • (1992) Pharmacology and Therapeutics , vol.54 , pp. 319-355
    • Gentry, G.A.1
  • 43
    • 0028865886 scopus 로고
    • The intracellular phosphorylation of (-)-2′-deoxy-3′-thiacytidine (3TC) and the incorporation of 3-TC 5′-monophosphate into DNA by HIV-1 reverse transcriptase and human DNA polymerase gamma
    • Gray NM, Marr CL, Penn CR, Cameron JM & Bethell RC (1995) The intracellular phosphorylation of (-)-2′-deoxy-3′-thiacytidine (3TC) and the incorporation of 3-TC 5′-monophosphate into DNA by HIV-1 reverse transcriptase and human DNA polymerase gamma. 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.M.4    Bethell, R.C.5
  • 44
    • 0028982940 scopus 로고
    • Anticancer activity of β-L-dioxolanecytidine, a novel nucleoside analogue with the unnatural L configuration
    • Grove KL, Guo X, Liu SH, Gao Z, Chu CK & Cheng Y-C (1995) Anticancer activity of β-L-dioxolanecytidine, a novel nucleoside analogue with the unnatural L configuration. Cancer Research 55:3008-3011.
    • (1995) Cancer Research , vol.55 , pp. 3008-3011
    • Grove, K.L.1    Guo, X.2    Liu, S.H.3    Gao, Z.4    Chu, C.K.5    Cheng, Y.-C.6
  • 45
    • 0025924850 scopus 로고
    • L-[3H]adenosine, a new metabolically stable enantiomeric probe for adenosine transport systems in rat brain synaptoneurosomes
    • Gu JG, Delaney S, Sawka AN & Geiger JD (1991) L-[3H]adenosine, a new metabolically stable enantiomeric probe for adenosine transport systems in rat brain synaptoneurosomes. Journal of Neurochemistry 56:548-552.
    • (1991) Journal of Neurochemistry , vol.56 , pp. 548-552
    • Gu, J.G.1    Delaney, S.2    Sawka, A.N.3    Geiger, J.D.4
  • 46
    • 0026094411 scopus 로고
    • Evolution of Herpes virus thymidine kinase from cellular deoxycytidine kinase
    • Harrison P, Thompson R & Davison A (1991) Evolution of Herpes virus thymidine kinase from cellular deoxycytidine kinase. Journal of General Virology 72:2583-2586.
    • (1991) Journal of General Virology , vol.72 , pp. 2583-2586
    • Harrison, P.1    Thompson, R.2    Davison, A.3
  • 47
    • 0026651622 scopus 로고
    • Effects of (-)-2′-deoxy-3′-thiacytidine (3TC) 5′-triphosphate on human immunodeficiency virus reverse transcriptase and mammalian DNA polymerases alpha, beta, and gamma
    • Hart GJ, Orr DC, Penn CR, Figueiredo HT, Gray NM, Boehme RE & Cameron LM (1992) Effects of (-)-2′-deoxy-3′-thiacytidine (3TC) 5′-triphosphate on human immunodeficiency virus reverse transcriptase and mammalian DNA polymerases alpha, beta, and gamma. Antimicrobial Agents and Chemotherapy 36:1688-1694.
    • (1992) Antimicrobial Agents and Chemotherapy , vol.36 , pp. 1688-1694
    • Hart, G.J.1    Orr, D.C.2    Penn, C.R.3    Figueiredo, H.T.4    Gray, N.M.5    Boehme, R.E.6    Cameron, L.M.7
  • 49
    • 0027365750 scopus 로고
    • Kinetic mechanism of the DNA-dependent DNA polymerase activity of human immunodeficiency virus reverse transcriptase
    • Hsieh J-C, Zinnen S & Modrich P (1993) Kinetic mechanism of the DNA-dependent DNA polymerase activity of human immunodeficiency virus reverse transcriptase. Journal of Biological Chemistry 268:24607-24613.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 24607-24613
    • Hsieh, J.-C.1    Zinnen, S.2    Modrich, P.3
  • 50
    • 0030035038 scopus 로고    scopus 로고
    • Hsp90 is required for the activity of a hepatits B virus reverse transcriptase
    • Hu J & Seeger C (1996) Hsp90 is required for the activity of a hepatits B virus reverse transcriptase. Proceeding of the National Academy of Sciences, USA 93:1060-1064.
    • (1996) Proceeding of the National Academy of Sciences, USA , vol.93 , pp. 1060-1064
    • Hu, J.1    Seeger, C.2
  • 51
    • 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 (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
  • 52
    • 0022378459 scopus 로고
    • Regulation of deoxyadenosine and nucleoside analog phosphorylation by human placental adenosine kinase
    • Hurley MC, Lin BB & Fox IH (1985) Regulation of deoxyadenosine and nucleoside analog phosphorylation by human placental adenosine kinase. Journal of Biological Chemistry 260:15675-15681.
    • (1985) Journal of Biological Chemistry , vol.260 , pp. 15675-15681
    • Hurley, M.C.1    Lin, B.B.2    Fox, I.H.3
  • 53
    • 0025570249 scopus 로고
    • New approaches to the synthesis of antiviral nucleosides
    • Hutchinson DW (1990) New approaches to the synthesis of antiviral nucleosides. TIBTECH 8:348-353.
    • (1990) TIBTECH , vol.8 , pp. 348-353
    • Hutchinson, D.W.1
  • 54
    • 0028928572 scopus 로고
    • Acyclic guanosine analogs inhibit DNA polymerases α, δ, and ε with very different potencies and have unique mechanisms of action
    • Ilsley DD, Lee S-H, Miller WH & Kuchta RD (1995) Acyclic guanosine analogs inhibit DNA polymerases α, δ, and ε with very different potencies and have unique mechanisms of action. Biochemistry 34:2504-2510.
    • (1995) Biochemistry , vol.34 , pp. 2504-2510
    • Ilsley, D.D.1    Lee, S.-H.2    Miller, W.H.3    Kuchta, R.D.4
  • 57
    • 0029689120 scopus 로고    scopus 로고
    • Structure activity relationships for phosphorylation of nucleoside analogs to monophosphates by nucleoside kinases
    • Johansson NG & Eriksson S (1996) Structure activity relationships for phosphorylation of nucleoside analogs to monophosphates by nucleoside kinases. Acta Biochimica Polonica 43:143-160.
    • (1996) Acta Biochimica Polonica , vol.43 , pp. 143-160
    • Johansson, N.G.1    Eriksson, S.2
  • 58
    • 0024435381 scopus 로고
    • Phosphorylation of 2′,3′-dideoxyinosine by cytosolic 5′-nucleotidase of human lymphoid cells
    • Johnson MA & Fridland A (1989) Phosphorylation of 2′,3′-dideoxyinosine by cytosolic 5′-nucleotidase of human lymphoid cells. Molecular Pharmacology 36:291-295.
    • (1989) Molecular Pharmacology , vol.36 , pp. 291-295
    • Johnson, M.A.1    Fridland, A.2
  • 59
    • 0040908098 scopus 로고    scopus 로고
    • Supramolecular aspects of enzyme enantioselectivity
    • Edited by Murakami I. Oxford: Elsevier
    • Jongejan JA & Duine JA (1996) Supramolecular aspects of enzyme enantioselectivity. In Comprehensive supramolecular chemistry, vol. 2. Edited by Murakami I. Oxford: Elsevier.
    • (1996) Comprehensive Supramolecular Chemistry , vol.2
    • Jongejan, J.A.1    Duine, J.A.2
  • 61
    • 0023074558 scopus 로고
    • Stereochemical considerations in the enzymatic phosphorylation and antiviral activity of acyclonucleosides. I. Phosphorylation of 2′-nor-2′-deoxyguanosine
    • Karkas JD, Germershausen J, Tolman RL, MacCoss M, Wagner AF, Liou R & Bostedor R (1987) Stereochemical considerations in the enzymatic phosphorylation and antiviral activity of acyclonucleosides. I. Phosphorylation of 2′-nor-2′-deoxyguanosine. Biochimica et Biophysics Acta 911:127-135.
    • (1987) Biochimica et Biophysics Acta , vol.911 , pp. 127-135
    • Karkas, J.D.1    Germershausen, J.2    Tolman, R.L.3    Maccoss, M.4    Wagner, A.F.5    Liou, R.6    Bostedor, R.7
  • 62
    • 0027169694 scopus 로고
    • Synthesis of nucleosides and related compounds XXXI. Resolution of 9-[c-4,t-5-Bis(hydroxymethyl)cyclopent-2-en-r-1-yl]-9H-adenine [(±)-BCA] by means of high-pressure-mediated deamination with adenosine deaminase
    • Katagiri N, Shiraishi T, Toyota A, Sato H, Kaneko C & Aikawa T (1993) Synthesis of nucleosides and related compounds XXXI. Resolution of 9-[c-4,t-5-Bis(hydroxymethyl)cyclopent-2-en-r-1-yl]-9H-adenine [(±)-BCA] by means of high-pressure-mediated deamination with adenosine deaminase. Chemical and Pharmaceutical Bulletin 41:1012-1029.
    • (1993) Chemical and Pharmaceutical Bulletin , vol.41 , pp. 1012-1029
    • Katagiri, N.1    Shiraishi, T.2    Toyota, A.3    Sato, H.4    Kaneko, C.5    Aikawa, T.6
  • 63
    • 0032479324 scopus 로고    scopus 로고
    • Crystal structure of the ternary complex of E. Coli purine nucleoside phosphorylase with formycin b, a structural analogue of the substrate inosine, and phosphate (sulphate) at 2.1 Å resolution
    • Koellner G, Luic M, Shugar D, Saenger W & Bzowska A (1998) Crystal structure of the ternary complex of E. coli purine nucleoside phosphorylase with formycin B, a structural analogue of the substrate inosine, and phosphate (sulphate) at 2.1 Å resolution. Journal of Molecular Biology 280:153-166.
    • (1998) Journal of Molecular Biology , vol.280 , pp. 153-166
    • Koellner, G.1    Luic, M.2    Shugar, D.3    Saenger, W.4    Bzowska, A.5
  • 64
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt LA, Wang J, Friedman JM, Rice PA & Steitz TA (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
  • 65
    • 0031780614 scopus 로고    scopus 로고
    • Interaction of β-L-2′-3′-dideoxy-2′,3′-didehydro-5-fluoro-CTP with human immunodeficiency virus-1 reverse transcriptase and human DNA polymerases: Implications for human immunodeficiency virus drug design
    • Kukhanova M, Li X, Chen S-H, King I, Doyle T, Prusoff W & Cheng Y-C (1998a) Interaction of β-L-2′-3′-dideoxy-2′,3′-didehydro-5-fluoro-CTP with human immunodeficiency virus-1 reverse transcriptase and human DNA polymerases: Implications for human immunodeficiency virus drug design. Molecular Pharmacology 53:801-807.
    • (1998) Molecular Pharmacology , vol.53 , pp. 801-807
    • Kukhanova, M.1    Li, X.2    Chen, S.-H.3    King, I.4    Doyle, T.5    Prusoff, W.6    Cheng, Y.-C.7
  • 66
    • 0032523016 scopus 로고    scopus 로고
    • Unique inhibitory effect of 1-(2′-deoxy-2′-fluoro-β-L-arabinofuranosyl)-5-methyluracil 5′-triphosphate on Epstein-Barr virus and human DNA polymerases
    • Kukhanova M, Lin Z-Y, Yas'co M & Cheng Y-C (1998b) Unique inhibitory effect of 1-(2′-deoxy-2′-fluoro-β-L-arabinofuranosyl)-5-methyluracil 5′-triphosphate on Epstein-Barr virus and human DNA polymerases. Biochemical Pharmacology 55:1181-1187.
    • (1998) Biochemical Pharmacology , vol.55 , pp. 1181-1187
    • Kukhanova, M.1    Lin, Z.-Y.2    Yas'co, M.3    Cheng, Y.-C.4
  • 67
    • 0029088833 scopus 로고
    • L- and D-enantiomers of 2′,3′-dideoxycytidine 5′-triphosphate analogs as substrates fr human DNA polymerases
    • Kukhanova M, Liu S-H, Mozzherin D, Lin T-S, Chu CK & Cheng Y-C (1995) L- and D-enantiomers of 2′,3′-dideoxycytidine 5′-triphosphate analogs as substrates fr human DNA polymerases. Journal of Biological Chemistry 270:23055-23059.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 23055-23059
    • Kukhanova, M.1    Liu, S.-H.2    Mozzherin, D.3    Lin, T.-S.4    Chu, C.K.5    Cheng, Y.-C.6
  • 68
    • 0028209910 scopus 로고
    • Structure-activity relationships and conformational features of anthiherpetic pyrirnidine and purine nucleoside analogue. A review
    • Kulikowski T (1994) Structure-activity relationships and conformational features of anthiherpetic pyrirnidine and purine nucleoside analogue. A review. Pharmacy World and Science 16:127-138.
    • (1994) Pharmacy World and Science , vol.16 , pp. 127-138
    • Kulikowski, T.1
  • 71
    • 0032867862 scopus 로고    scopus 로고
    • Expression of an enzymatically active polymerase of human hepatitis B virus in a coupled transcription-translation system
    • Li Z & Tyrrell DL (1999) Expression of an enzymatically active polymerase of human hepatitis B virus in a coupled transcription-translation system. Biochemistry and Cell Biology 77:119-126.
    • (1999) Biochemistry and Cell Biology , vol.77 , pp. 119-126
    • Li, Z.1    Tyrrell, D.L.2
  • 72
    • 0028212546 scopus 로고
    • Synthesis and biological evaluation of 2′,3′-dideoxy-L-pyrimidine nucleosides as potential antiviral agents against human immunodeficiency virus (HIV) and hepatitis B virus (HBV)
    • Lin T-S, Luo M-Z, Liu M-C, Pai SB, Dutschman GE & Cheng Y-C (1994) Synthesis and biological evaluation of 2′,3′-dideoxy-L-pyrimidine nucleosides as potential antiviral agents against human immunodeficiency virus (HIV) and hepatitis B virus (HBV). Journal of Medicinal Chemistry 37:798-803.
    • (1994) Journal of Medicinal Chemistry , vol.37 , pp. 798-803
    • Lin, T.-S.1    Luo, M.-Z.2    Liu, M.-C.3    Pai, S.B.4    Dutschman, G.E.5    Cheng, Y.-C.6
  • 73
    • 0031979178 scopus 로고    scopus 로고
    • Unique metabolism of a novel antiviral L-nucleoside analog, 2′-fluoro-5-methyl-β-L-arabinofuranosyluracil. A substrate for both thymidine kinase and deoxycytidine kinase
    • Liu SH, Grove KL & Cheng Y-C (1998) Unique metabolism of a novel antiviral L-nucleoside analog, 2′-fluoro-5-methyl-β-L-arabinofuranosyluracil. A substrate for both thymidine kinase and deoxycytidine kinase. Antimicrobial Agents and Chemotherapy 42:833-839.
    • (1998) Antimicrobial Agents and Chemotherapy , vol.42 , pp. 833-839
    • Liu, S.H.1    Grove, K.L.2    Cheng, Y.-C.3
  • 74
    • 0033557321 scopus 로고    scopus 로고
    • Molecular basis for the enantioselectivity of HIV-1 reverse transcriptase: Role of the 3′-hydroxyl group of the L-(beta)-ribose in chiral discrimination between D- and L-enantiomers of deoxy- and dideoxy-nucleoside triphosphate analogs
    • Maga G, Amacker M, Hübscher U, Gosselin G, Imbach J-L, Mathe C, Faraj A, Sommadossi J-P & Spadari S (1999) Molecular basis for the enantioselectivity of HIV-1 reverse transcriptase: role of the 3′-hydroxyl group of the L-(beta)-ribose in chiral discrimination between D- and L-enantiomers of deoxy- and dideoxy-nucleoside triphosphate analogs. Nucleic Acids Research 27:972-978.
    • (1999) Nucleic Acids Research , vol.27 , pp. 972-978
    • Maga, G.1    Amacker, M.2    Hübscher, U.3    Gosselin, G.4    Imbach, J.-L.5    Mathe, C.6    Faraj, A.7    Sommadossi, J.-P.8    Spadari, S.9
  • 75
    • 0028169328 scopus 로고
    • Kinetic studies with N2-phenylguanines and with L-thymidine indicate that Herpes simplex virus type 1 thymidine kinase and thymidylate kinase share a common active site
    • Maga G, Focher F, Wright GE, Capobianco M, Garbesi A, Bendiscoli A & Spadari S (1994) Kinetic studies with N2-phenylguanines and with L-thymidine indicate that Herpes simplex virus type 1 thymidine kinase and thymidylate kinase share a common active site. Biochemical Journal 302:279-282.
    • (1994) Biochemical Journal , vol.302 , pp. 279-282
    • Maga, G.1    Focher, F.2    Wright, G.E.3    Capobianco, M.4    Garbesi, A.5    Bendiscoli, A.6    Spadari, S.7
  • 79
    • 0031572855 scopus 로고    scopus 로고
    • The crystal structure of Escherichia coli purine nucleoside phosphorylase: A comparison with the human enzyme reveals a conserved topology
    • Mao C, Cook WJ, Zhou M, Koszalka GW, Krenitsky TA & Ealick SE (1997) The crystal structure of Escherichia coli purine nucleoside phosphorylase: A comparison with the human enzyme reveals a conserved topology. Structure 5:1373-1383.
    • (1997) Structure , vol.5 , pp. 1373-1383
    • Mao, C.1    Cook, W.J.2    Zhou, M.3    Koszalka, G.W.4    Krenitsky, T.A.5    Ealick, S.E.6
  • 81
    • 0032506161 scopus 로고    scopus 로고
    • Structure of human adenosine kinase at 1.5 A resolution
    • Mathews II, Erion MD & Ealick SE (1998) Structure of human adenosine kinase at 1.5 A resolution. Biochemistry 37:15607-15620.
    • (1998) Biochemistry , vol.37 , pp. 15607-15620
    • Mathews, I.I.1    Erion, M.D.2    Ealick, S.E.3
  • 84
    • 0029646092 scopus 로고
    • X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 Å resolution
    • Morera S, Lacombe M-L, Xu Y, LeBras G & Janin J (1995) X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 Å resolution. Structure 3:1307-1314.
    • (1995) Structure , vol.3 , pp. 1307-1314
    • Morera, S.1    Lacombe, M.-L.2    Xu, Y.3    Lebras, G.4    Janin, J.5
  • 86
    • 0029795132 scopus 로고    scopus 로고
    • Study of analogues of thymidine-5′-monophosphate and thymidine as substrates or inhibitors of chick embryo liver thymidylate kinase
    • Navé J-F, Neises B & Eschbach A (1996) Study of analogues of thymidine-5′-monophosphate and thymidine as substrates or inhibitors of chick embryo liver thymidylate kinase. Nucleosides and Nucleotides 15:1469-1479.
    • (1996) Nucleosides and Nucleotides , vol.15 , pp. 1469-1479
    • Navé, J.-F.1    Neises, B.2    Eschbach, A.3
  • 87
    • 0343230444 scopus 로고
    • Discrimination of cellular and viral DNA polymerases in retrovirus-infected cells: Principles and applications
    • Ono K (1987) Discrimination of cellular and viral DNA polymerases in retrovirus-infected cells: principles and applications. Bulletin de l'Institut Pasteur 85:3-35.
    • (1987) Bulletin de l'institut Pasteur , vol.85 , pp. 3-35
    • Ono, K.1
  • 88
    • 0031904278 scopus 로고    scopus 로고
    • Mode of action of (1′s,2′R)-9-{[1′,2′-Bis(hydroxymethyl)cycloprop- 1′-yl]methyl}guanine (A-5021) against Herpes simplex virus type 1 and type 2 and varicella-zoster virus
    • Ono N, Iwayama S, Suzuki K, Sekiyama T, Nakazawa H, Tsuji T, Okunishi T, Daikoru T & Nishiyama Y (1998) Mode of action of (1′S,2′R)-9-{[1′,2′-Bis(hydroxymethyl)cycloprop- 1′-yl]methyl}guanine (A-5021) against Herpes simplex virus type 1 and type 2 and varicella-zoster virus. Antimicrobial Agents and Chemotherapy 42:2095-2102.
    • (1998) Antimicrobial Agents and Chemotherapy , vol.42 , pp. 2095-2102
    • Ono, N.1    Iwayama, S.2    Suzuki, K.3    Sekiyama, T.4    Nakazawa, H.5    Tsuji, T.6    Okunishi, T.7    Daikoru, T.8    Nishiyama, Y.9
  • 89
    • 0030045732 scopus 로고    scopus 로고
    • Inhibition of hepatitis B virus by a novel L-nucleoside 2′-fluoro-5-methyl-β-L-arabinofuranosyl uracil
    • Pai SB, Liu S-H, Zhu Y, Chu CK & Cheng Y-C (1996) Inhibition of hepatitis B virus by a novel L-nucleoside 2′-fluoro-5-methyl-β-L-arabinofuranosyl uracil. Antimicrobial Agents and Chemotherapy 40:380-386.
    • (1996) Antimicrobial Agents and Chemotherapy , vol.40 , pp. 380-386
    • Pai, S.B.1    Liu, S.-H.2    Zhu, Y.3    Chu, C.K.4    Cheng, Y.-C.5
  • 90
    • 0026443015 scopus 로고
    • Oxidation of carbovir, a carbocyclic nucleoside, by rat liver cytosolic enzymes
    • Patanella JE & Walsh JS (1992) Oxidation of carbovir, a carbocyclic nucleoside, by rat liver cytosolic enzymes. Drug metabolism Disposition 20:912-919.
    • (1992) Drug Metabolism Disposition , vol.20 , pp. 912-919
    • Patanella, J.E.1    Walsh, J.S.2
  • 91
    • 0030781982 scopus 로고    scopus 로고
    • Enzymatic properties of the unnatural β-L-enantiomers of 2′,3′-dideoxyadenosine and 2′,3′-didehydro-2′,3′-dideoxyadenosine
    • Pelicano H, Pierra C, Eriksson S, Gosselin G, Imbach J-L & Maury G (1997) Enzymatic properties of the unnatural β-L-enantiomers of 2′,3′-dideoxyadenosine and 2′,3′-didehydro-2′,3′-dideoxyadenosine. Journal of Medicinal Chemistry 40:3969-3973.
    • (1997) Journal of Medicinal Chemistry , vol.40 , pp. 3969-3973
    • Pelicano, H.1    Pierra, C.2    Eriksson, S.3    Gosselin, G.4    Imbach, J.-L.5    Maury, G.6
  • 92
    • 85037957722 scopus 로고    scopus 로고
    • Pelicano H, Rittinger K, Gosselin G, Imbach J-L, Sommadossi J-P, Goody RS & Maury G (unpublished results)
    • Pelicano H, Rittinger K, Gosselin G, Imbach J-L, Sommadossi J-P, Goody RS & Maury G (unpublished results).
  • 93
    • 0000946769 scopus 로고
    • Nucleic acid derived allenols: Unusual analogues of nucleosides with antiretroviral activity
    • Phadtare S & Zemlicka J (1989) Nucleic acid derived allenols: Unusual analogues of nucleosides with antiretroviral activity. Journal of the American Chemical Society 111:5925-5931.
    • (1989) Journal of the American Chemical Society , vol.111 , pp. 5925-5931
    • Phadtare, S.1    Zemlicka, J.2
  • 95
    • 0012013712 scopus 로고
    • An introduction to enzyme kinetics
    • Second edition. Oxford: Oxford Science Publications
    • Price NC & Stevens L (1989) An introduction to enzyme kinetics. In Fundamentals of enzymology pp. 136-180. Second edition. Oxford: Oxford Science Publications.
    • (1989) Fundamentals of Enzymology , pp. 136-180
    • Price, N.C.1    Stevens, L.2
  • 97
    • 0027414018 scopus 로고
    • Human immunodeficiency virus reverse transcriptase. A kinetic analysis of RNA-dependent and DNA-dependent DNA polymerisation
    • Reardon JE (1993) Human immunodeficiency virus reverse transcriptase. A kinetic analysis of RNA-dependent and DNA-dependent DNA polymerisation. Journal of Biological Chemistry 268:8743-8751.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 8743-8751
    • Reardon, J.E.1
  • 99
    • 0029150042 scopus 로고
    • Human immunodeficiency virus reverse transcriptase substrate-induced conformational changes and the mechanism of inhibition by nonnucleoside inhibitors
    • Rittinger K, Divita G & Goody RS (1995) Human immunodeficiency virus reverse transcriptase substrate-induced conformational changes and the mechanism of inhibition by nonnucleoside inhibitors. Proceedings of the National Academy of Sciences, USA 92:8046-8049.
    • (1995) Proceedings of the National Academy of Sciences, USA , vol.92 , pp. 8046-8049
    • Rittinger, K.1    Divita, G.2    Goody, R.S.3
  • 101
    • 16044369181 scopus 로고    scopus 로고
    • Inhibition of hepatitis B virus DNA polymerase by enantiomers of penciclovir triphosphate and metabolic basis for selective inhibition of HBV replication by penciclovir
    • Saw T, Mok SS & Locarnini SA (1996) Inhibition of hepatitis B virus DNA polymerase by enantiomers of penciclovir triphosphate and metabolic basis for selective inhibition of HBV replication by penciclovir. Hepatology 24:996-1002.
    • (1996) Hepatology , vol.24 , pp. 996-1002
    • Saw, T.1    Mok, S.S.2    Locarnini, S.A.3
  • 104
    • 0023225120 scopus 로고
    • Resolution of racemic carbocyclic analogues of purine nucleosides through the action of adenosine deaminase. Antiviral activity of the carbocyclic 2′-deoxyguanosine enantiomers
    • Secrist III JA, Montgomery JA, Shealy YF, O'Dell CA & Clayton SJ (1987) Resolution of racemic carbocyclic analogues of purine nucleosides through the action of adenosine deaminase. Antiviral activity of the carbocyclic 2′-deoxyguanosine enantiomers. Journal of Medicinal Chemistry 30:746-749.
    • (1987) Journal of Medicinal Chemistry , vol.30 , pp. 746-749
    • Secrist J.A. III1    Montgomery, J.A.2    Shealy, Y.F.3    O'Dell, C.A.4    Clayton, S.J.5
  • 108
    • 0029031381 scopus 로고
    • Mechanism of inhibition of duck hepatitis B virus polymerase by (-)-β-L-2′,3′-dideoxy-3′-thiacytidine
    • Severini A, Liu XY, Wilson JS & Tyrrell DL (1995) Mechanism of inhibition of duck hepatitis B virus polymerase by (-)-β-L-2′,3′-dideoxy-3′-thiacytidine. Antimicrobial Agents and Chemotherapy 39:1430-1435.
    • (1995) Antimicrobial Agents and Chemotherapy , vol.39 , pp. 1430-1435
    • Severini, A.1    Liu, X.Y.2    Wilson, J.S.3    Tyrrell, D.L.4
  • 112
    • 0027417199 scopus 로고
    • Affinity of the antiviral enantiomers of oxathiolane cytosine nucleosides for human 2′-deoxycytidine kinase
    • Shewach DS, Liotta DC & Schinazi RF (1993) Affinity of the antiviral enantiomers of oxathiolane cytosine nucleosides for human 2′-deoxycytidine kinase. Biochemical Pharmacology 45:1540-1543.
    • (1993) Biochemical Pharmacology , vol.45 , pp. 1540-1543
    • Shewach, D.S.1    Liotta, D.C.2    Schinazi, R.F.3
  • 113
    • 0027431843 scopus 로고
    • Biochemical basis for the differential anti-human immunodeficiency virus activity of two cis enantiomers of dideoxy-3′-thiacytidine
    • Skalski V, Chang C-N, Dutschman G & Cheng Y-C (1993) Biochemical basis for the differential anti-human immunodeficiency virus activity of two cis enantiomers of dideoxy-3′-thiacytidine. Journal of Biological Chemistry 268:23324-23328.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 23324-23328
    • Skalski, V.1    Chang, C.-N.2    Dutschman, G.3    Cheng, Y.-C.4
  • 114
    • 0027407484 scopus 로고
    • Nucleoside analogs: Similarities and differences
    • Sommadossi J-P (1993) Nucleoside analogs: Similarities and differences. Clinical Infectious Diseases 16(Suppl. 1):S7-S15.
    • (1993) Clinical Infectious Diseases , vol.16 , Issue.SUPPL. 1
    • Sommadossi, J.-P.1
  • 115
    • 0029036828 scopus 로고
    • 5-Iodo-2′-deoxy-L-uridine and (E)-5-(2-bromovmyl)-2'-deoxy-L-uridine: Selective phosphorylation by Herpes simplex virus type 1 thymidine kinase, antiherpetic activity and cytotoxicity studies
    • Spadari S, Ciarrocchi G, Focher F, Verri A, Maga G, Arcamone F, Iafrate E, Manzini S & Garbesi A (1995a) 5-Iodo-2′-deoxy-L-uridine and (E)-5-(2-bromovmyl)-2'-deoxy-L-uridine: Selective phosphorylation by Herpes simplex virus type 1 thymidine kinase, antiherpetic activity and cytotoxicity studies. Molecular Pharmacology 47:1231-1238.
    • (1995) Molecular Pharmacology , vol.47 , pp. 1231-1238
    • Spadari, S.1    Ciarrocchi, G.2    Focher, F.3    Verri, A.4    Maga, G.5    Arcamone, F.6    Iafrate, E.7    Manzini, S.8    Garbesi, A.9
  • 117
    • 0029618709 scopus 로고
    • Lack of stereospecificity of some cellular and viral enzymes involved in the synthesis of deoxyribonudeotides and DNA: Molecular basis for the antiviral activity of unnatural L-β-nucleosides
    • Spadari S, Maga G, Verri A, Bendiscioli A, Tondelli L, Capobianco M, Colonna F, Garbesi A & Focher F (1995b) Lack of stereospecificity of some cellular and viral enzymes involved in the synthesis of deoxyribonudeotides and DNA: molecular basis for the antiviral activity of unnatural L-β-nucleosides. Biochimie 77:861-867.
    • (1995) Biochimie , vol.77 , pp. 861-867
    • Spadari, S.1    Maga, G.2    Verri, A.3    Bendiscioli, A.4    Tondelli, L.5    Capobianco, M.6    Colonna, F.7    Garbesi, A.8    Focher, F.9
  • 120
    • 0027456640 scopus 로고
    • The resolution and absolute stereochemistry of the enantiomers of cis-1-2-(hydroxymethyl)-1,3-oxathiolan-5-ylcytosine (BCH189): Equipotent anti-HIV agents
    • Storer R, Clemens IR, Lamont B, Noble SA, Williamson C & Belleau B (1993) The resolution and absolute stereochemistry of the enantiomers of cis-1-2-(hydroxymethyl)-1,3-oxathiolan-5-yl)cytosine (BCH189): Equipotent anti-HIV agents. Nucleosides and Nucleotides 12:225-236.
    • (1993) Nucleosides and Nucleotides , vol.12 , pp. 225-236
    • Storer, R.1    Clemens, I.R.2    Lamont, B.3    Noble, S.A.4    Williamson, C.5    Belleau, B.6
  • 121
    • 0026001583 scopus 로고
    • Inhibition of herpes simplex virus type 1 DNA polymerase by [1R(1a, 2b, 3a)]-9-[2,3-bis(hydroxymethyl)cyclobutyl]guanine
    • Terry BJ, Cianci CW & Hagen ME (1991) Inhibition of herpes simplex virus type 1 DNA polymerase by [1R(1a, 2b, 3a)]-9-[2,3-bis(hydroxymethyl)cyclobutyl]guanine. Molecular Pharmacology 40:591-596.
    • (1991) Molecular Pharmacology , vol.40 , pp. 591-596
    • Terry, B.J.1    Cianci, C.W.2    Hagen, M.E.3
  • 122
    • 0031833635 scopus 로고    scopus 로고
    • Chemo-enzymatic synthesis of a new type of enantiomerically pure carbocyclic nucleoside analogues with strong inhibitory effects on terminal deoxynucleotidyl transferase
    • Theil F, Ballschuh S, Flateau S, von Janta-Lipinski M & Matthes E (1998) Chemo-enzymatic synthesis of a new type of enantiomerically pure carbocyclic nucleoside analogues with strong inhibitory effects on terminal deoxynucleotidyl transferase. Bioorganic and Medicinal Chemistry 6:701-706.
    • (1998) Bioorganic and Medicinal Chemistry , vol.6 , pp. 701-706
    • Theil, F.1    Ballschuh, S.2    Flateau, S.3    Von Janta-Lipinski, M.4    Matthes, E.5
  • 123
    • 0342578188 scopus 로고
    • Structural requirements for enzymatic activation of acyclonucleotide analogues
    • Tolman RL (1989) Structural requirements for enzymatic activation of acyclonucleotide analogues. ACS Symposium Series 401:35-50.
    • (1989) ACS Symposium Series , vol.401 , pp. 35-50
    • Tolman, R.L.1
  • 125
    • 0028086249 scopus 로고
    • Synthesis and biological evaluation of pyrimidine and purine α-L-2′,3′-dideoxy nucleosides
    • Van Draanen NA & Koszalka GW (1994) Synthesis and biological evaluation of pyrimidine and purine α-L-2′,3′-dideoxy nucleosides. Nucleosides and Nucleotides 13:1679-1693.
    • (1994) Nucleosides and Nucleotides , vol.13 , pp. 1679-1693
    • Van Draanen, N.A.1    Koszalka, G.W.2
  • 128
    • 0027511640 scopus 로고
    • Famciclovir and penciclovir. The mode of action of famciclovir including its conversion to penciclovir
    • Vere Hodge R (1993) Famciclovir and penciclovir. The mode of action of famciclovir including its conversion to penciclovir. Antiviral Chemistry and Chemotherapy 4:67-84.
    • (1993) Antiviral Chemistry and Chemotherapy , vol.4 , pp. 67-84
    • Vere Hodge, R.1
  • 130
    • 0027145142 scopus 로고
    • Use of isotopically chiral [4′-C-13]penciclovir and C-13 nmr to determine the specificity and absolute configuration of penciclovir phosphate esters formed in HSV-1 infected and HSV-2 infected cells and by HSV-1 encoded thymidine kinase
    • Vere Hodge RA, Darlison SJ, Earnshaw DL & Readshaw SA (1993) Use of isotopically chiral [4′-C-13]penciclovir and C-13 nmr to determine the specificity and absolute configuration of penciclovir phosphate esters formed in HSV-1 infected and HSV-2 infected cells and by HSV-1 encoded thymidine kinase. Chirality 5:583-588.
    • (1993) Chirality , vol.5 , pp. 583-588
    • Vere Hodge, R.A.1    Darlison, S.J.2    Earnshaw, D.L.3    Readshaw, S.A.4
  • 131
    • 0031028279 scopus 로고    scopus 로고
    • Lack of enantioselectivity of human 2′-deoxycytidine kinase: Relevance for the activation of β-L-deoxycytidine analogs as antineoplastic and antiviral agents
    • Verri A, Focher F, Priori G, Gosselin G, Imbach J-L, Capobianco M, Garbesi A & Spadari S (1997a) Lack of enantioselectivity of human 2′-deoxycytidine kinase: relevance for the activation of β-L-deoxycytidine analogs as antineoplastic and antiviral agents. Molecular Pharmacology 51:132-138.
    • (1997) Molecular Pharmacology , vol.51 , pp. 132-138
    • Verri, A.1    Focher, F.2    Priori, G.3    Gosselin, G.4    Imbach, J.-L.5    Capobianco, M.6    Garbesi, A.7    Spadari, S.8
  • 134
    • 0030664953 scopus 로고    scopus 로고
    • Relaxed enantioselectivity of human mitochondrial thymidine kinase and chemotherapeutic uses of L-nucleoside analogues
    • Verri A, Priori G, Spadari S, Tondelli L & Focher F (1997b) Relaxed enantioselectivity of human mitochondrial thymidine kinase and chemotherapeutic uses of L-nucleoside analogues. Biochemical Journal 328:317-320.
    • (1997) Biochemical Journal , vol.328 , pp. 317-320
    • Verri, A.1    Priori, G.2    Spadari, S.3    Tondelli, L.4    Focher, F.5
  • 135
    • 0032482449 scopus 로고    scopus 로고
    • Newly synthesized L-enantiomers of 3′-fluoro-modified β-2′-deoxyribonucleoside 5′-triphosphates inhibit hepatitis B DNA polymerases but not the five cellular DNA polymerases α, β, γ, δ, and ε nor HIV-1 reverse transcriptase
    • von Janta-Lipinski M, Costisella B, Ochs H, Hübscher U, Hafkemeyer P & Matthes E (1998) Newly synthesized L-enantiomers of 3′-fluoro-modified β-2′-deoxyribonucleoside 5′-triphosphates inhibit hepatitis B DNA polymerases but not the five cellular DNA polymerases α, β, γ, δ, and ε nor HIV-1 reverse transcriptase. Journal of Medicinal Chemistry 41:2040-2046.
    • (1998) Journal of Medicinal Chemistry , vol.41 , pp. 2040-2046
    • Von Janta-Lipinski, M.1    Costisella, B.2    Ochs, H.3    Hübscher, U.4    Hafkemeyer, P.5    Matthes, E.6
  • 136
  • 137
    • 0027494086 scopus 로고
    • A novel mechanism for reverse transcription in hepatitis B viruses
    • Wang G-H & Seeger C (1993) A novel mechanism for reverse transcription in hepatitis B viruses. Journal of Virology 67:6507-6512.
    • (1993) Journal of Virology , vol.67 , pp. 6507-6512
    • Wang, G.-H.1    Seeger, C.2
  • 139
    • 0030586292 scopus 로고    scopus 로고
    • Cloning and expression of human mitochondrial deoxyguanosine kinase cDNA
    • Wang L, Hellman U & Eriksson S (1996) Cloning and expression of human mitochondrial deoxyguanosine kinase cDNA. FEBS Letters 390:39-43.
    • (1996) FEBS Letters , vol.390 , pp. 39-43
    • Wang, L.1    Hellman, U.2    Eriksson, S.3
  • 140
    • 0029020644 scopus 로고
    • The three-dimensional structure of thymid ne kinase from Herpes simplex virus type 1
    • Wild K, Bohner T, Aubry A, Folkers G & Schulz GE (1995) The three-dimensional structure of thymid ne kinase from Herpes simplex virus type 1. FEBS Letters 368:289-292.
    • (1995) FEBS Letters , vol.368 , pp. 289-292
    • Wild, K.1    Bohner, T.2    Aubry, A.3    Folkers, G.4    Schulz, G.E.5
  • 141
    • 0030829025 scopus 로고    scopus 로고
    • The structures of thymidine kinase from Herpes simplex virus type-1 in complex with substrates and a substrate analogue
    • Wild K, BohnerT, Folkers G & Schulz GE (1997) The structures of thymidine kinase from Herpes simplex virus type-1 in complex with substrates and a substrate analogue. Protein Science 6:2097-2106.
    • (1997) Protein Science , vol.6 , pp. 2097-2106
    • Wild, K.1    Folkers, G.2    Schulz, G.E.3
  • 142
    • 0027398949 scopus 로고
    • A pre-transition-state mimic of an enzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water
    • Wilson DK & Quiocho FA (1993) A pre-transition-state mimic of an enzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water. Biochemistry 32:1689-1694.
    • (1993) Biochemistry , vol.32 , pp. 1689-1694
    • Wilson, D.K.1    Quiocho, F.A.2
  • 143
    • 0026434561 scopus 로고
    • Atomic stucture of adenosine deaminase complexed with a transition-state analog: Understanding catalysis and immunodeficiency mutations
    • Wilson DK, Rudolph FB & Quiocho FA (1991) Atomic stucture of adenosine deaminase complexed with a transition-state analog: Understanding catalysis and immunodeficiency mutations. Science 252:1278-1284.
    • (1991) Science , vol.252 , pp. 1278-1284
    • Wilson, D.K.1    Rudolph, F.B.2    Quiocho, F.A.3
  • 145
    • 0000251275 scopus 로고
    • Enzymes in synthetic organic chemistry
    • Edited by Baldwin JE and PD Magnus. Oxford: Elsevier Sciences
    • Wong CH & Whitesides GM (1994) Enzymes in synthetic organic chemistry. In Tetrahedron organic chemistry series, vol.12. Edited by Baldwin JE and PD Magnus. Oxford: Elsevier Sciences, pp. 1-33.
    • (1994) Tetrahedron Organic Chemistry Series , vol.12 , pp. 1-33
    • Wong, C.H.1    Whitesides, G.M.2
  • 146
    • 0030049613 scopus 로고    scopus 로고
    • Cytidine deaminase complexed to 3-deazacytidine: A "valence buffer" in zinc enzyme catalysis
    • Xiang S, Short SA, Wolfenden R & Carter Jr CW (1996) Cytidine deaminase complexed to 3-deazacytidine: A "valence buffer" in zinc enzyme catalysis. Biochemistry 35:1335-1341.
    • (1996) Biochemistry , vol.35 , pp. 1335-1341
    • Xiang, S.1    Short, S.A.2    Wolfenden, R.3    Carter C.W., Jr.4
  • 147
    • 0030887895 scopus 로고    scopus 로고
    • The structure of the cytidine deaminase-product complex provides evidences for efficient proton transfer and ground-state destabilization
    • Xiang S, Short SA, Wolfenden R & Carter Jr. CW (1997) The structure of the cytidine deaminase-product complex provides evidences for efficient proton transfer and ground-state destabilization. Biochemistry 36:4768-4774.
    • (1997) Biochemistry , vol.36 , pp. 4768-4774
    • Xiang, S.1    Short, S.A.2    Wolfenden, R.3    Carter C.W., Jr.4
  • 148
    • 0028207542 scopus 로고
    • Chiral discrimination of enantiomeric 2′-deoxythymidine 5′-triphosphate by HIV-1 reverse transcriptase and eukaryotic DNA polymerases
    • Yamaguchi T, Iwanami N, Shudo K & Saneyoshi M (1994) Chiral discrimination of enantiomeric 2′-deoxythymidine 5′-triphosphate by HIV-1 reverse transcriptase and eukaryotic DNA polymerases. Biochemical and Biophysical Research Communications 200:1023-1027.
    • (1994) Biochemical and Biophysical Research Communications , vol.200 , pp. 1023-1027
    • Yamaguchi, T.1    Iwanami, N.2    Shudo, K.3    Saneyoshi, M.4
  • 149
    • 0029940584 scopus 로고    scopus 로고
    • Inhibition of Epstein-Barr virus replication by a novel L-nucleoside, 2′-fluoro-5-methyl-β-L-arabinofuranosyluracil
    • Yao G-Q, Liu S-H, Chou E, Kukhanova M, Chu CK & Cheng Y-C (1996) Inhibition of Epstein-Barr virus replication by a novel L-nucleoside, 2′-fluoro-5-methyl-β-L-arabinofuranosyluracil. Biochemical Pharmacology 51:941-947.
    • (1996) Biochemical Pharmacology , vol.51 , pp. 941-947
    • Yao, G.-Q.1    Liu, S.-H.2    Chou, E.3    Kukhanova, M.4    Chu, C.K.5    Cheng, Y.-C.6
  • 150
    • 0031808360 scopus 로고    scopus 로고
    • Anti-hepatitis B virus activity and metabolism of 2′,3′-dideoxy2′,3′-didehydro-β-L(-)-5- fluorocytidine
    • Zhu Y, Dutschman GE, Liu S, Bridges EG & Cheng Y-C (1998) Anti-hepatitis B virus activity and metabolism of 2′,3′-dideoxy2′,3′-didehydro-β-L(-)-5- fluorocytidine. Antimicrobial Agents and Chemotherapy 42:1805-1810.
    • (1998) Antimicrobial Agents and Chemotherapy , vol.42 , pp. 1805-1810
    • Zhu, Y.1    Dutschman, G.E.2    Liu, S.3    Bridges, E.G.4    Cheng, Y.-C.5
  • 151
    • 0030032079 scopus 로고    scopus 로고
    • 2′,3′-dideoxy-β-L-fluorocytidine inhibits duck hepatitis B virus reverse transcription and suppresses viral DNA synthesis in hepatocytes, both in vitro and in vivo
    • Zoulim F, Dannaoui E, Borel C, Hantz O, Lin T-S, Liu S-H, Trepo C & Cheng Y-C (1996) 2′,3′-Dideoxy-β-L-fluorocytidine inhibits duck hepatitis B virus reverse transcription and suppresses viral DNA synthesis in hepatocytes, both in vitro and in vivo. Antimicrobial Agents and Chemotherapy 40:448-453.
    • (1996) Antimicrobial Agents and Chemotherapy , vol.40 , pp. 448-453
    • Zoulim, F.1    Dannaoui, E.2    Borel, C.3    Hantz, O.4    Lin, T.-S.5    Liu, S.-H.6    Trepo, C.7    Cheng, Y.-C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.