메뉴 건너뛰기




Volumn 86, Issue 1, 2010, Pages 101-120

Human and viral nucleoside/nucleotide kinases involved in antiviral drug activation: Structural and catalytic properties

Author keywords

Adenylate kinase; Brivudin; Bromovinyldeoxyuridine; Deoxycytidine kinase; Deoxyguanosine kinase; Ganciclovir; Herpes simplex virus; Lamivudine; Nm23; Nucleoside diphosphate kinase; Phosphoglycerate kinase; Telbivudine; Tenofovir; Thymidine kinase; Thymidylate kinase; Vaccinia virus

Indexed keywords

5 (2 BROMOVINYL) 2' DEOXYURIDINE; ACICLOVIR; ADEFOVIR; ADENYLATE KINASE; ANTIVIRUS AGENT; CIDOFOVIR; DEOXYGUANOSINE KINASE; DNA POLYMERASE; GANCICLOVIR; GUANYLATE KINASE; IDOXURIDINE; LAMIVUDINE; NUCLEOSIDE DIPHOSPHATE KINASE; PHOSPHOGLYCERATE KINASE; STAVUDINE; TELBIVUDINE; TENOFOVIR DISOPROXIL; THYMIDINE KINASE; THYMIDYLATE SYNTHASE; URIDINE PHOSPHATE; ZIDOVUDINE;

EID: 77952263334     PISSN: 01663542     EISSN: 18729096     Source Type: Journal    
DOI: 10.1016/j.antiviral.2010.02.001     Document Type: Review
Times cited : (103)

References (207)
  • 1
    • 36148979311 scopus 로고    scopus 로고
    • NMR identification of transient complexes critical to adenylate kinase catalysis
    • Aden J., Wolf-Watz M. NMR identification of transient complexes critical to adenylate kinase catalysis. J. Am. Chem. Sci. 2007, 1219:14003-14012.
    • (2007) J. Am. Chem. Sci. , vol.1219 , pp. 14003-14012
    • Aden, J.1    Wolf-Watz, M.2
  • 3
    • 77950842908 scopus 로고    scopus 로고
    • Plakoglobin interacts with and increases the protein levels of metastasis suppressor Nm23-H2 and regulates the expression of Nm23-H1
    • January 25 [Epub ahead of print]
    • Aktary Z., Chapman K., Lam L., Lo A., Ji C., Graham K., Cook L., Li L., Mackey J.R., Pasdar M. Plakoglobin interacts with and increases the protein levels of metastasis suppressor Nm23-H2 and regulates the expression of Nm23-H1. Oncogene 2010, January 25 [Epub ahead of print].
    • (2010) Oncogene
    • Aktary, Z.1    Chapman, K.2    Lam, L.3    Lo, A.4    Ji, C.5    Graham, K.6    Cook, L.7    Li, L.8    Mackey, J.R.9    Pasdar, M.10
  • 5
    • 74649083314 scopus 로고    scopus 로고
    • Fusion enzymes containing HSV1-thymidine kinase mutants and guanylate kinase enhance prodrug senitivity in vitro and in vivo
    • Ardiani A., Sanchez-Bonilla M., Black M.E. Fusion enzymes containing HSV1-thymidine kinase mutants and guanylate kinase enhance prodrug senitivity in vitro and in vivo. Cancer Gene Ther. 2009, 17:86-96.
    • (2009) Cancer Gene Ther. , vol.17 , pp. 86-96
    • Ardiani, A.1    Sanchez-Bonilla, M.2    Black, M.E.3
  • 6
    • 0029162556 scopus 로고
    • Mammalian deoxyribonucleoside kinases
    • Arner E.S.J., Eriksson S. Mammalian deoxyribonucleoside kinases. Pharmacol. Ther. 1995, 67:155-186.
    • (1995) Pharmacol. Ther. , vol.67 , pp. 155-186
    • Arner, E.S.J.1    Eriksson, S.2
  • 8
    • 0027480081 scopus 로고
    • Differential mechanism of cytostatic effect of [E]-5-(2-bromovinyl)-2′-deoxyuridine, 9-(1,3-dihydroxy-2-propoxymethyl)guanine, and other antiherpetic drugs on tumor cells transfected by the thymidine kinase gene of herpes simplex virus type 1 or type2
    • Balzarini J., Bohman C., De Clercq E. Differential mechanism of cytostatic effect of [E]-5-(2-bromovinyl)-2′-deoxyuridine, 9-(1,3-dihydroxy-2-propoxymethyl)guanine, and other antiherpetic drugs on tumor cells transfected by the thymidine kinase gene of herpes simplex virus type 1 or type2. J. Biol. Chem. 1993, 268:6332-6337.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6332-6337
    • Balzarini, J.1    Bohman, C.2    De Clercq, E.3
  • 9
    • 0021843802 scopus 로고
    • Murine mammary FM3A carcinome cells transformed with the herpes simplex virus type 1 thymidine kinase gene are highly sensitive to the growth-inhibitory properties of (E)-5-(2-bromovinyl)-2′-deoxyuridine and related compounds
    • Balzarini J., De Clercq E., Ayusawa D., Seno T. Murine mammary FM3A carcinome cells transformed with the herpes simplex virus type 1 thymidine kinase gene are highly sensitive to the growth-inhibitory properties of (E)-5-(2-bromovinyl)-2′-deoxyuridine and related compounds. FEBS Lett. 1985, 185:95-100.
    • (1985) FEBS Lett. , vol.185 , pp. 95-100
    • Balzarini, J.1    De Clercq, E.2    Ayusawa, D.3    Seno, T.4
  • 10
    • 0026020310 scopus 로고
    • Intracellular metabolism and mechanism of anti-retrovirus action of 9-(2-phosphonylmethoxyethyl)adenine, a potent anti-human immunodeficiency virus compound
    • Balzarini J., Hao Z., Herdewijn P., Johns D.G., De Clercq E. Intracellular metabolism and mechanism of anti-retrovirus action of 9-(2-phosphonylmethoxyethyl)adenine, a potent anti-human immunodeficiency virus compound. Proc. Natl. Acad. Sci. U.S.A. 1991, 88:1499-1503.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 1499-1503
    • Balzarini, J.1    Hao, Z.2    Herdewijn, P.3    Johns, D.G.4    De Clercq, E.5
  • 11
    • 0037150096 scopus 로고    scopus 로고
    • The A167Y mutation converts the herpes simplex virus type 1 thymidine kinase into a guanosine analogue kinase
    • Balzarini J., Liekens S., Esnouf R., De Clercq E. The A167Y mutation converts the herpes simplex virus type 1 thymidine kinase into a guanosine analogue kinase. Biochemistry 2002, 41:6517-6524.
    • (2002) Biochemistry , vol.41 , pp. 6517-6524
    • Balzarini, J.1    Liekens, S.2    Esnouf, R.3    De Clercq, E.4
  • 12
    • 33745834321 scopus 로고    scopus 로고
    • Engineering of a single conserved amino acid residue of herpes simplex virus type 1 thymidine kinase allows a predominant shift from pyrimidine to purine nucleoside phosphorylation
    • Balzarini J., Liekens S., Solaroli N., El Omari K., Stammers D.K., Karlsson A. Engineering of a single conserved amino acid residue of herpes simplex virus type 1 thymidine kinase allows a predominant shift from pyrimidine to purine nucleoside phosphorylation. J. Biol. Chem. 2006, 281:19273-19279.
    • (2006) J. Biol. Chem. , vol.281 , pp. 19273-19279
    • Balzarini, J.1    Liekens, S.2    Solaroli, N.3    El Omari, K.4    Stammers, D.K.5    Karlsson, A.6
  • 13
    • 0037045009 scopus 로고    scopus 로고
    • Metabolic activation of nucleoside and nucleotide reverse transcriptase inhibitors in dendritic and Langerhans cells
    • Balzarini J., Van Herrewege Y., Vanham G. Metabolic activation of nucleoside and nucleotide reverse transcriptase inhibitors in dendritic and Langerhans cells. AIDS 2002, 16:2159-2163.
    • (2002) AIDS , vol.16 , pp. 2159-2163
    • Balzarini, J.1    Van Herrewege, Y.2    Vanham, G.3
  • 14
    • 0034306265 scopus 로고    scopus 로고
    • Novel ribofuranosylnucleoside lead compounds for potent and selective inhibitors of mitochondrial thymidine kinase-2
    • Balzarini J., Zhu C., De Clercq E., Pérez-Pérez M.-J., Chamorro C., Camarasa M.-J., Karlsson A. Novel ribofuranosylnucleoside lead compounds for potent and selective inhibitors of mitochondrial thymidine kinase-2. Biochem. J. 2000, 351:167-171.
    • (2000) Biochem. J. , vol.351 , pp. 167-171
    • Balzarini, J.1    Zhu, C.2    De Clercq, E.3    Pérez-Pérez, M.-J.4    Chamorro, C.5    Camarasa, M.-J.6    Karlsson, A.7
  • 16
    • 0348224028 scopus 로고    scopus 로고
    • Tight binding of deoxyribonucleoside triphosphates to human thymidine kinase 2 expressed in E. coli. Purification and partial purification to its dimeric and tetrameric forms
    • Barroso J.F., Elholm M., Flatmark T. Tight binding of deoxyribonucleoside triphosphates to human thymidine kinase 2 expressed in E. coli. Purification and partial purification to its dimeric and tetrameric forms. Biochemistry 2003, 42:15158-15169.
    • (2003) Biochemistry , vol.42 , pp. 15158-15169
    • Barroso, J.F.1    Elholm, M.2    Flatmark, T.3
  • 18
    • 48849089984 scopus 로고    scopus 로고
    • Nucleoside diphosphate kinase B (NDPKB) scaffolds endoplamic reticulum membranes in vitro
    • Baughman C., Morin-Leisk J., Lee T. Nucleoside diphosphate kinase B (NDPKB) scaffolds endoplamic reticulum membranes in vitro. Exp. Cell Res. 2008, 314:2702-2714.
    • (2008) Exp. Cell Res. , vol.314 , pp. 2702-2714
    • Baughman, C.1    Morin-Leisk, J.2    Lee, T.3
  • 19
    • 70349108450 scopus 로고    scopus 로고
    • Glucuronidation of the antiretroviral drug efavirenz by UGT2B7 and in vitro investigation of drug-drug interaction with zidovudine
    • Belanger A.S., Caron P., Harvey M., Zimmerman P.A., Mehlotra R.K., Guillemette C. Glucuronidation of the antiretroviral drug efavirenz by UGT2B7 and in vitro investigation of drug-drug interaction with zidovudine. Drug Metab. Dispos. 2009, 37:1793-1796.
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 1793-1796
    • Belanger, A.S.1    Caron, P.2    Harvey, M.3    Zimmerman, P.A.4    Mehlotra, R.K.5    Guillemette, C.6
  • 20
    • 77956945325 scopus 로고
    • Chemical basis of biological phosphoryl transfer
    • Academic Press, New York
    • Benkovic S.J., Schray K.J. Chemical basis of biological phosphoryl transfer. The Enzymes 1968, vol. 8:201-238. Academic Press, New York.
    • (1968) The Enzymes , vol.8 , pp. 201-238
    • Benkovic, S.J.1    Schray, K.J.2
  • 21
    • 0011822891 scopus 로고
    • Enzymatic phosphorylation of nucleoside diphosphates
    • Berg P., Joklik W.K. Enzymatic phosphorylation of nucleoside diphosphates. J. Biol. Chem. 1954, 210:657-672.
    • (1954) J. Biol. Chem. , vol.210 , pp. 657-672
    • Berg, P.1    Joklik, W.K.2
  • 25
    • 33747141729 scopus 로고    scopus 로고
    • Antiviral drugs for cytomegalovirus diseases
    • Biron K.K. Antiviral drugs for cytomegalovirus diseases. Antiviral Res. 2006, 71:154-163.
    • (2006) Antiviral Res. , vol.71 , pp. 154-163
    • Biron, K.K.1
  • 27
    • 0035300565 scopus 로고    scopus 로고
    • Herpes simplex virus-1 thymidine kinase mutants created by semi-random sequence mutagenesis improve prodrug-mediated tumor cell killing
    • Black M.E., Kokoris M.S., Sabo P. Herpes simplex virus-1 thymidine kinase mutants created by semi-random sequence mutagenesis improve prodrug-mediated tumor cell killing. Cancer Res. 2001, 61:3022-3026.
    • (2001) Cancer Res. , vol.61 , pp. 3022-3026
    • Black, M.E.1    Kokoris, M.S.2    Sabo, P.3
  • 28
    • 0029883624 scopus 로고    scopus 로고
    • Creation of drug-specific herpes simplex virus type 1 thymidine kinase mutants for gene therapy
    • Black M.E., Newcomb T.G., Wilson H.M., Loeb L.A. Creation of drug-specific herpes simplex virus type 1 thymidine kinase mutants for gene therapy. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:3525-3529.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 3525-3529
    • Black, M.E.1    Newcomb, T.G.2    Wilson, H.M.3    Loeb, L.A.4
  • 29
    • 0028291887 scopus 로고
    • Improved spectrophotometric assay of nucleoside monophosphate kinase activity using the pyruvate kinase/lactate dehydrogenase coupling system
    • Blondin C., Serina L., Wiesmuller L., Gilles A.-M., Barzu O. Improved spectrophotometric assay of nucleoside monophosphate kinase activity using the pyruvate kinase/lactate dehydrogenase coupling system. Anal. Biochem. 1994, 220:219-221.
    • (1994) Anal. Biochem. , vol.220 , pp. 219-221
    • Blondin, C.1    Serina, L.2    Wiesmuller, L.3    Gilles, A.-M.4    Barzu, O.5
  • 30
    • 0021739206 scopus 로고
    • Phosphorylation of the antiviral precursor 9-(1,3-dihydroxy-2-propoxymethyl)guanine monophosphate by guanylate kinase isozymes
    • Boehme R. Phosphorylation of the antiviral precursor 9-(1,3-dihydroxy-2-propoxymethyl)guanine monophosphate by guanylate kinase isozymes. J. Biol. Chem. 1984, 259:12346-12349.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12346-12349
    • Boehme, R.1
  • 33
    • 68649100167 scopus 로고    scopus 로고
    • Recent progress in gene-directed enzyme prodrug therapy: an emerging cancer treatment
    • Both G.W. Recent progress in gene-directed enzyme prodrug therapy: an emerging cancer treatment. Curr. Opin. Mol. Ther. 2009, 4:421-432.
    • (2009) Curr. Opin. Mol. Ther. , vol.4 , pp. 421-432
    • Both, G.W.1
  • 39
    • 80855134713 scopus 로고    scopus 로고
    • The role of herpes simplex virus-1 thymidine kinase alanine 168 in substrate specificity
    • Candice L.W., Django S., Black M.E. The role of herpes simplex virus-1 thymidine kinase alanine 168 in substrate specificity. Open Biochem. J. 2008, 2:60-66.
    • (2008) Open Biochem. J. , vol.2 , pp. 60-66
    • Candice, L.W.1    Django, S.2    Black, M.E.3
  • 40
    • 0018264671 scopus 로고
    • Association of thymidylate kinase activity with pyrimidine deoxyribonucleoside kinase induced by herpes simplex virus
    • Chen M.S., Prusoff W. Association of thymidylate kinase activity with pyrimidine deoxyribonucleoside kinase induced by herpes simplex virus. J. Biol. Chem. 1978, 235:1325-1327.
    • (1978) J. Biol. Chem. , vol.235 , pp. 1325-1327
    • Chen, M.S.1    Prusoff, W.2
  • 41
    • 0041825376 scopus 로고    scopus 로고
    • Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to proteine kinases
    • Chen Y., Gallois-Montbrun S., Schneider B., Veron M., Morera S., Deville-Bonne D., Janin J. Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to proteine kinases. J. Mol. Biol. 2003, 332:915-926.
    • (2003) J. Mol. Biol. , vol.332 , pp. 915-926
    • Chen, Y.1    Gallois-Montbrun, S.2    Schneider, B.3    Veron, M.4    Morera, S.5    Deville-Bonne, D.6    Janin, J.7
  • 43
    • 48949120865 scopus 로고    scopus 로고
    • Identification of a putative human mitochondrial thymidine monophosphate kinase associated with monocytic/macrophage terminal differenciation
    • Chen Y.L., Lin D.W., Chang Z.F. Identification of a putative human mitochondrial thymidine monophosphate kinase associated with monocytic/macrophage terminal differenciation. Genes Cells 2008, 13:679-689.
    • (2008) Genes Cells , vol.13 , pp. 679-689
    • Chen, Y.L.1    Lin, D.W.2    Chang, Z.F.3
  • 44
    • 0034804684 scopus 로고    scopus 로고
    • L-Nucleoside analogues against cancer-causing viruses have potential in the prevention, delayed onset and treatment of viral associated cancers
    • Cheng Y.-C. l-Nucleoside analogues against cancer-causing viruses have potential in the prevention, delayed onset and treatment of viral associated cancers. Antiviral Chem. Chemother. 2001, 12(Suppl. 1):5-11.
    • (2001) Antiviral Chem. Chemother. , vol.12 , Issue.1 SUPPL. , pp. 5-11
    • Cheng, Y.-C.1
  • 45
    • 0019413792 scopus 로고
    • Differential affinities of 5-(2-halogenovinyl)-2′-deoxyuridines for deoxythymidine kinases of various origins
    • Cheng Y.C., Dutschman G., De Clercq E., Jones A.S., Rahim S.G., Verhelst G., Walker R.T. Differential affinities of 5-(2-halogenovinyl)-2′-deoxyuridines for deoxythymidine kinases of various origins. Mol. Pharmacol. 1981, 20:230-233.
    • (1981) Mol. Pharmacol. , vol.20 , pp. 230-233
    • Cheng, Y.C.1    Dutschman, G.2    De Clercq, E.3    Jones, A.S.4    Rahim, S.G.5    Verhelst, G.6    Walker, R.T.7
  • 46
    • 0033037012 scopus 로고    scopus 로고
    • Directed evolution of thymidine kinase for AZT phosphorylation using DNA family shuffling
    • Christians F.C., Scapozza L., Crameri A., Folkers G., Stemmer W.P.C. Directed evolution of thymidine kinase for AZT phosphorylation using DNA family shuffling. Nat. Biotechnol. 1999, 17:259-264.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 259-264
    • Christians, F.C.1    Scapozza, L.2    Crameri, A.3    Folkers, G.4    Stemmer, W.P.C.5
  • 47
    • 0030480275 scopus 로고    scopus 로고
    • Identification of enzymes catalyzing two-step phosphorylation of cidofovir and the effect of cytomegalovirus infection on their activities in host cells
    • Cihlar T., Chen M.S. Identification of enzymes catalyzing two-step phosphorylation of cidofovir and the effect of cytomegalovirus infection on their activities in host cells. Mol. Pharmacol. 1996, 50:1502-1510.
    • (1996) Mol. Pharmacol. , vol.50 , pp. 1502-1510
    • Cihlar, T.1    Chen, M.S.2
  • 48
    • 0037394125 scopus 로고    scopus 로고
    • Antiherpesvirus drugs: a promising spectrum of new drugs and drug targets
    • Coen D.M., Schaffer P.A. Antiherpesvirus drugs: a promising spectrum of new drugs and drug targets. Nat. Rev. Drug Discov. 2003, 2:278-288.
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 278-288
    • Coen, D.M.1    Schaffer, P.A.2
  • 49
    • 0026772206 scopus 로고
    • In vivo gene transfer with retroviral vector-producer cells for treatment of experimental brain tumors
    • Culver K.W., Ram Z., Wallbridge S., Ishii H., Oldfield E.H., Blaese R.M. In vivo gene transfer with retroviral vector-producer cells for treatment of experimental brain tumors. Science 1992, 256:1550-1552.
    • (1992) Science , vol.256 , pp. 1550-1552
    • Culver, K.W.1    Ram, Z.2    Wallbridge, S.3    Ishii, H.4    Oldfield, E.H.5    Blaese, R.M.6
  • 50
    • 7544248773 scopus 로고    scopus 로고
    • Discovery and development of BVDU (brivudin) as a therapeutic for the treatment of herpes zoster
    • De Clercq E. Discovery and development of BVDU (brivudin) as a therapeutic for the treatment of herpes zoster. Biochem. Pharmacol. 2004, 68:2301-2315.
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 2301-2315
    • De Clercq, E.1
  • 51
    • 27844455955 scopus 로고    scopus 로고
    • Acyclic nucleoside phosphonates: a key class of antiviral drugs
    • De Clercq E., Holy A. Acyclic nucleoside phosphonates: a key class of antiviral drugs. Nat. Rev. Drug Discov. 2005, 4:928-940.
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 928-940
    • De Clercq, E.1    Holy, A.2
  • 52
    • 4444250212 scopus 로고    scopus 로고
    • Therapeutic potential of nucleoside/nucleotide analogues againt poxvirus infections
    • De Clercq E., Neyts J. Therapeutic potential of nucleoside/nucleotide analogues againt poxvirus infections. Rev. Med. Virol. 2004, 14:289-300.
    • (2004) Rev. Med. Virol. , vol.14 , pp. 289-300
    • De Clercq, E.1    Neyts, J.2
  • 53
    • 0033664250 scopus 로고    scopus 로고
    • Selective abolishment of pyrimidine nucleoside kinase activity of herpes simplex virus type 1 thymidine kinase by mutation of alanine 167 to tyrosine
    • Degrève B., Esnouf R., De Clercq E., Balzarini J. Selective abolishment of pyrimidine nucleoside kinase activity of herpes simplex virus type 1 thymidine kinase by mutation of alanine 167 to tyrosine. Mol. Pharmacol. 2000, 58:1326-1332.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1326-1332
    • Degrève, B.1    Esnouf, R.2    De Clercq, E.3    Balzarini, J.4
  • 56
    • 13544271167 scopus 로고    scopus 로고
    • Mechanistic insights into the suppression of drug resistance by human immunodeficiency virus type 1 reverse transcriptase using alpha-boranophosphate nucleoside analogs
    • Deval J., Alvarez K., Selmi B., Bermond M., Boretto J., Guerreiro C., Mulard L., Canard L. Mechanistic insights into the suppression of drug resistance by human immunodeficiency virus type 1 reverse transcriptase using alpha-boranophosphate nucleoside analogs. J. Biol. Chem. 2005, 280:3838-3846.
    • (2005) J. Biol. Chem. , vol.280 , pp. 3838-3846
    • Deval, J.1    Alvarez, K.2    Selmi, B.3    Bermond, M.4    Boretto, J.5    Guerreiro, C.6    Mulard, L.7    Canard, L.8
  • 57
    • 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., Véron M. Phosphorylation of nucleoside diphosphate kinase at the active site studied by steady-state and time-resolved fluorescence. Biochemistry 1996, 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    Véron, M.6
  • 59
    • 21844468220 scopus 로고    scopus 로고
    • Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis
    • Dombrauckas J.D., Santarsiero B.D., Mesecar A.D. Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis. Biochemistry 2005, 44:9417-9423.
    • (2005) Biochemistry , vol.44 , pp. 9417-9423
    • Dombrauckas, J.D.1    Santarsiero, B.D.2    Mesecar, A.D.3
  • 61
    • 0030795311 scopus 로고    scopus 로고
    • Metabolism and activities of 3′-azido-2′,3′-dideoxythymidine and 2′,3′-didehydro-2′,3′-dideoxythymidine in herpesvirus thymidine kinase transduced T-lymphocytes
    • Drake R.R., Mcmasters R., Krisa S., Hume S.D., Rechtin T.M., Saylors R.L., Chiang Y., Govindarajan R., Munshi N. Metabolism and activities of 3′-azido-2′,3′-dideoxythymidine and 2′,3′-didehydro-2′,3′-dideoxythymidine in herpesvirus thymidine kinase transduced T-lymphocytes. Antiviral Res. 1997, 35:177-185.
    • (1997) Antiviral Res. , vol.35 , pp. 177-185
    • Drake, R.R.1    Mcmasters, R.2    Krisa, S.3    Hume, S.D.4    Rechtin, T.M.5    Saylors, R.L.6    Chiang, Y.7    Govindarajan, R.8    Munshi, N.9
  • 62
    • 33750999341 scopus 로고    scopus 로고
    • Structure of vaccinia virus thymidine kinase in complex with dTTP: insights for drug design
    • El Omari K., Solaroli N., Karlsson A., Balzarini J., Stammers D.K. Structure of vaccinia virus thymidine kinase in complex with dTTP: insights for drug design. BMC Struct. Biol. 2006, 6:22-31.
    • (2006) BMC Struct. Biol. , vol.6 , pp. 22-31
    • El Omari, K.1    Solaroli, N.2    Karlsson, A.3    Balzarini, J.4    Stammers, D.K.5
  • 66
    • 35948991804 scopus 로고    scopus 로고
    • In vitro suppression of K65R reverse transcritase-mediated tenofovir- and adefovir-5′-diphosphate resistance conferred by the boranophosphonate derivatives
    • Frangeul A., Barral K., Alvarez K., Canard B. In vitro suppression of K65R reverse transcritase-mediated tenofovir- and adefovir-5′-diphosphate resistance conferred by the boranophosphonate derivatives. Antimicrob. Agents Chemother. 2007, 51:3162-3167.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 3162-3167
    • Frangeul, A.1    Barral, K.2    Alvarez, K.3    Canard, B.4
  • 69
    • 0020066676 scopus 로고
    • Differential phosphorylation of (E)-5-(2-bromovinyl)-2′-deoxyuridine monophosphate by thymidylate kinases from herpes simplex viruses types 1 and 2 and varicella zoster virus
    • Fyfe J.A. Differential phosphorylation of (E)-5-(2-bromovinyl)-2′-deoxyuridine monophosphate by thymidylate kinases from herpes simplex viruses types 1 and 2 and varicella zoster virus. Mol. Pharmacol. 1982, 21:432-437.
    • (1982) Mol. Pharmacol. , vol.21 , pp. 432-437
    • Fyfe, J.A.1
  • 70
    • 0018251481 scopus 로고
    • Thymidine kinase from herpes simplex virus phosphorylates the new antiviral compound, 9-(2-hydroxyethoxymethyl)guanine
    • Fyfe J.A., Keller P.M., Furman P.A., Miller R.L., Elion G.B. Thymidine kinase from herpes simplex virus phosphorylates the new antiviral compound, 9-(2-hydroxyethoxymethyl)guanine. J. Biol. Chem. 1978, 253:8721-8727.
    • (1978) J. Biol. Chem. , vol.253 , pp. 8721-8727
    • Fyfe, J.A.1    Keller, P.M.2    Furman, P.A.3    Miller, R.L.4    Elion, G.B.5
  • 74
    • 2642535305 scopus 로고    scopus 로고
    • Resistance to gemcitabine in a human lymphoma cell line is due to partial deletion of the deoxycytidine kinase gene
    • Galmarini C.M., Clarke M.L., Jordheim L., Santos C.L., Cros E., Mackey J.R., Dumontet C. Resistance to gemcitabine in a human lymphoma cell line is due to partial deletion of the deoxycytidine kinase gene. BMC Pharmacol. 2004, 4:8.
    • (2004) BMC Pharmacol. , vol.4 , pp. 8
    • Galmarini, C.M.1    Clarke, M.L.2    Jordheim, L.3    Santos, C.L.4    Cros, E.5    Mackey, J.R.6    Dumontet, C.7
  • 75
    • 0014473526 scopus 로고
    • Kinetic studies of yeast nucleoside diphosphate kinase
    • Garces E., Cleland W.W. Kinetic studies of yeast nucleoside diphosphate kinase. Biochemistry 1969, 8:633-640.
    • (1969) Biochemistry , vol.8 , pp. 633-640
    • Garces, E.1    Cleland, W.W.2
  • 76
    • 0141594761 scopus 로고    scopus 로고
    • Structural basis for the dual thymidine and thymidylate kinase activity of herpes thymidine kinases
    • Gardberg A., Shuvalova L., Monnerjahn C., Konrad M., Lavie A. Structural basis for the dual thymidine and thymidylate kinase activity of herpes thymidine kinases. Structure 2003, 11:1265-1277.
    • (2003) Structure , vol.11 , pp. 1265-1277
    • Gardberg, A.1    Shuvalova, L.2    Monnerjahn, C.3    Konrad, M.4    Lavie, A.5
  • 77
    • 42249114000 scopus 로고    scopus 로고
    • MAGUK proteins: new targets for pharmacological intervention in the glutamatergic synapse
    • Gardoni F. MAGUK proteins: new targets for pharmacological intervention in the glutamatergic synapse. Eur. J. Pharmacol. 2008, 585:147-152.
    • (2008) Eur. J. Pharmacol. , vol.585 , pp. 147-152
    • Gardoni, F.1
  • 78
    • 0032738846 scopus 로고    scopus 로고
    • Low enantioselectiviies of human deoxycytidine kinase and human deoxyguanosine kinase with respect to 2′-deoxyadenosine,2′-deoxyguanosine and their analogs
    • Gaubert G., Gosselin G., Boudou V., Imbach J.L., Eriksson S., Maury G. Low enantioselectiviies of human deoxycytidine kinase and human deoxyguanosine kinase with respect to 2′-deoxyadenosine,2′-deoxyguanosine and their analogs. Biochimie 1999, 81:1041-1047.
    • (1999) Biochimie , vol.81 , pp. 1041-1047
    • Gaubert, G.1    Gosselin, G.2    Boudou, V.3    Imbach, J.L.4    Eriksson, S.5    Maury, G.6
  • 79
    • 0033774619 scopus 로고    scopus 로고
    • Analysis of large libraries of protein mutants using flow cytometry
    • Georgiou G. Analysis of large libraries of protein mutants using flow cytometry. Adv. Protein Chem. 2000, 55:293-315.
    • (2000) Adv. Protein Chem. , vol.55 , pp. 293-315
    • Georgiou, G.1
  • 80
    • 34249939115 scopus 로고    scopus 로고
    • Non-homologous recombinaison of deoxyribonucleoside kinases from human and Drosophila melanogaster yields human-like enzymes with novel activities
    • Gerth M.L., Lutz S. Non-homologous recombinaison of deoxyribonucleoside kinases from human and Drosophila melanogaster yields human-like enzymes with novel activities. J. Mol. Biol. 2007, 370:742-751.
    • (2007) J. Mol. Biol. , vol.370 , pp. 742-751
    • Gerth, M.L.1    Lutz, S.2
  • 81
    • 0025914104 scopus 로고
    • Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme
    • Gilles A.M., Presecan E., Vonica A., Lascu I. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J. Biol. Chem. 1991, 266:8784-8789.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8784-8789
    • Gilles, A.M.1    Presecan, E.2    Vonica, A.3    Lascu, I.4
  • 83
    • 0033151762 scopus 로고    scopus 로고
    • Catalytic mechanism of nucleoside diphosphate kinase investigated using nucleotide analogues, viscosity effects and X-ray crystallography
    • Gonin P., Xu Y., Milon L., Dabernat S., Morr M., Kumar R., Lacombe M.-L., Janin J., Lascu I. Catalytic mechanism of nucleoside diphosphate kinase investigated using nucleotide analogues, viscosity effects and X-ray crystallography. Biochemistry 1999, 38:7265-7272.
    • (1999) Biochemistry , vol.38 , pp. 7265-7272
    • Gonin, P.1    Xu, Y.2    Milon, L.3    Dabernat, S.4    Morr, M.5    Kumar, R.6    Lacombe, M.-L.7    Janin, J.8    Lascu, I.9
  • 84
    • 0031724984 scopus 로고    scopus 로고
    • The Epstein-Barr virus thymidine kinase does not phosphorylate ganciclovir or acyclovir and demonstrates a narrow substrate specificity compared to herpes simplex type 1 thymidine kinase
    • Gustafson E.A., Chillemi A.C., Sage D.R., Fingeroth J.D. The Epstein-Barr virus thymidine kinase does not phosphorylate ganciclovir or acyclovir and demonstrates a narrow substrate specificity compared to herpes simplex type 1 thymidine kinase. Antimicrob. Agents Chemother. 1998, 42:2923-2931.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2923-2931
    • Gustafson, E.A.1    Chillemi, A.C.2    Sage, D.R.3    Fingeroth, J.D.4
  • 85
    • 64349104090 scopus 로고    scopus 로고
    • Extending thymidine kinase activity to the catalytic repertoire of human deoxycytidine kinase
    • Hazra S., Sabini E., Ort S., Konrad M., Lavie A. Extending thymidine kinase activity to the catalytic repertoire of human deoxycytidine kinase. Biochemistry 2009, 48:1256-1263.
    • (2009) Biochemistry , vol.48 , pp. 1256-1263
    • Hazra, S.1    Sabini, E.2    Ort, S.3    Konrad, M.4    Lavie, A.5
  • 87
    • 0242560897 scopus 로고    scopus 로고
    • Substrate specificity of human recombinant mitochondrial 2′-deoxyguanosine kinase with cytostatic and antiviral purine and pyrimidine analogs
    • Herrström S.A., Wang L.Y., Eriksson S. Substrate specificity of human recombinant mitochondrial 2′-deoxyguanosine kinase with cytostatic and antiviral purine and pyrimidine analogs. Mol. Pharmacol. 1998, 53:270-273.
    • (1998) Mol. Pharmacol. , vol.53 , pp. 270-273
    • Herrström, S.A.1    Wang, L.Y.2    Eriksson, S.3
  • 88
    • 33748801478 scopus 로고    scopus 로고
    • Crystal structures of GMP kinase in complex with ganciclovir monophosphate and Ap5G
    • Hible G., Daalova P., Gilles A.M., Cherfils J. Crystal structures of GMP kinase in complex with ganciclovir monophosphate and Ap5G. Biochimie 2006, 88:1157-1164.
    • (2006) Biochimie , vol.88 , pp. 1157-1164
    • Hible, G.1    Daalova, P.2    Gilles, A.M.3    Cherfils, J.4
  • 90
    • 36249016299 scopus 로고    scopus 로고
    • Directed evolution for drug and nucleic acid delivery
    • Hida K., Hanes J., Ostermeier M. Directed evolution for drug and nucleic acid delivery. Adv. Drug Deliv. Rev. 2007, 59:1562-1578.
    • (2007) Adv. Drug Deliv. Rev. , vol.59 , pp. 1562-1578
    • Hida, K.1    Hanes, J.2    Ostermeier, M.3
  • 91
    • 0034636067 scopus 로고    scopus 로고
    • Conservative mutations of glutamine-125 in herpes simplex virus type 1 thymidine kinase result in a ganciclovir kinase with minimal deoxypyrimidine kinase activities
    • Hinds T.A., Compadre C., Hurlburt B.K., Drake R.R. Conservative mutations of glutamine-125 in herpes simplex virus type 1 thymidine kinase result in a ganciclovir kinase with minimal deoxypyrimidine kinase activities. Biochemistry 2000, 39:4105-4111.
    • (2000) Biochemistry , vol.39 , pp. 4105-4111
    • Hinds, T.A.1    Compadre, C.2    Hurlburt, B.K.3    Drake, R.R.4
  • 92
    • 34248344120 scopus 로고    scopus 로고
    • Comparison of the phosphorylation of 4′-ethynyl 2′,3′-dihydro 3′-deoxythymidine with that of other anti-human immunodeficiency virus thymidine analogs
    • Hsu C.-H., Hu R., Dutschman G.E., Yang G., Krishnan P., Tanaka H., Baba M., Cheng Y.-C. Comparison of the phosphorylation of 4′-ethynyl 2′,3′-dihydro 3′-deoxythymidine with that of other anti-human immunodeficiency virus thymidine analogs. Antimicrob. Agents Chemother. 2007, 51:1687-1693.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 1687-1693
    • Hsu, C.-H.1    Hu, R.2    Dutschman, G.E.3    Yang, G.4    Krishnan, P.5    Tanaka, H.6    Baba, M.7    Cheng, Y.-C.8
  • 93
    • 18244402627 scopus 로고    scopus 로고
    • Behavior of thymidylate kinase toward monophosphate metabolites and its role in the metabolism of 1-(2′-deoxy-2′-fluoro-beta-l-arabinofuranosyl)-5-methyluracil (Clevudine) and 2′,3′-didehydro-2′,3′-dideoxythymidine in cells
    • Hu R., Li L., Degreve B., Dutschman G.E., Lam W., Cheng Y.C. Behavior of thymidylate kinase toward monophosphate metabolites and its role in the metabolism of 1-(2′-deoxy-2′-fluoro-beta-l-arabinofuranosyl)-5-methyluracil (Clevudine) and 2′,3′-didehydro-2′,3′-dideoxythymidine in cells. Antimicrob. Agents Chemother. 2005, 49:2044-2049.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 2044-2049
    • Hu, R.1    Li, L.2    Degreve, B.3    Dutschman, G.E.4    Lam, W.5    Cheng, Y.C.6
  • 94
    • 0027931438 scopus 로고
    • Human dTMP kinase: gene expression and enzymatic activity coinciding with cell cycle progression and cell growth
    • Huang S.H., Tang A., Drisco B., Zhang S.Q., Seeger R., Li C., Jong A. Human dTMP kinase: gene expression and enzymatic activity coinciding with cell cycle progression and cell growth. DNA Cell. Biol. 1994, 13:461-471.
    • (1994) DNA Cell. Biol. , vol.13 , pp. 461-471
    • Huang, S.H.1    Tang, A.2    Drisco, B.3    Zhang, S.Q.4    Seeger, R.5    Li, C.6    Jong, A.7
  • 95
    • 0034487212 scopus 로고    scopus 로고
    • Phosphoryl transfer by a concerted reaction mechanism in UMP-CMP kinase
    • Hutter M.C., Helms V. Phosphoryl transfer by a concerted reaction mechanism in UMP-CMP kinase. Protein Sci. 2000, 9:2225-2231.
    • (2000) Protein Sci. , vol.9 , pp. 2225-2231
    • Hutter, M.C.1    Helms, V.2
  • 96
    • 0036405268 scopus 로고    scopus 로고
    • Nucleoside-diphosphate kinase: structural and kinetic analysis of reaction pathway and phosphohistidine intermediate
    • Janin J., Deville-Bonne D. Nucleoside-diphosphate kinase: structural and kinetic analysis of reaction pathway and phosphohistidine intermediate. Methods Enzymol. 2002, 354:118-134.
    • (2002) Methods Enzymol. , vol.354 , pp. 118-134
    • Janin, J.1    Deville-Bonne, D.2
  • 100
    • 35848960127 scopus 로고    scopus 로고
    • Review of recent studies on resistance to cytotoxic deoxynucleoside analogues
    • Jordheim L.P., Dumontet C. Review of recent studies on resistance to cytotoxic deoxynucleoside analogues. Biochem. Biophys. Acta 2007, 1776:138-159.
    • (2007) Biochem. Biophys. Acta , vol.1776 , pp. 138-159
    • Jordheim, L.P.1    Dumontet, C.2
  • 101
    • 70349730029 scopus 로고    scopus 로고
    • Human papillomavirus 16 E7 inactivator of retinoblastoma family proteins complements human cytomegalovirus lacking UL97 protein kinase
    • Kamil J.P., Hume A.J., Jurak I., Kalejta R.F., Coen D.M. Human papillomavirus 16 E7 inactivator of retinoblastoma family proteins complements human cytomegalovirus lacking UL97 protein kinase. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:16823-16828.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 16823-16828
    • Kamil, J.P.1    Hume, A.J.2    Jurak, I.3    Kalejta, R.F.4    Coen, D.M.5
  • 102
    • 58749102067 scopus 로고    scopus 로고
    • Mutational, inhibitory and microcalorimetric analyses of Plasmodium falciparum TMP kinase. Implications for drug discovery
    • Kandeel M., Ando T., Kitamura Y., Abdel-Aziz M., Kitade Y. Mutational, inhibitory and microcalorimetric analyses of Plasmodium falciparum TMP kinase. Implications for drug discovery. Parasitology 2009, 136:11-25.
    • (2009) Parasitology , vol.136 , pp. 11-25
    • Kandeel, M.1    Ando, T.2    Kitamura, Y.3    Abdel-Aziz, M.4    Kitade, Y.5
  • 103
    • 66149112136 scopus 로고    scopus 로고
    • Reversible phosphorylation of histidine residues in proteins from vertebrates
    • Klumpp S., Krieglstein J. Reversible phosphorylation of histidine residues in proteins from vertebrates. Sci. Signal. 2009, 2:13.
    • (2009) Sci. Signal. , vol.2 , pp. 13
    • Klumpp, S.1    Krieglstein, J.2
  • 104
    • 0037007213 scopus 로고    scopus 로고
    • A few amino acid substitutions can convert deoxyribonucleoside kinase specificity from pyrimidines to purines
    • Knecht W., Sandrini M.P., Johansson K., Eklund H., Munch-Petersen B., Piskur J. A few amino acid substitutions can convert deoxyribonucleoside kinase specificity from pyrimidines to purines. EMBO J. 2002, 21:1873-1880.
    • (2002) EMBO J. , vol.21 , pp. 1873-1880
    • Knecht, W.1    Sandrini, M.P.2    Johansson, K.3    Eklund, H.4    Munch-Petersen, B.5    Piskur, J.6
  • 106
    • 0036708008 scopus 로고    scopus 로고
    • Characterization of herpes simplex virus type 1 thymidine kinase mutants engineered for improved ganciclovir or acyclovir activity
    • Kokoris M.S., Black M.E. Characterization of herpes simplex virus type 1 thymidine kinase mutants engineered for improved ganciclovir or acyclovir activity. Protein Sci. 2002, 11:2267-2272.
    • (2002) Protein Sci. , vol.11 , pp. 2267-2272
    • Kokoris, M.S.1    Black, M.E.2
  • 107
    • 0034098464 scopus 로고    scopus 로고
    • In vitro evaluation of mutant HSV-1 thymidine kinases for suicide gene therapy
    • Kokoris M.S., Sabo P., Black M.E. In vitro evaluation of mutant HSV-1 thymidine kinases for suicide gene therapy. Anticancer Res. 2000, 20:959-963.
    • (2000) Anticancer Res. , vol.20 , pp. 959-963
    • Kokoris, M.S.1    Sabo, P.2    Black, M.E.3
  • 109
    • 0037085269 scopus 로고    scopus 로고
    • Phosphorylation of pyrimidine deoxynucleoside analog diphosphates: selective phosphorylation of l-nucleoside analog diphosphates by 3-phosphoglycerate kinase
    • Krishnan P., Fu Q., Lam W., Liou J.C., Dutschman G.E., Cheng Y.-C. Phosphorylation of pyrimidine deoxynucleoside analog diphosphates: selective phosphorylation of l-nucleoside analog diphosphates by 3-phosphoglycerate kinase. J. Biol. Chem. 2002, 277:5453-5459.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5453-5459
    • Krishnan, P.1    Fu, Q.2    Lam, W.3    Liou, J.C.4    Dutschman, G.E.5    Cheng, Y.-C.6
  • 110
    • 0037200016 scopus 로고    scopus 로고
    • Phosphorylation of pyrimidine l-deoxynucleoside analog diphosphates: kinetics of phosphorylation and dephosphorylation of nucleoside analog diphosphates and triphosphates by 3-phosphoglycerate kinase
    • Krishnan P., Liou J.-Y., Cheng Y.-C. Phosphorylation of pyrimidine l-deoxynucleoside analog diphosphates: kinetics of phosphorylation and dephosphorylation of nucleoside analog diphosphates and triphosphates by 3-phosphoglycerate kinase. J. Biol. Chem. 2002, 277:31593-31600.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31593-31600
    • Krishnan, P.1    Liou, J.-Y.2    Cheng, Y.-C.3
  • 111
    • 0020633163 scopus 로고
    • Characterization of abnormal thymidine kinases induced by drug-resistant strains of herpes simplex virus type-1
    • Larder B.A., Cheng Y.-C., Darby G. Characterization of abnormal thymidine kinases induced by drug-resistant strains of herpes simplex virus type-1. J. Gen. Virol. 1983, 64:523-532.
    • (1983) J. Gen. Virol. , vol.64 , pp. 523-532
    • Larder, B.A.1    Cheng, Y.-C.2    Darby, G.3
  • 112
    • 0033795931 scopus 로고    scopus 로고
    • The catalytic mechanism of nucleoside diphosphate kinases
    • Lascu I., Gonin P. The catalytic mechanism of nucleoside diphosphate kinases. J. Bioenerg. Biomembr. 2000, 32:237-246.
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 237-246
    • Lascu, I.1    Gonin, P.2
  • 113
    • 3042750453 scopus 로고    scopus 로고
    • Structural requirements for efficient phosphorylation of nucleotide analogs by human thymidylate kinase
    • Lavie A., Konrad M. Structural requirements for efficient phosphorylation of nucleotide analogs by human thymidylate kinase. Mini Rev. Med. Chem. 2004, 4:351-359.
    • (2004) Mini Rev. Med. Chem. , vol.4 , pp. 351-359
    • Lavie, A.1    Konrad, M.2
  • 114
    • 0032539978 scopus 로고    scopus 로고
    • Crystal structure of yeast thymidylate kinase complexed with the bisubstrate inhibitor P1-(5′-adenosyl) P5-(5′-thymidyl) pentaphosphate (TP5A) at 2.0 A resolution: implications for catalysis and AZT activation
    • Lavie A., Konrad M., Brundiers R., Goody R.S., Schlichting I., Reinstein J. Crystal structure of yeast thymidylate kinase complexed with the bisubstrate inhibitor P1-(5′-adenosyl) P5-(5′-thymidyl) pentaphosphate (TP5A) at 2.0 A resolution: implications for catalysis and AZT activation. Biochemistry 1998, 37:3677-3686.
    • (1998) Biochemistry , vol.37 , pp. 3677-3686
    • Lavie, A.1    Konrad, M.2    Brundiers, R.3    Goody, R.S.4    Schlichting, I.5    Reinstein, J.6
  • 117
    • 48849091390 scopus 로고    scopus 로고
    • Restoration of the antiviral activity of 3′-azido-3′-deoxythymidine (AZT) against AZT-resistant human immunodeficiency virus by delivery of engineered thymidylate kinase to T cells
    • Lavie A., Su Y., Ghassemi M., Novak R.M., Caffrey M., Sekulic N., Monnerjahn C., Konrad M., Cook J.L. Restoration of the antiviral activity of 3′-azido-3′-deoxythymidine (AZT) against AZT-resistant human immunodeficiency virus by delivery of engineered thymidylate kinase to T cells. J. Gen. Virol. 2008, 89:1672-1679.
    • (2008) J. Gen. Virol. , vol.89 , pp. 1672-1679
    • Lavie, A.1    Su, Y.2    Ghassemi, M.3    Novak, R.M.4    Caffrey, M.5    Sekulic, N.6    Monnerjahn, C.7    Konrad, M.8    Cook, J.L.9
  • 119
    • 0037040232 scopus 로고    scopus 로고
    • Structural basis for nucleotide-dependent regulation of membrane-associated guanylate kinase-like domains
    • Li Y., Spangenberg O., Paarman I., Konrad M., Lavie A. Structural basis for nucleotide-dependent regulation of membrane-associated guanylate kinase-like domains. J. Biol. Chem. 2002, 277:4159-4165.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4159-4165
    • Li, Y.1    Spangenberg, O.2    Paarman, I.3    Konrad, M.4    Lavie, A.5
  • 120
    • 0037086275 scopus 로고    scopus 로고
    • Characterization of human UMP/CMP kinase and its phosphorylation of d- and l-form deoxycytidine analogue monophosphates
    • Liou J.C., Dutschman G.E., Lam W., Jiang Z., Cheng Y.-C. Characterization of human UMP/CMP kinase and its phosphorylation of d- and l-form deoxycytidine analogue monophosphates. Cancer Res. 2002, 62:1624-1631.
    • (2002) Cancer Res. , vol.62 , pp. 1624-1631
    • Liou, J.C.1    Dutschman, G.E.2    Lam, W.3    Jiang, Z.4    Cheng, Y.-C.5
  • 121
    • 67949109571 scopus 로고    scopus 로고
    • Directed evolution of an orthogonal nucleoside analog kinase via fluorescence-activated cell sorting
    • Liu L., Li Y., Liotta D., Lutz S. Directed evolution of an orthogonal nucleoside analog kinase via fluorescence-activated cell sorting. Nucleic Acids Res. 2009, 37:4472-4481.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 4472-4481
    • Liu, L.1    Li, Y.2    Liotta, D.3    Lutz, S.4
  • 122
    • 33747158845 scopus 로고    scopus 로고
    • L-Nucleoside enantiomers as antiviral drugs
    • Mathé C., Gosselin G. l-Nucleoside enantiomers as antiviral drugs. Antiviral Res. 2006, 71:276-281.
    • (2006) Antiviral Res. , vol.71 , pp. 276-281
    • Mathé, C.1    Gosselin, G.2
  • 123
    • 27644474083 scopus 로고    scopus 로고
    • Concentrations of glycolytic enzymes and other cytosolic proteins in the diffusible fraction of a vertebrate muscle proteome
    • Maughan D.W., Henkin J.A., Vigoreaux J.O. Concentrations of glycolytic enzymes and other cytosolic proteins in the diffusible fraction of a vertebrate muscle proteome. Mol. Cell. Proteomics 2005, 4:1541-1549.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1541-1549
    • Maughan, D.W.1    Henkin, J.A.2    Vigoreaux, J.O.3
  • 125
    • 70449700393 scopus 로고    scopus 로고
    • Nucleoside diphosphate kinase (NDPK, NM23, AWD): recent regulatory advances in endocytosis, metastasis, psoriasis, insulin release, fetal erythroid lineage and heart failure; translational medicine exemplified
    • Mehta A., Orchad S. Nucleoside diphosphate kinase (NDPK, NM23, AWD): recent regulatory advances in endocytosis, metastasis, psoriasis, insulin release, fetal erythroid lineage and heart failure; translational medicine exemplified. Mol. Cell. Biochem. 2009, 329:3-35.
    • (2009) Mol. Cell. Biochem. , vol.329 , pp. 3-35
    • Mehta, A.1    Orchad, S.2
  • 126
    • 0034679569 scopus 로고    scopus 로고
    • Structural basis for activation of alpha-boranophosphate nucleotide analogues targeting drug-resistant reverse transcriptase
    • Meyer P., Schneider B., Sarfati S., Deville-Bonne D., Guerreiro C., Boretto J., Janin J., Véron M., Canard B. Structural basis for activation of alpha-boranophosphate nucleotide analogues targeting drug-resistant reverse transcriptase. EMBO J. 2000, 19:3520-3529.
    • (2000) EMBO J. , vol.19 , pp. 3520-3529
    • Meyer, P.1    Schneider, B.2    Sarfati, S.3    Deville-Bonne, D.4    Guerreiro, C.5    Boretto, J.6    Janin, J.7    Véron, M.8    Canard, B.9
  • 127
    • 0029841220 scopus 로고    scopus 로고
    • The UL97 gene product of human cytomegalovirus is an early-late protein with a nuclear localization but is not a nucleoside kinase
    • Michel D., Pavic I., Zimmermann A., Haupt E., Wunderlich K., Heuschmid M., Mertens T. The UL97 gene product of human cytomegalovirus is an early-late protein with a nuclear localization but is not a nucleoside kinase. J. Virol. 1996, 70:6340-6346.
    • (1996) J. Virol. , vol.70 , pp. 6340-6346
    • Michel, D.1    Pavic, I.2    Zimmermann, A.3    Haupt, E.4    Wunderlich, K.5    Heuschmid, M.6    Mertens, T.7
  • 128
    • 0019321437 scopus 로고
    • Phosphorylation of acyclovir (acycloguanosine) monophosphate by GMP kinase
    • Miller W.H., Miller R.L. Phosphorylation of acyclovir (acycloguanosine) monophosphate by GMP kinase. J. Biol. Chem. 1980, 255:7204-7207.
    • (1980) J. Biol. Chem. , vol.255 , pp. 7204-7207
    • Miller, W.H.1    Miller, R.L.2
  • 129
    • 0020408238 scopus 로고
    • Phosphorylation of acyclovir diphosphate by cellular enzymes
    • Miller W.H., Miller R.L. Phosphorylation of acyclovir diphosphate by cellular enzymes. Biochem. Pharmacol. 1982, 31:3879-3884.
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 3879-3884
    • Miller, W.H.1    Miller, R.L.2
  • 130
    • 0025241769 scopus 로고
    • Curability of tumors bearing herpes thymidine kinase genes transferred by retroviral vectors
    • Moolten F., Wells J.M. Curability of tumors bearing herpes thymidine kinase genes transferred by retroviral vectors. J. Natl. Cancer Inst. 1990, 82:297-300.
    • (1990) J. Natl. Cancer Inst. , vol.82 , pp. 297-300
    • Moolten, F.1    Wells, J.M.2
  • 131
    • 0029646092 scopus 로고
    • X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2A resolution
    • Moréra S., Lacombe M.-L., Xu Y.W., LeBras G., Janin J. X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2A resolution. Structure 1995, 3:1307-1374.
    • (1995) Structure , vol.3 , pp. 1307-1374
    • Moréra, S.1    Lacombe, M.-L.2    Xu, Y.W.3    LeBras, G.4    Janin, J.5
  • 132
    • 0028063891 scopus 로고
    • Adenosine 5′-diphosphate binding and the active site of nucleoside diphosphate kinase
    • Moréra S., Lascu I., Dumas C., LeBras G., Briozzo P., Véron M., Janin J. Adenosine 5′-diphosphate binding and the active site of nucleoside diphosphate kinase. Biochemistry 1994, 33:459-467.
    • (1994) Biochemistry , vol.33 , pp. 459-467
    • Moréra, S.1    Lascu, I.2    Dumas, C.3    LeBras, G.4    Briozzo, P.5    Véron, M.6    Janin, J.7
  • 133
    • 0001142643 scopus 로고
    • Poxviridae and their replication
    • Raven Press Ltd., New York, B.N. Fields, D.M. Knipe (Eds.)
    • Moss B. Poxviridae and their replication. Virology 1990, 2079-2111. Raven Press Ltd., New York. B.N. Fields, D.M. Knipe (Eds.).
    • (1990) Virology , pp. 2079-2111
    • Moss, B.1
  • 134
    • 0025916482 scopus 로고
    • Diverging substrate specificity of pure human thymidine kinases 1 and 2 against antiviral dideoxynucleosides
    • Munch-Petersen B., Cloos L., Tyrsted G., Eriksson S. Diverging substrate specificity of pure human thymidine kinases 1 and 2 against antiviral dideoxynucleosides. J. Biol. Chem. 1991, 266:9032-9038.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9032-9038
    • Munch-Petersen, B.1    Cloos, L.2    Tyrsted, G.3    Eriksson, S.4
  • 135
    • 0035066472 scopus 로고    scopus 로고
    • Recent developments in herpesvirus therapy
    • Naesens L., De Clercq E. Recent developments in herpesvirus therapy. Herpes 2001, 8:12-16.
    • (2001) Herpes , vol.8 , pp. 12-16
    • Naesens, L.1    De Clercq, E.2
  • 136
    • 70449715871 scopus 로고    scopus 로고
    • Developmental function of Nm23/awd: a mediator of endocytosis
    • Nallamothu G., Dammai V., Hsu T. Developmental function of Nm23/awd: a mediator of endocytosis. Mol. Cell. Biochem. 2009, 329:35-44.
    • (2009) Mol. Cell. Biochem. , vol.329 , pp. 35-44
    • Nallamothu, G.1    Dammai, V.2    Hsu, T.3
  • 138
    • 0034660675 scopus 로고    scopus 로고
    • Insights into the phosphoryltransfer mechanism of human thymidylate kinase gained from crystal structures of enzyme complexes along the reaction coordinate
    • Ostermann N., Schlichting I., Brundiers R., Konrad M., Reinstein J., Veit T., Goody R.S., Lavie A. Insights into the phosphoryltransfer mechanism of human thymidylate kinase gained from crystal structures of enzyme complexes along the reaction coordinate. Structure 2000, 8:629-642.
    • (2000) Structure , vol.8 , pp. 629-642
    • Ostermann, N.1    Schlichting, I.2    Brundiers, R.3    Konrad, M.4    Reinstein, J.5    Veit, T.6    Goody, R.S.7    Lavie, A.8
  • 139
    • 0242500963 scopus 로고    scopus 로고
    • Structures of human thymidylate kinase in complex with prodrugs: implications for the structure-based design of novel compounds
    • Ostermann N., Segura-Pena D., Meier C., Veit T., Monnerjahn C., Konrad M., Lavie A. Structures of human thymidylate kinase in complex with prodrugs: implications for the structure-based design of novel compounds. Biochemistry 2003, 42:2568-2577.
    • (2003) Biochemistry , vol.42 , pp. 2568-2577
    • Ostermann, N.1    Segura-Pena, D.2    Meier, C.3    Veit, T.4    Monnerjahn, C.5    Konrad, M.6    Lavie, A.7
  • 140
    • 0017381166 scopus 로고
    • Substrate positions and induced-fit in crystalline adenylate kinase
    • Pai E.F., Sachsenheimer W., Schirmer R.H., Schulz G.E. Substrate positions and induced-fit in crystalline adenylate kinase. J. Mol. Biol. 1977, 114:37-45.
    • (1977) J. Mol. Biol. , vol.114 , pp. 37-45
    • Pai, E.F.1    Sachsenheimer, W.2    Schirmer, R.H.3    Schulz, G.E.4
  • 143
    • 0034717330 scopus 로고    scopus 로고
    • Compulsory order of substrate binding to herpes simplex virus type 1 thymidine kinase
    • Perozzo R., Jelesarov I., Bosshard H.R., Folkers G., Scapozza L. Compulsory order of substrate binding to herpes simplex virus type 1 thymidine kinase. J. Biol. Chem. 2000, 275:16139-16145.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16139-16145
    • Perozzo, R.1    Jelesarov, I.2    Bosshard, H.R.3    Folkers, G.4    Scapozza, L.5
  • 144
    • 0033527750 scopus 로고    scopus 로고
    • Substrate diversity of herpes simplex virus thymidine kinase: impact of the kinematics of the enzyme
    • Pilger B.D., Perozzo R., Alber F., Wurth C., Folkers G., Scapozza L. Substrate diversity of herpes simplex virus thymidine kinase: impact of the kinematics of the enzyme. J. Biol. Chem. 1999, 274:31967-31973.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31967-31973
    • Pilger, B.D.1    Perozzo, R.2    Alber, F.3    Wurth, C.4    Folkers, G.5    Scapozza, L.6
  • 147
    • 0027293728 scopus 로고
    • Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis
    • Postel E.H., Berberich S.J., Flint S.J., Ferrone C.A. Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis. Science 1993, 261:478-480.
    • (1993) Science , vol.261 , pp. 478-480
    • Postel, E.H.1    Berberich, S.J.2    Flint, S.J.3    Ferrone, C.A.4
  • 148
    • 61649087653 scopus 로고    scopus 로고
    • Targeted deletion of Nm23/nucleoside diphosphate kinase A and B reveals their requirement for definitive erythropoiesis in the mouse embryo
    • Postel E.H., Wohlman I., Zou X., Juan T., Sun N., D'Agostin D., Cuellar M., Choi T., Notterman D.A., La Perle K.M. Targeted deletion of Nm23/nucleoside diphosphate kinase A and B reveals their requirement for definitive erythropoiesis in the mouse embryo. Dev. Dyn. 2009, 238:775-787.
    • (2009) Dev. Dyn. , vol.238 , pp. 775-787
    • Postel, E.H.1    Wohlman, I.2    Zou, X.3    Juan, T.4    Sun, N.5    D'Agostin, D.6    Cuellar, M.7    Choi, T.8    Notterman, D.A.9    La Perle, K.M.10
  • 149
    • 29744449915 scopus 로고    scopus 로고
    • Human cytomegalovirus UL97 kinase is required for normal intranuclear distribution of pp65 and virion morphogenesis
    • Prichard M., Britt W.J., Daily S.L., Hartline C.B., Kern E.R. Human cytomegalovirus UL97 kinase is required for normal intranuclear distribution of pp65 and virion morphogenesis. J. Virol. 2005, 79:15494-15502.
    • (2005) J. Virol. , vol.79 , pp. 15494-15502
    • Prichard, M.1    Britt, W.J.2    Daily, S.L.3    Hartline, C.B.4    Kern, E.R.5
  • 151
    • 12344316420 scopus 로고
    • Discussion of the possible mechanisms of action of 5-iodo-2′-deoxyuridine and chymotrypsin in the treatment of herpes simplex keratitis
    • Prusoff W.H. Discussion of the possible mechanisms of action of 5-iodo-2′-deoxyuridine and chymotrypsin in the treatment of herpes simplex keratitis. Trans. Am. Acad. Ophthalmol. Otolaryngol. 1963, 67:707-709.
    • (1963) Trans. Am. Acad. Ophthalmol. Otolaryngol. , vol.67 , pp. 707-709
    • Prusoff, W.H.1
  • 152
    • 34248334746 scopus 로고
    • Incorporation of 5-iodo-2′-deoxyuridine into the deoxyribonucleic acid of vaccinia virus
    • Prusoff W.H., Bakhle Y.S., McCrea J.F. Incorporation of 5-iodo-2′-deoxyuridine into the deoxyribonucleic acid of vaccinia virus. Nature 1963, 199:1310-1311.
    • (1963) Nature , vol.199 , pp. 1310-1311
    • Prusoff, W.H.1    Bakhle, Y.S.2    McCrea, J.F.3
  • 155
    • 0029123494 scopus 로고
    • Metabolic pathways for activation of the antiviral agent 9-(2-phosphonylmethoxyethyl)adenine in human lymphoid cells
    • Robbins B.L., Greenhaw J., Connelly M.C., Fridland A. Metabolic pathways for activation of the antiviral agent 9-(2-phosphonylmethoxyethyl)adenine in human lymphoid cells. Antimicrob. Agents Chemother. 1995, 39:2304-2308.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2304-2308
    • Robbins, B.L.1    Greenhaw, J.2    Connelly, M.C.3    Fridland, A.4
  • 157
    • 34347230952 scopus 로고    scopus 로고
    • Nonenantioselectivity property of human deoxcytidine kinase explained by structures of the enzyme in complex with l- and d-nucleosides
    • Sabini E., Hazra S., Konrad M., Lavie A. Nonenantioselectivity property of human deoxcytidine kinase explained by structures of the enzyme in complex with l- and d-nucleosides. J. Med. Chem. 2007, 50:3004-3014.
    • (2007) J. Med. Chem. , vol.50 , pp. 3004-3014
    • Sabini, E.1    Hazra, S.2    Konrad, M.3    Lavie, A.4
  • 158
    • 0038419639 scopus 로고    scopus 로고
    • Structure of human dCK suggests strategies to improve anticancer and antiviral therapy
    • Sabini E., Ort S., Monnerjahn C., Konrad M., Lavie A. Structure of human dCK suggests strategies to improve anticancer and antiviral therapy. Nat. Struct. Biol. 2003, 10:513-519.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 513-519
    • Sabini, E.1    Ort, S.2    Monnerjahn, C.3    Konrad, M.4    Lavie, A.5
  • 159
    • 70349572867 scopus 로고    scopus 로고
    • Single and multiple mutations in the human cytomegalovirus UL97 gene and their relationship to the enzymatic activity of UL97 kinase for ganciclovir phosphorylation
    • Sanchez Puch S.I., Mathet V.L., Porta M., Cuestas M.L., Oubina J.R., Videla C.M., Salomon H.E. Single and multiple mutations in the human cytomegalovirus UL97 gene and their relationship to the enzymatic activity of UL97 kinase for ganciclovir phosphorylation. Antiviral Res. 2009, 84:194-198.
    • (2009) Antiviral Res. , vol.84 , pp. 194-198
    • Sanchez Puch, S.I.1    Mathet, V.L.2    Porta, M.3    Cuestas, M.L.4    Oubina, J.R.5    Videla, C.M.6    Salomon, H.E.7
  • 160
    • 34247194881 scopus 로고    scopus 로고
    • Engineered human TMPK/AZT as a novel enzyme/prodrug axis for suicide gene therapy
    • Sato T., Neschadim A., Konrad M., Fowler D.H., Lavie A., Medin J.A. Engineered human TMPK/AZT as a novel enzyme/prodrug axis for suicide gene therapy. Mol. Ther. 2007, 15:962-970.
    • (2007) Mol. Ther. , vol.15 , pp. 962-970
    • Sato, T.1    Neschadim, A.2    Konrad, M.3    Fowler, D.H.4    Lavie, A.5    Medin, J.A.6
  • 161
    • 0032489470 scopus 로고    scopus 로고
    • Substrate specificity of human nucleoside diphosphate kinase revealed by transient kinatic analysis
    • Schaertl S., Konrad M., Geeves M. Substrate specificity of human nucleoside diphosphate kinase revealed by transient kinatic analysis. J. Biol. Chem. 1998, 273:5662-5669.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5662-5669
    • Schaertl, S.1    Konrad, M.2    Geeves, M.3
  • 164
    • 0035425268 scopus 로고    scopus 로고
    • A spectrophotometric assay for quantitative determination of kcat of herpes simplex virus type 1 thymidine kinase substrates
    • Schelling P., Folkers G., Scapozza L. A spectrophotometric assay for quantitative determination of kcat of herpes simplex virus type 1 thymidine kinase substrates. Anal. Biochem. 2001, 295:82-87.
    • (2001) Anal. Biochem. , vol.295 , pp. 82-87
    • Schelling, P.1    Folkers, G.2    Scapozza, L.3
  • 165
    • 0030739172 scopus 로고    scopus 로고
    • Structures of the active conformations of UMP kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative
    • Schlichting I., Reichstein J. Structures of the active conformations of UMP kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative. Biochemistry 1997, 36:9290-9296.
    • (1997) Biochemistry , vol.36 , pp. 9290-9296
    • Schlichting, I.1    Reichstein, J.2
  • 166
    • 0032769396 scopus 로고    scopus 로고
    • PH influences fluoride coordination number of the AlFX phosphoryl transfer transition state analog
    • Schlichting I., Reinstein J. pH influences fluoride coordination number of the AlFX phosphoryl transfer transition state analog. Nat. Struct. Biol. 1999, 6:721-725.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 721-725
    • Schlichting, I.1    Reinstein, J.2
  • 169
    • 36749053510 scopus 로고    scopus 로고
    • Quaternary structure change as a mechanism for the regulation of thymidine kinase 1-like enzymes
    • Segura-Pena D., Lichter J., Trani M., Konrad M., Lavie A., Lutz S. Quaternary structure change as a mechanism for the regulation of thymidine kinase 1-like enzymes. Structure 2007, 15:1555-1566.
    • (2007) Structure , vol.15 , pp. 1555-1566
    • Segura-Pena, D.1    Lichter, J.2    Trani, M.3    Konrad, M.4    Lavie, A.5    Lutz, S.6
  • 170
    • 4043166269 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in human UMP/CMP kinase
    • Segura-Pena D., Sekulic N., Ort S., Konrad M., Lavie A. Substrate-induced conformational changes in human UMP/CMP kinase. J. Biol. Chem. 2004, 279:33882-33889.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33882-33889
    • Segura-Pena, D.1    Sekulic, N.2    Ort, S.3    Konrad, M.4    Lavie, A.5
  • 171
    • 0037119431 scopus 로고    scopus 로고
    • Structural characterization of the closed conformation of mouse guanylate kinase
    • Sekulic N., Shuvalova L., Spangenberg O., Konrad M., Lavie A. Structural characterization of the closed conformation of mouse guanylate kinase. J. Biol. Chem. 2002, 277:30236-30243.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30236-30243
    • Sekulic, N.1    Shuvalova, L.2    Spangenberg, O.3    Konrad, M.4    Lavie, A.5
  • 173
    • 0027417199 scopus 로고
    • Affinity of the antiviral enantiomers of oxathiolane cytosine nucleosides for human 2′-deoxycytidine kinase
    • Shewach D., Liotta D., Schinazi R. Affinity of the antiviral enantiomers of oxathiolane cytosine nucleosides for human 2′-deoxycytidine kinase. Biochem. Pharmacol. 1993, 45:1540-1543.
    • (1993) Biochem. Pharmacol. , vol.45 , pp. 1540-1543
    • Shewach, D.1    Liotta, D.2    Schinazi, R.3
  • 174
    • 0037282199 scopus 로고    scopus 로고
    • A review of compounds exhibiting anti-orthopoxvirus activity in animal models
    • Smee D.F., Sidwell R.W. A review of compounds exhibiting anti-orthopoxvirus activity in animal models. Antiviral Res. 2003, 57:41-52.
    • (2003) Antiviral Res. , vol.57 , pp. 41-52
    • Smee, D.F.1    Sidwell, R.W.2
  • 176
    • 34247115538 scopus 로고    scopus 로고
    • Biophysical characterization of vaccinia virus thymidine kinase substrate utilization
    • Smith R.F., Freyer M.W., Lewis E.A. Biophysical characterization of vaccinia virus thymidine kinase substrate utilization. J. Virol. Methods 2007, 142:151-158.
    • (2007) J. Virol. Methods , vol.142 , pp. 151-158
    • Smith, R.F.1    Freyer, M.W.2    Lewis, E.A.3
  • 179
    • 0026720227 scopus 로고
    • A protein kinase homologue controls phosphorylation of ganciclovir in human cytomegalovirus-infected cells
    • Sullivan V., Talarico C.L., Stanat S.C., Davis M., Coen D.M., Biron K.K. A protein kinase homologue controls phosphorylation of ganciclovir in human cytomegalovirus-infected cells. Nature 1992, 358:162-164.
    • (1992) Nature , vol.358 , pp. 162-164
    • Sullivan, V.1    Talarico, C.L.2    Stanat, S.C.3    Davis, M.4    Coen, D.M.5    Biron, K.K.6
  • 180
    • 0344386222 scopus 로고
    • Specific inhibition of replication of animal viruses
    • Tamm I., Eggers H. Specific inhibition of replication of animal viruses. Science 1963, 142:24-33.
    • (1963) Science , vol.142 , pp. 24-33
    • Tamm, I.1    Eggers, H.2
  • 181
  • 183
    • 54449101307 scopus 로고    scopus 로고
    • The nucleoside diphosphate kinase D (NM23-H4) binds the inner mitochondrial membrane with high affinity to cardiolipin and couples nucleotide transfer with respiration
    • Tokarska-Schlattner M., Boissan M., Munier A., Borot C., Mailleau C., Speer O., Schlattner U., Lacombe M.L. The nucleoside diphosphate kinase D (NM23-H4) binds the inner mitochondrial membrane with high affinity to cardiolipin and couples nucleotide transfer with respiration. J. Biol. Chem. 2008, 283:26198-26207.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26198-26207
    • Tokarska-Schlattner, M.1    Boissan, M.2    Munier, A.3    Borot, C.4    Mailleau, C.5    Speer, O.6    Schlattner, U.7    Lacombe, M.L.8
  • 187
    • 0028060456 scopus 로고
    • Substrate specificity of Epstein-Barr virus thymidine kinase
    • Tung P.P., Summers W.C. Substrate specificity of Epstein-Barr virus thymidine kinase. Antimicrob. Agents Chemother. 1994, 38:2175-2179.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 2175-2179
    • Tung, P.P.1    Summers, W.C.2
  • 188
    • 0033614850 scopus 로고    scopus 로고
    • A pre-steady-state kinetic analysis of substrate binding to human recombinant deoxycytidine kinase: a model for nucleoside kinase action
    • Turk B., Awad R., Usova E.V., Björk I., Eriksson S. A pre-steady-state kinetic analysis of substrate binding to human recombinant deoxycytidine kinase: a model for nucleoside kinase action. Biochemistry 2009, 38:8555-8561.
    • (2009) Biochemistry , vol.38 , pp. 8555-8561
    • Turk, B.1    Awad, R.2    Usova, E.V.3    Björk, I.4    Eriksson, S.5
  • 189
    • 0032817023 scopus 로고    scopus 로고
    • Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterisation of the human enzyme
    • Van Rompay A.R., Johansson M., Karlsson A. Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterisation of the human enzyme. Mol. Pharmacol. 1999, 56:562-569.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 562-569
    • Van Rompay, A.R.1    Johansson, M.2    Karlsson, A.3
  • 190
    • 0033796942 scopus 로고    scopus 로고
    • Substrate specificity and phosphorylation of nucleosides and nucleosides analogs by mammalian nucleoside monophosphate kinases
    • Van Rompay A.R., Johansson M., Karlsson A. Substrate specificity and phosphorylation of nucleosides and nucleosides analogs by mammalian nucleoside monophosphate kinases. Pharmacol. Ther. 2000, 87:189-198.
    • (2000) Pharmacol. Ther. , vol.87 , pp. 189-198
    • Van Rompay, A.R.1    Johansson, M.2    Karlsson, A.3
  • 191
    • 0242552804 scopus 로고    scopus 로고
    • Substrate specificity and phosphorylation of antiviral and anticancer nucleoside analogues by human deoxyribonucleoside kinases and ribonucleoside kinases
    • Van Rompay A.R., Johansson M., Karlsson A. Substrate specificity and phosphorylation of antiviral and anticancer nucleoside analogues by human deoxyribonucleoside kinases and ribonucleoside kinases. Pharmacol. Ther. 2003, 100:119-139.
    • (2003) Pharmacol. Ther. , vol.100 , pp. 119-139
    • Van Rompay, A.R.1    Johansson, M.2    Karlsson, A.3
  • 192
    • 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. Relaxed enantioselectivity of human mitochondrial thymidine kinase and chemotherapeutic uses of l-nucleoside analogues. Biochem. J. 1997, 328:317-320.
    • (1997) Biochem. J. , vol.328 , pp. 317-320
    • Verri, A.1    Priori, G.2    Spadari, S.3    Tondelli, L.4    Focher, F.5
  • 194
    • 0029644728 scopus 로고
    • Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases
    • Vonrheim C., Schlauderer G.J., Schulz G.E. Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases. Structure 1995, 3:483-490.
    • (1995) Structure , vol.3 , pp. 483-490
    • Vonrheim, C.1    Schlauderer, G.J.2    Schulz, G.E.3
  • 195
    • 0023488512 scopus 로고
    • Intracellular phosphorylation of broad-spectrum anti-DNA virus agent (S)-9-(3-hydroxy-2-phosphonylmethoxypropyl)adenine and inhibition of viral DNA synthesis
    • Votruba I., Bernaerts R., Sakuma T., De Clercq E., Merta A., Rosenberg I., Holy A. Intracellular phosphorylation of broad-spectrum anti-DNA virus agent (S)-9-(3-hydroxy-2-phosphonylmethoxypropyl)adenine and inhibition of viral DNA synthesis. Mol. Pharmacol. 1987, 32:524-529.
    • (1987) Mol. Pharmacol. , vol.32 , pp. 524-529
    • Votruba, I.1    Bernaerts, R.2    Sakuma, T.3    De Clercq, E.4    Merta, A.5    Rosenberg, I.6    Holy, A.7
  • 196
    • 0033736202 scopus 로고    scopus 로고
    • Pronucleotides: toward the in vivo delivery of antiviral and anticancer nucleotides
    • Wagner C.R., Iyer V.V., McIntee E.J. Pronucleotides: toward the in vivo delivery of antiviral and anticancer nucleotides. Med. Res. Rev. 2000, 20:417-451.
    • (2000) Med. Res. Rev. , vol.20 , pp. 417-451
    • Wagner, C.R.1    Iyer, V.V.2    McIntee, E.J.3
  • 197
    • 0033592879 scopus 로고    scopus 로고
    • Stereoisomeric selectivity of human deoxyribonucleoside kinases
    • Wang L., Choudhury D., Chattopadhyaya J., Eriksson S. Stereoisomeric selectivity of human deoxyribonucleoside kinases. Biochemistry 1999, 38:16993-16999.
    • (1999) Biochemistry , vol.38 , pp. 16993-16999
    • Wang, L.1    Choudhury, D.2    Chattopadhyaya, J.3    Eriksson, S.4
  • 199
    • 0029020644 scopus 로고
    • The three-dimensional structure of thymidine kinase from Herpes Simplex Virus type 1
    • Wild K., Bohner A., Aubry A., Folkers G., Schulz G.E. The three-dimensional structure of thymidine kinase from Herpes Simplex Virus type 1. FEBS Lett. 1995, 368:289-295.
    • (1995) FEBS Lett. , vol.368 , pp. 289-295
    • Wild, K.1    Bohner, A.2    Aubry, A.3    Folkers, G.4    Schulz, G.E.5
  • 200
    • 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., Bohner T., Folkers G., Schulz G.E. The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue. Protein Sci. 1997, 6:2097-2106.
    • (1997) Protein Sci. , vol.6 , pp. 2097-2106
    • Wild, K.1    Bohner, T.2    Folkers, G.3    Schulz, G.E.4
  • 202
    • 0035104129 scopus 로고    scopus 로고
    • The effect of substrate binding on the conformation and structural stability of herpes simplex virus type 1 thymidine kinase
    • Wurth C., Kessler U., Vogt J., Schulz G.E., Folkers G., Scapozza L. The effect of substrate binding on the conformation and structural stability of herpes simplex virus type 1 thymidine kinase. Protein Sci. 2001, 10:63-73.
    • (2001) Protein Sci. , vol.10 , pp. 63-73
    • Wurth, C.1    Kessler, U.2    Vogt, J.3    Schulz, G.E.4    Folkers, G.5    Scapozza, L.6
  • 204
    • 0030610719 scopus 로고    scopus 로고
    • AlF3 mimics the transition state of protein phosphorylation in the crystal structure of nucleoside diphosphate kinase and MgADP
    • Xu Y.W., Morera S., Janin J., Cherfils J. AlF3 mimics the transition state of protein phosphorylation in the crystal structure of nucleoside diphosphate kinase and MgADP. Proc. Natl. Acad. Sci. USA 1997, 94:3579-3584.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3579-3584
    • Xu, Y.W.1    Morera, S.2    Janin, J.3    Cherfils, J.4
  • 205
    • 17644435744 scopus 로고    scopus 로고
    • Nucleoside monophosphate kinases: structure, mechanism and substrate specificity
    • Yan H., Tsai M.-D. Nucleoside monophosphate kinases: structure, mechanism and substrate specificity. Adv. Enzymol. 1999, 73:103-134.
    • (1999) Adv. Enzymol. , vol.73 , pp. 103-134
    • Yan, H.1    Tsai, M.-D.2
  • 206
    • 48749085061 scopus 로고    scopus 로고
    • Human equilibrative nucleoside transporter (ENT) family of nucleoside and nucleobase transporter proteins
    • Young J.D., Yao S.Y.M., Sun L., Cass C.E., Baldwin S.A. Human equilibrative nucleoside transporter (ENT) family of nucleoside and nucleobase transporter proteins. Xenobiotica 2008, 38:995-1021.
    • (2008) Xenobiotica , vol.38 , pp. 995-1021
    • Young, J.D.1    Yao, S.Y.M.2    Sun, L.3    Cass, C.E.4    Baldwin, S.A.5
  • 207
    • 0030782932 scopus 로고    scopus 로고
    • Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia viruses
    • Zimmermann A., Michel D., Pavic I., Hampl W., Lüske A., Neyts J., De Clerq E., Mertens T. Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia viruses. Antiviral Res. 1997, 36:35-42.
    • (1997) Antiviral Res. , vol.36 , pp. 35-42
    • Zimmermann, A.1    Michel, D.2    Pavic, I.3    Hampl, W.4    Lüske, A.5    Neyts, J.6    De Clerq, E.7    Mertens, T.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.