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Volumn 87, Issue 2-3, 2000, Pages 189-198

Phosphorylation of nucleosides and nucleoside analogs by mammalian nucleoside monophosphate kinases

Author keywords

Anticancer therapy; Antiviral therapy; Monophosphate kinases; Nucleoside analogs; Nucleoside kinases

Indexed keywords

1 BETA DEXTRO ARABINOFURANOSYLADENINE; 2 CHLORODEOXYADENOSINE; 9 (2 PHOSPHONOMETHOXYPROPYL)ADENINE; ADEFOVIR; ADENYLATE KINASE; CIDOFOVIR; CYTARABINE; DIDANOSINE; GEMCITABINE; GUANYLATE KINASE; ISOENZYME; LAMIVUDINE; NUCLEOSIDE; NUCLEOSIDE DERIVATIVE; NUCLEOSIDE MONOPHOSPHATE KINASE; STAVUDINE; THYMIDYLATE KINASE; UNCLASSIFIED DRUG; URIDYLATE CYTIDYLATE KINASE; ZALCITABINE; ZIDOVUDINE;

EID: 0033796942     PISSN: 01637258     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0163-7258(00)00048-6     Document Type: Review
Times cited : (192)

References (74)
  • 1
    • 0017869256 scopus 로고
    • Guanylate kinases from human erythrocytes, hog brain, and rat liver
    • Agarwal K.C., Miech R.P., Parks R.E. Jr. Guanylate kinases from human erythrocytes, hog brain, and rat liver. Methods Enzymol. 51:1978;483-490.
    • (1978) Methods Enzymol , vol.51 , pp. 483-490
    • Agarwal, K.C.1    Miech, R.P.2    Parks, R.E.3
  • 2
    • 0029895282 scopus 로고    scopus 로고
    • 2′,3′-Didehydro-3′-deoxythymidine: Regulation of its metabolic activation by modulators of thymidine-5′-triphosphate biosynthesis
    • Ahluwalia G.S., Gao W.Y., Mitsuya H., Johns D.G. 2′,3′-Didehydro-3′-deoxythymidine. regulation of its metabolic activation by modulators of thymidine-5′-triphosphate biosynthesis Mol Pharmacol. 50:1996;160-165.
    • (1996) Mol Pharmacol , vol.50 , pp. 160-165
    • Ahluwalia, G.S.1    Gao, W.Y.2    Mitsuya, H.3    Johns, D.G.4
  • 4
    • 0017740850 scopus 로고
    • Characterization of pyrimidine nucleoside monophosphokinase in normal and malignant tissues
    • Arima T., Akiyoshi H., Fujii S. Characterization of pyrimidine nucleoside monophosphokinase in normal and malignant tissues. Cancer Res. 37:1977;1593-1597.
    • (1977) Cancer Res , vol.37 , pp. 1593-1597
    • Arima, T.1    Akiyoshi, H.2    Fujii, S.3
  • 5
    • 0029162556 scopus 로고
    • Mammalian deoxyribonucleoside kinases
    • Arnér E.S.J., Eriksson S. Mammalian deoxyribonucleoside kinases. Pharmacol Ther. 67:1995;155-186.
    • (1995) Pharmacol Ther , vol.67 , pp. 155-186
    • Arnér, E.S.J.1    Eriksson, S.2
  • 6
    • 0024592935 scopus 로고
    • Differential patterns of intracellular metabolism of 2′,3′-didehydro-2′,3′-dideoxythymidine and 3′-azido-2′,3′-dideoxythymidine, two potent anti-human immunodeficiency virus compounds
    • Balzarini J., Herdewijn P., De Clercq E. Differential patterns of intracellular metabolism of 2′,3′-didehydro-2′,3′-dideoxythymidine and 3′-azido-2′,3′-dideoxythymidine, two potent anti-human immunodeficiency virus compounds. J Biol Chem. 264:1989;6127-6133.
    • (1989) J Biol Chem , vol.264 , pp. 6127-6133
    • Balzarini, J.1    Herdewijn, P.2    De Clercq, E.3
  • 8
    • 0020445220 scopus 로고
    • Selective expansion of mitochondrial nucleoside triphosphate pools in antimetabolite-treated HeLa cells
    • Bestwick R.K., Moffett G.L., Mathews C.K. Selective expansion of mitochondrial nucleoside triphosphate pools in antimetabolite-treated HeLa cells. J Biol Chem. 257:1982;9300-9304.
    • (1982) J Biol Chem , vol.257 , pp. 9300-9304
    • Bestwick, R.K.1    Moffett, G.L.2    Mathews, C.K.3
  • 10
    • 0029927011 scopus 로고    scopus 로고
    • Cellular phosphorylation of anti-HIV nucleosides. Role of nucleoside diphosphate kinase
    • Bourdais J., Biondi R., Sarfati S., Guerreiro C., Lascu I., Janin J., Veron M. Cellular phosphorylation of anti-HIV nucleosides. Role of nucleoside diphosphate kinase. J Biol Chem. 271:1996;7887-7890.
    • (1996) J Biol Chem , vol.271 , pp. 7887-7890
    • Bourdais, J.1    Biondi, R.2    Sarfati, S.3    Guerreiro, C.4    Lascu, I.5    Janin, J.6    Veron, M.7
  • 11
    • 0029896252 scopus 로고    scopus 로고
    • Cloning, characterization, and modeling of mouse and human guanylate kinases
    • Brady W.A., Kokoris M.S., Fitzgibbon M., Black M.E. Cloning, characterization, and modeling of mouse and human guanylate kinases. J Biol Chem. 271:1996;16734-16740.
    • (1996) J Biol Chem , vol.271 , pp. 16734-16740
    • Brady, W.A.1    Kokoris, M.S.2    Fitzgibbon, M.3    Black, M.E.4
  • 12
    • 0019920785 scopus 로고
    • Gene order and localization of enzyme loci on the short arm of chromosome 1
    • Carritt B., King J., Welch H.M. Gene order and localization of enzyme loci on the short arm of chromosome 1. Ann Hum Genet. 46:1982;329-335.
    • (1982) Ann Hum Genet , vol.46 , pp. 329-335
    • Carritt, B.1    King, J.2    Welch, H.M.3
  • 13
    • 0031921349 scopus 로고    scopus 로고
    • Function of p55 and its nonerythroid homologues
    • Chishti A.H. Function of p55 and its nonerythroid homologues. Curr Opin Hematol. 5:1998;116-121.
    • (1998) Curr Opin Hematol , vol.5 , pp. 116-121
    • Chishti, A.H.1
  • 14
    • 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. 50:1996;1502-1510.
    • (1996) Mol Pharmacol , vol.50 , pp. 1502-1510
    • Cihlar, T.1    Chen, M.S.2
  • 15
    • 0018562513 scopus 로고
    • Report of the committee on the genetic constitution of chromosome 1
    • Cook P.J.L., Hamerton J.L. Report of the committee on the genetic constitution of chromosome 1. Cytogenet Cell Genet. 25:1979;9-20.
    • (1979) Cytogenet Cell Genet , vol.25 , pp. 9-20
    • Cook, P.J.L.1    Hamerton, J.L.2
  • 17
    • 0027306127 scopus 로고
    • Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: Implications for chemotherapy with 5-fluoropyrimidines
    • el Kouni M.H., el Kouni M.M., Naguib F.N. Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases. implications for chemotherapy with 5-fluoropyrimidines Cancer Res. 53:1993;3687-3693.
    • (1993) Cancer Res , vol.53 , pp. 3687-3693
    • El Kouni, M.H.1    El Kouni, M.M.2    Naguib, F.N.3
  • 18
    • 0030014023 scopus 로고    scopus 로고
    • Human guanylate kinase (GUK1): CDNA sequence, expression and chromosomal localisation
    • Fitzgibbon J., Katsanis N., Wells D., Delhanty J., Vallins W., Hunt D.M. Human guanylate kinase (GUK1). cDNA sequence, expression and chromosomal localisation FEBS Lett. 385:1996;185-188.
    • (1996) FEBS Lett , vol.385 , pp. 185-188
    • Fitzgibbon, J.1    Katsanis, N.2    Wells, D.3    Delhanty, J.4    Vallins, W.5    Hunt, D.M.6
  • 19
    • 0029937408 scopus 로고    scopus 로고
    • Ancient divergence of long and short isoforms of adenylate kinase: Molecular evolution of the nucleoside monophosphate kinase family
    • Fukami-Kobayashi K., Nosaka M., Nakazawa A., Gö M. Ancient divergence of long and short isoforms of adenylate kinase. molecular evolution of the nucleoside monophosphate kinase family FEBS Lett. 385:1996;214-220.
    • (1996) FEBS Lett , vol.385 , pp. 214-220
    • Fukami-Kobayashi, K.1    Nosaka, M.2    Nakazawa, A.3    Gö, M.4
  • 21
    • 0027371703 scopus 로고
    • Enzymes of the cyclic GMP metabolism in bovine retina. I. Cloning and expression of the gene for guanylate kinase
    • Gaidarov I.O., Suslov O.N., Abdulaev N.G. Enzymes of the cyclic GMP metabolism in bovine retina. I. Cloning and expression of the gene for guanylate kinase. FEBS Lett. 335:1993;81-84.
    • (1993) FEBS Lett , vol.335 , pp. 81-84
    • Gaidarov, I.O.1    Suslov, O.N.2    Abdulaev, N.G.3
  • 22
    • 0014343681 scopus 로고
    • Comparative study of the thymidine kinase and thymidylate kinase activities and of the feedback inhibition of thymidine kinase in normal and neoplastic human tissue
    • Gordon H.L., Bardos T.J., Chmielewicz Z.F., Ambrus J.L. Comparative study of the thymidine kinase and thymidylate kinase activities and of the feedback inhibition of thymidine kinase in normal and neoplastic human tissue. Cancer Res. 28:1968;2068-2077.
    • (1968) Cancer Res , vol.28 , pp. 2068-2077
    • Gordon, H.L.1    Bardos, T.J.2    Chmielewicz, Z.F.3    Ambrus, J.L.4
  • 23
    • 0022894780 scopus 로고
    • Purification and properties of guanylate kinase from bovine retinas and rod outer segments
    • Hall S.W., Kuhn H. Purification and properties of guanylate kinase from bovine retinas and rod outer segments. Eur J Biochem. 161:1986;551-556.
    • (1986) Eur J Biochem , vol.161 , pp. 551-556
    • Hall, S.W.1    Kuhn, H.2
  • 24
    • 0029947983 scopus 로고    scopus 로고
    • Retroviral transfer of deoxycytidine kinase into tumor cell lines enhances nucleoside toxicity
    • Hapke D.M., Stegmann A.P., Mitchell B.S. Retroviral transfer of deoxycytidine kinase into tumor cell lines enhances nucleoside toxicity. Cancer Res. 56:1996;2343-2347.
    • (1996) Cancer Res , vol.56 , pp. 2343-2347
    • Hapke, D.M.1    Stegmann, A.P.2    Mitchell, B.S.3
  • 25
    • 0023783698 scopus 로고
    • Comparison of the cellular pharmacokinetics and toxicity of 2′,2′-difluorodeoxycytidine and 1-beta-D-arabinofuranosylcytosine
    • Heinemann V., Hertel L.W., Grindey G.B., Plunkett W. Comparison of the cellular pharmacokinetics and toxicity of 2′,2′-difluorodeoxycytidine and 1-beta-D-arabinofuranosylcytosine. Cancer Res. 48:1988;4024-4031.
    • (1988) Cancer Res , vol.48 , pp. 4024-4031
    • Heinemann, V.1    Hertel, L.W.2    Grindey, G.B.3    Plunkett, W.4
  • 27
    • 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. 13:1994;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
  • 28
    • 0016675762 scopus 로고
    • Studies on the properties and tissue distribution of the isozymes of guanylate kinase in man
    • Jamil T., Fisher R.A., Harris H. Studies on the properties and tissue distribution of the isozymes of guanylate kinase in man. Hum Hered. 25:1975;402-413.
    • (1975) Hum Hered , vol.25 , pp. 402-413
    • Jamil, T.1    Fisher, R.A.2    Harris, H.3
  • 29
    • 0029037121 scopus 로고
    • Differences in kinetic properties of pure recombinant human and mouse deoxycytidine kinase
    • Johansson M., Karlsson A. Differences in kinetic properties of pure recombinant human and mouse deoxycytidine kinase. Biochem Pharmacol. 50:1995;163-168.
    • (1995) Biochem Pharmacol , vol.50 , pp. 163-168
    • Johansson, M.1    Karlsson, A.2
  • 30
    • 0033588215 scopus 로고    scopus 로고
    • Cloning and characterization of the deoxyribonucleoside kinase of Drosophila melanogaster
    • Johansson M., Van Rompay A.R., Degrève B., Balzarini J., Karlsson A. Cloning and characterization of the deoxyribonucleoside kinase of Drosophila melanogaster. J Biol Chem. 274:1999;23814-23819.
    • (1999) J Biol Chem , vol.274 , pp. 23814-23819
    • Johansson, M.1    Van Rompay, A.R.2    Degrève, B.3    Balzarini, J.4    Karlsson, A.5
  • 31
    • 0029689120 scopus 로고    scopus 로고
    • Structure-activity relationships for phosphorylation of nucleoside analogs to monophosphates by nucleoside kinases
    • Johansson N.G., Eriksson S. Structure-activity relationships for phosphorylation of nucleoside analogs to monophosphates by nucleoside kinases. Acta Biochim Pol. 43:1996;143-160.
    • (1996) Acta Biochim Pol , vol.43 , pp. 143-160
    • Johansson, N.G.1    Eriksson, S.2
  • 32
    • 0025124373 scopus 로고
    • The metabolism of 3′-azido-2′,3′-dideoxyguanosine in CEM cells
    • Karlsson A., Reichard P., Eckstein F. The metabolism of 3′-azido-2′,3′-dideoxyguanosine in CEM cells. Biochem Biophys Res Commun. 166:1990;273-279.
    • (1990) Biochem Biophys Res Commun , vol.166 , pp. 273-279
    • Karlsson, A.1    Reichard, P.2    Eckstein, F.3
  • 33
    • 0023802655 scopus 로고
    • Sequences contained within the promoter of the human thymidine kinase gene can direct cell-cycle regulation of heterologous fusion genes
    • Kim Y.K., Wells S., Lau Y.F., Lee A.S. Sequences contained within the promoter of the human thymidine kinase gene can direct cell-cycle regulation of heterologous fusion genes. Proc Natl Acad Sci USA. 85:1988;5894-5898.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5894-5898
    • Kim, Y.K.1    Wells, S.2    Lau, Y.F.3    Lee, A.S.4
  • 35
    • 0032564339 scopus 로고    scopus 로고
    • Structural basis for efficient phosphorylation of 3′-azidothymidine monophosphate by Escherichia coli thymidylate kinase
    • Lavie A., Ostermann N., Brundiers R., Goody R.S., Reinstein J., Konrad M., Schlichting I. Structural basis for efficient phosphorylation of 3′-azidothymidine monophosphate by Escherichia coli thymidylate kinase. Proc Natl Acad Sci USA. 95:1998;14045-14050.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14045-14050
    • Lavie, A.1    Ostermann, N.2    Brundiers, R.3    Goody, R.S.4    Reinstein, J.5    Konrad, M.6    Schlichting, I.7
  • 36
    • 0017698076 scopus 로고
    • Human thymidylate kinase. Purification, characterization, and kinetic behavior of the thymidylate kinase derived from chronic myelocytic leukemia
    • Lee L.S., Cheng Y. Human thymidylate kinase. Purification, characterization, and kinetic behavior of the thymidylate kinase derived from chronic myelocytic leukemia. J Biol Chem. 252:1977;5686-5691.
    • (1977) J Biol Chem , vol.252 , pp. 5686-5691
    • Lee, L.S.1    Cheng, Y.2
  • 39
    • 0025351196 scopus 로고
    • Comparison of pyrimidine nucleotide synthetic enzymes involved in 5-fluorouracil metabolism between human adenocarcinomas and squamous cell carcinomas
    • Maehara Y., Moriguchi S., Emi Y., Watanabe A., Kohnoe S., Tsujitani S., Sugimachi K. Comparison of pyrimidine nucleotide synthetic enzymes involved in 5-fluorouracil metabolism between human adenocarcinomas and squamous cell carcinomas. Cancer. 66:1990;156-161.
    • (1990) Cancer , vol.66 , pp. 156-161
    • Maehara, Y.1    Moriguchi, S.2    Emi, Y.3    Watanabe, A.4    Kohnoe, S.5    Tsujitani, S.6    Sugimachi, K.7
  • 40
    • 0016796260 scopus 로고
    • A pyrimidine nucleoside monophosphate kinase from rat liver
    • Maness P., Orengo A. A pyrimidine nucleoside monophosphate kinase from rat liver. Biochemistry. 14:1975;1484-1489.
    • (1975) Biochemistry , vol.14 , pp. 1484-1489
    • Maness, P.1    Orengo, A.2
  • 41
    • 0024390429 scopus 로고
    • Human adenylate kinase deficiency associated with hemolytic anemia. A single base substitution affecting solubility and catalytic activity of the cytosolic adenylate kinase
    • Matsuura S., Igarashi M., Tanizawa Y., Yamada M., Kishi F., Kajii T., Fujii H., Miwa S., Sakurai M., Nakazawa A. Human adenylate kinase deficiency associated with hemolytic anemia. A single base substitution affecting solubility and catalytic activity of the cytosolic adenylate kinase. J Biol Chem. 264:1989;10148-10155.
    • (1989) J Biol Chem , vol.264 , pp. 10148-10155
    • Matsuura, S.1    Igarashi, M.2    Tanizawa, Y.3    Yamada, M.4    Kishi, F.5    Kajii, T.6    Fujii, H.7    Miwa, S.8    Sakurai, M.9    Nakazawa, A.10
  • 42
    • 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. 266:1991;9032-9038.
    • (1991) J Biol Chem , vol.266 , pp. 9032-9038
    • Munch-Petersen, B.1    Cloos, L.2    Tyrsted, G.3    Eriksson, S.4
  • 43
    • 0031036704 scopus 로고    scopus 로고
    • HPMPC (cidofovir), PMEA (adefovir) and related acyclic nucleoside phosphonate analogues: A review of their pharmacology and clinical potential in the treatment of viral infections
    • Naesens L., Snoeck R., Andrei G., Balzarini J., Neyts J., De Clercq E. HPMPC (cidofovir), PMEA (adefovir) and related acyclic nucleoside phosphonate analogues. a review of their pharmacology and clinical potential in the treatment of viral infections Antiviral Chem Chemother. 8:1996;1-23.
    • (1996) Antiviral Chem Chemother , vol.8 , pp. 1-23
    • Naesens, L.1    Snoeck, R.2    Andrei, G.3    Balzarini, J.4    Neyts, J.5    De Clercq, E.6
  • 44
    • 0013929922 scopus 로고
    • Metabolism of deoxyribonucleotides. II. Enzymatic phosphorylation of deoxycytidylic acid in normal rat liver and rat ascites hepatoma cells
    • Nakamura H., Sugino Y. Metabolism of deoxyribonucleotides. II. Enzymatic phosphorylation of deoxycytidylic acid in normal rat liver and rat ascites hepatoma cells. Cancer Res. 26:1966;1425-1429.
    • (1966) Cancer Res , vol.26 , pp. 1425-1429
    • Nakamura, H.1    Sugino, Y.2
  • 45
    • 0032491901 scopus 로고    scopus 로고
    • CDNA cloning and tissue-specific expression of the gene encoding human adenylate kinase isozyme 2
    • Noma T., Song S., Yoon Y.-Y., Tanaks S., Nakazawa A. cDNA cloning and tissue-specific expression of the gene encoding human adenylate kinase isozyme 2. Biochim Biophys Acta. 1395:1998;34-39.
    • (1998) Biochim Biophys Acta , vol.1395 , pp. 34-39
    • Noma, T.1    Song, S.2    Yoon, Y.-Y.3    Tanaks, S.4    Nakazawa, A.5
  • 46
    • 0027452523 scopus 로고
    • Site-directed mutagenesis of AMP-binding residues in adenylate kinase. Alteration of substrate specificity
    • Okajima T., Tanizawa K., Fukui T. Site-directed mutagenesis of AMP-binding residues in adenylate kinase. Alteration of substrate specificity. FEBS Lett. 334:1993;86-88.
    • (1993) FEBS Lett , vol.334 , pp. 86-88
    • Okajima, T.1    Tanizawa, K.2    Fukui, T.3
  • 47
    • 0026637308 scopus 로고
    • Resistance to 1-beta-D-arabinofuranosylcytosine in human T-lymphoblasts mediated by mutations within the deoxycytidine kinase gene
    • Owens J.K., Shewach D.S., Ullman B., Mitchell B.S. Resistance to 1-beta-D-arabinofuranosylcytosine in human T-lymphoblasts mediated by mutations within the deoxycytidine kinase gene. Cancer Res. 52:1992;2389-2393.
    • (1992) Cancer Res , vol.52 , pp. 2389-2393
    • Owens, J.K.1    Shewach, D.S.2    Ullman, B.3    Mitchell, B.S.4
  • 49
    • 0023925454 scopus 로고
    • Interactions between deoxyribonucleotide and DNA synthesis
    • Reichard P. Interactions between deoxyribonucleotide and DNA synthesis. Annu Rev Biochem. 57:1988;349-374.
    • (1988) Annu Rev Biochem , vol.57 , pp. 349-374
    • Reichard, P.1
  • 50
    • 0027180521 scopus 로고
    • 2′,2′-Difluoro-deoxycytidine (gemcitabine) incorporation into RNA and DNA of tumour cell lines
    • Ruiz van Haperen V.W., Veerman G., Vermorken J.B., Peters G.J. 2′,2′-Difluoro-deoxycytidine (gemcitabine) incorporation into RNA and DNA of tumour cell lines. Biochem Pharmacol. 46:1993;762-766.
    • (1993) Biochem Pharmacol , vol.46 , pp. 762-766
    • Ruiz Van Haperen, V.W.1    Veerman, G.2    Vermorken, J.B.3    Peters, G.J.4
  • 54
    • 0242560897 scopus 로고    scopus 로고
    • Substrate specificity of human recombinant mitochondrial deoxyguanosine kinase with cytostatic and antiviral purine and pyrimidine analogs
    • Sjoberg A.H., Wang L., Eriksson S. Substrate specificity of human recombinant mitochondrial deoxyguanosine kinase with cytostatic and antiviral purine and pyrimidine analogs. Mol Pharmacol. 53:1998;270-273.
    • (1998) Mol Pharmacol , vol.53 , pp. 270-273
    • Sjoberg, A.H.1    Wang, L.2    Eriksson, S.3
  • 55
    • 0025969987 scopus 로고
    • Molecular cloning and expression of the human deoxythymidylate kinase gene in yeast
    • Su J.Y., Sclafani R.A. Molecular cloning and expression of the human deoxythymidylate kinase gene in yeast. Nucleic Acids Res. 19:1991;823-827.
    • (1991) Nucleic Acids Res , vol.19 , pp. 823-827
    • Su, J.Y.1    Sclafani, R.A.2
  • 56
    • 0029118503 scopus 로고
    • Purine nucleoside analogs: Emerging roles in indolent lymphoproliferative disorders
    • Tallman M.S., Hakimian D. Purine nucleoside analogs. emerging roles in indolent lymphoproliferative disorders Blood. 86:1995;2463-2474.
    • (1995) Blood , vol.86 , pp. 2463-2474
    • Tallman, M.S.1    Hakimian, D.2
  • 57
    • 0027418855 scopus 로고
    • Tissue-specific and developmentally regulated expression of the genes encoding adenylate kinase isozymes
    • Tanabe T., Yamada M., Noma T., Kajii T., Nakazawa A. Tissue-specific and developmentally regulated expression of the genes encoding adenylate kinase isozymes. J Biochem. 113:1993;200-207.
    • (1993) J Biochem , vol.113 , pp. 200-207
    • Tanabe, T.1    Yamada, M.2    Noma, T.3    Kajii, T.4    Nakazawa, A.5
  • 58
    • 0018375417 scopus 로고
    • Mitochondrial GTP-AMP phosphotransferase. 2. Kinetic and equilibrium dialysis studies
    • Tomasselli A.G., Noda L.H. Mitochondrial GTP-AMP phosphotransferase. 2. Kinetic and equilibrium dialysis studies. Eur J Biochem. 93:1979;263-270.
    • (1979) Eur J Biochem , vol.93 , pp. 263-270
    • Tomasselli, A.G.1    Noda, L.H.2
  • 59
    • 0024210541 scopus 로고
    • Genetic analysis of 2′,3′-dideoxycytidine incorporation into cultured human T lymphoblasts
    • Ullman B., Coons T., Rockwell S., McCartan K. Genetic analysis of 2′,3′-dideoxycytidine incorporation into cultured human T lymphoblasts. J Biol Chem. 263:1988;12391-12396.
    • (1988) J Biol Chem , vol.263 , pp. 12391-12396
    • Ullman, B.1    Coons, T.2    Rockwell, S.3    McCartan, K.4
  • 60
    • 0033561360 scopus 로고    scopus 로고
    • Identification of a novel human adenylate kinase: CDNA cloning, expression analysis, chromosome localization and characterization of the recombinant protein
    • a
    • Van Rompay A.R., Johansson M., Karlsson A. Identification of a novel human adenylate kinase. cDNA cloning, expression analysis, chromosome localization and characterization of the recombinant protein Eur J Biochem. 261:1999;509-516. a.
    • (1999) Eur J Biochem , vol.261 , pp. 509-516
    • Van Rompay, A.R.1    Johansson, M.2    Karlsson, A.3
  • 61
    • 0032817023 scopus 로고    scopus 로고
    • Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase; Molecular characterisation of the human enzyme
    • b
    • 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. 56:1999;562-569. b.
    • (1999) Mol Pharmacol , vol.56 , pp. 562-569
    • Van Rompay, A.R.1    Johansson, M.2    Karlsson, A.3
  • 63
    • 0027476495 scopus 로고
    • Nucleoside monophosphate kinase may be the key enzyme preventing salvage of DNA 5-methylcytosine
    • Vilpo J.A., Vilpo L.M. Nucleoside monophosphate kinase may be the key enzyme preventing salvage of DNA 5-methylcytosine. Mutat Res. 286:1993;217-220.
    • (1993) Mutat Res , vol.286 , pp. 217-220
    • Vilpo, J.A.1    Vilpo, L.M.2
  • 64
    • 0029888564 scopus 로고    scopus 로고
    • Phosphorylation of the anti-hepatitis B nucleoside analog 1-(2′-deoxy-2′-fluoro-1-beta-D-arabinofuranosyl)-5-iodouracil (FIAU) by human cytosolic and mitochondrial thymidine kinase and implications for cytotoxicity
    • Wang J., Eriksson S. Phosphorylation of the anti-hepatitis B nucleoside analog 1-(2′-deoxy-2′-fluoro-1-beta-D-arabinofuranosyl)-5-iodouracil (FIAU) by human cytosolic and mitochondrial thymidine kinase and implications for cytotoxicity. Antimicrob Agents Chemother. 40:1996;1555-1557.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 1555-1557
    • Wang, J.1    Eriksson, S.2
  • 65
    • 0027381413 scopus 로고
    • Substrate specificity of mitochondrial 2′-deoxyguanosine kinase. Efficient phosphorylation of 2-chlorodeoxyadenosine
    • Wang L., Karlsson A., Arner E.S., Eriksson S.J. Substrate specificity of mitochondrial 2′-deoxyguanosine kinase. Efficient phosphorylation of 2-chlorodeoxyadenosine. Biol Chem. 268:1993;22847-22852.
    • (1993) Biol Chem , vol.268 , pp. 22847-22852
    • Wang, L.1    Karlsson, A.2    Arner, E.S.3    Eriksson, S.J.4
  • 66
    • 0017279867 scopus 로고
    • Adenylate kinases in man: Evidence for a third locus
    • Wilson D.E., Povey S., Harris H. Adenylate kinases in man. evidence for a third locus Ann Hum Genet. 39:1976;305-313.
    • (1976) Ann Hum Genet , vol.39 , pp. 305-313
    • Wilson, D.E.1    Povey, S.2    Harris, H.3
  • 67
    • 0026693145 scopus 로고
    • Characterization of human adenylate kinase 3 (AK3) cDNA and mapping of the AK3 pseudogene to an intron of the NF1 gene
    • Xu G., O'Connell P., Stevens J., White R. Characterization of human adenylate kinase 3 (AK3) cDNA and mapping of the AK3 pseudogene to an intron of the NF1 gene. Genomics. 13:1992;537-542.
    • (1992) Genomics , vol.13 , pp. 537-542
    • Xu, G.1    O'Connell, P.2    Stevens, J.3    White, R.4
  • 69
    • 0024818830 scopus 로고
    • Cloning and characterization of cDNA for mitochondrial GTP:AMP phosphotransferase of bovine liver
    • Yamada M., Shahjahan M., Tanabe T., Kishi F., Nakazawa A. Cloning and characterization of cDNA for mitochondrial GTP:AMP phosphotransferase of bovine liver. J Biol Chem. 264:1989;19192-19199.
    • (1989) J Biol Chem , vol.264 , pp. 19192-19199
    • Yamada, M.1    Shahjahan, M.2    Tanabe, T.3    Kishi, F.4    Nakazawa, A.5
  • 70
    • 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 Relat Areas Mol Biol. 73:1999;103-134.
    • (1999) Adv Enzymol Relat Areas Mol Biol , vol.73 , pp. 103-134
    • Yan, H.1    Tsai, M.D.2
  • 71
    • 0032570036 scopus 로고    scopus 로고
    • Identification of a novel adenylate kinase system in brain: Cloning of the fourth adenylate kinase
    • Yoneda T., Sato M., Maeda M., Takagi H. Identification of a novel adenylate kinase system in brain. cloning of the fourth adenylate kinase Mol Brain Res. 62:1998;187-195.
    • (1998) Mol Brain Res , vol.62 , pp. 187-195
    • Yoneda, T.1    Sato, M.2    Maeda, M.3    Takagi, H.4
  • 72
    • 0032531671 scopus 로고    scopus 로고
    • Phosphorylation of anticancer nucleoside analogs by human mitochondrial deoxyguanosine kinase
    • a
    • Zhu C., Johansson M., Permert J., Karlsson A. Phosphorylation of anticancer nucleoside analogs by human mitochondrial deoxyguanosine kinase. Biochem Pharmacol. 56:1998;1035-1040. a.
    • (1998) Biochem Pharmacol , vol.56 , pp. 1035-1040
    • Zhu, C.1    Johansson, M.2    Permert, J.3    Karlsson, A.4
  • 73
    • 0032510972 scopus 로고    scopus 로고
    • Enhanced cytotoxicity of nucleoside analogs by overexpression of mitochondrial deoxyguanosine kinase in cancer cell lines
    • b
    • Zhu C., Johansson M., Permert J., Karlsson A. Enhanced cytotoxicity of nucleoside analogs by overexpression of mitochondrial deoxyguanosine kinase in cancer cell lines. J Biol Chem. 273:1998;14707-14711. b.
    • (1998) J Biol Chem , vol.273 , pp. 14707-14711
    • Zhu, C.1    Johansson, M.2    Permert, J.3    Karlsson, A.4
  • 74
    • 0027457144 scopus 로고
    • Purification and sequence determination of guanylate kinase from pig brain
    • Zschocke P.D., Schiltz E., Schulz G.E. Purification and sequence determination of guanylate kinase from pig brain. Eur J Biochem. 213:1993;263-269.
    • (1993) Eur J Biochem , vol.213 , pp. 263-269
    • Zschocke, P.D.1    Schiltz, E.2    Schulz, G.E.3


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