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Volumn 387, Issue 12, 2006, Pages 1575-1581

Evaluation of Bacillus anthracis thymidine kinase as a potential target for the development of antibacterial nucleoside analogs

Author keywords

5 fluoro deoxyuridine; Characterization; Growth inhibition; Kinetics; Thymidine

Indexed keywords

5 (2 BROMOVINYL) 2' DEOXYURIDINE; ACICLOVIR; ADENOSINE TRIPHOSPHATE; ANTHRAX VACCINE; BROXURIDINE; CLADRIBINE; CYTARABINE; DEOXYURIDINE DERIVATIVE; FLUOROURACIL; FLUOROURIDINE; GANCICLOVIR; HYDROXYUREA; MERCAPTOPURINE; NUCLEOSIDE DERIVATIVE; STAVUDINE; THYMIDINE; THYMIDINE KINASE;

EID: 33751520341     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2006.196     Document Type: Article
Times cited : (10)

References (27)
  • 1
    • 3042520589 scopus 로고    scopus 로고
    • The role of thymidine kinase in the activation of pyrimidine nucleoside analogues
    • Al-Madhoun, A., Tjarks, W., and Eriksson, S. (2004). The role of thymidine kinase in the activation of pyrimidine nucleoside analogues. Mini Rev. Med. Chem. 4, 341-350.
    • (2004) Mini Rev. Med. Chem. , vol.4 , pp. 341-350
    • Al-Madhoun, A.1    Tjarks, W.2    Eriksson, S.3
  • 2
    • 0000257609 scopus 로고
    • Studies on immunity in anthrax. VI. Immunizing activity of protective antigen against various strains of Bacillus anthracis
    • Auerbach, S. and Wright, G. (1955). Studies on immunity in anthrax. VI. Immunizing activity of protective antigen against various strains of Bacillus anthracis. J. Immunol. 75, 129-133.
    • (1955) J. Immunol. , vol.75 , pp. 129-133
    • Auerbach, S.1    Wright, G.2
  • 3
    • 0024592935 scopus 로고
    • Differential patterns of intracellular metabolism of 2′,3′- didehydro2′,3′-dideoxythymidine and 3′-azido-2′, 3′-dideoxythymidine, two potential anti-human immunodeficiency virus compounds
    • Balzarini, J., Herdewijn, P., and De Clercq, E. (1989). Differential patterns of intracellular metabolism of 2′,3′-didehydro2′, 3′-dideoxythymidine and 3′-azido-2′,3′-dideoxythymidine, two potential anti-human immunodeficiency virus compounds. J. Biol. Chem. 264, 6127-6133.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6127-6133
    • Balzarini, J.1    Herdewijn, P.2    De Clercq, E.3
  • 4
    • 13444267623 scopus 로고    scopus 로고
    • Comparative molecular field analysis and comparative molecular similarity indices analysis of human thymidine kinase 1 substrates
    • Bandyopadhyaya, A., Johnsamuel, J., Al-Madhoun, A., Eriksson, S., and Tjarks, W. (2005). Comparative molecular field analysis and comparative molecular similarity indices analysis of human thymidine kinase 1 substrates. Bioorg. Med. Chem. 13, 1681-1689.
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 1681-1689
    • Bandyopadhyaya, A.1    Johnsamuel, J.2    Al-Madhoun, A.3    Eriksson, S.4    Tjarks, W.5
  • 5
    • 0025130909 scopus 로고
    • Identification of the ATP-binding domain of vaccinia virus thymidine kinase
    • Black, M. and Hruby, D. (1990). Identification of the ATP-binding domain of vaccinia virus thymidine kinase. J. Biol. Chem. 265, 17584-17592.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17584-17592
    • Black, M.1    Hruby, D.2
  • 6
    • 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., and Barzu, O. (1994). Improved spectrophotometric assay of nucleoside monophosphate kinase activity using the pyruvate kinase/lactate dehydrogenase coupling system. Anal. Biochem. 220, 219-221.
    • (1994) Anal. Biochem. , vol.220 , pp. 219-221
    • Blondin, C.1    Serina, L.2    Wiesmuller, L.3    Gilles, A.4    Barzu, O.5
  • 8
    • 0242606204 scopus 로고    scopus 로고
    • Molecular characterization of thymidine kinase from Ureaplasma urealyticum: Nucleoside analogues as potent inhibitors of mycoplasma growth
    • Carnrot, C., Wehelie, R., Eriksson, S., Bölske, G., and Wang, L. (2003). Molecular characterization of thymidine kinase from Ureaplasma urealyticum: nucleoside analogues as potent inhibitors of mycoplasma growth. Mol. Microbiol. 50, 771-780.
    • (2003) Mol. Microbiol. , vol.50 , pp. 771-780
    • Carnrot, C.1    Wehelie, R.2    Eriksson, S.3    Bölske, G.4    Wang, L.5
  • 9
    • 0030332138 scopus 로고    scopus 로고
    • The specter of biological weapons
    • Cole, L. (1996). The specter of biological weapons. Sci. Am. 275, 60-65.
    • (1996) Sci. Am. , vol.275 , pp. 60-65
    • Cole, L.1
  • 10
    • 4544350893 scopus 로고    scopus 로고
    • The role of radiotherapy in the treatment of liver metastases
    • Dawson, L. and Lawrence, T. (2004). The role of radiotherapy in the treatment of liver metastases. Cancer J. 10, 139-144.
    • (2004) Cancer J. , vol.10 , pp. 139-144
    • Dawson, L.1    Lawrence, T.2
  • 12
    • 0034565445 scopus 로고    scopus 로고
    • Anthrax: Clinical features, pathogenesis, and potential biological warfare threat
    • Friedlander, A. (2000). Anthrax: clinical features, pathogenesis, and potential biological warfare threat. Curr. Clin. Top. Infect. Dis. 20, 335-349.
    • (2000) Curr. Clin. Top. Infect. Dis. , vol.20 , pp. 335-349
    • Friedlander, A.1
  • 14
    • 0022996630 scopus 로고
    • Phosphorylation of 3′-azido-3′-deoxythymidine and selective interaction of the 5′-triphosphate with human immunodeficiency virus reverse transcriptase
    • Furman, P., Fyfe, J., St Clair, M., Weinhold, K., Rideout, J., Freeman, G., Nusinoff Lehrmann, S., Bolognesi, D., Broder, S., et al. (1986). Phosphorylation of 3′-azido-3′-deoxythymidine and selective interaction of the 5′-triphosphate with human immunodeficiency virus reverse transcriptase. Proc. Natl. Acad. Sci. USA 83, 8333-8337.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8333-8337
    • Furman, P.1    Fyfe, J.2    St Clair, M.3    Weinhold, K.4    Rideout, J.5    Freeman, G.6    Nusinoff Lehrmann, S.7    Bolognesi, D.8    Broder, S.9
  • 15
    • 43349098749 scopus 로고
    • Observations on the prophylaxis of experimental pulmonary anthrax in the monkey
    • Henderson, D., Peacock, S., and Belton, F. (1956). Observations on the prophylaxis of experimental pulmonary anthrax in the monkey. J. Hyg. 54, 28-36.
    • (1956) J. Hyg. , vol.54 , pp. 28-36
    • Henderson, D.1    Peacock, S.2    Belton, F.3
  • 17
    • 33751543879 scopus 로고    scopus 로고
    • Clinical trials report
    • Jernigan, J. (2001). Clinical trials report. Curr. Infect. Dis. Rep. 3, 505-511.
    • (2001) Curr. Infect. Dis. Rep. , vol.3 , pp. 505-511
    • Jernigan, J.1
  • 18
    • 0029689120 scopus 로고    scopus 로고
    • Structure-activity relationships for phosphorylation of nucleoside analogs to monophosphates by nucleoside kinases
    • Johansson, N. and Eriksson, S. (1996). Structure-activity relationships for phosphorylation of nucleoside analogs to monophosphates by nucleoside kinases. Acta Biochim. Pol. 43, 143-160.
    • (1996) Acta Biochim. Pol. , vol.43 , pp. 143-160
    • Johansson, N.1    Eriksson, S.2
  • 19
    • 29144442291 scopus 로고    scopus 로고
    • Structure of the substrate complex of thymidine kinase from Ureaplasma urealyticum and investigations of possible drug targets for the enzyme
    • Kosinska, U., Carnrot, C., Eriksson, S., Wang, L., and Eklund, H. (2005). Structure of the substrate complex of thymidine kinase from Ureaplasma urealyticum and investigations of possible drug targets for the enzyme. FEBS J. 272, 6365-6372.
    • (2005) FEBS J. , vol.272 , pp. 6365-6372
    • Kosinska, U.1    Carnrot, C.2    Eriksson, S.3    Wang, L.4    Eklund, H.5
  • 20
    • 13044283431 scopus 로고    scopus 로고
    • Synthesis of 5-(carboranylalkylmercapto)-2′-deoxyuridines and 3-(carboranylalkyl)thymidines and their evaluation as substrates for human thymidine kinases 1 and 2
    • Lunato, A., Wang, J., Woollard, J., Anisuzzaman, A., Ji, W., Rong, F., Ikeda, S., Soloway, A., Eriksson, S., Ives, D., et al. (1999). Synthesis of 5-(carboranylalkylmercapto)-2′-deoxyuridines and 3-(carboranylalkyl) thymidines and their evaluation as substrates for human thymidine kinases 1 and 2. J. Med. Chem. 42, 3378-3389.
    • (1999) J. Med. Chem. , vol.42 , pp. 3378-3389
    • Lunato, A.1    Wang, J.2    Woollard, J.3    Anisuzzaman, A.4    Ji, W.5    Rong, F.6    Ikeda, S.7    Soloway, A.8    Eriksson, S.9    Ives, D.10
  • 21
    • 0026050699 scopus 로고
    • Developments of the fluoropyrimidines as inhibitors of thymidylate synthase: Pharmacologic and clinical aspects
    • Machover, D. (1991). Developments of the fluoropyrimidines as inhibitors of thymidylate synthase: pharmacologic and clinical aspects. J. Surg. Oncol. Suppl. 2, 42-50.
    • (1991) J. Surg. Oncol. Suppl. , vol.2 , pp. 42-50
    • Machover, D.1
  • 22
    • 0035522659 scopus 로고    scopus 로고
    • Thymidylate synthase pharmacogenetics in colorectal cancer
    • Marsh, S. and McLeod, H. (2001). Thymidylate synthase pharmacogenetics in colorectal cancer. Clin. Colorectal Cancer 1, 175-178.
    • (2001) Clin. Colorectal Cancer , vol.1 , pp. 175-178
    • Marsh, S.1    McLeod, H.2
  • 23
    • 0027185675 scopus 로고
    • Reversible ATP-dependent transition between two forms of human cytosolic thymidine kinase with different enzymatic properties
    • Munch-Petersen, B., Tyrsted, G., and Cloos, L. (1993). Reversible ATP-dependent transition between two forms of human cytosolic thymidine kinase with different enzymatic properties. J. Biol. Chem. 268, 15621-15625.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15621-15625
    • Munch-Petersen, B.1    Tyrsted, G.2    Cloos, L.3
  • 24
    • 78651143700 scopus 로고
    • Deoxythymidine kinase of Escherichia coli. II. Kinetics and feedback control
    • Okazaki, R. and Kornberg, A. (1964). Deoxythymidine kinase of Escherichia coli. II. Kinetics and feedback control. J. Biol. Chem. 239, 269-274.
    • (1964) J. Biol. Chem. , vol.239 , pp. 269-274
    • Okazaki, R.1    Kornberg, A.2
  • 26
    • 18844367487 scopus 로고    scopus 로고
    • Deoxyribonucleoside kinases: Two enzyme families catalyze the same reaction
    • Sandrini, M. and Piskur, J. (2005). Deoxyribonucleoside kinases: two enzyme families catalyze the same reaction. Trends Biochem. Sci. 30, 225-228.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 225-228
    • Sandrini, M.1    Piskur, J.2


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