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Reply to “Improving AZT efficacy”

Nature Medicinevolume 4page132 (1998) | Download Citation

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References

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    Lavie, A. et al. The bottleneck in AZT activation. Nature Med. 3, 922–924 (1997).

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    Balzarini, J. et al. The in vitro and in vivo anti-retro-virus activity, and intracellular metabolism of 3′-azido-2′,3′-dideoxythymidine and 2′,3′-dideoxy-cytidine are highly dependent on the cell species. Biochem. Pharmacol. 37, 897–903 (1988).

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    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, 6127–6133 (1989).

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    Frick, L.W. et al. Effects of 3′-azido-3′-deoxythymidine on the deoxynucleotide triphosphate pools of cultured human cells. Biochem. Biophys. Res. Comm. 154, 124–129 (1988).

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    Guettari, N., Loubiere, L., Brisson, E. & Klatzmann, D. Use of Herpes-simplex Virus Thymidine Kinase to Imporve the Antiviral Activity of Zidovudine. Virology 235, 398–405 (1997).

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    Meier, C., Habel, L., Laux, W., Declercq, E., & Balzarini, J. Homo Dinucleoside-alpha-hydroxyphosphonate Diesters as Prodrugs of the Antiviral Nucleoside Analogues 2′,3′-Dideoxythymidine and 3′-Azido-2′,3′Dideoxythymidine. Nudeosides & Nudeotides 14, 759–762 (1995).

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    Lavie, A. et al. Crystal Structure of Yeast Thymidylate Kinase Complexed with the Bisubstrate Inhibitor P1-(5′-Adenosyl)P5-(5′-Thymidyl)Pentaphosphate (TP5A) at 2.0 Å Resolution: Implications for Catalysis and AZT Activation Biochem. In the press.

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  1. Max-Planck-Institute for Molecular Physiology, Department of Physical Biochemistry, Rheinlanddamm 201, 44139, Dortmund, Germany

    • Arnon Lavie
    • , Jochen Reinstein
    • , Roger S. Goody
    •  & Ilme Schlichting
  2. Max-Planck-Institute for Biophysical Chemistry, Department of Molecular Genetics, 37018, Gottingen, Germany

    • Manfred Konrad

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https://doi.org/10.1038/nm0298-132b