Phosphorylation of 3'-azido-3'-deoxythymidine and selective interaction of the 5'-triphosphate with human immunodeficiency virus reverse transcriptase.

  title={Phosphorylation of 3'-azido-3'-deoxythymidine and selective interaction of the 5'-triphosphate with human immunodeficiency virus reverse transcriptase.},
  author={Phillip A. Furman and James A. Fyfe and Marty H. St. Clair and Kent J. Weinhold and J. L. Rideout and George Andrew Freeman and Sandra Nusinoff Lehrman and Dani P. Bolognesi and Samuel E. Broder and Hiroaki Mitsuya},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  volume={83 21},
  • P. FurmanJ. A. Fyfe H. Mitsuya
  • Published 1 November 1986
  • Biology, Chemistry
  • Proceedings of the National Academy of Sciences of the United States of America
The thymidine analog 3'-azido-3'-deoxythymidine (BW A509U, azidothymidine) can inhibit human immunodeficiency virus (HIV) replication effectively in the 50-500 nM range [Mitsuya, H., Weinhold, K. J., Furman, P. A., St. Clair, M. H., Nusinoff-Lehrman, S., Gallo, R. C., Bolognesi, D., Barry, D. W. & Broder, S. (1985) Proc. Natl. Acad. Sci. USA 82, 7096-7100]. In contrast, inhibition of the growth of uninfected human fibroblasts and lymphocytes has been observed only at concentrations above 1 mM… 

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Phosphorylation of 3'-azido-2',3'-dideoxyuridine and preferential inhibition of human and simian immunodeficiency virus reverse transcriptases by its 5'-triphosphate

The different affinities of 3'-azido-2',3'-dideoxyuridine and 3'-zido-3'-deoxythymidine for the thymidine kinase and the Km values observed with these compounds as substrates may explain the difference in effects on human immunodeficiency virus type 1 replication in infected peripheral blood mononuclear cells observed when equimolar concentrations of the two compounds are compared.

Effects of 3'-deoxynucleoside 5'-triphosphate concentrations on chain termination by nucleoside analogs during human immunodeficiency virus type 1 reverse transcription of minus-strand strong-stop DNA

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Different patterns of inhibition of avian myeloblastosis virus reverse transcriptase activity by 3'-azido-3'-deoxythymidine 5'-triphosphate and its threo isomer

Kinetic analysis of the (rA)n X (dT)12-18 (a standard template primer complex of polyriboadenylate and oligodeoxythymidylate of indicated length)-directed reaction revealed that erythro-AZT-TP was a competitive inhibitor with respect to dTTP, whereas threo-AZTs was a noncompetitive inhibitor.

Inhibition of human immunodeficiency virus 1 reverse transcriptase by 3'-azidothymidine triphosphate.

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