Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation.

This publication has 19 references indexed in Scilit:

• 3′-Azidothymidine (Zidovudine) Inhibits Glycosylation and Dramatically Alters Glycosphingolipid Synthesis in Whole Cells at Clinically Relevant Concentrations
  Published by Elsevier ,1995
• The three‐dimensional structure of thymidine kinase from Herpes simplex virus type 1
  FEBS Letters, 1995
• Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases
  Structure, 1995
• Metabolism of 3′-azido-3′-deoxythymidine (AZT) in human placentae trophoblasts and Hofbauer cells
  Biochemical Pharmacology, 1994
• Mechanism of adenylate kinase: site-directed mutagenesis versus x-ray and NMR
  Biochemistry, 1991
• The P-loop — a common motif in ATP- and GTP-binding proteins
  Trends in Biochemical Sciences, 1990
• In vitro mutagenesis studies at the arginine residues of adenylate kinase. A revised binding site for AMP in the x-ray-deduced model
  Biochemistry, 1990
• 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
  Journal of Biological Chemistry, 1989
• Effects of 3′-azido-3′-deoxythymidine on the deoxynucleotide triphosphate pools of cultured human cells
  Biochemical and Biophysical Research Communications, 1988
• Phosphorylation of 3'-azido-3'-deoxythymidine and selective interaction of the 5'-triphosphate with human immunodeficiency virus reverse transcriptase.
  Proceedings of the National Academy of Sciences, 1986