Differential activity of potential antiviral nucleoside analogs on herpes simplex virus-induced and human cellular thymidine kinases was written by Cheng, Y. C.; Dutschman, G.; Fox, J. J.; Watanabe, K. A.; Machida, H.. And the article was included in Antimicrobial Agents and Chemotherapy on September 30,1981.Recommanded Product: 69256-17-3 The following contents are mentioned in the article:
The rates of phosphorylation of the potential antiviral nucleoside analogs I (R = I, Me, CH:CHBr; R1 = H, F, OH) and II (R = I, Me) by purified thymidine kinase [9002-06-6] from both human and herpes simplex virus sources were studied. Most of the analogs were phosphorylated by both human and viral kinases. The analogs were competitive inhibitors of thymidine phosphorylation by the kinases; on the assumption that inhibition constants (Ki) reflect binding affinity, Ki values of the analogs were determined In general, the analogs have a greater affinity for the viral kinases than for the human kinases. The amount of the analogs phosphorylated to the monophosphate form, which is presumably necessary for cytotoxic activity, was dependent on both the phosphorylation rates and binding affinities. All of the analogs act as preferential substrates for the viral kinases at low concentrations, which may be one of the main reasons for their selective antiviral action. The structure-activity relations of the analogs are discussed. This study involved multiple reactions and reactants, such as 1-((2R,3S,4R,5R)-3-Fluoro-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl)-5-methylpyrimidine-2,4(1H,3H)-dione (cas: 69256-17-3Recommanded Product: 69256-17-3).
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