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- W2020283319 endingPage "198" @default.
- W2020283319 startingPage "189" @default.
- W2020283319 abstract "Nucleoside monophosphate kinases catalyze the reversible phosphotransferase reaction between nucleoside triphosphates and monophosphates, i.e., monophosphates are converted to their corresponding diphosphate form. These enzymes play an important role in the synthesis of nucleotides that are required for a variety of cellular metabolic processes, as well as for RNA and DNA synthesis. Human tissues contain a thymidylate kinase, a uridylate-cytidylate kinase, five isozymes of adenylate kinase, and several guanylate kinases. Nucleoside monophosphate kinases are also required for the pharmacological activation of therapeutic nucleoside and nucleotide analogs. This overview is focused on the substrate specificity, tissue distribution, and subcellular location of the mammalian monophosphate kinases and their role in the activation of nucleoside and nucleotide analogs." @default.
- W2020283319 created "2016-06-24" @default.
- W2020283319 creator A5036534119 @default.
- W2020283319 creator A5062239666 @default.
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- W2020283319 date "2000-08-01" @default.
- W2020283319 modified "2023-10-16" @default.
- W2020283319 title "Phosphorylation of nucleosides and nucleoside analogs by mammalian nucleoside monophosphate kinases" @default.
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- W2020283319 doi "https://doi.org/10.1016/s0163-7258(00)00048-6" @default.
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