Potentiating AZT activation: Structure of wild-type and mutant human 
thymidylate kinase suggest reasons for the mutants' improved kinetics with the 
HIV prodrug metabolite AZTMP.

Ostermann, N.; Lavie, A.; Padiyar, S.; Brundiers, R.; Veit, T.; Reinstein, J.; Goody, R. S.; Konrad, M.; Schlichting, I.

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Potentiating AZT activation: Structure of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP.

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Brundiers, R.
Department of Molecular Genetics, MPI for biophysical chemistry, Max Planck Society;

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Konrad, M.
Research Group of Enzyme Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Ostermann, N., Lavie, A., Padiyar, S., Brundiers, R., Veit, T., Reinstein, J., et al. (2000). Potentiating AZT activation: Structure of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP. Journal of Molecular Biology, 304, 43-53.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-F90D-2

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