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.

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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0012-F90D-2 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0027-E8A6-3

Genre: Journal Article

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Creators:
Ostermann, N., Author
Lavie, A., Author
Padiyar, S., Author
Brundiers, R.¹, Author
Veit, T., Author
Reinstein, J., Author
Goody, R. S., Author
Konrad, M.², Author
Schlichting, I., Author

Affiliations:
1Department of Molecular Genetics, MPI for biophysical chemistry, Max Planck Society, ou_578622
2Research Group of Enzyme Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578612

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Language(s): eng - English

Dates: Date issued: 2000

Publication Status: Issued

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Identifiers: eDoc: 233448
Other: 23010

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Title: Journal of Molecular Biology

Source Genre: Journal

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Pages: - Volume / Issue: 304 Sequence Number: - Start / End Page: 43 - 53 Identifier: -