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

MPS-Authors

Lavie,  Arnon
Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons98734

Vetter,  Ingrid R.
Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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

http://pubman.mpdl.mpg.de/cone/persons/resource/persons98693

Goody,  Roger S.
Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons94928

Reinstein,  Jochen
Molecular chaperones, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons95189

Schlichting,  Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Lavie, A., Vetter, I. R., Konrad, M., Goody, R. S., Reinstein, J., & Schlichting, I. (1997). Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation. Nature structural biology, 4, 601-604. doi:10.1038/nsb0897-601.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-3FA5-6
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