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

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.

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 Creators:
Lavie, Arnon1, Author
Vetter, Ingrid R.2, Author           
Konrad, Manfred3, Author
Goody, Roger S.1, Author           
Reinstein, Jochen4, Author           
Schlichting, Ilme5, Author           
Affiliations:
1Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753289              
2Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753287              
3Research Group of Enzyme Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578612              
4Molecular chaperones, Max Planck Institute for Medical Research, Max Planck Society, ou_1497728              
5Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Dates: 1997
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1038/nsb0897-601
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Title: Nature structural biology
Source Genre: Journal
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Publ. Info: New York, NY : Nature Pub. Co.
Pages: - Volume / Issue: 4 Sequence Number: - Start / End Page: 601 - 604 Identifier: ISSN: 1072-8368
CoNE: https://pure.mpg.de/cone/journals/resource/111073404672000