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  Crystal structure of yeast thymidylate kinase complexed with the bisubstrate inhibitor P1-(5′-adenosyl)P5-(5′-thymidyl) pentaphosphate (TP5A) at 2.0 Å resolution: Implications for catalysis and AZT activation.

Lavie, A., Konrad, M., Brundiers, R., Goody, R. S., Schlichting, I., & Reinstein, J. (1998). Crystal structure of yeast thymidylate kinase complexed with the bisubstrate inhibitor P1-(5′-adenosyl)P5-(5′-thymidyl) pentaphosphate (TP5A) at 2.0 Å resolution: Implications for catalysis and AZT activation. Biochemistry, 37, 3677-3686.

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 Creators:
Lavie, A., Author
Konrad, M.1, Author           
Brundiers, R.2, Author           
Goody, R. S., Author
Schlichting, I., Author
Reinstein, J., Author
Affiliations:
1Research Group of Enzyme Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578612              
2Department of Molecular Genetics, MPI for biophysical chemistry, Max Planck Society, ou_578622              

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Language(s): eng - English
 Dates: 1998
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 228769
Other: 534
 Degree: -

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Title: Biochemistry
Source Genre: Journal
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Pages: - Volume / Issue: 37 Sequence Number: - Start / End Page: 3677 - 3686 Identifier: -