Stabilization of Active Site Dynamics Leads to Increased Activity with 3′-Azido-3′-deoxythymidine Monophosphate for F105Y Mutant Human Thymidylate Kinase-Reference-Cited by-同舟云学术

Stabilization of Active Site Dynamics Leads to Increased Activity with 3′-Azido-3′-deoxythymidine Monophosphate for F105Y Mutant Human Thymidylate Kinase

Published:2020-01-31 Issue:5 Volume:5 Page:2355-2367
ISSN:2470-1343
Container-title:ACS Omega
language:en
Short-container-title:ACS Omega

Author:

Fucci Ian J.¹,Sinha Kaustubh¹,Rule Gordon S.¹^ORCID

Affiliation:

1. Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, United States

Funder

Mellon College of Science, Carnegie Mellon University

Publisher

American Chemical Society (ACS)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.acs.org/doi/pdf/10.1021/acsomega.9b03766

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2. RIBONUCLEOTIDE REDUCTASES

3. Human dTMP Kinase: Gene Expression and Enzymatic Activity Coinciding with Cell Cycle Progression and Cell Growth

4. Control of dTTP pool size by anaphase promoting complex/cyclosome is essential for the maintenance of genetic stability

5. Thymidylate kinase is critical for DNA repair via ATM‐dependent Tip60 complex formation

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