Probing the Flexibility of the Catalytic Nucleophile in the Lyase Catalytic Pocket of Human DNA Polymerase β with Unnatural Lysine Analogues
Author:
Affiliation:
1. Biodesign Center for BioEnergetics and School of Molecular Sciences, Arizona State University, Tempe, Arizona 85287, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.6b00807
Reference50 articles.
1. DNA Repair in Mammalian Cells
2. Two Pathways for Base Excision Repair in Mammalian Cells
3. Requirement of mammalian DNA polymerase-β in base-excision repair
4. Studies of the domain structure of mammalian DNA polymerase beta. Identification of a discrete template binding domain.
5. Excision of Deoxyribose Phosphate Residues by DNA Polymerase β During DNA Repair
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1. An assay for DNA polymerase β lyase inhibitors that engage the catalytic nucleophile for binding;Bioorganic & Medicinal Chemistry;2020-09
2. In vitro genetic code reprogramming and expansion to study protein function and discover macrocyclic peptide ligands;Current Opinion in Chemical Biology;2018-10
3. Study of the Lyase Activity of Human DNA Polymerase β Using Analogues of the Intermediate Schiff Base Complex;Biochemistry;2018-04-06
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