Structure–Activity Relationships Reveal Key Features of 8-Oxoguanine: A Mismatch Detection by the MutY Glycosylase
Author:
Affiliation:
1. Department of Chemistry, University of California at Davis, One Shields Avenue, Davis, California 95616, United States
2. Department of Chemistry, University of Richmond, Richmond, Virginia 23173, United States
Funder
National Cancer Institute
Dow Chemical Company
National Science Foundation
Department of Chemistry, University of California, Davis
Publisher
American Chemical Society (ACS)
Subject
Molecular Medicine,General Medicine,Biochemistry
Link
http://pubs.acs.org/doi/pdf/10.1021/acschembio.7b00389
Reference48 articles.
1. Unnatural substrates reveal the importance of 8-oxoguanine for in vivo mismatch repair by MutY
2. Base-excision repair of oxidative DNA damage
3. Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage
4. Chemistry of Glycosylases and Endonucleases Involved in Base-Excision Repair
5. The GO Repair Pathway: OGG1 and MUTYH
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3. FSHing for DNA Damage: Key Features of MutY Detection of 8-Oxoguanine:Adenine Mismatches;Accounts of Chemical Research;2024-03-12
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