Escherichia coli Double-Strand Uracil-DNA Glycosylase: Involvement in Uracil-Mediated DNA Base Excision Repair and Stimulation of Activity by Endonuclease IV
Author:
Affiliation:
1. Departments of Environmental and Molecular Toxicology and Biochemistry and Biophysics and the Environmental Health Science Center, Oregon State University, Corvallis, Oregon 97731
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi0007066
Reference49 articles.
1. Specific mutator effects of ung (uracil-DNA glycosylase) mutations in Escherichia coli
2. Sequence analysis, expression, and conservation of Escherichia coli uracil DNA glycosylase and its gene (ung).
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2. The lyase activity of bifunctional DNA glycosylases and the 3′-diesterase activity of APE1 contribute to the repair of oxidized bases in nucleosomes;Nucleic Acids Research;2019-01-16
3. Role of endonuclease III enzymes in uracil repair;Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis;2019-01
4. Transient protein–protein complexes in base excision repair;Journal of Biomolecular Structure and Dynamics;2018-12-31
5. Nucleosomes Suppress the Formation of Double-strand DNA Breaks during Attempted Base Excision Repair of Clustered Oxidative Damages;Journal of Biological Chemistry;2014-07
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