Interplay between base excision repair activity and toxicity of 3-methyladenine DNA glycosylases in an E. coli complementation system-Reference-Cited by-同舟云学术

Interplay between base excision repair activity and toxicity of 3-methyladenine DNA glycosylases in an E. coli complementation system

Published:2014-05 Issue: Volume:763-764 Page:64-73
ISSN:0027-5107
Container-title:Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis
language:en
Short-container-title:Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis

Author:

Troll Christopher J.,Adhikary Suraj,Cueff Marie,Mitra Ileena,Eichman Brandt F.,Camps Manel

Publisher

Elsevier BV

Subject

Health, Toxicology and Mutagenesis,Genetics,Molecular Biology

Reference41 articles.

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3. DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the AlkA enzyme in Escherichia coli;Bjelland;J. Biol. Chem.,1994

4. Escherichia coli, Saccharomyces cerevisiae, rat and human 3-methyladenine DNA glycosylases repair 1 N6-ethenoadenine when present in DNA;Saparbaev;Nucleic Acids Res.,1995

5. Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases;Saparbaev;Proc. Natl. Acad. Sci. U. S. A.,1994

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