Repair of Oxidative DNA Damage: Mechanisms and Functions
- 1 January 2001
- journal article
- review article
- Published by Springer Nature in Cell Biochemistry and Biophysics
- Vol. 35 (2) , 141-170
- https://doi.org/10.1385/cbb:35:2:141
Abstract
Cellular genomes suffer extensive damage from exogenous agents and reactive oxygen species formed during normal metabolism. The MutT homologs (MutT/MTH) reKeywords
This publication has 20 references indexed in Scilit:
- Characterization of a Novel 8-Oxoguanine-DNA Glycosylase Activity in Escherichia coli and Identification of the Enzyme as Endonuclease VIIIJournal of Biological Chemistry, 2000
- The MutT motif family of nucleotide phosphohydrolases in man and human pathogens (review).International Journal of Molecular Medicine, 1999
- The Oxidized Forms of dATP Are Substrates for the Human MutT Homologue, the hMTH1 ProteinJournal of Biological Chemistry, 1999
- The presence of two distinct 8-oxoguanine repair enzymes in human cells: their potential complementary roles in preventing mutationNucleic Acids Research, 1998
- Evidence that MutY is a monofunctional glycosylase capable of forming a covalent Schiff base intermediate with substrate DNANucleic Acids Research, 1998
- Enzymatic Processing of Radiation-Induced Free Radical Damage in DNARadiation Research, 1998
- Chemistry of Glycosylases and Endonucleases Involved in Base-Excision RepairChemical Reviews, 1998
- Cloning, Overexpression, and Biochemical Characterization of the Catalytic Domain of MutYBiochemistry, 1997
- DNA glycosylasesMutation Research/DNA Repair, 1997
- Mechanistic studies of ionizing radiation and oxidative mutagenesis: genetic effects of a single 8-hydroxyguanine (7-hydro-8-oxoguanine) residue inserted at a unique site in a viral genomeBiochemistry, 1990