Characterization of the Substrate Specificity of a Human 5-Hydroxymethyluracil Glycosylase Activity
- 13 December 2001
- journal article
- research article
- Published by American Chemical Society (ACS) in Chemical Research in Toxicology
- Vol. 15 (1) , 33-39
- https://doi.org/10.1021/tx010113b
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- Investigation of the substrate spectrum of the human mismatch‐specific DNA N ‐glycosylase MED1 (MBD4): Fundamental role of the catalytic domainJournal of Cellular Physiology, 2000
- Separating Substrate Recognition from Base Hydrolysis in Human Thymine DNA Glycosylase by Mutational AnalysisJournal of Biological Chemistry, 2000
- Biphasic Kinetics of the Human DNA Repair Protein MED1 (MBD4), a Mismatch-specific DNA N-GlycosylaseJournal of Biological Chemistry, 2000
- Differential Destabilization of the DNA Oligonucleotide Double Helix by a T·G Mismatch, 3,N4-Ethenocytosine, 3,N4-Ethanocytosine, or an 8-(Hydroxymethyl)-3,N4-ethenocytosine Adduct Incorporated into the Same Sequence ContextsChemical Research in Toxicology, 2000
- The α/β fold uracil DNA glycosylases: a common origin with diverse fatesGenome Biology, 2000
- Crystal structure of a thwarted mismatch glycosylase DNA repair complexThe EMBO Journal, 1999
- The Type of DNA Glycosylase Determines the Base Excision Repair Pathway in Mammalian CellsJournal of Biological Chemistry, 1999
- Kinetics of the Action of Thymine DNA GlycosylaseJournal of Biological Chemistry, 1998
- Base Analog and Neighboring Base Effects on Substrate Specificity of Recombinant Human G:T Mismatch-Specific Thymine DNA−GlycosylaseBiochemistry, 1996
- Synthesis of oligonucleotides containing 5-(hydroxymethyl)-2'-deoxyuridine at defined sitesThe Journal of Organic Chemistry, 1993