Ape1 Abasic Endonuclease Activity is Regulated by Magnesium and Potassium Concentrations and is Robust on Alternative DNA Structures
- 4 February 2005
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 345 (5) , 1003-1014
- https://doi.org/10.1016/j.jmb.2004.11.028
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- Interplay between DNA replication, recombination and repair based on the structure of RecG helicasePhilosophical Transactions Of The Royal Society B-Biological Sciences, 2004
- Properties of and Substrate Determinants for the Exonuclease Activity of Human Apurinic Endonuclease Ape1Journal of Molecular Biology, 2003
- Determinants in nuclease specificity of ape1 and ape2, human homologues of Escherichia coli exonuclease IIIJournal of Molecular Biology, 2002
- The “A” rule revisited: polymerases as determinants of mutational specificityDNA Repair, 2002
- Mapping the protein-DNA interface and the metal-binding site of the major human apurinic/apyrimidinic endonucleaseJournal of Molecular Biology, 2000
- Regulation of cellular magnesiumFrontiers in Bioscience-Landmark, 2000
- Human Apurinic/Apyrimidinic Endonuclease Is Processive,Biochemistry, 1999
- The role of Mg2+ and specific amino acid residues in the catalytic reaction of the major human abasic endonuclease: new insights from EDTA-resistant incision of acyclic abasic site analogs and site-directed mutagenesisJournal of Molecular Biology, 1999
- Deletion analysis of human AP-endonuclease: minimum sequence required for the endonuclease activityCarcinogenesis: Integrative Cancer Research, 1998
- MUTAGENESIS BY APURINIC/APYRIMIDINIC SITESAnnual Review of Genetics, 1986