Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The exonuclease activity of human apurinic/apyrimidinic endonuclease (APE1). Biochemical properties and inhibition by the natural dinucleotide Gp4G.

The Journal of biological chemistry - 16 May 2003

Chou Kai-Ming, Cheng Yung-Chi

Abstract excerpt

Human DNA apurinic/apyrimidinic endonuclease (APE1) plays a key role in the DNA base excision repair process. In this study, we further characterized the exonuclease activity of APE1. The magnesium requirement and pH dependence of the exonuclease and endonuclease activities of APE1 are significantly different. APE1 showed a similar K(m) value for matched, 3' mispaired, or nucleoside analog...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acids
Share to Carbon-Oxygen Lyases
Share to CpG Islands

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytosine

Share to DNA-(Apurinic or Apyrimidinic Site) Lyase

Share to Hydrogen-Ion Concentration

Share to Nickel

Share to Substrate Specificity

Source

Identifiers

PMID: 12624104
DOI: 10.1074/jbc.M212143200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The exonuclease activity of human apurinic/apyrimidinic endonuclease (APE1). Biochemical properties and inhibition by the natural dinucleotide Gp4G.PMID 12624104Read ↗

Human Apurinic/Apyrimidinic Endonuclease 1Semantic proximity Read ↗

Characterization of the endoribonuclease active site of human apurinic/apyrimidinic endonuclease 1.Semantic proximity Read ↗

[Mutational and Kinetic Analysis of APE1 Endoribonuclease Activity].Semantic proximity Read ↗

Pre-steady-state kinetic and mutational insights into mechanisms of endo- and exonuclease DNA processing by mutant forms of human AP endonuclease.Semantic proximity Read ↗

Genetic and biochemical characterization of human AP endonuclease 1 mutants deficient in nucleotide incision repair activity.Semantic proximity Read ↗

Human Ape2 protein has a 3'-5' exonuclease activity that acts preferentially on mismatched base pairs.Semantic proximity Read ↗

Uracil in duplex DNA is a substrate for the nucleotide incision repair pathway in human cellsSemantic proximity Read ↗

Lys98 substitution in human AP endonuclease 1 affects the kinetic mechanism of enzyme action in base excision and nucleotide incision repair pathways.Semantic proximity Read ↗

Processing of oxidatively damaged DNA dirty ends by APE1Semantic proximity Read ↗

Structural comparison of AP endonucleases from the exonuclease III family reveals new amino acid residues in human AP endonuclease 1 that are involved in incision of damaged DNA.Semantic proximity Read ↗

Determinants in nuclease specificity of Ape1 and Ape2, human homologues of Escherichia coli exonuclease III.Semantic proximity Read ↗

Molecular and structural characterization of disease-associated APE1 polymorphisms.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.