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

Characterization of the endoribonuclease active site of human apurinic/apyrimidinic endonuclease 1.

Journal of molecular biology - 2 Sept 2011

Kim Wan-Cheol, Berquist Brian R, Chohan Manbir, Uy Christopher, Wilson David M, Lee Chow H

Abstract excerpt

Apurinic/apyrimidinic endonuclease 1 (APE1) is the major mammalian enzyme in DNA base excision repair that cleaves the DNA phosphodiester backbone immediately 5' to abasic sites. Recently, we identified APE1 as an endoribonuclease that cleaves a specific coding region of c-myc mRNA in vitro, regulating c-myc mRNA level and half-life in cells. Here, we further characterized the endoribonuclease activity of APE1,...

Read the complete abstract on PubMed

Topics

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

Share to Catalytic Domain
Share to DNA-(Apurinic or Apyrimidinic Site) Lyase

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Electrophoretic Mobility Shift Assay

Share to Endoribonucleases

Share to Hydrolysis

Share to Proto-Oncogene Proteins c-myc

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 21762700
DOI: 10.1016/j.jmb.2011.06.050
PMCID: PMC4598366

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of the endoribonuclease active site of human apurinic/apyrimidinic endonuclease 1.PMID 21762700Read ↗

Human Apurinic/Apyrimidinic Endonuclease 1Semantic proximity Read ↗

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

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

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

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

Posttranslational modification of mammalian AP endonuclease (APE1)Semantic proximity Read ↗

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

Processing of oxidatively damaged DNA dirty ends by APE1Semantic 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 ↗

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

Structure and function of apurinic/apyrimidinic endonucleasesSemantic proximity Read ↗

Functional characterization of Ape1 variants identified in the human population.Semantic proximity Read ↗

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