Evidence map›Paper›PMID 23776569›Full record

ArticlePloS one2013

Functional assessment of population and tumor-associated APE1 protein variants.

Jennifer L Illuzzi, Nicole A Harris, Brittney A Manvilla, Daemyung Kim, Mengxia Li, Alexander C Drohat, David M Wilson

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.2field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 33 citations in OpenAlex.

  1. The Link Between Human Alkyladenine DNA Glycosylase and Cancer Development.International journal of molecular sciences · 2025
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  16. Base excision repair of oxidative DNA damage: from mechanism to disease.Frontiers in bioscience (Landmark edition) · 2017
    Review
  17. Review
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  19. Capturing snapshots of APE1 processing DNA damage.Nature structural & molecular biology · 2015
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

Jennifer L IlluzziLaboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health, Baltimore, Maryland, United States of America.
Nicole A Harris
Brittney A Manvilla
Daemyung Kim
Mengxia Li
Alexander C Drohat
David M Wilson
National Institutes of Health · USUniversity of Maryland, Baltimore · USCheongju University · KRSanford Burnham Prebys Medical Discovery Institute · US

Funding

MULTIDISCIPLINARY CARDIAC SCIENCEST32HL007381 · NHLBI · UNIVERSITY OF CHICAGO · PI JEANNE M DECARA, Yoav Gilad · 1985 to 2026
$12.5M
Base Excision DNA Repair in Disease Susceptibility and TreatmentZIAAG000750 · NIA · NATIONAL INSTITUTE ON AGING · PI BOHR, VILHELM A · 2009 to 2019
$5.4M
Structure and Mechanism of CpG specific DNA glycosylasesR01GM072711 · NIGMS · WADSWORTH CENTER · PI DROHAT, ALEX C · 2005 to 2020
$5.0M
Graduate Training at The Chemistry Biology InterfaceT32GM066706 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI SELEY-RADTKE, KATHERINE L, SMITH, AARON T · 2004 to 2023
$3.3M
Intramural NIH HHSNHLBI NIH HHS T32 HL007381NIGMS NIH HHS R01 GM072711NIGMS NIH HHS R01-GM72711NIGMS NIH HHS T32 GM066706NIGMS NIH HHS T32GM 066706-07
6 · The paper itself

Abstract

Apurinic/apyrimidinic endonuclease 1 (APE1) is the predominant AP site repair enzyme in mammals. APE1 also maintains 3'-5' exonuclease and 3'-repair activities, and regulates transcription factor DNA binding through its REF-1 function. Since complete or severe APE1 deficiency leads to embryonic lethality and cell death, it has been hypothesized that APE1 protein variants with slightly impaired function will contribute to disease etiology. Our data indicate that except for the endometrial cancer-associated APE1 variant R237C, the polymorphic variants Q51H, I64V and D148E, the rare population variants G241R, P311S and A317V, and the tumor-associated variant P112L exhibit normal thermodynamic stability of protein folding; abasic endonuclease, 3'-5' exonuclease and REF-1 activities; coordination during the early steps of base excision repair; and intracellular distribution when expressed exogenously in HeLa cells. The R237C mutant displayed reduced AP-DNA complex stability, 3'-5' exonuclease activity and 3'-damage processing. Re-sequencing of the exonic regions of APE1 uncovered no novel amino acid substitutions in the 60 cancer cell lines of the NCI-60 panel, or in HeLa or T98G cancer cell lines; only the common D148E and Q51H variants were observed. Our results indicate that APE1 missense mutations are seemingly rare and that the cancer-associated R237C variant may represent a reduced-function susceptibility allele.

Indexed as

Amino Acid SubstitutionCell Line, TumorDNA-(Apurinic or Apyrimidinic Site) LyaseDNA RepairEndometrial NeoplasmsFemaleHeLa CellsHumansMutationMutation, MissenseNeoplasmsSubstrate SpecificityAPEX1 protein, humanDNA-(Apurinic or Apyrimidinic Site) Lyase

Identifiers

PMID23776569
PMCPMC3679070
OpenAlexW2106422943

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.