Evidence map›Paper›PMID 30509560›Full record

ArticleDNA repair2019

Human AP-endonuclease (Ape1) activity on telomeric G4 structures is modulated by acetylatable lysine residues in the N-terminal sequence.

Silvia Burra, Daniela Marasco, Matilde Clarissa Malfatti, Giulia Antoniali, Antonella Virgilio, Veronica Esposito, Bruce Demple, Aldo Galeone, Gianluca Tell

Abstract read
In one paragraph

Article in DNA repair, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

40 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
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  5. 8-Oxoguanine: A Lesion, an Epigenetic Mark, or a Molecular Signal?International journal of molecular sciences · 2025
    Review
  6. Review
  7. Article
  8. Position-Dependent Effects of AP Sites Within anInternational journal of molecular sciences · 2025
    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

9 authors at 3 institutions in 2 countries.

Silvia BurraLaboratory of Molecular Biology and DNA Repair, Department of Medicine (DAME), University of Udine, Udine, Italy.
Daniela MarascoDepartment of Pharmacy, University of Naples "Federico II", Via D. Montesano 49, 80131, Naples, Italy.
Matilde Clarissa MalfattiLaboratory of Molecular Biology and DNA Repair, Department of Medicine (DAME), University of Udine, Udine, Italy.
Giulia AntonialiLaboratory of Molecular Biology and DNA Repair, Department of Medicine (DAME), University of Udine, Udine, Italy.
Antonella VirgilioDepartment of Pharmacy, University of Naples "Federico II", Via D. Montesano 49, 80131, Naples, Italy.
Veronica EspositoDepartment of Pharmacy, University of Naples "Federico II", Via D. Montesano 49, 80131, Naples, Italy.
Bruce DempleDepartment of Pharmacological Sciences, Stony Brook University, School of Medicine, Stony Brook, NY, 11794-8651, USA.
Aldo GaleoneDepartment of Pharmacy, University of Naples "Federico II", Via D. Montesano 49, 80131, Naples, Italy.
Gianluca TellLaboratory of Molecular Biology and DNA Repair, Department of Medicine (DAME), University of Udine, Udine, Italy. Electronic address: gianluca.tell@uniud.it.
University of Naples Federico II · ITUniversity of Udine · ITStony Brook University · US

Funding

The Ape1-NPM1 Axis and Telomere MaintenanceR21CA191856 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI DEMPLE, BRUCE F. · 2016 to 2017
$374k
NCI NIH HHS R21 CA191856
6 · The paper itself

Abstract

Loss of telomeres stability is a hallmark of cancer cells. Exposed telomeres are prone to aberrant end-joining reactions leading to chromosomal fusions and translocations. Human telomeres contain repeated TTAGGG elements, in which the 3' exposed strand may adopt a G-quadruplex (G4) structure. The guanine-rich regions of telomeres are hotspots for oxidation forming 8-oxoguanine, a lesion that is handled by the base excision repair (BER) pathway. One key player of this pathway is Ape1, the main human endonuclease processing abasic sites. Recent evidences showed an important role for Ape1 in telomeric physiology, but the molecular details regulating Ape1 enzymatic activities on G4-telomeric sequences are lacking. Through a combination of in vitro assays, we demonstrate that Ape1 can bind and process different G4 structures and that this interaction involves specific acetylatable lysine residues (i.e. K

Indexed as

G-QuadruplexesAcetylationCell Line, TumorDNA-(Apurinic or Apyrimidinic Site) LyaseHumansLysineNucleophosminOsmolar ConcentrationTelomereAPEX1 protein, humanDNA-(Apurinic or Apyrimidinic Site) LyaseLysineNPM1 protein, humanNucleophosminAbasic sitesAcetylationApe1G4 structureNPM1Telomeres

Identifiers

PMID30509560
PMCPMC6420783
OpenAlexW2901464742

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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.