Evidence map›Paper›PMID 40427542›Full record

ArticleBiomolecules2025

Mechanisms of DNA Damage Recognition by UDG and PARP1 in the Nucleosome.

Safwen Ghediri, Parvathy A P Sarma, Vinnarasi Saravanan, Corinne Abbadie, Ralf Blossey, Fabrizio Cleri

Abstract read
In one paragraph

Article in Biomolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. Molecular basis of nick ligation in the nucleosome by DNA Ligase IIIα.bioRxiv : the preprint server for biology · 2026
    Article
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

6 authors.

Safwen GhediriUniversité de Lille, Institut d'Electronique Microelectronique et Nanotechnologie (IEMN CNRS, UMR8520) and Département de Physique, F59652 Villeneuve d'Ascq, France.
Parvathy A P SarmaUniversité de Lille, Institut d'Electronique Microelectronique et Nanotechnologie (IEMN CNRS, UMR8520) and Département de Physique, F59652 Villeneuve d'Ascq, France.ORCID 0009-0004-4684-1910
Vinnarasi SaravananUniversité de Lille, Unité de Glycobiologie Structurale et Fonctionnelle (UGSF CNRS UMR8576), F59000 Lille, France.ORCID 0000-0002-8822-5399
Corinne AbbadieUniversité de Lille, CNRS UMR9020 and Inserm U1277-CANTHER-Cancer Heterogeneity, Plasticity and Resistance to Therapies, F59000 Lille, France.ORCID 0000-0002-8174-2393
Ralf BlosseyUniversité de Lille, Unité de Glycobiologie Structurale et Fonctionnelle (UGSF CNRS UMR8576), F59000 Lille, France.ORCID 0000-0002-4823-7037
Fabrizio CleriUniversité de Lille, Institut d'Electronique Microelectronique et Nanotechnologie (IEMN CNRS, UMR8520) and Département de Physique, F59652 Villeneuve d'Ascq, France.ORCID 0000-0003-0272-7441

Funding

ANR Agence Nationale de la Recherche ANR-21-CE45-0032Université de Lille PEARL H2020 Marie-Sklodowska-Curie 847568
6 · The paper itself

Abstract

The DNA base-excision repair (BER) pathway shares the second part of its enzymatic chain with the single-strand break (SSB) repair pathway. BER is initiated by a glycosylase, such as UDG, while SSBR is initiated by the multifunctional enzyme PARP1. The very early steps in the identification of the DNA damage are crucial to the correct initiation of the repair chains, and become even more complex when considering the realistic environment of damage to the DNA in the nucleosome. We performed molecular dynamics computer simulations of the interaction between the glycosylase UDG and a mutated uracil (as could result from oxidative deamination of cytosine), and between the Zn1-Zn2 fragment of PARP1 and a simulated SSB. The model system is a whole nucleosome in which DNA damage is inserted at various typical positions along the 145-bp sequence. It is shown that damage recognition by the enzymes requires very strict conditions, unlikely to be matched by pure random search along the DNA. We propose that mechanical deformation of the DNA around the defective sites may help signaling the presence of the defect, accelerating the search process.

Indexed as

DNA DamageNucleosomesPoly (ADP-Ribose) Polymerase-1Uracil-DNA GlycosidaseDNADNA RepairHumansMolecular Dynamics SimulationProtein BindingDNANucleosomesPARP1 protein, humanPoly (ADP-Ribose) Polymerase-1Uracil-DNA GlycosidaseDNA damageDNA repairMolecular dynamicsNucleosomeSingle-strand breakUracil base excision

Identifiers

PMID40427542
PMCPMC12108792

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.