Evidence map›Paper›PMID 33925271›Full record

ArticleInternational journal of molecular sciences2021

NEIL1 and NEIL2 Are Recruited as Potential Backup for OGG1 upon OGG1 Depletion or Inhibition by TH5487.

Bishoy M F Hanna, Maurice Michel, Thomas Helleday, Oliver Mortusewicz

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Action-at-a-distance mutations by 8-oxo-7,8-dihydroguanine: adenine pair triggered by MUTYH.Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2025
    Article
  5. Review
  6. Research progress on the role of the NEIL family in cancer.Frontiers in cell and developmental biology · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. OGG1 in the Kidney: Beyond Base Excision Repair.Oxidative medicine and cellular longevity · 2022
    Review
  14. 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

4 authors at 1 institution in 2 countries.

Bishoy M F HannaScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, 171 65 Stockholm, Sweden.ORCID 0000-0001-7027-6553
Maurice MichelScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, 171 65 Stockholm, Sweden.ORCID 0000-0003-3261-2493
Thomas HelledayScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, 171 65 Stockholm, Sweden.
Oliver MortusewiczScience for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, 171 65 Stockholm, Sweden.ORCID 0000-0002-4290-4994
Science for Life Laboratory · SE

Funding

Barncancerfonden BCF PR2018-0095Horizon 2020 Framework Programme 722729The European Research Council ERC-AdG-695376The European Research Council TAROX ProgrammeThe Helleday foundation n.a.The Swedish Cancer Society CAN2018/0658The Swedish Research Council 2015-00162The Torsten and Ragnar Söderberg Foundation n.a.
6 · The paper itself

Abstract

DNA damage caused by reactive oxygen species may result in genetic mutations or cell death. Base excision repair (BER) is the major pathway that repairs DNA oxidative damage in order to maintain genomic integrity. In mammals, eleven DNA glycosylases have been reported to initiate BER, where each recognizes a few related DNA substrate lesions with some degree of overlapping specificity. 7,8-dihydro-8-oxoguanine (8-oxoG), one of the most abundant DNA oxidative lesions, is recognized and excised mainly by 8-oxoguanine DNA glycosylase 1 (OGG1). Further oxidation of 8-oxoG generates hydantoin lesions, which are recognized by NEIL glycosylases. Here, we demonstrate that NEIL1, and to a lesser extent NEIL2, can potentially function as backup BER enzymes for OGG1 upon pharmacological inhibition or depletion of OGG1. NEIL1 recruitment kinetics and chromatin binding after DNA damage induction increase in cells treated with OGG1 inhibitor TH5487 in a dose-dependent manner, whereas NEIL2 accumulation at DNA damage sites is prolonged following OGG1 inhibition. Furthermore, depletion of OGG1 results in increased retention of NEIL1 and NEIL2 at damaged chromatin. Importantly, oxidatively stressed NEIL1- or NEIL2-depleted cells show excessive genomic 8-oxoG lesions accumulation upon OGG1 inhibition, suggesting a prospective compensatory role for NEIL1 and NEIL2. Our study thus exemplifies possible backup mechanisms within the base excision repair pathway.

Indexed as

BenzimidazolesCell LineDNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA DamageDNA GlycosylasesDNA RepairGuanineHumansKineticsMutationOxidative StressPiperidinesProspective StudiesReactive Oxygen Species8-hydroxyguanineBenzimidazolesDNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA GlycosylasesGuanineNEIL1 protein, humanNEIL2 protein, humanoxoguanine glycosylase 1, humanPiperidinesReactive Oxygen SpeciesTH54878-oxoguaninebackup pathwaybase excision repairchromatin binding dynamicsDNA oxidative damageNEIL1 glycosylaseNEIL2OGG1 inhibitorrecruitment kineticsTH5487

Identifiers

PMID33925271
PMCPMC8123590
OpenAlexW3158465240

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.