Evidence map›Paper›PMID 28575236›Full record

ArticleNucleic acids research2017

Monitoring of the spatial and temporal dynamics of BER/SSBR pathway proteins, including MYH, UNG2, MPG, NTH1 and NEIL1-3, during DNA replication.

Karine Ø Bj Rås, Mirta M L Sousa, Animesh Sharma, Davi M Fonseca, Caroline K S Gaard, Magnar Bj Rås, Marit Otterlei

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Research progress on the role of the NEIL family in cancer.Frontiers in cell and developmental biology · 2025
    Review
  2. Article
  3. Article
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  5. Article
  6. Article
  7. Review
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  9. The complexity and regulation of repair of alkylation damage to nucleic acids.Critical reviews in biochemistry and molecular biology · 2021
    Review
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  11. Article
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  15. Article
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  18. CREBBP and p300 lysine acetyl transferases in the DNA damage response.Cellular and molecular life sciences : CMLS · 2018
    Review
  19. 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

7 authors at 1 institution in 1 country.

Karine Ø Bj RåsDepartment of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology (NTNU), N-7491 Trondheim, Norway.
Mirta M L SousaDepartment of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology (NTNU), N-7491 Trondheim, Norway.
Animesh SharmaDepartment of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology (NTNU), N-7491 Trondheim, Norway.
Davi M FonsecaDepartment of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology (NTNU), N-7491 Trondheim, Norway.
Caroline K S GaardDepartment of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology (NTNU), N-7491 Trondheim, Norway.
Magnar Bj RåsDepartment of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology (NTNU), N-7491 Trondheim, Norway.
Marit OtterleiDepartment of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology (NTNU), N-7491 Trondheim, Norway.
Norwegian University of Science and Technology · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Base lesions in DNA can stall the replication machinery or induce mutations if bypassed. Consequently, lesions must be repaired before replication or in a post-replicative process to maintain genomic stability. Base excision repair (BER) is the main pathway for repair of base lesions and is known to be associated with DNA replication, but how BER is organized during replication is unclear. Here we coupled the iPOND (isolation of proteins on nascent DNA) technique with targeted mass-spectrometry analysis, which enabled us to detect all proteins required for BER on nascent DNA and to monitor their spatiotemporal orchestration at replication forks. We demonstrate that XRCC1 and other BER/single-strand break repair (SSBR) proteins are enriched in replisomes in unstressed cells, supporting a cellular capacity of post-replicative BER/SSBR. Importantly, we identify for the first time the DNA glycosylases MYH, UNG2, MPG, NTH1, NEIL1, 2 and 3 on nascent DNA. Our findings suggest that a broad spectrum of DNA base lesions are recognized and repaired by BER in a post-replicative process.

Indexed as

DNA Breaks, Single-StrandedDNA RepairDNA ReplicationCell Line, TumorDeoxyribonuclease (Pyrimidine Dimer)DNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA-Binding ProteinsDNA GlycosylasesDNA Repair EnzymesHEK293 CellsHeLa CellsHumansImmunoblottingMass SpectrometryN-Glycosyl HydrolasesCCNO protein, humanDeoxyribonuclease (Pyrimidine Dimer)DNADNA-3-methyladenine glycosidase IIDNA-(Apurinic or Apyrimidinic Site) LyaseDNA-Binding ProteinsDNA GlycosylasesDNA Repair EnzymesmutY adenine glycosylaseNEIL1 protein, humanNEIL2 protein, humanNEIL3 protein, humanN-Glycosyl HydrolasesNTHL1 protein, humanX-ray Repair Cross Complementing Protein 1XRCC1 protein, human

Identifiers

PMID28575236
PMCPMC5737410
OpenAlexW2617348801

What OpenQuestion holds

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Registered trials

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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.