Evidence map›Paper›PMID 26338705›Full record

ArticleThe Journal of biological chemistry2015

Formation and Repair of Mismatches Containing Ribonucleotides and Oxidized Bases at Repeated DNA Sequences.

Piera Cilli, Anna Minoprio, Cecilia Bossa, Margherita Bignami, Filomena Mazzei

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

24 citing papers in PubMed, 29 citations in OpenAlex.

  1. Ribonucleotide errors, RNase HII, and ribonucleotide excision repair.Critical reviews in biochemistry and molecular biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
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  9. RNA: a double-edged sword in genome maintenance.Nature reviews. Genetics · 2020
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Unlike theThe Journal of biological chemistry · 2019
    Article
  15. Article
  16. Current perspectives on mechanisms of ribonucleotide incorporation and processing in mammalian DNA.Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2019
    Review
  17. Ribonucleotide discrimination by translesion synthesis DNA polymerases.Critical reviews in biochemistry and molecular biology · 2018
    Review
  18. Article
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

Piera CilliFrom the Department of Environment and Primary Prevention, Istituto Superiore di Sanità, 00161 Roma and the Department of Science, University Roma Tre, 00154 Roma, Italy.
Anna MinoprioFrom the Department of Environment and Primary Prevention, Istituto Superiore di Sanità, 00161 Roma and.
Cecilia BossaFrom the Department of Environment and Primary Prevention, Istituto Superiore di Sanità, 00161 Roma and.
Margherita BignamiFrom the Department of Environment and Primary Prevention, Istituto Superiore di Sanità, 00161 Roma and margherita.bignami@gmail.com.
Filomena MazzeiFrom the Department of Environment and Primary Prevention, Istituto Superiore di Sanità, 00161 Roma and.
Roma Tre University · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cellular pool of ribonucleotide triphosphates (rNTPs) is higher than that of deoxyribonucleotide triphosphates. To ensure genome stability, DNA polymerases must discriminate against rNTPs and incorporated ribonucleotides must be removed by ribonucleotide excision repair (RER). We investigated DNA polymerase β (POL β) capacity to incorporate ribonucleotides into trinucleotide repeated DNA sequences and the efficiency of base excision repair (BER) and RER enzymes (OGG1, MUTYH, and RNase H2) when presented with an incorrect sugar and an oxidized base. POL β incorporated rAMP and rCMP opposite 7,8-dihydro-8-oxoguanine (8-oxodG) and extended both mispairs. In addition, POL β was able to insert and elongate an oxidized rGMP when paired with dA. We show that RNase H2 always preserves the capacity to remove a single ribonucleotide when paired to an oxidized base or to incise an oxidized ribonucleotide in a DNA duplex. In contrast, BER activity is affected by the presence of a ribonucleotide opposite an 8-oxodG. In particular, MUTYH activity on 8-oxodG:rA mispairs is fully inhibited, although its binding capacity is retained. This results in the reduction of RNase H2 incision capability of this substrate. Thus complex mispairs formed by an oxidized base and a ribonucleotide can compromise BER and RER in repeated sequences.

Indexed as

Base Pair MismatchDNADNA Polymerase betaOxidation-ReductionRibonucleotidesDNADNA Polymerase betaRibonucleotides8-oxoguanine (8-oxoG)8-oxoguanine glycosylase (OGG1)DNA damageDNA polymeraseDNA repairmutY homolog (MUTYH)ribonuclease

Identifiers

PMID26338705
PMCPMC4646274
OpenAlexW1786470925

What OpenQuestion holds

Textmetadata
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.