Evidence map›Paper›PMID 28629775›Full record

ReviewDNA repair2017

8-Oxo-7,8-dihydroguanine, friend and foe: Epigenetic-like regulator versus initiator of mutagenesis.

Aaron M Fleming, Cynthia J Burrows

Open access · greenAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in DNA repair, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

80 citing papers in PubMed, 141 citations in OpenAlex.

  1. Article
  2. Review
  3. 8-Oxoguanine: A Lesion, an Epigenetic Mark, or a Molecular Signal?International journal of molecular sciences · 2025
    Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Aberrant Repair of 8-Oxoguanine in Short DNA Bulges.Doklady. Biochemistry and biophysics · 2023
    Article
  19. Review
  20. Article

20 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Aaron M FlemingDepartment of Chemistry, University of Utah, 315 S 1400 East, Salt Lake City, UT 84112-0850, USA. Electronic address: afleming@chem.utah.edu.
Cynthia J BurrowsDepartment of Chemistry, University of Utah, 315 S 1400 East, Salt Lake City, UT 84112-0850, USA. Electronic address: burrows@chem.utah.edu.
University of Utah · US

Funding

Chemistry and Biology of Oxidized Purine Lesions in DNAR01CA090689 · NCI · UNIVERSITY OF UTAH · PI BURROWS, CYNTHIA J, DAVID, SHEILA SUE · 2002 to 2019
$5.5M
NCI NIH HHS R01 CA090689
6 · The paper itself

Abstract

A high flux of reactive oxygen species during oxidative stress results in oxidative modification of cellular components including DNA. Oxidative DNA "damage" to the heterocyclic bases is considered deleterious because polymerases may incorrectly read the modifications causing mutations. A prominent member in this class is the oxidized guanine base 8-oxo-7,8-dihydroguanine (OG) that is moderately mutagenic effecting G→T transversion mutations. Recent reports have identified that formation of OG in G-rich regulatory elements in the promoters of the VEGF, TNFα, and SIRT1 genes can increase transcription via activation of the base excision repair (BER) pathway. Work in our laboratory with the G-rich sequence in the promoter of VEGF concluded that BER drives a shift in structure to a G-quadruplex conformation leading to gene activation in mammalian cells. More specifically, removal of OG from the duplex context by 8-oxoguanine glycosylase 1 (OGG1) produces an abasic site (AP) that destabilizes the duplex, shifting the equilibrium toward the G-quadruplex fold because of preferential extrusion of the AP into a loop. The AP is bound but inefficiently cleaved by apurinic/apyrimidinic endoDNase I (APE1) that likely allows recruitment of activating transcription factors for gene induction. The ability of OG to induce transcription ascribes a regulatory or epigenetic-like role for this oxidatively modified base. We compare OG to the 5-methylcytosine (5mC) epigenetic pathway including its oxidized derivatives, some of which poise genes for transcription while also being substrates for BER. The mutagenic potential of OG to induce only ∼one-third the number of mutations (G→T) compared to deamination of 5mC producing C→T mutations is described. These comparisons blur the line between friendly epigenetic base modifications and those that are foes, i.e. DNA "damage," causing genetic mutations.

Indexed as

DNA DamageDNA RepairEpigenesis, GeneticMutagenesisAnimalsDNADNA Repair EnzymesGuanineHumansPromoter Regions, Genetic8-hydroxyguanineDNADNA Repair EnzymesGuanine8-Oxo-7,8-dihydroguanineBase excision repairEpigeneticsG-quadruplexMutagenesisOxidative stress

Identifiers

PMID28629775
PMCPMC5548303
OpenAlexW2622681512

What OpenQuestion holds

Textmetadata
LicenceTDM
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.