Evidence map›Paper›PMID 29718661›Full record

ArticleBiochemistry2018

The Fifth Domain in the G-Quadruplex-Forming Sequence of the Human NEIL3 Promoter Locks DNA Folding in Response to Oxidative Damage.

Carla A Omaga, Aaron M Fleming, Cynthia J Burrows

Abstract read
In one paragraph

Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 27 citations in OpenAlex.

  1. 8-Oxoguanine: A Lesion, an Epigenetic Mark, or a Molecular Signal?International journal of molecular sciences · 2025
    Review
  2. Article
  3. Review
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  5. Article
  6. Article
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  8. The Intertwined Role of 8-oxodG and G4 in Transcription Regulation.International journal of molecular sciences · 2023
    Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. HumanJournal of the American Chemical Society · 2019
    Article
  19. Article
  20. Impact of Oxidative Lesions on the Human Telomeric G-Quadruplex.Journal of the American Chemical Society · 2019
    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

3 authors at 1 institution in 1 country.

Carla A OmagaDepartment of Chemistry , University of Utah , Salt Lake City , Utah 84112-0850 , United States.
Aaron M FlemingDepartment of Chemistry , University of Utah , Salt Lake City , Utah 84112-0850 , United States.ORCID 0000-0002-2000-0310
Cynthia J BurrowsDepartment of Chemistry , University of Utah , Salt Lake City , Utah 84112-0850 , United States.ORCID 0000-0001-7253-8529
University of Utah · US

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI KATHARINE S ULLMAN · 1986 to 2026
$72.6M
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 P30 CA042014NCI NIH HHS R01 CA090689
6 · The paper itself

Abstract

DNA oxidation is an inevitable and usually detrimental process, but the cell is capable of reversing this state because the cell possesses a highly developed set of DNA repair machineries, including the DNA glycosylase NEIL3 that is encoded by the NEIL3 gene. In this work, the G-rich promoter region of the human NEIL3 gene was shown to fold into a dynamic G-quadruplex (G4) structure under nearly physiological conditions using spectroscopic techniques (e.g., nuclear magnetic resonance, circular dichroism, fluorescence, and ultraviolet-visible) and DNA polymerase stop assays. The presence of 8-oxo-7,8-dihydroguanine (OG) modified the properties of the NEIL3 G4 and entailed the recruitment of the fifth domain to function as a "spare tire", in which an undamaged fifth G-track is swapped for the damaged section of the G4. The polymerase stop assay findings also revealed that owing to its dynamic polymorphism, the NEIL3 G4 is more readily bypassed by DNA polymerase I (Klenow fragment) than well-known oncogene G4s are. This study identifies the NEIL3 promoter possessing a G-rich element that can adopt a G4 fold, and when OG is incorporated, the sequence can lock into a more stable G4 fold via recruitment of the fifth track of Gs.

Indexed as

Nucleic Acid ConformationCircular DichroismDNADNA RepairG-QuadruplexesGuanosineHumansN-Glycosyl HydrolasesOxidation-ReductionOxidative StressPromoter Regions, GeneticProtein DomainsTelomereDNAGuanosineNEIL3 protein, humanN-Glycosyl Hydrolases

Identifiers

PMID29718661
PMCPMC6002760
OpenAlexW2800184461

What OpenQuestion holds

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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.