Evidence map›Paper›PMID 23612479›Full record

ArticleFree radical biology & medicine2013

8-Oxoguanine DNA glycosylase-1 links DNA repair to cellular signaling via the activation of the small GTPase Rac1.

Gyorgy Hajas, Attila Bacsi, Leopoldo Aguilera-Aguirre, Muralidhar L Hegde, K Hazra Tapas, Sanjiv Sur, Zsolt Radak, Xueqing Ba, Istvan Boldogh

Open access · bronzeAbstract read
In one paragraph

Article in Free radical biology & medicine, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

45 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. 8-Oxoguanine: A Lesion, an Epigenetic Mark, or a Molecular Signal?International journal of molecular sciences · 2025
    Review
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  14. Review
  15. Short-duration hyperoxia causes genotoxicity in mouse lungs: protection by volatile anesthetic isoflurane.American journal of physiology. Lung cellular and molecular physiology · 2019
    Article
  16. The roles of base excision repair enzyme OGG1 in gene expression.Cellular and molecular life sciences : CMLS · 2018
    Review
  17. Article
  18. Article
  19. Review
  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

9 authors at 1 institution in 1 country.

Gyorgy HajasDepartment of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, TX 77555, USA.
Attila BacsiDepartment of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, TX 77555, USA.
Leopoldo Aguilera-AguirreDepartment of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, TX 77555, USA.
Muralidhar L HegdeDepartment of Biochemistry & Molecular Biology, University of Texas Medical Branch at Galveston, Galveston, TX 77555, USA.
K Hazra TapasDepartment of Internal Medicine, University of Texas Medical Branch at Galveston, Galveston, TX 77555, USA; Sealy Center for Molecular Medicine, University of Texas Medical Branch at Galveston, Galveston, TX 77555, USA; Department of Biochemistry & Molecular Biology, University of Texas Medical Branch at Galveston, Galveston, TX 77555, USA.
Sanjiv SurDepartment of Internal Medicine, University of Texas Medical Branch at Galveston, Galveston, TX 77555, USA; Sealy Center for Molecular Medicine, University of Texas Medical Branch at Galveston, Galveston, TX 77555, USA.
Zsolt RadakDepartment of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, TX 77555, USA.
Xueqing BaDepartment of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, TX 77555, USA.
Istvan BoldoghDepartment of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, TX 77555, USA; Sealy Center for Molecular Medicine, University of Texas Medical Branch at Galveston, Galveston, TX 77555, USA. Electronic address: sboldogh@utmb.edu.
The University of Texas Medical Branch at Galveston · US

Funding

Virus, Tissue Culture and ImmunoassayP01AI062885 · NIAID · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI GAROFALO, ROBERTO P · 2005 to 2022
$23.9M
Synthetic Organic Chemistry CoreP30ES006676 · NIEHS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI ELFERINK, CORNELIS JOHAN · 1995 to 2017
$21.7M
Molecular Mechanisms of Environmental InjuryT32ES007254 · NIEHS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI AMEREDES, BILL T · 1990 to 2022
$6.6M
OXIDATIVE STRESS,REPAIR OF OXIDIZED GUANINES IN AGED CELLSP01AG021830 · NIA · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI PAPACONSTANTINOU, JOHN NMN · 2004 to 2010
$6.4M
Preferential single-strand break repair in the active genes of mammalian cellsR01NS073976 · NINDS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI HAZRA, TAPAS K · 2012 to 2021
$3.3M
Linkage of Lung Inflammation to 8-oxoguanine and OGG1R01ES018948 · NIEHS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI BOLDOGH, ISTVAN STEVEN · 2010 to 2014
$1.5M
NIAID NIH HHS AI062885NIAID NIH HHS P01 AI062885NIA NIH HHS AG021830NIA NIH HHS P01 AG021830NIEHS NIH HHS P30 ES006676NIEHS NIH HHS R01 ES018948NIEHS NIH HHS R01ES018948NIEHS NIH HHS T32 ES007254NIEHS NIH HHS T32ES007254NINDS NIH HHS R01 NS073976NINDS NIH HHS R01NS073976
6 · The paper itself

Abstract

8-Oxo-7,8-dihydroguanine (8-oxoG) is one of the most abundant DNA base lesions induced by reactive oxygen species (ROS). Accumulation of 8-oxoG in the mammalian genome is considered a marker of oxidative stress, to be causally linked to inflammation, and is thought to contribute to aging processes and various aging-related diseases. Unexpectedly, mice that lack 8-oxoguanine DNA glycosylase-1 (OGG1) activity and accumulate 8-oxoG in their genome have a normal phenotype and longevity; in fact, they show increased resistance to both inflammation and oxidative stress. OGG1 excises and generates free 8-oxoG base during DNA base-excision repair (BER) processes. In the present study, we report that in the presence of the 8-oxoG base, OGG1 physically interacts with guanine nucleotide-free and GDP-bound Rac1 protein. This interaction results in rapid GDP→GTP, but not GTP→GDP, exchange in vitro. Importantly, a rise in the intracellular 8-oxoG base levels increases the proportion of GTP-bound Rac1. In turn Rac1-GTP mediates an increase in ROS levels via nuclear membrane-associated NADPH oxidase type 4. These results show a novel mechanism by which OGG1 in complex with 8-oxoG is linked to redox signaling and cellular responses.

Indexed as

DNA RepairSignal TransductionAnimalsDNA GlycosylasesFemaleGuanineMiceMice, Inbred BALB CNADPH Oxidase 4NADPH OxidasesNeuropeptidesrac1 GTP-Binding ProteinReactive Oxygen Species8-hydroxyguanineDNA GlycosylasesGuanineNADPH Oxidase 4NADPH OxidasesNeuropeptidesNox4 protein, mouseOgg1 protein, mouserac1 GTP-Binding ProteinRac1 protein, mouseReactive Oxygen Species8-Oxoguanine8-Oxoguanine DNA glycosylase-1Rac1 GTPase

Identifiers

PMID23612479
PMCPMC3795866
OpenAlexW2165079456

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.