Evidence map›Paper›PMID 22568941›Full record

ArticleThe Journal of biological chemistry2012

Activation of ras signaling pathway by 8-oxoguanine DNA glycosylase bound to its excision product, 8-oxoguanine.

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

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed, 1 pooled it
6.0field-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

73 citing papers in PubMed, 1 synthesis or guideline pooled it, 129 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. 8-Oxoguanine: A Lesion, an Epigenetic Mark, or a Molecular Signal?International journal of molecular sciences · 2025
    Review
  4. Article
  5. Review
  6. Review
  7. Hormesis and Muscle Plasticity.Advances in experimental medicine and biology · 2025
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. OGG1 in Lung-More than Base Excision Repair.Antioxidants (Basel, Switzerland) · 2022
    Review
  13. Article
  14. OGG1 in the Kidney: Beyond Base Excision Repair.Oxidative medicine and cellular longevity · 2022
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article

13 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

9 authors at 1 institution in 1 country.

Istvan BoldoghDepartment of Microbiology and Immunology, University of Texas Medical Branch,Galveston, Texas 77555, USA.
Gyorgy Hajas
Leopoldo Aguilera-Aguirre
Muralidhar L Hegde
Zsolt Radak
Attila Bacsi
Sanjiv Sur
Tapas K Hazra
Sankar Mitra
The University of Texas Medical Branch at Galveston · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
Virus, Tissue Culture and ImmunoassayP01AI062885 · NIAID · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI CASOLA, ANTONELLA · 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
Repair of Oxidized Bases in Mammalian GenomesR01CA081063 · NCI · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI MITRA, SANKAR · 1999 to 2012
$3.1M
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
NCI NIH HHS P01 CA092584NCI NIH HHS R01 CA081063NCI NIH HHS R01CA81063NHLBI NIH HHS N01HV00245NIAID NIH HHS P01 AI062885NIEHS NIH HHS P30 ES006676NIEHS NIH HHS R01 ES018948NIEHS NIH HHS T32ES007254PHS HHS 021830PHS HHS NIAID/AI062885-01
6 · The paper itself

Abstract

8-Oxo-7,8-dihydroguanine (8-oxoG), arguably the most abundant base lesion induced in mammalian genomes by reactive oxygen species, is repaired via the base excision repair pathway that is initiated with the excision of 8-oxoG by OGG1. Here we show that OGG1 binds the 8-oxoG base with high affinity and that the complex then interacts with canonical Ras family GTPases to catalyze replacement of GDP with GTP, thus serving as a guanine nuclear exchange factor. OGG1-mediated activation of Ras leads to phosphorylation of the mitogen-activated kinases MEK1,2/ERK1,2 and increasing downstream gene expression. These studies document for the first time that in addition to its role in repairing oxidized purines, OGG1 has an independent guanine nuclear exchange factor activity when bound to 8-oxoG.

Indexed as

DNA GlycosylasesDNA RepairFibroblastsGenome, HumanGuanineGuanosine DiphosphateGuanosine TriphosphateHeLa CellsHumansMAP Kinase Signaling SystemMitogen-Activated Protein Kinase KinasesPhosphorylationras Proteins8-hydroxyguanineDNA GlycosylasesGuanineGuanosine DiphosphateGuanosine TriphosphateMitogen-Activated Protein Kinase Kinasesoxoguanine glycosylase 1, humanras Proteins

Identifiers

PMID22568941
PMCPMC3375501
OpenAlexW2043020194

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.