Evidence map›Paper›PMID 19029246›Full record

ArticleMolecular and cellular biology2009

Dynamic compartmentalization of base excision repair proteins in response to nuclear and mitochondrial oxidative stress.

Lyra M Griffiths, Dan Swartzlander, Kellen L Meadows, Keith D Wilkinson, Anita H Corbett, Paul W Doetsch

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

25 citing papers in PubMed, 47 citations in OpenAlex.

  1. Artificial targeting of the NEIL1 DNA glycosylase to the mitochondria.Environmental and molecular mutagenesis · 2024
    Article
  2. Article
  3. Article
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  5. In vivo measurements of interindividual differences in DNA glycosylases and APE1 activities.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Protecting the mitochondrial powerhouse.Trends in cell biology · 2015
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  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

6 authors at 4 institutions in 3 countries.

Lyra M GriffithsDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
Dan Swartzlander
Kellen L Meadows
Keith D Wilkinson
Anita H Corbett
Paul W Doetsch
Cancer Institute (WIA) · INEmory Healthcare · USEmory University · USInstitut thématique Génétique, génomique et bioinformatique · FR

Funding

Resistance to UV Damage: Role of Gene RegulationP01ES011163 · NIEHS · EMORY UNIVERSITY · PI DOETSCH, PAUL WILLIAM · 2002 to 2012
$12.6M
PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM008490 · NIGMS · EMORY UNIVERSITY · PI BOSS, JEREMY M. · 1993 to 2022
$8.0M
MOLECULAR BASIS OF RAN MEDIATED NUCLEAR TRANSPORTR01GM058728 · NIGMS · EMORY UNIVERSITY · PI CORBETT, ANITA H. · 1999 to 2016
$5.4M
Functions of Ub-like Proteins &Processing ProteasesR01GM066355 · NIGMS · EMORY UNIVERSITY · PI WILKINSON, KEITH D · 2002 to 2009
$2.5M
NIEHS NIH HHS ES 011163NIEHS NIH HHS P01 ES011163NIGMS NIH HHS GM008490NIGMS NIH HHS GM0 58728NIGMS NIH HHS GM066355NIGMS NIH HHS R01 GM058728NIGMS NIH HHS R01 GM066355NIGMS NIH HHS T32 GM008490
6 · The paper itself

Abstract

DNAs harbored in both nuclei and mitochondria of eukaryotic cells are subject to continuous oxidative damage resulting from normal metabolic activities or environmental insults. Oxidative DNA damage is primarily reversed by the base excision repair (BER) pathway, initiated by N-glycosylase apurinic/apyrimidinic (AP) lyase proteins. To execute an appropriate repair response, BER components must be distributed to accommodate levels of genotoxic stress that may vary considerably between nuclei and mitochondria, depending on the growth state and stress environment of the cell. Numerous examples exist where cells respond to signals, resulting in relocalization of proteins involved in key biological transactions. To address whether such dynamic localization contributes to efficient organelle-specific DNA repair, we determined the intracellular localization of the Saccharomyces cerevisiae N-glycosylase/AP lyases, Ntg1 and Ntg2, in response to nuclear and mitochondrial oxidative stress. Fluorescence microscopy revealed that Ntg1 is differentially localized to nuclei and mitochondria, likely in response to the oxidative DNA damage status of the organelle. Sumoylation is associated with targeting of Ntg1 to nuclei containing oxidative DNA damage. These studies demonstrate that trafficking of DNA repair proteins to organelles containing high levels of oxidative DNA damage may be a central point for regulating BER in response to oxidative stress.

Indexed as

DNA RepairOxidative StressAmino Acid SequenceAntimycin ACell CompartmentationCell NucleusDNA-(Apurinic or Apyrimidinic Site) LyaseDNA DamageHydrogen PeroxideMethyl MethanesulfonateMitochondriaModels, BiologicalMolecular Sequence DataMutant ProteinsOxygenProtein Processing, Post-TranslationalantimycinAntimycin ADNA-(Apurinic or Apyrimidinic Site) LyaseHydrogen PeroxideMethyl MethanesulfonateMutant ProteinsNTG1 protein, S cerevisiaeNTG2 protein, S cerevisiaeOxygenSaccharomyces cerevisiae ProteinsSmall Ubiquitin-Related Modifier Proteins

Identifiers

PMID19029246
PMCPMC2630693
OpenAlexW2121569061

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.