Evidence map›Paper›PMID 21601577›Full record

ArticleJournal of molecular biology2011

Escherichia coli Fpg glycosylase is nonrendundant and required for the rapid global repair of oxidized purine and pyrimidine damage in vivo.

Brandy J Schalow, Charmain T Courcelle, Justin Courcelle

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

15 citing papers in PubMed, 27 citations in OpenAlex.

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  8. Evaluation of oxidative stress responses in human circulating blood cells after imatinib mesylate treatment - Implications to its mechanism of action.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2019
    Article
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  11. UvrA expression ofJournal of food science and technology · 2017
    Article
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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.

Brandy J SchalowDepartment of Biology, Portland State University, PO Box 751, Portland, OR 97207, USA. brans@pdx.edu
Charmain T Courcelle
Justin Courcelle
Portland State University · US

Funding

R15 AREA: Replication in the Presence of Oxidative DNA damageR15ES021594 · NIEHS · PORTLAND STATE UNIVERSITY · PI COURCELLE, JUSTIN · 2012 to 2012
$437k
Transcription-coupled repair of Oxidative DNA damage in vivoR21ES018940 · NIEHS · PORTLAND STATE UNIVERSITY · PI COURCELLE, JUSTIN · 2010 to 2011
$398k
NIEHS NIH HHS 1R21ES018940-1NIEHS NIH HHS R15 ES021594NIEHS NIH HHS R21 ES018940
6 · The paper itself

Abstract

Endonuclease (Endo) III and formamidopyrimidine-N-glycosylase (Fpg) are two of the predominant DNA glycosylases in Escherichia coli that remove oxidative base damage. In cell extracts and purified form, Endo III is generally more active toward oxidized pyrimidines, while Fpg is more active towards oxidized purines. However, the substrate specificities of these enzymes partially overlap in vitro. Less is known about the relative contribution of these enzymes in restoring the genomic template following oxidative damage. In this study, we examined how efficiently Endo III and Fpg repair their oxidative substrates in vivo following treatment with hydrogen peroxide. We found that Fpg was nonredundant and required to rapidly remove its substrate lesions on the chromosome. In addition, Fpg also repaired a significant portion of the lesions recognized by Endo III, suggesting that it plays a prominent role in the global repair of both purine damage and pyrimidine damage in vivo. By comparison, Endo III did not affect the repair rate of Fpg substrates and was only responsible for repairing a subset of its own substrate lesions in vivo. The absence of Endo VIII or nucleotide excision repair did not significantly affect the global repair of either Fpg or Endo III substrates in vivo. Surprisingly, replication recovered after oxidative DNA damage in all mutants examined, even when lesions persisted in the DNA, suggesting the presence of an efficient mechanism to process or overcome oxidative damage encountered during replication.

Indexed as

DNA DamageDNA RepairDeoxyribonuclease (Pyrimidine Dimer)DNA, BacterialDNA-Formamidopyrimidine GlycosylaseEscherichia coliEscherichia coli ProteinsOxidation-ReductionSubstrate SpecificityDeoxyribonuclease (Pyrimidine Dimer)DNA, BacterialDNA-Formamidopyrimidine GlycosylaseDNA-formamidopyrimidine glycosylase, E coliEscherichia coli Proteins

Identifiers

PMID21601577
PMCPMC3156590
OpenAlexW2157786292

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.