Evidence map›Paper›PMID 24406253›Full record

ArticleMechanisms of ageing and development2014

Cockayne Syndrome group B protein stimulates NEIL2 DNA glycosylase activity.

Maria D Aamann, Christina Hvitby, Venkateswarlu Popuri, Meltem Muftuoglu, Lasse Lemminger, Cecilie K Skeby, Guido Keijzers, Byungchan Ahn, Magnar Bjørås, Vilhelm A Bohr and 1 more

Abstract read
In one paragraph

Article in Mechanisms of ageing and development, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

29 citing papers in PubMed, 43 citations in OpenAlex.

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  11. DNA glycosylase NEIL2 functions in multiple cellular processes.Progress in biophysics and molecular biology · 2021
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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

11 authors at 5 institutions in 4 countries.

Maria D AamannDanish Center for Molecular Gerontology and Danish Aging Research Center, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.
Christina HvitbyDanish Center for Molecular Gerontology and Danish Aging Research Center, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.
Venkateswarlu PopuriLaboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health, Baltimore, MD, USA.
Meltem MuftuogluCenter for Healthy Aging, University of Copenhagen, Copenhagen, Denmark.
Lasse LemmingerDanish Center for Molecular Gerontology and Danish Aging Research Center, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.
Cecilie K SkebyDanish Center for Molecular Gerontology and Danish Aging Research Center, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.
Guido KeijzersDanish Center for Molecular Gerontology and Danish Aging Research Center, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark; Center for Healthy Aging, University of Copenhagen, Copenhagen, Denmark.
Byungchan AhnDanish Center for Molecular Gerontology and Danish Aging Research Center, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark; University of Ulsan, Republic of Korea.
Magnar BjøråsLaboratory for Molecular Biology, Center for Molecular Biology and Neuroscience, Oslo University Hospital, Oslo, Norway.
Vilhelm A BohrLaboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health, Baltimore, MD, USA.
Tinna StevnsnerDanish Center for Molecular Gerontology and Danish Aging Research Center, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark. Electronic address: tvs@mb.au.dk.
Aarhus University · DKUniversity of Copenhagen · DKNational Institute on Aging · USNational Institutes of Health · USOslo University Hospital · NO

Funding

The role of the Cockayne syndrome proteinZIAAG000722 · NIA · NATIONAL INSTITUTE ON AGING · PI FERRUCCI, LUIGI · 2009 to 2023
$9.1M
Oxidative DNA Damage And Its ProcessingZIAAG000727 · NIA · NATIONAL INSTITUTE ON AGING · PI FERRUCCI, LUIGI · 2009 to 2022
$8.4M
REPAIR OF OXIDATIVE DNA DAMAGEZ01AG000727 · NIA · NATIONAL INSTITUTE ON AGING · PI BOHR, VILHELM A · 1994 to 2008
$1.3M
Intramural NIH HHS Z01 AG000727Intramural NIH HHS ZIA AG000722
6 · The paper itself

Abstract

Cockayne Syndrome is a segmental premature aging syndrome, which can be caused by loss of function of the CSB protein. CSB is essential for genome maintenance and has numerous interaction partners with established roles in different DNA repair pathways including transcription coupled nucleotide excision repair and base excision repair. Here, we describe a new interaction partner for CSB, the DNA glycosylase NEIL2. Using both cell extracts and recombinant proteins, CSB and NEIL2 were found to physically interact independently of DNA. We further found that CSB is able to stimulate NEIL2 glycosylase activity on a 5-hydroxyl uracil lesion in a DNA bubble structure substrate in vitro. A novel 4,6-diamino-5-formamidopyrimidine (FapyA) specific incision activity of NEIL2 was also stimulated by CSB. To further elucidate the biological role of the interaction, immunofluorescence studies were performed, showing an increase in cytoplasmic CSB and NEIL2 co-localization after oxidative stress. Additionally, stalling of the progression of the transcription bubble with α-amanitin resulted in increased co-localization of CSB and NEIL2. Finally, CSB knockdown resulted in reduced incision of 8-hydroxyguanine in a DNA bubble structure using whole cell extracts. Taken together, our data supports a biological role for CSB and NEIL2 in transcription associated base excision repair.

Indexed as

Gene Expression Regulation, EnzymologicCytoplasmDNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA GlycosylasesDNA HelicasesDNA RepairDNA Repair EnzymesEscherichia coliGuanineHeLa CellsHumansMicroscopy, FluorescenceOxidative StressPoly-ADP-Ribose Binding ProteinsRecombinant Proteins8-hydroxyguanineDNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA GlycosylasesDNA HelicasesDNA Repair EnzymesERCC6 protein, humanGuanineNEIL2 protein, humanPoly-ADP-Ribose Binding ProteinsRecombinant ProteinsVitamin K 3Base excision repairCockayne SyndromeCSBNEIL2Oxidative damage

Identifiers

PMID24406253
PMCPMC3954709
OpenAlexW2030782110

What OpenQuestion holds

Textmetadata
LicenceTDM
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.