Evidence map›Paper›PMID 19179336›Full record

ArticleThe Journal of biological chemistry2009

Cockayne syndrome group B protein stimulates repair of formamidopyrimidines by NEIL1 DNA glycosylase.

Meltem Muftuoglu, Nadja C de Souza-Pinto, Arin Dogan, Maria Aamann, Tinna Stevnsner, Ivana Rybanska, Güldal Kirkali, Miral Dizdaroglu, Vilhelm A Bohr

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

55 citing papers in PubMed, 106 citations in OpenAlex.

  1. Review
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  8. 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

9 authors at 6 institutions in 3 countries.

Meltem MuftuogluLaboratory of Molecular Gerontology, NIA Intramural Research Program, National Institutes of Health, Baltimore, Maryland 21224, USA.
Nadja C de Souza-Pinto
Arin Dogan
Maria Aamann
Tinna Stevnsner
Ivana Rybanska
Güldal Kirkali
Miral Dizdaroglu
Vilhelm A Bohr
Dokuz Eylül University · TRNational Institute on Drug Abuse · USNational Institutes of Health · USAarhus University · DKNational Institute of Standards and Technology · USUniversity of Copenhagen · DK

Funding

REGULATION OF GADD135 BY GROWTH ARREST, DIFFERENTIATION, AND METABOLIC STRESSESZ01AG000722 · NIA · AGING · PI HOLBROOK, N J · 1992 to 1993
–
Intramural NIH HHS
6 · The paper itself

Abstract

Cockayne syndrome (CS) is a premature aging condition characterized by sensitivity to UV radiation. However, this phenotype does not explain the progressive neurodegeneration in CS patients. It could be due to the hypersensitivity of CSB-deficient cells to oxidative stress. So far most studies on the role of CSB in repair of oxidatively induced DNA lesions have focused on 7,8-dihydro-8-oxoguanine. This study examines the role of CSB in the repair of formamidopyrimidines 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyGua) and 4,6-diamino-5-formamidopyrimidine (FapyAde), which are substrates for endonuclease VIII-like (NEIL1) DNA glycosylase. Results presented here show that csb(-/-) mice have a higher level of endogenous FapyAde and FapyGua in DNA from brain and kidney than wild type mice as well as higher levels of endogenous FapyAde in genomic DNA and mtDNA from liver. In addition, CSB stimulates NEIL1 incision activity in vitro, and CSB and NEIL1 co-immunoprecipitate and co-localize in HeLa cells. When CSB and NEIL1 are depleted from HeLa cells by short hairpin RNA knockdown, repair of induced FapyGua is strongly inhibited. These results suggest that CSB plays a role in repair of formamidopyrimidines, possibly by interacting with and stimulating NEIL1, and that accumulation of such modifications may have a causal role in the pathogenesis of CS.

Indexed as

Adenosine TriphosphatasesAnimalsDNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA GlycosylasesDNA HelicasesDNA RepairDNA Repair EnzymesHeLa CellsHumansMiceMice, KnockoutPoly-ADP-Ribose Binding ProteinsProtein BindingPyrimidinesSubstrate Specificity4,6-diamino-5-N-formamidopyrimidineAdenosine TriphosphatasesDNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA GlycosylasesDNA HelicasesDNA Repair EnzymesERCC6 protein, humanErcc6 protein, mouseNEIL1 protein, humanPoly-ADP-Ribose Binding ProteinsPyrimidines

Identifiers

PMID19179336
PMCPMC2666579
OpenAlexW2019618509

What OpenQuestion holds

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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.