Evidence map›Paper›PMID 23139746›Full record

ArticlePloS one2012

The human homolog of Escherichia coli endonuclease V is a nucleolar protein with affinity for branched DNA structures.

Cathrine Fladeby, Erik Sebastian Vik, Jon K Laerdahl, Christine Gran Neurauter, Julie E Heggelund, Eirik Thorgaard, Pernille Strøm-Andersen, Magnar Bjørås, Bjørn Dalhus, Ingrun Alseth

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. 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
1.5field-weighted citation impact, top 19% 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, 25 citations in OpenAlex.

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  14. Endonuclease V cleaves at inosines in RNA.Nature communications · 2013
    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

10 authors at 2 institutions in 1 country.

Cathrine FladebyDepartment of Microbiology, Oslo University Hospital HF and University of Oslo, Rikshospitalet, Oslo, Norway.
Erik Sebastian Vik
Jon K Laerdahl
Christine Gran Neurauter
Julie E Heggelund
Eirik Thorgaard
Pernille Strøm-Andersen
Magnar Bjørås
Bjørn Dalhus
Ingrun Alseth
Oslo University Hospital · NOUniversity of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Loss of amino groups from adenines in DNA results in the formation of hypoxanthine (Hx) bases with miscoding properties. The primary enzyme in Escherichia coli for DNA repair initiation at deaminated adenine is endonuclease V (endoV), encoded by the nfi gene, which cleaves the second phosphodiester bond 3' of an Hx lesion. Endonuclease V orthologs are widespread in nature and belong to a family of highly conserved proteins. Whereas prokaryotic endoV enzymes are well characterized, the function of the eukaryotic homologs remains obscure. Here we describe the human endoV ortholog and show with bioinformatics and experimental analysis that a large number of transcript variants exist for the human endonuclease V gene (ENDOV), many of which are unlikely to be translated into functional protein. Full-length ENDOV is encoded by 8 evolutionary conserved exons covering the core region of the enzyme, in addition to one or more 3'-exons encoding an unstructured and poorly conserved C-terminus. In contrast to the E. coli enzyme, we find recombinant ENDOV neither to incise nor bind Hx-containing DNA. While both enzymes have strong affinity for several branched DNA substrates, cleavage is observed only with E. coli endoV. We find that ENDOV is localized in the cytoplasm and nucleoli of human cells. As nucleoli harbor the rRNA genes, this may suggest a role for the protein in rRNA gene transactions such as DNA replication or RNA transcription.

Indexed as

Nucleic Acid ConformationSequence Homology, Amino AcidAlternative SplicingCell CycleCell LineCell NucleolusComputational BiologyDeoxyribonuclease (Pyrimidine Dimer)DNAEscherichia coli ProteinsGene Expression Regulation, NeoplasticGreen Fluorescent ProteinsHumansModels, MolecularMutant ProteinsNeoplasmsDeoxyribonuclease (Pyrimidine Dimer)DNAenhanced green fluorescent proteinEscherichia coli ProteinsGreen Fluorescent ProteinsMutant ProteinsNuclear Proteins

Identifiers

PMID23139746
PMCPMC3489907
OpenAlexW1990953759

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.