Evidence map›Paper›PMID 30838409›Full record

ArticleNucleic acids research2019

Uracil-DNA glycosylase UNG1 isoform variant supports class switch recombination and repairs nuclear genomic uracil.

Antonio Sarno, Marie Lundbæk, Nina Beate Liabakk, Per Arne Aas, Robin Mjelle, Lars Hagen, Mirta M L Sousa, Hans E Krokan, Bodil Kavli

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

19 citing papers in PubMed, 34 citations in OpenAlex.

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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 1 institution in 1 country.

Antonio SarnoDepartment of Clinical and Molecular Medicine, NTNU-Norwegian University of Science and Technology, NO-7491 Trondheim, Norway.
Marie LundbækDepartment of Clinical and Molecular Medicine, NTNU-Norwegian University of Science and Technology, NO-7491 Trondheim, Norway.
Nina Beate LiabakkDepartment of Clinical and Molecular Medicine, NTNU-Norwegian University of Science and Technology, NO-7491 Trondheim, Norway.
Per Arne AasDepartment of Clinical and Molecular Medicine, NTNU-Norwegian University of Science and Technology, NO-7491 Trondheim, Norway.
Robin MjelleDepartment of Clinical and Molecular Medicine, NTNU-Norwegian University of Science and Technology, NO-7491 Trondheim, Norway.
Lars HagenDepartment of Clinical and Molecular Medicine, NTNU-Norwegian University of Science and Technology, NO-7491 Trondheim, Norway.
Mirta M L SousaDepartment of Clinical and Molecular Medicine, NTNU-Norwegian University of Science and Technology, NO-7491 Trondheim, Norway.
Hans E KrokanDepartment of Clinical and Molecular Medicine, NTNU-Norwegian University of Science and Technology, NO-7491 Trondheim, Norway.
Bodil KavliDepartment of Clinical and Molecular Medicine, NTNU-Norwegian University of Science and Technology, NO-7491 Trondheim, Norway.
Norwegian University of Science and Technology · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

UNG is the major uracil-DNA glycosylase in mammalian cells and is involved in both error-free base excision repair of genomic uracil and mutagenic uracil-processing at the antibody genes. However, the regulation of UNG in these different processes is currently not well understood. The UNG gene encodes two isoforms, UNG1 and UNG2, each possessing unique N-termini that mediate translocation to the mitochondria and the nucleus, respectively. A strict subcellular localization of each isoform has been widely accepted despite a lack of models to study them individually. To determine the roles of each isoform, we generated and characterized several UNG isoform-specific mouse and human cell lines. We identified a distinct UNG1 isoform variant that is targeted to the cell nucleus where it supports antibody class switching and repairs genomic uracil. We propose that the nuclear UNG1 variant, which in contrast to UNG2 lacks a PCNA-binding motif, may be specialized to act on ssDNA through its ability to bind RPA. RPA-coated ssDNA regions include both transcribed antibody genes that are targets for deamination by AID and regions in front of the moving replication forks. Our findings provide new insights into the function of UNG isoforms in adaptive immunity and DNA repair.

Indexed as

AnimalsCell LineCell NucleusCRISPR-Cas SystemsDNA GlycosylasesDNA RepairDNA ReplicationDNA, Single-StrandedGene Knockout TechniquesGenomeHumansImmunoglobulin Class SwitchingMiceProliferating Cell Nuclear AntigenProtein IsoformsRecombination, GeneticCCNO protein, humanDNA GlycosylasesDNA, Single-StrandedProliferating Cell Nuclear AntigenProtein IsoformsUracilUracil-DNA Glycosidase

Identifiers

PMID30838409
PMCPMC6511853
OpenAlexW2921918395

What OpenQuestion holds

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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.