Evidence map›Paper›PMID 41394509›Full record

ReviewNAR cancer2025

What is in a name? Rethinking SMUG1 in genome maintenance.

Natalie Rudolfova, Alexander Myhr Skjetne, Nicola P Montaldo, Torkild Visnes, Hilde Loge Nilsen, Maurice Michel

Abstract readReview
In one paragraph

Review in NAR cancer, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Distinct repair processes produce APOBEC-induced deletions, tandem substitutions, and complex mutations in yeast and human cells.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
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

6 authors.

Natalie RudolfovaDepartment of Oncology and Pathology, Science for Life Laboratory, Karolinska Institute, Stockholm, Solna, 17165, Sweden.
Alexander Myhr SkjetneDepartment of Microbiology, Oslo University Hospital, Norway; Institute of Clinical Medicine, University of Oslo, Norway; CRESCO-Centre for Embryology and Healthy Development, University of Oslo, 0424 Oslo, Norway.
Nicola P MontaldoDepartment of Microbiology, Oslo University Hospital, Norway; Institute of Clinical Medicine, University of Oslo, Norway; CRESCO-Centre for Embryology and Healthy Development, University of Oslo, 0424 Oslo, Norway.ORCID 0000-0003-3434-615X
Torkild VisnesDepartment of Biotechnology and Nanomedicine, SINTEF Industry,7034 Trondheim, Norway.ORCID 0000-0003-1047-988X
Hilde Loge NilsenDepartment of Microbiology, Oslo University Hospital, Norway; Institute of Clinical Medicine, University of Oslo, Norway; CRESCO-Centre for Embryology and Healthy Development, University of Oslo, 0424 Oslo, Norway.ORCID 0000-0003-2115-2663
Maurice MichelDepartment of Oncology and Pathology, Science for Life Laboratory, Karolinska Institute, Stockholm, Solna, 17165, Sweden.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small base lesions in DNA are primarily repaired through the base excision repair pathway, which is initiated by DNA glycosylases. This review focuses on single-strand selective monofunctional uracil-DNA glycosylase (SMUG1), an enzyme whose name incompletely captures its broader biological roles. SMUG1 excises a wide range of substrates beyond uracil, shows a preference for double-stranded DNA, and has been reported to be a bifunctional DNA glycosylase with a weak lyase activity. Moreover, SMUG1 plays roles extending beyond DNA repair, including functions in RNA quality control and RNA biogenesis. Recently, genetic interactions have been described between SMUG1 and proteins that safeguard stressed replication forks, implicating a function for SMUG1 in cancer cell biology. Understanding SMUG1's full repertoire is key to uncovering its role in genome maintenance and unlocking its potential as a therapeutic target. Here, we review the biochemical properties reported for SMUG1 and its distinct functions from other uracil-DNA glycosylases

Indexed as

DNA RepairNeoplasmsUracil-DNA GlycosidaseAnimalsDNA DamageGenomic InstabilityHumansSMUG1 protein, humanUracil-DNA Glycosidase

Identifiers

PMID41394509
PMCPMC12699328

What Socratic 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 Socratic graph.