Evidence map›Paper›PMID 31654852›Full record

ArticleiScience2019

WRNIP1 Protects Reversed DNA Replication Forks from SLX4-Dependent Nucleolytic Cleavage.

Bartlomiej Porebski, Sebastian Wild, Sandra Kummer, Sarah Scaglione, Pierre-Henri L Gaillard, Kerstin Gari

Open access · goldAbstract read
In one paragraph

Article in iScience, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. The function of Mgs1/WRNIP1 in genome maintenance.Frontiers in molecular biosciences · 2026
    Review
  2. Article
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  4. Cellular Responses to Widespread DNA Replication Stress.International journal of molecular sciences · 2023
    Review
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  18. Roles of OB-Fold Proteins in Replication Stress.Frontiers in cell and developmental biology · 2020
    Review
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 at 2 institutions in 3 countries.

Bartlomiej PorebskiInstitute of Molecular Cancer Research, University of Zurich, 8057 Zurich, Switzerland. Electronic address: bartlomiej.porebski@ki.se.
Sebastian WildInstitute of Molecular Cancer Research, University of Zurich, 8057 Zurich, Switzerland.
Sandra KummerInstitute of Molecular Cancer Research, University of Zurich, 8057 Zurich, Switzerland.
Sarah ScaglioneCentre de Recherche en Cancérologie de Marseille, CNRS, INSERM, Aix-Marseille Université, Institut Paoli-Calmettes, 13009 Marseille, France.
Pierre-Henri L GaillardCentre de Recherche en Cancérologie de Marseille, CNRS, INSERM, Aix-Marseille Université, Institut Paoli-Calmettes, 13009 Marseille, France.
Kerstin GariInstitute of Molecular Cancer Research, University of Zurich, 8057 Zurich, Switzerland. Electronic address: gari@imcr.uzh.ch.
University of Zurich · CHCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During DNA replication stress, stalled replication forks need to be stabilized to prevent fork collapse and genome instability. The AAA + ATPase WRNIP1 (Werner Helicase Interacting Protein 1) has been implicated in the protection of stalled replication forks from nucleolytic degradation, but the underlying molecular mechanism has remained unclear. Here we show that WRNIP1 exerts its protective function downstream of fork reversal. Unexpectedly though, WRNIP1 is not part of the well-studied BRCA2-dependent branch of fork protection but seems to protect the junction point of reversed replication forks from SLX4-mediated endonucleolytic degradation, possibly by directly binding to reversed replication forks. This function is specific to the shorter, less abundant, and less conserved variant of WRNIP1. Overall, our data suggest that in the absence of BRCA2 and WRNIP1 different DNA substrates are generated at reversed forks but that nascent strand degradation in both cases depends on the activity of exonucleases and structure-specific endonucleases.

Indexed as

Biological SciencesCell BiologyMolecular Biology

Identifiers

PMID31654852
PMCPMC6820244
OpenAlexW2979457360

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.