Evidence map›Paper›PMID 29021206›Full record

ArticleEMBO reports2017

RADX interacts with single-stranded DNA to promote replication fork stability.

Lisa Schubert, Teresa Ho, Saskia Hoffmann, Peter Haahr, Claire Guérillon, Niels Mailand

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

27 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Structure of RADX and mechanism for regulation of RAD51 nucleofilaments.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Article
  7. Article
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  9. Article
  10. Structure of RADX and mechanism for regulation of RAD51 nucleofilaments.bioRxiv : the preprint server for biology · 2023
    Article
  11. Genes · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Replication Fork Reversal and Protection.Frontiers in cell and developmental biology · 2021
    Review
  20. 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 1 institution in 1 country.

Lisa SchubertNovo Nordisk Foundation Center for Protein Research, University of Copenhagen, Copenhagen, Denmark.
Teresa HoNovo Nordisk Foundation Center for Protein Research, University of Copenhagen, Copenhagen, Denmark.
Saskia HoffmannNovo Nordisk Foundation Center for Protein Research, University of Copenhagen, Copenhagen, Denmark.
Peter HaahrNovo Nordisk Foundation Center for Protein Research, University of Copenhagen, Copenhagen, Denmark.
Claire GuérillonNovo Nordisk Foundation Center for Protein Research, University of Copenhagen, Copenhagen, Denmark.
Niels MailandNovo Nordisk Foundation Center for Protein Research, University of Copenhagen, Copenhagen, Denmark niels.mailand@cpr.ku.dk.ORCID 0000-0002-6623-709X
University of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-stranded DNA (ssDNA) regions form as an intermediate in many DNA-associated transactions. Multiple cellular proteins interact with ssDNA via the oligonucleotide/oligosaccharide-binding (OB) fold domain. The heterotrimeric, multi-OB fold domain-containing Replication Protein A (RPA) complex has an essential genome maintenance role, protecting ssDNA regions from nucleolytic degradation and providing a recruitment platform for proteins involved in responses to replication stress and DNA damage. Here, we identify the uncharacterized protein RADX (CXorf57) as an ssDNA-binding factor in human cells. RADX binds ssDNA via an N-terminal OB fold cluster, which mediates its recruitment to sites of replication stress. Deregulation of RADX expression and ssDNA binding leads to enhanced replication fork stalling and degradation, and we provide evidence that a balanced interplay between RADX and RPA ssDNA-binding activities is critical for avoiding these defects. Our findings establish RADX as an important component of cellular pathways that promote DNA replication integrity under basal and stressful conditions by means of multiple ssDNA-binding proteins.

Indexed as

DNA RepairDNA ReplicationBinding SitesCell Line, TumorDNA-Binding ProteinsDNA DamageDNA, Single-StrandedHCT116 CellsHumansModels, MolecularOsteoblastsProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsReplication Protein ADNA-Binding ProteinsDNA, Single-StrandedReplication Protein ARNA, Small InterferingDNA replicationgenome integrityreplication protein Areplication stresssingle‐stranded DNA

Identifiers

PMID29021206
PMCPMC5666600
OpenAlexW2760968141

What OpenQuestion holds

Textmetadata
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.