Evidence map›Paper›PMID 24800743›Full record

ArticlePLoS biology2014

The RSF1 histone-remodelling factor facilitates DNA double-strand break repair by recruiting centromeric and Fanconi Anaemia proteins.

Fabio Pessina, Noel F Lowndes

Expression of concernErratum issuedOpen access · goldAbstract read
In one paragraph

Article in PLoS biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It carries an expression of concern. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

32 citing papers in PubMed, 45 citations in OpenAlex.

  1. Pro-ATO/Allicin Liposomes for Dual-Pathway Targeting of p53-Mutant Tumors.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. The RPA-RNF20-SNF2H cascade promotes proper chromosome segregation and homologous recombination repair.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. RSF1 in cancer: interactions and functions.Cancer cell international · 2021
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Breaking up with ATM.Journal of immunological sciences · 2018
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Fabio PessinaGenome Stability Laboratory, Centre for Chromosome Biology, School of Natural Science, National University of Ireland Galway, Ireland.
Noel F LowndesGenome Stability Laboratory, Centre for Chromosome Biology, School of Natural Science, National University of Ireland Galway, Ireland.
Ollscoil na Gaillimhe – University of Galway · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ATM is a central regulator of the cellular responses to DNA double-strand breaks (DSBs). Here we identify a biochemical interaction between ATM and RSF1 and we characterise the role of RSF1 in this response. The ATM-RSF1 interaction is dependent upon both DSBs and ATM kinase activity. Together with SNF2H/SMARCA5, RSF1 forms the RSF chromatin-remodelling complex. Although RSF1 is specific to the RSF complex, SNF2H/SMARCA5 is a catalytic subunit of several other chromatin-remodelling complexes. Although not required for checkpoint signalling, RSF1 is required for efficient repair of DSBs via both end-joining and homology-directed repair. Specifically, the ATM-dependent recruitment to sites of DSBs of the histone fold proteins CENPS/MHF1 and CENPX/MHF2, previously identified at centromeres, is RSF1-dependent. In turn these proteins recruit and regulate the mono-ubiquitination of the Fanconi Anaemia proteins FANCD2 and FANCI. We propose that by depositing CENPS/MHF1 and CENPX/MHF2, the RSF complex either directly or indirectly contributes to the reorganisation of chromatin around DSBs that is required for efficient DNA repair.

Indexed as

DNA End-Joining RepairRecombinational DNA RepairAdenosine TriphosphatasesAnimalsAtaxia Telangiectasia Mutated ProteinsB-LymphocytesCell Line, TumorChickensChromatinChromosomal Proteins, Non-HistoneDNADNA-Binding ProteinsDNA Breaks, Double-StrandedEpithelial CellsFanconi Anemia Complementation Group D2 ProteinFanconi Anemia Complementation Group ProteinsAdenosine TriphosphatasesAtaxia Telangiectasia Mutated ProteinsATM protein, humanCENPX protein, humanChromatinChromosomal Proteins, Non-HistoneDNADNA-Binding ProteinsFANCD2 protein, humanFANCI protein, humanFanconi Anemia Complementation Group D2 ProteinFanconi Anemia Complementation Group ProteinsHistonesNuclear ProteinsRSF1 protein, humanSMARCA5 protein, humanTrans-Activators

Identifiers

PMID24800743
PMCPMC4011676
OpenAlexW2025209634

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.