Evidence map›Paper›PMID 22002307›Full record

ArticleOncogene2012

The RAD9-RAD1-HUS1 (9.1.1) complex interacts with WRN and is crucial to regulate its response to replication fork stalling.

P Pichierri, S Nicolai, L Cignolo, M Bignami, A Franchitto

Open access · bronzeAbstract read
In one paragraph

Article in Oncogene, 2012. 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
1.6field-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.

  1. Article
  2. The function of Mgs1/WRNIP1 in genome maintenance.Frontiers in molecular biosciences · 2026
    Review
  3. Article
  4. Review
  5. Article
  6. RecQ DNA Helicase Rqh1 Promotes Rad3Molecular and cellular biology · 2020
    Article
  7. Article
  8. Werner Syndrome Protein and DNA Replication.International journal of molecular sciences · 2018
    Review
  9. Article
  10. Article
  11. Review
  12. Replication fork recovery and regulation of common fragile sites stability.Cellular and molecular life sciences : CMLS · 2014
    Review
  13. Article
  14. Review
  15. Replicating damaged DNA in eukaryotes.Cold Spring Harbor perspectives in biology · 2013
    Review
  16. Article
  17. Article
  18. Article
  19. 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

5 authors at 2 institutions in 2 countries.

P PichierriDepartment of Environment and Primary Prevention, Istituto Superiore di Sanità, Rome, Italy. pietro.pichierri@iss.it
S Nicolai
L Cignolo
M Bignami
A Franchitto
Istituto Superiore di Sanità · ITSanford Burnham Prebys Medical Discovery Institute · US

Funding

Telethon GGP04094
6 · The paper itself

Abstract

The WRN protein belongs to the RecQ family of DNA helicases and is implicated in replication fork restart, but how its function is regulated remains unknown. We show that WRN interacts with the 9.1.1 complex, one of the central factors of the replication checkpoint. This interaction is mediated by the binding of the RAD1 subunit to the N-terminal region of WRN and is instrumental for WRN relocalization in nuclear foci and its phosphorylation in response to replication arrest. We also find that ATR-dependent WRN phosphorylation depends on TopBP1, which is recruited by the 9.1.1 complex in response to replication arrest. Finally, we provide evidence for a cooperation between WRN and 9.1.1 complex in preventing accumulation of DNA breakage and maintaining genome integrity at naturally occurring replication fork stalling sites. Taken together, our data unveil a novel functional interplay between WRN helicase and the replication checkpoint, contributing to shed light into the molecular mechanism underlying the response to replication fork arrest.

Indexed as

DNA ReplicationAtaxia Telangiectasia Mutated ProteinsBlotting, WesternCarrier ProteinsCell Cycle ProteinsChromosome Fragile SitesDNA-Binding ProteinsDNA DamageExodeoxyribonucleasesExonucleasesFluorescent Antibody TechniqueHeLa CellsHumansImmunoprecipitationIn Situ Hybridization, FluorescenceNuclear ProteinsAtaxia Telangiectasia Mutated ProteinsATR protein, humanCarrier ProteinsCell Cycle ProteinsDNA-Binding ProteinsExodeoxyribonucleasesExonucleasesHUS1 protein, humanNuclear ProteinsProtein Serine-Threonine KinasesRad1 protein, humanrad9 proteinRecQ HelicasesRNA, Small InterferingTOPBP1 protein, humanWerner Syndrome HelicaseWRN protein, human

Identifiers

PMID22002307
PMCPMC3272477
OpenAlexW1982586042

What OpenQuestion holds

Textmetadata
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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.