Evidence map›Paper›PMID 21210717›Full record

ArticleJournal of proteome research2011

Proteome-wide identification of WRN-interacting proteins in untreated and nuclease-treated samples.

Sophie Lachapelle, Jean-Philippe Gagné, Chantal Garand, Myriam Desbiens, Yan Coulombe, Vilhelm A Bohr, Michael J Hendzel, Jean-Yves Masson, Guy G Poirier, Michel Lebel

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2011. 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
1.7field-weighted citation impact, top 15% 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, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Human RecQ Helicases in DNA Double-Strand Break Repair.Frontiers in cell and developmental biology · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Genetics and genomics in Peru: Clinical and research perspective.Molecular genetics & genomic medicine · 2018
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

10 authors at 5 institutions in 2 countries.

Sophie LachapelleCentre de Recherche en Cancérologie de l'Université Laval, Hôpital Hôtel-Dieu de Québec, Québec City, Québec, G1R 2J6, Canada.
Jean-Philippe Gagné
Chantal Garand
Myriam Desbiens
Yan Coulombe
Vilhelm A Bohr
Michael J Hendzel
Jean-Yves Masson
Guy G Poirier
Michel Lebel
Hôtel-Dieu de Québec · CAUniversité Laval · CACentre hospitalier de l'Université Laval · CANational Institute on Aging · USUniversity of Alberta · CA

Funding

The Function of Werner Syndrome ProteinZIAAG000721 · NIA · NATIONAL INSTITUTE ON AGING · PI FERRUCCI, LUIGI · 2009 to 2022
$7.7M
CIHRIntramural NIH HHS ZIA AG000721
6 · The paper itself

Abstract

Werner syndrome (WS) is characterized by the premature onset of several age-associated pathologies. The protein defective in WS patients (WRN) is a helicase/exonuclease involved in DNA repair, replication, telomere maintenance, and transcription. Here, we present the results of a large-scale proteome analysis to determine protein partners of WRN. We expressed fluorescent tagged-WRN (eYFP-WRN) in human 293 embryonic kidney cells and detected interacting proteins by co-immunoprecipitation from cell extract. We identified by mass spectrometry 220 nuclear proteins that complexed with WRN. This number was reduced to 40 when broad-spectrum nucleases were added to the lysate. We consider these 40 proteins as directly interacting with WRN. Some of these proteins have previously been shown to interact with WRN, whereas most are new partners. Among the top 15 hits, we find the new interactors TMPO, HNRNPU, RPS3, RALY, RPS9 DDX21, and HNRNPM. These proteins are likely important components in understanding the function of WRN in preventing premature aging and deserve further investigation. We have confirmed endogenous WRN interaction with endogenous RPS3, a ribosomal protein with endonuclease activities involved in oxidative DNA damage recognition. Our results suggest that the use of nucleases during cell lysis severely restricts interacting protein partners and thus enhances specificity.

Indexed as

AnimalsChromatography, LiquidDeoxyribonucleasesExodeoxyribonucleasesHEK293 CellsHeLa CellsHumansProtein BindingProteomeRecombinant Fusion ProteinsRecQ HelicasesReproducibility of ResultsRibosomal ProteinsTandem Mass SpectrometryWerner SyndromeWerner Syndrome HelicaseDeoxyribonucleasesExodeoxyribonucleasesProteomeRecombinant Fusion ProteinsRecQ HelicasesRibosomal ProteinsRPS3A protein, humanWerner Syndrome HelicaseWRN protein, human

Identifiers

PMID21210717
PMCPMC4586248
OpenAlexW2332913832

What OpenQuestion holds

Textmetadata
LicenceTDM
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.