Evidence map›Paper›PMID 22542292›Full record

ArticleDNA repair2012

RECQ1 plays a distinct role in cellular response to oxidative DNA damage.

Sudha Sharma, Pornima Phatak, Alexei Stortchevoi, Maria Jasin, Jeannine R Larocque

Abstract read
In one paragraph

Article in DNA repair, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

37 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Human RecQ Helicases in DNA Double-Strand Break Repair.Frontiers in cell and developmental biology · 2021
    Review
  11. Review
  12. Article
  13. Article
  14. Stress Marks on the Genome: Use or Lose?International journal of molecular sciences · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  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

5 authors at 3 institutions in 1 country.

Sudha SharmaDepartment of Biochemistry and Molecular Biology, College of Medicine, Howard University, 520 W Street, NW, Washington, DC 20059, USA. sudha.sharma@howard.edu
Pornima Phatak
Alexei Stortchevoi
Maria Jasin
Jeannine R Larocque
Howard University · USGeorgetown University Medical Center · USMemorial Sloan Kettering Cancer Center · US

Funding

Training and Career Development CoreU54CA132378 · NCI · CITY COLLEGE OF NEW YORK · PI Tim Alan Ahles, ADRIANA ESPINOSA · 2008 to 2026
$28.9M
Training and Career Development and Education CoreU54CA137788 · NCI · SLOAN-KETTERING INST CAN RESEARCH · PI Daniel Alan Heller · 2008 to 2026
$28.1M
STRUCTURAL/FUNCTIONAL CHARACTERIZATION OF AMINOGLYCOSIDEG12RR003048 · NCRR · HOWARD UNIVERSITY · PI SOUTHERLAND, WILLIAM M. · 1985 to 2011
$19.0M
PROTEOMICS CORE FACILITYG12MD007597 · NIMHD · HOWARD UNIVERSITY · PI SOUTHERLAND, WILLIAM M. · 2012 to 2018
$14.8M
Molecular Analysis of RECQ1 Functions in Genome MaintenanceSC1GM093999 · NIGMS · HOWARD UNIVERSITY · PI SHARMA, SUDHA · 2010 to 2019
$3.0M
NCI NIH HHS U54 CA132378NCI NIH HHS U54 CA137788NCI NIH HHS U54CA137788/U54CA132378NCRR NIH HHS 2 G12RR003048NCRR NIH HHS G12 RR003048NIGMS NIH HHS 7SC1GM093999-02NIGMS NIH HHS SC1 GM093999NIMHD NIH HHS G12 MD007597
6 · The paper itself

Abstract

RECQ1 is the most abundant RecQ homolog in humans but its functions have remained mostly elusive. Biochemically, RECQ1 displays distinct substrate specificities from WRN and BLM, indicating that these RecQ helicases likely perform non-overlapping functions. Our earlier work demonstrated that RECQ1-deficient cells display spontaneous genomic instability. We have obtained key evidence suggesting a unique role of RECQ1 in repair of oxidative DNA damage. We show that similar to WRN, RECQ1 associates with PARP-1 in nuclear extracts and exhibits direct protein interaction in vitro. Deficiency in WRN or BLM helicases have been shown to result in reduced homologous recombination and hyperactivation of PARP under basal condition. However, RECQ1-deficiency did not lead to PARP activation in undamaged cells and nor did it result in reduction in homologous recombination repair. In stark contrast to what is seen in WRN-deficiency, RECQ1-deficient cells hyperactivate PARP in a specific response to H₂O₂treatment. RECQ1-deficient cells are more sensitive to oxidative DNA damage and exposure to oxidative stress results in a rapid and reversible recruitment of RECQ1 to chromatin. Chromatin localization of RECQ1 precedes WRN helicase, which has been shown to function in oxidative DNA damage repair. However, oxidative DNA damage-induced chromatin recruitment of these RecQ helicases is independent of PARP activity. As other RecQ helicases are known to interact with PARP-1, this study provides a paradigm to delineate specialized and redundant functions of RecQ homologs in repair of oxidative DNA damage.

Indexed as

DNA DamageDNA RepairBlotting, WesternCell Line, TumorCell NucleusChromatinDNA Breaks, Single-StrandedEnzyme ActivationHeLa CellsHomologous RecombinationHumansHydrogen PeroxideImmunoprecipitationOxidantsOxidative StressPoly(ADP-ribose) PolymerasesChromatinHydrogen PeroxideOxidantsPoly(ADP-ribose) PolymerasesRecQ HelicasesRECQL protein, human

Identifiers

PMID22542292
PMCPMC3420015
OpenAlexW2091350694

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.