Evidence map›Paper›PMID 34083132›Full record

ArticleDNA repair2021

RNA helicase, DDX3X, is actively recruited to sites of DNA damage in live cells.

Michael J Cargill, Alicia Morales, Shashidhar Ravishankar, Edus H Warren

Open access · greenAbstract read
In one paragraph

Article in DNA repair, 2021. 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
1.7field-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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  6. Review
  7. Role of DEAD/DEAH-box helicases in immunity, infection and cancers.Cell communication and signaling : CCS · 2025
    Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
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  16. Liquid-liquid phase separation in tumor biology.Signal transduction and targeted therapy · 2022
    Review
  17. Article
  18. Review
  19. 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

4 authors at 2 institutions in 1 country.

Michael J CargillClinical Research Division, Fred Hutchinson Cancer Research Center, Seattle, WA, USA; Department of Laboratory Medicine and Pathology, University of Washington, Seattle, WA, USA. Electronic address: mcargill@fredhutch.org.
Alicia MoralesClinical Research Division, Fred Hutchinson Cancer Research Center, Seattle, WA, USA.
Shashidhar RavishankarClinical Research Division, Fred Hutchinson Cancer Research Center, Seattle, WA, USA.
Edus H WarrenClinical Research Division, Fred Hutchinson Cancer Research Center, Seattle, WA, USA; Department of Laboratory Medicine and Pathology, University of Washington, Seattle, WA, USA; Department of Medicine, University of Washington, Seattle, WA, USA.
Fred Hutch Cancer Center · USUniversity of Washington · US

Funding

Translational Bioimaging Core Shared ResourceP30CA015704 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI Eric Collisson · 1985 to 2026
$296.4M
High-Performance Compute Cluster for Comprehensive Cancer and Infectious Diseases ResearchS10OD028685 · OD · FRED HUTCHINSON CANCER RESEARCH CENTER · PI BRADLEY, PHILIP · 2020 to 2020
$2.0M
NCI NIH HHS P30 CA015704NIH HHS S10 OD028685
6 · The paper itself

Abstract

Recent studies have suggested that human RNA helicase, DDX3X, is important for DNA repair, but little is known about the nuclear activity of this protein. In vitro analysis of nuclear DDX3X interactions and localization with DNA damage pointed to a direct role for DDX3X in the DNA damage response. We aimed to investigate whether DDX3X plays a direct role in the DNA damage response in live cells. In order to track nuclear DDX3X, we generated a nuclear-export deficient DDX3X mutant construct and performed microirradiation in live cells. We found that DDX3X accumulates at sites of microirradiation shortly after DNA damage induction. We further found DDX3X recruitment to be mediated by its intrinsically disordered domains, similar to other RNA binding proteins that are recruited to sites of DNA damage. Inhibition of liquid-liquid phase separation also reduced DDX3X recruitment. CRISPR/Cas9-mediated knockout of PARP1 ablated DDX3X recruitment, which was restored upon transgenic expression of wild-type PARP1 but not catalytically inactive PARP1, suggesting that DDX3X recruitment is PARP1-dependent.

Indexed as

DNA DamageDNA RepairPoly (ADP-Ribose) Polymerase-1Cell LineCell NucleusDEAD-box RNA HelicasesDNAHEK293 CellsHumansDDX3X protein, humanDEAD-box RNA HelicasesDNAPARP1 protein, humanPoly (ADP-Ribose) Polymerase-1DDX3XDNA damageRNA helicase

Identifiers

PMID34083132
PMCPMC8544569
OpenAlexW3161680498

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.