Evidence map›Paper›PMID 28653661›Full record

ArticleNature communications2017

The structural and functional characterization of human RecQ4 reveals insights into its helicase mechanism.

Sebastian Kaiser, Florian Sauer, Caroline Kisker

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. 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
1.8field-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, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Frontiers in plant science · 2023
    Article
  11. Article
  12. Review
  13. RecQ Helicase Somatic Alterations in Cancer.Frontiers in molecular biosciences · 2022
    Review
  14. miR-376a Provokes Rectum AdenocarcinomaFrontiers in cell and developmental biology · 2021
    Article
  15. Molecular Mechanisms of the RECQ4 Pathogenic Mutations.Frontiers in molecular biosciences · 2021
    Review
  16. Human RecQ Helicases in DNA Double-Strand Break Repair.Frontiers in cell and developmental biology · 2021
    Review
  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

3 authors at 1 institution in 1 country.

Sebastian KaiserRudolf-Virchow-Center for Experimental Biomedicine, Institute of Structural Biology, Josef-Schneider-Str. 2/D15, Wuerzburg 97080, Germany.
Florian SauerRudolf-Virchow-Center for Experimental Biomedicine, Institute of Structural Biology, Josef-Schneider-Str. 2/D15, Wuerzburg 97080, Germany.
Caroline KiskerRudolf-Virchow-Center for Experimental Biomedicine, Institute of Structural Biology, Josef-Schneider-Str. 2/D15, Wuerzburg 97080, Germany.
Institute for Biomedicine · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RecQ4 is a member of the RecQ helicase family, an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair and replication. While reduced RecQ4 activity is associated with cancer predisposition and premature aging, RecQ4 upregulation is related to carcinogenesis and metastasis. Within the RecQ family, RecQ4 assumes an exceptional position, lacking several characteristic RecQ domains. Here we present the crystal structure of human RecQ4, encompassing the conserved ATPase core and a novel C-terminal domain that lacks resemblance to the RQC domain observed in other RecQ helicases. The new domain features a zinc-binding site and two distinct types of winged-helix domains, which are not involved in canonical DNA binding or helicase activity. Based on our structural and functional analysis, we propose that RecQ4 exerts a helicase mechanism, which may be more closely related to bacterial RecQ helicases than to its human family members.

Indexed as

Binding SitesBiocatalysisDNA HelicasesDNA RepairHumansProtein DomainsRecQ HelicasesZincDNA HelicasesRecQ HelicasesRECQL4 protein, humanZinc

Identifiers

PMID28653661
PMCPMC5490261
OpenAlexW2725043166

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.