Evidence map›Paper›PMID 23393192›Full record

ArticleNucleic acids research2013

Single-molecule sorting reveals how ubiquitylation affects substrate recognition and activities of FBH1 helicase.

Tokiha Masuda-Ozawa, Trish Hoang, Yeon-Soo Seo, Lin-Feng Chen, Maria Spies

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.7field-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

26 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Making Choices: DNA Replication Fork Recovery Mechanisms.Seminars in cell & developmental biology · 2021
    Review
  10. Replication Fork Reversal and Protection.Frontiers in cell and developmental biology · 2021
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Single-molecule sorting of DNA helicases.Methods (San Diego, Calif.) · 2016
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  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 1 institution in 1 country.

Tokiha Masuda-OzawaDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Trish Hoang
Yeon-Soo Seo
Lin-Feng Chen
Maria Spies
University of Illinois Urbana-Champaign · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA repair helicases function in the cell to separate DNA duplexes or remodel nucleoprotein complexes. These functions are influenced by sensing and signaling; the cellular pool of a DNA helicase may contain subpopulations of enzymes carrying different post-translational modifications and performing distinct biochemical functions. Here, we report a novel experimental strategy, single-molecule sorting, which overcomes difficulties associated with comprehensive analysis of heterologously modified pool of proteins. This methodology was applied to visualize human DNA helicase F-box-containing DNA helicase (FBH1) acting on the DNA structures resembling a stalled or collapsed replication fork and its interactions with RAD51 nucleoprotein filament. Individual helicase molecules isolated from human cells with their native post-translational modifications were analyzed using total internal reflection fluorescence microscopy. Separation of the activity trajectories originated from ubiquitylated and non-ubiquitylated FBH1 molecules revealed that ubiquitylation affects FBH1 interaction with the RAD51 nucleoprotein filament, but not its translocase and helicase activities.

Indexed as

UbiquitinationBinding SitesDNADNA-Binding ProteinsDNA HelicasesDNA ReplicationHEK293 CellsHumansProtein Structure, TertiaryRad51 RecombinaseDNADNA-Binding ProteinsDNA HelicasesFBH1 protein, humanRad51 Recombinase

Identifiers

PMID23393192
PMCPMC3616717
OpenAlexW2150587062

What OpenQuestion holds

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LicenceCC BY-NC
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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.