Evidence map›Paper›PMID 30295604›Full record

ArticleeLife2018

BRCT domains of the DNA damage checkpoint proteins TOPBP1/Rad4 display distinct specificities for phosphopeptide ligands.

Matthew Day, Mathieu Rappas, Katie Ptasinska, Dominik Boos, Antony W Oliver, Laurence H Pearl

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

22 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  4. Review
  5. Article
  6. Pre-rRNA Facilitates TopBP1-Mediated DNA Double-Strand Break Response.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  7. Untousling the Role of Tousled-like Kinase 1 in DNA Damage Repair.International journal of molecular sciences · 2023
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. The lncRNA Rhno1/miR-6979-5p/BMP2 Axis Modulates Osteoblast Differentiation.International journal of biological sciences · 2020
    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

6 authors at 2 institutions in 2 countries.

Matthew DayCancer Research UK DNA Repair Enzymes Group, Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, United Kingdom.
Mathieu RappasCancer Research UK DNA Repair Enzymes Group, Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, United Kingdom.
Katie PtasinskaGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, United Kingdom.
Dominik BoosFakultät für Biologie, Universität Duisburg-Essen, Germany, United Kingdom.
Antony W OliverCancer Research UK DNA Repair Enzymes Group, Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, United Kingdom.ORCID https://orcid.org/0000-0002-2912-8273
Laurence H PearlCancer Research UK DNA Repair Enzymes Group, Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, United Kingdom.ORCID https://orcid.org/0000-0002-6910-1809
University of Sussex · GBUniversity of Duisburg-Essen · DE

Funding

Cancer Research UK 14532Cancer Research UK 24386Cancer Research UK C302/A14532Cancer Research UK C302/A24386Wellcome Trust
6 · The paper itself

Abstract

TOPBP1 and its fission yeast homologueRad4, are critical players in a range of DNA replication, repair and damage signalling processes. They are composed of multiple BRCT domains, some of which bind phosphorylated motifs in other proteins. They thus act as multi-point adaptors bringing proteins together into functional combinations, dependent on post-translational modifications downstream of cell cycle and DNA damage signals. We have now structurally and/or biochemically characterised a sufficient number of high-affinity complexes for the conserved N-terminal region of TOPBP1 and Rad4 with diverse phospho-ligands, including human RAD9 and Treslin, and

Indexed as

Protein DomainsAmino Acid SequenceCarrier ProteinsDNA-Binding ProteinsDNA DamageHumansLigandsModels, MolecularNuclear ProteinsPhosphopeptidesPhosphorylationProtein BindingSchizosaccharomycesSchizosaccharomyces pombe ProteinsTransglutaminasesCarrier ProteinsDNA-Binding ProteinsLigandsNuclear ProteinsPhosphopeptidesRAD4 protein, S pombeSchizosaccharomyces pombe ProteinsTOPBP1 protein, humanTransglutaminasesbiochemistrychemical biologyDNA Repairhumanmolecular biophysicsphosphorylationpost-translational modificationScaffold proteinsS. pombestructural biology

Identifiers

PMID30295604
PMCPMC6175577
OpenAlexW2828312391

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.