Evidence map›Paper›PMID 31996740›Full record

ArticleScientific reports2020

Differential Repair Protein Recruitment at Sites of Clustered and Isolated DNA Double-Strand Breaks Produced by High-Energy Heavy Ions.

Burkhard Jakob, Monika Dubiak-Szepietowska, Ellen Janiel, Alina Schmidt, Marco Durante, Gisela Taucher-Scholz

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
2.4field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.

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  5. High-LET charged particles: radiobiology and application for new approaches in radiotherapy.Strahlentherapie und Onkologie : Organ der Deutschen Rontgengesellschaft ... [et al] · 2023
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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 1 country.

Burkhard JakobDepartment of Biophysics, GSI Helmholtzzentrum für Schwerionenforschung, 64291, Darmstadt, Germany. b.jakob@gsi.de.
Monika Dubiak-SzepietowskaDepartment of Biophysics, GSI Helmholtzzentrum für Schwerionenforschung, 64291, Darmstadt, Germany.
Ellen JanielDepartment of Biophysics, GSI Helmholtzzentrum für Schwerionenforschung, 64291, Darmstadt, Germany.
Alina SchmidtDepartment of Biophysics, GSI Helmholtzzentrum für Schwerionenforschung, 64291, Darmstadt, Germany.
Marco DuranteDepartment of Biophysics, GSI Helmholtzzentrum für Schwerionenforschung, 64291, Darmstadt, Germany. m.durante@gsi.de.
Gisela Taucher-ScholzDepartment of Biophysics, GSI Helmholtzzentrum für Schwerionenforschung, 64291, Darmstadt, Germany.
GSI Helmholtz Centre for Heavy Ion Research · DETechnical University of Darmstadt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA double-strand break (DSB) repair is crucial to maintain genomic stability. The fidelity of the repair depends on the complexity of the lesion, with clustered DSBs being more difficult to repair than isolated breaks. Using live cell imaging of heavy ion tracks produced at a high-energy particle accelerator we visualised simultaneously the recruitment of different proteins at individual sites of complex and simple DSBs in human cells. NBS1 and 53BP1 were recruited in a few seconds to complex DSBs, but in 40% of the isolated DSBs the recruitment was delayed approximately 5 min. Using base excision repair (BER) inhibitors we demonstrate that some simple DSBs are generated by enzymatic processing of base damage, while BER did not affect the complex DSBs. The results show that DSB processing and repair kinetics are dependent on the complexity of the breaks and can be different even for the same clastogenic agent.

Indexed as

DNA Breaks, Double-StrandedBinding SitesCell Cycle ProteinsCell Line, TumorDNADNA RepairHeavy IonsHumansNeoplasmsNuclear ProteinsProtein BindingSynchrotronsTumor Suppressor p53-Binding Protein 1Cell Cycle ProteinsDNANBN protein, humanNuclear ProteinsTP53BP1 protein, humanTumor Suppressor p53-Binding Protein 1

Identifiers

PMID31996740
PMCPMC6989695
OpenAlexW3003449700

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.