Evidence map›Paper›PMID 23801766›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Combined optical and topographic imaging reveals different arrangements of human RAD54 with presynaptic and postsynaptic RAD51-DNA filaments.

Humberto Sanchez, Aryandi Kertokalio, Sari van Rossum-Fikkert, Roland Kanaar, Claire Wyman

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. 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
1.3field-weighted citation impact, top 20% 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, 36 citations in OpenAlex.

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  11. Studying protein-DNA interactions using atomic force microscopy.Seminars in cell & developmental biology · 2018
    Review
  12. Article
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  15. Novel insights into RAD51 activity and regulation during homologous recombination and DNA replication.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2016
    Review
  16. Article
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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

5 authors at 1 institution in 1 country.

Humberto SanchezDepartment of Genetics, Erasmus Medical Center, Rotterdam 3000 CA, The Netherlands.
Aryandi Kertokalio
Sari van Rossum-Fikkert
Roland Kanaar
Claire Wyman
Erasmus MC · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Essential genome transactions, such as homologous recombination, are achieved by concerted and dynamic interactions of multiple protein components with DNA. Which proteins do what and how, will be reflected in their relative arrangements. However, obtaining high-resolution structural information on the variable arrangements of these complex assemblies is a challenge. Here we demonstrate the versatility of a combined total internal reflection fluorescence and scanning force microscope (TIRF-SFM) to pinpoint fluorescently labeled human homologous recombination protein RAD54 interacting with presynaptic (ssDNA) and postsynaptic (dsDNA) human recombinase RAD51 nucleoprotein filaments. Labeled proteins were localized by superresolution imaging on complex structures in the SFM image with high spatial accuracy. We observed some RAD54 at RAD51 filament ends, as expected. More commonly, RAD54 interspersed along RAD51-DNA filaments. RAD54 promotes RAD51-mediated DNA strand exchange and has been described to both stabilize and destabilize RAD51-DNA filaments. The different architectural arrangements we observe for RAD54 with RAD51-DNA filaments may reflect the diverse roles of this protein in homologous recombination.

Indexed as

DNADNA-Binding ProteinsDNA HelicasesFluorescent DyesHumansMicroscopyNuclear ProteinsRad51 RecombinaseSynapsesDNADNA-Binding ProteinsDNA HelicasesFluorescent DyesNuclear ProteinsRAD51 protein, humanRad51 RecombinaseRAD54L protein, humanDNA break repairDNA–protein interactiongenome stabilityimage registrationsingle-molecule microscopy

Identifiers

PMID23801766
PMCPMC3710881
OpenAlexW2042461423

What OpenQuestion holds

Textmetadata
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.