Evidence map›Paper›PMID 19122145›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Direct imaging of human Rad51 nucleoprotein dynamics on individual DNA molecules.

Jovencio Hilario, Ichiro Amitani, Ronald J Baskin, Stephen C Kowalczykowski

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

98 citing papers in PubMed, 161 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. RAD51AP1 is a versatile RAD51 modulator.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  11. Review
  12. ATP hydrolysis-driven structural transitions within thebioRxiv : the preprint server for biology · 2025
    Article
  13. Review
  14. Article
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  16. Article
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  19. BRCA2 chaperones RAD51 to single molecules of RPA-coated ssDNA.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. Article

38 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Jovencio HilarioDepartments of Microbiology and Molecular and Cellular Biology, University of California, Davis, CA 95616-8665, USA.
Ichiro Amitani
Ronald J Baskin
Stephen C Kowalczykowski
University of California, Davis · US

Funding

Single-Molecule Assembly of Protein-DNA ComplexesR01GM064745 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI KOWALCZYKOWSKI, STEPHEN CHARLES · 2002 to 2018
$4.3M
NIGMS NIH HHS GM-64745NIGMS NIH HHS R01 GM064745
6 · The paper itself

Abstract

Rad51 protein (Rad51) is central to recombinational repair of double-strand DNA breaks. It polymerizes onto DNA and promotes strand exchange between homologous chromosomes. We visualized the real-time assembly and disassembly of human Rad51 nucleoprotein filaments on double-stranded DNA by single-molecule fluorescence microscopy. Rad51 assembly extends the DNA by approximately 65%. Nucleoprotein filament formation occurs via rapid nucleation followed by growth from these nuclei. Growth does not continue indefinitely, however, and nucleoprotein filaments terminate when approximately 2 mum in length. The dependence of nascent filament formation on Rad51 concentration suggests that 2-3 Rad51 monomers are involved in nucleation. Rad51 nucleoprotein filaments are stable and remain extended when ATP hydrolysis is prevented; however, when permitted, filaments decrease in length as a result of conversion to ADP-bound nucleoprotein complexes and partial protein dissociation. Dissociation of Rad51 from dsDNA is slow and incomplete, thereby rationalizing the need for other proteins that facilitate disassembly.

Indexed as

Optical TweezersAdenosine DiphosphateDiagnostic ImagingDNAHumansIntermediate Filament ProteinsKineticsMicroscopy, FluorescenceNucleoproteinsProtein BindingRad51 RecombinaseAdenosine DiphosphateDNAIntermediate Filament ProteinsNucleoproteinsRad51 Recombinase

Identifiers

PMID19122145
PMCPMC2613362
OpenAlexW2009309406

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.