Evidence map›Paper›PMID 21827943›Full record

ArticleStructure (London, England : 1993)2011

Real-time observation of strand exchange reaction with high spatiotemporal resolution.

Kaushik Ragunathan, Chirlmin Joo, Taekjip Ha

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

39 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. NProceedings of the National Academy of Sciences of the United States of America · 2025
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  8. Helicase-like functions in phosphate loop containing beta-alpha polypeptides.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Mismatch sensing by nucleofilament deciphers mechanism of RecA-mediated homologous recombination.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. The intrinsic ability of double-stranded DNA to carry out D-loop and R-loop formation.Computational and structural biotechnology journal · 2020
    Review
  12. Article
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  14. Review
  15. Article
  16. Article
  17. A time for promiscuity in a eukaryotic recombinase.The Journal of biological chemistry · 2017
    Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Kaushik RagunathanCenter for Biophysics and Computational Biology, Department of Physics, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Chirlmin Joo
Taekjip Ha
University of Illinois Urbana-Champaign · USHoward Hughes Medical Institute · US

Funding

Single Molecule Study of Helicase MechanismsR01GM065367 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI HA, TAEKJIP · 2002 to 2014
$3.6M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM065367
6 · The paper itself

Abstract

RecA binds to single-stranded (ss) DNA to form a helical filament that catalyzes strand exchange with a homologous double-stranded (ds) DNA. The study of strand exchange in ensemble assays is limited by the diffusion limited homology search process, which masks the subsequent strand exchange reaction. We developed a single-molecule fluorescence assay with a few base-pair and millisecond resolution that can separate initial docking from the subsequent propagation of joint molecule formation. Our data suggest that propagation occurs in 3 bp increments with destabilization of the incoming dsDNA and concomitant pairing with the reference ssDNA. Unexpectedly, we discovered the formation of a dynamic complex between RecA and the displaced DNA that remains bound transiently after joint molecule formation. This finding could have important implications for the irreversibility of strand exchange. Our model for strand exchange links structural models of RecA to its catalytic function.

Indexed as

Crossing Over, GeneticAdenosine TriphosphateBase SequenceDNA, Single-StrandedEscherichia coli ProteinsFluorescence Resonance Energy TransferHydrolysisImmobilized ProteinsKineticsRec A RecombinasesSpectrometry, FluorescenceAdenosine TriphosphateDNA, Single-StrandedEscherichia coli ProteinsImmobilized ProteinsRec A Recombinases

Identifiers

PMID21827943
PMCPMC3163668
OpenAlexW2072683019

What OpenQuestion holds

Textmetadata
LicenceTDM
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.