Evidence map›Paper›PMID 17392343›Full record

ArticleNucleic acids research2007

High-resolution AFM imaging of single-stranded DNA-binding (SSB) protein--DNA complexes.

Loïc Hamon, David Pastré, Pauline Dupaigne, Cyrille Le Breton, Eric Le Cam, Olivier Piétrement

Open access · goldAbstract readEvaluation Study
In one paragraph

Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
2.7field-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

63 citing papers in PubMed, 144 citations in OpenAlex.

  1. Nanoscale Analysis of SSB-RecO Interplay in SSB Interaction with the Target.International journal of molecular sciences · 2026
    Article
  2. Article
  3. CoNanoscale · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. 3D Generation of Multipurpose Atomic Force Microscopy Tips.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Article
  14. Article
  15. Article
  16. Review
  17. Stochastic Modelling ofMolecules (Basel, Switzerland) · 2021
    Article
  18. Article
  19. A comparative study of protein-ssDNA interactions.NAR genomics and bioinformatics · 2021
    Article
  20. Article

3 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

6 authors at 4 institutions in 1 country.

Loïc HamonLaboratoire de Structure et Activité des Biomolécules Normales et Pathologiques, INSERM U829, Université d'Evry-Val d'Essonne EA3637, Evry, F-91025, France. loic.hamon@univ-evry.fr
David Pastré
Pauline Dupaigne
Cyrille Le Breton
Eric Le Cam
Olivier Piétrement
Laboratoire des Biomolécules · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRInserm · FRInstitut Gustave Roussy · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA in living cells is generally processed via the generation and the protection of single-stranded DNA involving the binding of ssDNA-binding proteins (SSBs). The studies of SSB-binding mode transition and cooperativity are therefore critical to many cellular processes like DNA repair and replication. However, only a few atomic force microscopy (AFM) investigations of ssDNA nucleoprotein filaments have been conducted so far. The point is that adsorption of ssDN A-SSB complexes on mica, necessary for AFM imaging, is not an easy task. Here, we addressed this issue by using spermidine as a binding agent. This trivalent cation induces a stronger adsorption on mica than divalent cations, which are commonly used by AFM users but are ineffective in the adsorption of ssDNA-SSB complexes. At low spermidine concentration (<0.3 mM), we obtained AFM images of ssDNA-SSB complexes (E. coli SSB, gp32 and yRPA) on mica at both low and high ionic strengths. In addition, partially or fully saturated nucleoprotein filaments were studied at various monovalent salt concentrations thus allowing the observation of SSB-binding mode transition. In association with conventional biochemical techniques, this work should make it possible to study the dynamics of DNA processes involving DNA-SSB complexes as intermediates by AFM.

Indexed as

Aluminum SilicatesDNA-Binding ProteinsDNA, Single-StrandedElectrophoresis, Agar GelEscherichia coli ProteinsMicroscopy, Atomic ForceSpermidineAluminum SilicatesDNA-Binding ProteinsDNA, Single-StrandedEscherichia coli ProteinsmicaSpermidine

Identifiers

PMID17392343
PMCPMC1885666
OpenAlexW2128923895

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.