Evidence map›Paper›PMID 18689438›Full record

ArticleNucleic acids research2008

Interactions between branched DNAs and peptide inhibitors of DNA repair.

Kevin V Kepple, Namita Patel, Peter Salamon, Anca M Segall

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

20 citing papers in PubMed, 37 citations in OpenAlex.

  1. Trial
  2. Review
  3. Supramolecular Recognition of a DNA Four-Way Junction by an MAngewandte Chemie (International ed. in English) · 2025
    Article
  4. Review
  5. DNA Holliday Junction: History, Regulation and Bioactivity.International journal of molecular sciences · 2022
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Antimicrobial metallopeptides with broad nuclease and ribonuclease activity.Chemical communications (Cambridge, England) · 2013
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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.

Kevin V KeppleCenter for Microbial Sciences and Department of Biology, San Diego State University, San Diego, CA 92182, USA.
Namita Patel
Peter Salamon
Anca M Segall
San Diego State University · US

Funding

PATHWAYS OF LAMBDA SITE SPECIFIC RECOMBINATIONR01GM052847 · NIGMS · SAN DIEGO STATE UNIVERSITY · PI SEGALL, ANCA MARA · 1996 to 2010
$2.4M
Novel antibiotics that trap Holliday junctionsR01AI058253 · NIAID · SAN DIEGO STATE UNIVERSITY · PI SEGALL, ANCA MARA · 2004 to 2008
$2.3M
NIAID NIH HHS R01 AI058253NIAID NIH HHS R01 AI58253NIGMS NIH HHS R01 GM052847
6 · The paper itself

Abstract

The RecG helicase of Escherichia coli unwinds both Holliday junction (HJ) and replication fork DNA substrates. Our lab previously identified and characterized peptides (WRWYCR and KWWCRW) that block the activity of RecG on these substrates. We determined that the peptides bind HJ DNA and prevent the binding of RecG. Herein, we present further evidence that the peptides are competitive inhibitors of RecG binding to its substrates. We have generated structural models of interactions between WRWYCR and a junction substrate. Using the fluorescent probe 2-aminopurine, we show that inhibitors interact with highest affinity with HJs (K(d) = 14 nM) and approximately 4- to 9-fold more weakly with replication fork substrates. The fluorescence assay results agree with the structural model, and predict the molecular basis for interactions between HJ-trapping peptides and branched DNA molecules. Specifically, aromatic amino acids in the peptides stack with bases at the center of the DNA substrates. These interactions are stabilized by hydrogen bonds to the DNA and by intrapeptide interactions. These peptides inhibit several proteins involved in DNA repair in addition to RecG, have been useful as tools to dissect recombination, and possess antibiotic activity. Greater understanding of the peptides' mechanism of action will further increase their utility.

Indexed as

Binding, CompetitiveDithiothreitolDNADNA, CruciformDNA HelicasesDNA RepairDNA ReplicationEnzyme InhibitorsEscherichia coli ProteinsModels, MolecularNucleic Acid ConformationOligopeptidesProtein BindingDithiothreitolDNADNA, CruciformDNA HelicasesEnzyme InhibitorsEscherichia coli ProteinsOligopeptidesRecG protein, E coli

Identifiers

PMID18689438
PMCPMC2532710
OpenAlexW2063764249

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.