Evidence map›Paper›PMID 28934502›Full record

ArticleNucleic acids research2017

Blocking the RecA activity and SOS-response in bacteria with a short α-helical peptide.

Alexander Yakimov, Georgii Pobegalov, Irina Bakhlanova, Mikhail Khodorkovskii, Michael Petukhov, Dmitry Baitin

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.6field-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

25 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Snapshots ofiScience · 2025
    Article
  8. Article
  9. mLife · 2024
    Review
  10. Article
  11. Article
  12. Structural basis for regulation of SOS response in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Role of the SOS Response in the Generation of Antibiotic ResistanceAntimicrobial agents and chemotherapy · 2021
    Article
  18. Article
  19. Review
  20. Targeting evolution of antibiotic resistance by SOS response inhibition.Computational and structural biotechnology journal · 2021
    Review
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 1 institution in 1 country.

Alexander YakimovDepartment of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute (B.P.Konstantinov of National Research Centre 'Kurchatov Institute'), Gatchina 188300, Russia.
Georgii PobegalovPeter the Great St Petersburg Polytechnic University, St Petersburg 195251, Russia.
Irina BakhlanovaDepartment of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute (B.P.Konstantinov of National Research Centre 'Kurchatov Institute'), Gatchina 188300, Russia.
Mikhail KhodorkovskiiPeter the Great St Petersburg Polytechnic University, St Petersburg 195251, Russia.
Michael PetukhovDepartment of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute (B.P.Konstantinov of National Research Centre 'Kurchatov Institute'), Gatchina 188300, Russia.
Dmitry BaitinDepartment of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute (B.P.Konstantinov of National Research Centre 'Kurchatov Institute'), Gatchina 188300, Russia.
Peter the Great St. Petersburg Polytechnic University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The RecX protein, a very active natural RecA protein inhibitor, can completely disassemble RecA filaments at nanomolar concentrations that are two to three orders of magnitude lower than that of RecA protein. Based on the structure of RecX protein complex with the presynaptic RecA filament, we designed a short first in class α-helical peptide that both inhibits RecA protein activities in vitro and blocks the bacterial SOS-response in vivo. The peptide was designed using SEQOPT, a novel method for global sequence optimization of protein α-helices. SEQOPT produces artificial peptide sequences containing only 20 natural amino acids with the maximum possible conformational stability at a given pH, ionic strength, temperature, peptide solubility. It also accounts for restrictions due to known amino acid residues involved in stabilization of protein complexes under consideration. The results indicate that a few key intermolecular interactions inside the RecA protein presynaptic complex are enough to reproduce the main features of the RecX protein mechanism of action. Since the SOS-response provides a major mechanism of bacterial adaptation to antibiotics, these results open new ways for the development of antibiotic co-therapy that would not cause bacterial resistance.

Indexed as

Circular DichroismDNAEscherichia coliEscherichia coli ProteinsModels, MolecularPeptidesProtein ConformationProtein StabilityRec A RecombinasesSOS Response, GeneticsUltraviolet RaysDNAEscherichia coli ProteinsPeptidesRec A RecombinasesRecX protein, E coli

Identifiers

PMID28934502
PMCPMC5766188
OpenAlexW2741120159

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.