Evidence map›Paper›PMID 27438853›Full record

ArticleToxins2016

Mapping Protein-Protein Interactions of the Resistance-Related Bacterial Zeta Toxin-Epsilon Antitoxin Complex (ε₂ζ₂) with High Affinity Peptide Ligands Using Fluorescence Polarization.

María Isabel Fernández-Bachiller, Iwona Brzozowska, Norbert Odolczyk, Urszula Zielenkiewicz, Piotr Zielenkiewicz, Jörg Rademann

Open access · goldAbstract read
In one paragraph

Article in Toxins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed, 1 pooled it
1.2field-weighted citation impact, top 16% 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

10 citing papers in PubMed, 1 synthesis or guideline pooled it, 14 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. TheToxins · 2018
    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

6 authors at 3 institutions in 2 countries.

María Isabel Fernández-BachillerInstitute of Pharmacy, Pharmaceutical and Medicinal Chemistry, Freie Universität Berlin, Königin-Luise-Str. 2+4, 14195 Berlin, Germany. isabelfernandezb77@yahoo.es.
Iwona BrzozowskaInstitute of Biochemistry and Biophysics, PAS, Pawińskiego 5a, 02-106 Warszawa, Poland. iwonab@ibb.waw.pl.
Norbert OdolczykInstitute of Biochemistry and Biophysics, PAS, Pawińskiego 5a, 02-106 Warszawa, Poland. nodolczyk@ibb.waw.pl.
Urszula ZielenkiewiczInstitute of Biochemistry and Biophysics, PAS, Pawińskiego 5a, 02-106 Warszawa, Poland. ulazet@ibb.waw.pl.
Piotr ZielenkiewiczInstitute of Biochemistry and Biophysics, PAS, Pawińskiego 5a, 02-106 Warszawa, Poland. piotr@ibb.waw.pl.
Jörg RademannInstitute of Pharmacy, Pharmaceutical and Medicinal Chemistry, Freie Universität Berlin, Königin-Luise-Str. 2+4, 14195 Berlin, Germany. joerg.rademann@fu-berlin.de.
Institute of Biochemistry and Biophysics, Polish Academy of Sciences · PLFreie Universität Berlin · DEUniversity of Warsaw · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Toxin-antitoxin systems constitute a native survival strategy of pathogenic bacteria and thus are potential targets of antibiotic drugs. Here, we target the Zeta-Epsilon toxin-antitoxin system, which is responsible for the stable maintenance of certain multiresistance plasmids in Gram-positive bacteria. Peptide ligands were designed on the basis of the ε₂ζ₂ complex. Three α helices of Zeta forming the protein-protein interaction (PPI) site were selected and peptides were designed conserving the residues interacting with Epsilon antitoxin while substituting residues binding intramolecularly to other parts of Zeta. Designed peptides were synthesized with an N-terminal fluoresceinyl-carboxy-residue for binding assays and provided active ligands, which were used to define the hot spots of the ε₂ζ₂ complex. Further shortening and modification of the binding peptides provided ligands with affinities <100 nM, allowing us to determine the most relevant PPIs and implement a robust competition binding assay.

Indexed as

Drug Resistance, Multiple, BacterialFluorescence PolarizationProtein Interaction MapsAnti-Bacterial AgentsAntitoxinsBacteriaBacterial ToxinsBinding, CompetitiveDrug DesignLigandsModels, MolecularPeptidesProtein BindingProtein Conformation, alpha-HelicalProtein Interaction MappingStructure-Activity RelationshipAnti-Bacterial AgentsAntitoxinsBacterial ToxinsLigandsPeptidesbacterial resistancedrug discoveryfluorescence polarizationprotein–protein interactionstoxin–antitoxin system

Identifiers

PMID27438853
PMCPMC4963854
OpenAlexW2498196872

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.