Evidence map›Paper›PMID 27025527›Full record

ReviewAntibiotics (Basel, Switzerland)2016

Glycosyltransferases and Transpeptidases/Penicillin-Binding Proteins: Valuable Targets for New Antibacterials.

Eric Sauvage, Mohammed Terrak

Open access · goldAbstract readReview
In one paragraph

Review in Antibiotics (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed, 1 pooled it
5.0field-weighted citation impact, top 4% 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

69 citing papers in PubMed, 1 synthesis or guideline pooled it, 142 citations in OpenAlex.

  1. Drug-resistantClinical microbiology reviews · 2025
    Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. JACS Au · 2026
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Penicillin-Binding Proteins inAntibiotics (Basel, Switzerland) · 2026
    Review
  12. Article
  13. Article
  14. Review
  15. Combining live fluorescence imaging with in situ cryoelectron tomography sheds light on the septation process inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Lipopeptide antibiotics disrupt interactions of undecaprenyl phosphate with UptA.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article

9 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

2 authors at 1 institution in 1 country.

Eric SauvageCentre d'Ingénierie des Protéines, University of Liège, B6a, Quartier Agora, allée du six Août 11, 4000 Liège 1, Belgium. eric.sauvage@ulg.ac.be.
Mohammed TerrakCentre d'Ingénierie des Protéines, University of Liège, B6a, Quartier Agora, allée du six Août 11, 4000 Liège 1, Belgium. mterrak@ulg.ac.be.
University of Liège · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptidoglycan (PG) is an essential macromolecular sacculus surrounding most bacteria. It is assembled by the glycosyltransferase (GT) and transpeptidase (TP) activities of multimodular penicillin-binding proteins (PBPs) within multiprotein complex machineries. Both activities are essential for the synthesis of a functional stress-bearing PG shell. Although good progress has been made in terms of the functional and structural understanding of GT, finding a clinically useful antibiotic against them has been challenging until now. In contrast, the TP/PBP module has been successfully targeted by β-lactam derivatives, but the extensive use of these antibiotics has selected resistant bacterial strains that employ a wide variety of mechanisms to escape the lethal action of these antibiotics. In addition to traditional β-lactams, other classes of molecules (non-β-lactams) that inhibit PBPs are now emerging, opening new perspectives for tackling the resistance problem while taking advantage of these valuable targets, for which a wealth of structural and functional knowledge has been accumulated. The overall evidence shows that PBPs are part of multiprotein machineries whose activities are modulated by cofactors. Perturbation of these systems could lead to lethal effects. Developing screening strategies to take advantage of these mechanisms could lead to new inhibitors of PG assembly. In this paper, we present a general background on the GTs and TPs/PBPs, a survey of recent issues of bacterial resistance and a review of recent works describing new inhibitors of these enzymes.

Indexed as

antibiotics resistanceglycosyltransferaselipid IIpenicillin-binding proteinspeptidoglycantranspeptidaseβ-lactam

Identifiers

PMID27025527
PMCPMC4810414
OpenAlexW2275498402

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.