Evidence map›Paper›PMID 30233559›Full record

ArticleFrontiers in microbiology2018

The Fluorescent D-Amino Acid NADA as a Tool to Study the Conditional Activity of Transpeptidases in

Alejandro Montón Silva, Christian Otten, Jacob Biboy, Eefjan Breukink, Michael VanNieuwenhze, Waldemar Vollmer, Tanneke den Blaauwen

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Activity Profiling of Mycobacterial L,D-Transpeptidases.bioRxiv : the preprint server for biology · 2026
    Article
  4. Peptidoglycan LD-Transpeptidases.Antibiotics (Basel, Switzerland) · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Cleavage of Braun's lipoprotein Lpp from the bacterial peptidoglycan by a paralog of l,d-transpeptidases, LdtF.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Article
  17. Review
  18. A How-To Guide for Mode of Action Analysis of Antimicrobial Peptides.Frontiers in cellular and infection microbiology · 2020
    Review
  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

7 authors at 4 institutions in 3 countries.

Alejandro Montón SilvaBacterial Cell Biology and Physiology, Swammerdam Institute for Life Sciences, University of Amsterdam, Amsterdam, Netherlands.
Christian OttenCentre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, United Kingdom.
Jacob BiboyCentre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, United Kingdom.
Eefjan BreukinkDepartment of Membrane Biochemistry and Biophysics, Institute of Biomembranes, Utrecht University, Utrecht, Netherlands.
Michael VanNieuwenhzeDepartment of Chemistry, Indiana University Bloomington, Bloomington, IN, United States.
Waldemar VollmerCentre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, United Kingdom.
Tanneke den BlaauwenBacterial Cell Biology and Physiology, Swammerdam Institute for Life Sciences, University of Amsterdam, Amsterdam, Netherlands.
Newcastle University · GBUniversity of Amsterdam · NLIndiana University Bloomington · USUtrecht University · NL

Funding

Dynamics of bacterial peptidoglycan synthesisR01GM113172 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI BRUN, YVES V, VANNIEUWENHZE, MICHAEL S · 2015 to 2018
$3.5M
Medical Research Council MR/N501840/1NIGMS NIH HHS R01 GM113172
6 · The paper itself

Abstract

The enzymes responsible for the synthesis of the peptidoglycan (PG) layer constitute a fundamental target for a large group of antibiotics. The family of β-lactam antibiotics inhibits the DD-transpeptidase (TPase) activity of the penicillin binding proteins (PBPs), whereas its subgroup of carbapenems can also block the TPase activity of the LD-TPases. D-Ala fluorescent probes, such as NADA, are incorporated into the PG presumably by TPases in

Indexed as

aztreonamcell divisionE. coliLdtDNADApeptidoglycantranspeptidases

Identifiers

PMID30233559
PMCPMC6131605
OpenAlexW2890250468

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.