Evidence map›Paper›PMID 41023391›Full record

ArticleCommunications chemistry2025

Mechanistic insight into the dynamics of Mur ligase through a comprehensive timescale-specific approach.

Iza Ogris, Barbara Zupančič, Izidor Sosič, Franci Merzel, Simona Golič Grdadolnik

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Communications chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. 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

5 authors.

Iza OgrisLaboratory for Molecular Structural Dynamics, Theory Department, National Institute of Chemistry, Ljubljana, Slovenia.ORCID http://orcid.org/0000-0001-6690-1985
Barbara ZupančičLaboratory for Molecular Structural Dynamics, Theory Department, National Institute of Chemistry, Ljubljana, Slovenia. barbara.zupancic@ki.si.ORCID http://orcid.org/0000-0001-7296-8086
Izidor SosičFaculty of Pharmacy, University of Ljubljana, Ljubljana, Slovenia.ORCID http://orcid.org/0000-0002-3370-4587
Franci MerzelLaboratory for Molecular Structural Dynamics, Theory Department, National Institute of Chemistry, Ljubljana, Slovenia.ORCID http://orcid.org/0000-0002-2748-4901
Simona Golič GrdadolnikLaboratory for Molecular Structural Dynamics, Theory Department, National Institute of Chemistry, Ljubljana, Slovenia. simona.grdadolnik@ki.si.ORCID http://orcid.org/0000-0002-0873-9593

Funding

The Slovenian Research and Innovation Agency (ARIS) J1-4400The Slovenian Research and Innovation Agency (ARIS) P1-0010The Slovenian Research and Innovation Agency (ARIS) P1-0208
6 · The paper itself

Abstract

Muramyl ligases are multidomain enzymes involved in intracellular steps of bacterial peptidoglycan synthesis and are considered promising targets for the development of new antibacterial agents. Among them, Mur ligase D (MurD) has been most widely used for structure-based design, but success has been limited. Here, we determine the

Identifiers

PMID41023391
PMCPMC12480691

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.