Evidence map›Paper›PMID 39704542›Full record

ArticlemBio2025

Identification and characterization of the functional tetrameric UDP-glucose pyrophosphorylase from

Isabel Ramón Roth, Pavel Kats, Timm Fiebig, Françoise Routier, Roman Fedorov, Larissa Dirr, Jana I Führing

Abstract read
In one paragraph

Article in mBio, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Quorum sensing geneFrontiers in microbiology · 2026
    Article
  3. 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.

Isabel Ramón RothInstitute of Clinical Biochemistry, Hannover Medical School, Hannover, Germany.ORCID 0000-0003-2768-9736
Pavel KatsInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.ORCID 0009-0003-0908-6621
Timm FiebigInstitute of Clinical Biochemistry, Hannover Medical School, Hannover, Germany.ORCID 0000-0002-2021-7296
Françoise RoutierInstitute of Clinical Biochemistry, Hannover Medical School, Hannover, Germany.ORCID 0000-0002-7163-0590
Roman FedorovInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.ORCID 0000-0002-5240-4205
Larissa DirrInstitute for Biomedicine and Glycomics, Griffith University, Gold Coast, Southport, Australia.ORCID 0000-0002-5794-266X
Jana I FühringInstitute of Clinical Biochemistry, Hannover Medical School, Hannover, Germany.ORCID 0000-0001-7174-0442

Funding

Australian Research Council (ARC) Linkage Infrastructure, Equipment and Facilities LE220100068Deutsche Forschungsgemeinschaft (DFG) EXC 2155Deutsche Forschungsgemeinschaft (DFG) FE 1510/2-1DHAC | National Health and Medical Research Council (NHMRC) GNT1157150
6 · The paper itself

Abstract

In all kingdoms of life, the enzyme uridine diphosphate-glucose pyrophosphorylase (UGP) occupies a central role in metabolism, as its reaction product uridine diphosphate-glucose (UDP-Glc) is involved in various crucial cellular processes. Pathogens, including fungi, parasites, and bacteria, depend on UGP for the synthesis of virulence factors; in particular, various bacterial species utilize UDP-Glc and its derivatives for the synthesis of lipopolysaccharides, capsular polysaccharides, and biofilm exopolysaccharides. UGPs have, therefore, gained attention as anti-bacterial drug target candidates, prompting us to study their structure-function relationships to provide a basis for the rational development of specific inhibitors. UGP function is tied to its oligomeric state, and the majority of bacterial homologs have been described as tetramers encoded by the

Indexed as

Bacterial ProteinsKlebsiella pneumoniaeUTP-Glucose-1-Phosphate UridylyltransferaseModels, MolecularProtein MultimerizationStructure-Activity RelationshipBacterial ProteinsUTP-Glucose-1-Phosphate UridylyltransferaseAlphaFold modelantibacterial drug targetdimerizationenzymatic mechanismgalFgalUKlebsiella pneumoniaenucleotidyltransferaseprotein oligomerizationstructure-function relationshiptetramerizationUDP-glucose pyrophosphorylase

Identifiers

PMID39704542
PMCPMC11796359

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.