Evidence map›Paper›PMID 39669780›Full record

ArticleFrontiers in microbiology2024

Structure-based targeting of the lipid A-modifying enzyme PmrC to contrast colistin resistance in

Maria Romano, Federico Falchi, Eliana De Gregorio, Maria Stabile, Antonella Migliaccio, Alessia Ruggiero, Valeria Napolitano, Ida Autiero, Flavia Squeglia, Rita Berisio

Abstract read
In one paragraph

Article in Frontiers in microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. PFK-158 enhances colistin efficacy against resistantFrontiers in veterinary science · 2026
    Article
  4. 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

10 authors.

Maria Romano *Department of Biomedical Sciences, Institute of Biostructures and Bioimaging, National Research Council (CNR), Napoli, Italy.
Federico Falchi *Department of Pharmacy and Biotechnology, Alma Mater Studiorum-University of Bologna, Bologna, Italy.
Eliana De GregorioDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Naples, Italy.
Maria StabileDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Naples, Italy.
Antonella MigliaccioDepartment of Public Health, University of Naples Federico II, Naples, Italy.
Alessia RuggieroDepartment of Biomedical Sciences, Institute of Biostructures and Bioimaging, National Research Council (CNR), Napoli, Italy.
Valeria NapolitanoDepartment of Biomedical Sciences, Institute of Biostructures and Bioimaging, National Research Council (CNR), Napoli, Italy.
Ida AutieroDepartment of Biomedical Sciences, Institute of Biostructures and Bioimaging, National Research Council (CNR), Napoli, Italy.
Flavia SquegliaDepartment of Biomedical Sciences, Institute of Biostructures and Bioimaging, National Research Council (CNR), Napoli, Italy.
Rita BerisioDepartment of Biomedical Sciences, Institute of Biostructures and Bioimaging, National Research Council (CNR), Napoli, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Introduction: Antimicrobial-resistant pathogens are an ongoing threat to human and animal health. According to the World Health Organization (WHO), colistin is considered the last resort antibiotic against human infections due to multidrug-resistant Gram-negative organisms-including Methods: The recombinant production of large membrane proteins in their native forms is a bottleneck in modern molecular biology. In this study, we recombinantly produced PmrC and biophysically characterised it in solution. We employed Results: We successfully produced PmrC PetN transferase membrane protein in high yields and showed that PmrC is a stable α-β protein, with melting temperature T Discussion: Our study provides a molecular characterisation of PmrC and demonstrates the importance of PmrC as a drug target and the strong potential of PmrC binding molecules to act as colistin adjuvants, operating as synergistic tools to combat multiresistant nosocomial pathogens.

Indexed as

cell wallcolistin resistancepEtN transferaseprotein structurevirtual screening

Identifiers

PMID39669780
PMCPMC11634806

What OpenQuestion holds

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Registered trials

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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.