Evidence map›Paper›PMID 41848420›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2026

Inhibition of prolyl-tRNA synthetase and efflux pumps as a dual-targeting strategy against multidrug-resistant bacteria.

Cristiane Tambascia, Jaqueline Cristina Silva, Barbara Carvalho Dos Reis, Camila Fernanda Silva Camilo, Carlos Abrunhosa Tairum Junior, Thais Hancio, Valquiria Graia Correia, Ronaldo Aloise Pilli, Andre Schützer de Godoy, Benoît Laleu and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

14 authors.

Cristiane TambasciaBrazilian Biosciences National Laboratory (LNBio), Brazilian Centre for Research in Energy and Materials (CNPEM), Campinas, SP, Brazil.
Jaqueline Cristina SilvaBrazilian Biosciences National Laboratory (LNBio), Brazilian Centre for Research in Energy and Materials (CNPEM), Campinas, SP, Brazil.
Barbara Carvalho Dos ReisBrazilian Biosciences National Laboratory (LNBio), Brazilian Centre for Research in Energy and Materials (CNPEM), Campinas, SP, Brazil.
Camila Fernanda Silva CamiloBrazilian Biosciences National Laboratory (LNBio), Brazilian Centre for Research in Energy and Materials (CNPEM), Campinas, SP, Brazil.
Carlos Abrunhosa Tairum JuniorBrazilian Biosciences National Laboratory (LNBio), Brazilian Centre for Research in Energy and Materials (CNPEM), Campinas, SP, Brazil.
Thais HancioBrazilian Biosciences National Laboratory (LNBio), Brazilian Centre for Research in Energy and Materials (CNPEM), Campinas, SP, Brazil.
Valquiria Graia CorreiaInstituto de Química, Universidade Estadual de Campinas (UNICAMP), Campinas, SP, Brazil.
Ronaldo Aloise PilliInstituto de Química, Universidade Estadual de Campinas (UNICAMP), Campinas, SP, Brazil.
Andre Schützer de GodoyMMV Medicines for Malaria Venture, ICC, Geneva, Switzerland.
Benoît LaleuMMV Medicines for Malaria Venture, ICC, Geneva, Switzerland.
Maurício Luís SforçaBrazilian Biosciences National Laboratory (LNBio), Brazilian Centre for Research in Energy and Materials (CNPEM), Campinas, SP, Brazil.
Silvana Aparecida RoccoBrazilian Biosciences National Laboratory (LNBio), Brazilian Centre for Research in Energy and Materials (CNPEM), Campinas, SP, Brazil.
Celso Eduardo BenedettiBrazilian Biosciences National Laboratory (LNBio), Brazilian Centre for Research in Energy and Materials (CNPEM), Campinas, SP, Brazil.
Gustavo Fernando MercaldiBrazilian Biosciences National Laboratory (LNBio), Brazilian Centre for Research in Energy and Materials (CNPEM), Campinas, SP, Brazil.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aminoacyl-tRNA synthetases have been widely exploited as targets for antiparasitic and antifungal inhibitors; however, they have received little attention as targets in multidrug-resistant (MDR) bacteria. Here we describe the biochemical characterisation of Prolyl-tRNA synthetase from

Indexed as

Amino Acyl-tRNA SynthetasesAnti-Bacterial AgentsDrug Resistance, Multiple, BacterialEnzyme InhibitorsEscherichia coliKlebsiella pneumoniaeStaphylococcus aureusDose-Response Relationship, DrugMicrobial Sensitivity TestsMolecular StructureStructure-Activity RelationshipAmino Acyl-tRNA SynthetasesAnti-Bacterial AgentsEnzyme Inhibitorsprolyl T RNA synthetaseaminoacyl-tRNA synthetase inhibitorsantimicrobial resistanceefflux pump inhibitorsgram-negative bacteriaKlebsiella pneumoniae

Identifiers

PMID41848420
PMCPMC13003883

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.