Evidence map›Paper›PMID 39919438›Full record

ArticleEuropean journal of medicinal chemistry2025

Different chemical scaffolds bind to L-phe site in Mycobacterium tuberculosis Phe-tRNA synthetase.

Priyanka Gade, Changsoo Chang, Denise S Pryde, Daniel Fletcher, Sarah Niven, Luma Godoy Magalhaes, David Robinson, Jagmohan Saini, Peter E G F Ibrahim, Barbara Forte and 6 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in European journal of medicinal chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

16 authors.

Priyanka GadeCenter for Structural Biology of Infectious Diseases, Consortium for Advanced Science and Engineering, University of Chicago, Chicago, IL, 60667, USA; Structural Biology Center, X-ray Science Division, Argonne National Laboratory, Lemont, IL, 60439, USA.
Changsoo ChangCenter for Structural Biology of Infectious Diseases, Consortium for Advanced Science and Engineering, University of Chicago, Chicago, IL, 60667, USA; Structural Biology Center, X-ray Science Division, Argonne National Laboratory, Lemont, IL, 60439, USA.
Denise S PrydeDrug Discovery Unit, Wellcome Centre for Anti-Infectives Research, Division of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, DD1 5EH, UK.
Daniel FletcherDrug Discovery Unit, Wellcome Centre for Anti-Infectives Research, Division of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, DD1 5EH, UK.
Sarah NivenDrug Discovery Unit, Wellcome Centre for Anti-Infectives Research, Division of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, DD1 5EH, UK.
Luma Godoy MagalhaesDrug Discovery Unit, Wellcome Centre for Anti-Infectives Research, Division of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, DD1 5EH, UK.
David RobinsonDrug Discovery Unit, Wellcome Centre for Anti-Infectives Research, Division of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, DD1 5EH, UK.
Jagmohan SainiDrug Discovery Unit, Wellcome Centre for Anti-Infectives Research, Division of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, DD1 5EH, UK.
Peter E G F IbrahimDrug Discovery Unit, Wellcome Centre for Anti-Infectives Research, Division of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, DD1 5EH, UK.
Barbara ForteDrug Discovery Unit, Wellcome Centre for Anti-Infectives Research, Division of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, DD1 5EH, UK.
Jacek WowerDepartment of Animal Sciences, Auburn University, Auburn, AL, 36849, USA.
Michael J BodkinDrug Discovery Unit, Wellcome Centre for Anti-Infectives Research, Division of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, DD1 5EH, UK.
Beatriz BaragañaDrug Discovery Unit, Wellcome Centre for Anti-Infectives Research, Division of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, DD1 5EH, UK. Electronic address: B.Baragana@dundee.ac.uk.
Ian H GilbertDrug Discovery Unit, Wellcome Centre for Anti-Infectives Research, Division of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, DD1 5EH, UK.
Karolina MichalskaCenter for Structural Biology of Infectious Diseases, Consortium for Advanced Science and Engineering, University of Chicago, Chicago, IL, 60667, USA; Structural Biology Center, X-ray Science Division, Argonne National Laboratory, Lemont, IL, 60439, USA.
Andrzej JoachimiakCenter for Structural Biology of Infectious Diseases, Consortium for Advanced Science and Engineering, University of Chicago, Chicago, IL, 60667, USA; Structural Biology Center, X-ray Science Division, Argonne National Laboratory, Lemont, IL, 60439, USA; Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL, 60367, USA. Electronic address: andrzejj@anl.gov.

Funding

THE MIDWEST CENTER FOR STRUCTURAL GENOMICSP50GM062414 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ JOACHIMIAK · 2000 to 2004
$33.2M
TO PROVIDE SCIENTIFIC SUPPORT TO THE CENTERS FOR RESEARCH ON STRUCTURAL BIOLOGY OF INFECTIOUS DISEASES.75N93022C00035 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SATCHELL, KARLA · 2022 to 2025
$20.7M
The Midwest Center for Structural Genomics - Community ResourceR24GM115586 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ · 2015 to 2017
$2.8M
Gates Foundation INV-026519NIAID NIH HHS 75N93022C00035NIGMS NIH HHS P50 GM062414NIGMS NIH HHS R24 GM115586Wellcome Trust
6 · The paper itself

Abstract

Tuberculosis (TB), caused by Mycobacterium tuberculosis (Mt), is one of the deadliest infectious diseases. The rise of multidrug-resistant strains represents a major public health threat, requiring new therapeutic options. Bacterial aminoacyl-tRNA synthetases (aaRS) have been shown to be highly promising drug targets, including for TB treatment. These enzymes play an essential role in translating the DNA gene code into protein sequence by attaching specific amino acid to their cognate tRNAs. They have multiple binding sites that can be targeted for inhibitor discovery: amino acid binding pocket, ATP binding pocket, tRNA binding site and an editing domain. Recently we reported several high-resolution structures of M. tuberculosis phenylalanyl-tRNA synthetase (MtPheRS) complexed with tRNA

Indexed as

Mycobacterium tuberculosisPhenylalanine-tRNA LigaseAntitubercular AgentsBinding SitesCarboxinDose-Response Relationship, DrugEnzyme InhibitorsModels, MolecularMolecular StructurePhenylalanineStructure-Activity RelationshipAntitubercular AgentsCarboxinEnzyme InhibitorsPhenylalaninePhenylalanine-tRNA Ligase

Identifiers

PMID39919438
PMCPMC12447630

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.