Evidence map›Paper›PMID 39900984›Full record

ArticleScientific reports2025

Identification of new ClpC1-NTD binders for Mycobacterium tuberculosis drug development.

Katharina Weinhäupl, Louis Meuret, Sandy Desrat, Fanny Roussi, Nelly Morellet, Sandra Beaupierre, Catherine Guillou, Carine van Heijenoort, Olga Abian, Sonia Vega and 7 more

Erratum issuedAbstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. 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

5 · Who and what money

Authors and funding

17 authors.

Katharina WeinhäuplInstitute for Research and Innovation in HealthI3S, Porto, Portugal. kathi.weinhaeupl@gmail.com.
Louis MeuretInstitut de Chimie des Substances Naturelles (ICSN), Centre national de la recherche scientifique (CNRS) , Gif-Sur-Yvette, France.
Sandy DesratInstitut de Chimie des Substances Naturelles (ICSN), Centre national de la recherche scientifique (CNRS) , Gif-Sur-Yvette, France.
Fanny RoussiInstitut de Chimie des Substances Naturelles (ICSN), Centre national de la recherche scientifique (CNRS) , Gif-Sur-Yvette, France.
Nelly MorelletInstitut de Chimie des Substances Naturelles (ICSN), Centre national de la recherche scientifique (CNRS) , Gif-Sur-Yvette, France.
Sandra BeaupierreInstitut de Chimie des Substances Naturelles (ICSN), Centre national de la recherche scientifique (CNRS) , Gif-Sur-Yvette, France.
Catherine GuillouInstitut de Chimie des Substances Naturelles (ICSN), Centre national de la recherche scientifique (CNRS) , Gif-Sur-Yvette, France.
Carine van HeijenoortInstitut de Chimie des Substances Naturelles (ICSN), Centre national de la recherche scientifique (CNRS) , Gif-Sur-Yvette, France.
Olga AbianInstitute for Health Research Aragon (IIS Aragon), Zaragoza, Spain.
Sonia VegaInstitute of Biocomputation and Physics of Complex Systems (BIFI), University of Zaragoza, Zaragoza, Spain.
Ian WolfHarvard School of Public Health, Boston, USA.
Tatos AkopianHarvard School of Public Health, Boston, USA.
Olga KrandorHarvard School of Public Health, Boston, USA.
Eric RubinHarvard School of Public Health, Boston, USA.
Adrian Velazquez-CampoyInstitute for Health Research Aragon (IIS Aragon), Zaragoza, Spain.
Diego GautoInstitut de Chimie des Substances Naturelles (ICSN), Centre national de la recherche scientifique (CNRS) , Gif-Sur-Yvette, France. diego.gauto@cnrs.fr.
Hugo FragaInstitute for Research and Innovation in HealthI3S, Porto, Portugal. hugo.fraga@i3s.up.pt.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MtbClpC1 is a promising drug target against tuberculosis. Recent studies have shown that several natural product antibiotics targeting the unfoldase N-terminal domain can impair MtbClpC1 function resulting in cell death. While the pharmacological properties of these natural product antibiotics prevent their use in the clinic, similar molecules binding to the same binding pockets can result in new drugs against Mtb. Here we demonstrate that we successfully used in silico screening to identify new ClpC1 N-terminal domain binders with micromolar affinity from a small compound library. In addition, we experimentally demonstrate that the new compounds bind to the same pockets used by the natural product antibiotics and inhibit ClpC1 function.

Indexed as

Antitubercular AgentsBacterial ProteinsDrug DevelopmentMycobacterium tuberculosisBinding SitesHeat-Shock ProteinsHumansProtein BindingSmall Molecule LibrariesTuberculosisAntitubercular AgentsBacterial ProteinsClpC1 protein, Mycobacterium tuberculosisHeat-Shock ProteinsSmall Molecule LibrariesChaperoneClpC1In silicoProtagsTuberculosis

Identifiers

PMID39900984
PMCPMC11791199

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.