Evidence map›Paper›PMID 31067645›Full record

ReviewInternational journal of molecular sciences2019

ClpP Protease, a Promising Antimicrobial Target.

Carlos Moreno-Cinos, Kenneth Goossens, Irene G Salado, Pieter Van Der Veken, Hans De Winter, Koen Augustyns

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
7.1field-weighted citation impact, top 2% of its field
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

59 citing papers in PubMed, 129 citations in OpenAlex.

  1. Review
  2. Article
  3. Repurposing Birabresib to target Gram‑positive bacteria.npj antimicrobials and resistance · 2026
    Article
  4. Bacterial warfare at the molecular level:Current research in microbial sciences · 2026
    Article
  5. The Effect ofInternational journal of molecular sciences · 2025
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Fighting Antimicrobial Resistance: Innovative Drugs in Antibacterial Research.Angewandte Chemie (International ed. in English) · 2025
    Review
  11. Article
  12. Linalool exhibit antimicrobial ability againstCurrent research in microbial sciences · 2025
    Article
  13. Article
  14. Article
  15. Protein degradation by a component of the chaperonin-linked protease ClpP.Genes to cells : devoted to molecular & cellular mechanisms · 2024
    Review
  16. Article
  17. Bacterial persisters: molecular mechanisms and therapeutic development.Signal transduction and targeted therapy · 2024
    Review
  18. Review
  19. Article
  20. 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

6 authors at 1 institution in 1 country.

Carlos Moreno-CinosLaboratory of Medicinal Chemistry, University of Antwerp, Universiteitsplein 1, B-2610 Antwerp, Belgium. carlos.morenocinos@uantwerpen.be.ORCID 0000-0003-2176-2883
Kenneth GoossensLaboratory of Medicinal Chemistry, University of Antwerp, Universiteitsplein 1, B-2610 Antwerp, Belgium. kenneth.goossens@uantwerpen.be.
Irene G SaladoLaboratory of Medicinal Chemistry, University of Antwerp, Universiteitsplein 1, B-2610 Antwerp, Belgium. irenegarciasalado@gmail.com.
Pieter Van Der VekenLaboratory of Medicinal Chemistry, University of Antwerp, Universiteitsplein 1, B-2610 Antwerp, Belgium. pieter.vanderveken@uantwerpen.be.
Hans De WinterLaboratory of Medicinal Chemistry, University of Antwerp, Universiteitsplein 1, B-2610 Antwerp, Belgium. hans.dewinter@uantwerpen.be.ORCID 0000-0002-4450-7677
Koen AugustynsLaboratory of Medicinal Chemistry, University of Antwerp, Universiteitsplein 1, B-2610 Antwerp, Belgium. koen.augustyns@uantwerpen.be.
University of Antwerp · BE

Funding

H2020 Marie Skłodowska-Curie Actions 642620
6 · The paper itself

Abstract

The caseinolytic protease proteolytic subunit (ClpP) is a serine protease playing an important role in proteostasis of eukaryotic organelles and prokaryotic cells. Alteration of ClpP function has been proved to affect the virulence and infectivity of a number of pathogens. Increased bacterial resistance to antibiotics has become a global problem and new classes of antibiotics with novel mechanisms of action are needed. In this regard, ClpP has emerged as an attractive and potentially viable option to tackle pathogen fitness without suffering cross-resistance to established antibiotic classes and, when not an essential target, without causing an evolutionary selection pressure. This opens a greater window of opportunity for the host immune system to clear the infection by itself or by co-administration with commonly prescribed antibiotics. A comprehensive overview of the function, regulation and structure of ClpP across the different organisms is given. Discussion about mechanism of action of this protease in bacterial pathogenesis and human diseases are outlined, focusing on the compounds developed in order to target the activation or inhibition of ClpP.

Indexed as

Anti-Bacterial AgentsBacteriaBacterial ProteinsDepsipeptidesDrug DesignEndopeptidase ClpAnti-Bacterial AgentsBacterial ProteinsDepsipeptidesEndopeptidase ClpantibioticsantivirulenceClpP

Identifiers

PMID31067645
PMCPMC6540193
OpenAlexW2942675709

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.