Evidence map›Paper›PMID 40407370›Full record

ArticleMicrobiology spectrum2025

The ClpXP protease and the ClpX unfoldase control virulence, cell division, and autolysis in

Viktor H Mebus, Supradipta De, Larissa M Busch, Manuela Gesell Salazar, Rabea Schlüter, Uwe Völker, Sven Hammerschmidt, Dorte Frees

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Microbiology spectrum, 2025. 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. Article
  3. 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

8 authors.

Viktor H MebusDepartment of Veterinary and Animal Sciences, University of Copenhagen, Copenhagen, Capital Region of Denmark, Denmark.ORCID 0009-0009-2332-2866
Supradipta DeDepartment of Molecular Genetics and Infection Biology, Interfaculty Institute for Genetics and Functional Genomics, Center for Functional Genomics of Microbes, University of Greifswald, Greifswald, Mecklenburg-Vorpommern, Germany.
Larissa M BuschDepartment of Functional Genomics, Interfaculty Institute for Genetics and Functional Genomics, Center for Functional Genomics of Microbes, University Medicine Greifswald, Greifswald, Mecklenburg-Vorpommern, Germany.
Manuela Gesell SalazarDepartment of Functional Genomics, Interfaculty Institute for Genetics and Functional Genomics, Center for Functional Genomics of Microbes, University Medicine Greifswald, Greifswald, Mecklenburg-Vorpommern, Germany.
Rabea SchlüterImaging Center of the Department of Biology, University of Greifswald, Greifswald, Mecklenburg-Vorpommern, Germany.
Uwe VölkerDepartment of Functional Genomics, Interfaculty Institute for Genetics and Functional Genomics, Center for Functional Genomics of Microbes, University Medicine Greifswald, Greifswald, Mecklenburg-Vorpommern, Germany.ORCID 0000-0002-5689-3448
Sven HammerschmidtDepartment of Molecular Genetics and Infection Biology, Interfaculty Institute for Genetics and Functional Genomics, Center for Functional Genomics of Microbes, University of Greifswald, Greifswald, Mecklenburg-Vorpommern, Germany.
Dorte FreesDepartment of Veterinary and Animal Sciences, University of Copenhagen, Copenhagen, Capital Region of Denmark, Denmark.ORCID 0000-0003-4946-2890

Funding

Deutsche Forschungsgemeinschaft DFG-GRK 2719/1Independent research fund Denmark, Technology and Production 0136-00200Independent Research Fund Denmark Tecknology and Production 4264-00028B
6 · The paper itself

Abstract

In all living cells, molecular chaperones and ATP-dependent proteases are essential for protein homeostasis. The ClpXP protease is a chaperone-protease complex conserved between bacteria and mitochondria. Proteolytic activity resides in the caseinolytic protease (ClpP) subunits that associate to form a tetradecameric serine protease that degrades substrates recognized and unfolded by the ClpX ATPase. In the important human pathogen

Indexed as

Bacterial ProteinsCell DivisionEndopeptidase ClpStreptococcus pneumoniaeAnimalsAutolysisHumansMolecular ChaperonesPneumococcal InfectionsVirulenceBacterial ProteinsClpP protein, Streptococcus pneumoniaeEndopeptidase ClpMolecular Chaperonescell divisioncell wallchaperonesClpXPGalleria melonellalipoteichoic acidLytAStreptococcus pneumoniae

Identifiers

PMID40407370
PMCPMC12211083

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.