ArticleMolecular microbiology2021
ClpP1P2 peptidase activity promotes biofilm formation in Pseudomonas aeruginosa.
Article in Molecular microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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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.
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.
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Who cites it
20 citing papers in PubMed, 30 citations in OpenAlex.
- Mode of action guided metagenomic natural product discovery reveals convergent evolution of a ClpP-targeting motif.Nature communications · 2026Article
- ClpP2 modulates ClpXP assembly to promote multiple pathogenic phenotypes inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structural and mechanistic insights into caseinolytic protease inhibition for antimicrobial development against Pseudomonas plecoglossicida.PLoS pathogens · 2026Article
- Translation quality control in Pseudomonas aeruginosa: current knowledge and perspectives.FEMS microbiology reviews · 2026Review
- Structural insights into the Pseudomonas aeruginosa ClpP1•ClpP2 heterocomplex and its interactions with the AAA+ ClpX unfoldase.Protein science : a publication of the Protein Society · 2025Article
- Structural Insights into Bortezomib-Induced Activation of the Caseinolytic Chaperone-Protease System in Mycobacterium tuberculosis.Nature communications · 2025Article
- Genetic and virulence factors behind the success of high-riskFrontiers in microbiology · 2025Article
- Article
- Carbon Source and Substrate Surface Affect Biofilm Formation by the Plant-Associated BacteriumInternational journal of molecular sciences · 2024Article
- Genetics of conditional extended mycelial cell viability ofFrontiers in microbiology · 2024Article
- Article
- A closed translocation channel in the substrate-free AAA+ ClpXP protease diminishes rogue degradation.Nature communications · 2023Article
- Cell-Free Supernatants (CFSs) from the Culture ofMicroorganisms · 2022Article
- ESKAPE Pathogens: Looking at Clp ATPases as Potential Drug Targets.Antibiotics (Basel, Switzerland) · 2022Review
- Article
- The essentialScience advances · 2022Article
- Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis.Critical reviews in biochemistry and molecular biology · 2022Review
- Cellular functions of the ClpP protease impacting bacterial virulence.Frontiers in molecular biosciences · 2022Review
- Proteomic profiling spotlights the molecular targets and the impact of the natural antivirulent umbelliferone on stress response, virulence factors, and the quorum sensing network ofFrontiers in cellular and infection microbiology · 2022Article
- Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Caseinolytic proteases (Clp) are central to bacterial proteolysis and control cellular physiology and stress responses. They are composed of a double-ring compartmentalized peptidase (ClpP) and a AAA+ unfoldase (ClpX or ClpA/ClpC). Unlike many bacteria, the opportunistic pathogen Pseudomonas aeruginosa contains two ClpP homologs: ClpP1 and ClpP2. The specific functions of these homologs, however, are largely elusive. Here, we report that the active form of PaClpP2 is a part of a heteromeric PaClpP1
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Registered trials
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.