ReviewThe Journal of antibiotics2017
Bacterial proteases, untapped antimicrobial drug targets.
Review in The Journal of antibiotics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 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.
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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
106 citing papers in PubMed, 244 citations in OpenAlex.
- Tail-specific protease (Tsp)-mediated envelope remodeling and beta-lactam tolerance inMicrobiology spectrum · 2026Article
- N-terminal processing unlocks global dynamics for substrate engagement in Spl proteases.Science advances · 2026Article
- Covalent Inhibitors in Antimicrobial Drug Development-Beyond β-Lactams.Molecules (Basel, Switzerland) · 2026Review
- Minute-scale control of ubiquitin-mediated degradation reveals dynamics of bacterial secreted effector-functions.Nature communications · 2026Article
- Repurposing Birabresib to target Gram‑positive bacteria.npj antimicrobials and resistance · 2026Article
- Ligand-based discovery of novel N-arylpyrrole derivatives as broad-spectrum antimicrobial agents with antibiofilm and anti-virulence activity.Journal of enzyme inhibition and medicinal chemistry · 2025Article
- Revealing the Bacterial HslV Protease Activation Potential with Triazine Derivatives via Experimental and Computational Approaches.The protein journal · 2025Article
- Allosteric regulation of proteolytic machines unveiled by the synergy between cryo-EM and solution NMR spectroscopy.The Biochemical journal · 2025Review
- Inhibitors of Proteases: A Well-Grounded Strategy in Drug Development.Molecules (Basel, Switzerland) · 2025Article
- Antechodynamics and Antechokinetics: Dynamics and Kinetics of Antibiotic Resistance Biomolecules.Biomolecules · 2025Review
- Antimicrobial Activity of a Synthetic Brevibacillin Analog Against Multidrug-ResistantInternational journal of molecular sciences · 2025Article
- MdfA is a novel ClpC adaptor protein that functions in the developingGenes & development · 2025Article
- Fighting Antimicrobial Resistance: Innovative Drugs in Antibacterial Research.Angewandte Chemie (International ed. in English) · 2025Review
- Borrelia burgdorferi serine protease HtrA is a pleiotropic regulator of stress response, motility, flagellar hemostasis, and infectivity.Communications biology · 2025Article
- Molecular dynamic simulations to assess the structural variability of ClpV fromFrontiers in bioinformatics · 2025Article
- TargetingFrontiers in cellular and infection microbiology · 2025Article
- TamGen: drug design with target-aware molecule generation through a chemical language model.Nature communications · 2024Article
- Advanced Imaging Methodology in Bacterial Biofilms with a Fluorescent Enzymatic Sensor for pepN Activity.Biosensors · 2024Article
- Support Enzyme Loading Influences the Effect of Aldehyde Dextran Modification on the Specificity of Immobilized Ficin for Large Proteins.Molecules (Basel, Switzerland) · 2024Article
- Toxin-based screening of C-terminal tags inbioRxiv : the preprint server for biology · 2024Article
46 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial proteases are an extensive collection of enzymes that have vital roles in cell viability, stress response and pathogenicity. Although their perturbation clearly offers the potential for antimicrobial drug development, both as traditional antibiotics and anti-virulence drugs, they are not yet the target of any clinically used therapeutics. Here we describe the potential for and recent progress in the development of compounds targeting bacterial proteases with a focus on AAA+ family proteolytic complexes and signal peptidases (SPs). Caseinolytic protease (ClpP) belongs to the AAA+ family of proteases, a group of multimeric barrel-shaped complexes whose activity is tightly regulated by associated AAA+ ATPases. The opportunity for chemical perturbation of these complexes is demonstrated by compounds targeting ClpP for inhibition, activation or perturbation of its associated ATPase. Meanwhile, SPs are also a proven antibiotic target. Responsible for the cleavage of targeting peptides during protein secretion, both type I and type II SPs have been successfully targeted by chemical inhibitors. As the threat of pan-antibiotic resistance continues to grow, these and other bacterial proteases offer an arsenal of novel antibiotic targets ripe for development.
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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.