ReviewFrontiers in genetics2022
Biochemical exploration of β-lactamase inhibitors.
Review in Frontiers in genetics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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.
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.
Who cites it
23 citing papers in PubMed.
- Partial purification and environmental application of CTX-type ESBL beta-lactamases from wastewater-derived E. coli isolates.BMC microbiology · 2026Article
- Alternative enzymatic pathways to penicillin antibiotics.Nature communications · 2026Article
- Comparative analysis of treatment outcomes and risk factors associated with different combination antimicrobial regimens in patients with multidrug-resistant Acinetobacter baumannii pneumonia.Frontiers in cellular and infection microbiology · 2026Article
- A Review ofInternational journal of microbiology · 2026Review
- Old drugs, new weapons: current trends in repurposing therapies against antimicrobial resistance.Journal of pharmacy & pharmaceutical sciences : a publication of the Canadian Society for Pharmaceutical Sciences, Societe canadienne des sciences pharmaceutiques · 2026Review
- Targeted Drug Delivery Strategies in Overcoming Antimicrobial Resistance: Advances and Future Directions.Pharmaceutics · 2025Review
- Mechanistic basis for inhibition of the extended-spectrum β-lactamase GES-1 by enmetazobactam and tazobactam.FEBS letters · 2025Article
- Efficacy of imipenem combined with dimercaptosuccinic acid in a murine sepsis model using Pseudomonas aeruginosa.Scientific reports · 2025Article
- Harder than Metal: Challenging Antimicrobial Resistance with Metallo-β-lactamase Inhibitors.Journal of medicinal chemistry · 2025Review
- Strategic re-engineering of antibiotics.Nature reviews bioengineering · 2025Article
- Inhibitory activity of meso-dimercaptosuccinic acid against IMP metallo-β-lactamase variants in Pseudomonas aeruginosa.FEMS microbiology letters · 2025Article
- Beyond antibiotics: exploring multifaceted approaches to combat bacterial resistance in the modern era: a comprehensive review.Frontiers in cellular and infection microbiology · 2025Review
- Failure or future? Exploring alternative antibacterials: a comparative analysis of antibiotics and naturally derived biopolymers.Frontiers in microbiology · 2025Review
- Mechanisms of antimicrobial resistance: From genetic evolution to clinical manifestations.AIMS microbiology · 2025Review
- Current Strategy for Targeting Metallo-β-Lactamase with Metal-Ion-Binding Inhibitors.Molecules (Basel, Switzerland) · 2024Review
- Unveiling the Secrets ofInternational journal of molecular sciences · 2024Review
- Restricted Rotational Flexibility of the C5α-Methyl-Substituted Carbapenem NA-1-157 Leads to Potent Inhibition of the GES-5 Carbapenemase.ACS infectious diseases · 2024Article
- Revisiting the Checkerboard to Inform Development of β-Lactam/β-Lactamase Inhibitor Combinations.Antibiotics (Basel, Switzerland) · 2024Article
- Role of β-Lactamase Inhibitors as Potentiators in Antimicrobial Chemotherapy Targeting Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2024Review
- Potentiation of Antibiotic Activity of Aztreonam against Metallo-β-Lactamase-Producing Multidrug-ResistantPharmaceutics · 2024Article
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The alarming rise of microbial resistance to antibiotics has severely limited the efficacy of current treatment options. The prevalence of β-lactamase enzymes is a significant contributor to the emergence of antibiotic resistance. There are four classes of β-lactamases: A, B, C, and D. Class B is the metallo-β-lactamase, while the rest are serine β-lactamases. The clinical use of β-lactamase inhibitors began as an attempt to combat β-lactamase-mediated resistance. Although β-lactamase inhibitors alone are ineffective against bacteria, research has shown that combining inhibitors with antibiotics is a safe and effective treatment that not only prevents β-lactamase formation but also broadens the range of activity. These inhibitors may cause either temporary or permanent inhibition. The development of new β-lactamase inhibitors will be a primary focus of future research. This study discusses recent advances in our knowledge of the biochemistry behind β-lactam breakdown, with special emphasis on the mechanism of inhibitors for β-lactam complexes with β-lactamase. The study also focuses on the pharmacokinetic and pharmacodynamic properties of all inhibitors and then applies them in clinical settings. Our analysis and discussion of the challenges that exist in designing inhibitors might help pharmaceutical researchers address root issues and develop more effective inhibitors.
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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.