ArticleAntimicrobial agents and chemotherapy2017
Cyclic Boronates Inhibit All Classes of β-Lactamases.
Article in Antimicrobial agents and chemotherapy, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers, 1 of them a synthesis that pooled it.
What it found
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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
64 citing papers in PubMed, 1 synthesis or guideline pooled it, 119 citations in OpenAlex.
- Tackling the Antibiotic Resistance Caused by Class AInternational journal of molecular sciences · 2018Pooled it
- Predatory myxobacteria lay at the cross-roads of metallo-β-lactamase evolution.Communications biology · 2026Article
- Development of Water-Trapping Pyrrole-2-carboxylic Acids as Broad-Spectrum Metallo-β-lactamase Inhibitors.Journal of medicinal chemistry · 2026Article
- Repurposing insights: experimental and pharmacological approach on L-captopril and dimercaprol as metallo-β-lactamase inhibitors.FEMS microbiology letters · 2026Article
- Structural comparison of substrate-binding pockets of serine β-lactamases in classes A, C, and D.Journal of enzyme inhibition and medicinal chemistry · 2025Review
- Navigating the complexities of drug development for metallo-β-lactamase inhibitors.RSC medicinal chemistry · 2025Review
- Recent Development of Boron-Containing Small-Molecule Anticancer Agents.ACS pharmacology & translational science · 2025Review
- Carbapenem Resistance inMicroorganisms · 2025Review
- Harder than Metal: Challenging Antimicrobial Resistance with Metallo-β-lactamase Inhibitors.Journal of medicinal chemistry · 2025Review
- Trends on Potential Boron-containing Drugs by Advancements in Ligand-protein Crystals Complexes.Current medicinal chemistry · 2025Review
- Identification of Potential Inhibitors of Three NDM Variants ofCurrent computer-aided drug design · 2025Article
- ESKAPE pathogens: antimicrobial resistance, epidemiology, clinical impact and therapeutics.Nature reviews. Microbiology · 2024Review
- Approachable Synthetic Methodologies for Second-GenerationPharmaceuticals (Basel, Switzerland) · 2024Review
- Drug Discovery in the Field of β-Lactams: An Academic Perspective.Antibiotics (Basel, Switzerland) · 2024Review
- Enhancing the activity of β-lactamase inhibitory protein-II with cell-penetrating peptide against KPC-2-carrying Klebsiella pneumoniae.PloS one · 2024Article
- Non-β Lactam Inhibitors of the Serine β-Lactamase blaCTX-M15 in Drug-ResistantJournal of chemical information and modeling · 2023Article
- Efflux Pump (QacA, QacB, and QacC) and β-Lactamase Inhibitors? An Evaluation of 1,8-Naphthyridines againstMolecules (Basel, Switzerland) · 2023Article
- Structure, function, and evolution of metallo-β-lactamases from the B3 subgroup-emerging targets to combat antibiotic resistance.Frontiers in chemistry · 2023Review
- Direct Colorimetry of Imipenem Decomposition as a Novel Cost-Effective Method for Detecting Carbapenemase-Producing Enterobacteria.Microbiology spectrum · 2022Article
- Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 1 country.
Funding
Abstract
β-Lactamase-mediated resistance is a growing threat to the continued use of β-lactam antibiotics. The use of the β-lactam-based serine-β-lactamase (SBL) inhibitors clavulanic acid, sulbactam, and tazobactam and, more recently, the non-β-lactam inhibitor avibactam has extended the utility of β-lactams against bacterial infections demonstrating resistance via these enzymes. These molecules are, however, ineffective against the metallo-β-lactamases (MBLs), which catalyze their hydrolysis. To date, there are no clinically available metallo-β-lactamase inhibitors. Coproduction of MBLs and SBLs in resistant infections is thus of major clinical concern. The development of "dual-action" inhibitors, targeting both SBLs and MBLs, is of interest, but this is considered difficult to achieve due to the structural and mechanistic differences between the two enzyme classes. We recently reported evidence that cyclic boronates can inhibit both serine- and metallo-β-lactamases. Here we report that cyclic boronates are able to inhibit all four classes of β-lactamase, including the class A extended spectrum β-lactamase CTX-M-15, the class C enzyme AmpC from
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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.