ReviewCurrent opinion in chemical biology2019
Will morphing boron-based inhibitors beat the β-lactamases?
Review in Current opinion in chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed, 85 citations in OpenAlex.
- Development of Water-Trapping Pyrrole-2-carboxylic Acids as Broad-Spectrum Metallo-β-lactamase Inhibitors.Journal of medicinal chemistry · 2026Article
- Structural perspectives on clinical β-lactamase inhibitors: From mechanism to resistance.Journal of microbiology (Seoul, Korea) · 2026Review
- Luminescent Electro-Spun Nanofibers Crosslinked with Boronic Esters Exhibiting Controlled Release of Carbon Dots for Detection of Wound pHs and Enhanced Antimicrobial.Macromolecular bioscience · 2025Article
- Boronate-Based Inhibitors of Penicillin-Binding Proteins: An Underestimated Avenue for Antibiotic Discovery?Pharmaceuticals (Basel, Switzerland) · 2025Article
- Small-molecule strategies to combat antibiotic resistance: mechanisms, modifications, and contemporary approaches.RSC advances · 2025Review
- Discovery of Boronic Acids-Based β-Lactamase Inhibitors Through In Situ Click Chemistry.International journal of molecular sciences · 2025Article
- Decarboxylation of the Catalytic Lysine Residue by the C5α-Methyl-Substituted Carbapenem NA-1-157 Leads to Potent Inhibition of the OXA-58 Carbapenemase.ACS infectious diseases · 2024Article
- Approachable Synthetic Methodologies for Second-GenerationPharmaceuticals (Basel, Switzerland) · 2024Review
- Structural basis of metallo-β-lactamase resistance to taniborbactam.Antimicrobial agents and chemotherapy · 2024Article
- Aromatic Diboronic Acids as Effective KPC/AmpC Inhibitors.Molecules (Basel, Switzerland) · 2023Article
- Strategies to combat Gram-negative bacterial resistance to conventional antibacterial drugs: a review.Osong public health and research perspectives · 2023Article
- Integrating Siderophore Substructures in Thiol-Based Metallo-β-Lactamase Inhibitors.Molecules (Basel, Switzerland) · 2023Article
- β-Lactam Antibiotics and β-Lactamase Enzymes Inhibitors, Part 2: Our Limited Resources.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Assessment of Activity and Resistance Mechanisms to Cefepime in Combination with the Novel β-Lactamase Inhibitors Zidebactam, Taniborbactam, and Enmetazobactam against a Multicenter Collection of Carbapenemase-ProducingAntimicrobial agents and chemotherapy · 2022Article
- β-Lactam antibiotic targets and resistance mechanisms: from covalent inhibitors to substrates.RSC medicinal chemistry · 2021Review
- Recent developments in the medicinal chemistry of single boron atom-containing compounds.Acta pharmaceutica Sinica. B · 2021Review
- High-Throughput Crystallography Reveals Boron-Containing Inhibitors of a Penicillin-Binding Protein with Di- and Tricovalent Binding Modes.Journal of medicinal chemistry · 2021Article
- Design and enantioselective synthesis of 3-(α-acrylic acid) benzoxaboroles to combat carbapenemase resistance.Chemical communications (Cambridge, England) · 2021Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Structural Basis of Metallo-β-lactamase Inhibition byACS infectious diseases · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The β-lactams remain the most important antibacterials, but their use is increasingly compromised by resistance, importantly by β-lactamases. Although β-lactam and non-β-lactam inhibitors forming stable acyl-enzyme complexes with nucleophilic serine β-lactamases (SBLs) are widely used, these are increasingly susceptible to evolved SBLs and do not inhibit metallo-β-lactamases (MBLs). Boronic acids and boronate esters, especially cyclic ones, can potently inhibit both SBLs and MBLs. Vaborbactam, a monocyclic boronate, is approved for clinical use, but its β-lactamase coverage is limited. Bicyclic boronates rapidly react with SBLs and MBLs forming stable enzyme-inhibitor complexes that mimic the common anionic high-energy tetrahedral intermediates in SBL/MBL catalysis, as revealed by crystallography. The ability of boronic acids to 'morph' between sp
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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.