ReviewJournal of medicinal chemistry2025
Harder than Metal: Challenging Antimicrobial Resistance with Metallo-β-lactamase Inhibitors.
Review in Journal of medicinal chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
5 citing papers in PubMed.
- Metallo-beta-lactamase α-helix fragment modified peptide N10 is a multifunctional antimicrobial peptide.Microbiology spectrum · 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
- Structure-Based Ligandability Exploration of a G‑Quadruplex-Forming Sequence from theACS medicinal chemistry letters · 2025Article
- Antimicrobial Resistance Profiles of Clinically Relevant Enterobacteriaceae Isolates: A Retrospective Study at a Southern Italian Hospital.Antibiotics (Basel, Switzerland) · 2025Article
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The spread of antimicrobial resistance (AMR) represents a major global health challenge, weakening the efficacy of antibiotics such as β-lactams, which are, nowadays, the most widely used drugs for treating bacterial infections. Among the different resistance mechanisms, the production of β-lactamases, particularly metallo-β-lactamases (MBLs), significantly compromises the activity of these antibiotics. Despite progress in developing serine-β-lactamase inhibitors (SBLi), no MBL inhibitors (MBLi) are currently available in clinical practice. This Perspective provides an outlook on AMR mechanisms, with a focus on the expression of MBL enzymes, and showcases the main classes of MBLi proposed to date, which mainly act through coordination of the zinc ion(s) populating the active site of the MBL class of enzymes. Furthermore, the Perspective describes current strategies aimed at overcoming the limited cellular permeability of MBLi, one of the major hurdles preventing their translation into clinical studies.
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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.