ArticleRSC medicinal chemistry2023
α-Aminophosphonate inhibitors of metallo-β-lactamases NDM-1 and VIM-2.
Article in RSC medicinal chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 5 citations in OpenAlex.
- Dual-Mechanism Antimicrobial Peptides from a Nature-Inspired Scaffold.Journal of medicinal chemistry · 2026Article
- From Microbes to Medicine: Targeting Metalloprotein Pathways for Innovative Antibacterial Strategies.International journal of molecular sciences · 2026Review
- Recent advances in natural and synthetic phosphonate therapeutics.Current opinion in microbiology · 2025Review
- Dynamically chiral phosphonic acid-type metallo-β-lactamase inhibitors.Communications chemistry · 2025Article
- Approachable Synthetic Methodologies for Second-GenerationPharmaceuticals (Basel, Switzerland) · 2024Review
- The key phosphorus moieties in drug design: antimicrobials and beyond.Future medicinal chemistry · 2024Article
- Carbapenem-ResistantInfection and drug resistance · 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
11 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The upswing of antibiotic resistance is an escalating threat to human health. Resistance mediated by bacterial metallo-β-lactamases is of particular concern as these enzymes degrade β-lactams, our most frequently prescribed class of antibiotics. Inhibition of metallo-β-lactamases could allow the continued use of existing β-lactam antibiotics, such as penicillins, cephalosporins and carbapenems, whose applicability is becoming ever more limited. The design, synthesis, and NDM-1, VIM-2, and GIM-1 inhibitory activities (IC
Identifiers
What OpenQuestion holds
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.