ArticleChemistry (Weinheim an der Bergstrasse, Germany)2018
Cyclobutanone Mimics of Intermediates in Metallo-β-Lactamase Catalysis.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- Ring Strain Energies in Four-Membered Heterocycles Containing an Element of Groups 13-16.Inorganic chemistry · 2025Article
- Cyclobutanone Inhibitors of Diaminopimelate Desuccinylase (DapE) as Potential New Antibiotics.International journal of molecular sciences · 2024Article
- Small-molecule inhibitors of bacterial-producing metallo-β-lactamases: insights into their resistance mechanisms and biochemical analyses of their activities.RSC medicinal chemistry · 2023Review
- In Silico Binding of 2-Aminocyclobutanones to SARS-CoV-2 Nsp13 Helicase and Demonstration of Antiviral Activity.International journal of molecular sciences · 2023Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Cyclobutanone Inhibitor of Cobalt-Functionalized Metallo-γ-Lactonase AiiA with Cyclobutanone Ring Opening in the Active Site.ACS omega · 2021Article
- Metallo-β-Lactamase Inhibitors Inspired on Snapshots from the Catalytic Mechanism.Biomolecules · 2020Review
- Both the mono- and di-anions of ellagic acid are effective inhibitors of the serine β-lactamase CTX-M-15.RSC advances · 2019Article
- β-Lactamases and β-Lactamase Inhibitors in the 21st Century.Journal of molecular biology · 2019Review
- Will morphing boron-based inhibitors beat the β-lactamases?Current opinion in chemical biology · 2019Review
- Targeting Metalloenzymes for Therapeutic Intervention.Chemical reviews · 2019Review
- The Continuing Challenge of Metallo-β-Lactamase Inhibition: Mechanism Matters.Trends in pharmacological sciences · 2018Review
- Cyclobutanone Mimics of Intermediates in Metallo-β-Lactamase Catalysis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2018Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
The most important resistance mechanism to β-lactam antibiotics involves hydrolysis by two β-lactamase categories: the nucleophilic serine and the metallo-β-lactamases (SBLs and MBLs, respectively). Cyclobutanones are hydrolytically stable β-lactam analogues with potential to inhibit both SBLs and MBLs. We describe solution and crystallographic studies on the interaction of a cyclobutanone penem analogue with the clinically important MBL SPM-1. NMR experiments using
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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.