ArticleRSC advances2020
Revealing electronic features governing hydrolysis of cephalosporins in the active site of the L1 metallo-β-lactamase.
Article in RSC advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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
4 citing papers in PubMed.
- Quantum Chemical Insights into Antibiotic Structure-Activity Relationships and Mechanisms of Action: A Review.Molecules (Basel, Switzerland) · 2026Review
- Navigating the complexities of drug development for metallo-β-lactamase inhibitors.RSC medicinal chemistry · 2025Review
- Cefiderocol "under siege"? Understanding the rise of NDM-mediated resistance to novel agents.Chemical science · 2025Article
- Boronic Acids as Prospective Inhibitors of Metallo-β-Lactamases: Efficient Chemical Reaction in the Enzymatic Active Site Revealed by Molecular Modeling.Molecules (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The QM/MM simulations followed by electron density feature analysis are carried out to deepen the understanding of the reaction mechanism of cephalosporin hydrolysis in the active site of the L1 metallo-β-lactamase. The differences in reactivity of ten similar cephalosporin compounds are explained by using an extended set of bonding descriptors. The limiting step of the reaction is characterized by the proton transfer to the nitrogen atom of the cephalosporin thiazine ring accompanied with formation of the C
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Registered trials
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