ArticleACS infectious diseases2025
Standardized Residue Numbering and Secondary Structure Nomenclature in the Class D β-Lactamases.
Article in ACS infectious diseases, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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.
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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
7 citing papers in PubMed.
- β-lactamase genes in clinical isolates of Capnocytophaga canimorsus and description of a novel class D β-lactamase, OXA-1422.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026Article
- The Novel Carbapenem, JDB/PQ-1-219, Has Potent Broad Spectrum Activity against Multi-Drug ResistantACS infectious diseases · 2026Article
- CAGE-TRX expands the scope of time-resolved crystallography through genetically encoded active-site photocaging.bioRxiv : the preprint server for biology · 2026Article
- Diversity and function of OXA-48-like β-lactamase variants in environmentalApplied and environmental microbiology · 2026Article
- Are Putative Beta-Lactamases Posing a Potential Future Threat?Antibiotics (Basel, Switzerland) · 2025Article
- Dual mechanism of the OXA-23 carbapenemase inhibition by the carbapenem NA-1-157.Antimicrobial agents and chemotherapy · 2025Article
- Diversity in the Common Fold: Structural Insights into Class D β-Lactamases from Gram-Negative Pathogens.Pathogens (Basel, Switzerland) · 2025Article
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2 authors.
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Abstract
Over 1370 class D β-lactamases are currently known, and they pose a serious threat to the effective treatment of many infectious diseases, particularly in some pathogenic bacteria where evolving carbapenemase activity has been reported. Detailed understanding of their molecular biology, enzymology, and structural biology are critically important, but the lack of a standardized residue numbering scheme and inconsistent secondary structure annotation has made comparative analyses sometimes difficult and cumbersome. Compounding this, in the post-AlphaFold world where we currently find ourselves, an extraordinary wealth of detailed structural information on these enzymes is literally at our fingertips; therefore it is vitally important that a standard numbering system is in place to facilitate the accurate and straightforward analysis of their structures. Here we present a residue numbering and secondary structure scheme for the class D enzymes based on the sequence and structure of OXA-48 and apply it to test targets to demonstrate the ease with which it can be used.
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