ArticleNature communications2021
Structural and functional insights into esterase-mediated macrolide resistance.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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.
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Who cites it
28 citing papers in PubMed, 58 citations in OpenAlex.
- Hydration and hydrolysis define antibiotic resistance conferred by macrolide esterases.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Article
- [Molecular mechanisms underlying the development and spread of antibiotic resistance].Bundesgesundheitsblatt, Gesundheitsforschung, Gesundheitsschutz · 2026Review
- Proteomic Insights into Antimicrobial Resistance Mechanisms in Human-Associated Bacterial Pathogens.Microbial ecology · 2026Review
- Klebsiella pneumoniae in the global AMR: resistance mechanisms and genomic adaptation.World journal of microbiology & biotechnology · 2026Review
- Functional characterization of macrolide esterase from cyanobacteria and their potential dissemination risk.npj antimicrobials and resistance · 2026Article
- Antimicrobial Resistance: Enzymes, Proteins, and Computational Resources.Current pharmaceutical design · 2026Review
- Antibiotic resistance inFrontiers in microbiology · 2026Review
- Establishing Selectivity Trends with Reactions of Thioesterases and Semi-Synthetic Polyketides.Journal of the American Chemical Society · 2025Article
- Review
- Enzyme-mediated aminoglycoside resistance without target mimicry.Communications chemistry · 2025Article
- Computational investigation of natural compounds as inhibitors against macrolide-resistant protein using virtual screening, molecular docking and MD simulations.Scientific reports · 2025Article
- Bacterial Extracellular Vesicles and Antimicrobial Peptides: A Synergistic Approach to Overcome Antimicrobial Resistance.Antibiotics (Basel, Switzerland) · 2025Review
- Effects of ciprofloxacin on bacterial abundance and enrichments in samples taken from the sea surface microlayer and underlying waters in the southern North Sea.Frontiers in microbiology · 2025Article
- Elucidating the biotechnological potential of the genera Parageobacillus and Saccharococcus through comparative genomic and pan-genome analysis.BMC genomics · 2024Article
- Pangenome comparison ofmSystems · 2024Article
- The global distribution of the macrolide esterase EstX from the alpha/beta hydrolase superfamily.Communications biology · 2024Article
- Developing a novel magnetic organic polymer for selective extraction and determination of 16 macrolides in water and honey samples.RSC advances · 2024Article
- Pangenome comparison ofbioRxiv : the preprint server for biology · 2023Article
- Antibiotic Potentiation as a Promising Strategy to Combat Macrolide Resistance in Bacterial Pathogens.Antibiotics (Basel, Switzerland) · 2023Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Macrolides are a class of antibiotics widely used in both medicine and agriculture. Unsurprisingly, as a consequence of their exensive usage a plethora of resistance mechanisms have been encountered in pathogenic bacteria. One of these resistance mechanisms entails the enzymatic cleavage of the macrolides' macrolactone ring by erythromycin esterases (Eres). The most frequently identified Ere enzyme is EreA, which confers resistance to the majority of clinically used macrolides. Despite the role Eres play in macrolide resistance, research into this family enzymes has been sparse. Here, we report the first three-dimensional structures of an erythromycin esterase, EreC. EreC is an extremely close homologue of EreA, displaying more than 90% sequence identity. Two structures of this enzyme, in conjunction with in silico flexible docking studies and previously reported mutagenesis data allowed for the proposal of a detailed catalytic mechanism for the Ere family of enzymes, labeling them as metal-independent hydrolases. Also presented are substrate spectrum assays for different members of the Ere family. The results from these assays together with an examination of residue conservation for the macrolide binding site in Eres, suggests two distinct active site archetypes within the Ere enzyme family.
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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.