ArticleFrontiers in cellular and infection microbiology2024
APH(3')-Ie, an aminoglycoside-modifying enzyme discovered in a rabbit-derived
Article in Frontiers in cellular and infection microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
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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
3 citing papers in PubMed.
- Identification and characteristics of a novel acquired aminoglycoside phosphotransferase, APH(3')-IVb, fromAntimicrobial agents and chemotherapy · 2026Article
- Phenotypic and genomic characterization ofMicrobiology spectrum · 2026Article
- Genomic and In Vivo Characterization of Antimicrobial Resistance and Virulence in UPECACS omega · 2025Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background: Aminoglycoside-modifying enzymes (AMEs) play an essential role in bacterial resistance to aminoglycoside antimicrobials. With the development of sequencing techniques, more bacterial genomes have been sequenced, which has aided in the discovery of an increasing number of novel resistance mechanisms. Methods: The bacterial species was identified by 16S rRNA gene homology and average nucleotide identity (ANI) analyses. The minimum inhibitory concentration (MIC) of each antimicrobial was determined by the agar dilution method. The protein was expressed with the pCold I vector in Results: A novel aminoglycoside resistance gene, designated Conclusion: In this work, a novel chromosomal aminoglycoside resistance gene, designated
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