ArticleACS infectious diseases2015
Comparative Study of Eis-like Enzymes from Pathogenic and Nonpathogenic Bacteria.
Article in ACS infectious diseases, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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.
The trial behind it
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Who cites it
19 citing papers in PubMed, 22 citations in OpenAlex.
- Multicentre preclinical profiling of apramycin for the treatment of nontuberculous mycobacteria.EBioMedicine · 2026Article
- Crystal structures and low-affinity complex formation of halogenase CtcP and FAD reductase CtcQ from the chlortetracycline biosynthetic pathway.Bioscience reports · 2025Article
- Discovery and Mechanistic Analysis of Structurally Diverse Inhibitors of Acetyltransferase Eis among FDA-Approved Drugs.Biochemistry · 2023Article
- Discovery and development of inhibitors of acetyltransferase Eis to combat Mycobacterium tuberculosis.Methods in enzymology · 2023Article
- Discovery of substituted benzyloxy-benzylamine inhibitors of acetyltransferase Eis and their anti-mycobacterial activity.European journal of medicinal chemistry · 2022Article
- Structure-Guided Optimization of Inhibitors of Acetyltransferase Eis fromACS chemical biology · 2020Article
- Mycobacterial Aminoglycoside Acetyltransferases: A Little of Drug Resistance, and a Lot of Other Roles.Frontiers in microbiology · 2019Article
- Comprehensive review of chemical strategies for the preparation of new aminoglycosides and their biological activities.Chemical Society reviews · 2018Review
- Acetylation by Eis and Deacetylation by Rv1151c of Mycobacterium tuberculosis HupB: Biochemical and Structural Insight.Biochemistry · 2018Article
- Combating Enhanced Intracellular Survival (Eis)-Mediated Kanamycin Resistance of Mycobacterium tuberculosis by Novel Pyrrolo[1,5-a]pyrazine-Based Eis Inhibitors.ACS infectious diseases · 2017Article
- Sulfonamide-Based Inhibitors of Aminoglycoside Acetyltransferase Eis Abolish Resistance to Kanamycin in Mycobacterium tuberculosis.Journal of medicinal chemistry · 2016Article
- Discovery and Optimization of Two Eis Inhibitor Families as Kanamycin Adjuvants against Drug-ResistantACS medicinal chemistry letters · 2016Article
- Expanding Aminoglycoside Resistance Enzyme Regiospecificity by Mutation and Truncation.Biochemistry · 2016Article
- Potent Inhibitors of Acetyltransferase Eis Overcome Kanamycin Resistance in Mycobacterium tuberculosis.ACS chemical biology · 2016Article
- Arginine-linked neomycin B dimers: synthesis, rRNA binding, and resistance enzyme activity.MedChemComm · 2016Article
- Mechanisms of Resistance to Aminoglycoside Antibiotics: Overview and Perspectives.MedChemComm · 2016Article
- Synthesis and Bioactivities of Kanamycin B-Derived Cationic Amphiphiles.Journal of medicinal chemistry · 2015Article
- Amphiphilic Tobramycin Analogues as Antibacterial and Antifungal Agents.Antimicrobial agents and chemotherapy · 2015Article
- A review of patents (2011-2015) towards combating resistance to and toxicity of aminoglycosides.MedChemCommArticle
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Antibiotic resistance is a growing problem worldwide. Of particular importance is the resistance of Mycobacterium tuberculosis (Mtb) to currently available antibiotics used in the treatment of infected patients. Up-regulation of an aminoglycoside (AG) acetyltransferase, the enhanced intracellular survival (Eis) protein of Mtb (Eis_Mtb), is responsible for resistance to the second-line injectable drug kanamycin A in a number of Mtb clinical isolates. This acetyltransferase is known to modify AGs, not at a single position, as usual for this type of enzyme, but at multiple amine sites. We identified, using in silico techniques, 22 homologues from a wide variety of bacteria, that we then cloned, purified, and biochemically studied. From the selected Eis homologues, 7 showed the ability to modify AGs to various degrees and displayed both similarities and differences when compared to Eis_Mtb. In addition, an inhibitor proved to be active against all homologues tested. Our findings show that this family of acetyltransferase enzymes exists in both mycobacteria and non-mycobacteria and in both pathogenic and nonpathogenic species. The bacterial strains described herein should be monitored for rising resistance rates to AGs.
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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.