ArticleJournal of biomolecular screening2013
A high-throughput screen of the GTPase activity of Escherichia coli EngA to find an inhibitor of bacterial ribosome biogenesis.
Article in Journal of biomolecular screening, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- Structural and functional characterization of mycobacterial PhoH2 and identification of potential inhibitor of its enzymatic activity.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024Article
- High-Throughput Screening of Natural Product and Synthetic Molecule Libraries for Antibacterial Drug Discovery.Metabolites · 2023Review
- Antibiotics targeting bacterial ribosomal subunit biogenesis.The Journal of antimicrobial chemotherapy · 2020Review
- Article
- Substrate independent ATPase activity may complicate high throughput screening.Analytical biochemistry · 2016Article
- Heterologous Expression of Der Homologs in an Escherichia coli der Mutant and Their Functional Complementation.Journal of bacteriology · 2016Article
- Article
- Chemical modulators of ribosome biogenesis as biological probes.Nature chemical biology · 2015Article
- Structural insights into the function of a unique tandem GTPase EngA in bacterial ribosome assembly.Nucleic acids research · 2014Article
- Rank ordering plate data facilitates data visualization and normalization in high-throughput screening.Journal of biomolecular screening · 2014Article
- Validation of a fluorescence-based screening concept to identify ribosome assembly defects in Escherichia coli.Nucleic acids research · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The synthesis of ribosomes is an essential process, which is aided by a variety of trans-acting factors in bacteria. Among these is a group of GTPases essential for bacterial viability and emerging as promising targets for new antibacterial agents. Herein, we describe a robust high-throughput screening process for inhibitors of one such GTPase, the Escherichia coli EngA protein. The primary screen employed an assay of phosphate production in a 384-well density. Reaction conditions were chosen to maximize sensitivity for the discovery of competitive inhibitors while maintaining a strong signal amplitude and low noise. In a pilot screen of 31,800 chemical compounds, 44 active compounds were identified. Furthermore, we describe the elimination of nonspecific inhibitors that were detergent sensitive or reactive as well as those that interfered with the high-throughput phosphate assay. Four inhibitors survived these common counterscreens for nonspecificity, but these chemicals were also inhibitors of the unrelated enzyme dihydrofolate reductase, suggesting that they too were promiscuously active. The high-throughput screen of the EngA protein described here provides a meticulous pilot study in the search for specific inhibitors of GTPases involved in ribosome biogenesis.
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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.