ArticleChemistry & biology2009
Identification of distinct thiopeptide-antibiotic precursor lead compounds using translation machinery assays.
Article in Chemistry & biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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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Who cites it
12 citing papers in PubMed, 26 citations in OpenAlex.
- Distinct tRNA Accommodation Intermediates Observed on the Ribosome with the Antibiotics Hygromycin A and A201A.Molecular cell · 2015Article
- Cryo-EM structure of the tetracycline resistance protein TetM in complex with a translating ribosome at 3.9-Å resolution.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structural basis and dynamics of multidrug recognition in a minimal bacterial multidrug resistance system.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structure-activity relationships of thiostrepton derivatives: implications for rational drug design.Journal of computer-aided molecular design · 2014Article
- The bacterial translation stress response.FEMS microbiology reviews · 2014Review
- Structural basis for potent inhibitory activity of the antibiotic tigecycline during protein synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.Natural product reports · 2013Review
- Elongation factor G is a critical target during oxidative damage to the translation system of Escherichia coli.The Journal of biological chemistry · 2012Article
- Differential effects of thiopeptide and orthosomycin antibiotics on translational GTPases.Chemistry & biology · 2011Article
- Thiazolyl peptide antibiotic biosynthesis: a cascade of post-translational modifications on ribosomal nascent proteins.The Journal of biological chemistry · 2010Review
- Probing translation with small-molecule inhibitors.Chemistry & biology · 2010Review
- Manipulation of thiocillin variants by prepeptide gene replacement: structure, conformation, and activity of heterocycle substitution mutants.Journal of the American Chemical Society · 2010Article
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
Most thiopeptide antibiotics target the translational machinery: thiostrepton (ThS) and nosiheptide (NoS) target the ribosome and inhibit translation factor function, whereas GE2270A/T binds to the elongation factor EF-Tu and prevents ternary complex formation. We have used several in vitro translational machinery assays to screen a library of thiopeptide antibiotic precursor compounds and identified four families of precursor compounds that are either themselves inhibitory or are able to relieve the inhibitory effects of ThS, NoS, or GE2270T. Some of these precursors represent distinct compounds with respect to their ability to bind to ribosomes. The results not only provide insight into the mechanism of action of thiopeptide compounds but also demonstrate the potential of such assays for identifying lead compounds that might be missed using conventional inhibitory screening protocols.
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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.