ArticleChembiochem : a European journal of chemical biology2012
Targeting a regulatory element in human thymidylate synthase mRNA.
Article in Chembiochem : a European journal of chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- Genome-Wide Identification and Analysis of the Phosphoenolpyruvate Carboxylase Gene Family inFrontiers in plant science · 2021Article
- Article
- Analysis of mRNA recognition by human thymidylate synthase.Bioscience reports · 2014Article
- Functional conservation despite structural divergence in ligand-responsive RNA switches.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Screening for inhibitors of the hepatitis C virus internal ribosome entry site RNA.Bioorganic & medicinal chemistry · 2013Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Thymidylate synthase (TS) is a key enzyme in the biosynthesis of thymidine. The use of TS inhibitors in cancer chemotherapy suffers from resistance development in tumors through upregulation of TS expression. Autoregulatory translation control has been implicated with TS overexpression. TS binding at its own mRNA, which leads to sequestration of the start codon, is abolished when the enzyme forms an inhibitor complex, thereby relieving translation suppression. We have used the protein-binding site from the TS mRNA in the context of a bicistronic expression system to validate targeting the regulatory motif with stabilizing ligands that prevent ribosomal initiation. Stabilization of the RNA by mutations, which were studied as surrogates of ligand binding, suppresses translation of the TS protein. Compounds that stabilize the TS-binding RNA motif and thereby inhibit ribosomal initiation might be used in combination with existing TS enzyme-targeting drugs to overcome resistance development during chemotherapy.
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Registered trials
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