ArticleNature communications2025
Position-specific ORF nucleoside-ribose modifications enabled by complete chemical synthesis enhance mRNA stability and translation.
Article in Nature communications, 2025. 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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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
5 citing papers in PubMed.
- Bioengineering strategies for improving the immunogenicity of mRNA vaccines.Signal transduction and targeted therapy · 2026Review
- 2'-hydroxyl modification improves enzymatic and thermal stability of mRNA.Molecular therapy. Nucleic acids · 2026Article
- Synthesis of long and functionally active RNAs facilitated by acetal levulinic ester chemistry.Nucleic acids research · 2026Article
- Characterization of nuclease stability and poly(A)-binding protein binding activity of chemically modified poly(A) tail forRSC chemical biology · 2025Article
- From genetic code to global health: the impact of nucleic acid vaccines on disease prevention and treatment.RSC medicinal chemistry · 2025Review
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Authors and funding
17 authors.
Funding
Abstract
Despite the remarkable success of mRNA vaccines, improving the translational efficiency of mRNA therapeutics remains a critical challenge to their widespread clinical application. Here we systematically evaluate chemical modifications to improve the translational activity and stability of uncapped mRNA. We employ a primarily chemistry-based synthetic approach, which is crucial for the position-specific introduction of chemical modifications, enabling detailed structure-activity relationship studies, hitherto unattainable with conventional methods. A pivotal innovation herein is the introduction of 2´-F modification at the first nucleoside of the codon in the open reading frame, which significantly bolsters the stability of mRNA without compromising its translation. Additional modifications at the 5´-UTR and poly(A) tail with other types of nucleoside and phosphate analogs also exemplify the importance of terminal modifications for improved translation. Precise control of these modification patterns achieves higher peptide expression than conventional in vitro-transcribed mRNA. These findings offer a unique framework for designing effective mRNA-based therapeutics.
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