ArticleProceedings of the National Academy of Sciences of the United States of America2025
5'-terminal glycosylation of protein-coding transcripts: An epitranscriptomic modification that prolongs mRNA lifetimes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- Bacterial small regulatory RNAs.Nature reviews. Microbiology · 2026Review
- Crystal structure of mouse DXO in complex with the UDP-N-acetylglucosamine cap and molecular mechanism for the decapping reactions.Nucleic acids research · 2026Article
- Omnivore RNA pyrophosphatase: a versatile enzyme that efficiently removes diverse protecting groups from the 5' end of RNA.Nucleic acids research · 2026Article
- Sugar caps protect mRNAs from decay.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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3 authors.
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Abstract
Glycosylation is among the most common molecular modifications in living organisms, one that affects the function of myriad macromolecules: mostly proteins, lipids, and polysaccharides of various kinds but also a few specific noncoding RNAs that undergo glycosylation at an internal site. Here we expand the glycome by showing that protein-coding transcripts can also be glycosylated, but in the form of a 5'-terminal glucose cap. These caps are present on up to 30 to 40% of the 5' ends of U-initiated mRNAs in
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