ArticleGlycoconjugate journal2024
Processing of N-glycans in the ER and Golgi influences the production of surface sialylated glycoRNA.
Article in Glycoconjugate journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
The trial behind it
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Who cites it
6 citing papers in PubMed.
- In situ tracking of glycoRNAs on single-cell surface to reveal RNA heterogeneity and transport mechanism.Nucleic acids research · 2026Article
- GlycoRNA biology, a naive field with unlimited horizons.Glycoconjugate journal · 2026Article
- GlycoRNA research: from unknown unknowns to known unknowns.Protein & cell · 2026Review
- Functional regulation of GlycoRNA and progress in malignant tumors.Journal of translational medicine · 2026Review
- Glycosylated RNAs: discovery and implications in cancer biology.Frontiers in oncology · 2026Review
- RNA on Display: Cell Surface RNA as a Novel Layer of Cellular Regulation.Research (Washington, D.C.) · 2026Review
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Glycoconjugates, including glycans on proteins and lipids, have obtained significant attention due to their critical roles in both intracellular and intercellular biological functions and processes. Notably, recent discoveries have revealed the presence of glycosylated RNAs (glycoRNAs) on cell surfaces. Despite the well-characterized roles of RNA modifications, RNA glycosylation remains relatively unexplored. In this study, we investigate the relationship between N-glycosylation and RNA glycosylation. Using a recombinant Siglec11-Fc as a probe, we detected surface sialylated glycoRNAs in human cell lines and identified their dependency on the catalytic isoforms of the oligosaccharyltransferase (OST) complex, implicating STT3A-dependent protein glycosylation as a predominant contributor for affecting indirect generation of glycoRNAs. Additionally, perturbations in N-glycan biosynthesis pathways or changes in N-glycan structure impact surface sialylated glycoRNA levels, indicating a regulatory role of glycan metabolic pathways in RNA glycosylation. Together, our results underscore the intricate relationship between protein N-glycosylation and processing and RNA biology.
Indexed as
Identifiers
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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.