ReviewCommunications biology2026
Glycosylation as a dynamic regulator of RLR and cGAS-STING innate immune signalling pathways.
Review in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Beyond Sequence: Posttranslational Remodeling of Antigens in Autoimmunity.Immunological reviews · 2026Review
- cGAMP suppresses FTO expression to promote mCellular and molecular life sciences : CMLS · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Innate immune sensing by RIG-I-like receptors (RLRs) and the cGAS-STING pathway is tightly regulated by glycosylation. This review summarizes how distinct glycosylation modalities shape antiviral signaling at multiple levels. N-glycosylation in the ER-Golgi is essential for STING folding, stability, and signaling competence, whereas aberrant glycan states disrupt DNA sensing. In contrast, cytosolic O-GlcNAcylation dynamically modulates RLR-cGAS pathways by regulating MAVS aggregation, suppressing IRF3 and NF-κB activation, and interfering with cGAS-DNA binding. We further discuss crosstalk between glycosylation, ubiquitination, and phosphorylation, metabolic regulation of UDP-GlcNAc flux, and pathogen- or tumor-driven glycosylation reprogramming, highlighting glycosylation enzymes as potential immunomodulatory targets.
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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.