ReviewInternational journal of molecular sciences2026
Distinct O-Linked Glycosylation Systems in Signaling and Immune Regulation.
Review in International journal of molecular sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
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
O-linked glycosylation comprises distinct regulatory systems, including secretory-pathway mucin-type O-GalNAc glycosylation and intracellular O-GlcNAcylation. These modifications both target serine/threonine residues but differ in glycan structure, cellular compartment, enzymatic machinery, and biological function. This narrative review was based on targeted searches of PubMed, Web of Science, and related literature using keywords related to O-glycosylation, O-GalNAc glycosylation, O-GlcNAcylation, immune regulation, cell signaling, glycoproteomics, and congenital disorders of glycosylation (CDG). We summarize evidence that mucin-type O-glycosylation regulates receptor behavior, cell adhesion, immune checkpoints, immunoglobulin function, antigen recognition, and pathogen-host interactions, whereas O-GlcNAcylation mainly modulates intracellular signaling, transcriptional control, stress responses, post-translational modification crosstalk, and innate immune pathways. We also discuss how glycosylation defects, including CDG and selected O-linked glycosylation disorders, connect genetic variation with disease phenotypes. Recent advances in site-specific glycoproteomics, O-glycoprotease-assisted workflows, LC-MS/MS-based glycopeptide analysis, and spatial or temporal profiling have improved mechanistic interpretation but still face limitations in site localization, structural resolution, and functional validation. Overall, the evidence supports the hypothesis that distinct O-linked glycosylation systems act through different molecular mechanisms but converge on signaling regulation, immune homeostasis, and disease susceptibility.
Indexed as
Identifiers
What OpenQuestion holds
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.