ReviewThe Journal of biological chemistry2026
Decoding the regulatory code: O-GlcNAcylation in epithelial-mesenchymal transition (EMT).
Review in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
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
1 citing paper in PubMed.
- Serum Starvation Promotes the Proteolysis of OGT by Activating AMPK and the CUL1/SKP1/SKP2 E3 Ubiquitin Ligase in 3T3-L1 Cells.Biomolecules & therapeutics · 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
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
O-linked N-acetylglucosamine (O-GlcNAc) is a monosaccharide modification occurring on serine or threonine residues of most eukaryotic proteins. Only two enzymes, O-GlcNAc transferase and O-GlcNAc hydrolase, regulate the dynamic flux of O-GlcNAc modification, rendering it extremely responsive to nutrition and stress conditions. O-GlcNAcylation stands at the center of epithelial-mesenchymal transition (EMT), sensing nutrient and stress signals to direct the transcriptional and signaling programs that enable phenotypic plasticity, thereby establishing its fundamental role in fibrosis and tumor metastasis. EMT is an essential biological event that confers mesenchymal characteristics to epithelial cells, characterized by the suppression of E-cadherin, a key epithelial adhesion molecule, and the overexpression of N-cadherin, a mesenchymal cadherin that promotes motility, or Vimentin, a mesenchymal intermediate filament protein. This review covers recent insights on the multiple canonical and non-canonical roles of O-GlcNAc, presenting O-GlcNAc cycling as a significant post-translational mechanism involved in various aspects of EMT. Furthermore, we systematically examine the functional connections between O-GlcNAcylation and EMT, focusing on identifying key O-GlcNAcylated proteins that regulate EMT and evaluating the relative contributions of transcriptional and post-translational mechanisms mediated by this modification. A comprehensive understanding of the intricate molecular circuitry governing the interplay between O-GlcNAcylation and EMT will deepen our mechanistic insights into cellular plasticity and offer novel therapeutic avenues for combating metastasis and other EMT-associated pathologies.
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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.