ReviewThe Journal of biological chemistry2014
The making of a sweet modification: structure and function of O-GlcNAc transferase.
Review in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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
40 citing papers in PubMed, 65 citations in OpenAlex.
- OGT as a metabolic-epigenetic integrator in cancer: context-dependent mechanisms and therapeutic vulnerabilities.Molecular medicine (Cambridge, Mass.) · 2026Review
- 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
- Glycosyltransferases: glycoengineers in human milk oligosaccharide synthesis and manufacturing.Frontiers in molecular biosciences · 2025Review
- Article
- OGT and OGA: Sweet guardians of the genome.The Journal of biological chemistry · 2024Review
- Review
- Article
- Hormogonium Development and Motility in Filamentous Cyanobacteria.Applied and environmental microbiology · 2023Review
- The role of O-GlcNAcylation in innate immunity and inflammation.Journal of molecular cell biology · 2023Review
- Article
- Structural basis for SdgB- and SdgA-mediated glycosylation of staphylococcal adhesive proteins.Acta crystallographica. Section D, Structural biology · 2021Article
- Glycation and Glycosylation in Cardiovascular Remodeling: Focus on Advanced Glycation End Products and O-Linked Glycosylations as Glucose-Related Pathogenetic Factors and Disease Markers.Journal of clinical medicine · 2021Review
- O-GlcNAcylation: the "stress and nutrition receptor" in cell stress response.Cell stress & chaperones · 2021Review
- Article
- Intracellular Hydrolysis of Small-MoleculeMolecules (Basel, Switzerland) · 2020Article
- Synthetic Glycobiology: Parts, Systems, and Applications.ACS synthetic biology · 2020Review
- Protein Glycoengineering: An Approach for Improving Protein Properties.Frontiers in chemistry · 2020Review
- Expression of messenger RNA encoding two cellular metabolic regulators, AMP-activated protein kinase (AMPK) and O-GlcNAc transferase (OGT), in channel catfish: Their tissue distribution and relationship with changes in food intake.Comparative biochemistry and physiology. Part A, Molecular & integrative physiology · 2019Article
- Aspartate Residues Far from the Active Site Drive O-GlcNAc Transferase Substrate Selection.Journal of the American Chemical Society · 2019Article
- Protein O-GlcNAcylation Is Essential for the Maintenance of Renal Energy Homeostasis and FunctionJournal of the American Society of Nephrology : JASN · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
O-GlcNAc transferase is an essential mammalian enzyme responsible for transferring a single GlcNAc moiety from UDP-GlcNAc to specific serine/threonine residues of hundreds of nuclear and cytoplasmic proteins. This modification is dynamic and has been implicated in numerous signaling pathways. An unexpected second function for O-GlcNAc transferase as a protease involved in cleaving the epigenetic regulator HCF-1 has also been reported. Recent structural and biochemical studies that provide insight into the mechanism of glycosylation and HCF-1 cleavage will be described, with outstanding questions highlighted.
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.