ReviewCurrent opinion in structural biology2019
Structural characterization of the O-GlcNAc cycling enzymes: insights into substrate recognition and catalytic mechanisms.
Review in Current opinion in structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 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
48 citing papers in PubMed, 94 citations in OpenAlex.
- Human O-GlcNAcase catalytic-stalk dimer anchors flexible histone binding domains.Communications chemistry · 2025Article
- Protein O-GlcNAcylation in Health and Diseases.MedComm · 2025Review
- Dissecting the Mechanisms Underlying Substrate Recognition and Functional Regulation of O-GlcNAc Cycling Enzymes.ACS chemical biology · 2025Review
- Protein O-GlcNAcylation in reproductive biology and the impact of metabolic disease.Human reproduction update · 2025Review
- HumanResearch square · 2025Article
- Photoactivatable O-GlcNAc Transferase Library Enables Covalent Chemical Capture of Solvent-Exposed TPR Domain Interactions.Chembiochem : a European journal of chemical biology · 2025Article
- Recent Progress of Small-molecule Inhibitors of O-GlcNAcase for Alzheimer's Disease.Mini reviews in medicinal chemistry · 2025Review
- Ultradeep O-GlcNAc proteomics reveals widespread O-GlcNAcylation on tyrosine residues of proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The non-catalytic domains of O-GlcNAc cycling enzymes present new opportunities for function-specific control.Current opinion in chemical biology · 2024Review
- OGA mutant aberrantly hydrolyzes O-GlcNAc modification from PDLIM7 to modulate p53 and cytoskeleton in promoting cancer cell malignancy.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Dissecting OGT's TPR domain to identify determinants of cellular function.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- OGT and OGA: Sweet guardians of the genome.The Journal of biological chemistry · 2024Review
- Review
- O-GlcNAcylation Inhibition Upregulates Connexin43 Expression in the Endothelium to Protect the Tight Junction Barrier in Diabetic Retinopathy.Investigative ophthalmology & visual science · 2023Article
- Cryo-EM structure of human O-GlcNAcylation enzyme pair OGT-OGA complex.Nature communications · 2023Article
- Phage display uncovers a sequence motif that drives polypeptide binding to a conserved regulatory exosite of O-GlcNAc transferase.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Regulation of phosphoglycerate kinase 1 and its critical role in cancer.Cell communication and signaling : CCS · 2023Review
- Geometric Remodeling of Nitrilase Active Pocket Based on ALF-Scanning Strategy To Enhance Aromatic Nitrile Substrate Preference and Catalytic Efficiency.Applied and environmental microbiology · 2023Article
- Extracellular arginine availability modulates eIF2α O-GlcNAcylation and heme oxygenase 1 translation for cellular homeostasis.Journal of biomedical science · 2023Article
- Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY.Nature communications · 2023Article
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 at 2 institutions in 1 country.
Funding
Abstract
Dysregulation of nuclear and cytoplasmic O-linked β-N-acetylglucosamine (O-GlcNAc) cycling is implicated in a range of diseases including diabetes and cancer. This modification maintains cellular homeostasis by regulating several biological processes, such as cell signaling. This highly regulated cycle is governed by two sole essential enzymes, O-GlcNAc transferase and O-GlcNAcase that add O-GlcNAc and remove it from over a thousand substrates, respectively. Until recently, due to lack of structural information, the mechanism of substrate recognition has eluted researchers. Here, we review recent successes in structural characterization of these enzymes and how this information has illuminated key features essential for catalysis and substrate recognition. Additionally, we highlight recent studies which have used this information to expand our understanding of substrate specificity by each enzyme.
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.