ArticleAmino acids2011
Substrate and product analogues as human O-GlcNAc transferase inhibitors.
Article in Amino acids, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 70 citations in OpenAlex.
- O-GlcNAcylation: A molecular switch linking brain health to neurodegeneration.Neural regeneration research · 2026Article
- Cross-talk between glycosylation pathways: Mechanistic insights and implications for human diseases.Molecular metabolism · 2026Review
- Synthesis and Evaluation of Iminosugar-Based Analogs of UDP-GlcNAc as Putative OGT Inhibitors.ChemMedChem · 2026Article
- A Genetically Encoded Assay System to Quantify O-GlcNAc Transferase (OGT) Activity in Live Cells.Angewandte Chemie (International ed. in English) · 2025Article
- OSMI-4-based PROTACs do not influenceRSC advances · 2025Article
- Structural insights into mechanism and specificity of the plant protein O-fucosyltransferase SPINDLY.Nature communications · 2022Article
- O-GlcNAcylation: an important post-translational modification and a potential therapeutic target for cancer therapy.Molecular medicine (Cambridge, Mass.) · 2022Review
- Role ofPhysiological reviews · 2021Review
- C-Terminal Tag Location Hampers in Vitro Profiling of OGT Peptide Substrates by mRNA Display.Chembiochem : a European journal of chemical biology · 2021Article
- Pharmacological Inhibition of O-GlcNAc Transferase Promotes mTOR-Dependent Autophagy in Rat Cortical Neurons.Brain sciences · 2020Article
- O-GlcNAcylation as a Therapeutic Target for Alzheimer's Disease.Neuromolecular medicine · 2020Review
- An intellectual disability syndrome with single-nucleotide variants in O-GlcNAc transferase.European journal of human genetics : EJHG · 2020Review
- Inhibition ofMedChemComm · 2018Article
- A small molecule that inhibits OGT activity in cells.ACS chemical biology · 2015Article
- The making of a sweet modification: structure and function of O-GlcNAc transferase.The Journal of biological chemistry · 2014Review
- Substrate specificity of cytoplasmic N-glycosyltransferase.The Journal of biological chemistry · 2014Article
- The role of O-GlcNAc signaling in the pathogenesis of diabetic retinopathy.Proteomics. Clinical applications · 2014Review
- Bisubstrate UDP-peptide conjugates as human O-GlcNAc transferase inhibitors.The Biochemical journal · 2014Article
- Dynamic O-GlcNAcylation and its roles in the cellular stress response and homeostasis.Cell stress & chaperones · 2013Article
- Protein O-GlcNAcylation in diabetes and diabetic complications.Expert review of proteomics · 2013Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Protein glycosylation on serine/threonine residues with N-acetylglucosamine (O-GlcNAc) is a dynamic, inducible and abundant post-translational modification. It is thought to regulate many cellular processes and there are examples of interplay between O-GlcNAc and protein phosphorylation. In metazoa, a single, highly conserved and essential gene encodes the O-GlcNAc transferase (OGT) that transfers GlcNAc onto substrate proteins using UDP-GlcNAc as the sugar donor. Specific inhibitors of human OGT would be useful tools to probe the role of this post-translational modification in regulating processes in the living cell. Here, we describe the synthesis of novel UDP-GlcNAc/UDP analogues and evaluate their inhibitory properties and structural binding modes in vitro alongside alloxan, a previously reported weak OGT inhibitor. While the novel analogues are not active on living cells, they inhibit the enzyme in the micromolar range and together with the structural data provide useful templates for further optimisation.
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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.