ArticleNature structural & molecular biology2015
The active site of O-GlcNAc transferase imposes constraints on substrate sequence.
Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 78 papers, 1 of them a synthesis that pooled it.
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
78 citing papers in PubMed, 1 synthesis or guideline pooled it, 131 citations in OpenAlex.
- The human O-GlcNAcome database and meta-analysis.Scientific data · 2021Pooled it
- Revealing and Exploiting the Biochemistry ofBiochemistry · 2026Review
- Glycan-related genes and genetic disorders.Journal of human genetics · 2026Review
- Human O-GlcNAcase catalytic-stalk dimer anchors flexible histone binding domains.Communications chemistry · 2025Article
- Protein β-O-glucosylation by Legionella LtpM through short consensus sequons G-T/S and S-G.Nature chemical biology · 2025Article
- Dermatophyte-Selective Imidazole-Thiosemicarbazides: Potent In Vitro Activity AgainstInternational journal of molecular sciences · 2025Article
- HumanResearch square · 2025Article
- O-linked β-N-acetylglucosamine modification in diabetic foot ulcer pathogenesis.Burns & trauma · 2025Review
- Rapid and large-scale glycopeptide enrichment strategy based on chemical ligation.National science review · 2024Article
- OGT and OGA: Sweet guardians of the genome.The Journal of biological chemistry · 2024Review
- O-GlcNAcylation determines the translational regulation and phase separation of YTHDF proteins.Nature cell biology · 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
- Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023Review
- Article
- O-GlcNAc Modification Alters the Chaperone Activity of HSP27 Charcot-Marie-Tooth Type 2 (CMT2) Variants in a Mutation-Selective Fashion.ACS chemical biology · 2023Article
- An O-GlcNAc transferase pathogenic variant linked to intellectual disability affects pluripotent stem cell self-renewal.Disease models & mechanisms · 2023Article
- Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY.Nature communications · 2023Article
- OGT Binding Peptide-Tagged Strategy Increases Protein O-GlcNAcylation Level inMolecules (Basel, Switzerland) · 2023Article
- ProteinMetabolites · 2022Review
18 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
O-GlcNAc transferase (OGT) glycosylates a diverse range of intracellular proteins with O-linked N-acetylglucosamine (O-GlcNAc), an essential and dynamic post-translational modification in metazoans. Although this enzyme modifies hundreds of proteins with O-GlcNAc, it is not understood how OGT achieves substrate specificity. In this study, we describe the application of a high-throughput OGT assay to a library of peptides. We mapped sites of O-GlcNAc modification by electron transfer dissociation MS and found that they correlate with previously detected O-GlcNAc sites. Crystal structures of four acceptor peptides in complex with Homo sapiens OGT suggest that a combination of size and conformational restriction defines sequence specificity in the -3 to +2 subsites. This work reveals that although the N-terminal TPR repeats of OGT may have roles in substrate recognition, the sequence restriction imposed by the peptide-binding site makes a substantial contribution to O-GlcNAc site specificity.
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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.