ArticleNature communications2021
Chemoenzymatic modular assembly of O-GalNAc glycans for functional glycomics.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Defining substrate specificities ofOrganic chemistry frontiers : an international journal of organic chemistry · 2026Article
- Selective epimerization of GlcNAc to GalNAc through steady-state tuning under kinetic network control.Nature chemistry · 2026Article
- The Critical Role of GALNTs-Regulated O-GalNAc Glycosylation in Cancer Malignancy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Review
- An in vitro approach for simulating divergent Golgi O-glycosylation of tumor-associated MUC1 from normal MUC1.Nature communications · 2026Article
- Structure and characterisation of CMP-Kdn synthetase from the haptophyte microalgaeRSC chemical biology · 2026Article
- Process Safety Assessment of the Iron-Catalyzed 1,2-Research square · 2026Article
- Glycoengineering strategies for constructing defined Mucin O-glycans.Frontiers in molecular biosciences · 2026Review
- Iron-Catalyzed Highly Stereospecific Glycosylation with Glycal Epoxides.Angewandte Chemie (International ed. in English) · 2025Article
- Stereoselective Multigram-Scale Tn Antigen Synthesis via the Iron-Catalyzed Glycal 1,2-Organic letters · 2025Article
- A Bacteroides thetaiotaomicron genetic locus encodes activities consistent with mucin O-glycoprotein processing and N-acetylgalactosamine metabolism.Nature communications · 2025Article
- Divergent synthesis of amino acid-linked O-GalNAc glycan core structures.Nature protocols · 2025Review
- Silver Oxide Promoted Synthesis of AlphaThe Journal of organic chemistry · 2025Article
- Alcohol induces α2-6sialo mucin O-glycans that kill U937 macrophages mediated by sialic acid-binding immunoglobulin-like lectin 7 (Siglec 7).FEBS open bio · 2025Article
- Enzymatic Synthesis of Disialyllacto-N-Tetraose (DSLNT) and Related Human Milk Oligosaccharides Reveals Broad Siglec Recognition of the Atypical Neu5Acα2-6GlcNAc Motif.Angewandte Chemie (International ed. in English) · 2024Article
- Genetic and functional diversity of β-N-acetylgalactosamine-targeting glycosidases expanded by deep-sea metagenome analysis.Nature communications · 2024Article
- Highly stereoselective α-glycosylation with GalNChemical science · 2024Article
- Serum antibody screening using glycan arrays.Chemical Society reviews · 2024Review
- Oxidative Release ofAnalytical chemistry · 2023Article
- Abnormal glycosylation in glioma: related changes in biology, biomarkers and targeted therapy.Biomarker research · 2023Review
- Convergent chemoenzymatic synthesis ofChemical science · 2023Article
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Authors and funding
14 authors.
Funding
Abstract
O-GalNAc glycans (or mucin O-glycans) play pivotal roles in diverse biological and pathological processes, including tumor growth and progression. Structurally defined O-GalNAc glycans are essential for functional studies but synthetic challenges and their inherent structural diversity and complexity have limited access to these compounds. Herein, we report an efficient and robust chemoenzymatic modular assembly (CEMA) strategy to construct structurally diverse O-GalNAc glycans. The key to this strategy is the convergent assembly of O-GalNAc cores 1-4 and 6 from three chemical building blocks, followed by enzymatic diversification of the cores by 13 well-tailored enzyme modules. A total of 83 O-GalNAc glycans presenting various natural glycan epitopes are obtained and used to generate a unique synthetic mucin O-glycan microarray. Binding specificities of glycan-binding proteins (GBPs) including plant lectins and selected anti-glycan antibodies towards these O-GalNAc glycans are revealed by this microarray, promoting their applicability in functional O-glycomics. Serum samples from colorectal cancer patients and healthy controls are assayed using the array reveal higher bindings towards less common cores 3, 4, and 6 than abundant cores 1 and 2, providing insights into O-GalNAc glycan structure-activity relationships.
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