ArticleNature communications2015
9-O-Acetylation of sialic acids is catalysed by CASD1 via a covalent acetyl-enzyme intermediate.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
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Who cites it
76 citing papers in PubMed.
- Targeting virus-glycan recognition in influenza viruses and coronaviruses: from the molecular principles to glycomimetic antivirals strategies.RSC chemical biology · 2026Review
- Interplay of SLC33A1-dependent and -independent Golgi sialic acid O-acetylation in CASD1 catalysis.Nature communications · 2026Article
- Forgotten Gangliosides:International journal of molecular sciences · 2026Review
- FUT1- and GAL3ST2-mediated cellular glycan remodeling broadly restricts sialic acid-dependent viral infections.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Chemoenzymatically Synthesized O-Acetylated GD3 Gangliosides to Examine Viral Receptor Specificities in a Cellular Context.Angewandte Chemie (International ed. in English) · 2026Article
- Identification and Evaluation of CMP-Sialic Acids.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Loss of ST8Sia6 mediated α-2,8-linked di-sialylation enhances T cell-dependent antibody responses and promotes autoimmunity in aged mice.Frontiers in immunology · 2026Article
- Analysis of sulfated sialic acids by liquid chromatography coupled with high-resolution mass spectrometry and fluorescence detection.BBA advances · 2026Article
- The Emerging Role of Sialic Acids in Obesity and Diabetes: Molecular Mechanisms and Therapeutic Perspectives.Biomolecules · 2025Review
- Loss of sialic acid side-chainProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Temporal and Sex-DependentInternational journal of molecular sciences · 2025Article
- NXPE1 alters the sialoglycome by acetylating sialic acids in the human colon.Nature communications · 2025Article
- Acyltransferases that Modify Cell Surface Polymers Across the Membrane.Biochemistry · 2025Review
- Anti-OAcGD2 antibody in combination with ceramide kinase inhibitor mediates potent antitumor cytotoxicity against breast cancer and diffuse intrinsic pontine glioma cells.Molecular and cellular biochemistry · 2025Article
- The Ulcerative Colitis-Associated Gene NXPE1 Catalyzes Glycan Modifications on Colonic Mucin.Journal of the American Chemical Society · 2025Article
- Extended receptor repertoire of an adenovirus associated with human obesity.PLoS pathogens · 2025Article
- ASGR1 deficiency improves atherosclerosis but alters liver metabolism in ApoECardiovascular diabetology · 2024Article
- Non-targeted N-glycome profiling reveals multiple layers of organ-specific diversity in mice.Nature communications · 2024Article
- The HCoV-HKU1 N-Terminal Domain Binds a Wide Range of 9-ACS infectious diseases · 2024Article
- Synthetic Sialosides Terminated with 8-N-Substituted Sialic Acid as Selective Substrates for Sialidases from Bacteria and Influenza Viruses.Angewandte Chemie (International ed. in English) · 2024Article
16 more citing papers are in PubMed but not listed here.
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8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Sialic acids, terminal sugars of glycoproteins and glycolipids, play important roles in development, cellular recognition processes and host-pathogen interactions. A common modification of sialic acids is 9-O-acetylation, which has been implicated in sialoglycan recognition, ganglioside biology, and the survival and drug resistance of acute lymphoblastic leukaemia cells. Despite many functional implications, the molecular basis of 9-O-acetylation has remained elusive thus far. Following cellular approaches, including selective gene knockout by CRISPR/Cas genome editing, we here show that CASD1--a previously identified human candidate gene--is essential for sialic acid 9-O-acetylation. In vitro assays with the purified N-terminal luminal domain of CASD1 demonstrate transfer of acetyl groups from acetyl-coenzyme A to CMP-activated sialic acid and formation of a covalent acetyl-enzyme intermediate. Our study provides direct evidence that CASD1 is a sialate O-acetyltransferase and serves as key enzyme in the biosynthesis of 9-O-acetylated sialoglycans.
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