ArticleJournal of the American Chemical Society2019
Redox-Controlled Site-Specific α2-6-Sialylation.
Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- An Automation Platform for the Chemoenzymatic Synthesis of Complex Sulfated and Branched Glycans.Journal of the American Chemical Society · 2026Article
- Carbohydrate Synthesis is Entering the Data-Driven Digital Era.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Review
- Orthogonal-Group-Controlled Site-Selective I-Branching of Poly-N-acetyllactosamine Chains Reveals Unique Binding Specificities of Proteins towards I-Antigens.Angewandte Chemie (International ed. in English) · 2025Article
- Sialylation-immune-related lncRNAFrontiers in immunology · 2025Article
- Chemoenzymatic Synthesis of Keratan Sulfate Oligosaccharides Using UDP-Galactose-6-aldehyde To Control Sulfation at Galactosides.Organic letters · 2024Article
- A Biomimetic Synthetic Strategy Can Provide Keratan Sulfate I and II Oligosaccharides with Diverse Fucosylation and Sulfation Patterns.Journal of the American Chemical Society · 2024Article
- Phosphates as Assisting Groups in Glycan Synthesis.ACS central science · 2024Article
- Convergent chemoenzymatic synthesis ofChemical science · 2023Article
- Article
- Evolution of Human-Specific Alleles Protecting Cognitive Function of Grandmothers.Molecular biology and evolution · 2022Article
- Sialoglycan-binding patterns of bacterial ABThe Journal of biological chemistry · 2022Article
- Recent progress in synthesis of carbohydrates with sugar nucleotide-dependent glycosyltransferases.Current opinion in chemical biology · 2021Review
- Biochemical characterization of Helicobacter pylori α1-3-fucosyltransferase and its application in the synthesis of fucosylated human milk oligosaccharides.Carbohydrate research · 2019Article
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Authors and funding
11 authors.
Funding
Abstract
The first bacterial α2-6-sialyltransferase cloned from Photobacterium damselae (Pd2,6ST) has been widely applied for the synthesis of various α2-6-linked sialosides. However, the extreme substrate flexibility of Pd2,6ST makes it unsuitable for site-specific α2-6-sialylation of complex substrates containing multiple galactose and/or N-acetylgalactosamine units. To tackle this problem, a general redox-controlled site-specific sialylation strategy using Pd2,6ST is described. This approach features site-specific enzymatic oxidation of galactose units to mask the unwanted sialylation sites and precisely controlling the site-specific α2-6-sialylation at intact galactose or N-acetylgalactosamine units.
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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.