ArticleNature chemical biology2024
Immobilized enzyme cascade for targeted glycosylation.
Article in Nature chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Article
- Iterative Bump-and-Hole Engineering Creates a Bioorthogonal Reporter forJournal of the American Chemical Society · 2026Article
- EnzymeHunter: Achieving fine-grained enzyme function prediction with a hierarchically aware contrastive learning framework.Patterns (New York, N.Y.) · 2026Article
- Delineating the Transcriptional and Phenotypic Impact from Biotherapeutic Glycoengineering.bioRxiv : the preprint server for biology · 2026Article
- Iterative Bump-and-hole engineering creates a bioorthogonal reporter forbioRxiv : the preprint server for biology · 2026Article
- GLYCO-BUILD: an enzymatic pipeline for the synthesis of peptides carrying eukaryotic N-glycans.Nature communications · 2025Article
- A modular, reusable biocatalytic flow system for UDP-GlcNAc production.Reaction chemistry & engineering · 2025Article
- Immobilization of alginate C-5 epimerases usingApplied and environmental microbiology · 2025Article
- Advancing recombinant protein expression in Komagataella phaffii: opportunities and challenges.FEMS yeast research · 2025Review
- Spatially-resolved characterization of the metabolic andRSC advances · 2025Article
- Molecular Mechanisms Underlying the Loop-Closing Dynamics of β-1,4 Galactosyltransferase 1.Journal of chemical information and modeling · 2025Article
- A Bioorthogonal Precision Tool for HumanJournal of the American Chemical Society · 2024Article
- Session commentaries: synthetic and constructive biology.Biophysical reviews · 2024Review
- Accurately predicting enzyme functions through geometric graph learning on ESMFold-predicted structures.Nature communications · 2024Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Glycosylation is a critical post-translational protein modification that affects folding, half-life and functionality. Glycosylation is a non-templated and heterogeneous process because of the promiscuity of the enzymes involved. We describe a platform for sequential glycosylation reactions for tailored sugar structures (SUGAR-TARGET) that allows bespoke, controlled N-linked glycosylation in vitro enabled by immobilized enzymes produced with a one-step immobilization/purification method. We reconstruct a reaction cascade mimicking a glycosylation pathway where promiscuity naturally exists to humanize a range of proteins derived from different cellular systems, yielding near-homogeneous glycoforms. Immobilized β-1,4-galactosyltransferase is used to enhance the galactosylation profile of three IgGs, yielding 80.2-96.3% terminal galactosylation. Enzyme recycling is demonstrated for a reaction time greater than 80 h. The platform is easy to implement, modular and reusable and can therefore produce homogeneous glycan structures derived from various hosts for functional and clinical evaluation.
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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.