ArticleNature communications2022
A universal glycoenzyme biosynthesis pipeline that enables efficient cell-free remodeling of glycans.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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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.
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Who cites it
22 citing papers in PubMed, 41 citations in OpenAlex.
- From Glycocode to Precision Oncology: Therapeutic Strategies Targeting Aberrant O-GalNAc Glycosylation in Cancer.Chemical reviews · 2026Review
- Beyond Small Molecules: Orchestrating Cell Fate with Engineered Water-Soluble Membrane Proteins.Biomolecules · 2026Article
- Topological reprogramming transforms an integral membrane oligosaccharyltransferase into a water-soluble glycosylation catalyst.bioRxiv : the preprint server for biology · 2026Article
- Glycoengineering strategies for constructing defined Mucin O-glycans.Frontiers in molecular biosciences · 2026Review
- GLYCO-BUILD: an enzymatic pipeline for the synthesis of peptides carrying eukaryotic N-glycans.Nature communications · 2025Article
- Carbon source-dependent transcriptomic regulation and monosaccharide remodeling of exopolysaccharide biosynthesis in Pediococcus pceusentosa LL-07.BMC microbiology · 2025Article
- Chemical tools to study and modulate glycan-mediated host-bacteria interactions.Current opinion in chemical biology · 2025Review
- Mammalian Cell Surface Display for High-Throughput Protein Engineering of Glycosyltransferases.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Recent Progress in Developing Extracellular Vesicles as Nanovehicles to Deliver Carbohydrate-Based Therapeutics and Vaccines.Vaccines · 2025Review
- Enzyme cascades for nucleotide sugar regeneration in glycoconjugate synthesis.Applied microbiology and biotechnology · 2025Review
- Article
- BeyondChemical reviews · 2025Review
- Unveiling the GT114 family: Structural characterization of A075L, a glycosyltransferase from Paramecium bursaria chlorella virus-1 (PBCV-1).Protein science : a publication of the Protein Society · 2024Article
- Immobilized enzyme cascade for targeted glycosylation.Nature chemical biology · 2024Article
- Considerations for Glycoprotein Production.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The vertebrate sialylation machinery: structure-function and molecular evolution of GT-29 sialyltransferases.Glycoconjugate journal · 2023Review
- GlycoCAP: A Cell-Free, Bacterial Glycosylation Platform for Building Clickable Azido-Sialoglycoproteins.ACS synthetic biology · 2023Article
- Glycoprotein In Vitro N-Glycan Processing Using Enzymes Expressed inMolecules (Basel, Switzerland) · 2023Article
- Cell-freeFrontiers in molecular biosciences · 2023Article
- Targeting protein glycosylation to regulate inflammation in the respiratory tract: novel diagnostic and therapeutic candidates for chronic respiratory diseases.Frontiers in immunology · 2023Review
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 1 country.
Funding
Abstract
The ability to reconstitute natural glycosylation pathways or prototype entirely new ones from scratch is hampered by the limited availability of functional glycoenzymes, many of which are membrane proteins that fail to express in heterologous hosts. Here, we describe a strategy for topologically converting membrane-bound glycosyltransferases (GTs) into water soluble biocatalysts, which are expressed at high levels in the cytoplasm of living cells with retention of biological activity. We demonstrate the universality of the approach through facile production of 98 difficult-to-express GTs, predominantly of human origin, across several commonly used expression platforms. Using a subset of these water-soluble enzymes, we perform structural remodeling of both free and protein-linked glycans including those found on the monoclonal antibody therapeutic trastuzumab. Overall, our strategy for rationally redesigning GTs provides an effective and versatile biosynthetic route to large quantities of diverse, enzymatically active GTs, which should find use in structure-function studies as well as in biochemical and biomedical applications involving complex glycomolecules.
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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.