ArticleNature chemical biology2018
Design of glycosylation sites by rapid synthesis and analysis of glycosyltransferases.
Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 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
71 citing papers in PubMed, 141 citations in OpenAlex.
- Decoding the complex substrate specificities of GalNAc-Ts.Glycobiology · 2025Review
- Protein β-O-glucosylation by Legionella LtpM through short consensus sequons G-T/S and S-G.Nature chemical biology · 2025Article
- Characterizing and engineering post-translational modifications with high-throughput cell-free expression.Nature communications · 2025Article
- Cell-free protein synthesis and vesicle systems for programmable therapeutic manufacturing and delivery.Journal of biological engineering · 2025Review
- Accelerated enzyme engineering by machine-learning guided cell-free expression.Nature communications · 2025Article
- Cell-Free Gene Expression: Methods and Applications.Chemical reviews · 2025Review
- Supramolecular assembly of multifunctional protein gels via anMolecular systems design & engineering · 2024Article
- Carbohydrate-active enzyme (CAZyme) discovery and engineeringRSC chemical biology · 2024Review
- Exposing the molecular heterogeneity of glycosylated biotherapeutics.Nature communications · 2024Article
- Combining machine learning with structure-based protein design to predict and engineer post-translational modifications of proteins.PLoS computational biology · 2024Article
- Cell-Free Systems for the Production of Glycoproteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- At-Home, Cell-Free Synthetic Biology Education Modules for Transcriptional Regulation and Environmental Water Quality Monitoring.ACS synthetic biology · 2023Article
- Modulating antibody effector functions by Fc glycoengineering.Biotechnology advances · 2023Review
- Molecular basis for bacterial N-glycosylation by a soluble HMW1C-like N-glycosyltransferase.Nature communications · 2023Article
- Rewiring the pneumococcal capsule pathway for investigating glycosyltransferase specificity and genetic glycoengineering.Science advances · 2023Article
- Article
- A Cell-Free Protein Synthesis Platform to Produce a Clinically Relevant Allergen Panel.ACS synthetic biology · 2023Article
- A rapid cell-free expression and screening platform for antibody discovery.Nature communications · 2023Article
- Rapid biosynthesis of glycoprotein therapeutics and vaccines from freeze-dried bacterial cell lysates.Nature protocols · 2023Review
- GlycoCAP: A Cell-Free, Bacterial Glycosylation Platform for Building Clickable Azido-Sialoglycoproteins.ACS synthetic biology · 2023Article
11 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycosylation is an abundant post-translational modification that is important in disease and biotechnology. Current methods to understand and engineer glycosylation cannot sufficiently explore the vast experimental landscapes required to accurately predict and design glycosylation sites modified by glycosyltransferases. Here we describe a systematic platform for glycosylation sequence characterization and optimization by rapid expression and screening (GlycoSCORES), which combines cell-free protein synthesis and mass spectrometry of self-assembled monolayers. We produced six N- and O-linked polypeptide-modifying glycosyltransferases from bacteria and humans in vitro and rigorously determined their substrate specificities using 3,480 unique peptides and 13,903 unique reaction conditions. We then used GlycoSCORES to optimize and design small glycosylation sequence motifs that directed efficient N-linked glycosylation in vitro and in the Escherichia coli cytoplasm for three heterologous proteins, including the human immunoglobulin Fc domain. We find that GlycoSCORES is a broadly applicable method to facilitate fundamental understanding of glycosyltransferases and engineer synthetic glycoproteins.
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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.