ArticleNature chemical biology2023
A high-throughput screening platform for enzymes active on mucin-type O-glycoproteins.
Article in Nature chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The trial behind it
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
10 citing papers in PubMed.
- Functional conservation of divergent peptidase_M60 O-glycopeptidases in enterococcus.Glycobiology · 2026Article
- Glycoengineering strategies for constructing defined Mucin O-glycans.Frontiers in molecular biosciences · 2026Review
- Mucinase fromFrontiers in microbiology · 2026Article
- A gasdermin-based life-death evolution system for reprogramming protease specificity.Nature chemical biology · 2026Article
- Reshaping of a Glycoside Hydrolase Active Site through Expression-Compensated Droplet-Based Microfluidic Screening Provides Useful Tools for Glycomics.ACS central science · 2025Article
- A Bacteroides thetaiotaomicron genetic locus encodes activities consistent with mucin O-glycoprotein processing and N-acetylgalactosamine metabolism.Nature communications · 2025Article
- Recent advances in recombinant production of soluble proteins in E. coli.Microbial cell factories · 2025Review
- UnravelingAnalytical chemistry · 2024Article
- Carbohydrate-active enzyme (CAZyme) discovery and engineeringRSC chemical biology · 2024Review
- Recent Advances in Fluorescent Probes for Cancer Biomarker Detection.Molecules (Basel, Switzerland) · 2024Review
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Mucin-type O-glycosylation is a post-translational modification present at the interface between cells where it has important roles in cellular communication. However, deciphering the function of O-glycoproteins and O-glycans can be challenging, especially as few enzymes are available for their assembly or selective degradation. Here, to address this deficiency, we developed a genetically encoded screening methodology for the discovery and engineering of the diverse classes of enzymes that act on O-glycoproteins. The method uses Escherichia coli that have been engineered to produce an O-glycosylated fluorescence resonance energy transfer probe that can be used to screen for O-glycopeptidase activity. Subsequent cleavage of the substrate by O-glycopeptidases provides a read-out of the glycosylation state of the probe, allowing the method to also be used to assay glycosidases and glycosyltransferases. We further show the potential of this methodology in the first ultrahigh-throughput-directed evolution of an O-glycopeptidase.
Indexed as
Identifiers
37592157What OpenQuestion holds
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.