ArticleNature communications2018
Direct quality control of glycoengineered erythropoietin variants.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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
42 citing papers in PubMed.
- Rapid quantitation of erythropoietin and identification of its glycans using membranes for capture and digestion.Talanta · 2026Article
- Unveiling the Accurate Site-SpecificAnalytical chemistry · 2025Article
- Intestinal mucus: the unsung hero in the battle against viral gastroenteritis.Gut pathogens · 2025Review
- AsymmetricJournal of the American Chemical Society · 2024Article
- Mammalian cell-based production of glycans, glycopeptides and glycomodules.Nature communications · 2024Article
- Full-length single-molecule protein fingerprinting.Nature nanotechnology · 2024Article
- Exposing the molecular heterogeneity of glycosylated biotherapeutics.Nature communications · 2024Article
- Proteoform-Resolved Profiling of Plasminogen Activation Reveals Novel Abundant Phosphorylation Site and Primary N-Terminal Cleavage Site.Molecular & cellular proteomics : MCP · 2024Article
- Uncovering the Role ofJournal of the American Chemical Society · 2023Article
- A universal GlycoDesign for lysosomal replacement enzymes to improve circulation time and biodistribution.Frontiers in bioengineering and biotechnology · 2023Article
- Native Top-Down Mass Spectrometry Reveals a Role for Interfacial Glycans on Therapeutic Cytokine and Hormone Assemblies.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- Native Top-Down Mass Spectrometry Reveals a Role for Interfacial Glycans on Therapeutic Cytokine and Hormone Assemblies.Angewandte Chemie (International ed. in English) · 2022Article
- Charting the Proteoform Landscape of Serum Proteins in Individual Donors by High-Resolution Native Mass Spectrometry.Analytical chemistry · 2022Article
- An etanercept O-glycovariant with enhanced potency.Molecular therapy. Methods & clinical development · 2022Article
- Approaches to Heterogeneity in Native Mass Spectrometry.Chemical reviews · 2022Review
- High-Resolution Native Mass Spectrometry.Chemical reviews · 2022Review
- Exploring the glycosylation of mucins by use of O-glycodomain reporters recombinantly expressed in glycoengineered HEK293 cells.The Journal of biological chemistry · 2022Article
- Review
- Cellular and Molecular Engineering of Glycan Sialylation in Heterologous Systems.Molecules (Basel, Switzerland) · 2021Review
- The lysosomal endopeptidases Cathepsin D and L are selective and effective proteases for the middle-down characterization of antibodies.The FEBS journal · 2021Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Recombinant production of glycoprotein therapeutics like erythropoietin (EPO) in mammalian CHO cells rely on the heterogeneous N-glycosylation capacity of the cell. Recently, approaches for engineering the glycosylation capacities of mammalian cells for custom designed glycoforms have been developed. With these opportunities there is an increasing need for fast, sensitive, and global analysis of the glycoproteoform landscape produced to evaluate homogeneity and consistency. Here we use high-resolution native mass spectrometry to measure the glycoproteoform profile of 24 glycoengineered variants of EPO. Based on the unique mass and intensity profiles of each variant, we classify them according to similarities in glycosylation profiles. The classification distinguishes EPO variants with varying levels of glycan branchingand sialylation, which are crucial parameters in biotherapeutic efficacy. We propose that our methods could be of great benefit in the characterization of other glycosylated biopharmaceuticals, ranging from the initial clonal selection to batch-to-batch controls, and the assessment of similarity between biosimilar/biobetter products.
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