ArticleNature2017
Comparative glycoproteomics of stem cells identifies new players in ricin toxicity.
Article in Nature, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers, 1 of them a synthesis that pooled it.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
61 citing papers in PubMed, 1 synthesis or guideline pooled it, 165 citations in OpenAlex.
- Recent Advances in Software Tools for More Generic and Precise Intact Glycopeptide Analysis.Molecular & cellular proteomics : MCP · 2021Pooled it
- Article
- Tumor sialylation regulates G-CSF stability and promotes neutrophil-mediated immunosuppression in breast cancer.Nature communications · 2026Article
- Ultradeep N-glycoproteome atlas of mouse reveals spatiotemporal signatures of brain aging and neurodegenerative diseases.Nature communications · 2025Article
- Uncovering protein glycosylation dynamics and heterogeneity using deep quantitative glycoprofiling (DQGlyco).Nature structural & molecular biology · 2025Article
- Inter-tissue glycan heterogeneity: site-specific glycoform analysis of mouse tissue N-glycoproteomes using MS1-based glycopeptide detection method assisted by lectin microarray.Analytical and bioanalytical chemistry · 2025Article
- Improving Glycoproteomic Analysis Workflow by Systematic Evaluation of Glycopeptide Enrichment, Quantification, Mass Spectrometry Approach, and Data Analysis Strategies.Analytical chemistry · 2024Article
- Deciphering fucosylated protein-linked O-glycans in oral Tannerella serpentiformis: Insights from NMR spectroscopy and glycoproteomics.Glycobiology · 2024Article
- Uncovering missing glycans and unexpected fragments with pGlycoNovo for site-specific glycosylation analysis across species.Nature communications · 2024Article
- Article
- Article
- Deciphering the Properties and Functions of Glycoproteins Using Quantitative Proteomics.Journal of proteome research · 2023Review
- Identification of indocyanine green as a STT3B inhibitor against mushroom α-amanitin cytotoxicity.Nature communications · 2023Article
- A whole-genome scan for Artemisinin cytotoxicity reveals a novel therapy for human brain tumors.EMBO molecular medicine · 2023Article
- High-throughput site-specificNational science review · 2023Article
- pGlycoQuant with a deep residual network for quantitative glycoproteomics at intact glycopeptide level.Nature communications · 2022Article
- High-Throughput Glycomic Methods.Chemical reviews · 2022Review
- Targeting glycans for CAR therapy: The advent of sweet CARs.Molecular therapy : the journal of the American Society of Gene Therapy · 2022Review
- Glyco-Decipher enables glycan database-independent peptide matching and in-depth characterization of site-specific N-glycosylation.Nature communications · 2022Article
- TMT-Based Multiplexed Quantitation ofACS omega · 2022Article
1 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
Glycosylation, the covalent attachment of carbohydrate structures onto proteins, is the most abundant post-translational modification. Over 50% of human proteins are glycosylated, which alters their activities in diverse fundamental biological processes. Despite the importance of glycosylation in biology, the identification and functional validation of complex glycoproteins has remained largely unexplored. Here we develop a novel quantitative approach to identify intact glycopeptides from comparative proteomic data sets, allowing us not only to infer complex glycan structures but also to directly map them to sites within the associated proteins at the proteome scale. We apply this method to human and mouse embryonic stem cells to illuminate the stem cell glycoproteome. This analysis nearly doubles the number of experimentally confirmed glycoproteins, identifies previously unknown glycosylation sites and multiple glycosylated stemness factors, and uncovers evolutionarily conserved as well as species-specific glycoproteins in embryonic stem cells. The specificity of our method is confirmed using sister stem cells carrying repairable mutations in enzymes required for fucosylation, Fut9 and Slc35c1. Ablation of fucosylation confers resistance to the bioweapon ricin, and we discover proteins that carry a fucosylation-dependent sugar code for ricin toxicity. Mutations disrupting a subset of these proteins render cells ricin resistant, revealing new players that orchestrate ricin toxicity. Our comparative glycoproteomics platform, SugarQb, enables genome-wide insights into protein glycosylation and glycan modifications in complex biological systems.
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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.