ArticleAngewandte Chemie (International ed. in English)2017
Specific Identification of Glycoproteins Bearing the Tn Antigen in Human Cells.
Article in Angewandte Chemie (International ed. in English), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
39 citing papers in PubMed, 58 citations in OpenAlex.
- Systematic Quantification of Protein O-GlcNAcylation Reveals Common and Cell-Type-Specific Responses to N-Glycosylation Inhibition in Human Cells.Analytical chemistry · 2026Article
- Mass Spectrometry-Based Proteomics Methods for Systematic Identification and Quantification of Protein O-Glycosylation in Complex Biological Samples.Journal of the American Society for Mass Spectrometry · 2026Review
- Breast cancer immunotherapy: mechanisms of immune evasion, biomarkers, and emerging therapeutic strategies.Molecular cancer · 2026Review
- A Chemoenzymatic Labeling Strategy for Site-Specific Analysis of Tumor-Associated Sialyl Thomsen-Friedenreich Antigen.JACS Au · 2026Article
- Asialoglycoprotein receptor 1: a multifaceted receptor in the liver and cardiovascular system.Frontiers in medicine · 2025Review
- MOTAI: A Novel Method for the Study of O-GalNAcylation and Complex O-Glycosylation in Cancer.Analytical chemistry · 2024Article
- Mass Spectrometry Strategies forCells · 2024Review
- Systematic analysis of the impact of phosphorylation and O-GlcNAcylation on protein subcellular localization.Cell reports · 2023Article
- Review
- Systematic characterization of extracellular glycoproteins using mass spectrometry.Mass spectrometry reviews · 2023Review
- Glycomimetic Peptides as Therapeutic Tools.Pharmaceutics · 2023Review
- Recombinant mucin biotechnology and engineering.Advanced drug delivery reviews · 2023Review
- Recent development of analytical methods for disease-specific proteinRSC advances · 2022Review
- Synthesis of Azido-Globo H Analogs for Immunogenicity Evaluation.ACS central science · 2022Article
- Cancer glycomics offers potential biomarkers and therapeutic targets in the framework of 3P medicine.Frontiers in endocrinology · 2022Review
- [Recent advances in glycopeptide enrichment and mass spectrometry data interpretation approaches for glycoproteomics analyses].Se pu = Chinese journal of chromatography · 2021Review
- Putting the pieces together: mapping the O-glycoproteome.Current opinion in biotechnology · 2021Review
- Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-SpecificInternational journal of molecular sciences · 2021Article
- Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021Review
- Unraveling the surface glycoprotein interaction network by integrating chemical crosslinking with MS-based proteomics.Chemical science · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Glycoproteins contain a wealth of valuable information regarding the development and disease status of cells. In cancer cells, some glycans (such as the Tn antigen) are highly up-regulated, but this remains largely unknown for glycoproteins with a particular glycan. Herein, an innovative method combining enzymatic and chemical reactions was first designed to enrich glycoproteins with the Tn antigen. Using synthetic glycopeptides with O-GalNAc (the Tn antigen) or O-GlcNAc, we demonstrated that the method is selective for glycopeptides with O-GalNAc and can distinguish between these two modifications. The diagnostic ions from the tagged O-GalNAc further confirmed the effectiveness of the method and confidence in the identification of glycopeptides with the Tn antigen by mass spectrometry. Using this method, we identified 96 glycoproteins with the Tn antigen in Jurkat cells. The method can be extensively applied in biological and biomedical research.
Indexed as
Identifiers
What 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.