ArticleJournal of the American Society for Mass Spectrometry2015
Mass spectrometric analysis of the cell surface N-glycoproteome by combining metabolic labeling and click chemistry.
Article in Journal of the American Society for Mass Spectrometry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 48 citations in OpenAlex.
- 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
- Mapping the cancer surface proteome in search of target antigens for immunotherapy.Molecular therapy : the journal of the American Society of Gene Therapy · 2024Review
- Deciphering the Properties and Functions of Glycoproteins Using Quantitative Proteomics.Journal of proteome research · 2023Review
- Systematic characterization of extracellular glycoproteins using mass spectrometry.Mass spectrometry reviews · 2023Review
- Time-Resolved and Comprehensive Analysis of Surface Glycoproteins Reveals Distinct Responses of Monocytes and Macrophages to Bacterial Infection.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021Article
- Time-Resolved and Comprehensive Analysis of Surface Glycoproteins Reveals Distinct Responses of Monocytes and Macrophages to Bacterial Infection.Angewandte Chemie (International ed. in English) · 2021Article
- Design and Synthesis of Metabolic Chemical Reporters for the Visualization and Identification of Glycoproteins.RSC chemical biology · 2021Article
- Enhancing Comprehensive Analysis of Secreted Glycoproteins from Cultured Cells without Serum Starvation.Analytical chemistry · 2021Article
- A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry-Based Glycoproteomics.Molecular & cellular proteomics : MCP · 2021Review
- CIRFESS: An Interactive Resource for Querying the Set of Theoretically Detectable Peptides for Cell Surface and Extracellular Enrichment Proteomic Studies.Journal of the American Society for Mass Spectrometry · 2020Article
- Systematic quantification of the dynamics of newly synthesized proteins unveiling their degradation pathways in human cells.Chemical science · 2020Article
- Recent Advances in Glycoproteomic Analysis by Mass Spectrometry.Analytical chemistry · 2020Review
- Global and site-specific analysis of protein glycosylation in complex biological systems with Mass Spectrometry.Mass spectrometry reviews · 2019Review
- Mapping human N-linked glycoproteins and glycosylation sites using mass spectrometry.Trends in analytical chemistry : TRAC · 2019Article
- Enzymatic Tagging of Glycoproteins on the Cell Surface for Their Global and Site-Specific Analysis with Mass Spectrometry.Analytical chemistry · 2019Article
- Article
- Systematic and site-specific analysis of N-glycoproteins on the cell surface by integrating bioorthogonal chemistry and MS-based proteomics.Methods in enzymology · 2019Article
- Mass Spectrometry Approaches to Glycomic and Glycoproteomic Analyses.Chemical reviews · 2018Review
- Mass Spectrometry-Based Chemical and Enzymatic Methods for Global Analysis of Protein Glycosylation.Accounts of chemical research · 2018Review
- Membrane glycomics reveal heterogeneity and quantitative distribution of cell surface sialylation.Chemical science · 2018Article
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
No grant is acknowledged in the PubMed record.
Abstract
Cell surface N-glycoproteins play extraordinarily important roles in cell-cell communication, cell-matrix interactions, and cellular response to environmental cues. Global analysis is exceptionally challenging because many N-glycoproteins are present at low abundances and effective separation is difficult to achieve. Here, we have developed a novel strategy integrating metabolic labeling, copper-free click chemistry, and mass spectrometry (MS)-based proteomics methods to analyze cell surface N-glycoproteins comprehensively and site-specifically. A sugar analog containing an azido group, N-azidoacetylgalactosamine, was fed to cells to label glycoproteins. Glycoproteins with the functional group on the cell surface were then bound to dibenzocyclooctyne-sulfo-biotin via copper-free click chemistry under physiological conditions. After protein extraction and digestion, glycopeptides with the biotin tag were enriched by NeutrAvidin conjugated beads. Enriched glycopeptides were deglycosylated with peptide-N-glycosidase F in heavy-oxygen water, and in the process of glycan removal, asparagine was converted to aspartic acid and tagged with 18O for MS analysis. With this strategy, 144 unique N-glycopeptides containing 152 N-glycosylation sites were identified in 110 proteins in HEK293T cells. As expected, 95% of identified glycoproteins were membrane proteins, which were highly enriched. Many sites were located on important receptors, transporters, and cluster of differentiation proteins. The experimental results demonstrated that the current method is very effective for the comprehensive and site-specific identification of the cell surface N-glycoproteome and can be extensively applied to other cell surface protein studies.
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.