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We developed an automated glycopeptide enrichment method for the analysis of serum site-specific N-glycoproteome. This automated method allowed for processing one sample within 20 min. It showed higher enrichment specificity, more intact glycopeptide identifications, and better quantitative reproduc...
ORGANISM(S): Homo Sapiens (human) 
The heterogeneity and low abundance of protein glycosylation present challenging barriers to the analysis of intact glycopeptides, which is key to comprehensively understanding the role of glycosylation in an organism. Efficient and specific enrichment of intact glycopeptides could help greatly with...
ORGANISM(S): Human 
2021-04-28 | MSV000087324 | MassIVE
In this study, we conducted a systematic investigation into a glycoproteomic workflow. Firstly, Label-free and TMT labeling strategies were utilized for intact N-glycopeptide quantification. A total of 2,924 unique intact N-glycopeptides can be quantified after being labeled using TMT approach. Comp...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2025-05-07 | PXD054874 | Pride
This study introduced the use of cotton in 200µL tips, namely cotton HILIC as a convenient tool for enriching large-scale glycopeptides before MS analysis in this study. The optimal loading buffer for cotton HILIC was investigated by using mouse brain as a complex test sample. Subsequently, the perf...
ORGANISM(S): Mus musculus (Mouse) 
2023-03-04 | PXD035078 | Pride
In this work, we developed a glycocarrier strategy to amplify MS signals with isobaric labeling for highly sensitive intact N-glycopeptide characterization from single and small numbers of cells without enrichment. Successful application in cell lines and microglia from the regional mouse brain demo...
ORGANISM(S): Homo Sapiens Mus Musculus 
2022-11-18 | PXD038212 |
Large-scale identification of N-linked intact glycopeptides by liquid chromatography coupled tandem mass spectrometry (LC-MS/MS) in human serum is challenging due to the wide dynamic range of serum protein abundances, the lack of a complete serum N-Glycan database and the existence of non-specifical...
ORGANISM(S): Armoracia rusticana Homo sapiens (Human) Gallus gallus (Chicken) 
2020-04-21 | PXD015622 | Pride
Heterogeneity of protein glycosylation poses great challenge for analysis that is key to un-puzzle systems glycobiology in diseases. Resolving this conundrum requires global enrichment of glycopeptides for identification and quantitation. To this aim, hydrophilic interaction chromatography (HILIC) h...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2018-07-02 | MSV000082566 | MassIVE
A fully automated HILIC-based enrichment and separation system for glycopeptide (AutoGP), which needs no sample collection, was developed in this study.
ORGANISM(S): Mus musculus (Mouse) 
2024-05-06 | PXD050391 | Pride
Mass spectrometry is the premier tool for identifying and quantifying site-specific protein glycosylation globally. Analysis of intact glycopeptides often requires an enrichment step, after which the samples remain highly complex and exhibit a broad dynamic range of abundance. Here, we evaluated th...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD038673 | Pride
Heterogeneity of protein glycosylation poses great challenge for analysis that is key to un-puzzle systems glycobiology in diseases. Resolving this conundrum requires global enrichment of glycopeptides for identification and quantitation. To this aim, hydrophilic interaction chromatography (HILIC) h...
ORGANISM(S): Homo sapiens (Human) 
2017-10-19 | PXD005145 | Pride
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