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In this study, we employed artificial intelligence to address the challenges in identifying core fucose due to migration effects. By knocking out the FUT8 gene in normal mouse brains, we ensured accurate labeling of non-core fucosylated glycans, enabling the identification of mannose glycans with co...
ORGANISM(S): Mus musculus (Mouse) 
2025-09-29 | PXD062880 | Pride
N-Linked glycoprotein is a highly interesting class of proteins for clinical and biological research. The large-scale characterization of N-linked glycoproteins accomplished by mass spectrometry-based glycoproteomics has provided valuable insights into the interdependence of glycoprotein structure a...
ORGANISM(S): Homo sapiens (Human) 
2022-02-23 | PXD005232 | Pride
In this study, we applied the recently developed software, StrucGP to large-scale characterize glycoproteins, and IGPs, as well as precise site-specific glycan structures in human spermatozoa. Furthermore, bioinformatical analyses were conducted to systematically describe the potential functions of ...
ORGANISM(S): Homo sapiens (Human) 
2022-05-19 | PXD026649 | Pride
Spike (S) protein plays a key role in COVID-19 (SARS-CoV-2) infection and host-cell entry. Previous studies have systematically analyzed site-specific glycans compositions of S protein. Here, we further provide structure-clear N-glycosylation of S protein at site-specific level by using our recently...
ORGANISM(S): Homo sapiens (Human) 
2022-10-13 | PXD034086 | Pride
N-Linked glycoprotein is a highly interesting class of proteins for clinical and biological research. The large-scale characterization of N-linked glycoproteins accomplished by mass spectrometry-based glycoproteomics has provided valuable insights into the interdependence of glycoprotein structure a...
ORGANISM(S): Homo sapiens (Human) 
2019-11-08 | PXD005143 | Pride
N-linked glycoproteins are known to be important for spermatozoa development and gametes fusion. However, little is known about detailed information of these glycoproteins, particularly the glycosylation sites and its corresponding glycan structures in human spermatozoa. In present study, an in hous...
ORGANISM(S): Homo sapiens (Human) 
2023-03-04 | PXD020286 | 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
This study is aimed to comprehensively and globally characterize seminal plasma glycoproteins in a site-specific manner with information of N-glycosites and corresponding glycan structures, as well as glycan isomers using mass spectrometry. Furthermore, the function of specific glycan structures is ...
ORGANISM(S): Homo sapiens (Human) 
2023-03-04 | PXD030804 | Pride
In this work, we investigate the differences of site-specific N-glycosylation between young (2-month-old) and middle-aged (12-month-old) mouse ovarian tissues by integrating N-glycoproteomics and proteomic approaches with tandem mass tag (TMT) labeling.To identify signalling pathways associated with...
ORGANISM(S): Mus Musculus 
In this study, we employed StrucGP to generate the first high-resolution and site-specific N- glycoproteomic atlas across 24 diverse mouse tissues. This comprehensive dataset provides an unprecedented insight into the tissue-specific landscape of N-glycosylation, revealing how distinct glycan struct...
ORGANISM(S): Mus Musculus 
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