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Circulating biomarkers play important roles in diagnosis of malignant tumors. N-glycosylation is an important post-translation patter and obviously affect biological behaviors of malignant tumor cells. However, the role of N-glycosylation sites in early diagnosis of tumors still remains further inve...
ORGANISM(S): Homo sapiens (Human) 
2023-03-11 | PXD036198 | Pride
Protein N-glycosylation plays a crucial role in the human liver, impacting key functions like hepatocyte lipid metabolism hepatocyte apoptosis, and inflammatory response. Despite its significance, the site-specific N-glycosylation patterns and their variations of liver biosy samples between healthy ...
ORGANISM(S): Homo Sapiens 
2024-07-04 | PXD053626 |
We performed quantitative chemical proteomics to identify more than 800 N-homocysteinylated proteins as well as 304 N-homocysteinylated sites directly from HTL-treated HeLa cells.
ORGANISM(S): Homo Sapiens 
2024-10-09 | PXD056640 |
This dataset reports a comprehensive N-glycoproteomic profiling of serum-derived humanized antibodies expressed in transgenic mice using an intact glycopeptide (IGP)–based LC–MS/MS workflow. The study aimed to identify and characterize site-specific N-glycosylation modifications of mouse serum prote...
ORGANISM(S): Mus musculus (Mouse) 
2025-12-08 | PXD070488 | Pride
N-glycosylation protein modifications play a crucial regulatory role in numerous biological processes, although their contribution to male reproduction in mammals remains largely undefined. Here, we found that Ribophorin I (RPN1), a subunit of oligosaccharyltransferase complex, is indispensable for ...
ORGANISM(S): Mus musculus (Mouse) 
2025-05-06 | PXD051379 | Pride
Protein N-phosphorylation enrichment is faced with great difficulties due to the intrinsic instability of the N-P bond, which has seriously hindered its biological function unraveling. Current methods for N-phosphopeptides enrichment are challenging to fulfil high selectivity for all types of N-phos...
ORGANISM(S): Homo Sapiens Escherichia Coli Mus Musculus 
2024-12-12 | PXD058797 |
N-glycosylation protein modification plays a crucial regulatory role in numerous biological processes, although their contribution to male reproduction in mammals remains largely undefined. Here, we found that Ribophorin I (RPN1), a subunit of oligosaccharyltransferase complex, is indispensable for ...
ORGANISM(S): Mus musculus (Mouse) 
2025-05-07 | PXD056290 | Pride
We aimed to in-depth characterize and quantify salivary N-glycoproteomics. HILIC enrichment and LC-MS/MS were combined to investigate salivary glycosylation both at deglycopeptides level and glycopepeptides level, and alterations in site-specific glycoforms for human saliva were detected between lun...
ORGANISM(S): Homo sapiens (Human) 
2023-02-08 | PXD030670 | Pride
Glycosylation is largely involved in development and progression of cancer and provides multiple novel targets for diagnostic application and therapeutic strategies. Recent advances in methods for enrichment and mass spectrometric interpreting of intact N-glycoprotein contribute to large-scale clini...
ORGANISM(S): Homo sapiens (Human) 
2025-06-16 | PXD055957 | Pride
The current depth of site-specific N-glycoproteomics is insufficient to fully characterize glycosylation events in biological samples. Herein, we achieved an ultradeep and precision analysis of the N-glycoproteome of mouse tissues by integrating multiple workflows. The largest N-glycoproteomic datas...
ORGANISM(S): Mus Musculus 
2025-03-04 | PXD061436 |
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