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N-glycoproteins are involved in various biological processes. More than one-third of plasma tumor protein biomarkers approved by the Food and Drug Administration (FDA) are glycoproteins which would enhance the specificity and/or sensitivity of cancer diagnosis. Therefore, the characterization of pla...
ORGANISM(S): Homo sapiens (Human) 
2022-08-12 | PXD030622 | Pride
Site-specific N-glycosylation characterization requires intact N-glycopeptide analysis based on suitable tandem mass spectrometry (MS/MS) method. Electron-transfer/higher-energy collisional dissociation (EThcD), stepped collision energy/higher-energy collisional dissociation (sceHCD), and higher-ene...
ORGANISM(S): Homo sapiens (Human) 
2022-04-04 | PXD030288 | Pride
Monoclonal immunoglobulin produced by clonal plasma cells is the main cause in multiple myeloma and monoclonal gammopathy of renal significance. Because of the complicated purification method and the low stoichiometry of purified protein and glycans, site-specific N-glycosylation characterization fo...
ORGANISM(S): Homo sapiens (Human) 
2022-09-13 | PXD035757 | Pride
Proteins glycosylation is primarily characterized as N-glycosylation or O-glycosylation. Recognition of the consensus N-glycosylation sequon (N-X-S/T/C) has enabled the mapping of the glycosite occupancy of intact glycopeptides, whereas O-glycosylation consensus sequons do not exit, making the chara...
ORGANISM(S): Homo sapiens (Human) 
2024-04-25 | PXD042701 | Pride
The envelope (Env) glycoprotein on the surface of human immunodeficiency virus type 1 (HIV-1) which decorated with a dense array of glycans is a determinant for viral invasion and host immune response of HIV-1 and a major target for a preventive HIV-1 vaccine. Improved vaccine design requires an und...
ORGANISM(S): Homo sapiens (Human) 
2021-11-03 | PXD025078 | Pride
Proteins are ubiquitously modified with glycans of varied chemical structures via distinct glycosidic linkages, making the landscape of protein glycosylation challenging to map. Profiling of intact glycopeptides with mass spectrometry (MS) has recently emerged as a powerful tool for revealing match...
ORGANISM(S): Mus musculus (Mouse) 
2025-02-12 | PXD039144 | Pride
Proteins are ubiquitously modified with glycans of varied chemical structures via distinct glycosidic linkages, making the landscape of protein glycosylation challenging to map. Profiling of intact glycopeptides with mass spectrometry (MS) has recently emerged as a powerful tool for revealing match...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) 
2025-02-12 | PXD036190 | Pride
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