{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Dapeng Li"],"species":["Homo Sapiens"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0012727000"],"submitter_email":["dpli@scu.edu.cn"],"submitter_affiliation":["Sichuan University"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"additional_accession":[]},"is_claimable":false,"name":"Serum N-Glycoproteome Mapping Reveals Glycosite and Glycan Signatures in Type 2 Diabetes Mellitus Complicated with Coronary Heart Disease","description":"This study investigated the glycoproteomic alterations associated with the development of CHD in patients with T2DM, with a particular focus on dual-layer changes in N-glycosylation sites (N-glycosites) and intact N-glycopeptides. Serum samples were analyzed using a hydrophilic interaction liquid chromatography (HILIC)-based MS method to perform comprehensive glycoproteomic profiling at both the site-specific glycopeptide and intact N-glycopeptide levels. This approach enabled the simultaneous identification of glycosylation sites and their attached glycan structures, offering high-resolution insights into glycan heterogeneity across glycoproteins. These findings advance our understanding of the molecular mechanisms underlying T2DM&CHD and show the promising value of glycoproteomics for identifying disease-specific biomarkers.","dates":{"publication":"Thu Jul 24 00:00:00 BST 2025"},"accession":"PXD066505","cross_references":{"TAXONOMY":["9606"]}}