{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Hongqiang Qin"],"species":["Homo Sapiens"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0018767000"],"submitter_email":["qinhq@dlut.edu.cn"],"submitter_affiliation":["Dalian University of Technology"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"additional_accession":[]},"is_claimable":false,"name":"Integrated N- and O-glycoproteomics reveals site-specific glycosylation dysregulation in Alzheimer's disease","description":"This study performed integrated intact N- and O-glycoproteomic profiling of human serum from normal controls (n=10), patients with mild cognitive impairment (MCI, n=10), and patients with Alzheimer's disease (AD, n=9). A total of 2,433 intact N-glycopeptides and 3,864 intact O-glycopeptides were identified, providing a site-resolved view of systemic glycosylation changes during disease progression. Quantitative analysis revealed distinct remodeling patterns for N- and O-glycosylation, with early reduction of IGHG1 Asn180 N-glycoforms at MCI stage and progressive increase of APOE O-glycoforms from control to MCI and AD.","dates":{"publication":"Sat Aug 01 00:00:00 GMT+01:00 2026"},"accession":"PXD082052","cross_references":{"TAXONOMY":["9606"]}}