<HashMap><database>iProX</database><scores/><additional><omics_type>Proteomics</omics_type><submitter>Hongqiang Qin</submitter><species>Homo Sapiens</species><full_dataset_link>http://www.iprox.org/page/project.html?id=IPX0018767000</full_dataset_link><submitter_email>qinhq@dlut.edu.cn</submitter_email><submitter_affiliation>Dalian University of Technology</submitter_affiliation><sample_protocol></sample_protocol><repository>iProX</repository><data_protocol></data_protocol></additional><is_claimable>false</is_claimable><name>Integrated N- and O-glycoproteomics reveals site-specific glycosylation dysregulation in Alzheimer's disease</name><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.</description><dates><publication>Sat Aug 01 00:00:00 GMT+01:00 2026</publication></dates><accession>PXD082052</accession><cross_references><TAXONOMY>9606</TAXONOMY></cross_references></HashMap>