{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lih TM"],"funding":["NCI NIH HHS"],"pagination":["112409"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10247542"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["42(5)"],"pubmed_abstract":["Clear cell renal cell carcinoma (ccRCC), a common form of RCC, is responsible for the high mortality rate of kidney cancer. Dysregulations of glycoproteins have been shown to associate with ccRCC. However, the molecular mechanism has not been well characterized. Here, a comprehensive glycoproteomic analysis is conducted using 103 tumors and 80 paired normal adjacent tissues. Altered glycosylation enzymes and corresponding protein glycosylation are observed, while two of the major ccRCC mutations, BAP1 and PBRM1, show distinct glycosylation profiles. Additionally, inter-tumor heterogeneity and cross-correlation between glycosylation and phosphorylation are observed. The relation of glycoproteomic features to genomic, transcriptomic, proteomic, and phosphoproteomic changes shows the role of "],"journal":["Cell reports"],"pubmed_title":["Integrated glycoproteomic characterization of clear cell renal cell carcinoma."],"pmcid":["PMC10247542"],"funding_grant_id":["U24 CA210985","U24 CA271079"],"pubmed_authors":["Hu Y","Zhang H","Lih TM","Schnaubelt M","Cho KC"],"additional_accession":[]},"is_claimable":false,"name":"Integrated glycoproteomic characterization of clear cell renal cell carcinoma.","description":"Clear cell renal cell carcinoma (ccRCC), a common form of RCC, is responsible for the high mortality rate of kidney cancer. Dysregulations of glycoproteins have been shown to associate with ccRCC. However, the molecular mechanism has not been well characterized. Here, a comprehensive glycoproteomic analysis is conducted using 103 tumors and 80 paired normal adjacent tissues. Altered glycosylation enzymes and corresponding protein glycosylation are observed, while two of the major ccRCC mutations, BAP1 and PBRM1, show distinct glycosylation profiles. Additionally, inter-tumor heterogeneity and cross-correlation between glycosylation and phosphorylation are observed. The relation of glycoproteomic features to genomic, transcriptomic, proteomic, and phosphoproteomic changes shows the role of ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 May","modification":"2025-04-19T08:10:29.966Z","creation":"2025-04-19T08:10:29.966Z"},"accession":"S-EPMC10247542","cross_references":{"pubmed":["37074911"],"doi":["10.1016/j.celrep.2023.112409"]}}