{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Li J"],"funding":["National Natural Science Foundation of China","China Postdoctoral Science Foundation","National Key Research and Development Program of China"],"pagination":["2135-2152"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9168967"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(11)"],"pubmed_abstract":["Primary liver cancer, mainly comprising hepatocellular carcinoma (HCC) and intrahepatic cholangiocarcinoma (ICC), remains a major global health problem. Although ICC is clinically different from HCC, their molecular differences are still largely unclear. In this study, precision N-glycoproteomic analysis was performed on both ICC and HCC tumors as well as paracancer tissues to investigate their aberrant site-specific N-glycosylation. By using our newly developed glycoproteomic methods and novel algorithm, termed 'StrucGP', a total of 486 N-glycan structures attached on 1235 glycosites were identified from 894 glycoproteins in ICC and HCC tumors. Notably, glycans with uncommon LacdiNAc (GalNAcβ1-4GlcNAc) structures were distinguished from their isomeric glycans. In addition to several bi-an"],"journal":["Molecular oncology"],"pubmed_title":["Precision N-glycoproteomics reveals elevated LacdiNAc as a novel signature of intrahepatic cholangiocarcinoma."],"pmcid":["PMC9168967"],"funding_grant_id":["91853123","81773180","2019TQ0260","2019M663798","21705127","81800655","32101192","2019YFA09005200"],"pubmed_authors":["Dang L","Li J","Shen J","Ma C","Sun S","Mu F","Zhao T","Hu L","Zhu B","Liu D","Jia L"],"additional_accession":[]},"is_claimable":false,"name":"Precision N-glycoproteomics reveals elevated LacdiNAc as a novel signature of intrahepatic cholangiocarcinoma.","description":"Primary liver cancer, mainly comprising hepatocellular carcinoma (HCC) and intrahepatic cholangiocarcinoma (ICC), remains a major global health problem. Although ICC is clinically different from HCC, their molecular differences are still largely unclear. In this study, precision N-glycoproteomic analysis was performed on both ICC and HCC tumors as well as paracancer tissues to investigate their aberrant site-specific N-glycosylation. By using our newly developed glycoproteomic methods and novel algorithm, termed 'StrucGP', a total of 486 N-glycan structures attached on 1235 glycosites were identified from 894 glycoproteins in ICC and HCC tumors. Notably, glycans with uncommon LacdiNAc (GalNAcβ1-4GlcNAc) structures were distinguished from their isomeric glycans. In addition to several bi-an","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jun","modification":"2025-04-03T22:37:29.212Z","creation":"2025-04-03T22:37:29.212Z"},"accession":"S-EPMC9168967","cross_references":{"pubmed":["34855283"],"doi":["10.1002/1878-0261.13147"]}}