{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T13:31:07Z","timestamp":1791984667175,"version":"4.4.0"},"reference-count":99,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2024,3,1]],"date-time":"2024-03-01T00:00:00Z","timestamp":1709251200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,3,1]],"date-time":"2024-03-01T00:00:00Z","timestamp":1709251200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,10,20]],"date-time":"2023-10-20T00:00:00Z","timestamp":1697760000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000054","name":"National Cancer Institute","doi-asserted-by":"publisher","award":["1R01 CA160254"],"award-info":[{"award-number":["1R01 CA160254"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000054","name":"National Cancer Institute","doi-asserted-by":"publisher","award":["U01 CA225753"],"award-info":[{"award-number":["U01 CA225753"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Acta Pharmaceutica Sinica B"],"published-print":{"date-parts":[[2024,3]]},"DOI":"10.1016\/j.apsb.2023.10.014","type":"journal-article","created":{"date-parts":[[2023,10,26]],"date-time":"2023-10-26T21:36:17Z","timestamp":1698356177000},"page":"1098-1110","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":127,"title":["The role of N-glycosylation in cancer"],"prefix":"10.1016","volume":"14","author":[{"given":"Yu","family":"Lin","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David M.","family":"Lubman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.apsb.2023.10.014_bib1","series-title":"World health organization","year":"2022"},{"key":"10.1016\/j.apsb.2023.10.014_bib2","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1021\/acschembio.8b00902","article-title":"Developing workflow for simultaneous analyses of phosphopeptides and glycopeptides","volume":"14","author":"Cho","year":"2019","journal-title":"ACS Chem Biol"},{"key":"10.1016\/j.apsb.2023.10.014_bib3","doi-asserted-by":"crossref","first-page":"1347","DOI":"10.1016\/j.bbagen.2011.12.001","article-title":"Glycans as cancer biomarkers","volume":"1820","author":"Adamczyk","year":"2012","journal-title":"Biochim Biophys Acta Gen Subj"},{"key":"10.1016\/j.apsb.2023.10.014_bib4","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.bbcan.2014.07.005","article-title":"Sweet escape: sialic acids in tumor immune evasion","volume":"1846","author":"B\u00fcll","year":"2014","journal-title":"Biochim Biophys Acta Rev Cancer"},{"key":"10.1016\/j.apsb.2023.10.014_bib5","doi-asserted-by":"crossref","first-page":"1102","DOI":"10.1038\/s41419-018-1101-0","article-title":"Sialyltransferase ST3GAL1 promotes cell migration, invasion, and TGF-\u03b21-induced EMT and confers paclitaxel resistance in ovarian cancer","volume":"9","author":"Wu","year":"2018","journal-title":"Cell Death Dis"},{"key":"10.1016\/j.apsb.2023.10.014_bib6","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1158\/0008-5472.CAN-10-1303","article-title":"A novel sialyltransferase inhibitor suppresses FAK\/paxillin signaling and cancer angiogenesis and metastasis pathways","volume":"71","author":"Chen","year":"2011","journal-title":"Cancer Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib7","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1002\/jcp.22068","article-title":"A novel sialyltransferase inhibitor AL10 suppresses invasion and metastasis of lung cancer cells by inhibiting integrin-mediated signaling","volume":"223","author":"Chiang","year":"2010","journal-title":"J Cell Physiol"},{"key":"10.1016\/j.apsb.2023.10.014_bib8","doi-asserted-by":"crossref","first-page":"4645","DOI":"10.1158\/0008-5472.CAN-04-3117","article-title":"Hypersialylation of \u03b21 integrins, observed in colon adenocarcinoma, may contribute to cancer progression by up-regulating cell motility","volume":"65","author":"Seales","year":"2005","journal-title":"Cancer Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib9","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/1757-2215-1-3","article-title":"ST6Gal-I expression in ovarian cancer cells promotes an invasive phenotype by\u00a0altering integrin glycosylation and function","volume":"1","author":"Christie","year":"2008","journal-title":"J Ovarian Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib10","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1038\/73163","article-title":"Suppression of tumor growth and metastasis in Mgat5-deficient mice","volume":"6","author":"Granovsky","year":"2000","journal-title":"Nat Med"},{"key":"10.1016\/j.apsb.2023.10.014_bib11","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1126\/science.2953071","article-title":"\u03b21-6 Branching of Asn-linked oligosaccharides is directly associated with metastasis","volume":"236","author":"Dennis","year":"1987","journal-title":"Science"},{"key":"10.1016\/j.apsb.2023.10.014_bib12","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1093\/glycob\/9.3.235","article-title":"Control of metastasis by Asn-linked, \u03b21\u20136 branched oligosaccharides in mouse mammary cancer cells","volume":"9","author":"Seberger","year":"1999","journal-title":"Glycobiology"},{"key":"10.1016\/j.apsb.2023.10.014_bib13","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1126\/science.1102109","article-title":"Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis","volume":"306","author":"Partridge","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.apsb.2023.10.014_bib14","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.cell.2007.01.049","article-title":"Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation","volume":"129","author":"Lau","year":"2007","journal-title":"Cell"},{"key":"10.1016\/j.apsb.2023.10.014_bib15","doi-asserted-by":"crossref","first-page":"3278","DOI":"10.1021\/acs.jproteome.1c00175","article-title":"A panel of glycopeptides as candidate biomarkers for early diagnosis of NASH hepatocellular carcinoma using a stepped HCD method and PRM evaluation","volume":"20","author":"Lin","year":"2021","journal-title":"J Proteome Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib16","doi-asserted-by":"crossref","first-page":"818001","DOI":"10.3389\/fonc.2022.818001","article-title":"A fucosylated glycopeptide as a candidate biomarker for early diagnosis of NASH hepatocellular carcinoma using a stepped HCD method and PRM evaluation","volume":"12","author":"Lin","year":"2022","journal-title":"Front Oncol"},{"key":"10.1016\/j.apsb.2023.10.014_bib17","doi-asserted-by":"crossref","first-page":"630","DOI":"10.1073\/pnas.1220425110","article-title":"Fucosyltransferase 8 as a functional regulator of nonsmall cell lung cancer","volume":"110","author":"Chen","year":"2013","journal-title":"Proc Natl Acad Sci U\u00a0S\u00a0A"},{"key":"10.1016\/j.apsb.2023.10.014_bib18","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1016\/j.cell.2010.06.011","article-title":"Cell signaling by receptor tyrosine kinases","volume":"141","author":"Lemmon","year":"2010","journal-title":"Cell"},{"key":"10.1016\/j.apsb.2023.10.014_bib19","doi-asserted-by":"crossref","first-page":"3803","DOI":"10.1158\/0008-5472.CAN-07-6389","article-title":"Inhibition of N-linked glycosylation disrupts receptor tyrosine kinase signaling in tumor cells","volume":"68","author":"Contessa","year":"2008","journal-title":"Cancer Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib20","doi-asserted-by":"crossref","first-page":"4334","DOI":"10.1073\/pnas.1503262112","article-title":"N-Glycosylation as determinant of epidermal growth actor receptor conformation in membranes","volume":"112","author":"Kaszuba","year":"2015","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.apsb.2023.10.014_bib21","doi-asserted-by":"crossref","first-page":"11332","DOI":"10.1073\/pnas.1107385108","article-title":"Sialylation and fucosylation of epidermal growth factor receptor suppress its dimerization and activation in lung cancer cells","volume":"108","author":"Liu","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.apsb.2023.10.014_bib22","doi-asserted-by":"crossref","first-page":"2572","DOI":"10.1074\/jbc.M510893200","article-title":"Core fucosylation regulates epidermal growth factor receptor-mediated intracellular signaling","volume":"281","author":"Wang","year":"2006","journal-title":"J Biol Chem"},{"key":"10.1016\/j.apsb.2023.10.014_bib23","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1186\/s13048-018-0385-0","article-title":"Sialylation of EGFR by the ST6Gal-I sialyltransferase promotes EGFR activation and resistance to gefitinib-mediated cell death","volume":"11","author":"Britain","year":"2018","journal-title":"J Ovarian Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib24","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.cell.2007.03.022","article-title":"A method to the madness of N-glycan complexity?","volume":"129","author":"Stanley","year":"2007","journal-title":"Cell"},{"key":"10.1016\/j.apsb.2023.10.014_bib25","doi-asserted-by":"crossref","first-page":"9771","DOI":"10.1158\/0008-5472.CAN-06-4580","article-title":"Complex N-glycan and metabolic control in tumor cells","volume":"67","author":"Mendelsohn","year":"2007","journal-title":"Cancer Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib26","doi-asserted-by":"crossref","first-page":"828","DOI":"10.1093\/glycob\/cwm048","article-title":"Metabolic homeostasis and tissue renewal are dependent on \u03b21,6GlcNAc-branched N-glycans","volume":"17","author":"Cheung","year":"2007","journal-title":"Glycobiology"},{"key":"10.1016\/j.apsb.2023.10.014_bib27","doi-asserted-by":"crossref","first-page":"1569","DOI":"10.1111\/j.1600-0854.2009.00981.x","article-title":"Adaptive regulation at the cell surface by N-glycosylation","volume":"10","author":"Dennis","year":"2009","journal-title":"Traffic"},{"key":"10.1016\/j.apsb.2023.10.014_bib28","doi-asserted-by":"crossref","DOI":"10.1016\/j.mam.2020.100905","article-title":"True significance of N-acetylglucosaminyltransferases GnT-III, V and \u03b11,6 fucosyltransferase in epithelial-mesenchymal transition and cancer","volume":"79","author":"Taniguchi","year":"2021","journal-title":"Mol Aspect Med"},{"key":"10.1016\/j.apsb.2023.10.014_bib29","doi-asserted-by":"crossref","first-page":"3045","DOI":"10.1038\/sj.emboj.7601188","article-title":"Glycosaminoglycan modification of neuropilin-1 modulates VEGFR2 signaling","volume":"25","author":"Shintani","year":"2006","journal-title":"EMBO J"},{"key":"10.1016\/j.apsb.2023.10.014_bib30","doi-asserted-by":"crossref","first-page":"751","DOI":"10.3390\/cells2040751","article-title":"How do gangliosides regulate RTKs signaling?","volume":"2","author":"Julien","year":"2013","journal-title":"Cells"},{"key":"10.1016\/j.apsb.2023.10.014_bib31","doi-asserted-by":"crossref","first-page":"31164","DOI":"10.1074\/jbc.M110.149195","article-title":"N-Glycosylation gene DPAGT1 is a target of the Wnt\/\u03b2-catenin signaling pathway","volume":"285","author":"Sengupta","year":"2010","journal-title":"J Biol Chem"},{"key":"10.1016\/j.apsb.2023.10.014_bib32","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1111\/j.1365-2443.2007.01068.x","article-title":"Glycosylation and palmitoylation of Wnt-3a are coupled to produce an active form of Wnt-3a","volume":"12","author":"Komekado","year":"2007","journal-title":"Gene Cell"},{"key":"10.1016\/j.apsb.2023.10.014_bib33","doi-asserted-by":"crossref","first-page":"2783","DOI":"10.1016\/j.apsb.2021.01.001","article-title":"The biology, function, and applications of exosomes in cancer","volume":"11","author":"Liu","year":"2021","journal-title":"Acta Pharm Sin B"},{"key":"10.1016\/j.apsb.2023.10.014_bib34","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1042\/BJ20111923","article-title":"TGF-\u03b2 sensitivity is determined by N-linked glycosylation of the type II TGF-\u03b2 receptor","volume":"445","author":"Kim","year":"2012","journal-title":"Biochem J"},{"key":"10.1016\/j.apsb.2023.10.014_bib35","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1038\/ki.2013.95","article-title":"New wrinkles in old receptors: core fucosylation is yet another target to inhibit TGF-\u03b2 signaling","volume":"84","author":"Venkatachalam","year":"2013","journal-title":"Kidney Int"},{"key":"10.1016\/j.apsb.2023.10.014_bib36","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1186\/s13058-017-0904-8","article-title":"FUT8 promotes breast cancer cell invasiveness by remodeling TGF-\u03b2 receptor core fucosylation","volume":"19","author":"Tu","year":"2017","journal-title":"Breast Cancer Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib37","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1038\/bjc.2013.699","article-title":"Fucosylated TGF-\u03b2 receptors transduces a signal for epithelial\u2013mesenchymal transition in colorectal cancer cells","volume":"110","author":"Hirakawa","year":"2014","journal-title":"Br J Cancer"},{"key":"10.1016\/j.apsb.2023.10.014_bib38","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1038\/s41586-019-1526-3","article-title":"E-cadherin is required for metastasis in multiple models of breast cancer","volume":"573","author":"Padmanaban","year":"2019","journal-title":"Nature"},{"key":"10.1016\/j.apsb.2023.10.014_bib39","doi-asserted-by":"crossref","first-page":"5931","DOI":"10.1073\/pnas.1918167117","article-title":"The functional activity of E-cadherin controls tumor cell metastasis at multiple steps","volume":"117","author":"Na","year":"2020","journal-title":"Proc Natl Acad Sci U\u00a0S\u00a0A"},{"key":"10.1016\/j.apsb.2023.10.014_bib40","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1038\/sj.cr.7290243","article-title":"The expression of core fucosylated E-cadherin in cancer cells and lung cancer patients: prognostic implications","volume":"14","author":"Geng","year":"2004","journal-title":"Cell Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib41","doi-asserted-by":"crossref","first-page":"2690","DOI":"10.1016\/j.bbagen.2012.10.021","article-title":"E-cadherin and adherens-junctions stability in gastric carcinoma: functional implications of glycosyltransferases involving N-glycan branching biosynthesis, N-acetylglucosaminyltransferases III and V","volume":"1830","author":"Pinho","year":"2013","journal-title":"Biochim Biophys Acta Gen Subj"},{"key":"10.1016\/j.apsb.2023.10.014_bib42","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1093\/cvr\/cvv154","article-title":"Selectins: initiators of leucocyte adhesion and signalling at the vascular wall","volume":"107","author":"McEver","year":"2015","journal-title":"Cardiovasc Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib43","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1016\/j.apsb.2015.07.005","article-title":"Cancer metastases: challenges and opportunities","volume":"5","author":"Guan","year":"2015","journal-title":"Acta Pharm Sin B"},{"key":"10.1016\/j.apsb.2023.10.014_bib44","doi-asserted-by":"crossref","first-page":"3014","DOI":"10.1038\/bjc.2013.690","article-title":"Human fucosyltransferase 6 enables prostate cancer metastasis to bone","volume":"109","author":"Li","year":"2013","journal-title":"Br J Cancer"},{"key":"10.1016\/j.apsb.2023.10.014_bib45","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1038\/s41556-019-0309-2","article-title":"Bone vascular niche E-selectin induces mesenchymal\u2013epithelial transition and Wnt activation in cancer cells to promote bone metastasis","volume":"21","author":"Esposito","year":"2019","journal-title":"Nat Cell Biol"},{"key":"10.1016\/j.apsb.2023.10.014_bib46","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1038\/nrc2748","article-title":"Integrins in cancer: biological implications and therapeutic opportunities","volume":"10","author":"Desgrosellier","year":"2010","journal-title":"Nat Rev Cancer"},{"key":"10.1016\/j.apsb.2023.10.014_bib47","doi-asserted-by":"crossref","first-page":"a004994","DOI":"10.1101\/cshperspect.a004994","article-title":"Integrin structure, activation, and interactions","volume":"3","author":"Campbell","year":"2011","journal-title":"Cold Spring Harbor Perspect Biol"},{"key":"10.1016\/j.apsb.2023.10.014_bib48","doi-asserted-by":"crossref","first-page":"251","DOI":"10.4161\/cam.23840","article-title":"Integrins and metastasis","volume":"7","author":"Ganguly","year":"2013","journal-title":"Cell Adhes Migrat"},{"key":"10.1016\/j.apsb.2023.10.014_bib49","doi-asserted-by":"crossref","first-page":"2726","DOI":"10.1016\/j.apsb.2021.01.004","article-title":"Integrins as attractive targets for cancer therapeutics","volume":"11","author":"Li","year":"2021","journal-title":"Acta Pharm Sin B"},{"key":"10.1016\/j.apsb.2023.10.014_bib50","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1038\/nrm2799","article-title":"Integrins: masters and slaves of endocytic transport","volume":"10","author":"Caswell","year":"2009","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.1016\/j.apsb.2023.10.014_bib51","doi-asserted-by":"crossref","first-page":"4425","DOI":"10.1074\/jbc.RA118.005208","article-title":"A complex between phosphatidylinositol 4-kinase II\u03b1 and integrin \u03b13\u03b21 is required for N-glycan sialylation in cancer cells","volume":"294","author":"Isaji","year":"2019","journal-title":"J Biol Chem"},{"key":"10.1016\/j.apsb.2023.10.014_bib52","doi-asserted-by":"crossref","first-page":"29345","DOI":"10.1074\/jbc.M115.682229","article-title":"Integrin \u03b15 suppresses the phosphorylation of epidermal growth factor receptor and its cellular signaling of cell proliferation via N-glycosylation","volume":"290","author":"Hang","year":"2015","journal-title":"J Biol Chem"},{"key":"10.1016\/j.apsb.2023.10.014_bib53","doi-asserted-by":"crossref","first-page":"3199","DOI":"10.1158\/0008-5472.CAN-14-0728","article-title":"Sialic acids sweeten a tumor's life","volume":"74","author":"B\u00fcll","year":"2014","journal-title":"Cancer Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib54","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/j.bbamcr.2003.10.004","article-title":"Glycosylation profile of integrin \u03b13\u03b21 changes with melanoma progression","volume":"1643","author":"Poche\u0107","year":"2003","journal-title":"Biochim Biophys Acta Gen Subj"},{"key":"10.1016\/j.apsb.2023.10.014_bib55","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1038\/nrc727","article-title":"Role of integrins in cell invasion and migration","volume":"2","author":"Hood","year":"2002","journal-title":"Nat Rev Cancer"},{"key":"10.1016\/j.apsb.2023.10.014_bib56","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1038\/bjc.1997.8","article-title":"Involvement of hepatocyte growth factor in increased integrin expression on HepG2 cells triggered by adhesion to endothelial cells","volume":"75","author":"Kawakami-Kimura","year":"1997","journal-title":"Br J Cancer"},{"key":"10.1016\/j.apsb.2023.10.014_bib57","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1038\/nature13535","article-title":"The cancer glycocalyx mechanically primes integrin-mediated growth and survival","volume":"511","author":"Paszek","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.apsb.2023.10.014_bib58","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1038\/nrc3982","article-title":"Glycosylation in cancer: mechanisms and clinical implications","volume":"15","author":"Pinho","year":"2015","journal-title":"Nat Rev Cancer"},{"key":"10.1016\/j.apsb.2023.10.014_bib59","first-page":"6837","article-title":"Aberrant N-glycosylation of \u03b21 integrin causes reduced \u03b15\u03b21 integrin clustering and stimulates cell migration","volume":"62","author":"Guo","year":"2002","journal-title":"Cancer Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib60","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1111\/joim.12019","article-title":"VEGFA and tumour angiogenesis","volume":"273","author":"Claesson-Welsh","year":"2013","journal-title":"J Intern Med"},{"key":"10.1016\/j.apsb.2023.10.014_bib61","doi-asserted-by":"crossref","first-page":"6531","DOI":"10.1038\/onc.2017.243","article-title":"Contribution of vascular endothelial growth factor receptor-2 sialylation to the process of angiogenesis","volume":"36","author":"Chiodelli","year":"2017","journal-title":"Oncogene"},{"key":"10.1016\/j.apsb.2023.10.014_bib62","doi-asserted-by":"crossref","first-page":"13117","DOI":"10.1074\/jbc.RA119.008643","article-title":"N-Glycosylation regulates ligand-dependent activation and signaling of vascular endothelial growth factor receptor 2 (VEGFR2)","volume":"294","author":"Chandler","year":"2019","journal-title":"J Biol Chem"},{"key":"10.1016\/j.apsb.2023.10.014_bib63","doi-asserted-by":"crossref","first-page":"3746","DOI":"10.1038\/sj.onc.1211029","article-title":"Galectin-1, a novel ligand of neuropilin-1, activates VEGFR-2 signaling and modulates the migration of vascular endothelial cells","volume":"27","author":"Hsieh","year":"2008","journal-title":"Oncogene"},{"key":"10.1016\/j.apsb.2023.10.014_bib64","doi-asserted-by":"crossref","first-page":"6216","DOI":"10.1158\/0008-5472.CAN-09-4150","article-title":"Tumor cells secrete galectin-1 to enhance endothelial cell activity","volume":"70","author":"Thijssen","year":"2010","journal-title":"Cancer Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib65","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1016\/j.cell.2014.01.043","article-title":"Glycosylation-dependent lectin-receptor interactions preserve angiogenesis in anti-VEGF refractory tumors","volume":"156","author":"Croci Diego","year":"2014","journal-title":"Cell"},{"key":"10.1016\/j.apsb.2023.10.014_bib66","doi-asserted-by":"crossref","first-page":"29913","DOI":"10.1074\/jbc.M111.226423","article-title":"Galectin-3 protein modulates cell surface expression and activation of vascular endothelial growth factor receptor 2 in human endothelial cells","volume":"286","author":"Markowska","year":"2011","journal-title":"J Biol Chem"},{"key":"10.1016\/j.apsb.2023.10.014_bib67","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.canlet.2021.01.010","article-title":"The hexosamine biosynthetic pathway and cancer: current knowledge and future therapeutic strategies","volume":"503","author":"Lam","year":"2021","journal-title":"Cancer Lett"},{"key":"10.1016\/j.apsb.2023.10.014_bib68","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1038\/nchembio0607-307","article-title":"A sugar-coated switch for cellular growth and arrest","volume":"3","author":"Taniguchi","year":"2007","journal-title":"Nat Chem Biol"},{"key":"10.1016\/j.apsb.2023.10.014_bib69","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/j.canlet.2012.11.011","article-title":"Serum peptidomic biomarkers for pulmonary metastatic melanoma identified by means of a nanopore-based assay","volume":"334","author":"Fan","year":"2013","journal-title":"Cancer Lett"},{"key":"10.1016\/j.apsb.2023.10.014_bib70","doi-asserted-by":"crossref","first-page":"9327","DOI":"10.1038\/srep09327","article-title":"Circulating peptidome to indicate the tumor-resident proteolysis","volume":"5","author":"Deng","year":"2015","journal-title":"Sci Rep"},{"key":"10.1016\/j.apsb.2023.10.014_bib71","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1002\/mas.21583","article-title":"Glycoproteomic markers of hepatocellular carcinoma\u2013mass spectrometry based approaches","volume":"38","author":"Zhu","year":"2019","journal-title":"Mass Spectrom Rev"},{"key":"10.1016\/j.apsb.2023.10.014_bib72","doi-asserted-by":"crossref","first-page":"22850","DOI":"10.1021\/acsomega.2c02600","article-title":"Glycopeptides with sialyl lewis antigen in serum haptoglobin as candidate biomarkers for nonalcoholic steatohepatitis hepatocellular carcinoma using a higher-energy collision-induced dissociation parallel reaction monitoring-mass spectrometry method","volume":"7","author":"Lin","year":"2022","journal-title":"ACS Omega"},{"key":"10.1016\/j.apsb.2023.10.014_bib73","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1093\/jb\/mvn011","article-title":"Biological function of fucosylation in cancer biology","volume":"143","author":"Miyoshi","year":"2008","journal-title":"J Biochem"},{"key":"10.1016\/j.apsb.2023.10.014_bib74","doi-asserted-by":"crossref","first-page":"12467","DOI":"10.1021\/acsomega.3c00519","article-title":"Discovery of core-fucosylated glycopeptides as diagnostic biomarkers for early HCC in patients with NASH cirrhosis using LC-HCD-PRM-MS\/MS","volume":"8","author":"Tan","year":"2023","journal-title":"ACS Omega"},{"key":"10.1016\/j.apsb.2023.10.014_bib75","doi-asserted-by":"crossref","first-page":"1968","DOI":"10.1021\/acs.jproteome.5b00068","article-title":"Large-scale identification of core-fucosylated glycopeptide sites in pancreatic cancer serum using mass spectrometry","volume":"14","author":"Tan","year":"2015","journal-title":"J Proteome Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib76","doi-asserted-by":"crossref","first-page":"4541","DOI":"10.1021\/pr300330z","article-title":"Identification and confirmation of differentially expressed fucosylated glycoproteins in the serum of ovarian cancer patients using a lectin array and LC\u2012MS\/MS","volume":"11","author":"Wu","year":"2012","journal-title":"J Proteome Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib77","doi-asserted-by":"crossref","first-page":"2351","DOI":"10.1002\/elps.201700426","article-title":"The analysis of alpha-1-antitrypsin glycosylation with direct LC\u2012MS\/MS","volume":"39","author":"Yin","year":"2018","journal-title":"Electrophoresis"},{"key":"10.1016\/j.apsb.2023.10.014_bib78","doi-asserted-by":"crossref","first-page":"3452","DOI":"10.1021\/acs.jproteome.0c00270","article-title":"Glycopeptide biomarkers in serum haptoglobin for hepatocellular carcinoma detection in patients with non-alcoholic steatohepatitis","volume":"19","author":"Zhu","year":"2020","journal-title":"J Proteome Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib79","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/bs.acr.2022.07.005","article-title":"Mass spectrometry based biomarkers for early detection of HCC using a glycoproteomic approach","volume":"157","author":"Mechref","year":"2023","journal-title":"Adv Cancer Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib80","doi-asserted-by":"crossref","first-page":"1353","DOI":"10.1016\/S0140-6736(85)92643-1","article-title":"Fucosylated alpha-fetoprotein as marker of early hepatocellular carcinoma","volume":"326","author":"Aoyagi","year":"1985","journal-title":"Lancet"},{"key":"10.1016\/j.apsb.2023.10.014_bib81","doi-asserted-by":"crossref","first-page":"1427","DOI":"10.1056\/NEJM198405313102204","article-title":"Des-gamma-carboxy (abnormal) prothrombin as a serum marker of primary hepatocellular carcinoma","volume":"310","author":"Liebman","year":"1984","journal-title":"N Engl J Med"},{"key":"10.1016\/j.apsb.2023.10.014_bib82","doi-asserted-by":"crossref","first-page":"1294","DOI":"10.1074\/mcp.M112.023325","article-title":"Quantitative liquid chromatography-mass spectrometry-multiple reaction monitoring (LC\u2012MS-MRM) analysis of site-specific glycoforms of haptoglobin in liver disease","volume":"12","author":"Sanda","year":"2013","journal-title":"Mol Cell Proteomics"},{"key":"10.1016\/j.apsb.2023.10.014_bib83","doi-asserted-by":"crossref","first-page":"5561","DOI":"10.1021\/pr5005482","article-title":"Protein and site specificity of fucosylation in liver-secreted glycoproteins","volume":"13","author":"Pompach","year":"2014","journal-title":"J Proteome Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib84","doi-asserted-by":"crossref","first-page":"4876","DOI":"10.1021\/acs.jproteome.5b00718","article-title":"Mass-selected site-specific core-fucosylation of serum proteins in hepatocellular carcinoma","volume":"14","author":"Yin","year":"2015","journal-title":"J Proteome Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib85","doi-asserted-by":"crossref","first-page":"5388","DOI":"10.1021\/acs.jproteome.5b00792","article-title":"ESI\u2013LC\u2013MS method for haptoglobin fucosylation analysis in hepatocellular carcinoma and liver cirrhosis","volume":"14","author":"Zhang","year":"2015","journal-title":"J Proteome Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib86","doi-asserted-by":"crossref","first-page":"3624","DOI":"10.1021\/acs.jproteome.6b00429","article-title":"HILIC and ERLIC enrichment of glycopeptides derived from breast and brain cancer cells","volume":"15","author":"Zacharias","year":"2016","journal-title":"J Proteome Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib87","doi-asserted-by":"crossref","first-page":"1617","DOI":"10.1007\/s00216-017-0811-y","article-title":"Designation of fingerprint glycopeptides for targeted glycoproteomic analysis of serum haptoglobin: insights into gastric cancer biomarker discovery","volume":"410","author":"Lee","year":"2018","journal-title":"Anal Bioanal Chem"},{"key":"10.1016\/j.apsb.2023.10.014_bib88","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.jprot.2018.02.003","article-title":"Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC\u2012MS-MRM","volume":"189","author":"Ma","year":"2018","journal-title":"J Proteonomics"},{"key":"10.1016\/j.apsb.2023.10.014_bib89","doi-asserted-by":"crossref","first-page":"563","DOI":"10.3390\/metabo11080563","article-title":"PRM-MS quantitative analysis of isomeric N-glycopeptides derived from human serum haptoglobin of patients with cirrhosis and hepatocellular carcinoma","volume":"11","author":"Gutierrez Reyes","year":"2021","journal-title":"Metabolites"},{"key":"10.1016\/j.apsb.2023.10.014_bib90","doi-asserted-by":"crossref","first-page":"496","DOI":"10.1002\/mas.21707","article-title":"In-depth investigation of altered glycosylation in human haptoglobin associated cancer by mass spectrometry","volume":"42","author":"Oh","year":"2021","journal-title":"Mass Spectrom Rev"},{"key":"10.1016\/j.apsb.2023.10.014_bib91","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1016\/j.jhep.2005.05.028","article-title":"GP73, a resident Golgi glycoprotein, is a novel serum marker for hepatocellular carcinoma","volume":"43","author":"Marrero","year":"2005","journal-title":"J Hepatol"},{"key":"10.1016\/j.apsb.2023.10.014_bib92","doi-asserted-by":"crossref","first-page":"1687","DOI":"10.1136\/gut.2010.214916","article-title":"Golgi protein 73 (GOLPH2) is a valuable serum marker for hepatocellular carcinoma","volume":"59","author":"Mao","year":"2010","journal-title":"Gut"},{"key":"10.1016\/j.apsb.2023.10.014_bib93","first-page":"359","article-title":"Differential quantitative determination of site-specific intact N-glycopeptides in serum haptoglobin between hepatocellular carcinoma and cirrhosis using LC\u2012EThcD-MS\/MS","volume":"18","author":"Zhu","year":"2019","journal-title":"J Proteome Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib94","doi-asserted-by":"crossref","first-page":"2887","DOI":"10.1021\/pr500043k","article-title":"Mass-selected site-specific core-fucosylation of ceruloplasmin in alcohol-related hepatocellular carcinoma","volume":"13","author":"Yin","year":"2014","journal-title":"J Proteome Res"},{"key":"10.1016\/j.apsb.2023.10.014_bib95","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1515\/cclm-2018-0379","article-title":"Aberrant glycosylation and cancer biomarker discovery: a promising and thorny journey","volume":"57","author":"Wang","year":"2019","journal-title":"Clin Chem Lab Med"},{"key":"10.1016\/j.apsb.2023.10.014_bib96","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1038\/s41598-019-56947-1","article-title":"Tri-antennary tri-sialylated mono-fucosylated glycan of alpha-1 antitrypsin as a non-invasive biomarker for non-alcoholic steatohepatitis: a novel glycobiomarker for non-alcoholic steatohepatitis","volume":"10","author":"Ogawa","year":"2020","journal-title":"Sci Rep"},{"key":"10.1016\/j.apsb.2023.10.014_bib97","doi-asserted-by":"crossref","first-page":"1376","DOI":"10.1038\/bjc.2016.116","article-title":"Loss of N-acetylgalactosaminyltransferase 3 in poorly differentiated pancreatic cancer: augmented aggressiveness and aberrant ErbB family glycosylation","volume":"114","author":"Chugh","year":"2016","journal-title":"Br J Cancer"},{"key":"10.1016\/j.apsb.2023.10.014_bib98","doi-asserted-by":"crossref","first-page":"1795","DOI":"10.1016\/j.bbagen.2015.12.016","article-title":"Glycomic analysis of gastric carcinoma cells discloses glycans as modulators of RON receptor tyrosine kinase activation in cancer","volume":"1860","author":"Mereiter","year":"2016","journal-title":"Biochim Biophys Acta Gen Subj"},{"key":"10.1016\/j.apsb.2023.10.014_bib99","doi-asserted-by":"crossref","first-page":"256","DOI":"10.3390\/jcm7090256","article-title":"The Thomsen-Friedenreich antigen: a highly sensitive and specific predictor of microsatellite instability in gastric cancer","volume":"7","author":"Mereiter","year":"2018","journal-title":"J Clin Med"}],"container-title":["Acta Pharmaceutica Sinica B"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2211383523004082?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2211383523004082?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,31]],"date-time":"2025-10-31T17:08:57Z","timestamp":1761930537000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2211383523004082"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,3]]},"references-count":99,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2024,3]]}},"alternative-id":["S2211383523004082"],"URL":"https:\/\/doi.org\/10.1016\/j.apsb.2023.10.014","relation":{},"ISSN":["2211-3835"],"issn-type":[{"value":"2211-3835","type":"print"}],"subject":[],"published":{"date-parts":[[2024,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The role of N-glycosylation in cancer","name":"articletitle","label":"Article Title"},{"value":"Acta Pharmaceutica Sinica B","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.apsb.2023.10.014","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 The Authors. Published by Elsevier B.V. on behalf of Chinese Pharmaceutical Association and Institute of Materia Medica, Chinese Academy of Medical Sciences.","name":"copyright","label":"Copyright"}]}}