{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T23:13:24Z","timestamp":1793229204288,"version":"4.5.0"},"reference-count":180,"publisher":"Oxford University Press (OUP)","issue":"11","license":[{"start":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T00:00:00Z","timestamp":1760054400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2025,11,6]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The mammalian brain is unique in its cell types, mainly neurons and glial cells, and the glycoproteins expressed by these cells. Two of the most abundant types of modifications of cell surface glycoproteins are N-glycans linked to Asn residues and O-glycans linked via GalNAc to Ser\/Thr residues. Recent studies focused on glycoproteomics, glycomics and glycan localization in the brain reveal major differences in these protein modifications compared to other organs. Deficiencies in glycosylation are associated with the development of multiple brain disorders such as congenital disorders of glycosylation (CDG) that include brain structural abnormalities, epilepsy and seizures to more common disorders including schizophrenia and Alzheimer\u2019s disease. Here we summarize recent advances in the growing field of neuro-glycobiology and highlight key points that could be used as primer for future studies.<\/jats:p>","DOI":"10.1093\/glycob\/cwaf054","type":"journal-article","created":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T12:15:44Z","timestamp":1760012144000},"source":"Crossref","is-referenced-by-count":10,"title":["The Importance of N- and O-Glycosylation of Brain Cell Surface Glycoproteins"],"prefix":"10.1093","volume":"35","author":[{"given":"Maxence","family":"Noel","sequence":"first","affiliation":[{"name":"Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School , Boston, MA 02215 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yumi M","family":"Z\u00fcrcher","sequence":"additional","affiliation":[{"name":"Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School , Boston, MA 02215 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ea K C","family":"Tulin","sequence":"additional","affiliation":[{"name":"Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School , Boston, MA 02215 ,","place":["USA"]},{"name":"Department of Biotechnology, Visayas State University , Baybay City, Leyte 6521 ,","place":["Philippines"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8918-5034","authenticated-orcid":false,"given":"Richard D","family":"Cummings","sequence":"additional","affiliation":[{"name":"Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School , Boston, MA 02215 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2025,10,10]]},"reference":[{"key":"2025110901135346600_ref1","doi-asserted-by":"publisher","first-page":"2793","DOI":"10.1007\/s11064-022-03651-8","article-title":"Fut9 Deficiency Causes Abnormal Neural Development in the Mouse Cerebral Cortex and Retina","volume":"47","author":"Abdullah","year":"2022","journal-title":"Neurochem Res"},{"key":"2025110901135346600_ref2","doi-asserted-by":"publisher","first-page":"1024","DOI":"10.4049\/jimmunol.127.3.1024","article-title":"A differentiation antigen of human NK and K cells identified by a monoclonal antibody (HNK-1)","volume":"127","author":"Abo","year":"1981","journal-title":"J Immunol"},{"key":"2025110901135346600_ref3","doi-asserted-by":"publisher","first-page":"7397","DOI":"10.12998\/wjcc.v10.i21.7397","article-title":"Updated clinical and glycomic features of mannosyl-oligosaccharide glucosidase deficiency: Two case reports","volume":"10","author":"Abuduxikuer","year":"2022","journal-title":"World J Clin Cases"},{"key":"2025110901135346600_ref4","doi-asserted-by":"publisher","first-page":"92","DOI":"10.1684\/epd.2016.0802","article-title":"RFT1-congenital disorder of glycosylation (CDG) syndrome: a cause of early-onset severe epilepsy","volume":"18","author":"Aeby","year":"2016","journal-title":"Epileptic Disord"},{"key":"2025110901135346600_ref5","doi-asserted-by":"publisher","first-page":"1569","DOI":"10.3390\/biom10111569","article-title":"The Role of APP O-Glycosylation in Alzheimer\u2019s Disease","volume":"10","author":"Akasaka-Manya","year":"2020","journal-title":"Biomolecules"},{"key":"2025110901135346600_ref6","doi-asserted-by":"publisher","first-page":"595","DOI":"10.1002\/jnr.1190","article-title":"Developmental expression of a unique carbohydrate antigen, Tn antigen, in mouse central nervous tissues","volume":"65","author":"Akita","year":"2001","journal-title":"J. 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