{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T09:23:12Z","timestamp":1790673792059,"version":"4.1.0"},"reference-count":65,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2018,4,17]]},"abstract":"<jats:p>Glycosylation is a major form of enzymatic modification of organic molecules responsible for multiple biological processes in an organism. The biosynthesis of glycans is controlled by a series of glycosyltransferases, glycosidases and glycan-modifying enzymes that collectively assemble and process monosaccharide moieties into a diverse array of structures. Many studies have provided insight into various pathways of glycosylation at the ocular surface, such as those related to the biosynthesis of mucin-type O-glycans and N-glycans on proteins, but many others still remain largely unknown. This review provides an overview of the different classes of glycans described at the ocular surface focusing on their biosynthetic pathways and biological relevance. A precise understanding of these pathways under physiological and pathological conditions could help identify biomarkers and novel targets for therapeutic intervention.<\/jats:p>","DOI":"10.1042\/bst20170408","type":"journal-article","created":{"date-parts":[[2018,3,9]],"date-time":"2018-03-09T20:30:20Z","timestamp":1520627420000},"page":"343-350","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":33,"title":["Glycosylation pathways at the ocular surface"],"prefix":"10.1042","volume":"46","author":[{"given":"Maria C.","family":"Rodriguez Benavente","sequence":"first","affiliation":[{"name":"Schepens Eye Research Institute of Massachusetts Eye and Ear, Department of Ophthalmology, Harvard Medical School, Boston, MA, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pablo","family":"Arg\u00fceso","sequence":"additional","affiliation":[{"name":"Schepens Eye Research Institute of Massachusetts Eye and Ear, Department of Ophthalmology, Harvard Medical School, Boston, MA, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2018,3,9]]},"reference":[{"key":"2021111818064105700_BST-2017-0408CC1","first-page":"1","volume-title":"Essentials of glycobiology","author":"Varki","year":"2015"},{"key":"2021111818064105700_BST-2017-0408CC2","first-page":"65","volume-title":"Essentials of glycobiology","author":"Rini","year":"2015"},{"key":"2021111818064105700_BST-2017-0408CC3","doi-asserted-by":"publisher","first-page":"1235681","DOI":"10.1126\/science.1235681","article-title":"Emerging principles for the therapeutic exploitation of glycosylation","volume":"343","author":"Dalziel","year":"2014","journal-title":"Science"},{"key":"2021111818064105700_BST-2017-0408CC4","doi-asserted-by":"publisher","first-page":"119","DOI":"10.1007\/s00418-016-1526-4","article-title":"Eukaryotic protein glycosylation: a primer for histochemists and cell biologists","volume":"147","author":"Corfield","year":"2017","journal-title":"Histochem. 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