{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,8]],"date-time":"2026-07-08T05:32:39Z","timestamp":1783488759695,"version":"3.55.0"},"reference-count":245,"publisher":"Oxford University Press (OUP)","issue":"11","license":[{"start":{"date-parts":[[2023,11,1]],"date-time":"2023-11-01T00:00:00Z","timestamp":1698796800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"funder":[{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Frontiers in Research Fund"},{"DOI":"10.13039\/501100000196","name":"Canada Foundation for Innovation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000196","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100009056","name":"GlycoNet","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100009056","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010231","name":"Banting Research Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100010231","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2023,12,25]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>All cells are decorated with complex carbohydrate structures called glycans that serve as ligands for glycan-binding proteins (GBPs) to mediate a wide range of biological processes. Understanding the specific functions of glycans is key to advancing an understanding of human health and disease. However, the lack of convenient and accessible tools to study glycan-based interactions has been a defining challenge in glycobiology. Thus, the development of chemical and biochemical strategies to address these limitations has been a rapidly growing area of research. In this review, we describe the use of glycosyltransferases (GTs) as versatile tools to facilitate a greater understanding of the biological roles of glycans. We highlight key examples of how GTs have streamlined the preparation of well-defined complex glycan structures through chemoenzymatic synthesis, with an emphasis on synthetic strategies allowing for site- and branch-specific display of glyco-epitopes. We also describe how GTs have facilitated expansion of glyco-engineering strategies, on both glycoproteins and cell surfaces. Coupled with advancements in bioorthogonal chemistry, GTs have enabled selective glyco-epitope editing of glycoproteins and cells, selective glycan subclass labeling, and the introduction of novel biomolecule functionalities onto cells, including defined oligosaccharides, antibodies, and other proteins. Collectively, these approaches have contributed great insight into the fundamental biological roles of glycans and are enabling their application in drug development and cellular therapies, leaving the field poised for rapid expansion.<\/jats:p>","DOI":"10.1093\/glycob\/cwad092","type":"journal-article","created":{"date-parts":[[2023,11,13]],"date-time":"2023-11-13T21:23:08Z","timestamp":1699910588000},"page":"888-910","source":"Crossref","is-referenced-by-count":16,"title":["Glycosyltransferases as versatile tools to study the biology of glycans"],"prefix":"10.1093","volume":"33","author":[{"given":"Joshua M","family":"Kofsky","sequence":"first","affiliation":[{"name":"Queen\u2019s University Department of Chemistry, , 90 Bader Lane, Kingston, ON K7L 3N6, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jonathan L","family":"Babulic","sequence":"additional","affiliation":[{"name":"Queen\u2019s University Department of Biomedical and Molecular Sciences, , 18 Stuart Street, Kingston, ON K7L 2V7, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie E","family":"Boddington","sequence":"additional","affiliation":[{"name":"Queen\u2019s University Department of Biomedical and Molecular Sciences, , 18 Stuart Street, Kingston, ON K7L 2V7, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fabiola V","family":"De Le\u00f3n Gonz\u00e1lez","sequence":"additional","affiliation":[{"name":"Queen\u2019s University Department of Chemistry, , 90 Bader Lane, Kingston, ON K7L 3N6, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5977-8453","authenticated-orcid":false,"given":"Chantelle J","family":"Capicciotti","sequence":"additional","affiliation":[{"name":"Queen\u2019s University Department of Chemistry, , 90 Bader Lane, Kingston, ON K7L 3N6, Canada"},{"name":"Queen\u2019s University Department of Biomedical and Molecular Sciences, , 18 Stuart Street, Kingston, ON K7L 2V7, Canada"},{"name":"Queen\u2019s University Department of Surgery, , 76 Stuart Street, Kingston, ON K7L 2V7, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2023,11,13]]},"reference":[{"key":"2024021205300726900_ref1","doi-asserted-by":"crossref","first-page":"108249","DOI":"10.1016\/j.carres.2021.108249","article-title":"Development of BODIPY labelled sialic acids as sialyltransferase substrates for direct detection of terminal galactose on N- and O-linked glycans","volume":"500","author":"Abukar","year":"2021","journal-title":"Carbohydr Res"},{"issue":"8","key":"2024021205300726900_ref2","doi-asserted-by":"crossref","first-page":"2610","DOI":"10.1158\/1078-0432.CCR-18-1527","article-title":"Fucosylation enhances the efficacy of adoptively transferred antigen-specific cytotoxic T lymphocytes","volume":"25","author":"Alatrash","year":"2019","journal-title":"Clin Cancer 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