{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,9]],"date-time":"2026-09-09T21:09:49Z","timestamp":1788988189715,"version":"build-2803163510"},"reference-count":52,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100010067","name":"Gobierno de Arag\u00f3n","doi-asserted-by":"publisher","award":["E34_20R"],"award-info":[{"award-number":["E34_20R"]}],"id":[{"id":"10.13039\/501100010067","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100008530","name":"European Regional Development Fund","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100008530","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100014440","name":"Spain Ministry of Science Innovation and Universities","doi-asserted-by":"publisher","award":["PID2022-136362NB-I00"],"award-info":[{"award-number":["PID2022-136362NB-I00"]}],"id":[{"id":"10.13039\/100014440","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100014440","name":"Spain Ministry of Science Innovation and Universities","doi-asserted-by":"publisher","award":["PID2022-137973NB-I00"],"award-info":[{"award-number":["PID2022-137973NB-I00"]}],"id":[{"id":"10.13039\/100014440","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100014440","name":"Spain Ministry of Science Innovation and Universities","doi-asserted-by":"publisher","award":["PID2025-167711NB-I00"],"award-info":[{"award-number":["PID2025-167711NB-I00"]}],"id":[{"id":"10.13039\/100014440","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Current Opinion in Chemical Biology"],"published-print":{"date-parts":[[2026,10]]},"DOI":"10.1016\/j.cbpa.2026.102758","type":"journal-article","created":{"date-parts":[[2026,8,28]],"date-time":"2026-08-28T19:47:48Z","timestamp":1787946468000},"page":"102758","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Glycosyltransferases: Capturing catalytic states and conformational gating"],"prefix":"10.1016","volume":"94","author":[{"given":"Alejandro","family":"Montesa","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alejandro","family":"P\u00e9rez-Latorre","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pedro","family":"Merino","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3122-9401","authenticated-orcid":false,"given":"Ramon","family":"Hurtado-Guerrero","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.cbpa.2026.102758_bib1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.sbi.2017.03.003","article-title":"High-resolution cryo-EM: the nuts and bolts","volume":"46","author":"Elmlund","year":"2017","journal-title":"Curr Opin Struct Biol"},{"key":"10.1016\/j.cbpa.2026.102758_bib2","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1007\/978-1-0716-0775-6_25","article-title":"Protein structure analysis and validation with X-Ray crystallography","volume":"2178","author":"Papageorgiou","year":"2021","journal-title":"Methods Mol Biol"},{"key":"10.1016\/j.cbpa.2026.102758_bib3","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1007\/978-3-031-52193-5_9","article-title":"X-Ray crystallography for macromolecular complexes","volume":"3234","author":"Fernandez","year":"2024","journal-title":"Adv Exp Med Biol"},{"key":"10.1016\/j.cbpa.2026.102758_bib4","article-title":"Boltz-2: towards accurate and efficient binding affinity prediction","author":"Passaro","year":"2025","journal-title":"bioRxiv"},{"key":"10.1016\/j.cbpa.2026.102758_bib5","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1038\/s41586-024-07487-w","article-title":"Accurate structure prediction of biomolecular interactions with AlphaFold 3","volume":"630","author":"Abramson","year":"2024","journal-title":"Nature"},{"key":"10.1016\/j.cbpa.2026.102758_bib6","doi-asserted-by":"crossref","first-page":"1022","DOI":"10.1038\/s41589-023-01345-y","article-title":"Structural basis for Lewis antigen synthesis by the alpha1,3-fucosyltransferase FUT9","volume":"19","author":"Kadirvelraj","year":"2023","journal-title":"Nat Chem Biol"},{"key":"10.1016\/j.cbpa.2026.102758_bib7","doi-asserted-by":"crossref","first-page":"9898","DOI":"10.1002\/anie.201504617","article-title":"A native ternary complex trapped in a crystal reveals the catalytic mechanism of a retaining glycosyltransferase","volume":"54","author":"Albesa-Jove","year":"2015","journal-title":"Angew Chem Int Ed Engl"},{"key":"10.1016\/j.cbpa.2026.102758_bib8","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2023.104609","article-title":"Mechanism and linkage specificities of the dual retaining beta-Kdo glycosyltransferase modules of KpsC from bacterial capsule biosynthesis","volume":"299","author":"Doyle","year":"2023","journal-title":"J Biol Chem"},{"key":"10.1016\/j.cbpa.2026.102758_bib9","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1007\/978-3-030-58971-4_6","article-title":"Recent progress in structural studies on the GT-C superfamily of protein glycosyltransferases","volume":"96","author":"Bohl","year":"2021","journal-title":"Subcell Biochem"},{"key":"10.1016\/j.cbpa.2026.102758_bib10","doi-asserted-by":"crossref","DOI":"10.1016\/j.sbi.2023.102547","article-title":"Emerging structural insights into C-type glycosyltransferases","volume":"79","author":"Alexander","year":"2023","journal-title":"Curr Opin Struct Biol"},{"key":"10.1016\/j.cbpa.2026.102758_bib11","doi-asserted-by":"crossref","first-page":"1454","DOI":"10.1021\/acscentsci.1c00594","article-title":"Guidelines for O-Glycoside Formation from first principles","volume":"7","author":"Andreana","year":"2021","journal-title":"ACS Cent Sci"},{"key":"10.1016\/j.cbpa.2026.102758_bib12","doi-asserted-by":"crossref","first-page":"1577","DOI":"10.1021\/jacs.0c12096","article-title":"Ab initio molecular dynamics simulations of the S(N)1\/S(N)2 mechanistic continuum in glycosylation reactions","volume":"143","author":"Fu","year":"2021","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2026.102758_bib13","first-page":"521","article-title":"Glycosyltransferases: structures, functions, and mechanisms","volume":"vol. 77","author":"Lairson","year":"2008"},{"key":"10.1016\/j.cbpa.2026.102758_bib14","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.sbi.2016.07.007","article-title":"The conformational plasticity of glycosyltransferases","volume":"40","author":"Albesa-Jov\u00e9","year":"2016","journal-title":"Curr Opin Struct Biol"},{"key":"10.1016\/j.cbpa.2026.102758_bib15","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1038\/s41589-019-0350-2","article-title":"Emerging structural insights into glycosyltransferase-mediated synthesis of glycans","volume":"15","author":"Moremen","year":"2019","journal-title":"Nat Chem Biol"},{"key":"10.1016\/j.cbpa.2026.102758_bib52","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1006\/jmbi.2001.5159","article-title":"Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT-2 glycosyltransferase SpsA: a comparison with related NDP-sugar glycosyltransferases","volume":"314","author":"Tarbouriech","year":"2001","journal-title":"J Mol Biol"},{"key":"10.1016\/j.cbpa.2026.102758_bib53","doi-asserted-by":"crossref","first-page":"3413","DOI":"10.1002\/j.1460-2075.1994.tb06646.x","article-title":"Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose","volume":"13","author":"Vrielink","year":"1994","journal-title":"EMBO J"},{"key":"10.1016\/j.cbpa.2026.102758_sref38","article-title":"Structures of ALG3\/9\/12 reveal the assembly logic of the N-glycan oligomannose core","author":"Jan","year":"2026","journal-title":"Nat Chem Biol"},{"key":"10.1016\/j.cbpa.2026.102758_bib16","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1042\/BST20150177","article-title":"The reaction mechanism of retaining glycosyltransferases","volume":"44","author":"Ardevol","year":"2016","journal-title":"Biochem Soc Trans"},{"key":"10.1016\/j.cbpa.2026.102758_bib18","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1038\/s41580-020-00294-x","article-title":"Global view of human protein glycosylation pathways and functions","volume":"21","author":"Schjoldager","year":"2020","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.1016\/j.cbpa.2026.102758_bib19","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/j.sbi.2018.12.007","article-title":"Polypeptide GalNAc-Ts: from redundancy to specificity","volume":"56","author":"de Las Rivas","year":"2019","journal-title":"Curr Opin Struct Biol"},{"key":"10.1016\/j.cbpa.2026.102758_bib20","doi-asserted-by":"crossref","first-page":"8206","DOI":"10.1002\/anie.201402781","article-title":"Substrate-guided front-face reaction revealed by combined structural snapshots and metadynamics for the polypeptide N-acetylgalactosaminyltransferase 2","volume":"53","author":"Lira-Navarrete","year":"2014","journal-title":"Angew Chem Int Ed Engl"},{"key":"10.1016\/j.cbpa.2026.102758_bib21","doi-asserted-by":"crossref","first-page":"3649","DOI":"10.1021\/jacsau.4c00633","article-title":"Rational design of dual-domain binding inhibitors for N-Acetylgalactosamine transferase 2 with improved selectivity over the T1 and T3 isoforms","volume":"4","author":"Companon","year":"2024","journal-title":"JACS Au"},{"key":"10.1016\/j.cbpa.2026.102758_sref22","doi-asserted-by":"crossref","first-page":"3792","DOI":"10.1038\/s41467-024-48253-w","article-title":"A Toxoplasma gondii O-glycosyltransferase that modulates bradyzoite cyst wall rigidity is distinct from host homologues","volume":"15","author":"Kumar","year":"2024","journal-title":"Nat Commun"},{"key":"10.1016\/j.cbpa.2026.102758_bib23","doi-asserted-by":"crossref","first-page":"22636","DOI":"10.1074\/jbc.M113.528513","article-title":"Glycosylation and cross-linking in bone type I collagen","volume":"289","author":"Terajima","year":"2014","journal-title":"J Biol Chem"},{"key":"10.1016\/j.cbpa.2026.102758_bib24","doi-asserted-by":"crossref","first-page":"3624","DOI":"10.1038\/s41467-025-59017-5","article-title":"Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1\/COLGALT1","volume":"16","author":"De Marco","year":"2025","journal-title":"Nat Commun"},{"key":"10.1016\/j.cbpa.2026.102758_bib25","doi-asserted-by":"crossref","first-page":"2436","DOI":"10.1038\/s41467-025-57768-9","article-title":"The structural basis for the human procollagen lysine hydroxylation and dual-glycosylation","volume":"16","author":"Peng","year":"2025","journal-title":"Nat Commun"},{"key":"10.1016\/j.cbpa.2026.102758_bib26","doi-asserted-by":"crossref","first-page":"5064","DOI":"10.1074\/jbc.RA118.001796","article-title":"Structural basis for the glycosyltransferase activity of the Salmonella effector SseK3","volume":"293","author":"Esposito","year":"2018","journal-title":"J Biol Chem"},{"key":"10.1016\/j.cbpa.2026.102758_bib27","doi-asserted-by":"crossref","first-page":"922","DOI":"10.1016\/j.molcel.2019.03.028","article-title":"Structural and functional insights into host death domains inactivation by the bacterial arginine GlcNAcyltransferase effector","volume":"74","author":"Ding","year":"2019","journal-title":"Mol Cell"},{"key":"10.1016\/j.cbpa.2026.102758_sref28","doi-asserted-by":"crossref","first-page":"2550","DOI":"10.1021\/acscatal.5c07775","article-title":"Mechanism of bacterial arginine N-Glycosylation: a chemically challenging post-translational modification","volume":"16","author":"Piniello","year":"2026","journal-title":"ACS Catal"},{"key":"10.1016\/j.cbpa.2026.102758_bib29","first-page":"1279","volume":"vol. 5","author":"Ram\u00edrez-C\u00e1rdenas","year":"20255"},{"key":"10.1016\/j.cbpa.2026.102758_bib30","doi-asserted-by":"crossref","first-page":"5785","DOI":"10.1038\/s41467-023-41238-1","article-title":"Molecular basis for bacterial N-glycosylation by a soluble HMW1C-like N-glycosyltransferase","volume":"14","author":"Piniello","year":"2023","journal-title":"Nat Commun"},{"key":"10.1016\/j.cbpa.2026.102758_bib31","doi-asserted-by":"crossref","DOI":"10.1016\/j.cellin.2024.100211","article-title":"Roles of core fucosylation modification in immune system and diseases","volume":"4","author":"Pan","year":"2025","journal-title":"Cell Insight"},{"key":"10.1016\/j.cbpa.2026.102758_bib32","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1038\/s41467-020-14794-z","article-title":"Structural basis for substrate specificity and catalysis of alpha1,6-fucosyltransferase","volume":"11","author":"Garcia-Garcia","year":"2020","journal-title":"Nat Commun"},{"key":"10.1016\/j.cbpa.2026.102758_bib33","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-025-66871-w","article-title":"Structure, function, and implications of fucosyltransferases in health and disease","volume":"16","author":"Ghirardello","year":"2025","journal-title":"Nat Commun"},{"key":"10.1016\/j.cbpa.2026.102758_sref34","doi-asserted-by":"crossref","first-page":"3534","DOI":"10.1021\/acscatal.5c07826","article-title":"FUT8 catalysis involves GDP-Fucose-Induced loop activation promoting a reaction at the S(N)1-S(N)2 frontier","volume":"16","author":"Sanz-Martinez","year":"2026","journal-title":"ACS Catal"},{"key":"10.1016\/j.cbpa.2026.102758_bib35","doi-asserted-by":"crossref","DOI":"10.3389\/fpls.2022.897549","article-title":"Recent developments in deciphering the biological role of plant complex N-Glycans","volume":"13","author":"Strasser","year":"2022","journal-title":"Front Plant Sci"},{"key":"10.1016\/j.cbpa.2026.102758_sref36","doi-asserted-by":"crossref","first-page":"1960","DOI":"10.1038\/s41467-026-68786-6","article-title":"Plant fucosyltransferase FUT11 distorts the sugar acceptor to catalyze via a transient oxocarbenium intermediate mechanism","volume":"17","author":"Taleb","year":"2026","journal-title":"Nat Commun"},{"key":"10.1016\/j.cbpa.2026.102758_bib37","doi-asserted-by":"crossref","first-page":"10875","DOI":"10.1021\/jacs.4c11724","article-title":"Structure-Based mechanism and specificity of human galactosyltransferase beta3GalT5","volume":"147","author":"Lo","year":"2025","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2026.102758_bib39","doi-asserted-by":"crossref","first-page":"7028","DOI":"10.3390\/ijms26157028","article-title":"Hyaluronic acid and its synthases-current knowledge","volume":"26","author":"Palencarova","year":"2025","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.cbpa.2026.102758_bib40","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1038\/s41586-022-04534-2","article-title":"Structure, substrate recognition and initiation of hyaluronan synthase","volume":"604","author":"Maloney","year":"2022","journal-title":"Nature"},{"key":"10.1016\/j.cbpa.2026.102758_sref41","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1038\/s41594-024-01389-1","article-title":"Structural insights into translocation and tailored synthesis of hyaluronan","volume":"32","author":"Gorniak","year":"2025","journal-title":"Nat Struct Mol Biol"},{"key":"10.1016\/j.cbpa.2026.102758_bib42","doi-asserted-by":"crossref","first-page":"6577","DOI":"10.1021\/acscatal.4c00677","article-title":"Structural and functional analysis of Heparosan synthase 2 from Pasteurella multocida (PmHS2) to improve the synthesis of heparin","volume":"14","author":"Stancanelli","year":"2024","journal-title":"ACS Catal"},{"key":"10.1016\/j.cbpa.2026.102758_bib43","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1186\/s40643-025-00999-x","article-title":"Synthetic biology for heparin biomanufacturing","volume":"13","author":"Pan","year":"2026","journal-title":"Bioresour Bioprocess"},{"key":"10.1016\/j.cbpa.2026.102758_sref44","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1038\/s41589-024-01664-8","article-title":"Transition transferases prime bacterial capsule polymerization","volume":"21","author":"Litschko","year":"2025","journal-title":"Nat Chem Biol"},{"key":"10.1016\/j.cbpa.2026.102758_bib45","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1038\/nature11744","article-title":"Crystallographic snapshot of cellulose synthesis and membrane translocation","volume":"493","author":"Morgan","year":"2013","journal-title":"Nature"},{"key":"10.1016\/j.cbpa.2026.102758_bib46","doi-asserted-by":"crossref","first-page":"7798","DOI":"10.1038\/s41467-024-51838-0","article-title":"Insights into phosphoethanolamine cellulose synthesis and secretion across the Gram-negative cell envelope","volume":"15","author":"Verma","year":"2024","journal-title":"Nat Commun"},{"key":"10.1016\/j.cbpa.2026.102758_bib47","doi-asserted-by":"crossref","first-page":"8799","DOI":"10.1038\/s41467-024-53113-8","article-title":"Structural basis for synthase activation and cellulose modification in the E. coli Type II Bcs secretion system","volume":"15","author":"Anso","year":"2024","journal-title":"Nat Commun"},{"key":"10.1016\/j.cbpa.2026.102758_bib48","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1038\/s41594-021-00569-7","article-title":"Molecular organization of the E. coli cellulose synthase macrocomplex","volume":"28","author":"Acheson","year":"2021","journal-title":"Nat Struct Mol Biol"},{"key":"10.1016\/j.cbpa.2026.102758_bib49","doi-asserted-by":"crossref","first-page":"3331","DOI":"10.1111\/febs.17107","article-title":"A biological guide to glycosaminoglycans: current perspectives and pending questions","volume":"291","author":"Ricard-Blum","year":"2024","journal-title":"FEBS J"},{"key":"10.1016\/j.cbpa.2026.102758_sref50","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-025-66787-5","article-title":"Structural basis for human chondroitin sulfate chain polymerization","volume":"16","author":"Dutta","year":"2025","journal-title":"Nat Commun"},{"key":"10.1016\/j.cbpa.2026.102758_sref51","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-025-65968-6","article-title":"Structural basis of undecaprenyl phosphate glycosylation leading to polymyxin resistance in Gram-negative bacteria","volume":"16","author":"Ashraf","year":"2025","journal-title":"Nat Commun"}],"container-title":["Current Opinion in Chemical Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1367593126001079?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1367593126001079?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,9,9]],"date-time":"2026-09-09T20:34:50Z","timestamp":1788986090000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1367593126001079"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10]]},"references-count":52,"alternative-id":["S1367593126001079"],"URL":"https:\/\/doi.org\/10.1016\/j.cbpa.2026.102758","relation":{},"ISSN":["1367-5931"],"issn-type":[{"value":"1367-5931","type":"print"}],"subject":[],"published":{"date-parts":[[2026,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Glycosyltransferases: Capturing catalytic states and conformational gating","name":"articletitle","label":"Article Title"},{"value":"Current Opinion in Chemical Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cbpa.2026.102758","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Elsevier Ltd. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"102758"}}