{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T11:36:19Z","timestamp":1793100979040,"version":"4.5.0"},"reference-count":54,"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":[[2026,10,6]],"date-time":"2026-10-06T00:00:00Z","timestamp":1791244800000},"content-version":"vor","delay-in-days":5,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["22K14817"],"award-info":[{"award-number":["22K14817"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["19K05835"],"award-info":[{"award-number":["19K05835"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["21K05373"],"award-info":[{"award-number":["21K05373"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2026,10]]},"DOI":"10.1016\/j.jbc.2026.113626","type":"journal-article","created":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T06:44:08Z","timestamp":1791441848000},"page":"113626","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["Structural and biochemical basis for the formation of \u03b1-(1\u21923)-linked mannose residue in O-glycans of Saccharomyces cerevisiae"],"prefix":"10.1016","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1126-3725","authenticated-orcid":false,"given":"Daisuke","family":"Hira","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chihiro","family":"Kadooka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takuji","family":"Oka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2026.113626_bib1","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1534\/genetics.112.144485","article-title":"Architecture and biosynthesis of the Saccharomyces cerevisiae cell wall","volume":"192","author":"Orlean","year":"2012","journal-title":"Genetics"},{"key":"10.1016\/j.jbc.2026.113626_bib2","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/S0304-4165(98)00131-7","article-title":"Protein O-mannosylation","volume":"1426","author":"Strahl-Bolsinger","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2026.113626_bib3","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/S0304-4165(98)00134-2","article-title":"Mannosylphosphate transfer to yeast mannan","volume":"1426","author":"Jigami","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2026.113626_bib4","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/S0304-4165(98)00133-0","article-title":"The KTR and MNN1 mannosyltransferase families of Saccharomyces cerevisiae","volume":"1426","author":"Lussier","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2026.113626_bib5","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/j.ceb.2016.04.010","article-title":"Protein O-mannosylation in the early secretory pathway","volume":"41","author":"Neubert","year":"2016","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113626_bib6","doi-asserted-by":"crossref","first-page":"17499","DOI":"10.1016\/S0021-9258(19)77863-6","article-title":"Cloning and sequencing of the yeast gene for dolichol phosphate mannose synthase, an essential protein","volume":"263","author":"Orlean","year":"1988","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113626_bib7","doi-asserted-by":"crossref","first-page":"8164","DOI":"10.1073\/pnas.90.17.8164","article-title":"PMT1, the gene for a key enzyme of protein O-glycosylation in Saccharomyces cerevisiae","volume":"90","author":"Strahl-Bolsinger","year":"1993","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113626_bib8","doi-asserted-by":"crossref","first-page":"6846","DOI":"10.1073\/pnas.89.15.6846","article-title":"Yeast glycoprotein biosynthesis: MNT1 encodes an alpha-1,2-mannosyltransferase involved in O-glycosylation","volume":"89","author":"Hausler","year":"1992","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113626_bib9","doi-asserted-by":"crossref","first-page":"15527","DOI":"10.1074\/jbc.272.24.15527","article-title":"The Ktr1p, Ktr3p, and Kre2p\/Mnt1p mannosyltransferases participate in the elaboration of yeast O- and N-linked carbohydrate chains","volume":"272","author":"Lussier","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113626_bib10","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1093\/glycob\/9.10.1045","article-title":"Mnt2p and Mnt3p of Saccharomyces cerevisiae are members of the Mnn1p family of alpha-1,3-mannosyltransferases responsible for adding the terminal mannose residues of O-linked oligosaccharides","volume":"9","author":"Romero","year":"1999","journal-title":"Glycobiology"},{"key":"10.1016\/j.jbc.2026.113626_bib11","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1093\/glycob\/6.8.805","article-title":"Cloning and analysis of the MNN4 gene required for phosphorylation of N-linked oligosaccharides in Saccharomyces cerevisiae","volume":"6","author":"Odani","year":"1996","journal-title":"Glycobiology"},{"key":"10.1016\/j.jbc.2026.113626_bib12","doi-asserted-by":"crossref","first-page":"2979","DOI":"10.1007\/s00253-017-8101-3","article-title":"Abolishment of N-glycan mannosylphosphorylation in glyco-engineered Saccharomyces cerevisiae by double disruption of MNN4 and MNN14 genes","volume":"101","author":"Kim","year":"2017","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.jbc.2026.113626_bib13","doi-asserted-by":"crossref","first-page":"26836","DOI":"10.1074\/jbc.273.41.26836","article-title":"Identification of the MNN2 and MNN5 mannosyltransferases required for forming and extending the mannose branches of the outer chain mannans of Saccharomyces cerevisiae","volume":"273","author":"Rayner","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113626_bib14","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.jbc.2026.113626_bib15","doi-asserted-by":"crossref","first-page":"17921","DOI":"10.1074\/jbc.M312720200","article-title":"Structure of Kre2p\/Mnt1p: a yeast alpha1,2-mannosyltransferase involved in mannoprotein biosynthesis","volume":"279","author":"Lobsanov","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113626_bib16","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0136239","article-title":"Structure of the glycosyltransferase Ktr4p from Saccharomyces cerevisiae","volume":"10","author":"Possner","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2026.113626_bib17","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-018-35059-2","article-title":"Identification of two mannosyltransferases contributing to biosynthesis of the fungal-type galactomannan alpha-core-mannan structure in Aspergillus fumigatus","volume":"8","author":"Onoue","year":"2018","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2026.113626_bib18","doi-asserted-by":"crossref","first-page":"15407","DOI":"10.1074\/jbc.RA120.013742","article-title":"Structural basis for the core-mannan biosynthesis of cell wall fungal-type galactomannan in Aspergillus fumigatus","volume":"295","author":"Hira","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113626_bib19","doi-asserted-by":"crossref","DOI":"10.1098\/rsob.130022","article-title":"Yeast Mnn9 is both a priming glycosyltransferase and an allosteric activator of mannan biosynthesis","volume":"3","author":"Striebeck","year":"2013","journal-title":"Open Biol"},{"key":"10.1016\/j.jbc.2026.113626_bib20","doi-asserted-by":"crossref","first-page":"180","DOI":"10.2323\/jgam.2018.09.001","article-title":"Svp26 facilitates ER exit of mannosyltransferases Mnt2 and Mnt3 in Saccharomyces cerevisiae","volume":"65","author":"Tanabe","year":"2019","journal-title":"J. Gen. Appl. Microbiol."},{"key":"10.1016\/j.jbc.2026.113626_bib21","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1002\/bip.360221211","article-title":"Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features","volume":"22","author":"Kabsch","year":"1983","journal-title":"Biopolymers"},{"key":"10.1016\/j.jbc.2026.113626_bib22","doi-asserted-by":"crossref","first-page":"5326","DOI":"10.1093\/bioinformatics\/btz536","article-title":"Benchmarking fold detection by DaliLite v.5","volume":"35","author":"Holm","year":"2019","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jbc.2026.113626_bib23","doi-asserted-by":"crossref","first-page":"8544","DOI":"10.1073\/pnas.1703682114","article-title":"Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint","volume":"114","author":"Roversi","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113626_bib24","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1038\/s41589-020-0494-0","article-title":"A bifunctional O-antigen polymerase structure reveals a new glycosyltransferase family","volume":"16","author":"Clarke","year":"2020","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jbc.2026.113626_bib25","doi-asserted-by":"crossref","first-page":"23892","DOI":"10.1074\/jbc.M502344200","article-title":"Requirements for catalysis in mammalian glycogenin","volume":"280","author":"Hurley","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113626_bib26","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.102212","article-title":"Modularity of the hydrophobic core and evolution of functional diversity in fold A glycosyltransferases","volume":"298","author":"Venkat","year":"2022","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113626_bib27","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1146\/annurev.biochem.76.061005.092322","article-title":"Glycosyltransferases: structures, functions, and mechanisms","volume":"77","author":"Lairson","year":"2008","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.jbc.2026.113626_bib28","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1016\/j.sbi.2012.06.007","article-title":"Recent structures, evolution and mechanisms of glycosyltransferases","volume":"22","author":"Breton","year":"2012","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.jbc.2026.113626_bib29","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1038\/nchembio.628","article-title":"Mechanistic evidence for a front-side, SNi-type reaction in a retaining glycosyltransferase","volume":"7","author":"Lee","year":"2011","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jbc.2026.113626_bib30","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.jbc.2026.113626_bib31","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1042\/BJ20070081","article-title":"Chemical structure of the cell-wall mannan of Candida albicans serotype A and its difference in yeast and hyphal forms","volume":"404","author":"Shibata","year":"2007","journal-title":"Biochem. J."},{"key":"10.1016\/j.jbc.2026.113626_bib32","doi-asserted-by":"crossref","DOI":"10.1128\/microbiolspec.FUNK-0035-2016","article-title":"The fungal cell wall: structure, biosynthesis, and function","volume":"5","author":"Gow","year":"2017","journal-title":"Microbiol. Spectr."},{"key":"10.1016\/j.jbc.2026.113626_bib33","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1074\/jbc.M411413200","article-title":"Mnt1p and Mnt2p of Candida albicans are partially redundant alpha-1,2-mannosyltransferases that participate in O-linked mannosylation and are required for adhesion and virulence","volume":"280","author":"Munro","year":"2005","journal-title":"J. Biol. Chem."},{"issue":"5","key":"10.1016\/j.jbc.2026.113626_bib34","article-title":"An improved expression and purification protocol enables the structural characterization of Mnt1, an antifungal target from Candida albicans","volume":"11","author":"Silva","year":"2024","journal-title":"Fungal Biol. Biotechnol."},{"key":"10.1016\/j.jbc.2026.113626_bib35","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/j.copbio.2007.09.001","article-title":"Glycosylation engineering in yeast: the advent of fully humanized yeast","volume":"18","author":"Hamilton","year":"2007","journal-title":"Curr. Opin. Biotechnol."},{"key":"10.1016\/j.jbc.2026.113626_bib36","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1007\/978-1-4939-2760-9_8","article-title":"Engineering the Pichia pastoris N-glycosylation pathway using the GlycoSwitch technology","volume":"1321","author":"Laukens","year":"2015","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.jbc.2026.113626_bib37","doi-asserted-by":"crossref","first-page":"568","DOI":"10.1093\/glycob\/cwx028","article-title":"GfsA is a \u03b21,5-galactofuranosyltransferase involved in the biosynthesis of the galactofuran side chain of fungal-type galactomannan in Aspergillus fumigatus","volume":"27","author":"Katafuchi","year":"2017","journal-title":"Glycobiology"},{"key":"10.1016\/j.jbc.2026.113626_bib38","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"XDS","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113626_bib39","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1107\/S0907444909042589","article-title":"Molecular replacement with MOLREP","volume":"66","author":"Vagin","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113626_bib40","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1107\/S0907444994003112","article-title":"The CCP4 suite: programs for protein crystallography","volume":"50","year":"1994","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113626_bib41","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.113626_bib42","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1107\/S0907444911001314","article-title":"REFMAC5 for the refinement of macromolecular crystal structures","volume":"67","author":"Murshudov","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113626_bib43","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113626_bib44","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1107\/S0021889892009944","article-title":"PROCHECK: a program to check the stereochemical quality of protein structures","volume":"26","author":"Laskowski","year":"1993","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113626_bib45","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all-atom structure validation for macromolecular crystallography","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113626_bib46","unstructured":"DeLano, W. L. (2002) The PyMOL Molecular Graphics System, DeLano Scientific, San Carlos, CA"},{"key":"10.1016\/j.jbc.2026.113626_bib47","doi-asserted-by":"crossref","first-page":"2785","DOI":"10.1002\/jcc.21256","article-title":"AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility","volume":"30","author":"Morris","year":"2009","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jbc.2026.113626_bib48","first-page":"622","article-title":"GLYCAM06: a generalizable biomolecular force field","volume":"29","author":"Kirschner","year":"2008","journal-title":"Carbohydrates. J. Comput. Chem."},{"key":"10.1016\/j.jbc.2026.113626_bib49","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.softx.2015.06.001","article-title":"GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers","volume":"1-2","author":"Abraham","year":"2015","journal-title":"SoftwareX"},{"key":"10.1016\/j.jbc.2026.113626_bib50","doi-asserted-by":"crossref","first-page":"3696","DOI":"10.1021\/acs.jctc.5b00255","article-title":"ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB","volume":"11","author":"Maier","year":"2015","journal-title":"J. Chem. Theory Comput."},{"key":"10.1016\/j.jbc.2026.113626_bib51","doi-asserted-by":"crossref","first-page":"5535","DOI":"10.1021\/ja983854g","article-title":"Potential energy hypersurfaces of nucleotide sugars: ab initio calculations, force-field parametrization, and exploration of the flexibility","volume":"121","author":"Petrov\u00e1","year":"1999","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2026.113626_bib52","unstructured":"Case, D. A., Cerutti, D. S., Cheatham, T. E., III, Darden, T. A., Duke, R. E., Giese, T. J., Gohlke, H., Goetz, A. W., Greene, D., Homeyer, N., Izadi, S., Kovalenko, A., Lee, T. S., LeGrand, S., Li, P., et al. (2017) AMBER 2017 Reference Manual, University of California, San Francisco"},{"key":"10.1016\/j.jbc.2026.113626_bib53","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1186\/1756-0500-5-367","article-title":"ACPYPE - AnteChamber PYthon Parser interfacE","volume":"5","author":"Sousa da Silva","year":"2012","journal-title":"BMC Res. Notes"},{"key":"10.1016\/j.jbc.2026.113626_bib54","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: visual molecular dynamics","volume":"14","author":"Humphrey","year":"1996","journal-title":"J. Mol. Graph."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826024981?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826024981?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T11:21:14Z","timestamp":1793100074000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925826024981"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10]]},"references-count":54,"alternative-id":["S0021925826024981"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113626","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2026,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural and biochemical basis for the formation of \u03b1-(1\u21923)-linked mannose residue in O-glycans of Saccharomyces cerevisiae","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113626","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"113626"}}