{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T20:26:32Z","timestamp":1791663992223,"version":"4.3.4"},"reference-count":64,"publisher":"Elsevier BV","issue":"23","license":[{"start":{"date-parts":[[2020,6,1]],"date-time":"2020-06-01T00:00:00Z","timestamp":1590969600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,11,15]],"date-time":"2020-11-15T00:00:00Z","timestamp":1605398400000},"content-version":"vor","delay-in-days":167,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001691","name":"MEXT | Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["17K07356"],"award-info":[{"award-number":["17K07356"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"MEXT | Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["Initiative for Excellent Young Researchers"],"award-info":[{"award-number":["Initiative for Excellent Young Researchers"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003382","name":"MEXT | JST | Core Research for Evolutional Science and Technology","doi-asserted-by":"publisher","award":["18070267"],"award-info":[{"award-number":["18070267"]}],"id":[{"id":"10.13039\/501100003382","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100007449","name":"Takeda Science Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007449","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100008732","name":"Uehara Memorial Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008732","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":[[2020,6]]},"DOI":"10.1074\/jbc.ra120.013079","type":"journal-article","created":{"date-parts":[[2020,4,29]],"date-time":"2020-04-29T21:41:36Z","timestamp":1588196496000},"page":"7992-8004","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":39,"title":["The SH3 domain in the fucosyltransferase FUT8 controls FUT8 activity and localization and is essential for core fucosylation"],"prefix":"10.1016","volume":"295","author":[{"given":"Seita","family":"Tomida","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Misaki","family":"Takata","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1965-5405","authenticated-orcid":false,"given":"Tetsuya","family":"Hirata","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masamichi","family":"Nagae","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miyako","family":"Nakano","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yasuhiko","family":"Kizuka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA120.013079_bib1","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1093\/glycob\/cww086","article-title":"Biological roles of glycans","volume":"27","author":"Varki","year":"2017","journal-title":"Glycobiology"},{"key":"10.1074\/jbc.RA120.013079_bib2","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1038\/nrm3383","article-title":"Vertebrate protein glycosylation: diversity, synthesis and function","volume":"13","author":"Moremen","year":"2012","journal-title":"Nat. Rev. Mol. Cell Biol"},{"key":"10.1074\/jbc.RA120.013079_bib3","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1186\/s12014-019-9254-0","article-title":"N-GlycositeAtlas: a database resource for mass spectrometry-based human N-linked glycoprotein and glycosylation site mapping","volume":"16","author":"Sun","year":"2019","journal-title":"Clin. Proteomics"},{"key":"10.1074\/jbc.RA120.013079_bib4","series-title":"Essentials of Glycobiology","article-title":"N-glycans","author":"Stanley","year":"2017"},{"key":"10.1074\/jbc.RA120.013079_bib5","doi-asserted-by":"crossref","first-page":"1304","DOI":"10.1111\/j.1349-7006.2008.00839.x","article-title":"Functional roles of N-glycans in cell signaling and cell adhesion in cancer","volume":"99","author":"Zhao","year":"2008","journal-title":"Cancer Sci"},{"key":"10.1074\/jbc.RA120.013079_bib6","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1016\/j.cell.2006.08.019","article-title":"Glycosylation in cellular mechanisms of health and disease","volume":"126","author":"Ohtsubo","year":"2006","journal-title":"Cell"},{"key":"10.1074\/jbc.RA120.013079_bib7","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1038\/73163","article-title":"Suppression of tumor growth and metastasis in Mgat5-deficient mice","volume":"6","author":"Granovsky","year":"2000","journal-title":"Nat. Med"},{"key":"10.1074\/jbc.RA120.013079_bib8","doi-asserted-by":"crossref","first-page":"15791","DOI":"10.1073\/pnas.0507375102","article-title":"Dysregulation of TGF-\u03b21 receptor activation leads to abnormal lung development and emphysema-like phenotype in core fucose-deficient mice","volume":"102","author":"Wang","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA120.013079_bib9","doi-asserted-by":"crossref","first-page":"175","DOI":"10.15252\/emmm.201404438","article-title":"An aberrant sugar modification of BACE1 blocks its lysosomal targeting in Alzheimer's disease","volume":"7","author":"Kizuka","year":"2015","journal-title":"EMBO Mol. Med"},{"key":"10.1074\/jbc.RA120.013079_bib10","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.ceb.2016.03.021","article-title":"N-Linked glycosylation and homeostasis of the endoplasmic reticulum","volume":"41","author":"Cherepanova","year":"2016","journal-title":"Curr. Opin. Cell Biol"},{"key":"10.1074\/jbc.RA120.013079_bib11","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/S0300-9084(01)01298-6","article-title":"Structural and functional features of glycosyltransferases","volume":"83","author":"Breton","year":"2001","journal-title":"Biochimie"},{"key":"10.1074\/jbc.RA120.013079_bib12","doi-asserted-by":"crossref","first-page":"27810","DOI":"10.1074\/jbc.271.44.27810","article-title":"Purification and cDNA cloning of porcine brain GDP-l-Fuc:N-acetyl-\u03b2-d-glucosaminide \u03b11\u21926fucosyltransferase","volume":"271","author":"Uozumi","year":"1996","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013079_bib13","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1093\/oxfordjournals.jbchem.a021631","article-title":"Purification and cDNA cloning of GDP-l-Fuc:N-acetyl-\u03b2-d-glucosaminide:\u03b11\u20136 fucosyltransferase (\u03b11\u20136 FucT) from human gastric cancer MKN45 cells","volume":"121","author":"Yanagidani","year":"1997","journal-title":"J. Biochem"},{"key":"10.1074\/jbc.RA120.013079_bib14","doi-asserted-by":"crossref","first-page":"2572","DOI":"10.1074\/jbc.M510893200","article-title":"Core fucosylation regulates epidermal growth factor receptor-mediated intracellular signaling","volume":"281","author":"Wang","year":"2006","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013079_bib15","doi-asserted-by":"crossref","first-page":"1620","DOI":"10.1053\/j.gastro.2016.03.002","article-title":"Core fucosylation on T cells, required for activation of T-cell receptor signaling and induction of colitis in mice, is increased in patients with inflammatory bowel disease","volume":"150","author":"Fujii","year":"2016","journal-title":"Gastroenterology"},{"key":"10.1074\/jbc.RA120.013079_bib16","doi-asserted-by":"crossref","first-page":"17566","DOI":"10.1074\/jbc.M114.579938","article-title":"Loss of \u03b11,6-fucosyltransferase decreases hippocampal long term potentiation: implications for core fucosylation in the regulation of AMPA receptor heteromerization and cellular signaling","volume":"290","author":"Gu","year":"2015","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013079_bib17","doi-asserted-by":"crossref","first-page":"804","DOI":"10.1016\/j.ccell.2017.05.007","article-title":"A systems biology approach identifies FUT8 as a driver of melanoma metastasis","volume":"31","author":"Agrawal","year":"2017","journal-title":"Cancer Cell"},{"key":"10.1074\/jbc.RA120.013079_bib18","doi-asserted-by":"crossref","first-page":"3466","DOI":"10.1074\/jbc.M210665200","article-title":"The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity","volume":"278","author":"Shinkawa","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013079_bib19","first-page":"203","article-title":"Overexpression of \u03b11,6-fucosyltransferase in hepatoma enhances expression of Golgi phosphoprotein 2 in a fucosylation-independent manner","volume":"39","author":"Kawamoto","year":"2011","journal-title":"Int. J. Oncol"},{"key":"10.1074\/jbc.RA120.013079_bib20","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1093\/glycob\/cwl079","article-title":"Crystal structure of mammalian \u03b11,6-fucosyltransferase, FUT8","volume":"17","author":"Ihara","year":"2007","journal-title":"Glycobiology"},{"key":"10.1074\/jbc.RA120.013079_bib21","doi-asserted-by":"crossref","first-page":"2619","DOI":"10.1016\/j.febslet.2012.04.057","article-title":"Interfacial water molecules in SH3 interactions: getting the full picture on polyproline recognition by protein-protein interaction domains","volume":"586","author":"Zafra-Ruano","year":"2012","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.RA120.013079_bib22","doi-asserted-by":"crossref","first-page":"33973","DOI":"10.1074\/jbc.M111.327692","article-title":"A novel core fucose-specific lectin from the mushroom Pholiota squarrosa","volume":"287","author":"Kobayashi","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013079_bib23","doi-asserted-by":"crossref","first-page":"2352","DOI":"10.1105\/tpc.16.00519","article-title":"Structure of Arabidopsis thaliana FUT1 reveals a variant of the GT-B class fold and provides insight into xyloglucan fucosylation","volume":"28","author":"Rocha","year":"2016","journal-title":"Plant Cell"},{"key":"10.1074\/jbc.RA120.013079_bib24","doi-asserted-by":"crossref","first-page":"E6074","DOI":"10.3390\/ijms20236074","article-title":"Oligosaccharyltransferase: a gatekeeper of health and tumor progression","volume":"20","author":"Harada","year":"2019","journal-title":"Int. J. Mol. Sci"},{"key":"10.1074\/jbc.RA120.013079_bib25","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1093\/glycob\/cwy093","article-title":"Oligosaccharyltransferase structures provide novel insight into the mechanism of asparagine-linked glycosylation in prokaryotic and eukaryotic cells","volume":"29","author":"Shrimal","year":"2019","journal-title":"Glycobiology"},{"key":"10.1074\/jbc.RA120.013079_bib26","doi-asserted-by":"crossref","first-page":"1372","DOI":"10.1126\/science.aaz3505","article-title":"Cryo-electron microscopy structures of human oligosaccharyltransferase complexes OST-A and OST-B","volume":"366","author":"Ram\u00edrez","year":"2019","journal-title":"Science"},{"key":"10.1074\/jbc.RA120.013079_bib27","doi-asserted-by":"crossref","first-page":"9534","DOI":"10.1073\/pnas.0711846105","article-title":"Ribophorin I regulates substrate delivery to the oligosaccharyltransferase core","volume":"105","author":"Wilson","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA120.013079_bib28","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1242\/jcs.000729","article-title":"Ribophorin I acts as a substrate-specific facilitator of N-glycosylation","volume":"120","author":"Wilson","year":"2007","journal-title":"J. Cell Sci"},{"key":"10.1074\/jbc.RA120.013079_bib29","doi-asserted-by":"crossref","first-page":"1830","DOI":"10.1021\/cb400140u","article-title":"Donor assists acceptor binding and catalysis of human \u03b11,6-fucosyltransferase","volume":"8","author":"K\u00f6tzler","year":"2013","journal-title":"ACS Chem. Biol"},{"key":"10.1074\/jbc.RA120.013079_bib30","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1038\/s41467-020-14794-z","article-title":"Structural basis for substrate specificity and catalysis of \u03b11,6-fucosyltransferase","volume":"11","author":"Garc\u00eda-Garc\u00eda","year":"2020","journal-title":"Nat. Commun"},{"key":"10.1074\/jbc.RA120.013079_bib31","doi-asserted-by":"crossref","first-page":"6677","DOI":"10.1074\/jbc.RA120.013291","article-title":"Structural basis of substrate recognition and catalysis by fucosyltransferase 8","volume":"295","author":"J\u00e4rv\u00e5","year":"2020","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013079_bib32","doi-asserted-by":"crossref","first-page":"129596","DOI":"10.1016\/j.bbagen.2020.129596","article-title":"Involvement of the \u03b1-helical and Src homology 3 domains in the molecular assembly and enzymatic activity of human \u03b11,6-fucosyltransferase, FUT8","volume":"1864","author":"Ihara","year":"2020","journal-title":"Biochim. Biophys. Acta Gen. Subj"},{"key":"10.1074\/jbc.RA120.013079_bib33","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1016\/S0006-291X(76)80218-5","article-title":"The control of glycoprotein synthesis: N-acetylgluocosamine linkage to a mannose residue as a signal for the attachment of l-fucose to the asparagine-linked N-acetylglucosamine residue of glycopeptide from \u03b11-acid glycoprotein","volume":"72","author":"Wilson","year":"1976","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.RA120.013079_bib34","doi-asserted-by":"crossref","first-page":"14796","DOI":"10.1074\/jbc.M117.804070","article-title":"Revisiting the substrate specificity of mammalian \u03b11,6-fucosyltransferase reveals that it catalyzes core fucosylation of N-glycans lacking \u03b11,3-arm GlcNAc","volume":"292","author":"Yang","year":"2017","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013079_bib35","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1126\/science.aar7899","article-title":"Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum","volume":"360","author":"Braunger","year":"2018","journal-title":"Science"},{"key":"10.1074\/jbc.RA120.013079_bib36","doi-asserted-by":"crossref","first-page":"6945","DOI":"10.1073\/pnas.0812489106","article-title":"Oligosaccharyltransferase directly binds to ribosome at a location near the translocon-binding site","volume":"106","author":"Harada","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA120.013079_bib37","doi-asserted-by":"crossref","first-page":"38080","DOI":"10.1074\/jbc.M112.394288","article-title":"Malectin forms a complex with ribophorin I for enhanced association with misfolded glycoproteins","volume":"287","author":"Qin","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013079_bib38","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1016\/j.bbrc.2014.10.102","article-title":"Association of malectin with ribophorin I is crucial for attenuation of misfolded glycoprotein secretion","volume":"454","author":"Takeda","year":"2014","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.RA120.013079_bib39","doi-asserted-by":"crossref","first-page":"a005264","DOI":"10.1101\/cshperspect.a005264","article-title":"Mechanisms of protein retention in the Golgi","volume":"3","author":"Banfield","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol"},{"key":"10.1074\/jbc.RA120.013079_bib40","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1083\/jcb.117.2.245","article-title":"The 17-residue transmembrane domain of \u03b2-galactoside \u03b12,6-sialyltransferase is sufficient for Golgi retention","volume":"117","author":"Wong","year":"1992","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.RA120.013079_bib41","doi-asserted-by":"crossref","first-page":"4695","DOI":"10.1002\/j.1460-2075.1995.tb00151.x","article-title":"An investigation of the role of transmembrane domains in Golgi protein retention","volume":"14","author":"Munro","year":"1995","journal-title":"EMBO J"},{"key":"10.1074\/jbc.RA120.013079_bib42","doi-asserted-by":"crossref","first-page":"3577","DOI":"10.1002\/j.1460-2075.1991.tb04924.x","article-title":"Sequences within and adjacent to the transmembrane segment of \u03b1-2,6-sialyltransferase specify Golgi retention","volume":"10","author":"Munro","year":"1991","journal-title":"EMBO J"},{"key":"10.1074\/jbc.RA120.013079_bib43","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1002\/bies.950170313","article-title":"Biological consequences of targeting \u03b21,4-galactosyltransferase to two different subcellular compartments","volume":"17","author":"Evans","year":"1995","journal-title":"Bioessays"},{"key":"10.1074\/jbc.RA120.013079_bib44","doi-asserted-by":"crossref","first-page":"31437","DOI":"10.1074\/jbc.M111.257196","article-title":"Trans-activity of plasma membrane-associated ganglioside sialyltransferase in mammalian cells","volume":"286","author":"Vilcaes","year":"2011","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013079_bib45","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1002\/mrd.1120220309","article-title":"Expression and topographical localization of cell surface fucosyltransferase activity during epididymal sperm maturation in the mouse","volume":"22","author":"Ram","year":"1989","journal-title":"Gamete Res"},{"key":"10.1074\/jbc.RA120.013079_bib46","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/j.sbi.2004.09.006","article-title":"Structure and catalytic cycle of \u03b2-1,4-galactosyltransferase","volume":"14","author":"Ramakrishnan","year":"2004","journal-title":"Curr. Opin. Struct. Biol"},{"key":"10.1074\/jbc.RA120.013079_bib47","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1083\/jcb.113.3.637","article-title":"Laminin fragment E8 mediates PC12 cell neurite outgrowth by binding to cell surface \u03b21,4-galactosyltransferase","volume":"113","author":"Begovac","year":"1991","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.RA120.013079_bib48","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1038\/357589a0","article-title":"Complementarity between sperm surface \u03b2-l,4-galactosyl-transferase and egg-coat ZP3 mediates sperm-egg binding","volume":"357","author":"Miller","year":"1992","journal-title":"Nature"},{"key":"10.1074\/jbc.RA120.013079_bib49","doi-asserted-by":"crossref","first-page":"4121","DOI":"10.1242\/dev.124.20.4121","article-title":"Sperm from \u03b21,4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reactions and penetrate the zona pellucida poorly","volume":"124","author":"Lu","year":"1997","journal-title":"Development"},{"key":"10.1074\/jbc.RA120.013079_bib50","doi-asserted-by":"crossref","first-page":"4319","DOI":"10.1242\/jcs.00720","article-title":"Mutational analysis of the cytoplasmic domain of \u03b21,4-galactosyltransferase I: influence of phosphorylation on cell surface expression","volume":"116","author":"Hathaway","year":"2003","journal-title":"J. Cell Sci"},{"key":"10.1074\/jbc.RA120.013079_bib51","doi-asserted-by":"crossref","first-page":"14383","DOI":"10.1074\/jbc.RA119.009539","article-title":"Assembly of B4GALT1\/ST6GAL1 heteromers in the Golgi membranes involves lateral interactions via highly charged surface domains","volume":"294","author":"Khoder-Agha","year":"2019","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013079_bib52","doi-asserted-by":"crossref","first-page":"17771","DOI":"10.1074\/jbc.M110.103184","article-title":"Golgi N-glycosyltransferases form both homo- and heterodimeric enzyme complexes in live cells","volume":"285","author":"Hassinen","year":"2010","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013079_bib53","doi-asserted-by":"crossref","first-page":"13644","DOI":"10.1074\/jbc.M601453200","article-title":"Physical and functional association of glucuronyltransferases and sulfotransferase involved in HNK-1 biosynthesis","volume":"281","author":"Kizuka","year":"2006","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013079_bib54","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1093\/glycob\/cwi082","article-title":"Characterization of a novel galactose \u03b21,3-N-acetylglucosaminyltransferase (\u03b23Gn-T8): the complex formation of \u03b23Gn-T2 and \u03b23Gn-T8 enhances enzymatic activity","volume":"15","author":"Seko","year":"2005","journal-title":"Glycobiology"},{"key":"10.1074\/jbc.RA120.013079_bib55","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1073\/pnas.97.2.668","article-title":"The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate","volume":"97","author":"McCormick","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA120.013079_bib56","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":"10.1074\/jbc.RA120.013079_bib57","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1093\/glycob\/cwx034","article-title":"Biological functions of fucose in mammals","volume":"27","author":"Schneider","year":"2017","journal-title":"Glycobiology"},{"key":"10.1074\/jbc.RA120.013079_bib58","doi-asserted-by":"crossref","first-page":"2256","DOI":"10.1107\/S0907444904026460","article-title":"Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions","volume":"60","author":"Krissinel","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA120.013079_bib59","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1016\/j.chembiol.2017.08.023","article-title":"An alkynyl-fucose halts hepatoma cell migration and invasion by inhibiting GDP-fucose-synthesizing enzyme FX, TSTA3","volume":"24","author":"Kizuka","year":"2017","journal-title":"Cell Chem. Biol"},{"key":"10.1074\/jbc.RA120.013079_bib60","doi-asserted-by":"crossref","first-page":"782","DOI":"10.1016\/j.chembiol.2016.06.010","article-title":"High-sensitivity and low-toxicity fucose probe for glycan imaging and biomarker discovery","volume":"23","author":"Kizuka","year":"2016","journal-title":"Cell Chem. Biol"},{"key":"10.1074\/jbc.RA120.013079_bib61","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1093\/oxfordjournals.jbchem.a021424","article-title":"A fluorescent assay method for GDP-l-Fuc:N-acetyl-\u03b2-d-glucosaminide \u03b11\u20136fucosyltransferase activity, involving high performance liquid chromatography","volume":"120","author":"Uozumi","year":"1996","journal-title":"J. Biochem"},{"key":"10.1074\/jbc.RA120.013079_bib62","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.M111.009001","article-title":"Identification of glycan structure alterations on cell membrane proteins in desoxyepothilone B resistant leukemia cells","volume":"10","author":"Nakano","year":"2011","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/jbc.RA120.013079_bib63","doi-asserted-by":"crossref","first-page":"2854","DOI":"10.1002\/pmic.201600053","article-title":"Epigenetic regulation of neural N-glycomics","volume":"16","author":"Kizuka","year":"2016","journal-title":"Proteomics"},{"key":"10.1074\/jbc.RA120.013079_bib64","doi-asserted-by":"crossref","first-page":"2044","DOI":"10.1074\/mcp.RA119.001534","article-title":"Bisecting GlcNAc is a general suppressor of terminal modification of N-glycan","volume":"18","author":"Nakano","year":"2019","journal-title":"Mol. Cell. Proteomics"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925817494385?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925817494385?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA120.013079","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,12,31]],"date-time":"2021-12-31T11:16:34Z","timestamp":1640949394000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925817494385"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,6]]},"references-count":64,"journal-issue":{"issue":"23","published-print":{"date-parts":[[2020,6]]}},"alternative-id":["S0021925817494385"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra120.013079","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2020,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The SH3 domain in the fucosyltransferase FUT8 controls FUT8 activity and localization and is essential for core fucosylation","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA120.013079","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Tomida et al.","name":"copyright","label":"Copyright"}]}}