{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T22:46:20Z","timestamp":1789512380644,"version":"build-2803163510"},"reference-count":60,"publisher":"eLife Sciences Publications, Ltd","license":[{"start":{"date-parts":[[2016,4,29]],"date-time":"2016-04-29T00:00:00Z","timestamp":1461888000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2016,4,29]],"date-time":"2016-04-29T00:00:00Z","timestamp":1461888000000},"content-version":"am","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2016,4,29]],"date-time":"2016-04-29T00:00:00Z","timestamp":1461888000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["U54NS053672"],"award-info":[{"award-number":["U54NS053672"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100005202","name":"Muscular Dystrophy Association","doi-asserted-by":"publisher","award":["238219"],"award-info":[{"award-number":["238219"]}],"id":[{"id":"10.13039\/100005202","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01GM111939"],"award-info":[{"award-number":["R01GM111939"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["P41GM103390"],"award-info":[{"award-number":["P41GM103390"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000011","name":"Howard Hughes Medical Institute","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000011","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["P01GM107012"],"award-info":[{"award-number":["P01GM107012"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["P41GM103490"],"award-info":[{"award-number":["P41GM103490"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["RC2 NS069521-01"],"award-info":[{"award-number":["RC2 NS069521-01"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elifesciences.org"],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:p>\n                    Multiple glycosyltransferases are essential for the proper modification of alpha-dystroglycan, as mutations in the encoding genes cause congenital\/limb-girdle muscular dystrophies. Here we elucidate further the structure of an\n                    <jats:italic>O<\/jats:italic>\n                    -mannose-initiated glycan on alpha-dystroglycan that is required to generate its extracellular matrix-binding polysaccharide. This functional glycan contains a novel ribitol structure that links a phosphotrisaccharide to xylose. ISPD is a CDP-ribitol (ribose) pyrophosphorylase that generates the reduced sugar nucleotide for the insertion of ribitol in a phosphodiester linkage to the glycoprotein. TMEM5 is a UDP-xylosyl transferase that elaborates the structure. We demonstrate in a zebrafish model as well as in a human patient that defects in TMEM5 result in muscular dystrophy in combination with abnormal brain development. Thus, we propose a novel structure\u2014a ribitol in a phosphodiester linkage\u2014for the moiety on which TMEM5, B4GAT1, and LARGE act to generate the functional receptor for ECM proteins having LG domains.\n                  <\/jats:p>","DOI":"10.7554\/elife.14473","type":"journal-article","created":{"date-parts":[[2016,4,29]],"date-time":"2016-04-29T08:05:45Z","timestamp":1461917145000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.14473","source":"Crossref","is-referenced-by-count":115,"title":["The functional O-mannose glycan on \u03b1-dystroglycan contains a phospho-ribitol primed for matriglycan addition"],"prefix":"10.7554","volume":"5","author":[{"given":"Jeremy L","family":"Praissman","sequence":"first","affiliation":[{"name":"Complex Carbohydrate Research Center, University of Georgia, Athens, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tobias","family":"Willer","sequence":"additional","affiliation":[{"name":"Department of Molecular Physiology and Biophysics, Carver College of Medicine, University of Iowa, Iowa City, United States"},{"name":"Howard Hughes Medical Institute, University of Iowa, Iowa City, United States"},{"name":"Department of Neurology, Carver College of Medicine, University of Iowa, Iowa City, United States"},{"name":"Department of Internal Medicine, Carver College of Medicine, University of Iowa, Iowa City, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9481-8318","authenticated-orcid":true,"given":"M Osman","family":"Sheikh","sequence":"additional","affiliation":[{"name":"Complex Carbohydrate Research Center, University of Georgia, Athens, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ants","family":"Toi","sequence":"additional","affiliation":[{"name":"Department of Medical Imaging, Mount Sinai Hospital, Toronto, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Chitayat","sequence":"additional","affiliation":[{"name":"Division of Clinical and Metabolic Genetics, The Hospital for Sick Children, University of Toronto, Toronto, Canada"},{"name":"The Prenatal Diagnosis and Medical Genetics Program, Mount Sinai Hospital, Toronto, Canada"},{"name":"Department of Obstetrics and Gynecology, University of Toronto, Toronto, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0435-7694","authenticated-orcid":true,"given":"Yung-Yao","family":"Lin","sequence":"additional","affiliation":[{"name":"Blizard Institute, London, United Kingdom"},{"name":"Barts and The London School of Medicine and Dentistry, Queen Mary University of London, London, United Kingdom"},{"name":"Wellcome Trust Genome Campus, Wellcome Trust Sanger Institute, Hinxton, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hane","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Human Genetics, University of California, Los Angeles, Los Angeles, United States"},{"name":"David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United States"},{"name":"Department of Pathology and Laboratory Medicine, University of California, Los Angeles, Los Angeles, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephanie H","family":"Stalnaker","sequence":"additional","affiliation":[{"name":"Complex Carbohydrate Research Center, University of Georgia, Athens, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shuo","family":"Wang","sequence":"additional","affiliation":[{"name":"Complex Carbohydrate Research Center, University of Georgia, Athens, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pradeep Kumar","family":"Prabhakar","sequence":"additional","affiliation":[{"name":"Complex Carbohydrate Research Center, University of Georgia, Athens, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stanley F","family":"Nelson","sequence":"additional","affiliation":[{"name":"Department of Human Genetics, University of California, Los Angeles, Los Angeles, United States"},{"name":"David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United States"},{"name":"Department of Pathology and Laboratory Medicine, University of California, Los Angeles, Los Angeles, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Derek L","family":"Stemple","sequence":"additional","affiliation":[{"name":"Wellcome Trust Genome Campus, Wellcome Trust Sanger Institute, Hinxton, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven A","family":"Moore","sequence":"additional","affiliation":[{"name":"Department of Pathology, Carver College of Medicine, University of Iowa, Iowa City, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kelley W","family":"Moremen","sequence":"additional","affiliation":[{"name":"Complex Carbohydrate Research Center, University of Georgia, Athens, United States"},{"name":"Department of Biochemistry and Molecular Biology, University of Georgia, Athens, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2066-5889","authenticated-orcid":true,"given":"Kevin P","family":"Campbell","sequence":"additional","affiliation":[{"name":"Department of Molecular Physiology and Biophysics, Carver College of Medicine, University of Iowa, Iowa City, United States"},{"name":"Howard Hughes Medical Institute, University of Iowa, Iowa City, United States"},{"name":"Department of Neurology, Carver College of Medicine, University of Iowa, Iowa City, United States"},{"name":"Department of Internal Medicine, Carver College of Medicine, University of Iowa, Iowa City, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4956-5363","authenticated-orcid":true,"given":"Lance","family":"Wells","sequence":"additional","affiliation":[{"name":"Complex Carbohydrate Research Center, University of Georgia, Athens, United States"},{"name":"Department of Biochemistry and Molecular Biology, University of Georgia, Athens, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"4374","published-online":{"date-parts":[[2016,4,29]]},"reference":[{"key":"bib1","doi-asserted-by":"publisher","first-page":"7.20.1","DOI":"10.1002\/0471142905.hg0720s76","article-title":"Predicting functional effect of human missense mutations using polyphen-2","volume":"20","author":"Adzhubei","year":"2013","journal-title":"Curr Protoc Hum Genet Chapter 7, Unit 7"},{"key":"bib2","doi-asserted-by":"publisher","first-page":"599","DOI":"10.1042\/bj0640599","article-title":"The isolation of cytidine diphosphate glycerol, cytidine diphosphate ribitol and mannitol 1-phosphate from lactobacillus arabinosus","volume":"64","author":"Baddiley","year":"1956","journal-title":"The Biochemical Journal"},{"key":"bib3","doi-asserted-by":"publisher","first-page":"4618","DOI":"10.1021\/bi300319q","article-title":"NMR characterization of immunoglobulin G fc glycan motion on enzymatic sialylation","volume":"51","author":"Barb","year":"2012","journal-title":"Biochemistry"},{"key":"bib4","doi-asserted-by":"publisher","first-page":"696","DOI":"10.1038\/nm1059","article-title":"LARGE can functionally bypass alpha-dystroglycan glycosylation defects in distinct congenital muscular dystrophies","volume":"10","author":"Barresi","year":"2004","journal-title":"Nature Medicine"},{"key":"bib5","doi-asserted-by":"publisher","first-page":"1200","DOI":"10.1128\/JB.01120-08","article-title":"Synthesis of cdp-activated ribitol for teichoic acid precursors in streptococcus pneumoniae","volume":"191","author":"Baur","year":"2009","journal-title":"Journal of Bacteriology"},{"key":"bib6","doi-asserted-by":"publisher","first-page":"921","DOI":"10.1110\/ps.8.4.921","article-title":"A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation","volume":"8","author":"Beckett","year":"1999","journal-title":"Protein Science"},{"key":"bib7","doi-asserted-by":"publisher","first-page":"1033","DOI":"10.1086\/342975","article-title":"Mutations in the o-mannosyltransferase gene POMT1 give rise to the severe neuronal migration disorder walker-warburg syndrome","volume":"71","author":"Beltr\u00e1n-Valero de Bernab\u00e9","year":"2002","journal-title":"American Journal of Human Genetics"},{"key":"bib8","doi-asserted-by":"publisher","first-page":"200","DOI":"10.1002\/path.3020","article-title":"Cell-matrix interactions in muscle disease","volume":"226","author":"Carmignac","year":"2012","journal-title":"The Journal of Pathology"},{"key":"bib9","doi-asserted-by":"crossref","first-page":"2156","DOI":"10.1074\/jbc.272.4.2156","article-title":"Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin","volume":"272","author":"Chiba","year":"1997","journal-title":"The Journal of Biological Chemistry"},{"key":"bib10","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1093\/brain\/aws312","article-title":"ISPD gene mutations are a common cause of congenital and limb-girdle muscular dystrophies","volume":"136","author":"Cirak","year":"2013","journal-title":"Brain"},{"key":"bib11","doi-asserted-by":"publisher","first-page":"1248","DOI":"10.1074\/jbc.272.2.1248","article-title":"Sialic acid specificity of myelin-associated glycoprotein binding","volume":"272","author":"Collins","year":"1997","journal-title":"The Journal of Biological Chemistry"},{"key":"bib12","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1007\/978-1-4939-2343-4_1","article-title":"Annotation of glycomics MS and MS\/MS spectra using the glycoworkbench software tool","volume":"1273","author":"Damerell","year":"2015","journal-title":"Methods in Molecular Biology"},{"key":"bib13","doi-asserted-by":"publisher","first-page":"2849","DOI":"10.1007\/s00018-012-1193-0","article-title":"O-mannosylation and human disease","volume":"70","author":"Dobson","year":"2013","journal-title":"Cellular and Molecular Life Sciences"},{"key":"bib14","doi-asserted-by":"publisher","first-page":"273","DOI":"10.1212\/WNL.0000000000001162","article-title":"DAG1 mutations associated with asymptomatic hyperckemia and hypoglycosylation of \u03b1-dystroglycan","volume":"84","author":"Dong","year":"2015","journal-title":"Neurology"},{"key":"bib15","doi-asserted-by":"publisher","first-page":"1461","DOI":"10.1083\/jcb.142.6.1461","article-title":"Progressive muscular dystrophy in alpha-sarcoglycan-deficient mice","volume":"142","author":"Duclos","year":"1998","journal-title":"The Journal of Cell Biology"},{"key":"bib16","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1385\/1-59745-167-3:43","article-title":"O-mannosylation in mammalian cells","volume":"347","author":"Endo","year":"2006","journal-title":"Methods in Molecular Biology"},{"key":"bib17","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1093\/jb\/mvu066","article-title":"Glycobiology of \u03b1-dystroglycan and muscular dystrophy","volume":"157","author":"Endo","year":"2015","journal-title":"Journal of Biochemistry"},{"key":"bib18","doi-asserted-by":"publisher","first-page":"315","DOI":"10.1038\/345315a0","article-title":"Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle","volume":"345","author":"Ervasti","year":"1990","journal-title":"Nature"},{"key":"bib19","doi-asserted-by":"publisher","first-page":"1121","DOI":"10.1016\/0092-8674(91)90035-W","article-title":"Membrane organization of the dystrophin-glycoprotein complex","volume":"66","author":"Ervasti","year":"1991","journal-title":"Cell"},{"key":"bib20","doi-asserted-by":"publisher","first-page":"127","DOI":"10.1016\/j.ydbio.2006.01.028","article-title":"Minor proteins and enzymes of the drosophila eggshell matrix","volume":"293","author":"Fakhouri","year":"2006","journal-title":"Developmental Biology"},{"key":"bib21","doi-asserted-by":"publisher","first-page":"205","DOI":"10.1007\/s10048-013-0374-9","article-title":"Homozygous dystroglycan mutation associated with a novel muscle-eye-brain disease-like phenotype with multicystic leucodystrophy","volume":"14","author":"Geis","year":"2013","journal-title":"Neurogenetics"},{"key":"bib22","doi-asserted-by":"publisher","first-page":"939","DOI":"10.1056\/NEJMoa1006939","article-title":"A dystroglycan mutation associated with limb-girdle muscular dystrophy","volume":"364","author":"Hara","year":"2011","journal-title":"The New England Journal of Medicine"},{"key":"bib23","doi-asserted-by":"publisher","first-page":"17426","DOI":"10.1073\/pnas.1114836108","article-title":"Like-acetylglucosaminyltransferase (large)-dependent modification of dystroglycan at thr-317\/319 is required for laminin binding and arenavirus infection","volume":"108","author":"Hara","year":"2011","journal-title":"Proceedings of the National Academy of Sciences of the United States of America"},{"key":"bib24","doi-asserted-by":"publisher","first-page":"79","DOI":"10.1016\/S0014-5793(00)01195-9","article-title":"Biosynthesis of dystroglycan: Processing of a precursor propeptide","volume":"468","author":"Holt","year":"2000","journal-title":"FEBS Letters"},{"key":"bib25","doi-asserted-by":"publisher","first-page":"479","DOI":"10.1126\/science.1233675","article-title":"Deciphering the glycosylome of dystroglycanopathies using haploid screens for lassa virus entry","volume":"340","author":"Jae","year":"2013","journal-title":"Science"},{"key":"bib26","doi-asserted-by":"publisher","first-page":"2209","DOI":"10.1016\/j.celrep.2016.02.017","article-title":"Identification of a post-translational modification with ribitol-phosphate and its defect in muscular dystrophy","volume":"14","author":"Kanagawa","year":"2016","journal-title":"Cell Reports"},{"key":"bib27","doi-asserted-by":"publisher","first-page":"8692","DOI":"10.1021\/ac4015935","article-title":"In-gel \u03b2-elimination and aqueous-organic partition for improved O- and sulfoglycomics","volume":"85","author":"Kumagai","year":"2013","journal-title":"Analytical Chemistry"},{"key":"bib28","doi-asserted-by":"publisher","first-page":"1460","DOI":"10.1111\/j.1526-4610.2007.01002.x","article-title":"Phenotypic and genetic analysis of a large family with migraine-associated vertigo","volume":"48","author":"Lee","year":"2008","journal-title":"Headache"},{"key":"bib29","doi-asserted-by":"publisher","first-page":"646","DOI":"10.1186\/1471-2164-10-646","article-title":"Improving the efficiency of genomic loci capture using oligonucleotide arrays for high throughput resequencing","volume":"10","author":"Lee","year":"2009","journal-title":"BMC Genomics"},{"key":"bib30","doi-asserted-by":"publisher","first-page":"28526","DOI":"10.1074\/jbc.M112.367565","article-title":"Developmental expression of the neuron-specific n-acetylglucosaminyltransferase vb (GnT-Vb\/IX) and identification of its in vivo glycan products in comparison with those of its paralog, GnT-V","volume":"287","author":"Lee","year":"2012","journal-title":"The Journal of Biological Chemistry"},{"key":"bib31","doi-asserted-by":"publisher","first-page":"76","DOI":"10.1016\/j.ajhg.2009.06.006","article-title":"Deficiency of Dol-P-man synthase subunit DPM3 bridges the congenital disorders of glycosylation with the dystroglycanopathies","volume":"85","author":"Lefeber","year":"2009","journal-title":"American Journal of Human Genetics"},{"key":"bib32","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/1471-213X-6-1","article-title":"Proteomics of early zebrafish embryos","volume":"6","author":"Link","year":"2006","journal-title":"BMC Developmental Biology"},{"key":"bib33","doi-asserted-by":"publisher","first-page":"541","DOI":"10.1016\/j.ajhg.2012.07.009","article-title":"Exome sequencing and functional validation in zebrafish identify GTDC2 mutations as a cause of walker-warburg syndrome","volume":"91","author":"Manzini","year":"2012","journal-title":"American Journal of Human Genetics"},{"key":"bib34","doi-asserted-by":"publisher","first-page":"34680","DOI":"10.1074\/jbc.M113.519041","article-title":"Enzymatic basis for n-glycan sialylation: Structure of rat \u03b12,6-sialyltransferase (ST6GAL1) reveals conserved and unique features for glycan sialylation","volume":"288","author":"Meng","year":"2013","journal-title":"The Journal of Biological Chemistry"},{"key":"bib35","doi-asserted-by":"publisher","first-page":"417","DOI":"10.1038\/nature00837","article-title":"Post-translational disruption of dystroglycan\u2013ligand interactions in congenital muscular dystrophies","volume":"418","author":"Michele","year":"2002","journal-title":"Nature"},{"key":"bib36","doi-asserted-by":"publisher","first-page":"437","DOI":"10.1097\/WCO.0b013e32834a95e3","article-title":"Muscular dystrophies due to glycosylation defects: Diagnosis and therapeutic strategies","volume":"24","author":"Muntoni","year":"2011","journal-title":"Current Opinion in Neurology"},{"key":"bib37","doi-asserted-by":"crossref","first-page":"3505","DOI":"10.1242\/dev.129.14.3505","article-title":"Removal of dystroglycan causes severe muscular dystrophy in zebrafish embryos","volume":"129","author":"Parsons","year":"2002","journal-title":"Development"},{"key":"bib38","doi-asserted-by":"publisher","first-page":"395","DOI":"10.1016\/j.molmed.2011.01.014","article-title":"Oxidative stress, inflammation and carcinogenesis are controlled through the pentose phosphate pathway by transaldolase","volume":"17","author":"Perl","year":"2011","journal-title":"Trends in Molecular Medicine"},{"key":"bib39","doi-asserted-by":"publisher","first-page":"3066","DOI":"10.1021\/bi500153y","article-title":"Mammalian o-mannosylation pathway: Glycan structures, enzymes, and protein substrates","volume":"53","author":"Praissman","year":"2014","journal-title":"Biochemistry"},{"key":"bib40","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.03943","article-title":"B4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of \u03b1-dystroglycan","volume":"3","author":"Praissman","year":"2014","journal-title":"eLife"},{"key":"bib41","doi-asserted-by":"publisher","first-page":"79","DOI":"10.1038\/nbt1172","article-title":"Engineering and characterization of a superfolder green fluorescent protein","volume":"24","author":"P\u00e9delacq","year":"2006","journal-title":"Nature Biotechnology"},{"key":"bib42","doi-asserted-by":"publisher","first-page":"641","DOI":"10.1038\/89691","article-title":"Structure of 4-diphosphocytidyl-2-c- methylerythritol synthetase involved in mevalonate- independent isoprenoid biosynthesis","volume":"8","author":"Richard","year":"2001","journal-title":"Nature Structural Biology"},{"key":"bib43","doi-asserted-by":"publisher","first-page":"1643","DOI":"10.1016\/j.chembiol.2015.10.014","article-title":"Human ISPD is a cytidyltransferase required for dystroglycan o-mannosylation","volume":"22","author":"Riemersma","year":"2015","journal-title":"Chemistry & Biology"},{"key":"bib44","doi-asserted-by":"publisher","first-page":"2241","DOI":"10.1093\/hmg\/ddu742","article-title":"Disease mutations in cmp-sialic acid transporter SLC35A1 result in abnormal \u03b1-dystroglycan o-mannosylation, independent from sialic acid","volume":"24","author":"Riemersma","year":"2015","journal-title":"Human Molecular Genetics"},{"key":"bib45","doi-asserted-by":"publisher","first-page":"e78","DOI":"10.1371\/journal.pgen.0030078","article-title":"p53 activation by knockdown technologies","volume":"3","author":"Robu","year":"2007","journal-title":"PLoS Genetics"},{"key":"bib46","doi-asserted-by":"publisher","first-page":"581","DOI":"10.1038\/ng.2253","article-title":"Mutations in ISPD cause walker-warburg syndrome and defective glycosylation of \u03b1-dystroglycan","volume":"44","author":"Roscioli","year":"2012","journal-title":"Nature Genetics"},{"key":"bib47","doi-asserted-by":"publisher","first-page":"W452","DOI":"10.1093\/nar\/gks539","article-title":"SIFT web server: Predicting effects of amino acid substitutions on proteins","volume":"40","author":"Sim","year":"2012","journal-title":"Nucleic Acids Research"},{"key":"bib48","doi-asserted-by":"publisher","first-page":"24882","DOI":"10.1074\/jbc.M110.126474","article-title":"Site mapping and characterization of o-glycan structures on alpha-dystroglycan isolated from rabbit skeletal muscle","volume":"285","author":"Stalnaker","year":"2010","journal-title":"The Journal of Biological Chemistry"},{"key":"bib49","doi-asserted-by":"publisher","first-page":"603","DOI":"10.1016\/j.sbi.2011.09.001","article-title":"Mammalian o-mannosylation: Unsolved questions of structure\/function","volume":"21","author":"Stalnaker","year":"2011","journal-title":"Current Opinion in Structural Biology"},{"key":"bib50","doi-asserted-by":"publisher","first-page":"514","DOI":"10.1111\/j.1742-4658.2004.04493.x","article-title":"Comparison of the substrate specificity of two potyvirus proteases","volume":"272","author":"T\u00f6zs\u00e9r","year":"2005","journal-title":"The FEBS Journal"},{"key":"bib51","doi-asserted-by":"publisher","first-page":"21018","DOI":"10.1073\/pnas.1313446110","article-title":"Mining the o-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins","volume":"110","author":"Vester-Christensen","year":"2013","journal-title":"Proceedings of the National Academy of Sciences of the United States of America"},{"key":"bib52","doi-asserted-by":"publisher","first-page":"1135","DOI":"10.1016\/j.ajhg.2012.10.009","article-title":"Identification of mutations in TMEM5 and ISPD as a cause of severe cobblestone lissencephaly","volume":"91","author":"Vuillaumier-Barrot","year":"2012","journal-title":"American Journal of Human Genetics"},{"key":"bib53","doi-asserted-by":"publisher","first-page":"6930","DOI":"10.1074\/jbc.R112.438978","article-title":"The o-mannosylation pathway: Glycosyltransferases and proteins implicated in congenital muscular dystrophy","volume":"288","author":"Wells","year":"2013","journal-title":"The Journal of Biological Chemistry"},{"key":"bib54","doi-asserted-by":"publisher","first-page":"575","DOI":"10.1038\/ng.2252","article-title":"ISPD loss-of-function mutations disrupt dystroglycan o-mannosylation and cause walker-warburg syndrome","volume":"44","author":"Willer","year":"2012","journal-title":"Nature Genetics"},{"key":"bib55","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.03941","article-title":"The glucuronyltransferase B4GAT1 is required for initiation of LARGE-mediated \u03b1-dystroglycan functional glycosylation","volume":"3","author":"Willer","year":"2014","journal-title":"eLife"},{"key":"bib56","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1093\/oxfordjournals.jbchem.a123276","article-title":"Glycoprotein complex anchoring dystrophin to sarcolemma","volume":"108","author":"Yoshida","year":"1990","journal-title":"Journal of Biochemistry"},{"key":"bib57","doi-asserted-by":"publisher","first-page":"717","DOI":"10.1016\/S1534-5807(01)00070-3","article-title":"Muscular dystrophy and neuronal migration disorder caused by mutations in a glycosyltransferase, pomgnt1","volume":"1","author":"Yoshida","year":"2001","journal-title":"Developmental Cell"},{"key":"bib58","doi-asserted-by":"publisher","first-page":"88","DOI":"10.1126\/science.1180512","article-title":"O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding","volume":"327","author":"Yoshida-Moriguchi","year":"2010","journal-title":"Science"},{"key":"bib59","doi-asserted-by":"publisher","first-page":"896","DOI":"10.1126\/science.1239951","article-title":"SGK196 is a glycosylation-specific o-mannose kinase required for dystroglycan function","volume":"341","author":"Yoshida-Moriguchi","year":"2013","journal-title":"Science"},{"key":"bib60","doi-asserted-by":"publisher","first-page":"702","DOI":"10.1093\/glycob\/cwv021","article-title":"Matriglycan: A novel polysaccharide that links dystroglycan to the basement membrane","volume":"25","author":"Yoshida-Moriguchi","year":"2015","journal-title":"Glycobiology"}],"container-title":["eLife"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/cdn.elifesciences.org\/articles\/14473\/elife-14473-v3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/cdn.elifesciences.org\/articles\/14473\/elife-14473-v3.xml","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/elifesciences.org\/articles\/14473","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,11]],"date-time":"2023-10-11T20:50:06Z","timestamp":1697057406000},"score":1,"resource":{"primary":{"URL":"https:\/\/elifesciences.org\/articles\/14473"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,4,29]]},"references-count":60,"alternative-id":["10.7554\/eLife.14473"],"URL":"https:\/\/doi.org\/10.7554\/elife.14473","archive":["CLOCKSS"],"relation":{"has-review":[{"id-type":"doi","id":"10.7554\/eLife.14473.022","asserted-by":"object"},{"id-type":"doi","id":"10.7554\/eLife.14473.023","asserted-by":"object"}]},"ISSN":["2050-084X"],"issn-type":[{"value":"2050-084X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,4,29]]},"article-number":"e14473"}}