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Our results reveal that the stem domain of POMGnT1 modulates\n                    <jats:italic>O<\/jats:italic>\n                    -mannosylation of \u03b1-DG via its carbohydrate-binding activity. These findings explain how POMGnT1 attaches \u03b2-GlcNAc to clustered\n                    <jats:italic>O<\/jats:italic>\n                    -mannose sites and influences postphosphoryl modification of core M3. Our study provides important insight into how disease-associated mutations cause CMD pathogenesis.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1525545113","type":"journal-article","created":{"date-parts":[[2016,8,4]],"date-time":"2016-08-04T23:23:47Z","timestamp":1470353027000},"page":"9280-9285","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":77,"title":["Carbohydrate-binding domain of the POMGnT1 stem region modulates\n                    <i>O<\/i>\n                    -mannosylation sites of \u03b1-dystroglycan"],"prefix":"10.1073","volume":"113","author":[{"given":"Naoyuki","family":"Kuwabara","sequence":"first","affiliation":[{"name":"Photon Factory, Structural Biology Research Center, Institute of Materials Structure Science, High Energy Accelerator Research Organization, Tsukuba, Ibaraki 305-0801, 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