{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,26]],"date-time":"2026-03-26T11:07:33Z","timestamp":1774523253834,"version":"3.50.1"},"reference-count":34,"publisher":"American Society for Cell Biology (ASCB)","issue":"8","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["MBoC"],"published-print":{"date-parts":[[2008,8]]},"abstract":"<jats:p>\n                    N-Glycosylation starts in the endoplasmic reticulum (ER) where a 14-sugar glycan composed of three glucoses, nine mannoses, and two N-acetylglucosamines (Glc\n                    <jats:sub>3<\/jats:sub>\n                    Man\n                    <jats:sub>9<\/jats:sub>\n                    GlcNAc\n                    <jats:sub>2<\/jats:sub>\n                    ) is transferred to nascent proteins. The glucoses are sequentially trimmed by ER-resident glucosidases. The Glc\n                    <jats:sub>3<\/jats:sub>\n                    Man\n                    <jats:sub>9<\/jats:sub>\n                    GlcNAc\n                    <jats:sub>2<\/jats:sub>\n                    moiety is the substrate for oligosaccharyltransferase; the Glc\n                    <jats:sub>1<\/jats:sub>\n                    Man\n                    <jats:sub>9<\/jats:sub>\n                    GlcNAc\n                    <jats:sub>2<\/jats:sub>\n                    and Man\n                    <jats:sub>9<\/jats:sub>\n                    GlcNAc\n                    <jats:sub>2<\/jats:sub>\n                    intermediates are signals for glycoprotein folding and quality control in the calnexin\/calreticulin cycle. Here, we report a novel membrane-anchored ER protein that is highly conserved in animals and that recognizes the Glc\n                    <jats:sub>2<\/jats:sub>\n                    -N-glycan. Structure determination by nuclear magnetic resonance showed that its luminal part is a carbohydrate binding domain that recognizes glucose oligomers. Carbohydrate microarray analyses revealed a uniquely selective binding to a Glc\n                    <jats:sub>2<\/jats:sub>\n                    -N-glycan probe. The localization, structure, and binding specificity of this protein, which we have named malectin, open the way to studies of its role in the genesis, processing and secretion of N-glycosylated proteins.\n                  <\/jats:p>","DOI":"10.1091\/mbc.e08-04-0354","type":"journal-article","created":{"date-parts":[[2008,6,4]],"date-time":"2008-06-04T20:54:15Z","timestamp":1212612855000},"page":"3404-3414","source":"Crossref","is-referenced-by-count":254,"title":["Malectin: A Novel Carbohydrate-binding Protein of the Endoplasmic Reticulum and a Candidate Player in the Early Steps of Protein\n                    <i>N<\/i>\n                    -Glycosylation"],"prefix":"10.1091","volume":"19","author":[{"given":"Thomas","family":"Schallus","sequence":"first","affiliation":[{"name":"*European Molecular Biology Laboratory, 69117 Heidelberg, Germany;"},{"name":"Max-Planck-Institut for Medical Research, 69120 Heidelberg, Germany;"}]},{"given":"Christine","family":"Jaeckh","sequence":"additional","affiliation":[{"name":"Department of Developmental Biochemistry und University Medical Center G\u00f6ttingen, 37077 G\u00f6ttingen, Germany;"}]},{"given":"Krisztina","family":"Feh\u00e9r","sequence":"additional","affiliation":[{"name":"*European Molecular Biology Laboratory, 69117 Heidelberg, Germany;"},{"name":"Max-Planck-Institut for Medical Research, 69120 Heidelberg, Germany;"}]},{"given":"Angelina S.","family":"Palma","sequence":"additional","affiliation":[{"name":"The Glycosciences Laboratory, Faculty of Medicine, Imperial College London, Northwick Park and St. Mark's Hospital Campus, Harrow, Middlesex HA1 3UJ, United Kingdom; and"}]},{"given":"Yan","family":"Liu","sequence":"additional","affiliation":[{"name":"The Glycosciences Laboratory, Faculty of Medicine, Imperial College London, Northwick Park and St. Mark's Hospital Campus, Harrow, Middlesex HA1 3UJ, United Kingdom; and"}]},{"given":"Jeremy C.","family":"Simpson","sequence":"additional","affiliation":[{"name":"*European Molecular Biology Laboratory, 69117 Heidelberg, Germany;"}]},{"given":"Mukram","family":"Mackeen","sequence":"additional","affiliation":[{"name":"Oxford Glycobiology Institute, University of Oxford, Oxford OX1 3QU, United Kingdom"}]},{"given":"Gunter","family":"Stier","sequence":"additional","affiliation":[{"name":"*European Molecular Biology Laboratory, 69117 Heidelberg, Germany;"}]},{"given":"Toby J.","family":"Gibson","sequence":"additional","affiliation":[{"name":"*European Molecular Biology Laboratory, 69117 Heidelberg, Germany;"}]},{"given":"Ten","family":"Feizi","sequence":"additional","affiliation":[{"name":"The Glycosciences Laboratory, Faculty of Medicine, Imperial College London, Northwick Park and St. Mark's Hospital Campus, Harrow, Middlesex HA1 3UJ, United Kingdom; and"}]},{"given":"Tomas","family":"Pieler","sequence":"additional","affiliation":[{"name":"Department of Developmental Biochemistry und University Medical Center G\u00f6ttingen, 37077 G\u00f6ttingen, Germany;"}]},{"given":"Claudia","family":"Muhle-Goll","sequence":"additional","affiliation":[{"name":"*European Molecular Biology Laboratory, 69117 Heidelberg, Germany;"},{"name":"Max-Planck-Institut for Medical Research, 69120 Heidelberg, Germany;"}]}],"member":"1076","reference":[{"key":"B1","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/S1567-133X(03)00150-9","volume":"4","author":"Afelik S.","year":"2004","journal-title":"Gene Expr. 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