Article
ALG1-CDG: Clinical and Molecular Characterization of 39 Unreported Patients.
Human mutation - 1 Jul 2016
Ng Bobby G, Shiryaev Sergey A, Rymen Daisy, Eklund Erik A, Raymond Kimiyo, Kircher Martin, Abdenur Jose E, Alehan Fusun, Midro Alina T, Bamshad Michael J, Barone Rita, Berry Gerard T, Brumbaugh Jane E, Buckingham Kati J, Clarkson Katie, Cole F Sessions, O'Connor Shawn, Cooper Gregory M, Van Coster Rudy, Demmer Laurie A, Diogo Luisa, Fay Alexander J, Ficicioglu Can, Fiumara Agata, Gahl William A, Ganetzky Rebecca, Goel Himanshu, Harshman Lyndsay A, He Miao, Jaeken Jaak, James Philip M, Katz Daniel, Keldermans Liesbeth, Kibaek Maria, Kornberg Andrew J, Lachlan Katherine, Lam Christina, Yaplito-Lee Joy, Nickerson Deborah A, Peters Heidi L, Race Valerie, Régal Luc, Rush Jeffrey S, Rutledge S Lane, Shendure Jay, Souche Erika, Sparks Susan E, Trapane Pamela, Sanchez-Valle Amarilis, Vilain Eric, Vøllo Arve, Waechter Charles J, Wang Raymond Y, Wolfe Lynne A, Wong Derek A, Wood Tim, Yang Amy C, Matthijs Gert, Freeze Hudson H
Abstract excerpt
Congenital disorders of glycosylation (CDG) arise from pathogenic mutations in over 100 genes leading to impaired protein or lipid glycosylation. ALG1 encodes a β1,4 mannosyltransferase that catalyzes the addition of the first of nine mannose moieties to form a dolichol-lipid linked oligosaccharide intermediate required for proper N-linked glycosylation. ALG1 mutations cause a rare autosomal recessive disorder...
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