{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ng BG"],"funding":["Simons Foundation Autism Research Initiative","NIDDK NIH HHS","Medical Research Council","Region Skåne","NHGRI NIH HHS","NINDS NIH HHS","National Institutes of Health","JPB Foundation","National Human Genome Research Institute"],"pagination":["1333-1348"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7722193"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["43(6)"],"pubmed_abstract":["Asparagine-linked glycosylation 13 homolog (ALG13) encodes a nonredundant, highly conserved, X-linked uridine diphosphate (UDP)-N-acetylglucosaminyltransferase required for the synthesis of lipid linked oligosaccharide precursor and proper N-linked glycosylation. De novo variants in ALG13 underlie a form of early infantile epileptic encephalopathy known as EIEE36, but given its essential role in glycosylation, it is also considered a congenital disorder of glycosylation (CDG), ALG13-CDG. Twenty-four previously reported ALG13-CDG cases had de novo variants, but surprisingly, unlike most forms of CDG, ALG13-CDG did not show the anticipated glycosylation defects, typically detected by altered transferrin glycosylation. Structural homology modeling of two recurrent de novo variants, p.A81T and"],"journal":["Journal of inherited metabolic disease"],"pubmed_title":["Predominant and novel de novo variants in 29 individuals with ALG13 deficiency: Clinical description, biomarker status, biochemical analysis, and treatment suggestions."],"pmcid":["PMC7722193"],"funding_grant_id":["U01HG010218","R01DK099551","U01 HG010218","UM1 HG006493","MR/S007180/1","U54 NS115198","R01 DK099551","U24 HG008956","U01 HG007708","U01HG007708"],"pubmed_authors":["Zalan A","Shiryaev SA","Gardiner F","Si Y","Tuite A","Russo RS","Abbott MA","Graf WD","Ng BG","Freeze HH","Scheffer IE","Larson AA","Hammond K","Morava E","Christodoulou J","Monaghan KG","Palculict TB","Grunewald S","Rowe LJ","Schenone AB","Bernstein JA","Chelakkadan S","Eklund EA","Papazoglu GM","Rosenfeld JA","Schnur RE","Rhodes L","Hoganson GE","McCormack C","Liu P","Kohler JN","Hauser NS","Miller R","Asteggiano C","Thabet F","Chung WK","Ciliberto MA","Dong YY","Cousin J","Houck KM","Webster RI","Undiagnosed Diseases Network, University of Washington Center for Mendelian Genomics (UW-CMG)","Villanueva MM","Pletcher BA","Wang RY","Barr E","Nickerson DA","Madathil S","Bamshad MJ","Ghosh S","Wolfe LA","Wilson D","Meeks NJL","Serrano Russi AH"],"additional_accession":[]},"is_claimable":false,"name":"Predominant and novel de novo variants in 29 individuals with ALG13 deficiency: Clinical description, biomarker status, biochemical analysis, and treatment suggestions.","description":"Asparagine-linked glycosylation 13 homolog (ALG13) encodes a nonredundant, highly conserved, X-linked uridine diphosphate (UDP)-N-acetylglucosaminyltransferase required for the synthesis of lipid linked oligosaccharide precursor and proper N-linked glycosylation. De novo variants in ALG13 underlie a form of early infantile epileptic encephalopathy known as EIEE36, but given its essential role in glycosylation, it is also considered a congenital disorder of glycosylation (CDG), ALG13-CDG. Twenty-four previously reported ALG13-CDG cases had de novo variants, but surprisingly, unlike most forms of CDG, ALG13-CDG did not show the anticipated glycosylation defects, typically detected by altered transferrin glycosylation. Structural homology modeling of two recurrent de novo variants, p.A81T and","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Nov","modification":"2025-04-04T09:01:47.486Z","creation":"2022-02-10T08:17:55.824Z"},"accession":"S-EPMC7722193","cross_references":{"pubmed":["32681751"],"doi":["10.1002/jimd.12290"]}}