{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["75(1)"],"submitter":["Frank CG"],"pubmed_abstract":["Defects of lipid-linked oligosaccharide assembly lead to alterations of N-linked glycosylation known as \"type I congenital disorders of glycosylation\" (CDG). Dysfunctions along this stepwise assembly pathway are characterized by intracellular accumulation of intermediate lipid-linked oligosaccharides, the detection of which contributes to the identification of underlying enzymatic defects. Using this approach, we have found, in a patient with CDG, a deficiency of the ALG9 alpha 1,2 mannosyltransferase enzyme, which causes an accumulation of lipid-linked-GlcNAc(2)Man(6) and -GlcNAc(2)Man(8) structures, which was paralleled by the transfer of incomplete oligosaccharides precursors to protein. A homozygous point-mutation 1567G-->A (amino acid substitution E523K) was detected in the ALG9 gene."],"journal":["American journal of human genetics"],"pagination":["146-50"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1181998"],"repository":["biostudies-literature"],"pubmed_title":["Identification and functional analysis of a defect in the human ALG9 gene: definition of congenital disorder of glycosylation type IL."],"pmcid":["PMC1181998"],"pubmed_authors":["Aebi M","Berger EG","Grubenmann CE","Hennet T","Frank CG","Eyaid W"],"additional_accession":[]},"is_claimable":false,"name":"Identification and functional analysis of a defect in the human ALG9 gene: definition of congenital disorder of glycosylation type IL.","description":"Defects of lipid-linked oligosaccharide assembly lead to alterations of N-linked glycosylation known as \"type I congenital disorders of glycosylation\" (CDG). Dysfunctions along this stepwise assembly pathway are characterized by intracellular accumulation of intermediate lipid-linked oligosaccharides, the detection of which contributes to the identification of underlying enzymatic defects. Using this approach, we have found, in a patient with CDG, a deficiency of the ALG9 alpha 1,2 mannosyltransferase enzyme, which causes an accumulation of lipid-linked-GlcNAc(2)Man(6) and -GlcNAc(2)Man(8) structures, which was paralleled by the transfer of incomplete oligosaccharides precursors to protein. A homozygous point-mutation 1567G-->A (amino acid substitution E523K) was detected in the ALG9 gene.","dates":{"release":"2004-01-01T00:00:00Z","publication":"2004 Jul","modification":"2025-04-04T21:07:08.75Z","creation":"2019-03-27T01:09:11Z"},"accession":"S-EPMC1181998","cross_references":{"pubmed":["15148656"],"doi":["10.1086/422367"]}}