Figura, Kurt von

[["dc.bibliographiccitation.firstpage","6816"],["dc.bibliographiccitation.issue","23"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","6822"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Körner, Christian"],["dc.contributor.author","Knauer, Roland"],["dc.contributor.author","Stephani, Ulrich"],["dc.contributor.author","Marquardt, Thorsten"],["dc.contributor.author","Lehle, Ludwig"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:47Z"],["dc.date.available","2019-07-10T08:12:47Z"],["dc.date.issued","1999"],["dc.description.abstract","Type IV of the carbohydrate deficient glycoprotein syndromes (CDGp. is characterized by microcephaly, severe epilepsy, minimal psychomotor development and partial deficiency of sialic acids in serum glycoproteins. Here we show that the molecular defect in the index patient is a missense mutation in the gene encoding the mannosyltransferase that transfers mannose from dolichyl-phosphate mannose on to the lipid-linked oligosaccharide (LLO) intermediate Man5GlcNAc2-PP-dolichol. The defect results in the accumulation of the LLO intermediate and, due to its leaky nature, a residual formation of full-length LLOs. N-glycosylation is abnormal because of the transfer of truncated oligosaccharides in addition to that of full-length oligosaccharides and because of the incomplete utilization of N-glycosylation sites. The mannosyltransferase is the structural and functional orthologue of the Saccharomyces cerevisiae ALG3 gene."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3446"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61035"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","ALG3 gene; carbohydrate deficient glycoprotein syndrome"],["dc.subject.ddc","610"],["dc.title","Carbohydrate-deficient glycoprotein syndrome type IV: defieciency of dolichyl-P-Man:Man5GlcNAc2-PP-dolichyl mannosyltransferase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","73"],["dc.bibliographiccitation.journal","Nature Genetics"],["dc.bibliographiccitation.lastpage","76"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","Lübke, Torben"],["dc.contributor.author","Marquardt, Thorsten"],["dc.contributor.author","Etzioni, Amos"],["dc.contributor.author","Hartmann, Enno"],["dc.contributor.author","Figura, Kurt von"],["dc.contributor.author","Körner, Christian"],["dc.date.accessioned","2019-07-09T11:52:20Z"],["dc.date.available","2019-07-09T11:52:20Z"],["dc.date.issued","2001"],["dc.description.abstract","Congenital disorders of glycosylation (CDG) comprise a rapidly growing group of inherited disorders in which glycosylation of glycoproteins is defective due to mutations in genes required for the assembly of lipid-linked oligosaccharides, their transfer to nascent glycoproteins (CDG-I) or the processing of protein-bound glycans1, 2 (CDG-II). Previously' a defect in the GDP-fucose import into the lumen of the Golgi was identified in a person with CDG (A.C.) with a general deficiency of fucosyl residues in glycoproteins3. This patient presents the clinical features of leukocyte adhesion deficiency type II (LAD II) including mental retardation, short stature, facial stigmata, and recurrent bacterial peripheral infections with persistently elevated peripheral leukocytes4, 5, 6, 7. Using a fucose-specific, lectin-staining procedure for detection of fucosylated glycoproteins and a retroviral cDNA library, we isolated a cDNA complementing the fucosylation defect in the patient's fibroblasts. The cDNA encodes a highly hydrophobic protein of 364 amino acids with multiple putative transmembrane domains. Restoration of GDP-fucose import activity in Golgi-enriched vesicles from the patient's fibroblasts verified the GDP-fucose transporter activity of this protein. We identified two missense mutations in the GDP-fucose transporter cDNA of patient A.C. and of two other people with LAD II. Thus complementation cloning allowed us to identify the human GDP-fucose transporter cDNA and GDP-fucose transporter deficiency as a cause for a new type of CDG. Following the recent recommendations2, 8 for the nomenclature for CDG, this new type is classified as CDG-IIc (formerly LAD II)."],["dc.identifier.doi","10.1038/ng0501-73"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3448"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60161"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1061-4036"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","610"],["dc.title","Complementation cloning identifies CDG-IIc, a new type of congenital disorders of glycosylation, as a GDP-fucose transporter deficiency"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13200"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","13205"],["dc.bibliographiccitation.volume","95"],["dc.contributor.author","Körner, Christian"],["dc.contributor.author","Knauer, Roland"],["dc.contributor.author","Holzbach, Ulrike"],["dc.contributor.author","Hanefeld, Folker"],["dc.contributor.author","Lehle, Ludwig"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:46Z"],["dc.date.available","2019-07-10T08:12:46Z"],["dc.date.issued","1998"],["dc.description.abstract","Deficiency of dolichyl-P-Glc:Man9GlcNAc2- PP-dolichyl glucosyltransferase is the cause of an additional type of carbohydrate-deficient glycoprotein syndrome (CDGS type V). Clinically this type resembles the classical type Ia of CDGS caused by the deficiency of phosphomannomutase. As a result of the glucosyltransferase deficiency in CDGS type V nonglucosylated lipid-linked oligosaccharides accumulate. The defect is leaky and glucosylated oligosaccharides are found on nascent glycoproteins. The limited availability of glucosylated lipid-linked oligosaccharides explains the incomplete usage of N-glycosylation sites in glycoproteins. This finding is reflected in the presence of transferrin forms in serum that lack one or both of the two N-linked oligosaccharides and the reduction of mannose incorporation to about one-third of control in glycoproteins of fibroblasts."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3444"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61033"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","National Academy Sciences"],["dc.relation.issn","0027-8424"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","Carbohydrate-deficient glycoprotein syndrome type V"],["dc.subject.ddc","610"],["dc.title","Carbohydrate-deficient glycoprotein syndrome type V: Deficiency of dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","725"],["dc.bibliographiccitation.journal","Journal of Clinical Investigation"],["dc.bibliographiccitation.lastpage","733"],["dc.bibliographiccitation.volume","109"],["dc.contributor.author","Hanßke, Bengt"],["dc.contributor.author","Thiel, Christian"],["dc.contributor.author","Lübke, Torben"],["dc.contributor.author","Hasilik, Martin"],["dc.contributor.author","Höning, Stefan"],["dc.contributor.author","Peters, Verena"],["dc.contributor.author","Heidemann, Peter H."],["dc.contributor.author","Hoffmann, Georg F."],["dc.contributor.author","Berger, Eric G."],["dc.contributor.author","Figura, Kurt von"],["dc.contributor.author","Körner, Christian"],["dc.date.accessioned","2009-07-21T05:10:09Z"],["dc.date.accessioned","2021-10-27T13:22:30Z"],["dc.date.available","2009-07-21T05:10:09Z"],["dc.date.available","2021-10-27T13:22:30Z"],["dc.date.issued","2002"],["dc.description.abstract","Deficiency of the Golgi enzyme UDP-Gal:N-acetylglucosamine β-1,4-galactosyltransferase I (β4GalT I) (E.C.2.4.1.38) causes a new congenital disorder of glycosylation (CDG), designated type IId (CDG-IId), a severe neurologic disease characterized by a hydrocephalus, myopathy, and bloodclotting defects. Analysis of oligosaccharides from serum transferrin by HPLC, mass spectrometry, and lectin binding revealed the loss of sialic acid and galactose residues. In skin fibroblasts and leukocytes, galactosyltransferase activity was reduced to 5% that of controls. In fibroblasts, a truncated polypeptide was detected that was about 12 kDa smaller in size than wild-type β4GalT I and that failed to localize to the Golgi apparatus. Sequencing of the β4GalT I cDNA and gene revealed an insertion of a single nucleotide (1031-1032insC) leading to premature translation stop and loss of the C-terminal 50 amino acids of the enzyme. The patient was homozygous and his parents heterozygous for this mutation. Expression of a corresponding mutant cDNA in COS-7 cells led to the synthesis of a truncated, inactive polypeptide, which localized to the endoplasmic reticulum."],["dc.format.mimetype","application/pdf"],["dc.identifier.doi","10.1172/JCI200214010."],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3450"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/92100"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.issn","0021-9738"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","610"],["dc.title","Deficiency of UDP-galactose:N-acetylglucosamine β-1,4-galactosyltransferase I causes the congenital disorder of glycosylation type IId"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]