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• W2151486703 abstract "Processing of the glycan structures on glycoproteins by different glycosylation enzymes depends on, among other, the non-uniform distribution of these enzymes within the Golgi stacks. This compartmentalization is achieved by a balance between anterograde and retrograde vesicular trafficking. If the balance is disturbed, the glycosylation machinery is mislocalized, which can cause Congenital Disorders of Glycosylation type II (CDG-II), as illustrated by the identification of congenital defects in the Conserved Oligomeric Golgi (COG) complex in humans. We collected findings from different COG deficient cell types, such as CHO, yeast and human fibroblasts to hypothesize about structure and function of the COG complex, and compared the phenotypes and genotypes of the patients known with a COG deficiency. Among 35 CDG-II patients we found 5 patients with a COG defect. COG defects are a novel group of CDG-II with deficient N- as well as O-glycosylation." @default.
• W2151486703 created "2016-06-24" @default.
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• W2151486703 date "2008-01-01" @default.
• W2151486703 modified "2023-10-14" @default.
• W2151486703 title "Deficiencies in subunits of the Conserved Oligomeric Golgi (COG) complex define a novel group of Congenital Disorders of Glycosylation" @default.
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• W2151486703 doi "https://doi.org/10.1016/j.ymgme.2007.08.118" @default.
• W2151486703 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17904886" @default.
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