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Article

Deficiencies in subunits of the Conserved Oligomeric Golgi (COG) complex define a novel group of Congenital Disorders of Glycosylation.

Molecular genetics and metabolism - 1 Jan 2008

Zeevaert Renate, Foulquier François, Jaeken Jaak, Matthijs Gert

Abstract excerpt

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...

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Share to Adaptor Proteins, Vesicular Transport
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 17904886
DOI: 10.1016/j.ymgme.2007.08.118

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Deficiencies in subunits of the Conserved Oligomeric Golgi (COG) complex define a novel group of Congenital Disorders of Glycosylation.PMID 17904886Read ↗

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Mutations in COG2 encoding a subunit of the conserved oligomeric golgi complex cause a congenital disorder of glycosylation.Semantic proximity Read ↗

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Deficiency of the Cog8 subunit in normal and CDG-derived cells impairs the assembly of the COG and Golgi SNARE complexes.Semantic proximity Read ↗

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