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| http://purl.uniprot.org/citations/25666261 | http://www.w3.org/2000/01/rdf-schema#comment | "Nowhere else does the cell employ posttranslational protein modifications as extensively as in the endoplasmic reticulum (ER). In fact, such modifications can comprise the bulk of the mass of a mature protein in some cases. The most common modification is glycosylation, with N-linked glycans being the most commonly studied and best understood. However, the covalent modification of serine and threonine side chains with mannose or O-mannosylation has been gaining interest. Part of the attention comes from the realization that O-mannosylation is a conserved process found in most eukaryotes and defects in O-mannosylation can give rise to human disease. Long known to be important structural modification of some endomembrane system proteins, recent findings reveal that it is a common modification of unfolded proteins. For irreversibly misfolded proteins, O-mannosylation can aid in their disposal through ER or lysosomal pathways. The protein O-mannosylation pathway can also play an instrumental role in monitoring the folding of newly synthesized proteins. Proteins that fail to fold efficiently are O-mannosylated to remove them from harmful futile protein folding cycles and prepare them for disposal. Thus, O-mannosylation joins N-linked glycosylation as a major mechanism involved in the folding and quality control of newly synthesized proteins in the ER."xsd:string |
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| http://purl.uniprot.org/citations/25666261 | http://purl.uniprot.org/core/author | "Xu C."xsd:string |
| http://purl.uniprot.org/citations/25666261 | http://purl.uniprot.org/core/author | "Ng D.T."xsd:string |
| http://purl.uniprot.org/citations/25666261 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25666261 | http://purl.uniprot.org/core/name | "Semin Cell Dev Biol"xsd:string |
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| http://purl.uniprot.org/citations/25666261 | http://purl.uniprot.org/core/title | "O-mannosylation: The other glycan player of ER quality control."xsd:string |
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