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| http://purl.uniprot.org/citations/27161930 | http://www.w3.org/2000/01/rdf-schema#comment | "Protein O-mannosylation and N-glycosylation are essential post-translational modifications, which initiate in the endoplasmic reticulum (ER). In yeast, the two glycosylation machineries act at the Sec61 translocon complex where they can even compete for certain substrate proteins. N-linked glycans play a crucial role in the ER quality control of glycoproteins. In recent years, it became clear that in addition to its important functions for cell surface proteins, O-mannosylation impacts the ER protein homeostasis. These glycans can exclude unfavorable folding intermediates from futile folding attempts, increase the solubility of irreversibly misfolded proteins, and even mark them for degradation. O-Mannose glycoproteomics now captures the molecular complexity of this modification opening exciting opportunities to explore further roles of O-mannosylation in the early secretory pathway."xsd:string |
| http://purl.uniprot.org/citations/27161930 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.ceb.2016.04.010"xsd:string |
| http://purl.uniprot.org/citations/27161930 | http://purl.uniprot.org/core/author | "Neubert P."xsd:string |
| http://purl.uniprot.org/citations/27161930 | http://purl.uniprot.org/core/author | "Strahl S."xsd:string |
| http://purl.uniprot.org/citations/27161930 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/27161930 | http://purl.uniprot.org/core/name | "Curr Opin Cell Biol"xsd:string |
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| http://purl.uniprot.org/citations/27161930 | http://purl.uniprot.org/core/title | "Protein O-mannosylation in the early secretory pathway."xsd:string |
| http://purl.uniprot.org/citations/27161930 | http://purl.uniprot.org/core/volume | "41"xsd:string |
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