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| http://purl.uniprot.org/citations/25488986 | http://www.w3.org/2000/01/rdf-schema#comment | "N-Glycosylation efficiency is a key parameter when studying components of the protein N-glycosylation pathway, but was recently also recognized as an important factor in the production of glycosylated proteins. We have developed a novel assay to quantify N-glycosylation efficiency of proteins. This assay is based on the secreted activity of yeast acid phosphatase, the proper folding and hence secretion of which is strongly dependent on its N-glycosylation status. The results show that the reporter yields a quantitative measure for protein N-glycosylation in yeast, which is in good agreement with classically used assay based on protein migration patterns on SDS-PAGE. However, the assay is less laborious and is adaptable to high-throughput screening approaches as exemplified."xsd:string |
| http://purl.uniprot.org/citations/25488986 | http://purl.org/dc/terms/identifier | "doi:10.1093/glycob/cwu134"xsd:string |
| http://purl.uniprot.org/citations/25488986 | http://purl.uniprot.org/core/author | "Aebi M."xsd:string |
| http://purl.uniprot.org/citations/25488986 | http://purl.uniprot.org/core/author | "Frey A.D."xsd:string |
| http://purl.uniprot.org/citations/25488986 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25488986 | http://purl.uniprot.org/core/name | "Glycobiology"xsd:string |
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| http://purl.uniprot.org/citations/25488986 | http://purl.uniprot.org/core/title | "An enzyme-based screening system for the rapid assessment of protein N-glycosylation efficiency in yeast."xsd:string |
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