| http://purl.uniprot.org/citations/8020500 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8020500 | http://www.w3.org/2000/01/rdf-schema#comment | "The endoplasmic binding protein BiP and N-linked glycosylation are proposed to be essential components in the processing pathway of secreted protein. In Saccharomyces cerevisiae, BiP is encoded by the KAR2 gene; WBP1 encodes an essential component of the N-oligosaccharyltransferase complex. wbp1 mutations result in reduced oligosaccharyltransferase activity and a temperature-sensitive phenotype. We show that a combination of kar2 and wbp1 mutations results in a synthetic phenotype with a strongly reduced growth rate at the permissive temperature. To investigate the role of N-linked glycosylation in BiP function, the processing of non-glycosylated carboxypeptidase was followed in different kar2 strains at the permissive temperature. In all kar2 strains, the processing of non-glycosylated carboxypeptidase Y was drastically reduced. A specific BiP/non-glycosylated carboxypeptidase Y complex was detected in kar2-159 and kar2-203 cells whereas the kar2-1 mutation did not result in such a complex. Our data show that BiP and N-linked glycosylation are directly involved in the processing of secreted proteins. The results support the hypothesis that BiP stabilizes the folding-competent and assembly-competent state of a polypeptide, whereas N-linked oligosaccharides are structural components required in the folding process after the polypeptide is released from BiP."xsd:string |
| http://purl.uniprot.org/citations/8020500 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1994.tb18906.x"xsd:string |
| http://purl.uniprot.org/citations/8020500 | http://purl.uniprot.org/core/author | "Aebi M."xsd:string |
| http://purl.uniprot.org/citations/8020500 | http://purl.uniprot.org/core/author | "te Heesen S."xsd:string |
| http://purl.uniprot.org/citations/8020500 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/8020500 | http://purl.uniprot.org/core/name | "Eur J Biochem"xsd:string |
| http://purl.uniprot.org/citations/8020500 | http://purl.uniprot.org/core/pages | "631-637"xsd:string |
| http://purl.uniprot.org/citations/8020500 | http://purl.uniprot.org/core/title | "The genetic interaction of kar2 and wbp1 mutations. Distinct functions of binding protein BiP and N-linked glycosylation in the processing pathway of secreted proteins in Saccharomyces cerevisiae."xsd:string |
| http://purl.uniprot.org/citations/8020500 | http://purl.uniprot.org/core/volume | "222"xsd:string |
| http://purl.uniprot.org/citations/8020500 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8020500 |
| http://purl.uniprot.org/citations/8020500 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8020500 |
| http://purl.uniprot.org/uniprot/#_P00729-mappedCitation-8020500 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/8020500 |
| http://purl.uniprot.org/uniprot/#_P16474-mappedCitation-8020500 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/8020500 |
| http://purl.uniprot.org/uniprot/#_P33767-mappedCitation-8020500 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/8020500 |
| http://purl.uniprot.org/uniprot/P00729 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/8020500 |
| http://purl.uniprot.org/uniprot/P33767 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/8020500 |
| http://purl.uniprot.org/uniprot/P16474 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/8020500 |