| http://purl.uniprot.org/citations/10406794 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10406794 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10406794 | http://www.w3.org/2000/01/rdf-schema#comment | "Autophagy is an intracellular bulk degradation system that is ubiquitous for eukaryotic cells. In this process, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. We recently found that a protein conjugation system, in which Apg12p is covalently attached to Apg5p, is indispensable for autophagy in yeast. Here, we describe a novel coiled-coil protein, Apg16p, essential for autophagy. Apg16p interacts with Apg12p-conjugated Apg5p and less preferentially with unconjugated Apg5p. Moreover, the coiled-coil domain of Apg16p mediates self-multimerization that leads to cross-linking of Apg5p molecules and formation of a stable protein complex. Apg16p is not essential for the Apg12p-Apg5p conjugation reaction. These results suggest that the Apg12p-Apg5p conjugate requires Apg16p to accomplish its role in the autophagy pathway, and Apg16p is a key molecule as a linker to form the Apg12p-Apg5p-Apg16p multimer."xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://purl.org/dc/terms/identifier | "doi:10.1093/emboj/18.14.3888"xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://purl.org/dc/terms/identifier | "doi:10.1093/emboj/18.14.3888"xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://purl.uniprot.org/core/author | "Mizushima N."xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://purl.uniprot.org/core/author | "Mizushima N."xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://purl.uniprot.org/core/author | "Ohsumi Y."xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://purl.uniprot.org/core/author | "Ohsumi Y."xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://purl.uniprot.org/core/author | "Noda T."xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://purl.uniprot.org/core/author | "Noda T."xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10406794 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10406794 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://purl.uniprot.org/core/pages | "3888-3896"xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://purl.uniprot.org/core/pages | "3888-3896"xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://purl.uniprot.org/core/title | "Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway."xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://purl.uniprot.org/core/title | "Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway."xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://purl.uniprot.org/core/volume | "18"xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://purl.uniprot.org/core/volume | "18"xsd:string |
| http://purl.uniprot.org/citations/10406794 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10406794 |
| http://purl.uniprot.org/citations/10406794 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10406794 |
| http://purl.uniprot.org/citations/10406794 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10406794 |
| http://purl.uniprot.org/citations/10406794 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10406794 |