http://purl.uniprot.org/citations/26802743 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/26802743 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/26802743 | http://www.w3.org/2000/01/rdf-schema#comment | "Many cellular stresses cause damages of intracellular proteins, which are eventually degraded by the ubiquitin and proteasome system. The proteasome is a multicatalytic protease complex composed of 20S core particle and the proteasome activators that regulate the proteasome activity. Extracellular mutants 29 (Ecm29) is a 200 kDa protein encoded by KIAA0368 gene, associates with the proteasome, but its role is largely unknown. Here, we generated KIAA0368-deficient mice and investigated the function of Ecm29 in stress response. KIAA0368-deficient mice showed normal peptidase activity and proteasome formation at normal condition. Under stressed condition, 26S proteasome dissociates in wild-type cells, but not in KIAA0368(-/-) cells. This response was correlated with efficient degradation of damaged proteins and resistance to oxidative stress of KIAA0368(-/-) cells. Thus, Ecm29 is involved in the dissociation process of 26S proteasome, providing clue to analyse the mechanism of proteasomal degradation under various stress condition."xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.org/dc/terms/identifier | "doi:10.1093/jb/mvw006"xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.org/dc/terms/identifier | "doi:10.1093/jb/mvw006"xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/author | "Sato A."xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/author | "Sato A."xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/author | "Tsuruta F."xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/author | "Tsuruta F."xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/author | "Chiba T."xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/author | "Chiba T."xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/author | "Haratake K."xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/author | "Haratake K."xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/name | "J. Biochem."xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/name | "J. Biochem."xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/pages | "609-618"xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/pages | "609-618"xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/title | "KIAA0368-deficiency affects disassembly of 26S proteasome under oxidative stress condition."xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/title | "KIAA0368-deficiency affects disassembly of 26S proteasome under oxidative stress condition."xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/volume | "159"xsd:string |
http://purl.uniprot.org/citations/26802743 | http://purl.uniprot.org/core/volume | "159"xsd:string |
http://purl.uniprot.org/citations/26802743 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/26802743 |
http://purl.uniprot.org/citations/26802743 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/26802743 |