Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 이공주 | - |
dc.date.accessioned | 2016-08-28T10:08:35Z | - |
dc.date.available | 2016-08-28T10:08:35Z | - |
dc.date.issued | 2013 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.other | OAK-9847 | - |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/223513 | - |
dc.description.abstract | Background: FAF1, which has multiple ubiquitin-like domains, interacts with various proteins (VCP, Hsp70, and polyubiquitinated proteins). Results: Association of FAF1 UBX with VCP-Npl4-Ufd1 complex regulates ubiquitin binding to FAF1 UBA domain and promotes CD3 degradation in ERAD. Conclusion: FAF1 is a ubiquitin receptor that promotes ERAD by delivering polyubiquitinated proteins from UBX domain to UBA domain. Significance: FAF1 plays a role in ERAD by modulating domain-domain interaction. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc. | - |
dc.language | English | - |
dc.title | Complex of fas-associated Factor 1 (FAF1) with valosin-containing protein (VCP)-Npl4-Ufd1 and polyubiquitinated proteins promotes endoplasmic reticulum-associated degradation (ERAD)S | - |
dc.type | Article | - |
dc.relation.issue | 10 | - |
dc.relation.volume | 288 | - |
dc.relation.index | SCI | - |
dc.relation.index | SCIE | - |
dc.relation.index | SCOPUS | - |
dc.relation.startpage | 6998 | - |
dc.relation.lastpage | 7011 | - |
dc.relation.journaltitle | Journal of Biological Chemistry | - |
dc.identifier.doi | 10.1074/jbc.M112.417576 | - |
dc.identifier.wosid | WOS:000316002400022 | - |
dc.identifier.scopusid | 2-s2.0-84874871591 | - |
dc.author.google | Lee J.-J. | - |
dc.author.google | Park J.K. | - |
dc.author.google | Jeong J. | - |
dc.author.google | Jeon H. | - |
dc.author.google | Yoon J.-B. | - |
dc.author.google | Kim E.E. | - |
dc.author.google | Lee K.-J. | - |
dc.contributor.scopusid | 이공주(7501497635;57191532162) | - |
dc.date.modifydate | 20230208115507 | - |