View : 651 Download: 326

Full metadata record

DC Field Value Language
dc.contributor.author이공주-
dc.date.accessioned2016-08-28T10:08:35Z-
dc.date.available2016-08-28T10:08:35Z-
dc.date.issued2013-
dc.identifier.issn0021-9258-
dc.identifier.otherOAK-9847-
dc.identifier.urihttps://dspace.ewha.ac.kr/handle/2015.oak/223513-
dc.description.abstractBackground: 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.languageEnglish-
dc.titleComplex of fas-associated Factor 1 (FAF1) with valosin-containing protein (VCP)-Npl4-Ufd1 and polyubiquitinated proteins promotes endoplasmic reticulum-associated degradation (ERAD)S-
dc.typeArticle-
dc.relation.issue10-
dc.relation.volume288-
dc.relation.indexSCI-
dc.relation.indexSCIE-
dc.relation.indexSCOPUS-
dc.relation.startpage6998-
dc.relation.lastpage7011-
dc.relation.journaltitleJournal of Biological Chemistry-
dc.identifier.doi10.1074/jbc.M112.417576-
dc.identifier.wosidWOS:000316002400022-
dc.identifier.scopusid2-s2.0-84874871591-
dc.author.googleLee J.-J.-
dc.author.googlePark J.K.-
dc.author.googleJeong J.-
dc.author.googleJeon H.-
dc.author.googleYoon J.-B.-
dc.author.googleKim E.E.-
dc.author.googleLee K.-J.-
dc.contributor.scopusid이공주(7501497635;57191532162)-
dc.date.modifydate20230208115507-
Appears in Collections:
약학대학 > 약학과 > Journal papers
Files in This Item:
001.pdf(6.83 MB) Download
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

BROWSE