http://purl.uniprot.org/citations/26083744 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/26083744 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/26083744 | http://www.w3.org/2000/01/rdf-schema#comment | "The anaphase-promoting complex (APC/C) is a multimeric RING E3 ubiquitin ligase that controls chromosome segregation and mitotic exit. Its regulation by coactivator subunits, phosphorylation, the mitotic checkpoint complex and interphase early mitotic inhibitor 1 (Emi1) ensures the correct order and timing of distinct cell-cycle transitions. Here we use cryo-electron microscopy to determine atomic structures of APC/C-coactivator complexes with either Emi1 or a UbcH10-ubiquitin conjugate. These structures define the architecture of all APC/C subunits, the position of the catalytic module and explain how Emi1 mediates inhibition of the two E2s UbcH10 and Ube2S. Definition of Cdh1 interactions with the APC/C indicates how they are antagonized by Cdh1 phosphorylation. The structure of the APC/C with UbcH10-ubiquitin reveals insights into the initiating ubiquitination reaction. Our results provide a quantitative framework for the design of future experiments to investigate APC/C functions in vivo."xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.org/dc/terms/identifier | "doi:10.1038/nature14471"xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.org/dc/terms/identifier | "doi:10.1038/nature14471"xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/author | "Barford D."xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/author | "Barford D."xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/author | "Chang L."xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/author | "Chang L."xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/author | "McLaughlin S.H."xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/author | "McLaughlin S.H."xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/author | "Yang J."xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/author | "Yang J."xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/author | "Zhang Z."xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/author | "Zhang Z."xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/pages | "450-454"xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/pages | "450-454"xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/title | "Atomic structure of the APC/C and its mechanism of protein ubiquitination."xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/title | "Atomic structure of the APC/C and its mechanism of protein ubiquitination."xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/volume | "522"xsd:string |
http://purl.uniprot.org/citations/26083744 | http://purl.uniprot.org/core/volume | "522"xsd:string |