http://purl.uniprot.org/citations/20551172 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/20551172 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/20551172 | http://www.w3.org/2000/01/rdf-schema#comment | "Rapid Myc protein turnover is critical for maintaining basal levels of Myc activity in normal cells and a prompt response to changing growth signals. We characterize a new Myc-interacting factor, TRPC4AP (transient receptor potential cation channel, subfamily C, member 4-associated protein)/TRUSS (tumor necrosis factor receptor-associated ubiquitous scaffolding and signaling protein), which is the receptor for a DDB1 (damage-specific DNA-binding protein 1)-CUL4 (Cullin 4) E3 ligase complex for selective Myc degradation through the proteasome. TRPC4AP/TRUSS binds specifically to the Myc C terminus and promotes its ubiquitination and destruction through the recognition of evolutionarily conserved domains in the Myc N terminus. TRPC4AP/TRUSS suppresses Myc-mediated transactivation and transformation in a dose-dependent manner. Finally, we found that TRPC4AP/TRUSS expression is strongly down-regulated in most cancer cell lines, leading to Myc protein stabilization. These studies identify a novel pathway targeting Myc degradation that is suppressed in cancer cells."xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.org/dc/terms/identifier | "doi:10.1101/gad.1920310"xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.org/dc/terms/identifier | "doi:10.1101/gad.1920310"xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/author | "Gerber S.A."xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/author | "Gerber S.A."xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/author | "Choi S.H."xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/author | "Choi S.H."xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/author | "Cole M.D."xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/author | "Cole M.D."xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/author | "Wright J.B."xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/author | "Wright J.B."xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/name | "Genes Dev."xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/name | "Genes Dev."xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/pages | "1236-1241"xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/pages | "1236-1241"xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/title | "Myc protein is stabilized by suppression of a novel E3 ligase complex in cancer cells."xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/title | "Myc protein is stabilized by suppression of a novel E3 ligase complex in cancer cells."xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/volume | "24"xsd:string |
http://purl.uniprot.org/citations/20551172 | http://purl.uniprot.org/core/volume | "24"xsd:string |
http://purl.uniprot.org/citations/20551172 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20551172 |
http://purl.uniprot.org/citations/20551172 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20551172 |