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http://purl.uniprot.org/citations/23453757http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23453757http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23453757http://www.w3.org/2000/01/rdf-schema#comment"The modular SCF (Skp1, cullin, and F box) ubiquitin ligases feature a large family of F box protein substrate receptors that enable recognition of diverse targets. However, how the repertoire of SCF complexes is sustained remains unclear. Real-time measurements of formation and disassembly indicate that SCF(Fbxw7) is extraordinarily stable, but, in the Nedd8-deconjugated state, the cullin-binding protein Cand1 augments its dissociation by one-million-fold. Binding and ubiquitylation assays show that Cand1 is a protein exchange factor that accelerates the rate at which Cul1-Rbx1 equilibrates with multiple F box protein-Skp1 modules. Depletion of Cand1 from cells impedes recruitment of new F box proteins to pre-existing Cul1 and profoundly alters the cellular landscape of SCF complexes. We suggest that catalyzed protein exchange may be a general feature of dynamic macromolecular machines and propose a hypothesis for how substrates, Nedd8, and Cand1 collaborate to regulate the cellular repertoire of SCF complexes."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2013.02.024"xsd:string
http://purl.uniprot.org/citations/23453757http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2013.02.024"xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Liu X."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Liu X."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Zheng N."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Zheng N."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Lee J.E."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Lee J.E."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Hess S."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Hess S."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Clurman B.E."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Clurman B.E."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Deshaies R.J."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Deshaies R.J."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Shan S.O."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Shan S.O."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Graham R.L."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Graham R.L."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Pierce N.W."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Pierce N.W."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Larimore E.A."xsd:string
http://purl.uniprot.org/citations/23453757http://purl.uniprot.org/core/author"Larimore E.A."xsd:string