| http://purl.uniprot.org/citations/15200949 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15200949 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15200949 | http://www.w3.org/2000/01/rdf-schema#comment | "The cell division cycle of the yeast S. cerevisiae is driven by one Cdk (cyclin-dependent kinase), which becomes active when bound to one of nine cyclin subunits. Elucidation of Cdk substrates and other Cdk-associated proteins is essential for a full understanding of the cell cycle. Here, we report the results of a targeted proteomics study using affinity purification coupled to mass spectrometry. Our study identified numerous proteins in association with particular cyclin-Cdk complexes. These included phosphorylation substrates, ubiquitination-degradation proteins, adaptors, and inhibitors. Some associations were previously known, and for others, we confirmed their specificity and biological relevance. Using a hypothesis-driven mass spectrometric approach, we also mapped in vivo phosphorylation at Cdk consensus motif-containing peptides within several cyclin-associated candidate Cdk substrates. Our results demonstrate that this approach can be used to detect a host of transient and dynamic protein associations within a biological module."xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2004.05.025"xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2004.05.025"xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/author | "Chait B.T."xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/author | "Chait B.T."xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/author | "Rout M.P."xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/author | "Rout M.P."xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/author | "Cross F.R."xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/author | "Cross F.R."xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/author | "Archambault V."xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/author | "Archambault V."xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/author | "Drapkin B.J."xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/author | "Drapkin B.J."xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/author | "Chang E.J."xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/author | "Chang E.J."xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/pages | "699-711"xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/pages | "699-711"xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/title | "Targeted proteomic study of the cyclin-Cdk module."xsd:string |
| http://purl.uniprot.org/citations/15200949 | http://purl.uniprot.org/core/title | "Targeted proteomic study of the cyclin-Cdk module."xsd:string |