http://purl.uniprot.org/citations/17708934 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17708934 | http://www.w3.org/2000/01/rdf-schema#comment | "The activity of most protein kinases is highly regulated, typically via phosphorylation and/or subunit association. However, the folding of protein kinases into an active state or a form capable of activation is now emerging as another important step through which they can be regulated. The 50-kDa protein Cdc37 and the associated heat-shock protein Hsp90 have been found to bind to, and be required for the activity of, diverse protein kinases, including Cdk4, v-Src, Raf and SEVENLESS. Together, Cdc37 and Hsp90 may act as a general chaperone for protein kinases, in particular those involved in signal-transduction pathways and cell-cycle control."xsd:string |
http://purl.uniprot.org/citations/17708934 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0962-8924(97)01027-1"xsd:string |
http://purl.uniprot.org/citations/17708934 | http://purl.uniprot.org/core/author | "Hunter T."xsd:string |
http://purl.uniprot.org/citations/17708934 | http://purl.uniprot.org/core/author | "Poon R.Y."xsd:string |
http://purl.uniprot.org/citations/17708934 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
http://purl.uniprot.org/citations/17708934 | http://purl.uniprot.org/core/name | "Trends Cell Biol"xsd:string |
http://purl.uniprot.org/citations/17708934 | http://purl.uniprot.org/core/pages | "157-161"xsd:string |
http://purl.uniprot.org/citations/17708934 | http://purl.uniprot.org/core/title | "Cdc37: a protein kinase chaperone?"xsd:string |
http://purl.uniprot.org/citations/17708934 | http://purl.uniprot.org/core/volume | "7"xsd:string |
http://purl.uniprot.org/citations/17708934 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17708934 |
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