| http://purl.uniprot.org/citations/19498169 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19498169 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19498169 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/19498169 | http://www.w3.org/2000/01/rdf-schema#comment | "All living organisms face a variety of environmental stresses that cause the misfolding and aggregation of proteins. To eliminate damaged proteins, cells developed highly efficient stress response and protein quality control systems. We performed a biochemical and structural analysis of the bacterial CtsR/McsB stress response. The crystal structure of the CtsR repressor, in complex with DNA, pinpointed key residues important for high-affinity binding to the promoter regions of heat-shock genes. Moreover, biochemical characterization of McsB revealed that McsB specifically phosphorylates arginine residues in the DNA binding domain of CtsR, thereby impairing its function as a repressor of stress response genes. Identification of the CtsR/McsB arginine phospho-switch expands the repertoire of possible protein modifications involved in prokaryotic and eukaryotic transcriptional regulation."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.org/dc/terms/identifier | "doi:10.1126/science.1170088"xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.org/dc/terms/identifier | "doi:10.1126/science.1170088"xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/author | "Lehner A."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/author | "Lehner A."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/author | "Charpentier E."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/author | "Charpentier E."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/author | "Schmidt A."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/author | "Schmidt A."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/author | "Fuhrmann J."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/author | "Fuhrmann J."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/author | "Mechtler K."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/author | "Mechtler K."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/author | "Clausen T."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/author | "Clausen T."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/author | "Spiess S."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/author | "Spiess S."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/author | "Turgay K."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/author | "Turgay K."xsd:string |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19498169 | http://purl.uniprot.org/core/name | "Science"xsd:string |