| http://purl.uniprot.org/citations/10704466 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10704466 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10704466 | http://www.w3.org/2000/01/rdf-schema#comment | "The mitogen-activated protein (MAP) kinase p38 is a key component of stress response pathways and the target of cytokine-suppressing antiinflammatory drugs (CSAIDs). A genetic approach was employed to inactivate the gene encoding one p38 isoform, p38alpha. Mice null for the p38alpha allele die during embryonic development. p38alpha(1/)-embryonic stem (ES) cells grown in the presence of high neomycin concentrations demonstrated conversion of the wild-type allele to a targeted allele. p38alpha(-/)-ES cells lacked p38alpha protein and failed to activate MAP kinase-activated protein (MAPKAP) kinase 2 in response to chemical stress inducers. In contrast, p38alpha(1/+) ES cells and primary embryonic fibroblasts responded to stress stimuli and phosphorylated p38alpha, and activated MAPKAP kinase 2. After in vitro differentiation, both wild-type and p38alpha(-/)-ES cells yielded cells that expressed the interleukin 1 receptor (IL-1R). p38alpha(1/+) but not p38alpha(-/)-IL-1R-positive cells responded to IL-1 activation to produce IL-6. Comparison of chemical-induced apoptosis processes revealed no significant difference between the p38alpha(1/+) and p38alpha(-/)-ES cells. Therefore, these studies demonstrate that p38alpha is a major upstream activator of MAPKAP kinase 2 and a key component of the IL-1 signaling pathway. However, p38alpha does not serve an indispensable role in apoptosis."xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.org/dc/terms/identifier | "doi:10.1084/jem.191.5.859"xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.org/dc/terms/identifier | "doi:10.1084/jem.191.5.859"xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/author | "Svensson L."xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/author | "Svensson L."xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/author | "Allen M."xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/author | "Allen M."xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/author | "Hambor J."xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/author | "Hambor J."xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/author | "Gabel C.A."xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/author | "Gabel C.A."xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/author | "McNeish J."xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/author | "McNeish J."xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/author | "Roach M."xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/author | "Roach M."xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/name | "J. Exp. Med."xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/name | "J. Exp. Med."xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/pages | "859-870"xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/pages | "859-870"xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/title | "Deficiency of the stress kinase p38alpha results in embryonic lethality: characterization of the kinase dependence of stress responses of enzyme-deficient embryonic stem cells."xsd:string |
| http://purl.uniprot.org/citations/10704466 | http://purl.uniprot.org/core/title | "Deficiency of the stress kinase p38alpha results in embryonic lethality: characterization of the kinase dependence of stress responses of enzyme-deficient embryonic stem cells."xsd:string |