| http://purl.uniprot.org/citations/7518429 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7518429 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7518429 | http://www.w3.org/2000/01/rdf-schema#comment | "We have studied the signal transduction pathways of fibroblast growth factor receptor-4 (FGFR-4) and FGFR-1, which showed virtually identical acidic fibroblast growth factor binding profiles as well as tyrosine autophosphorylation upon activation in transfected L6 rat myoblasts and NIH3T3 mouse fibroblasts. A prominently tyrosyl-phosphorylated doublet of polypeptides of 85 kDa coprecipitated with activated FGFR-4 from both cell lines studied, but these polypeptides were not detected upon immunoprecipitation of activated FGFR-1. Furthermore, FGFR-4 induced only a weak tyrosyl phosphorylation of phospholipase C-gamma and no detectable tyrosyl phosphorylation of the SHC adaptor proteins in contrast to FGFR-1. No phosphorylation of Ras GTPase-activating protein, p64 Syp/PTP1D tyrosine phosphatase, or association of the GRB2 adaptor protein SH2 domain with these receptors was detected. Unlike FGFR-1, FGFR-4 induced only a barely detectable phosphorylation of the cellular serine/threonine kinase Raf-1 and a weaker tyrosyl phosphorylation of mitogen-activated protein kinases than FGFR-1. Despite these differences, stimulation of both receptors resulted in increased DNA synthesis."xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(17)32309-8"xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(17)32309-8"xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/author | "Pelicci P.G."xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/author | "Pelicci P.G."xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/author | "Joukov V."xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/author | "Joukov V."xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/author | "Bergman M."xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/author | "Bergman M."xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/author | "Alitalo K."xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/author | "Alitalo K."xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/author | "Vainikka S."xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/author | "Vainikka S."xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/author | "Wennstrom S."xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/author | "Wennstrom S."xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/pages | "18320-18326"xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/pages | "18320-18326"xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/title | "Signal transduction by fibroblast growth factor receptor-4 (FGFR-4). Comparison with FGFR-1."xsd:string |
| http://purl.uniprot.org/citations/7518429 | http://purl.uniprot.org/core/title | "Signal transduction by fibroblast growth factor receptor-4 (FGFR-4). Comparison with FGFR-1."xsd:string |