| http://purl.uniprot.org/citations/1688559 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1688559 | http://www.w3.org/2000/01/rdf-schema#comment | "The human epidermal growth factor receptor (EGFR) contains a large C' terminus distal to the protein tyrosine kinase domain that is conserved among members of its extended gene family. To investigate the C' terminus, a series of mutant EGFR cDNAs encoding progressive C'-terminal deletions were prepared and expressed in null recipient B82L cells. In vivo self-phosphorylation was retained in receptors truncated to residues 1052 and 1022 which lack the three identified sites of tyrosine self-phosphorylation. Receptors truncated to residue 991 did not undergo in vivo self-phosphorylation. Purified 1022 truncated receptor was self-phosphorylated to the extent of 1 mol of phosphate/mol of receptor protein. The deduced additional site of tyrosine self-phosphorylation at residue 992 was confirmed by tryptic phosphopeptide mapping and protein sequencing. EGFRs deleted to give C'-terminal residues 1052, 1022, 991, and 973 exhibited enhanced EGF-stimulated tyrosine phosphorylation of cell substrates in vivo, whereas deletion at residue 944 abolished all detectable EGF-stimulated protein tyrosine phosphorylation. These results indicate that ligand-induced self-phosphorylation is limited to the C' terminus of the EGFR and suggest that this region of the holoreceptor has an inhibitory function."xsd:string |
| http://purl.uniprot.org/citations/1688559 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(19)40080-x"xsd:string |
| http://purl.uniprot.org/citations/1688559 | http://purl.uniprot.org/core/author | "Rosenfeld M.G."xsd:string |
| http://purl.uniprot.org/citations/1688559 | http://purl.uniprot.org/core/author | "Chen W.S."xsd:string |
| http://purl.uniprot.org/citations/1688559 | http://purl.uniprot.org/core/author | "Gill G.N."xsd:string |
| http://purl.uniprot.org/citations/1688559 | http://purl.uniprot.org/core/author | "Walton G.M."xsd:string |
| http://purl.uniprot.org/citations/1688559 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
| http://purl.uniprot.org/citations/1688559 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/1688559 | http://purl.uniprot.org/core/pages | "1750-1754"xsd:string |
| http://purl.uniprot.org/citations/1688559 | http://purl.uniprot.org/core/title | "Analysis of deletions of the carboxyl terminus of the epidermal growth factor receptor reveals self-phosphorylation at tyrosine 992 and enhanced in vivo tyrosine phosphorylation of cell substrates."xsd:string |
| http://purl.uniprot.org/citations/1688559 | http://purl.uniprot.org/core/volume | "265"xsd:string |
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