| http://purl.uniprot.org/citations/20837704 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20837704 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20837704 | http://www.w3.org/2000/01/rdf-schema#comment | "The mechanisms by which signals are transmitted across the plasma membrane to regulate signaling are largely unknown for receptors with single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR). A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility. The crystal structure and disulfide cross-linking suggest that the 7-residue linker between the extracellular and transmembrane domains is flexible. Disulfide cross-linking of the transmembrane domain shows that EGF stimulates only moderate association in the first two α-helical turns, in contrast to association throughout the membrane over five α-helical turns in glycophorin A and integrin. Furthermore, systematic mutagenesis to leucine and phenylalanine suggests that no specific transmembrane interfaces are required for EGFR kinase activation. These results suggest that linkage between ligand-induced dimerization and tyrosine kinase activation is much looser than was previously envisioned."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.00742-10"xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.00742-10"xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/author | "Lu C."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/author | "Lu C."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/author | "Yokoyama S."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/author | "Yokoyama S."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/author | "Zhu J."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/author | "Zhu J."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/author | "Springer T.A."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/author | "Springer T.A."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/author | "Mi L.Z."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/author | "Mi L.Z."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/author | "Graef E."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/author | "Graef E."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/author | "Grey M.J."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/author | "Grey M.J."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/name | "Mol. Cell. Biol."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/name | "Mol. Cell. Biol."xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/pages | "5432-5443"xsd:string |
| http://purl.uniprot.org/citations/20837704 | http://purl.uniprot.org/core/pages | "5432-5443"xsd:string |