title: Receptor signaling: when dimerization is not enough.
abstract: Activation of receptors that signal via tyrosine kinase domains has been thought to involve receptor dimerization and transphosphorylation of juxtaposed catalytic domains. Recent results suggest things might be more complex - specific intersubunit conformational changes within a dimer can also be important.
authors.affiliation: Molecular Biology and Virology Laboratory, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, California 92037, USA.
authors.forename: G
authors.initials: G
authors.lastname: Jiang
authors.forename: T
authors.initials: T
authors.lastname: Hunter
mesh_terms: D000818:Animals; D019281:Dimerization; D008958:Models, Molecular; D010766:Phosphorylation; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000378:metabolism*; D017467:Receptors, Erythropoietin / Q000737:chemistry / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D011956:Receptors, Cell Surface; D017467:Receptors, Erythropoietin