Kluba, Malgorzata Engelborghs, Yves Hofkens, Johan Mizuno, Hideaki Mutational study of the EGFR feedback monomerization at the PLCγ binding sites. <p><sup>a</sup> F stands for the phosphodeficient mutation (phenylalanine substitution).</p><p><sup>b</sup> The strength of negative feedback scaled from as strong as for the EGFR<sup>wt</sup> (+ +) to none (—).</p><p><sup>c, d</sup> Minimum (D<sub>min</sub>) and maximum (D<sub>max</sub>) level of the diffusion coefficient.</p><p><sup>e</sup> The diffusion coefficient averaged over the whole measurement time after EGF addition (D<sub>avg</sub>).</p><p><sup>f</sup> Not determinable.</p><p>Mutational study of the EGFR feedback monomerization at the PLCγ binding sites.</p> EGFR dimer formation;receptor monomerization;monomeric state;feedback loop;pkd;epidermal growth factor receptor;protein kinase D;EGFR Signaling Dimerization;feedback mechanism;juxtamembrane threonine residues;raster image correlation spectroscopy;Signal transduction;dimerization state;oscillatory behavior;Receptor Dimerization;2.5 min 2015-10-14
    https://plos.figshare.com/articles/dataset/_Mutational_study_of_the_EGFR_feedback_monomerization_at_the_PLC_947_binding_sites_/1575197
10.1371/journal.pone.0139971.t001