Kluba, Malgorzata Engelborghs, Yves Hofkens, Johan Mizuno, Hideaki Mutational study of the EGFR monomer-dimer equilibrium at the JM domain phosphorylation sites. <p><sup>a</sup> A and E stand for the phosphodeficient and phosphomimic mutation (alanine and glutamate substitution, respectively).</p><p><sup>b</sup> The state towards which the monomer-dimer equilibrium is shifted after EGF addition.</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> Not determinable.</p><p>Mutational study of the EGFR monomer-dimer equilibrium at the JM domain phosphorylation 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_monomer_dimer_equilibrium_at_the_JM_domain_phosphorylation_sites_/1575198
10.1371/journal.pone.0139971.t002