TY - DATA T1 - Mutational study of the EGFR monomer-dimer equilibrium at the JM domain phosphorylation sites. PY - 2015/10/14 AU - Malgorzata Kluba AU - Yves Engelborghs AU - Johan Hofkens AU - Hideaki Mizuno UR - https://plos.figshare.com/articles/dataset/_Mutational_study_of_the_EGFR_monomer_dimer_equilibrium_at_the_JM_domain_phosphorylation_sites_/1575198 DO - 10.1371/journal.pone.0139971.t002 L4 - https://ndownloader.figshare.com/files/2359440 KW - EGFR dimer formation KW - receptor monomerization KW - monomeric state KW - feedback loop KW - pkd KW - epidermal growth factor receptor KW - protein kinase D KW - EGFR Signaling Dimerization KW - feedback mechanism KW - juxtamembrane threonine residues KW - raster image correlation spectroscopy KW - Signal transduction KW - dimerization state KW - oscillatory behavior KW - Receptor Dimerization KW - 2.5 min N2 - a A and E stand for the phosphodeficient and phosphomimic mutation (alanine and glutamate substitution, respectively).b The state towards which the monomer-dimer equilibrium is shifted after EGF addition.c, d Minimum (Dmin) and maximum (Dmax) level of the diffusion coefficient.e Not determinable.Mutational study of the EGFR monomer-dimer equilibrium at the JM domain phosphorylation sites. ER -