Mutational study of the EGFR monomer-dimer equilibrium at the JM domain phosphorylation sites.
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posted on 2015-10-14, 04:12 authored by Malgorzata Kluba, Yves Engelborghs, Johan Hofkens, Hideaki Mizunoa 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.
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EGFR dimer formationreceptor monomerizationmonomeric statefeedback looppkdepidermal growth factor receptorprotein kinase DEGFR Signaling Dimerizationfeedback mechanismjuxtamembrane threonine residuesraster image correlation spectroscopySignal transductiondimerization stateoscillatory behaviorReceptor Dimerization2.5 min
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