Mutational study of the EGFR feedback monomerization at the PLCγ binding sites.
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posted on 2015-10-14, 04:12 authored by Malgorzata Kluba, Yves Engelborghs, Johan Hofkens, Hideaki Mizunoa F stands for the phosphodeficient mutation (phenylalanine substitution).
b The strength of negative feedback scaled from as strong as for the EGFRwt (+ +) to none (—).
c, d Minimum (Dmin) and maximum (Dmax) level of the diffusion coefficient.
e The diffusion coefficient averaged over the whole measurement time after EGF addition (Davg).
f Not determinable.
Mutational study of the EGFR feedback monomerization at the PLCγ binding 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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