Molecular dynamics (MD) investigations of preformed structures of the transmembrane domain of the oncogenic Neu receptor dimer in a DMPC bilayer
Author:
Publisher
Wiley
Subject
Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics
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1. Lipid-dependent conformational landscape of the ErbB2 growth factor receptor dimers;Chemistry and Physics of Lipids;2020-08
2. Sequence dependent lipid-mediated effects modulate the dimerization of ErbB2 and its associative mutants;Physical Chemistry Chemical Physics;2013
3. Effects of the Oncogenic V664E Mutation on Membrane Insertion, Structure, and Sequence-Dependent Interactions of the Neu Transmembrane Domain in Micelles and Model Membranes: An Integrated Biophysical and Simulation Study;Biochemistry;2012-03-14
4. Sequence-Dependent Oligomerization of the Neu Transmembrane Domain Suggests Inhibition of “Conformational Switching” by an Oncogenic Mutant;Biochemistry;2010-03-10
5. Ectodomain orientation, conformational plasticity and oligomerization of ErbB1 receptors investigated by molecular dynamics;Journal of Structural Biology;2009-08
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