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
Author:
Affiliation:
1. Department of Biosciences, University of Nottingham, Nottingham, U.K.
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi201269w
Reference48 articles.
1. Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185
2. Increased tyrosine kinase activity associated with the protein encoded by the activated neu oncogene.
3. Oncogenic activation of the neu-encoded receptor protein by point mutation and deletion.
4. A point mutation in the neu oncogene mimics ligand induction of receptor aggregation
5. Sequence-Dependent Oligomerization of the Neu Transmembrane Domain Suggests Inhibition of “Conformational Switching” by an Oncogenic Mutant
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