Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations
Copyright policy )Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations
Cancer-associated mutations in the catalytically inactive receptor HER3 enhance its ability to activate other members of the human epidermal growth factor receptor family.
- University of California, San Francisco United States
- King’s University United States
- Columbia University United States
- D. E. Shaw Research United States
Models, Molecular, Protein Structure, Receptor, ErbB-3, 1.1 Normal biological development and functioning, Molecular Dynamics Simulation, Underpinning research, Models, ErbB-3, 2.1 Biological and endogenous factors, Site-Directed, erbB-3, Humans, Aetiology, Cloning, Molecular, Cancer, Molecular, Biological Sciences, Protein Structure, Tertiary, ErbB Receptors, Mutagenesis, Biochemistry and cell biology, Mutation, Mutagenesis, Site-Directed, Biochemistry and Cell Biology, Crystallization, Dimerization, Tertiary, Cloning, Receptor, Signal Transduction
Models, Molecular, Protein Structure, Receptor, ErbB-3, 1.1 Normal biological development and functioning, Molecular Dynamics Simulation, Underpinning research, Models, ErbB-3, 2.1 Biological and endogenous factors, Site-Directed, erbB-3, Humans, Aetiology, Cloning, Molecular, Cancer, Molecular, Biological Sciences, Protein Structure, Tertiary, ErbB Receptors, Mutagenesis, Biochemistry and cell biology, Mutation, Mutagenesis, Site-Directed, Biochemistry and Cell Biology, Crystallization, Dimerization, Tertiary, Cloning, Receptor, Signal Transduction
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