TNFR1 signaling is associated with backbone conformational changes of receptor dimers consistent with overactivation in the R92Q TRAPS mutant

Keyphrases

• Conformational Change 100%
• Ligand Binding 100%
• Tumor Necrosis Factor-α 100%
• Receptor Dimerization 100%
• R92Q 100%
• Overactivation 100%
• Network Formation 40%
• Structural Change 20%
• Ligand-independent 20%
• Ligand-receptor Binding 20%
• Oligomeric 20%
• Induced Activation 20%
• Receptor Activation 20%
• Intracellular Signaling 20%
• High Molecular Weight 20%
• Conformational Transition 20%
• Cytoplasmic Domain 20%
• Backbone Dynamics 20%
• Constitutively Active 20%
• Trimerization 20%
• Constitutive Behavior 20%
• Normal Mode Analysis 20%
• Dynamic Coupling 20%
• Active Conformation 20%
• Receptor Structure 20%
• Domain Mobility 20%

Biochemistry, Genetics and Molecular Biology

• Conformational Change 100%
• Ligand Binding 100%
• Tumor Necrosis Factor 100%
• Conformation 40%
• Fluorescence Resonance Energy Transfer 20%
• Dynamics 20%
• Wild Type 20%
• Crystal Structure 20%
• Intracellular Signaling 20%
• Molecular Weight 20%