Oligomerization-dependent changes in the thermodynamic properties of the TPR-MET receptor tyrosine kinase

Keyphrases

• Receptor Tyrosine Kinase 100%
• Thermodynamic Properties 100%
• Oligomerization 100%
• C-Met 83%
• Cytoplasmic Domain 50%
• MET Receptor 50%
• Oligomeric 33%
• Peptide Substrate 33%
• Oncoprotein 33%
• Substrate Binding 33%
• Oligomeric State 33%
• Phosphotyrosine Peptides 33%
• ATP Binding 16%
• Receptor Signaling 16%
• Conformational Change 16%
• Equilibrium Binding 16%
• Receptor Activation 16%
• Mechanistic Insight 16%
• Binding Region 16%
• Kinase Activation 16%
• Dissociation Constant 16%
• Binding Affinity 16%
• Coiled Coil 16%
• Binding Thermodynamics 16%
• Binding Conditions 16%
• Binding Kinetics 16%
• Dissociation Rate Constant 16%
• Thermodynamic Analysis 16%
• Stopped-flow Analysis 16%
• Dimerization Domain 16%
• C-terminal Tail 16%
• Folding Rate 16%
• Binding Data 16%
• Affinity Kinetics 16%
• Nuclear Pore Complex 16%
• Equilibrium Dissociation Constant 16%
• Active Fusion 16%
• MET Protein Expression 16%
• Association Rate Constant 16%
• Thermodynamic Changes 16%

Biochemistry, Genetics and Molecular Biology

• Receptor Tyrosine Kinase 100%
• Oligomerization 100%
• Phosphotransferase 85%
• Kinase 85%
• Adenosine Triphosphate 42%
• Tyrosine 28%
• Dissociation Constant 28%
• Binding Affinity 14%
• Conformational Change 14%
• C-Terminus 14%
• Dimerization 14%
• Coiled Coil 14%
• Binding Kinetics 14%
• Dissociation Rate Constant 14%
• Nuclear Pore Complex 14%
• Association Rate Constant 14%