Two Gα_i1 rate-modifying mutations act in concert to allow receptor-independent, steady-state measurements of RGS protein activity

Keyphrases

• Receptor-independent 100%
• Protein Activity 100%
• RGS Proteins 100%
• Steady-state Measurement 100%
• Guanosine Diphosphate 83%
• Guanosine Triphosphate 66%
• GTPase 50%
• G Protein-coupled Receptor Signaling 33%
• Monoclonal Antibody 16%
• Therapeutic Target 16%
• Hydrolysis 16%
• Steady State 16%
• Domain-domain Interaction 16%
• Binding Studies 16%
• Dissociation 16%
• Molecular Binding 16%
• Non-radioactive 16%
• GTPase Activity 16%
• Hydrolysis Rate 16%
• Detection Assay 16%
• Solution Phase 16%
• Fluorescence Polarization Immunoassay 16%
• Homogeneous Detection 16%
• Selective Modulation 16%
• Protein Effect 16%
• Transcreener 16%

Biochemistry, Genetics and Molecular Biology

• Steady State 100%
• Regulator of G Protein Signalling 100%
• Guanosine Diphosphate 83%
• Guanosine Triphosphate 66%
• GTPase 66%
• G Protein Coupled Receptor 50%
• Enzymatic Hydrolysis 33%
• Monoclonal Antibody 16%
• Immunoassay 16%
• Solution and Solubility 16%
• Binding Study 16%

Pharmacology, Toxicology and Pharmaceutical Science

• Receptor 100%
• RGS Protein 100%
• Guanosine Diphosphate 83%
• Guanosine Triphosphate 66%
• Guanosine Triphosphatase 66%
• G Protein Coupled Receptor 50%
• Monoclonal Antibody 16%
• Immunoassay 16%