New insights into human prostacyclin receptor structure and function through natural and synthetic mutations of transmembrane charged residues

Keyphrases

• Receptor Function 100%
• Transmembrane 100%
• Receptor Structure 100%
• Charged Residue 100%
• Prostacyclin Receptor 100%
• Salt Bridge 40%
• Induced Activation 20%
• Glutamine 20%
• G Protein-coupled Receptor 20%
• Cardiovascular Disease 20%
• Potential Interaction 20%
• Mutagenesis 20%
• Fold Increase 20%
• Platelets 20%
• Protective Behavior 20%
• Cardiovascular System 20%
• Vascular Smooth muscle Cells 20%
• Rational Design 20%
• Binding Pocket 20%
• Agonist Binding 20%
• Basal Activity 20%
• Transmembrane Helix 20%
• DNA Samples 20%
• Human Genomic DNA 20%
• Affective Expression 20%
• Naturally Occurring mutations 20%
• Human mutations 20%
• Full Agonist 20%
• Hydrophilic Residue 20%
• Core Residue 20%
• Prostacyclin Receptor Agonist 20%
• H-bond Network 20%

Pharmacology, Toxicology and Pharmaceutical Science

• G Protein Coupled Receptor 100%
• Prostacyclin Receptor 100%
• Receptor 50%
• Prostacyclin 50%
• Alanine 50%
• Mutagenesis 50%
• Glutamine 50%
• Genomic DNA 50%
• Hydrogen Bond 50%
• Cardiovascular Disease 50%

Biochemistry, Genetics and Molecular Biology

• Agonist 100%
• Prostacyclin Receptor 100%
• G Protein Coupled Receptor 50%
• Glutamine 25%
• Mutagenesis 25%
• Human Genomics 25%
• Prostacyclin 25%
• Platelet 25%
• Alanine 25%
• Deficiency 25%