Lysine trimethylation of retinoic acid receptor-α: A novel means to regulate receptor function

Keyphrases

• Lysine 100%
• Retinoic Acid Receptor 100%
• Receptor Function 100%
• Trimethylation 100%
• Hydrophobicity 20%
• Lysine Methylation 20%
• Mass Spectrometry Analysis 10%
• Site-directed mutagenesis 10%
• Glutamine 10%
• Methylation 10%
• Ligand-binding Domain 10%
• Phenylalanine 10%
• Nuclear Receptor 10%
• Mammalian Cells 10%
• Mutagenesis Studies 10%
• Hypermethylated 10%
• Insect Cells 10%
• Molecular Interactions 10%
• Protein Phosphorylation 10%
• Biological Consequences 10%
• CREB-binding Protein 10%
• Ligand-independent Activation 10%
• Hypomethylating Agents 10%
• Lysine Residue 10%
• Retinoid X Receptor 10%
• Methylated Lysine 10%
• Hydrophobic Amino Acids 10%
• Nuclear Receptor Superfamily 10%
• Non-histone Proteins 10%
• Receptor-interacting Protein 140 10%
• Modification Site 10%

Biochemistry, Genetics and Molecular Biology

• Retinoic Acid Receptor 100%
• Lysine 100%
• Methylation 30%
• Hydrophobicity 20%
• Nuclear Receptor 20%
• Amino Acids 10%
• Site-Directed Mutagenesis 10%
• Glutamine 10%
• Ligand Binding Domain 10%
• Molecular Interaction 10%
• Protein Phosphorylation 10%
• Retinoid X Receptor 10%
• Non-Histone Protein 10%
• CREB-binding Protein 10%
• Nuclear Receptor Co-Repressor 1 10%
• Alanine 10%
• Phenylalanine 10%