Structural and biochemical evaluation of bisubstrate inhibitors of protein arginine N-methyltransferases PRMT1 and CARM1 (PRMT4)

Pharmacology, Toxicology and Pharmaceutical Science

• Arginine 100%
• Guanidine 100%
• Methyltransferase 100%
• Mutagenesis 50%
• Amino Acid 50%
• Cardiovascular Disease 50%
• Glutamic Acid 50%
• Binding Site 50%
• Calorimetry 50%
• S-Adenosyl Methionine 50%
• Drug Discovery 50%
• Cardiovascular System Cancer 50%
• Diseases 50%
• Protein Arginine Methyltransferase 50%
• 2 Aminopyridine 50%

Keyphrases

• Structural Assessment 100%
• PRMT1 100%
• Biochemical Assessment 100%
• Bisubstrate Inhibitor 100%
• PRMT4 100%
• Guanidine 14%
• Cardiovascular Disease 7%
• Binding Site 7%
• Protein Function 7%
• Ligand Binding 7%
• Active Sites 7%
• Amino Acids 7%
• Amines 7%
• S-adenosylmethionine 7%
• Isothermal Titration Calorimetry 7%
• Activity Assay 7%
• Mutagenesis 7%
• Glutamate 7%
• Arginine 7%
• Structural Information 7%
• Electron Density 7%
• Binding Mode 7%
• Side-chain Conformation 7%
• Drug Discovery 7%
• Preferential Binding 7%
• Target Binding 7%
• 2-aminopyridine 7%
• Isosteric 7%

Biochemistry, Genetics and Molecular Biology

• Methyltransferase 100%
• Arginine 100%
• CARM1 100%
• PRMT1 100%
• Conformation 42%
• Enzyme 14%
• Binding Site 14%
• Amino Acids 14%
• Ligand Binding 14%
• Active Site 14%
• Crystal Structure 14%
• Isothermal Titration Calorimetry 14%
• Mutagenesis 14%
• Glutamic Acid 14%
• S-Adenosyl Methionine 14%