Naturally occurring cancer-associated mutations disrupt oligomerization and activity of protein arginine methyltransferase 1 (PRMT1)

Medicine & Life Sciences

• Protein-Arginine N-Methyltransferases 100%
• Dimerization 42%
• Mutation 36%
• Arginine 25%
• link protein 25%
• Methylation 25%
• Neoplasms 21%
• Methyltransferases 20%
• Protein Isoforms 15%
• Native Polyacrylamide Gel Electrophoresis 13%
• S-Adenosylmethionine 12%
• Catalogs 11%
• Ultracentrifugation 11%
• Molecular Dynamics Simulation 10%
• Site-Directed Mutagenesis 9%
• Methionine 9%
• Post Translational Protein Processing 9%
• DNA Repair 8%
• Proteins 6%
• Cell Proliferation 6%
• Apoptosis 5%
• Databases 5%
• Enzymes 5%

Chemical Compounds

• Arginine 65%
• Protein 26%
• Dimerization 23%
• L-Methionine 9%
• Monomer 7%
• Site-Directed Mutagenesis 6%
• Mammalian Cell 6%
• Oligomer 5%