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• W2978093497 abstract "One of the regulatory mechanisms of epigenetic gene expression is the post-translational methylation of arginine residues, which is catalyzed by protein arginine methyltransferases (PRMTs). Abnormal expression of PRMT4/CARM1, one of the PRMTs, is associated with various diseases, including cancers. Here, we designed and synthesized a Förster resonance energy transfer (FRET)-based probe, FRC, which contains coumarin and fluorescein fluorophores at the N-terminus and C-terminus of a peptide containing an arginine residue within an appropriate amino acid sequence to serve as a substrate of CARM1; the two fluorophores act as a FRET donor and a FRET acceptor, respectively. Since trypsin specifically hydrolyzes the arginine residue, but not a monomethylarginine or dimethylarginine residue, CARM1 activity can be evaluated from the change of the coumarin/fluorescein fluorescence ratio of FRC in the presence of trypsin." @default.
• W2978093497 created "2019-10-10" @default.
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• W2978093497 date "2019-11-01" @default.
• W2978093497 modified "2023-10-16" @default.
• W2978093497 title "Ratiometric assay of CARM1 activity using a FRET-based fluorescent probe" @default.
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• W2978093497 doi "https://doi.org/10.1016/j.bmcl.2019.126728" @default.
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