A Selenylation‐Isocyanation‐Amine Addition Strategy Targeting Prenylated Derivatives to Disrupt Oncogenic Rat Sarcoma Level

In recent years, significant strides have been made in protein prenylation research, a critical post‐translational modification essential for modulating cellular signaling. Central to this advancement is the selenylation‐isocyanation‐amine Addition strategy, which employs amine‐functionalized fluorescent or biotin‐tagged probes to selectively label or isolate prenylated molecules. Herein, Rat Sarcoma (RAS) protein regulation in HCT116 cell lines through the development of a novel prenylation labeling method is investigated. This approach provides insights into the functional dynamics of prenylated proteins and enables targeted manipulation of these molecules. While this work primarily establishes a methodological advance, it lays the foundation for future studies to elucidate RAS‐related oncogenic signaling pathways and explore therapeutic strategies targeting prenylation‐dependent processes.