HIGHLIGHTS
- What: The authors demonstrated that PRMT5 stabilizes the RORα protein mainly through the symmetric dimethylation of its highly conserved DBD domain.
- Who: Gaofeng Xiong and collaborators from the Department of Pharmacology and Nutritional Sciences, University of Kentucky, Lexington, KY, USA have published the article: Regulation of ROR Stability through PRMT5-Dependent Symmetric Dimethylation, in the Journal: Cancers 2024, x of /2024/
- How: The results showed that PRMT5 directly bound to RORα and PRMT5 mainly symmetrically dimethylated the DNA-binding domain (DBD) but not the ligand-binding domain (LBD) of RORα. The results showed . . .
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