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• W4309408849 startingPage "216008" @default.
• W4309408849 abstract "Post-translational modification (PTM) of proteins increases proteome diversity, which is critical for maintaining cellular homeostasis. The importance of protein methylation in the regulation of diverse biological processes has been highlighted in the past decades. Methylation of the arginine residue on proteins is catalyzed by members of the protein arginine methyltransferase (PRMT) family. PRMTs play indispensable roles in various pathways that regulate cancer development, progression, and drug response. In this review, we discuss the role of PRMT3, a member of the PRMT family, in controlling oncogenic processes. Additionally, the effects of PRMT3 on the methylation of regulatory proteins involved in transcription, post-transcriptional control, ribosomal maturation, translation, biological synthesis, and metabolic signaling are summarized. Moreover, recent progresses in the development of PRMT3 inhibitors are introduced. Overall, this review highlights the importance of PRMT3 in tumorigenesis and discusses the underlying mechanisms by which PRMT3 modulates cellular metabolism and gene expression. These results also provide a molecular basis for therapeutic modalities by targeting PRMT3." @default.
• W4309408849 created "2022-11-27" @default.
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• W4309408849 date "2023-02-01" @default.
• W4309408849 modified "2023-10-01" @default.
• W4309408849 title "Protein arginine methyltransferase 3: A crucial regulator in metabolic reprogramming and gene expression in cancers" @default.
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• W4309408849 doi "https://doi.org/10.1016/j.canlet.2022.216008" @default.
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