PRMT5 (Janus Kinase-binding Protein 1) Catalyzes the Formation of Symmetric Dimethylarginine Residues in Proteins
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference33 articles.
1. Analysis of the Yeast Arginine Methyltransferase Hmt1p/Rmt1p and Its in Vivo Function
2. Regulation of Transcription by a Protein Methyltransferase
3. Involvement of Receptor-Bound Protein Methyltransferase PRMT1 in Antiviral and Antiproliferative Effects of Type I Interferons
4. Protein-arginine Methyltransferase I, the Predominant Protein-arginine Methyltransferase in Cells, Interacts with and Is Regulated by Interleukin Enhancer-binding Factor 3
5. Arginine Methylation Inhibits the Binding of Proline-rich Ligands to Src Homology 3, but Not WW, Domains
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1. Role of PRMT1 and PRMT5 in Breast Cancer;International Journal of Molecular Sciences;2024-08-14
2. SART3 reads methylarginine-marked glycine- and arginine-rich motifs;Cell Reports;2024-07
3. ETD-Based Proteomic Profiling Improves Arginine Methylation Identification and Reveals Novel PRMT5 Substrates;Journal of Proteome Research;2024-01-25
4. Asymmetric and symmetric protein arginine methylation in methionine-addicted human cancer cells;PLOS ONE;2023-12-22
5. A unique binding pocket induced by a noncanonical SAH mimic to develop potent and selective PRMT inhibitors;Acta Pharmaceutica Sinica B;2023-12
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