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The protein arginine methyl transferase 5 (PRMT5) emerges as a therapeutic target in S-methyl-5'-thioadenosine phosphorylase (MTAP)-deleted cancers, where MTA accumulation partially inhibits its activity. However, It remains unclear whether other genetic alterations can dictate PRMT5 activity in can...
2026-04-30 | MTBLS14411 | MetaboLights
Histone arginine methylation by Prmt controls lung branching morphogenesis through transcriptional repression of Bmp
Arginine/R methylation (R-met) of proteins is a widespread post-translational modification (PTM), deposited by a family of protein arginine/R methyl transferase enzymes (PRMT). Regulations by R-met are involved in key biological processes deeply studied in metazoan. Among those, post-transcriptional...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2024-01-18 | PXD043460 | Pride
Protein arginine methylation, catalyzed by the protein arginine methyltransferase (PRMT) family, is recognized as a widespread post-translational modification (PTM) with implications in a plethora of biological processes in eukaryotes. PRMT proteins were classified into three types, type I, II and I...
ORGANISM(S): Homo sapiens (Human) 
2021-01-27 | PXD022424 | Pride
We report that a protein arginine methyltransferase Prmt and symmetric dimethylation at histone H arginine (HRsme) directly associates with chromatin of Bmp to suppress its transcription. Inactivation of Prmt in the lung epithelium results in halted branching morphogenesis, altered P-D airway patter...
ORGANISM(S): Mus musculus 
2019-01-30 | GSE108934 | GEO
A systematic survey of PRMT interactomes reveals key roles of arginine methylation in the global control of RNA splicing and translation [RNA-seq]
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