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PRMT1 encodes a member of the protein arginine N-methyltransferase (PRMT) family.
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The oncogenic roles of PRMT1 in the progression of ESCC.
we unraveled a dual function of PRMT1 in modulation of both EMT and senescence via regulating ZEB1.
Protein arginine methyltransferase 1 is regulated by the Interleukin-4 (show IL4 Proteins)/STAT6 (show STAT6 Proteins) signal pathway in epithelial cells, while in fibroblasts PRMT1 is activated by Interleukin-1 beta (show IL1B Proteins) through NF-kappa B (show NFKB1 Proteins).
Upon HBV infection, cellular mechanisms involving SETDB1 (show SETDB1 Proteins)-mediated H3K9me3 and HP1 (show DEFA1 Proteins) induce silencing of HBV cccDNA transcription through modulation of chromatin structure.
This study demonstrated that Loss of PRMT1 not only results in an increase of UMA FUS (show FUS Proteins) and a decrease of ADMA FUS (show FUS Proteins), but also in a significant increase of MMA (show MMD Proteins) FUS (show FUS Proteins).
findings suggest that PRMT1 is a central regulator of tissue remodeling and that the signaling sequence controlling its expression in primary human lung fibroblast is PDGF (show PDGFA Proteins)-ERK (show EPHB2 Proteins)-STAT1 (show STAT1 Proteins).
The authors demonstrate that RBM15 is methylated by protein arginine methyltransferase 1 (PRMT1) at residue R578, leading to its degradation via ubiquitylation by an E3 ligase (CNOT4 (show CNOT4 Proteins)).
Data unveils a novel mechanism of PRMT1-mediated CPC regulation through methylation of INCENP (show INCENP Proteins).
there is an imbalance in the vasoconstriction-vasodilation status toward constriction. It is our hypothesis that, in hypoxic stress, a key player in initiating this imbalance is the enzyme, protein arginine methyltransferase-1 (PRMT1).
Pharmacological inhibition of KDM4C (show KDM4C Proteins)/PRMT1 suppresses transcription and transformation ability of MLL (show MLL Proteins) fusions
A time-dependent decrease in serum and tissue ADMA and increase in mRNA expression of DDAH-1 and PRMT-1 as well as higher rates of mRNA expression of CAT-1 and lower rates of CAT-2A and CAT-2B were found after 8-week MCD diet.
PRMT1 is required for CNS development, especially for oligodendrocyte maturation processes
PRMT1 knockdown reduced H4R3me2a expression to alter potential H3K9/K14 (show KRT14 Proteins) acetylation by acetyltransferases, and to eventually result in diminished acH3K9/K14 (show KRT14 Proteins) modification in nucleus accumbens. PRMT1 is the main enzyme responsible for this modification.
Study provides evidence for loss of PRMT1 function as a consequence of cytoplasmic accumulation of FUS (show FUS Proteins) in the pathogenesis of amyotrophic lateral sclerosis, including changes in the histone code regulating gene transcription.
In vivo, levels of lipogenic proteins, inflammatory molecules, PGC-1alpha, and PRMT1 were increased in the livers of HFD mice compared with those fed a chow diet, and were ameliorated in HFD Txnip (show TXNIP Proteins)(-/-) mice.
GSK3- and PRMT-1-dependent modifications of desmoplakin control desmoplakin-cytoskeleton dynamics.
PRMT1 concentrates in cytoplasmic bodies, which respond to DNA injury in the cell nucleus
PRMT1-mediated arginine methylation could be implicated in the nucleus-cytoplasmic shuttling of FUS/TLS (show FUS Proteins).
PRMT1-dependent regulation of FoxO1 (show FOXO1 Proteins) is critical in hepatic glucose metabolism in vivo.
This gene encodes a member of the protein arginine N-methyltransferase (PRMT) family. Post-translational modification of target proteins by PRMTs plays an important regulatory role in many biological processes, whereby PRMTs methylate arginine residues by transferring methyl groups from S-adenosyl-L-methionine to terminal guanidino nitrogen atoms. The encoded protein is a type I PRMT and is responsible for the majority of cellular arginine methylation activity. Increased expression of this gene may play a role in many types of cancer. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, and a pseudogene of this gene is located on the long arm of chromosome 5.
HMT1 (hnRNP methyltransferase, S. cerevisiae)-like 2
, heterogeneous nuclear ribonucleoprotein methyltransferase 1-like 2
, histone-arginine N-methyltransferase PRMT1
, interferon receptor 1-bound protein 4
, protein arginine N-methyltransferase 1
, arginine N-methyltransferase 1
, heterogeneous nuclear ribonucleoproteins methyltransferase-like 2