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Protein arginine N-methyltransferases, such as CARM1, catalyze the transfer of a methyl group from S-adenosyl-L-methionine to the side chain nitrogens of arginine residues within proteins to form methylated arginine derivatives and S-adenosyl-L-homocysteine. Additionally we are shipping CARM1 Antibodies (188) and CARM1 Kits (3) and many more products for this protein.
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Here, the crystal structures of human CARM1 with the S-adenosylmethione (SAM (show TTN Proteins)) mimic sinefungin and three different peptide sequences from histone H3 (show HIST3H3 Proteins) and PABP1 (show PABPC1 Proteins) are presented, with both nonmethylated and singly methylated arginine residues exemplified.
CARM1 associates with major nonsense-mediated mRNA decay factor UPF1 (show UPF1 Proteins) and promotes its occupancy on premature terminating codon-containing transcripts in spinal muscular atrophy.
Monitoring of the CARM1-dependent production of monomethylated and dimethylated peptides over time by self-assembled monolayer and matrix-assisted laser desorption ionization mass spectrometry revealed that methylation by CARM1 is distributive.
no obvious association of CARM1 isoform expression and clinical correlates in breast cancer
disruption of CARM1 enhances the nuclear retention of mRNAs containing IRAlus
Data indicate that coactivator-associated arginine methyltransferase 1 (CARM1) regulates neural differentiation through Nanog homeobox (show NANOG Proteins) protein and microRNA miR92a.
Like insulin (show INS Proteins), CARM1 overexpression increased CDK2 (show CDK2 Proteins) and CDK4 (show CDK4 Proteins) expression. In addition, CARM1 knockdown reduced the number of insulin (show INS Proteins)-induced G2/M phase cells
a noncoding variant in the CARM1-promoter functions as a regulator of gene transcription and homocysteine levels
O-GlcNAcylation of CARM1 at its C-terminus is an important determinant for CARM1 substrate specificity.
PRMT4 has a role in arginine methylation, which negatively regulates retinoblastoma tumor suppressor protein (show TP53 Proteins) and promotes E2F-1 (show E2F1 Proteins) dissociation
Study identifies CARM1, which methylates histone H3 (show HIST3H3 Proteins) at arginine 26 (H3R26), as an upstream regulator of Sox21 (show SOX21 Proteins) expression. These results indicate that heterogeneity in gene expression patterns biases cell fate in the mouse embryo as early as the 4-cell stage.
findings demonstrate that CARM1-dependent histone arginine methylation is a crucial nuclear event in autophagy, and identify a new signalling axis of AMPK (show PRKAA1 Proteins)-SKP2-CARM1 in the regulation of autophagy induction after nutrient starvation
CARM1 haploinsufficiency impairs transdifferentiation and wound healing in a mouse model.
PRMT4 might be a key regulator of high-glucose-induced insulin (show INS Proteins) secretion from pancreatic beta cells via H3R17 methylation.
Data show that the methyltransferase CARM1 (coactivator-associated arginine methyltransferase 1; PRMT4) methylated Notch (show NOTCH1 Proteins) intracellular domain (NICD (show NOTCH1 Proteins)) at five conserved arginine residues.
we identify BAF155 (show SMARCC1 Proteins) as a substrate for arginine methyltransferase CARM1.
Arginine methylation of Pax7 (show PAX7 Proteins) by Carm1 functions as a molecular switch controlling the epigenetic induction of Myf5 (show MYF5 Proteins) during satellite stem cell asymmetric division and entry into the myogenic program.
CARM1 is a key epigenetic regulator of hematopoiesis that affects multiple lineages at various stages of differentiation.
our study provides evidence for a role of CARM1-mediated arginine methylation in regulation of histone acetylation and transcription.
PRMT4 is necessary for selective control of a specific gene expression program associated with glycogen (show GYS1 Proteins) metabolism.
a combinatorial role of PRMT4/CARM1 and PRMT5 (show PRMT5 Proteins) for proper myogenesis in zebrafish
Protein arginine N-methyltransferases, such as CARM1, catalyze the transfer of a methyl group from S-adenosyl-L-methionine to the side chain nitrogens of arginine residues within proteins to form methylated arginine derivatives and S-adenosyl-L-homocysteine. Protein arginine methylation has been implicated in signal transduction, metabolism of nascent pre-RNA, and transcriptional activation (Frankel et al., 2002
histone-arginine methyltransferase CARM1
, protein arginine N-methyltransferase 4
, coactivator-associated arginine methyltransferase 1
, protein arginine methyltransferase