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Type I protein arginine N-methyltransferases (PRMTs), such as PRMT3, catalyze the formation of asymmetric N(G),N(G)-dimethylarginine (ADMA) residues in proteins (Tang et al., 1998 [PubMed 9642256]).[supplied by OMIM, Mar 2008]..
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Arabidopsis PRMT3 (AtPRMT3) is required for ribosome biogenesis by affecting pre-rRNA processing.
PRMT3 translocation by palmitic acid is coupled to the binding of LXRalpha (show NR1H3 Proteins), which is responsible for the onset of fatty liver.
This work profilies substrates of protein arginine N-methyltransferase 3 with S-adenosyl-L-methionine analogues.
Mutational defects in PRMT3 is not the cause of frontotemporal lobar degeneration.
results show that protein arginine methyl transferase (PRMT)-3 and -5 methylate NaV1.5 (show SCN5A Proteins) in vitro, interact with NaV1.5 (show SCN5A Proteins) in human embryonic kidney (HEK (show EPHA3 Proteins)) cells, and increase NaV1.5 (show SCN5A Proteins) current density
The crystal structure of PRMT3 in complex with an inhibitor as well as kinetic analysis reveals an allosteric site of inhibition.
release of VHL30 from the E3 ligase complex, promotes the binding of VHL30 to a protein arginine methyltransferase (show PRMT1 Proteins), PRMT3
The Tyr87Cys and Tyr87Glu-PRMT3 variants had markedly decreased affinity to ribosomal protein S2 (show RPS2 Proteins) and, consequently, reduced enzymatic activity compared to the wild-type enzyme.
PRMT3 is a ribosomal protein methyltransferase that affects the cellular level of ribosomal subunits.
DAL-1/4.1B (show EPB41L3 Proteins) protein significantly inhibits PRMT3 methylation of cellular substrates, which may affect mechanism through which DAL-1/4.1B (show EPB41L3 Proteins) affects tumor cell growth.
Type I Arginine Methyltransferases PRMT1 (show PRMT1 Proteins) and PRMT-3 Act Distributively
The zinc-finger domain of mouse PRMT3 is necessary & sufficient for binding to human rpS2 (show RPS2 Proteins). rpS2 (show RPS2 Proteins) is methylated by PRMT3, implicating PRMT3 in ribosomal function & in the regulation of protein synthesis.
The present ontogenetic analysis of PRMT1 (show PRMT1 Proteins) and PRMT3 using Western blot methodology clearly revealed that PRMT3 develops during the perinatal stage and its expression is maintained even in adulthood.
mouse embryos with a targeted disruption of PRMT3 are small in size but survive after birth and attain a normal size in adulthood, thus displaying Minute-like characteristics
Type I protein arginine N-methyltransferases (PRMTs), such as PRMT3, catalyze the formation of asymmetric N(G),N(G)-dimethylarginine (ADMA) residues in proteins (Tang et al., 1998
HMT1 hnRNP methyltransferase-like 3
, heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3
, protein arginine N-methyltransferase 3
, heterogeneous nuclear ribonucleoprotein methyltransferase-like 3
, protein arginine N-methyltransferase 3(hnRNP methyltransferase S. cerevisiae)-like 3
, protein arginine methyltransferase 3