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ZNF277 and PRMT3 compete for uS5 binding, because overexpression of PRMT3 inhibited the formation of the ZNF277-uS5 complex, whereas depletion of cellular ZNF277 resulted in increased levels of uS5-PRMT3.
Findings uncover the existence of an extra-ribosomal complex consisting of PDCD2L, RPS2, and PRMT3 and support a role for PDCD2L in the late maturation of 40S ribosomal subunits.
PRMT3 translocation by palmitic acid is coupled to the binding of LXRalpha, 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 in vitro, interact with NaV1.5 in human embryonic kidney (HEK) cells, and increase NaV1.5 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, PRMT3
The Tyr87Cys and Tyr87Glu-PRMT3 variants had markedly decreased affinity to ribosomal protein S2 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 protein significantly inhibits PRMT3 methylation of cellular substrates, which may affect mechanism through which DAL-1/4.1B affects tumor cell growth.
Type I Arginine Methyltransferases PRMT1 and PRMT-3 Act Distributively
results suggest that the pathological mutation in the PABPN1 gene alters the protein conformation and induces a preferential interaction with type I PRMTs and Hsp70 chaperones
We have shown that PRMT3 acts as a specific co-activator for LXR-induced hepatic lipogenesis in vivo. Short-term combination treatment with the LXR agonist T0901317 and the PRMT3 inhibitor SGC707 is associated with a beneficial gene expression profile, that is, increased macrophage cholesterol efflux transcription with only limited hepatic lipogenesis gene induction.
The zinc-finger domain of mouse PRMT3 is necessary & sufficient for binding to human rpS2. rpS2 is methylated by PRMT3, implicating PRMT3 in ribosomal function & in the regulation of protein synthesis.
The present ontogenetic analysis of PRMT1 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
Arabidopsis PRMT3 (AtPRMT3) is required for ribosome biogenesis by affecting pre-rRNA processing.
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 methyltransferase 3
, protein arginine N-methyltransferase 3(hnRNP methyltransferase S. cerevisiae)-like 3