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Findings uncover the existence of an extra-ribosomal complex consisting of PDCD2L (zeige PDCD2L Proteine), RPS2 (zeige RPS2 Proteine), and PRMT3 and support a role for PDCD2L (zeige PDCD2L Proteine) in the late maturation of 40S ribosomal subunits.
PRMT3 translocation by palmitic acid is coupled to the binding of LXRalpha (zeige NR1H3 Proteine), 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 (zeige SCN5A Proteine) in vitro, interact with NaV1.5 (zeige SCN5A Proteine) in human embryonic kidney (HEK (zeige EPHA3 Proteine)) cells, and increase NaV1.5 (zeige SCN5A Proteine) 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 (zeige PRMT1 Proteine), PRMT3
The Tyr87Cys and Tyr87Glu-PRMT3 variants had markedly decreased affinity to ribosomal protein S2 (zeige RPS2 Proteine) 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 (zeige EPB41L3 Proteine) protein significantly inhibits PRMT3 methylation of cellular substrates, which may affect mechanism through which DAL-1/4.1B (zeige EPB41L3 Proteine) affects tumor cell growth.
The zinc-finger domain of mouse PRMT3 is necessary & sufficient for binding to human rpS2 (zeige RPS2 Proteine). rpS2 (zeige RPS2 Proteine) is methylated by PRMT3, implicating PRMT3 in ribosomal function & in the regulation of protein synthesis.
The present ontogenetic analysis of PRMT1 (zeige PRMT1 Proteine) 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