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Protein arginine methyltransferase 3

PRMT3, PRMT8, RMT3, protein arginine N-methyltransferase 3, protein arginine methyltransferase 3
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] (from NCBI)
Top mentioned proteins: Protein-Arginine N-Methyltransferase, ACID, CARM1, PRMT5, CAN
Papers on PRMT3
Protein Arginine Methyltransferase 8: Tetrameric Structure and Protein Substrate Specificity.
Ho et al., Taipei, Taiwan. In Biochemistry, Jan 2016
PRMT8 is one of the least characterized type I PRMTs, and its crystal structure has not been reported.
PRMT8 as a phospholipase regulates Purkinje cell dendritic arborization and motor coordination.
Fukamizu et al., Tsukuba, Japan. In Sci Adv, Dec 2015
We show that protein arginine methyltransferase 8 (PRMT8) acts as a phospholipase that directly hydrolyzes PC, generating choline and phosphatidic acid.
Arginine methyltransferases mediate an epigenetic ovarian response to endometriosis.
De La Fuente et al., Grand Rapids, United States. In Reproduction, Oct 2015
Ingenuity Pathway Analysis indicated that transcripts for chromatin-remodeling enzymes associated with reproductive system disease and cancer development were abnormally regulated, most prominently the arginine methyltransferases CARM1, PRMT2, and PRMT8.
New role of irisin in hepatocytes: The protective effect of hepatic steatosis in vitro.
Park et al., Kwangju, South Korea. In Cell Signal, Sep 2015
The preventive effects of irisin against lipogenesis and oxidative stress were mediated by the inhibition of protein arginine methyltransferase-3 (PRMT3).
A potent, selective and cell-active allosteric inhibitor of protein arginine methyltransferase 3 (PRMT3).
Vedadi et al., New York City, United States. In Angew Chem Int Ed Engl, May 2015
PRMT3 catalyzes the asymmetric dimethylation of arginine residues of various proteins.
Arginine increases development of in vitro-produced porcine embryos and affects the protein arginine methyltransferase?dimethylarginine dimethylaminohydrolase?nitric oxide axis.
Prather et al., In Reprod Fertil Dev, Apr 2015
Expression of the protein arginine methyltransferase (PRMT) genes PRMT1, PRMT3 and PRMT5 throughout development was not affected by arginine.
PRMT1 and PRMT8 regulate retinoic acid-dependent neuronal differentiation with implications to neuropathology.
Nagy et al., Debrecen, Hungary. In Stem Cells, Mar 2015
PRMT8 is a retinoid receptor target gene itself and acts as a cell type specific transcriptional coactivator of retinoid signaling at later stages of differentiation.
A novel BLAST-Based Relative Distance (BBRD) method can effectively group members of protein arginine methyltransferases and suggest their evolutionary relationship.
Li et al., T'ai-chung-shih, Taiwan. In Mol Phylogenet Evol, Mar 2015
The tree placed the uncharacterized PRMT9 with PRMT7 in the same clade, outside of all the Type I PRMTs including PRMT1 and its vertebrate paralogue PRMT8, PRMT3, PRMT6, PRMT2 and PRMT4.
Exploration of cyanine compounds as selective inhibitors of protein arginine methyltransferases: synthesis and biological evaluation.
Zheng et al., Athens, United States. In J Med Chem, Mar 2015
A pentamethine compound, E-84 (compound 50), showed inhibition on PRMT1 at the micromolar level and 6- to 25-fold selectivity over CARM1, PRMT5, and PRMT8.
PRMT3 regulates hepatic lipogenesis through direct interaction with LXRα.
Park et al., Kwangju, South Korea. In Diabetes, 2015
In this study, palmitic acid (PA) treatment increased PRMT3, which is correlated with the elevation of hepatic lipogenic proteins.
Arabidopsis protein arginine methyltransferase 3 is required for ribosome biogenesis by affecting precursor ribosomal RNA processing.
Cao et al., Beijing, China. In Proc Natl Acad Sci U S A, 2014
Here we show that Arabidopsis PRMT3 (AtPRMT3) is required for ribosome biogenesis by affecting pre-rRNA processing.
PRMT3: new binding molecule to RhoGDI-α during mycophenolic acid-induced β-cell death.
Kim et al., Seoul, South Korea. In Transplant Proc, 2014
Eighty-three real positives were obtained by Y2H analysis, and of these, arginine N-methyltransferase 3 (PRMT3) protein interacted with RhoGDI-α in INS-1E cells.
Lineage-specific regulation of epigenetic modifier genes in human liver and brain.
Leist et al., Konstanz, Germany. In Plos One, 2013
Neuro-specific EMGs were the histone deacetylases HDAC5 and HDAC7, and the arginine-methyltransferase PRMT8.
Evolutionarily conserved protein arginine methyltransferases in non-mammalian animal systems.
Li et al., T'ai-chung-shih, Taiwan. In Febs J, 2012
We show the conservation of the most typical type I PRMT1 and type II PRMT5 in all of the species examined, the wide yet different distribution of PRMT3, 4 and 7 in non-mammalian animals, the vertebrate-restricted distribution of PRMT8 and the special reptile/avian-deficient distribution of PRMT2 and 6.
Proteomic dissection of the von Hippel-Lindau (VHL) interactome.
Shiio et al., San Antonio, United States. In J Proteome Res, 2011
release of VHL30 from the E3 ligase complex, promotes the binding of VHL30 to a protein arginine methyltransferase, PRMT3
Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3).
Cmejla et al., Praha, Czech Republic. In Biochim Biophys Acta, 2011
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 essential for dendritic spine maturation in rat hippocampal neurons.
Tohyama et al., Suita, Japan. In Brain Res, 2010
PRMT3 possibly plays a pivotal role in neuronal translation by contributing to activity-dependent changes in the dendritic spines.
The distribution and characterization of endogenous protein arginine N-methyltransferase 8 in mouse CNS.
Tohyama et al., Suita, Japan. In Neuroscience, 2009
PRMT8 is a neuron-specific nuclear enzyme broadly distributed in the CNS neurons and the N-terminus does not contain the glycine end for myristoylation target
Loci influencing lipid levels and coronary heart disease risk in 16 European population cohorts.
ENGAGE Consortium et al., Rotterdam, Netherlands. In Nat Genet, 2009
The six newly identified loci in our cohort samples are ABCG5 (TC, P = 1.5 x 10(-11); LDL, P = 2.6 x 10(-10)), TMEM57 (TC, P = 5.4 x 10(-10)), CTCF-PRMT8 region (HDL, P = 8.3 x 10(-16)), DNAH11 (LDL, P = 6.1 x 10(-9)), FADS3-FADS2 (TC, P = 1.5 x 10(-10); LDL, P = 4.4 x 10(-13)) and MADD-FOLH1 region (HDL, P = 6 x 10(-11)).
Hsp70 chaperones and type I PRMTs are sequestered at intranuclear inclusions caused by polyalanine expansions in PABPN1.
Enguita et al., Lisbon, Portugal. In Plos One, 2008
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
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