PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation
about
Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology with microbial arginine deiminasesTob2, a novel anti-proliferative Tob/BTG1 family member, associates with a component of the CCR4 transcriptional regulatory complex capable of binding cyclin-dependent kinasesHeterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificityIdentification and characterization of novel spliced variants of PRMT2 in breast carcinomaIdentification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alphaPRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylationDiscovery of peptidylarginine deiminase-4 substrates by protein array: antagonistic citrullination and methylation of human ribosomal protein S2Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)Friend of Prmt1, a novel chromatin target of protein arginine methyltransferasesPromiscuous modification of the nuclear poly(A)-binding protein by multiple protein-arginine methyltransferases does not affect the aggregation behaviorKinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificityProtein methyltransferase 2 inhibits NF-kappaB function and promotes apoptosisThe arginine-1493 residue in QRRGRTGR1493G motif IV of the hepatitis C virus NS3 helicase domain is essential for NS3 protein methylation by the protein arginine methyltransferase 1.Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP functionMethylation of Tat by PRMT6 regulates human immunodeficiency virus type 1 gene expressionPRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunitsHuman SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genesCrystal structure of the conserved core of protein arginine methyltransferase PRMT3PRMT6 diminishes HIV-1 Rev binding to and export of viral RNAEffects of ADMA upon gene expression: an insight into the pathophysiological significance of raised plasma ADMA.Arginine methyltransferases as novel therapeutic targets for breast cancerStructure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptidesInsights into histone code syntax from structural and biochemical studies of CARM1 methyltransferaseCrystal Structure of the Plant Epigenetic Protein Arginine Methyltransferase 10Structural insight into arginine methylation by the mouse protein arginine methyltransferase 7: a zinc finger freezes the mimic of the dimeric state into a single active siteYeast ribosomal protein L12 is a substrate of protein-arginine methyltransferase 2.The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity.Yeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro formation of omega-N(G)-monomethylarginine in calf thymus histone H2A.Hsl7 is a substrate-specific type II protein arginine methyltransferase in yeast.Novel RING finger proteins, Air1p and Air2p, interact with Hmt1p and inhibit the arginine methylation of Npl3p.Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domainsPrmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase familyDeterminants of the interaction of the spinal muscular atrophy disease protein SMN with the dimethylarginine-modified box H/ACA small nucleolar ribonucleoprotein GAR1Antiproliferative proteins of the BTG/Tob family are degraded by the ubiquitin-proteasome systemNerve growth factor-mediated increases in protein methylation occur predominantly at type I arginine methylation sites and involve protein arginine methyltransferase 1DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivoProtein arginine methyltransferase I: substrate specificity and role in hnRNP assembly
P2860
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P2860
PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation
description
1998 nî lūn-bûn
@nan
1998 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
PRMT 3, a type I protein argin ...... te specificity, and regulation
@ast
PRMT 3, a type I protein argin ...... te specificity, and regulation
@en
PRMT 3, a type I protein argin ...... te specificity, and regulation
@en-gb
PRMT 3, a type I protein argin ...... te specificity, and regulation
@nl
type
label
PRMT 3, a type I protein argin ...... te specificity, and regulation
@ast
PRMT 3, a type I protein argin ...... te specificity, and regulation
@en
PRMT 3, a type I protein argin ...... te specificity, and regulation
@en-gb
PRMT 3, a type I protein argin ...... te specificity, and regulation
@nl
prefLabel
PRMT 3, a type I protein argin ...... te specificity, and regulation
@ast
PRMT 3, a type I protein argin ...... te specificity, and regulation
@en
PRMT 3, a type I protein argin ...... te specificity, and regulation
@en-gb
PRMT 3, a type I protein argin ...... te specificity, and regulation
@nl
P2093
P356
P1476
PRMT 3, a type I protein argin ...... te specificity, and regulation
@en
P2093
P304
P356
10.1074/JBC.273.27.16935
P407
P577
1998-07-03T00:00:00Z