Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family
about
The 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 carcinomaProtein arginine methyltransferase 5 functions in opposite ways in the cytoplasm and nucleus of prostate cancer cellssrGAP2 arginine methylation regulates cell migration and cell spreading through promoting dimerizationArginine methylation controls growth regulation by E2F-1PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylargininePRMT5 regulates Golgi apparatus structure through methylation of the golgin GM130Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteinsThe 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.Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein.The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteinsChemogenetic analysis of human protein methyltransferasesStructural insights into protein arginine symmetric dimethylation by PRMT5Structure of the Arginine Methyltransferase PRMT5-MEP50 Reveals a Mechanism for Substrate SpecificityStructural 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 PRMT5 arginine methyltransferase: many roles in development, cancer and beyondArginine methylation regulates the p53 responseA novel WD repeat protein component of the methylosome binds Sm proteinsIdentification of proteins interacting with the RNAPII FCP1 phosphatase: FCP1 forms a complex with arginine methyltransferase PRMT5 and it is a substrate for PRMT5-mediated methylationEffects of a novel arginine methyltransferase inhibitor on T-helper cell cytokine productionStructural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors.Characterization of PRMT1 from Plasmodium falciparumProtein arginine methyltransferase Prmt5-Mep50 methylates histones H2A and H4 and the histone chaperone nucleoplasmin in Xenopus laevis eggsModulation of Epstein-Barr virus nuclear antigen 2-dependent transcription by protein arginine methyltransferase 5.TbPRMT6 is a type I protein arginine methyltransferase that contributes to cytokinesis in Trypanosoma bruceiComparison of epigenetic mediator expression and function in mouse and human embryonic blastomeresInhibition of cardiomyocyte hypertrophy by protein arginine methyltransferase 5In vivo analysis of nucleolar proteins modified by the yeast arginine methyltransferase Hmt1/Rmt1p.The exon junction complex component Y14 modulates the activity of the methylosome in biogenesis of spliceosomal small nuclear ribonucleoproteinsArginine methylation regulates mitochondrial gene expression in Trypanosoma brucei through multiple effector proteins.Protein arginine methyltransferase 5 accelerates tumor growth by arginine methylation of the tumor suppressor programmed cell death 4.Left ventricular diastolic dysfunction and plasma asymmetric dimethylarginine concentration in persons with essential hypertensionHuman protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ω-NG-monomethylated arginine residues.Structural and sequence motifs of protein (histone) methylation enzymes.Alternative splicing regulates Prdm1/Blimp-1 DNA binding activities and corepressor interactionsHistone arginine methylation is required for vernalization-induced epigenetic silencing of FLC in winter-annual Arabidopsis thaliana.Pinellia pedatisecta agglutinin interacts with the methylosome and induces cancer cell death.Automethylation of protein arginine methyltransferase 8 (PRMT8) regulates activity by impeding S-adenosylmethionine sensitivityA remodeled protein arginine methyltransferase 1 (PRMT1) generates symmetric dimethylarginine.
P2860
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P2860
Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family
description
2001 nî lūn-bûn
@nan
2001 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Prmt5, which forms distinct ho ...... inine methyltransferase family
@ast
Prmt5, which forms distinct ho ...... inine methyltransferase family
@en
Prmt5, which forms distinct ho ...... inine methyltransferase family
@nl
type
label
Prmt5, which forms distinct ho ...... inine methyltransferase family
@ast
Prmt5, which forms distinct ho ...... inine methyltransferase family
@en
Prmt5, which forms distinct ho ...... inine methyltransferase family
@nl
prefLabel
Prmt5, which forms distinct ho ...... inine methyltransferase family
@ast
Prmt5, which forms distinct ho ...... inine methyltransferase family
@en
Prmt5, which forms distinct ho ...... inine methyltransferase family
@nl
P2093
P2860
P356
P1476
Prmt5, which forms distinct ho ...... inine methyltransferase family
@en
P2093
P2860
P304
P356
10.1074/JBC.M008660200
P407
P577
2001-04-06T00:00:00Z