PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine
about
The testis-specific factor CTCFL cooperates with the protein methyltransferase PRMT7 in H19 imprinting control region methylationPRMT5 regulates Golgi apparatus structure through methylation of the golgin GM130Accurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometryToward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexesThe histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4Protein methyltransferase 2 inhibits NF-kappaB function and promotes apoptosisTwo distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteinsPRMT6 diminishes HIV-1 Rev binding to and export of viral RNAThe Role of Protein Arginine Methyltransferases in Inflammatory ResponsesStructural and functional coordination of DNA and histone methylationArginine methyltransferases as novel therapeutic targets for breast cancerCurrent chemical biology approaches to interrogate protein methyltransferasesStructural 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 siteHistone methylation modifiers in cellular signaling pathwaysProtein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase δ catalytic subunit gene, POLD1Protein arginine methylation in mammals: who, what, and whyAsymmetric arginine dimethylation of heterogeneous nuclear ribonucleoprotein K by protein-arginine methyltransferase 1 inhibits its interaction with c-Src.Binding of the heterogeneous ribonucleoprotein K (hnRNP K) to the Epstein-Barr virus nuclear antigen 2 (EBNA2) enhances viral LMP2A expressionApproaches to measuring the activities of protein arginine N-methyltransferasesHistone arginine methylations: their roles in chromatin dynamics and transcriptional regulation.Expression of PRMT5 correlates with malignant grade in gliomas and plays a pivotal role in tumor growth in vitro.A Mendelian locus on chromosome 16 determines susceptibility to doxorubicin nephropathy in the mouse.Menin epigenetically represses Hedgehog signaling in MEN1 tumor syndrome.TbPRMT6 is a type I protein arginine methyltransferase that contributes to cytokinesis in Trypanosoma bruceiArginine methylation in subunits of mammalian pre-mRNA cleavage factor I.Trans-tail regulation of MLL4-catalyzed H3K4 methylation by H4R3 symmetric dimethylation is mediated by a tandem PHD of MLL4Tudor domains bind symmetrical dimethylated arginines.Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): the importance of acidic residues in the double E loop.Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain.Protein-arginine methyltransferase 1 (PRMT1) methylates Ash2L, a shared component of mammalian histone H3K4 methyltransferase complexes.A comprehensive view of the epigenetic landscape. Part II: Histone post-translational modification, nucleosome level, and chromatin regulation by ncRNAs.A transient kinetic analysis of PRMT1 catalysisProtein arginine methylation in parasitic protozoa.Protein arginine methyltransferase 7 promotes breast cancer cell invasion through the induction of MMP9 expressionMethylation of eukaryotic elongation factor 2 induced by basic fibroblast growth factor via mitogen-activated protein kinaseHuman protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ω-NG-monomethylated arginine residues.Tudor staphylococcal nuclease (Tudor-SN) participates in small ribonucleoprotein (snRNP) assembly via interacting with symmetrically dimethylated Sm proteins.Protein interfaces in signaling regulated by arginine methylation.Structural and sequence motifs of protein (histone) methylation enzymes.
P2860
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P2860
PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine
description
2005 nî lūn-bûn
@nan
2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
PRMT7, a new protein arginine ...... zes symmetric dimethylarginine
@ast
PRMT7, a new protein arginine ...... zes symmetric dimethylarginine
@en
PRMT7, a new protein arginine ...... zes symmetric dimethylarginine
@en-gb
PRMT7, a new protein arginine ...... zes symmetric dimethylarginine
@nl
type
label
PRMT7, a new protein arginine ...... zes symmetric dimethylarginine
@ast
PRMT7, a new protein arginine ...... zes symmetric dimethylarginine
@en
PRMT7, a new protein arginine ...... zes symmetric dimethylarginine
@en-gb
PRMT7, a new protein arginine ...... zes symmetric dimethylarginine
@nl
prefLabel
PRMT7, a new protein arginine ...... zes symmetric dimethylarginine
@ast
PRMT7, a new protein arginine ...... zes symmetric dimethylarginine
@en
PRMT7, a new protein arginine ...... zes symmetric dimethylarginine
@en-gb
PRMT7, a new protein arginine ...... zes symmetric dimethylarginine
@nl
P2093
P2860
P921
P356
P1476
PRMT7, a new protein arginine ...... zes symmetric dimethylarginine
@en
P2093
Arthur M Felix
Jeffry R Cook
Jin-Hyung Lee
Nicole Herth
Olga Mirochnitchenko
Ralf Hoffmann
Samuel I Gunderson
Sidney Pestka
Zhi-Hong Yang
P2860
P304
P356
10.1074/JBC.M405295200
P407
P577
2005-02-04T00:00:00Z