Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions.
about
The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificityIdentification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alphaAccurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometryPRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificityMethylation by protein arginine methyltransferase 1 increases stability of Axin, a negative regulator of Wnt signalingSam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1Developmentally essential protein flightless I is a nuclear receptor coactivator with actin binding activityCrystal structure of the conserved core of protein arginine methyltransferase PRMT3Differential export requirements for shuttling serine/arginine-type mRNA-binding proteins.Yeast Rrp8p, a novel methyltransferase responsible for m1A 645 base modification of 25S rRNAYeast arginine methyltransferase Hmt1p regulates transcription elongation and termination by methylating Npl3p.Conserved SR protein kinase functions in nuclear import and its action is counteracted by arginine methylation in Saccharomyces cerevisiaeYeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro formation of omega-N(G)-monomethylarginine in calf thymus histone H2A.Dynamic localization of the Swe1 regulator Hsl7 during the Saccharomyces cerevisiae cell cycleNovel RING finger proteins, Air1p and Air2p, interact with Hmt1p and inhibit the arginine methylation of Npl3p.Proteomic analysis of interactors for yeast protein arginine methyltransferase Hmt1 reveals novel substrate and insights into additional biological roles.The role of protein arginine methylation in the formation of silent chromatinThe Ccr4-Not complex interacts with the mRNA export machineryAsymmetric arginine dimethylation of heterogeneous nuclear ribonucleoprotein K by protein-arginine methyltransferase 1 inhibits its interaction with c-Src.Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export, and intranuclear protein interactions.Role of protein methylation in chromatin remodeling and transcriptional regulation.Enhanced methylarginine characterization by post-translational modification-specific targeted data acquisition and electron-transfer dissociation mass spectrometry.The AMT1 arginine methyltransferase gene is important for plant infection and normal hyphal growth in Fusarium graminearumGenetic interactions of yeast eukaryotic translation initiation factor 5A (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signalingA transient kinetic analysis of PRMT1 catalysisProtein arginine methylation in parasitic protozoa.Protein arginine methylation in Candida albicans: role in nuclear transport.RmtA, a Putative Arginine Methyltransferase, Regulates Secondary Metabolism and Development in Aspergillus flavus.Specific sequences within arginine-glycine-rich domains affect mRNA-binding protein function.Arginine methyltransferase affects interactions and recruitment of mRNA processing and export factors.Protein arginine methylation in Saccharomyces cerevisiae.Impact of Epigenetic Dietary Components on Cancer through Histone Modifications.PRMT1-Mediated Translation Regulation Is a Crucial Vulnerability of Cancer.The Major Protein Arginine Methyltransferase in Trypanosoma brucei Functions as an Enzyme-Prozyme Complex.Entamoeba histolytica: protein arginine transferase 1a methylates arginine residues and potentially modify the H4 histone.Requirement for multiple domains of the protein arginine methyltransferase CARM1 in its transcriptional coactivator function.Yeast proteins Gar1p, Nop1p, Npl3p, Nsr1p, and Rps2p are natively methylated and are substrates of the arginine methyltransferase Hmt1p.Myosin phosphatase and RhoA-activated kinase modulate arginine methylation by the regulation of protein arginine methyltransferase 5 in hepatocellular carcinoma cells.Protein arginine methylation facilitates cotranscriptional recruitment of pre-mRNA splicing factors.Role of pICLn in methylation of Sm proteins by PRMT5.
P2860
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P2860
Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions.
description
2000 nî lūn-bûn
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2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած
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2000 թվականի փետրվարին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Analysis of the yeast arginine ...... ng and substrate interactions.
@ast
Analysis of the yeast arginine ...... ng and substrate interactions.
@en
type
label
Analysis of the yeast arginine ...... ng and substrate interactions.
@ast
Analysis of the yeast arginine ...... ng and substrate interactions.
@en
prefLabel
Analysis of the yeast arginine ...... ng and substrate interactions.
@ast
Analysis of the yeast arginine ...... ng and substrate interactions.
@en
P2093
P2860
P356
P1476
Analysis of the yeast arginine ...... ing and substrate interactions
@en
P2093
P2860
P304
P356
10.1074/JBC.275.5.3128
P407
P577
2000-02-01T00:00:00Z