Methylation of histone H3 by coactivator-associated arginine methyltransferase 1
about
Transcriptional activation of human matrix metalloproteinase-9 gene expression by multiple co-activatorsThe novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificityThe kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignmentStructural basis for the methylation site specificity of SET7/9PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylationPromiscuous modification of the nuclear poly(A)-binding protein by multiple protein-arginine methyltransferases does not affect the aggregation behaviorTDRD3 is an effector molecule for arginine-methylated histone marksMethylation at arginine 17 of histone H3 is linked to gene activationPABP1 identified as an arginine methyltransferase substrate using high-density protein arraysSam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1Btg2 enhances retinoic acid-induced differentiation by modulating histone H4 methylation and acetylationMethylation of Tat by PRMT6 regulates human immunodeficiency virus type 1 gene expressionHuman SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genesHistone arginine methylation regulates pluripotency in the early mouse embryoLysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein associationmSin3A/histone deacetylase 2- and PRMT5-containing Brg1 complex is involved in transcriptional repression of the Myc target gene cadPosttranslational control of HuR functionArginine methyltransferases as novel therapeutic targets for breast cancerThe methyltransferases PRMT4/CARM1 and PRMT5 control differentially myogenesis in zebrafishInsights into histone code syntax from structural and biochemical studies of CARM1 methyltransferaseStructural basis for CARM1 inhibition by indole and pyrazole inhibitorsYeast ribosomal protein L12 is a substrate of protein-arginine methyltransferase 2.Proteomic analysis of interactors for yeast protein arginine methyltransferase Hmt1 reveals novel substrate and insights into additional biological roles.Ligand-dependent activation of the farnesoid X-receptor directs arginine methylation of histone H3 by CARM1Global regulation of post-translational modifications on core histonesA role for CARM1-mediated histone H3 arginine methylation in protecting histone acetylation by releasing corepressors from chromatinStructure and regulation of the mDot1 gene, a mouse histone H3 methyltransferasebeta-Catenin primes organizer gene expression by recruiting a histone H3 arginine 8 methyltransferase, Prmt2Protein arginine methyltransferase I: substrate specificity and role in hnRNP assemblySpecific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient miceDouble chromodomains cooperate to recognize the methylated histone H3 tailPRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X.Characterization of PRMT1 from Plasmodium falciparumAsymmetric arginine dimethylation of heterogeneous nuclear ribonucleoprotein K by protein-arginine methyltransferase 1 inhibits its interaction with c-Src.Readers of histone methylarginine marks.Quantitative proteomic analysis of histone modificationsInvolvement of histone methylation and phosphorylation in regulation of transcription by thyroid hormone receptor.Epigenetic modification affecting expression of cell polarity and cell fate genes to regulate lineage specification in the early mouse embryoTranscriptome asymmetry within mouse zygotes but not between early embryonic sister blastomeresDisruption of histone modification and CARM1 recruitment by arsenic represses transcription at glucocorticoid receptor-regulated promoters.
P2860
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P2860
Methylation of histone H3 by coactivator-associated arginine methyltransferase 1
description
2001 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մայիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2001
@ast
im Mai 2001 veröffentlicher wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2001/05/15)
@sk
vědecký článek publikovaný v roce 2001
@cs
wetenschappelijk artikel (gepubliceerd op 2001/05/15)
@nl
наукова стаття, опублікована в травні 2001
@uk
مقالة علمية (نشرت في 15-5-2001)
@ar
name
Methylation of histone H3 by coactivator-associated arginine methyltransferase 1
@ast
Methylation of histone H3 by coactivator-associated arginine methyltransferase 1
@en
Methylation of histone H3 by coactivator-associated arginine methyltransferase 1
@nl
type
label
Methylation of histone H3 by coactivator-associated arginine methyltransferase 1
@ast
Methylation of histone H3 by coactivator-associated arginine methyltransferase 1
@en
Methylation of histone H3 by coactivator-associated arginine methyltransferase 1
@nl
prefLabel
Methylation of histone H3 by coactivator-associated arginine methyltransferase 1
@ast
Methylation of histone H3 by coactivator-associated arginine methyltransferase 1
@en
Methylation of histone H3 by coactivator-associated arginine methyltransferase 1
@nl
P2093
P3181
P356
P1433
P1476
Methylation of histone H3 by coactivator-associated arginine methyltransferase 1
@en
P2093
A. Henschen-Edman
B. L. Hanson
B. T. Schurter
D. R. Mackay
D. W. Aswad
G. J. Bunick
J. M. Harp
M. R. Stallcup
P304
P3181
P356
10.1021/BI002631B
P407
P577
2001-05-15T00:00:00Z