Arginine methylation regulates IL-2 gene expression: a role for protein arginine methyltransferase 5 (PRMT5). - Wikidata - awgldk - TriplyDB

Arginine methylation regulates IL-2 gene expression: a role for protein arginine methyltransferase 5 (PRMT5).

Arginine methylation regulates IL-2 gene expression: a role for protein arginine methyltransferase 5 (PRMT5).

http://www.wikidata.org/entity/Q41927743

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Role of type II protein arginine methyltransferase 5 in the regulation of Circadian Per1 gene HOXA9 methylation by PRMT5 is essential for endothelial cell expression of leukocyte adhesion molecules Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes Roles of protein arginine methyltransferases in the control of glucose metabolism The proteomic investigation reveals interaction of mdig protein with the machinery of DNA double-strand break repair Mouse MAELSTROM: the link between meiotic silencing of unsynapsed chromatin and microRNA pathway?Effects of a novel arginine methyltransferase inhibitor on T-helper cell cytokine production The LIM protein AJUBA recruits protein arginine methyltransferase 5 to mediate SNAIL-dependent transcriptional repression Protein arginine methylation in mammals: who, what, and why Modulation of Epstein-Barr virus nuclear antigen 2-dependent transcription by protein arginine methyltransferase 5.Asymmetric Arginine dimethylation of Epstein-Barr virus nuclear antigen 2 promotes DNA targeting.Protein Arginine Methyltransferase 5 Inhibition Upregulates Foxp3+ Regulatory T Cells Frequency and Function during the Ulcerative Colitis Methylation of histone H3 and H4 by PRMT5 regulates ribosomal RNA gene transcription.Characterization of the PRMT gene family in rice reveals conservation of arginine methylation.Tumor necrosis factor (TNF)-α induction of CXCL10 in endothelial cells requires protein arginine methyltransferase 5 (PRMT5)-mediated nuclear factor (NF)-κB p65 methylation.Tudor domains bind symmetrical dimethylated arginines.The exon junction complex component Y14 modulates the activity of the methylosome in biogenesis of spliceosomal small nuclear ribonucleoproteins Arginine methylation by PRMT5 at a naturally occurring mutation site is critical for liver metabolic regulation by small heterodimer partner Protein arginine methyltransferase 5 (Prmt5) promotes gene expression of peroxisome proliferator-activated receptor γ2 (PPARγ2) and its target genes during adipogenesis.Loading of PAX3 to Mitotic Chromosomes Is Mediated by Arginine Methylation and Associated with Waardenburg Syndrome Preventative oral methylthioadenosine is anti-inflammatory and reduces DSS-induced colitis in mice.Lupus autoimmunity altered by cellular methylation metabolism.Overexpression of PRMT5 promotes tumor cell growth and is associated with poor disease prognosis in epithelial ovarian cancer.PRMT5-Selective Inhibitors Suppress Inflammatory T Cell Responses and Experimental Autoimmune Encephalomyelitis.Targets in epigenetics: inhibiting the methyl writers of the histone code Epigenetic regulation of kallikrein-related peptidases: there is a whole new world out there.Protein arginine methylation in Saccharomyces cerevisiae.Autoantigens: novel forms and presentation to the immune system.Discovery of selective protein arginine methyltransferase 5 inhibitors and biological evaluations.Emerging Role for Methylation in Multiple Sclerosis: Beyond DNA.JAK2V617F-mediated phosphorylation of PRMT5 downregulates its methyltransferase activity and promotes myeloproliferation.A thermally targeted peptide inhibitor of symmetrical dimethylation inhibits cancer-cell proliferation.The Kruppel-like zinc finger protein ZNF224 recruits the arginine methyltransferase PRMT5 on the transcriptional repressor complex of the aldolase A gene.The dual epigenetic role of PRMT5 in acute myeloid leukemia: gene activation and repression via histone arginine methylation.Myosin phosphatase and RhoA-activated kinase modulate arginine methylation by the regulation of protein arginine methyltransferase 5 in hepatocellular carcinoma cells.Novel inhibitors for PRMT1 discovered by high-throughput screening using activity-based fluorescence polarization.Molecular characterization, phylogenetic analysis and expression patterns of five protein arginine methyltransferase genes of channel catfish, Ictalurus punctatus (Rafinesque).The protein arginine methyltransferase Prmt5 is required for myogenesis because it facilitates ATP-dependent chromatin remodeling.Methylthioadenosine reverses brain autoimmune disease.Oxidative Modifications in Tissue Pathology and Autoimmune Disease.

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P2860

Arginine methylation regulates IL-2 gene expression: a role for protein arginine methyltransferase 5 (PRMT5).

http://www.wikidata.org/entity/Q41927743

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Arginine methylation regulates ...... e methyltransferase 5 (PRMT5).

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Arginine methylation regulates ...... e methyltransferase 5 (PRMT5).

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Mélanie Morel

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Patrick Cléroux

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Stéphane Richard

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P2860

Translating the Histone Code

Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3

Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1

The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity

Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha

Histone deimination antagonizes arginine methylation

PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation

A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor

PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity

The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase

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379-386

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scholarly article

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10.1042/BJ20040373

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P433

Pt 1

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388

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2005-05-01T00:00:00Z

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15654770

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1186728

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