Protein interfaces in signaling regulated by arginine methylation. - sprookjes - yvandenbroek - TriplyDB

Protein interfaces in signaling regulated by arginine methylation.

Protein interfaces in signaling regulated by arginine methylation.

http://www.wikidata.org/entity/Q36043261

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PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation Methylation by protein arginine methyltransferase 1 increases stability of Axin, a negative regulator of Wnt signaling Identification of proteins associated with an IFNγ-responsive promoter by a retroviral expression system for enChIP using CRISPR PRMT5-Mediated Methylation of NF-κB p65 at Arg174 Is Required for Endothelial CXCL11 Gene Induction in Response to TNF-α and IFN-γ Costimulation Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export, and intranuclear protein interactions.delayed flowering1 Encodes a basic leucine zipper protein that mediates floral inductive signals at the shoot apex in maize.Protein post-translational modifications: In silico prediction tools and molecular modeling.Arginines of the RGG box regulate FMRP association with polyribosomes and mRNA.Classification of rice (Oryza sativa L. Japonica nipponbare) immunophilins (FKBPs, CYPs) and expression patterns under water stress.TbPRMT6 is a type I protein arginine methyltransferase that contributes to cytokinesis in Trypanosoma brucei The MRE11 GAR motif regulates DNA double-strand break processing and ATR activation.Tumor necrosis factor (TNF)-α induction of CXCL10 in endothelial cells requires protein arginine methyltransferase 5 (PRMT5)-mediated nuclear factor (NF)-κB p65 methylation.The AMT1 arginine methyltransferase gene is important for plant infection and normal hyphal growth in Fusarium graminearum Autoregulation of ribosome biosynthesis by a translational response in fission yeast.Post-translational modifications of nucleosomal histones in oligodendrocyte lineage cells in development and disease.Identification of a novel lipin homologue from the parasitic protozoan Trypanosoma brucei.TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules MeMo: a web tool for prediction of protein methylation modifications.Coactivator-associated arginine methyltransferase 1 (CARM1) is a positive regulator of the Cyclin E1 gene.Protein arginine methylation in parasitic protozoa.Protein arginine methyltransferase 7 promotes breast cancer cell invasion through the induction of MMP9 expression Arginine methylation of DRBD18 differentially impacts its opposing effects on the trypanosome transcriptome.Arginine methylation of RNA-binding proteins regulates cell function and differentiation Arginine methylation-dependent regulation of ASK1 signaling by PRMT1 Protein arginine methylation in Candida albicans: role in nuclear transport.Tudor staphylococcal nuclease (Tudor-SN) participates in small ribonucleoprotein (snRNP) assembly via interacting with symmetrically dimethylated Sm proteins.CD28 costimulatory signal induces protein arginine methylation in T cells.Alternatively spliced protein arginine methyltransferase 1 isoform PRMT1v2 promotes the survival and invasiveness of breast cancer cells.Evaluating epigenetic landmarks in the brain of multiple sclerosis patients: a contribution to the current debate on disease pathogenesis Protein arginine methylation facilitates KCNQ channel-PIP2 interaction leading to seizure suppression.Specific sequences within arginine-glycine-rich domains affect mRNA-binding protein function.Identification of the RGG box motif in Shadoo: RNA-binding and signaling roles?Role of PRMTs in cancer: Could minor isoforms be leaving a mark?Transcriptional repression of hypoxia-inducible factor-1 (HIF-1) by the protein arginine methyltransferase PRMT1 Methylation of H2AR29 is a novel repressive PRMT6 target The protein arginine methyltransferases CARM1 and PRMT1 cooperate in gene regulation KSHV encoded ORF59 modulates histone arginine methylation of the viral genome to promote viral reactivation.Arginine methylation regulates telomere length and stability.PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling.Arginine methylation of hnRNPUL1 regulates interaction with NBS1 and recruitment to sites of DNA damage.

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P2860

Protein interfaces in signaling regulated by arginine methylation.

http://www.wikidata.org/entity/Q36043261

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2005 nî lūn-bûn

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Protein interfaces in signaling regulated by arginine methylation.

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Protein interfaces in signaling regulated by arginine methylation.

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Protein interfaces in signaling regulated by arginine methylation.

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Protein interfaces in signaling regulated by arginine methylation.

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Protein interfaces in signaling regulated by arginine methylation.

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Protein interfaces in signaling regulated by arginine methylation.

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STKE.2712005RE2

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Science's STKE : signal transduction knowledge environment

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Protein interfaces in signaling regulated by arginine methylation.

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Carol Anne Chénard

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François-Michel Boisvert

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Stéphane Richard

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P2860

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

Histone deimination antagonizes arginine methylation

FoxO3a regulates erythroid differentiation and induces BTG1, an activator of protein arginine methyl transferase 1

Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)

PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine

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

The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling

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271

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2005

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15713950

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