PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays - Test2 - elhamkhani - TriplyDB

PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays

PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays

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Interplay among coactivator-associated arginine methyltransferase 1, CBP, and CIITA in IFN-gamma-inducible MHC-II gene expression Embryonic poly(A)-binding protein stimulates translation in germ cells Structural basis of ligand recognition by PABC, a highly specific peptide-binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase.Discovery of peptidylarginine deiminase-4 substrates by protein array: antagonistic citrullination and methylation of human ribosomal protein S2 Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)Promiscuous modification of the nuclear poly(A)-binding protein by multiple protein-arginine methyltransferases does not affect the aggregation behavior CARM1 methylates chromatin remodeling factor BAF155 to enhance tumor progression and metastasis A Y2H-seq approach defines the human protein methyltransferase interactome Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association Poly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression Arginine methyltransferases as novel therapeutic targets for breast cancer Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase The protein arginine methyltransferase PRMT5 promotes D2-like dopamine receptor signaling Identifying and quantifying in vivo methylation sites by heavy methyl SILAC Enzymatic reactions on immobilised substrates CARM1 regulates proliferation of PC12 cells by methylating HuD Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice Biochemical control of CARM1 enzymatic activity by phosphorylation Protein arginine methylation in mammals: who, what, and why A protein-domain microarray identifies novel protein-protein interactions.Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition.Xenoestrogens regulate the activity of arginine methyltransferases.Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase.RNA helicases: emerging roles in viral replication and the host innate response.Emerging technologies to map the protein methylome.Identification of small-molecule enhancers of arginine methylation catalyzed by coactivator-associated arginine methyltransferase 1.Protein-arginine methyltransferase 1 (PRMT1) methylates Ash2L, a shared component of mammalian histone H3K4 methyltransferase complexes.Automethylation of CARM1 allows coupling of transcription and mRNA splicing Loss of CARM1 is linked to reduced HuR function in replicative senescence.Selective inhibitors of protein methyltransferases Protein arginine methyltransferase CARM1 attenuates the paraspeckle-mediated nuclear retention of mRNAs containing IRAlus The activity and stability of the transcriptional coactivator p/CIP/SRC-3 are regulated by CARM1-dependent methylation The multifunctional poly(A)-binding protein (PABP) 1 is subject to extensive dynamic post-translational modification, which molecular modelling suggests plays an important role in co-ordinating its activities.PRMT1 Is a Novel Regulator of Epithelial-Mesenchymal-Transition in Non-small Cell Lung Cancer.Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ω-NG-monomethylated arginine residues.Protein interfaces in signaling regulated by arginine methylation.Using oriented peptide array libraries to evaluate methylarginine-specific antibodies and arginine methyltransferase substrate motifs Surface-scanning mutational analysis of protein arginine methyltransferase 1: roles of specific amino acids in methyltransferase substrate specificity, oligomerization, and coactivator function.Carm1 regulates Pax7 transcriptional activity through MLL1/2 recruitment during asymmetric satellite stem cell divisions Novel CARM1-Interacting Protein, DZIP3, Is a Transcriptional Coactivator of Estrogen Receptor-α

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PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays

http://www.wikidata.org/entity/Q24522567

description

2002 nî lūn-bûn

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2002 թուականի Մարտին հրատարակուած գիտական յօդուած

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2002 թվականի մարտին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

PABP1 identified as an arginin ...... ng high-density protein arrays

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PABP1 identified as an arginin ...... ng high-density protein arrays

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PABP1 identified as an arginin ...... ng high-density protein arrays

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PABP1 identified as an arginin ...... ng high-density protein arrays

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PABP1 identified as an arginin ...... ng high-density protein arrays

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PABP1 identified as an arginin ...... ng high-density protein arrays

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PABP1 identified as an arginin ...... ng high-density protein arrays

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prefLabel

PABP1 identified as an arginin ...... ng high-density protein arrays

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PABP1 identified as an arginin ...... ng high-density protein arrays

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PABP1 identified as an arginin ...... ng high-density protein arrays

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PABP1 identified as an arginin ...... ng high-density protein arrays

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Jaeho Lee

http://www.w3.org/2001/XMLSchema#string

Mark T Bedford

http://www.w3.org/2001/XMLSchema#string

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A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation

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

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

MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates

A method for global protein expression and antibody screening on high-density filters of an arrayed cDNA library

X-ray structure of the human hyperplastic discs protein: an ortholog of the C-terminal domain of poly(A)-binding protein

A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding proteins.

The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae.

Arginine methylation facilitates the nuclear export of hnRNP proteins

Regulation of transcription by a protein methyltransferase

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268-73

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scholarly article

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496885

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10.1093/EMBO-REPORTS/KVF052

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3

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3

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2002-03-01T00:00:00Z

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11511776

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11850402

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1084016

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