A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor
about
Functional cloning and characterization of a novel nonhomeodomain protein that inhibits the binding of PBX1-HOX complexes to DNAHeterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificityCloning and characterization of a family of proteins associated with MplHepatitis C virus nonstructural protein NS3 binds to Sm-D1, a small nuclear ribonucleoprotein associated with autoimmune diseasePRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginineInteraction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complexThe arginine-1493 residue in QRRGRTGR1493G motif IV of the hepatitis C virus NS3 helicase domain is essential for NS3 protein methylation by the protein arginine methyltransferase 1.Principles of interleukin (IL)-6-type cytokine signalling and its regulationArrest of G(1)-S progression by the p53-inducible gene PC3 is Rb dependent and relies on the inhibition of cyclin D1 transcriptionPRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunitsCrystal structure of the conserved core of protein arginine methyltransferase PRMT3Methyltransferase PRMT1 is a binding partner of HBx and a negative regulator of hepatitis B virus transcriptionStructure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptidesYeast ribosomal protein L12 is a substrate of protein-arginine methyltransferase 2.The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity.Novel RING finger proteins, Air1p and Air2p, interact with Hmt1p and inhibit the arginine methylation of Npl3p.The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodiesArginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domainsPrmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase familyInteraction of PRMT1 with BTG/TOB proteins in cell signalling: molecular analysis and functional aspectsA novel WD repeat protein component of the methylosome binds Sm proteinsInterferons, interferon-like cytokines, and their receptorsProtein arginine methyltransferase I: substrate specificity and role in hnRNP assemblyArginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viableAsymmetric arginine dimethylation of heterogeneous nuclear ribonucleoprotein K by protein-arginine methyltransferase 1 inhibits its interaction with c-Src.Interferon induction and function at the mucosal surface.Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions.Pharmaceutical intervention in the JAK/STAT signaling pathway.Chemical and biochemical approaches in the study of histone methylation and demethylationLipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase.Role of protein methylation in chromatin remodeling and transcriptional regulation.The critical role of protein arginine methyltransferase prmt8 in zebrafish embryonic and neural development is non-redundant with its paralogue prmt1.Expression and immune characterization of a novel enzyme, protein arginine methyltransferase 1, from Schistosoma japonicumProtein interfaces in signaling regulated by arginine methylation.Structural and sequence motifs of protein (histone) methylation enzymes.Endogenous production of nitric oxide synthase inhibitors.Nucleocytoplasmic transport of macromoleculesSmall Molecule Inhibitors of Protein Arginine Methyltransferases.Novel functions of protein arginine methyltransferase 1 in thyroid hormone receptor-mediated transcription and in the regulation of metamorphic rate in Xenopus laevis.
P2860
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P2860
A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor
description
1997 nî lūn-bûn
@nan
1997 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
A protein-arginine methyltrans ...... the type I interferon receptor
@ast
A protein-arginine methyltrans ...... the type I interferon receptor
@en
A protein-arginine methyltrans ...... the type I interferon receptor
@en-gb
A protein-arginine methyltrans ...... the type I interferon receptor
@nl
type
label
A protein-arginine methyltrans ...... the type I interferon receptor
@ast
A protein-arginine methyltrans ...... the type I interferon receptor
@en
A protein-arginine methyltrans ...... the type I interferon receptor
@en-gb
A protein-arginine methyltrans ...... the type I interferon receptor
@nl
prefLabel
A protein-arginine methyltrans ...... the type I interferon receptor
@ast
A protein-arginine methyltrans ...... the type I interferon receptor
@en
A protein-arginine methyltrans ...... the type I interferon receptor
@en-gb
A protein-arginine methyltrans ...... the type I interferon receptor
@nl
P2093
P2860
P356
P1433
P1476
A protein-arginine methyltrans ...... the type I interferon receptor
@en
P2093
P2860
P356
10.1093/EMBOJ/16.2.260
P407
P577
1997-01-15T00:00:00Z