Clustering of glycine and NG,NG-dimethylarginine in nucleolar protein C23.
about
The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificityPurification and characterization of S-adenosylmethionine-protein-arginine N-methyltransferase from rat liverEnzymic methylation of arginyl residues in -gly-arg-gly- peptidesSymmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein.Spb1p is a yeast nucleolar protein associated with Nop1p and Nop58p that is able to bind S-adenosyl-L-methionine in vitroComponents of U3 snoRNA-containing complexes shuttle between nuclei and the cytoplasm and differentially localize in nucleoli: implications for assembly and functionAnalysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factorsNuclear activities of basic fibroblast growth factor: potentiation of low-serum growth mediated by natural or chimeric nuclear localization signalsStructure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptidesGAR1 is an essential small nucleolar RNP protein required for pre-rRNA processing in yeast.A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding proteins.The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae.Saccharomyces cerevisiae SSB1 protein and its relationship to nucleolar RNA-binding proteins.A yeast nucleolar protein related to mammalian fibrillarin is associated with small nucleolar RNA and is essential for viability.Arginine 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 familyDeterminants of the interaction of the spinal muscular atrophy disease protein SMN with the dimethylarginine-modified box H/ACA small nucleolar ribonucleoprotein GAR1Human fibrillarin forms a sub-complex with splicing factor 2-associated p32, protein arginine methyltransferases, and tubulins alpha 3 and beta 1 that is independent of its association with preribosomal ribonucleoprotein complexesDAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivoNucleolin: a multifunctional major nucleolar phosphoproteinProtein 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 viableProteomic Analysis of Arginine Methylation Sites in Human Cells Reveals Dynamic Regulation During Transcriptional ArrestNucleolin, the major nucleolar protein of growing eukaryotic cells: an unusual protein structure revealed by the nucleotide sequence.The carboxy-terminal fragment of nucleolin interacts with the nucleocapsid domain of retroviral gag proteins and inhibits virion assembly.Biochemical analysis of the arginine methylation of high molecular weight fibroblast growth factor-2.Arginine methylation and binding of Hrp1p to the efficiency element for mRNA 3'-end formation.In vivo analysis of nucleolar proteins modified by the yeast arginine methyltransferase Hmt1/Rmt1p.IGFBP-5 Promotes Fibrosis Independently of Its Translocation to the Nucleus and Its Interaction with Nucleolin and IGF.The RGG box motif of the herpes simplex virus ICP27 protein mediates an RNA-binding activity and determines in vivo methylation.Protein interfaces in signaling regulated by arginine methylation.Structural and sequence motifs of protein (histone) methylation enzymes.In vivo and in vitro arginine methylation of RNA-binding proteinsSequence and functional similarity between a yeast ribosomal protein and the Escherichia coli S5 ram proteinChemical mechanisms of histone lysine and arginine modificationsThe Gly/Arg-rich (GAR) domain of Xenopus nucleolin facilitates in vitro nucleic acid binding and in vivo nucleolar localization.Determination of the functional domains involved in nucleolar targeting of nucleolin.High affinity interactions of nucleolin with G-G-paired rDNA.A specific isoform of hnRNP D interacts with DNA in the LR1 heterodimer: canonical RNA binding motifs in a sequence-specific duplex DNA binding protein.PRMT3 is a distinct member of the protein arginine N-methyltransferase family. Conferral of substrate specificity by a zinc-finger domain.
P2860
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P2860
Clustering of glycine and NG,NG-dimethylarginine in nucleolar protein C23.
description
1985 nî lūn-bûn
@nan
1985年の論文
@ja
1985年学术文章
@wuu
1985年学术文章
@zh-cn
1985年学术文章
@zh-hans
1985年学术文章
@zh-my
1985年学术文章
@zh-sg
1985年學術文章
@yue
1985年學術文章
@zh
1985年學術文章
@zh-hant
name
Clustering of glycine and NG,NG-dimethylarginine in nucleolar protein C23.
@en
Clustering of glycine and NG,NG-dimethylarginine in nucleolar protein C23.
@nl
type
label
Clustering of glycine and NG,NG-dimethylarginine in nucleolar protein C23.
@en
Clustering of glycine and NG,NG-dimethylarginine in nucleolar protein C23.
@nl
prefLabel
Clustering of glycine and NG,NG-dimethylarginine in nucleolar protein C23.
@en
Clustering of glycine and NG,NG-dimethylarginine in nucleolar protein C23.
@nl
P2093
P356
P1433
P1476
Clustering of glycine and NG,NG-dimethylarginine in nucleolar protein C23.
@en
P2093
P304
P356
10.1021/BI00343A001
P407
P577
1985-10-01T00:00:00Z