Arginine Methylation
Mostrando 1-12 de 48 artigos, teses e dissertações.
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1. Estudos funcionais da proteína reguladora humana Ki-1/57 e seus parceiros de interação / Functional studies of the human regulatory protein Ki-1/57 and its interaction partners
The protein Ki-1/57 was discovered through cross reactivity of the monoclonal antibody Ki-1 in cells of Hodgkin lymphoma. Previously studies demonstrated that Ki-1/57 interacts with RACK-1 protein, undergoes phosphorylation by PKCs and methylation by PRMT1, an arginine methyltransferase that modulates several RNA binding proteins. Studies have shown that Ki-
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 12/07/2011
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2. Ki-1/57 e uma proteina intrinsecamente desordenada envolvida em mecanismos de regulação genica / Ki-1/57 is an intrinsically disordered protein involved in mechanisms of gene regulation
The Ki-1/57 protein has been discovered through the cross reactivity of the monoclonal antibody Ki-1 in Hodgkin lymphoma cells. Previously, it was demonstrated that Ki-1/57 undergoes phosphorylation by PKCs and methylation by PRMT1, an arginine methyltransferase that modulates many RNA binding proteins. Here, the interaction of Ki-1/57 with RNA polyuridine a
Publicado em: 2009
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3. Estudos funcionais e estruturais da proteina humana hnRNP Q/NSAP1 / Funcional and structural studies of human protein hnRNPQ
The members of the hnRNPs family (heterogenous nuclear ribonuclein proteins) play important roles in gene expression control and mRNAs metabolism. The proteins hnRNPD (AUF1) and hnRNPQ (NSAP1) were the main targets of this study. AUF1 has two RNA recognition motifs (RRM) and participates in the process of destabilization of a class of mRNAs that contain AU-r
Publicado em: 2008
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4. Analise das proteinas Ki-1/57 e PRMT1 : identificação, mapeamento e caracterização funcional da interação com outras proteinas / Analysis of the proteins Ki-1/57 and PRMT1: identification, mapping and characterization of the interaction with other proteins
The protein Ki-1/57 that is found both in the cytoplasm and nucleus is associated with serine/threonine protein kinase activity and gets phosphorylated on serine and threonine residues upon cellular activation. We demonstrated that Ki-1/57 interacts with the Chromatin-Helicase-DNA-binding domain protein 3 (CHD3) and with the adaptor/signaling protein RACK1 i
Publicado em: 2006
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5. Nuclear Export of hnRNP Hrp1p and Nuclear Export of hnRNP Npl3p Are Linked and Influenced by the Methylation State of Npl3p
Eukaryotic mRNA processing and export are mediated by a series of complexes composed of heterogeneous nuclear ribonucleoproteins (hnRNPs). Many of these hnRNPs are methylated at arginine residues within their RGG domains. Although cellular arginine methylation is required for the efficient nuclear export of several hnRNPs, its role in this process is unknown
American Society for Microbiology.
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6. The essential yeast RNA binding protein Npl3p is methylated
Arginine methylation is a prevalent modification found in many RNA binding proteins, yet little is known about its functional consequences. Using a monoclonal antibody, 1E4, we have shown that the yeast NPL3 gene product Npl3p, an essential RNA binding protein with repeated RGG motifs, is arginine-methylated in vivo. The 1E4 epitope can be generated by
The National Academy of Sciences of the USA.
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7. Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice
Arginine methylation has been implicated in the regulation of gene expression. The coactivator-associated arginine methyltransferase 1 (CARM1/PRMT4) binds the p160 family of steroid receptor coactivators (SRCs). This association enhances transcriptional activation by nuclear receptors. Here, we show that embryos with a targeted disruption of CARM1 are sm
National Academy of Sciences.
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8. Arginine methylation facilitates the nuclear export of hnRNP proteins
Eukaryotic mRNA processing and export is mediated by various heterogeneous nuclear ribonucleoproteins (hnRNPs). Many of these hnRNPs are methylated on arginine residues. In the yeast, Saccharomyces cerevisiae, the predominant enzyme responsible for arginine methylation is Hmt1p. Hmt1p methylates both Npl3p and Hrp1p, which are shuttling hnRNPs involved in mR
Cold Spring Harbor Laboratory Press.
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9. Arginine Methylation Increases the Stability of Human Immunodeficiency Virus Type 1 Tat▿
Arginine methylation of human immunodeficiency virus type 1 (HIV-1) Tat protein downregulates its key function in viral-gene transactivation. The fate of methylated Tat is unknown, so it is unclear whether methylated Tat is degraded or persists in the cell for additional functions. Here we show that the arginine methyltransferase PRMT6 increases Tat protein
American Society for Microbiology (ASM).
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10. Methylation at arginine 17 of histone H3 is linked to gene activation
The nuclear hormone receptor co-activator CARM1 has the potential to methylate histone H3 at arginine residues in vitro. The methyltransferase activity of CARM1 is necessary for its co-activator functions in transient transfection assays. However, the role of this methyltransferase in vivo is unclear, given that methylation of arginines is not easily detecta
Oxford University Press.
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11. Hepatitis Delta Virus Antigen Is Methylated at Arginine Residues, and Methylation Regulates Subcellular Localization and RNA Replication
Hepatitis delta virus (HDV) contains a circular RNA which encodes a single protein, hepatitis delta antigen (HDAg). HDAg exists in two forms, a small form (S-HDAg) and a large form (L-HDAg). S-HDAg can transactivate HDV RNA replication. Recent studies have shown that posttranslational modifications, such as phosphorylation and acetylation, of S-HDAg can modu
American Society for Microbiology.
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12. The 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
The NS3 protein of hepatitis C virus (HCV) contains protease and RNA helicase activities, both of which are likely to be essential for HCV propagation. An arginine residue present in the arginine-glycine (RG)-rich region of many RNA-binding proteins is posttranslationally methylated by protein arginine methyltransferases (PRMTs). Amino acid sequence analysis
American Society for Microbiology.