Arginine methylation facilitates the nuclear export of hnRNP proteins - Test2 - elhamkhani - TriplyDB

Arginine methylation facilitates the nuclear export of hnRNP proteins

Arginine methylation facilitates the nuclear export of hnRNP proteins

http://www.wikidata.org/entity/Q27931932

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Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1 The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine Friend of Prmt1, a novel chromatin target of protein arginine methyltransferases The host protein Staufen1 interacts with the Pr55Gag zinc fingers and regulates HIV-1 assembly via its N-terminus Purification and identification of a novel complex which is involved in androgen receptor-dependent transcription PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays Analysis of a noncanonical poly(A) site reveals a tripartite mechanism for vertebrate poly(A) site recognition ICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway.Deciphering the cellular pathway for transport of poly(A)-binding protein II Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1 The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits Crystal structure of the conserved core of protein arginine methyltransferase PRMT3 Disengaging polymerase: terminating RNA polymerase II transcription in budding yeast Coupling pre-mRNA processing to transcription on the RNA factory assembly line Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides Nuclear export of hnRNP Hrp1p and nuclear export of hnRNP Npl3p are linked and influenced by the methylation state of Npl3p.Differential export requirements for shuttling serine/arginine-type mRNA-binding proteins.Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p.A protein required for nuclear-protein import, Mog1p, directly interacts with GTP-Gsp1p, the Saccharomyces cerevisiae ran homologue.The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity.Phosphorylation by Sky1p promotes Npl3p shuttling and mRNA dissociation.Conserved SR protein kinase functions in nuclear import and its action is counteracted by arginine methylation in Saccharomyces cerevisiae Cap-binding protein 1-mediated and eukaryotic translation initiation factor 4E-mediated pioneer rounds of translation in yeast.Yeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro formation of omega-N(G)-monomethylarginine in calf thymus histone H2A.Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro.Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal protein Rps2 in Saccharomyces cerevisiae.The shuttling protein Npl3 promotes translation termination accuracy in Saccharomyces cerevisiae.Identification of Gbp2 as a novel poly(A)+ RNA-binding protein involved in the cytoplasmic delivery of messenger RNAs in yeast.Novel RING finger proteins, Air1p and Air2p, interact with Hmt1p and inhibit the arginine methylation of Npl3p.Proteomic analysis of interactors for yeast protein arginine methyltransferase Hmt1 reveals novel substrate and insights into additional biological roles.Messenger RNAs are recruited for nuclear export during transcription.Polyadenylation site choice in yeast is affected by competition between Npl3 and polyadenylation factor CFI.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 autoantibodies Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains Interaction of PRMT1 with BTG/TOB proteins in cell signalling: molecular analysis and functional aspects A novel WD repeat protein component of the methylosome binds Sm proteins

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Arginine methylation facilitates the nuclear export of hnRNP proteins

http://www.wikidata.org/entity/Q27931932

description

1998 nî lūn-bûn

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1998 թուականի Մարտին հրատարակուած գիտական յօդուած

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1998 թվականի մարտին հրատարակված գիտական հոդված

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1998年の論文

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1998年論文

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1998年論文

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1998年論文

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1998年論文

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1998年論文

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1998年论文

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name

Arginine methylation facilitates the nuclear export of hnRNP proteins

@ast

Arginine methylation facilitates the nuclear export of hnRNP proteins

@en

Arginine methylation facilitates the nuclear export of hnRNP proteins

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type

label

Arginine methylation facilitates the nuclear export of hnRNP proteins

@ast

Arginine methylation facilitates the nuclear export of hnRNP proteins

@en

Arginine methylation facilitates the nuclear export of hnRNP proteins

@nl

prefLabel

Arginine methylation facilitates the nuclear export of hnRNP proteins

@ast

Arginine methylation facilitates the nuclear export of hnRNP proteins

@en

Arginine methylation facilitates the nuclear export of hnRNP proteins

@nl

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P1433

Genes & Development

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Arginine methylation facilitates the nuclear export of hnRNP proteins

@en

P2093

E C Shen

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M F Henry

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M S Lee

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

P A Silver

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V H Weiss

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P2860

A nuclear export signal in hnRNP A1: a signal-mediated, temperature-dependent nuclear protein export pathway

hnRNP G: sequence and characterization of a glycosylated RNA-binding protein

Functional expression of cloned human splicing factor SF2: homology to RNA-binding proteins, U1 70K, and Drosophila splicing regulators

A nuclear cap binding protein complex involved in pre-mRNA splicing

The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase

A nuclear cap-binding complex binds Balbiani ring pre-mRNA cotranscriptionally and accompanies the ribonucleoprotein particle during nuclear export

A cap-binding protein complex mediating U snRNA export

Purification and characterization of S-adenosylmethionine-protein-arginine N-methyltransferase from rat liver

Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors

CRM1 is an export receptor for leucine-rich nuclear export signals

P304

679-691

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scholarly article

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10.1101/GAD.12.5.679

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5

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12

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Sandro R Valentini

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1998-03-01T00:00:00Z

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51298094

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9499403

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P932

316575

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