Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I. - Wikidata - thesis-toulmin - TriplyDB

Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I.

Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I.

http://www.wikidata.org/entity/Q34002244

about

Crystal structure of a human cleavage factor CFI(m)25/CFI(m)68/RNA complex provides an insight into poly(A) site recognition and RNA looping Roscovitine inhibits EBNA1 serine 393 phosphorylation, nuclear localization, transcription, and episome maintenance Comparative host protein interactions with HTLV-1 p30 and HTLV-2 p28: insights into difference in pathobiology of human retroviruses.Root morphogenic pathways in Eucalyptus grandis are modified by the activity of protein arginine methyltransferases.The Cleavage and Polyadenylation Specificity Factor 6 (CPSF6) Subunit of the Capsid-recruited Pre-messenger RNA Cleavage Factor I (CFIm) Complex Mediates HIV-1 Integration into Genes.Small Molecule Inhibitors of Protein Arginine Methyltransferases.The structure of human cleavage factor I(m) hints at functions beyond UGUA-specific RNA binding: a role in alternative polyadenylation and a potential link to 5' capping and splicing.Protein arginine methylation of non-histone proteins and its role in diseases.The Role of Protein Arginine Methylation in mRNP Dynamics Noncanonical Alternative Polyadenylation Contributes to Gene Regulation in Response to Hypoxia.Cleavage factor Im is a key regulator of 3' UTR length.

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P2860

Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I.

http://www.wikidata.org/entity/Q34002244

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

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2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

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2010年论文

@wuu

name

Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I.

@ast

Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I.

@en

Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I.

@nl

type

label

Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I.

@ast

Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I.

@en

Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I.

@nl

prefLabel

Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I.

@ast

Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I.

@en

Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I.

@nl

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Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I.

@en

P2093

Antje Ostareck-Lederer

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

Ashwin Chari

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Diana Blank

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Georges Martin

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Nils Neuenkirchen

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Sabine Dettwiler

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Ursula Rüegsegger

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Walter Keller

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P2860

Towards a proteome-scale map of the human protein–protein interaction network

Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors

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

Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization

Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha

A mechanism for the regulation of pre-mRNA 3' processing by human cleavage factor Im

FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues

PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine

Purification and characterization of human cleavage factor Im involved in the 3' end processing of messenger RNA precursors

PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation

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1646-1659

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scholarly article

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10.1261/RNA.2164210

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8

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16

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2010-06-18T00:00:00Z

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44686840

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20562214

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2905762

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