(Q46491561)

22 December 2017

title

The RISC subunit Tudor-SN binds to hyper-edited double-stranded RNA and promotes its cleavage (English)

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22 December 2017

author name string

Scadden AD

series ordinal

1

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22 December 2017

publication date

15 May 2005

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22 December 2017

Nature Structural & Molecular Biology

published in

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22 December 2017

volume

12

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22 December 2017

issue

6

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22 December 2017

page(s)

489-496

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22 December 2017

https://scigraph.springernature.com/pub.10.1038/nsmb936

exact match

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cites work

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The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs

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Specific cleavage of hyper-edited dsRNAs

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ADAR1 RNA deaminase limits short interfering RNA efficacy in mammalian cells

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A Dicer-2-dependent 80s complex cleaves targeted mRNAs during RNAi in Drosophila

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Differential alternative splicing activity of isoforms of polypyrimidine tract binding protein (PTB).

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Tudor domains in proteins that interact with RNA.

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The human EBNA-2 coactivator p100: multidomain organization and relationship to the staphylococcal nuclease fold and to the tudor protein involved in Drosophila melanogaster development

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Identification of p100 as a coactivator for STAT6 that bridges STAT6 with RNA polymerase II.

21 January 2018

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RNA editing of a miRNA precursor

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Systematic identification of abundant A-to-I editing sites in the human transcriptome

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The active form of Xp54 RNA helicase in translational repression is an RNA-mediated oligomer

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The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes.

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Preferential selection of adenosines for modification by double-stranded RNA adenosine deaminase.

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31 March 2020

Identifiers

DOI

10.1038/NSMB936

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22 December 2017

PubMed ID

15895094

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22 December 2017