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The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing

The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing

http://www.wikidata.org/entity/Q34000158

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Air2p is critical for the assembly and RNA-binding of the TRAMP complex and the KOW domain of Mtr4p is crucial for exosome activation RNA helicases at work: binding and rearranging The Pfam protein families database Rrp6: Integrated roles in nuclear RNA metabolism and transcription termination Threading the barrel of the RNA exosome Ski2-like RNA helicase structures: common themes and complex assemblies Processing of preribosomal RNA in Saccharomyces cerevisiae RNA helicase proteins as chaperones and remodelers Nuclear noncoding RNA surveillance: is the end in sight?Comparative Structural Analysis of Human DEAD-Box RNA Helicases The crystal structure of S. cerevisiae Ski2, a DExH helicase associated with the cytoplasmic functions of the exosome The RNA helicase Mtr4p modulates polyadenylation in the TRAMP complex.RNA unwinding by the Trf4/Air2/Mtr4 polyadenylation (TRAMP) complex The telomerase inhibitor Gno1p/PINX1 activates the helicase Prp43p during ribosome biogenesis.The RNA helicases AtMTR4 and HEN2 target specific subsets of nuclear transcripts for degradation by the nuclear exosome in Arabidopsis thaliana Mutations in Mtr4 Structural Domains Reveal Their Important Role in Regulating tRNAiMet Turnover in Saccharomyces cerevisiae and Mtr4p Enzymatic Activities In Vitro.Structure of the frequency-interacting RNA helicase: a protein interaction hub for the circadian clock.Sen1 has unique structural features grafted on the architecture of the Upf1-like helicase family Comparison of the yeast and human nuclear exosome complexes.Winged helix domains with unknown function in Hel308 and related helicases.Integrity of SRP RNA is ensured by La and the nuclear RNA quality control machinery.Conserved RNA helicase FRH acts nonenzymatically to support the intrinsically disordered neurospora clock protein FRQ.Unique properties of the Mtr4p-poly(A) complex suggest a role in substrate targeting.microRNAs targeting DEAD-box helicases are involved in salinity stress response in rice (Oryza sativa L.).The Mtr4 ratchet helix and arch domain both function to promote RNA unwinding Roles of DEAD-box proteins in RNA and RNP Folding.The fission yeast MTREC complex targets CUTs and unspliced pre-mRNAs to the nuclear exosome.Mycobacterium smegmatis HelY Is an RNA-Activated ATPase/dATPase and 3'-to-5' Helicase That Unwinds 3'-Tailed RNA Duplexes and RNA:DNA Hybrids.Immature large ribosomal subunits containing the 7S pre-rRNA can engage in translation in Saccharomyces cerevisiae Transcriptome-wide analysis of alternative routes for RNA substrates into the exosome complex Nuclear RNA surveillance: role of TRAMP in controlling exosome specificity.Superfamily 2 helicases Molecular basis for cytoplasmic RNA surveillance by uridylation-triggered decay in Drosophila.Attacked from All Sides: RNA Decay in Antiviral Defense.Targeting RNA for processing or destruction by the eukaryotic RNA exosome and its cofactors.Yeast nuclear RNA processing.Rarely at rest: RNA helicases and their busy contributions to RNA degradation, regulation and quality control.Exosome substrate targeting: the long and short of it.The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.The conformational plasticity of eukaryotic RNA-dependent ATPases.

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P2860

The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing

http://www.wikidata.org/entity/Q34000158

description

2010 nî lūn-bûn

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2010 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2010 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年学术文章

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2010年学术文章

@zh-cn

2010年学术文章

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2010年学术文章

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2010年学术文章

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2010年學術文章

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name

The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing

@ast

The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing

@en

The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing

@nl

type

label

The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing

@ast

The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing

@en

The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing

@nl

prefLabel

The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing

@ast

The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing

@en

The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing

@nl

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The EMBO Journal

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The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing

@en

P2093

A Alejandra Klauer

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

Ambro van Hoof

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

Howard Robinson

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

P2860

A new yeast poly(A) polymerase complex involved in RNA quality control

AU binding proteins recruit the exosome to degrade ARE-containing mRNAs

Reconstitution, activities, and structure of the eukaryotic RNA exosome

Functions of the exosome in rRNA, snoRNA and snRNA synthesis

Yeast exosome mutants accumulate 3'-extended polyadenylated forms of U4 small nuclear RNA and small nucleolar RNAs

The yeast exosome and human PM-Scl are related complexes of 3' --> 5' exonucleases

The N-terminal PIN domain of the exosome subunit Rrp44 harbors endonuclease activity and tethers Rrp44 to the yeast core exosome

TRAMP complex enhances RNA degradation by the nuclear exosome component Rrp6

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures

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2205-2216

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scholarly article

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10.1038/EMBOJ.2010.107

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13

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29

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Bradley J Hintze

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2010-05-28T00:00:00Z

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44639291

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20512111

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crystal structure

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2905245

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