DEAD-box proteins can completely separate an RNA duplex using a single ATP. - Wikidata - wikimedia - TriplyDB

DEAD-box proteins can completely separate an RNA duplex using a single ATP.

DEAD-box proteins can completely separate an RNA duplex using a single ATP.

http://www.wikidata.org/entity/Q37068571

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A motif unique to the human DEAD-box protein DDX3 is important for nucleic acid binding, ATP hydrolysis, RNA/DNA unwinding and HIV-1 replication SF1 and SF2 helicases: family matters RNA helicases at work: binding and rearranging DEAD-box proteins as RNA helicases and chaperones ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding DEAD-box helicases as integrators of RNA, nucleotide and protein binding RNA helicase proteins as chaperones and remodelers Structure of the Yeast DEAD Box Protein Mss116p Reveals Two Wedges that Crimp RNA Structural basis for RNA-duplex recognition and unwinding by the DEAD-box helicase Mss116p High-Throughput Genetic Identification of Functionally Important Regions of the Yeast DEAD-Box Protein Mss116p The DEAD-box protein Dbp2 functions with the RNA-binding protein Yra1 to promote mRNP assembly.Bacterial versatility requires DEAD-box RNA helicases The DEAD-box Protein Rok1 Orchestrates 40S and 60S Ribosome Assembly by Promoting the Release of Rrp5 from Pre-40S Ribosomes to Allow for 60S Maturation Single-molecule studies reveal that DEAD box protein DDX1 promotes oligomerization of HIV-1 Rev on the Rev response element.The regulatory protein RraA modulates RNA-binding and helicase activities of the E. coli RNA degradosome.The RNA helicase DHH1 is central to the correct expression of many developmentally regulated mRNAs in trypanosomes.Phosphate release contributes to the rate-limiting step for unwinding by an RNA helicase.Pathway of ATP utilization and duplex rRNA unwinding by the DEAD-box helicase, DbpA.Structure-guided mutational analysis of a yeast DEAD-box protein involved in mitochondrial RNA splicing.DEAD-box protein CYT-19 is activated by exposed helices in a group I intron RNA.A Co-Opted DEAD-Box RNA helicase enhances tombusvirus plus-strand synthesis.Roles of DEAD-box proteins in RNA and RNP Folding.Targeting the eIF4F translation initiation complex: a critical nexus for cancer development Insights into the mechanism of a G-quadruplex-unwinding DEAH-box helicase.Solution structures of DEAD-box RNA chaperones reveal conformational changes and nucleic acid tethering by a basic tail Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B The Helicase Activity of Ribonuclease R Is Essential for Efficient Nuclease Activity Nucleolar DEAD-Box RNA Helicase TOGR1 Regulates Thermotolerant Growth as a Pre-rRNA Chaperone in Rice.The eukaryotic initiation factor eIF4H facilitates loop-binding, repetitive RNA unwinding by the eIF4A DEAD-box helicase.Unwinding the mechanisms of a DEAD-box RNA helicase in cancer.The DbpA catalytic core unwinds double-helix substrates by directly loading on them A DEAD-box RNA helicase promotes thermodynamic equilibration of kinetically trapped RNA structures in vivo The DEAD-box helicase eIF4A: paradigm or the odd one out?Roles of helicases in translation initiation: a mechanistic view.Superfamily 2 helicases A conformational change in the helicase core is necessary but not sufficient for RNA unwinding by the DEAD box helicase YxiN.Melting of Duplex DNA in the Absence of ATP by the NS3 Helicase Domain through Specific Interaction with a Single-Strand/Double-Strand Junction Powering through ribosome assembly.The mechanism of ATP-dependent RNA unwinding by DEAD box proteins.Insight into helicase mechanism and function revealed through single-molecule approaches.

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DEAD-box proteins can completely separate an RNA duplex using a single ATP.

http://www.wikidata.org/entity/Q37068571

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

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scientific article published on 16 December 2008

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

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name

DEAD-box proteins can completely separate an RNA duplex using a single ATP.

@en

DEAD-box proteins can completely separate an RNA duplex using a single ATP.

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type

label

DEAD-box proteins can completely separate an RNA duplex using a single ATP.

@en

DEAD-box proteins can completely separate an RNA duplex using a single ATP.

@nl

prefLabel

DEAD-box proteins can completely separate an RNA duplex using a single ATP.

@en

DEAD-box proteins can completely separate an RNA duplex using a single ATP.

@nl

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PNAS.0811075106

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Proceedings of the National Academy of Sciences of the United States of America

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DEAD-box proteins can completely separate an RNA duplex using a single ATP.

@en

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Alan M Lambowitz

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

Jeffrey P Potratz

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

Mark Del Campo

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

Pilar Tijerina

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

Rick Russell

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

Yingfeng Chen

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

P2860

The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA

ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding

Structure of the P1 helix from group I self-splicing introns

The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function

ATP- and ADP-dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1.

Involvement of DEAD-box proteins in group I and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chaperone activity

Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA

Strategies for RNA folding and assembly

Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA.

The Escherichia coli DEAD protein DbpA recognizes a small RNA hairpin in 23S rRNA.

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20203-20208

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scholarly article

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10.1073/PNAS.0811075106

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51

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105

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2008-12-16T00:00:00Z

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23669128

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19088196

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2629298

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