eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism. - Wikidata - wikimedia - TriplyDB

eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism.

eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism.

http://www.wikidata.org/entity/Q34723572

about

DEAD-box helicases as integrators of RNA, nucleotide and protein binding RNA helicase proteins as chaperones and remodelers Coupling between the DEAD-box RNA helicases Ded1p and eIF4A Crystal structure of the human eIF4AIII-CWC22 complex shows how a DEAD-box protein is inhibited by a MIF4G domain Structural and functional analysis of the human spliceosomal DEAD-box helicase Prp28 Investigation of the conserved glutamate immediately following the DEAD box in eukaryotic translation initiation factor 4AI.Yeast eukaryotic initiation factor 4B (eIF4B) enhances complex assembly between eIF4A and eIF4G in vivo Cofactor-dependent specificity of a DEAD-box protein.ATPase activity of the DEAD-box protein Dhh1 controls processing body formation Human translation initiation factor eIF4G1 possesses a low-affinity ATP binding site facing the ATP-binding cleft of eIF4A in the eIF4G/eIF4A complex Quantitative studies of mRNA recruitment to the eukaryotic ribosome A mechanistic overview of translation initiation in eukaryotes Phosphorylation stoichiometries of human eukaryotic initiation factors The mechanism of eukaryotic translation initiation: new insights and challenges RNA helicase A activity is inhibited by oncogenic transcription factor EWS-FLI1.Molecular mechanism of scanning and start codon selection in eukaryotes.Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B Guiding strand passage: DNA-induced movement of the gyrase C-terminal domains defines an early step in the supercoiling cycle Mechanism of cytoplasmic mRNA translation.Potassium ions are required for nucleotide-induced closure of gyrase N-gate The role of the poly(A) binding protein in the assembly of the Cap-binding complex during translation initiation in plants.The DEAD-box helicase eIF4A: paradigm or the odd one out?Roles of helicases in translation initiation: a mechanistic view.Study on the Application of the Combination of TMD Simulation and Umbrella Sampling in PMF Calculation for Molecular Conformational Transitions.Human eIF4E promotes mRNA restructuring by stimulating eIF4A helicase activity Recruitment, Duplex Unwinding and Protein-Mediated Inhibition of the Dead-Box RNA Helicase Dbp2 at Actively Transcribed Chromatin Influence of Secondary-Structure Folding on the Mutually Exclusive Folding Process of GL5/I27 Protein: Evidence from Molecular Dynamics Simulations.Structural and biochemical analyses of the DEAD-box ATPase Sub2 in association with THO or Yra1.Toward a molecular understanding of RNA remodeling by DEAD-box proteins.Helicase-mediated changes in RNA structure at the single-molecule level.The diverse roles of the eIF4A family: you are the company you keep.The conformational plasticity of eukaryotic RNA-dependent ATPases.The molecular choreography of protein synthesis: translational control, regulation, and pathways.Protein cofactor competition regulates the action of a multifunctional RNA helicase in different pathways.Synergistic effects of ATP and RNA binding to human DEAD-box protein DDX1.Molecular dynamics simulation of the allosteric regulation of eIF4A protein from the open to closed state, induced by ATP and RNA substrates DEAD-box RNA helicase domains exhibit a continuum between complete functional independence and high thermodynamic coupling in nucleotide and RNA duplex recognition.Measuring helicase inhibition of the DEAD-box protein Dbp2 by Yra1.eIF4B, eIF4G and RNA regulate eIF4A activity in translation initiation by modulating the eIF4A conformational cycle.eIF4B stimulates eIF4A ATPase and unwinding activities by direct interaction through its 7-repeats region.

P2860

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P2860

eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism.

http://www.wikidata.org/entity/Q34723572

description

2010 nî lūn-bûn

@nan

2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի նոյեմբերին 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

@zh-tw

2010年论文

@wuu

name

eIF4G stimulates the activity ...... ormational guidance mechanism.

@ast

eIF4G stimulates the activity ...... ormational guidance mechanism.

@en

eIF4G stimulates the activity ...... ormational guidance mechanism.

@nl

type

label

eIF4G stimulates the activity ...... ormational guidance mechanism.

@ast

eIF4G stimulates the activity ...... ormational guidance mechanism.

@en

eIF4G stimulates the activity ...... ormational guidance mechanism.

@nl

prefLabel

eIF4G stimulates the activity ...... ormational guidance mechanism.

@ast

eIF4G stimulates the activity ...... ormational guidance mechanism.

@en

eIF4G stimulates the activity ...... ormational guidance mechanism.

@nl

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Nucleic Acids Research

P1476

eIF4G stimulates the activity ...... ormational guidance mechanism.

@en

P2093

Airat Gubaev

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

Dagmar Klostermeier

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

Fabian Kebbel

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

Manuel Hilbert

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

Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation

Structural basis for the enhancement of eIF4A helicase activity by eIF4G.

Crystallographic structure of the amino terminal domain of yeast initiation factor 4A, a representative DEAD-box RNA helicase.

Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A

Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase

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

Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions

The requirement for eukaryotic initiation factor 4A (elF4A) in translation is in direct proportion to the degree of mRNA 5' secondary structure.

Crystal structure of the ATPase domain of translation initiation factor 4A from Saccharomyces cerevisiae--the prototype of the DEAD box protein family

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2260-2270

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scholarly article

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10.1093/NAR/GKQ1127

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P433

6

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39

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2010-11-09T00:00:00Z

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47729269

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21062831

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3064780

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