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Human translation initiation factor eIF4G1 possesses a low-affinity ATP binding site facing the ATP-binding cleft of eIF4A in the eIF4G/eIF4A complex
scientific journal article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
25255371
retrieved
4 January 2017
title
Human translation initiation factor eIF4G1 possesses a low-affinity ATP binding site facing the ATP-binding cleft of eIF4A in the eIF4G/eIF4A complex
(English)
1 reference
stated in
PubMed
PubMed ID
25255371
retrieved
4 January 2017
main subject
Eukaryotic translation initiation factor 4 gamma 1
1 reference
stated in
GOA release 2020-03-11
molecular adaptor activity
1 reference
stated in
GOA release 2020-03-11
author name string
Sabine R. Akabayov
series ordinal
1
1 reference
stated in
PubMed
PubMed ID
25255371
retrieved
4 January 2017
Barak Akabayov
series ordinal
2
1 reference
stated in
PubMed
PubMed ID
25255371
retrieved
4 January 2017
Gerhard Wagner
series ordinal
3
1 reference
stated in
PubMed
PubMed ID
25255371
retrieved
4 January 2017
language of work or name
English
0 references
publication date
21 October 2014
1 reference
stated in
PubMed
PubMed ID
25255371
retrieved
4 January 2017
published in
Biochemistry
1 reference
stated in
PubMed
PubMed ID
25255371
retrieved
4 January 2017
volume
53
1 reference
stated in
PubMed
PubMed ID
25255371
retrieved
4 January 2017
page(s)
6422–6425
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stated in
PubMed
PubMed ID
25255371
retrieved
4 January 2017
issue
41
1 reference
stated in
PubMed
PubMed ID
25255371
retrieved
4 January 2017
cites work
Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation
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PubMed Central
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Purification and characterization of a new eukaryotic protein translation factor. Eukaryotic initiation factor 4H
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20 March 2017
Structural basis for the enhancement of eIF4A helicase activity by eIF4G.
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20 March 2017
Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase
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PubMed Central
reference URL
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20 March 2017
Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions
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PubMed Central
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20 March 2017
A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery
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PubMed Central
reference URL
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20 March 2017
Crystal structure of the eIF4A-PDCD4 complex
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PubMed Central
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20 March 2017
Using NMRView to visualize and analyze the NMR spectra of macromolecules
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PubMed Central
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Birth of the D-E-A-D box
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PubMed Central
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7 April 2017
Molecular crowding enhanced ATPase activity of the RNA helicase eIF4A correlates with compaction of its quaternary structure and association with eIF4G.
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PubMed Central
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29 September 2017
Binding of Mn-deoxyribonucleoside triphosphates to the active site of the DNA polymerase of bacteriophage T7
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Backbone resonance assignment of the HEAT1-domain of the human eukaryotic translation initiation factor 4GI.
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mRNA helicases: the tacticians of translational control
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29 September 2017
eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism
1 reference
stated in
PubMed Central
reference URL
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29 September 2017
Direct functional interaction of initiation factor eIF4G with type 1 internal ribosomal entry sites
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PubMed Central
reference URL
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29 September 2017
DNA recognition by the DNA primase of bacteriophage T7: a structure-function study of the zinc-binding domain
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PubMed Central
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29 September 2017
The ATPase cycle mechanism of the DEAD-box rRNA helicase, DbpA
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29 September 2017
Translation initiation: structures, mechanisms and evolution
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PubMed Central
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29 September 2017
ATHENA, ARTEMIS, HEPHAESTUS: data analysis for X-ray absorption spectroscopy using IFEFFIT.
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29 September 2017
Interaction between the NH2-terminal domain of eIF4A and the central domain of eIF4G modulates RNA-stimulated ATPase activity
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PubMed Central
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29 September 2017
The molecular mechanics of eukaryotic translation
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29 September 2017
Mn2+ as a probe of divalent metal ion binding and function in enzymes and other proteins.
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29 September 2017
The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor 4A is required for RNA binding and ATP hydrolysis
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Isomeric equilibria in complexes of adenosine 5'-triphosphate with divalent metal ions. Solution structures of M(ATP)2- complexes
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The ATP-dependent interaction of eukaryotic initiation factors with mRNA.
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29 September 2017
Characterization of eukaryotic initiation factor 4A, a protein involved in ATP-dependent binding of globin mRNA.
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27 November 2018
Coupled folding during translation initiation
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PubMed Central
reference URL
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27 November 2018
The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide
1 reference
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reference URL
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27 November 2018
RNA-stimulated ATPase activity of eukaryotic initiation factors
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/25255371
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1021/BI500600M
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PMCID
4204880
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PubMed ID
25255371
1 reference
stated in
PubMed
PubMed ID
25255371
retrieved
4 January 2017
ResearchGate publication ID
266152679
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