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eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation
scientific article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
20485439
retrieved
1 December 2016
title
eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation
(English)
1 reference
stated in
PubMed
PubMed ID
20485439
retrieved
1 December 2016
main subject
Translation initiation factor eIF2 subunit alpha YJR007W
1 reference
stated in
GOA release 2020-03-11
Translation initiation factor eIF5 YPR041W
1 reference
stated in
GOA release 2020-03-11
Translation initiation factor eIF2 subunit beta YPL237W
1 reference
stated in
GOA release 2020-03-11
Translation initiation factor eIF2 subunit gamma YER025W
1 reference
stated in
GOA release 2020-03-11
phosphorylation
1 reference
based on heuristic
inferred from title
corrigendum / erratum
Erratum: eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation
0 references
author
Martin D Jennings
object named as
Martin D Jennings
series ordinal
1
0 references
Graham D. Pavitt
object named as
Graham D Pavitt
series ordinal
2
0 references
language of work or name
English
0 references
publication date
20 May 2010
0 references
published in
Nature
1 reference
stated in
PubMed
PubMed ID
20485439
retrieved
1 December 2016
volume
465
0 references
page(s)
378-81
0 references
issue
7296
0 references
cites work
The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
20 March 2017
Multiple roles for the C-terminal domain of eIF5 in translation initiation complex assembly and GTPase activation
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
20 March 2017
Eukaryotic translation initiation factor 5 functions as a GTPase-activating protein
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
20 March 2017
Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
20 March 2017
eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
20 March 2017
Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
20 March 2017
Regulation of translation initiation in eukaryotes: mechanisms and biological targets
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
20 March 2017
Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factors
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
20 March 2017
Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
20 March 2017
GDIs: central regulatory molecules in Rho GTPase activation
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
20 March 2017
Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
7 April 2017
Translational regulation of GCN4 and the general amino acid control of yeast
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
7 April 2017
Dissociation of eIF1 from the 40S ribosomal subunit is a key step in start codon selection in vivo
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
29 September 2017
eIF2alpha phosphorylation bidirectionally regulates the switch from short- to long-term synaptic plasticity and memory
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
29 September 2017
An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
29 September 2017
Crystal structure of the C-terminal domain of S.cerevisiae eIF5.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
29 September 2017
Eukaryotic translation initiation factor 5 is critical for integrity of the scanning preinitiation complex and accurate control of GCN4 translation.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
29 September 2017
Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
29 September 2017
The molecular mechanics of eukaryotic translation
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
29 September 2017
Neutralizing innate host defenses to control viral translation in HSV-1 infected cells
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
29 September 2017
Tight binding of the phosphorylated alpha subunit of initiation factor 2 (eIF2alpha) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
29 September 2017
Eukaryotic translation initiation factor 5 (eIF5) acts as a classical GTPase-activator protein.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
29 September 2017
Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
29 September 2017
Modulation of tRNA(iMet), eIF-2, and eIF-2B expression shows that GCN4 translation is inversely coupled to the level of eIF-2.GTP.Met-tRNA(iMet) ternary complexes
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
29 September 2017
Mutations activating the yeast eIF-2 alpha kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
29 September 2017
Critical contacts between the eukaryotic initiation factor 2B (eIF2B) catalytic domain and both eIF2beta and -2gamma mediate guanine nucleotide exchange.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157
retrieved
2 June 2018
Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2FNATURE09003
retrieved
21 January 2018
Direct binding of translation initiation factor eIF2gamma-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2B epsilon.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2FNATURE09003
retrieved
21 January 2018
Identifiers
DOI
10.1038/NATURE09003
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4417656
Dimensions Publication ID
1025575444
0 references
OpenCitations bibliographic resource ID
4417656
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4417656
PMCID
2875157
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4417656
PubMed ID
20485439
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4417656
ResearchGate publication ID
44614161
0 references
Springer Nature article ID
10.1038/nature09003
0 references
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