eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation (Q27931061)

Translation initiation factor eIF5 YPR041W

1 reference

Translation initiation factor eIF2 subunit beta YPL237W

1 reference

Translation initiation factor eIF2 subunit gamma YER025W

1 reference

Erratum: eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation

phosphorylation

1 reference

based on heuristic

inferred from title

corrigendum / erratum

0 references

Martin D Jennings

1

0 references

Graham D. Pavitt

object named as

Graham D Pavitt

series ordinal

2

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language of work or name

English

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publication date

20 May 2010

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1 reference

1 December 2016

465

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issue

7296

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page(s)

378-81

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cites work

The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors.

1 reference

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Multiple roles for the C-terminal domain of eIF5 in translation initiation complex assembly and GTPase activation

20 March 2017

1 reference

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Eukaryotic translation initiation factor 5 functions as a GTPase-activating protein

20 March 2017

1 reference

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Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5

20 March 2017

1 reference

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eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange.

20 March 2017

1 reference

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Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2.

20 March 2017

1 reference

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Regulation of translation initiation in eukaryotes: mechanisms and biological targets

20 March 2017

1 reference

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Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factors

20 March 2017

1 reference

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Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis

20 March 2017

1 reference

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GDIs: central regulatory molecules in Rho GTPase activation

20 March 2017

1 reference

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Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method

20 March 2017

1 reference

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Translational regulation of GCN4 and the general amino acid control of yeast

7 April 2017

1 reference

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Dissociation of eIF1 from the 40S ribosomal subunit is a key step in start codon selection in vivo

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157

eIF2alpha phosphorylation bidirectionally regulates the switch from short- to long-term synaptic plasticity and memory

29 September 2017

1 reference

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An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation

29 September 2017

1 reference

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Crystal structure of the C-terminal domain of S.cerevisiae eIF5.

29 September 2017

1 reference

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Eukaryotic translation initiation factor 5 is critical for integrity of the scanning preinitiation complex and accurate control of GCN4 translation.

29 September 2017

1 reference

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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.

29 September 2017

1 reference

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The molecular mechanics of eukaryotic translation

29 September 2017

1 reference

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Neutralizing innate host defenses to control viral translation in HSV-1 infected cells

29 September 2017

1 reference

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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

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157

Eukaryotic translation initiation factor 5 (eIF5) acts as a classical GTPase-activator protein.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157

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.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157

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

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157

Mutations activating the yeast eIF-2 alpha kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157

Critical contacts between the eukaryotic initiation factor 2B (eIF2B) catalytic domain and both eIF2beta and -2gamma mediate guanine nucleotide exchange.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2875157

Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation

2 June 2018

1 reference

Crossref

https://api.crossref.org/works/10.1038%2FNATURE09003

Direct binding of translation initiation factor eIF2gamma-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2B epsilon

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1038%2FNATURE09003

21 January 2018

Identifiers

DOI

10.1038/NATURE09003

1 reference

Dimensions Publication ID

4417656

1025575444

0 references

4417656

1 reference

1 reference

1 reference