Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation (Q24309354)

22 June 2017

title

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

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22 June 2017

8

Nahum Sonenberg

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22 June 2017

Assen Marintchev

1

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Monika Oberer

object named as

Monika Oberer

5

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author name string

Katherine A Edmonds

2

1 reference

22 June 2017

Boriana Marintcheva

3

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22 June 2017

Elthea Hendrickson

4

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22 June 2017

Chikako Suzuki

6

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22 June 2017

Barbara Herdy

7

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22 June 2017

Gerhard Wagner

9

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22 June 2017

language of work or name

English

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publication date

1 February 2009

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22 June 2017

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22 June 2017

volume

136

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22 June 2017

issue

3

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22 June 2017

page(s)

447-460

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

22 June 2017

cites work

1 reference

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Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexes

19 March 2017

1 reference

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

19 March 2017

1 reference

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mRNA decay during herpes simplex virus (HSV) infections: protein-protein interactions involving the HSV virion host shutoff protein and translation factors eIF4H and eIF4A.

19 March 2017

1 reference

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A novel function of the MA-3 domains in transformation and translation suppressor Pdcd4 is essential for its binding to eukaryotic translation initiation factor 4A

19 March 2017

1 reference

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Large-scale induced fit recognition of an m(7)GpppG cap analogue by the human nuclear cap-binding complex

19 March 2017

1 reference

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

19 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656774

Purification and characterization of a new eukaryotic protein translation factor. Eukaryotic initiation factor 4H

19 March 2017

1 reference

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Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A

19 March 2017

1 reference

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Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E

19 March 2017

1 reference

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The path of messenger RNA through the ribosome

19 March 2017

1 reference

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A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery

19 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656774

eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation

19 March 2017

1 reference

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

19 March 2017

1 reference

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Dominant negative mutants of mammalian translation initiation factor eIF-4A define a critical role for eIF-4F in cap-dependent and cap-independent initiation of translation

19 March 2017

1 reference

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Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation

7 April 2017

1 reference

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Interactions between eIF4AI and its accessory factors eIF4B and eIF4H

7 April 2017

1 reference

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Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1.

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656774

Structural roles for human translation factor eIF3 in initiation of protein synthesis

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656774

Translation initiation: structures, mechanisms and evolution

27 September 2017

1 reference

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A general framework for development and data analysis of competitive high-throughput screens for small-molecule inhibitors of protein-protein interactions by fluorescence polarization

27 September 2017

1 reference

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Characterization of a novel RNA-binding region of eIF4GI critical for ribosomal scanning

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656774

eIF4A: the godfather of the DEAD box helicases

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656774

Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap-dependent translation, and the C-terminal one-third functions as a modulatory region

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656774

The DEAD box protein eIF4A. 2. A cycle of nucleotide and RNA-dependent conformational changes

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656774

The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide

29 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656774

RNA-stimulated ATPase activity of eukaryotic initiation factors

29 November 2018

1 reference

12 December 2020

NMR methods for studying protein-protein interactions involved in translation initiation

1 reference

12 December 2020

eIF4G and CBP80 share a common origin and similar domain organization: implications for the structure and function of eIF4G

1 reference

12 December 2020

Characterization of the two eIF4A-binding sites on human eIF4G-1

1 reference

12 December 2020

Mutually cooperative binding of eukaryotic translation initiation factor (eIF) 3 and eIF4A to human eIF4G-1

1 reference

Crossref

https://api.crossref.org/works/10.1016%2FJ.CELL.2009.01.014

7 January 2021

inferred from DOI database lookup

Identifiers

DOI

10.1016/J.CELL.2009.01.014

1 reference

OpenCitations bibliographic resource ID

22 June 2017

1778157

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1778157

1 reference