Interaction between the NH2-terminal domain of eIF4A and the central domain of eIF4G modulates RNA-stimulated ATPase activity (Q31125745)

29 June 2017

title

Interaction between the NH2-terminal domain of eIF4A and the central domain of eIF4G modulates RNA-stimulated ATPase activity (English)

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29 June 2017

Nadia L Korneeva

1

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29 June 2017

Eric A First

series ordinal

2

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29 June 2017

Clint A Benoit

series ordinal

3

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29 June 2017

Robert E Rhoads

series ordinal

4

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29 June 2017

language of work or name

English

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publication date

4 November 2004

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Journal of Biological Chemistry

29 June 2017

number of pages

10

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based on heuristic

inferred from page(s)

published in

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29 June 2017

volume

280

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29 June 2017

issue

3

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29 June 2017

page(s)

1872-1881

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

29 June 2017

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21 January 2018

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Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry

21 January 2018

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A prokaryotic-like mode of cytoplasmic eukaryotic ribosome binding to the initiation codon during internal translation initiation of hepatitis C and classical swine fever virus RNAs

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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The transformation suppressor Pdcd4 is a novel eukaryotic translation initiation factor 4A binding protein that inhibits translation

21 January 2018

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The Q motif: a newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis

21 January 2018

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Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP

21 January 2018

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Site-directed mutagenesis of motif III in PcrA helicase reveals a role in coupling ATP hydrolysis to strand separation.

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M406168200

1 reference

29 June 2017

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