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Eukaryotic Initiation Factor-4E

Known as: Eukaryotic Peptide Initiation Factor 4E, CDC33 Gene Product, Eukaryotic Initiation Factor-4E [Chemical/Ingredient] 
A peptide initiation factor that binds specifically to the 5' MRNA CAP STRUCTURE of MRNA in the CYTOPLASM. It is a component of the trimeric complex… Expand
National Institutes of Health

Papers overview

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Highly Cited
2007
Highly Cited
2007
Assembly of the eIF4E/eIF4G complex has a central role in the regulation of gene expression at the level of translation… Expand
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Review
2004
Review
2004
The contribution of the mRNA cap-binding protein, eIF-4E, to malignant transformation and progression has been illuminated over… Expand
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Highly Cited
2004
Highly Cited
2004
The mammalian target of rapamycin, mTOR, regulates cell growth and proliferation. Here we show that the initiation factor of… Expand
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Highly Cited
2002
Highly Cited
2002
We show here that the pvr2 locus in pepper, conferring recessive resistance against strains of potato virus Y (PVY), corresponds… Expand
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Highly Cited
2001
Highly Cited
2001
In most instances, translation is regulated at the initiation phase, when a ribosome is recruited to the 5' end of an mRNA. The… Expand
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Highly Cited
1999
Highly Cited
1999
The multisubunit eukaryotic translation initiation factor (eIF) 4F recruits 40S ribosomal subunits to the 5' end of mRNA. The… Expand
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Highly Cited
1999
Highly Cited
1999
Eukaryotic translation initiation factor 4E (eIF4E) binds to the mRNA 5' cap and brings the mRNA into a complex with other… Expand
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Highly Cited
1997
Highly Cited
1997
The proteins eIF-4E BP1 and p70 S6 kinase each undergo an insulin/mitogen-stimulated phosphorylation in situ that is partially… Expand
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Highly Cited
1995
Highly Cited
1995
Eukaryotic translation initiation factor 4E (eIF-4E), which possesses cap-binding activity, functions in the recruitment of mRNA… Expand
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Highly Cited
1992
Highly Cited
1992
Cellular eukaryotic mRNAs (except organellar) contain at the 5' terminus the structure m7(5')Gppp(5')N (where N is any nucleotide… Expand
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