Eukaryotic Initiation Factor-4G
"Eukaryotic Initiation Factor-4G" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A component of eukaryotic initiation factor-4F that is involved in multiple protein interactions at the site of translation initiation. Thus it may serve a role in bringing together various initiation factors at the site of translation initiation.
Descriptor ID |
D039603
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MeSH Number(s) |
D12.776.835.725.868.500.875
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Concept/Terms |
Eukaryotic Initiation Factor-4G- Eukaryotic Initiation Factor-4G
- Eukaryotic Initiation Factor 4G
- EIF4G
- Peptide Initiation Factor EIF-4G
- Peptide Initiation Factor EIF 4G
- Eukaryotic Translation Initiation Factor 4 gamma
- Eukaryotic-Translation Initiation Factor 4G
- Eukaryotic Translation Initiation Factor 4G
- EIF-4G
- EIF 4G
- Eukaryotic Peptide Initiation Factor-4G
- Eukaryotic Peptide Initiation Factor 4G
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Below are MeSH descriptors whose meaning is more general than "Eukaryotic Initiation Factor-4G".
Below are MeSH descriptors whose meaning is more specific than "Eukaryotic Initiation Factor-4G".
This graph shows the total number of publications written about "Eukaryotic Initiation Factor-4G" by people in this website by year, and whether "Eukaryotic Initiation Factor-4G" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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2003 | 1 | 0 | 1 |
2005 | 0 | 1 | 1 |
2007 | 2 | 0 | 2 |
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Below are the most recent publications written about "Eukaryotic Initiation Factor-4G" by people in Profiles.
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Perillyl alcohol and genistein differentially regulate PKB/Akt and 4E-BP1 phosphorylation as well as eIF4E/eIF4G interactions in human tumor cells. Arch Biochem Biophys. 2007 Sep 01; 465(1):266-73.
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Small-molecule inhibition of the interaction between the translation initiation factors eIF4E and eIF4G. Cell. 2007 Jan 26; 128(2):257-67.
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Folding transitions during assembly of the eukaryotic mRNA cap-binding complex. J Mol Biol. 2006 Mar 03; 356(4):982-92.
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Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E. Cell. 2003 Dec 12; 115(6):739-50.