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Validated All-in-One™ qPCR Primer for EIF4G1(NM_001194947.2) Search again
Product ID:
HQP147692
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
EIF-4G1, EIF4F, EIF4G, EIF4GI, P220, PARK18
Gene Description:
eukaryotic translation initiation factor 4 gamma 1
Target Gene Accession:
NM_001194947.2(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
The protein encoded by this gene is a component of the protein complex EIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure, and recruitment of mRNA to the ribosome. Alternative splicing results in five transcript variants encoding four distinct isoforms. [provided by RefSeq].
Gene References into function
- mass spectrometric analysis of N terminus reveals novel isoforms
- demonstrate that the expression of the amino-terminal one-third of eIF4G, which interacts with eIF4E and PABP, in Xenopus oocyte inhibits translation and progesterone-induced maturation
- data suggest that expression of the eIF4GI isoforms is partly controlled by a complex translation strategy involving both cap-dependent and cap-independent mechanisms
- X-ray structure of rotavirus NSP3-C bound to the 30 residue fragment of eIF4G that is also recognized by poly(A) binding protein (PABP)
- Vesicular stomatitis virus infection alters the eIF4F translation initiation complex and causes dephosphorylation of the eIF4E binding protein 4E-BP1
- proteolytic activity of HIV-1 protease on eIF4GI and eIF4GII and its implications for the translation of mRNAs
- Overexpression of EIF4G1 causes aberrant cell morphology and results in disruption of the localization of F-actin and the organization of microtubules.
- cleavage of EIF4G by Coxsackievirus 2A protease enhances the translation efficiency of EV71 IRES activity
- RoXaN is capable of interacting with NSP3 and eIF4G I in vivo and during rotavirus infection. Domains of interaction were mapped.
- Expression of fragments of eIF4GI reveals a nuclear localization sequence within the N-terminal apoptotic cleavage fragment N-FAG.
- eIF4F activation is an essential component of the malignant phenotype in breast carcinoma
- Adenovirus 100K protein blocks cellular protein synthesis by coopting eIF4G and cap-initiation complexes and displacing or blocking binding by Mnk1, which occurs only on preassembled complexes, resulting in dephosphorylation of eIF4E.
- eIF4G binding to Mnk is inhibted by Mnk1 phosphorylation by caspase-activated Pak2/gamma-PAK
- role of binding to adenoviral mRNA in ribosome shunting
- phoshorylation induced by human Cytomegalovirus infections is both mTOR and phosphatidylinositol kinase independent.
- intact eIF4GI protein is not required for the de novo synthesis of eIF4GI, suggesting its expression can continue under stress or infection conditions where eIF4GI is cleaved
- Results identify two conserved basic residues (K646 and R650) in human eukaryotic initiation factor 4GI (eIF4GI) that are important for foot-and-mouth disease virus leader proteinase binding.
- FN has a role in controlling translation through beta1 integrin and eukaryotic initiation factors 4 and 2 coordinated pathways
- The organization of the CBP80-CBP20 complex suggests how the activity of eIF4G in translation initiation could be regulated through a dynamic network of overlapping intra- and intermolecular interactions.
- Citrullinated eIF4G1 was identified as a candidate citrullinated autoantigen in RA patients.
- The X-ray structure of the C-terminal region of human eukaryotic translation initiation factor 4G (eIF4G) has been determined at 2.2 A resolution, revealing two atypical HEAT-repeat domains.
- eIF3e binds to eIF4G during the process of cap-dependent translation initiation
- We quantify the efficiency of eIF4GI promoter usage in mammalian cells and demonstrate that even though the longest isoform eIF4GIf was relatively poorly expressed when reintroduced, it was more efficient at promoting the translation of cellular mRNAs.
- analysis of cells of eIF4GIf molecules lacking either the PABP-binding site, the eIF3-binding site, the middle domain eIF4A-binding site, or the C-terminal segment that includes the second eIF4A-binding site
- Data show that coxsackievirus B3 proteases 2A and 3C induce apoptotic cell death through mitochondrial injury and cleavage of eIF4GI but not DAP5.
- Results show that three genes, namely FXR1, CLAPM1 and EIF4G, are most frequently overexpressed in the center of the amplified domain in squamous cell carcinomas.
- These results demonstrate that "pure" isoprenoids and genistein differentially impact cap-dependent translation in tumor cell lines.
- the PDCD4 MA3 domains compete with the eIF4G MA3 domain and RNA for eIF4A binding. PDCD4 inhibits translation initiation by displacing eIF4G and RNA from eIF4A.
- High levels of eIF4GI observed in many cancers might act to specifically increase proliferation, prevent autophagy, and release tumor cells from control by nutrient sensing.
- A feedforward loop involving c-Myc and eIF4F that serves to link transcription and translation and that could contribute to the effects of c-Myc on cell proliferation and neoplastic growth.
- kinetic analysis of assembly of the m7GpppG.eIF4E.eIF4G complex
- nuclear localization of PABP-C1 not only is dependent on the capacity of rotavirus NSP3 to interact with eIF4G but also requires the interaction of NSP3 with a specific region in RoXaN
- Study reports the topology of the eIF4A/4G/4H helicase complex, which is built from multiple experimentally observed domain-domain contacts.