Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Eukaryotic translation initiation factor-5 (EIF5) interacts with the 40S initiation complex to promote hydrolysis of bound GTP with concomitant joining of the 60S ribosomal subunit to the 40S initiation complex. Additionally we are shipping EIF5 Antibodies (66) and many more products for this protein.
Showing 8 out of 8 products:
The down-regulation of the GCN4 expression (Gcn(-) phenotype) in the eIF5(G31R) mutant was not because of leaky scanning defects; rather was due to the utilization of upUUG initiation codons at the 5' regulatory region present between uORF1 and the main GCN4 ORF.
overexpression of eIF5 and 5MP induces translation of ATF4 (show ATF4 Proteins)
it is eIF5-induced GTP (show AK3 Proteins) hydrolysis and Pi release that irreversibly trap the 48S complex, and this complex is further stabilized by eIF5B (show EIF5B Proteins) and 60S joining.
The N-terminal tail of eIF1A (show EIF1AX Proteins) mediates the interaction with eIF5 and eIF1 (show EIF1 Proteins).
Coordinated movements of eukaryotic translation initiation factors eIF1 (show EIF1 Proteins), eIF1A (show EIF1AX Proteins), and eIF5 trigger phosphate release from eIF2 (show EIF2S1 Proteins) in response to start codon recognition by the ribosomal preinitiation complex
This study provides mechanistic insight into the role of eIF5-carboxyl terminal domain's dynamic interplay with eIF1 and eIF2beta.
miR (show MLXIP Proteins)-5787 represses cell growth, in part, by targeting eIF5.
CK2 (show CSNK2A1 Proteins) may be involved in the regulation of cell cycle progression by associating with and phosphorylating a key molecule for translation initiation.
3-dimensional solution structure of N-terminal domain of human eIF5, has 2 (show HAS2 Proteins) subdomains, both reminiscent of nucleic-acid-binding modules. N-terminal subdomain contains "arginine finger" motif essential for GAP function.
The carboxy-terminal domain (CTD)of eIF5 is exclusively composed out of alpha-helices and is homologous to the carboxy-terminal domain of eIF2B (show EIF2B1 Proteins)-epsilon (eIF2Bepsilon (show EIF2B5 Proteins)-CTD). The binding sites of eIF2-beta, eIF3 (show EIF3A Proteins) and eIF1 (show EIF1 Proteins) were mapped onto the structure.
Eukaryotic translation initiation factor-5 (EIF5) interacts with the 40S initiation complex to promote hydrolysis of bound GTP with concomitant joining of the 60S ribosomal subunit to the 40S initiation complex. The resulting functional 80S ribosomal initiation complex is then active in peptidyl transfer and chain elongations (summary by Si et al., 1996
, eukaryotic initiation factor 5 (eIF-5)
, eukaryotic translation initiation factor 5