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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 Proteins (8) and many more products for this protein.
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Human Monoclonal EIF5 Primary Antibody for IF, WB - ABIN968343
Chevesich, Chaudhuri, Maitra: Characterization of mammalian translation initiation factor 5 (eIF-5). Demonstration that eIF-5 is a phosphoprotein and is present in cells as a single molecular form of apparent M(r) 58,000. in The Journal of biological chemistry 1993
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Chicken Polyclonal EIF5 Primary Antibody for WB - ABIN2785396
Olsen, Blagoev, Gnad, Macek, Kumar, Mortensen, Mann: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. in Cell 2006
it is eIF5-induced GTP (show AK3 Antibodies) hydrolysis and Pi release that irreversibly trap the 48S complex, and this complex is further stabilized by eIF5B (show EIF5B Antibodies) and 60S joining.
The N-terminal tail of eIF1A (show EIF1AX Antibodies) mediates the interaction with eIF5 and eIF1 (show EIF1 Antibodies).
Coordinated movements of eukaryotic translation initiation factors eIF1 (show EIF1 Antibodies), eIF1A (show EIF1AX Antibodies), and eIF5 trigger phosphate release from eIF2 (show EIF2S1 Antibodies) 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 Antibodies)-5787 represses cell growth, in part, by targeting eIF5.
CK2 (show CSNK2A1 Antibodies) 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 Antibodies) 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 Antibodies)-epsilon (eIF2Bepsilon (show EIF2B5 Antibodies)-CTD). The binding sites of eIF2-beta, eIF3 (show EIF3A Antibodies) and eIF1 (show EIF1 Antibodies) 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