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Translation initiation is mediated by specific recognition of the cap structure by eukaryotic translation initiation factor 4F (eIF4F), which is a cap binding protein complex that consists of three subunits: eIF4A, eIF4E and eIF4G. Additionally we are shipping EIF4G2 Antibodies (116) and EIF4G2 Proteins (4) and many more products for this protein.
DAP5 knockdown from human ESCs (show NR2E3 ELISA Kits) (hESCs) resulted in persistence of pluripotent gene expression, delayed induction of differentiation-associated genes in different cell lineages, and defective embryoid body formation
Data show that microRNA miR (show MLXIP ELISA Kits)-379 potentiated lung cancer (LCa (show CLTA ELISA Kits)) chemosensitivity via modulation of cisplatin (CDDP)-induced apoptosis by directly targeting the eukaryotic translation initiation factor 4 gamma 2 (EIF4G2) 3' UTR (show UTS2R ELISA Kits).
These results indicate that miR (show MLXIP ELISA Kits)-139 is capable of inhibiting chondrocyte proliferation and migration, thus being a possible therapeutic target for OA. The mechanism of miR (show MLXIP ELISA Kits)-139 in chondrocytes may be related to its regulation on EIF4G2 and IGF1R (show IGF1R ELISA Kits).
The Coxsackievirus B3 protease 2A-mediated cleavage of DAP5 results in the production of two truncates that exert differential effects on protein translation of the IRES-containing genes, leading to enhanced host cell death.
Knockdown of EIF4G2 recapitulated the effects of mir (show MLXIP ELISA Kits)-139, whereas restoring EIF4G2 expression rescued the mir (show MLXIP ELISA Kits)-139 phenotype. elevated miR (show MLXIP ELISA Kits)-139-5p expression is associated with a favorable outcome in acute myeloid leukemia (show BCL11A ELISA Kits).
findings provide the first mechanistic insights into the function of DAP5 as a selective regulator of cap-independent translation
Our results provide evidence that the tumor suppressor effect of miR-520c-3p is mediated through repression of translation while inducing senescence and that eIF4GII is a key effector of this anti-tumor activity.
DAP5, a translation initiation factor shown to positively regulate the translation of various internal ribosome entry sites containing mRNAs, promotes internal ribosome entry site-driven translation of p53 (show TP53 ELISA Kits) mRNA.
DAP5/p97 and DAP5/p86 enhanced the translation of the anti-apoptotic protein Bcl-2 (show BCL2 ELISA Kits) and inhibited cisplatin-induced apoptosis
Multiple isoforms of eIF4GII arise from multiple promoters & alternative splicing events. A non-canonical CUG initiation codon extends the eIF4GII N-terminus. The eIF4GII N-terminus plays an alternative role in initiation factor assembly.
analysis of the tandem MA-3 (show PDCD6 ELISA Kits) region of Pdcd4 (show PDCD4 ELISA Kits) protein and characterization of its interactions with eIF4A (show EIF4A1 ELISA Kits) and eIF4G (show EIF4G1 ELISA Kits)
Translation initiation is mediated by specific recognition of the cap structure by eukaryotic translation initiation factor 4F (eIF4F), which is a cap binding protein complex that consists of three subunits: eIF4A, eIF4E and eIF4G. The protein encoded by this gene shares similarity with the C-terminal region of eIF4G that contains the binding sites for eIF4A and eIF3\; eIF4G, in addition, contains a binding site for eIF4E at the N-terminus. Unlike eIF4G, which supports cap-dependent and independent translation, this gene product functions as a general repressor of translation by forming translationally inactive complexes. In vitro and in vivo studies indicate that translation of this mRNA initiates exclusively at a non-AUG (GUG) codon. Alternatively spliced transcript variants encoding different isoforms of this gene have been described.
eukaryotic translation initiation factor 4 gamma, 2
, eukaryotic translation initiation factor 4 gamma 2
, Eukaryotic translation initiation factor 4 gamma 2
, aging-associated protein 1
, death-associated protein 5
, eIF-4-gamma 2
, eIF-4G 2
, eIF4G 2
, eukaryotic translation initiation factor 4G-like 1
, eIF4G-related protein NAT1
, novel APOBEC-1 target 1
, translation repressor NAT1
, translation repressor Nat1