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The percentage at the S-stage was decreased in the miR-379 mimics and EIF4G2 shRNA groups.
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DAP5 knockdown from human ESCs (hESCs) resulted in persistence of pluripotent gene expression, delayed induction of differentiation-associated genes in different cell lineages, and defective embryoid body formation
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Data show that microRNA miR-379 potentiated lung cancer (LCa) chemosensitivity via modulation of cisplatin (CDDP)-induced apoptosis by directly targeting the eukaryotic translation initiation factor 4 gamma 2 (EIF4G2) 3' UTR.
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These results indicate that miR-139 is capable of inhibiting chondrocyte proliferation and migration, thus being a possible therapeutic target for OA. The mechanism of miR-139 in chondrocytes may be related to its regulation on EIF4G2 and IGF1R.
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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.
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Knockdown of EIF4G2 recapitulated the effects of mir-139, whereas restoring EIF4G2 expression rescued the mir-139 phenotype. elevated miR-139-5p expression is associated with a favorable outcome in acute myeloid leukemia.
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findings provide the first mechanistic insights into the function of DAP5 as a selective regulator of cap-independent translation
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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.
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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 mRNA.
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DAP5/p97 and DAP5/p86 enhanced the translation of the anti-apoptotic protein Bcl-2 and inhibited cisplatin-induced apoptosis
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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.
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crystal structure of C-terminal region (residues 540-897) of p97/EIF4G2 (at 2.0 Angstrom resolution): sequence/structure homology with EIF4G1
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crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5 is presented.
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Includes the functional analysis of a similar protein in yeast.
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The caspase-cleaved DAP5 protein supports internal ribosome entry site-mediated translation of death proteins
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proteolytic activity of HIV-1 protease on eIF4GI and eIF4GII and its implications for the translation of mRNAs
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endogenous eIF4GII was phosphorylated by Ca(2+)/calmodulin-dependent protein kinase I
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Cleavage of eIF4GII is induced in cells and in cell extracts by the FMDV leader protease (L(pro)) alone
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EIF4G2 transcripts exhibited three different expression patterns, downregulation was found in about 50% of the cases analyzed and EIF4G2 gene transcription was associated with invasive tumors.
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p97 is functionally different from the closely related C-terminal two-thirds of eIF4GI and it can positively promote protein synthesis and cell proliferation.
