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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Eukaryotic translation initiation factor 4E family member 3

EIF4E3 belongs to the EIF4E family of translational initiation factors that interact with the 5-prime cap structure of mRNA and recruit mRNA to the ribosome (Joshi et al., 2004 [PubMed 15153109]).[supplied by OMIM, Mar 2008] (from NCBI)
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Top mentioned proteins: eIF4E, CAN, 4EHP, V1a, FOXP1
Papers on eIF4E3
Transcriptome analysis reveals the molecular mechanisms underlying growth superiority in a novel grouper hybrid (Epinephelus fuscogutatus♀ × E. lanceolatus♂).
Zhang et al., Guangzhou, China. In Bmc Genet, Dec 2015
Meanwhile, expressions of genes related to the protein and glycogen synthesis pathway, such as PI3KC, PI3KR, Raptor, EIF4E3, and PP1 were up-regulated, while PYG expression was down-regulated.
The unique Leishmania EIF4E4 N-terminus is a target for multiple phosphorylation events and participates in critical interactions required for translation initiation.
Papadopoulou et al., Recife, Brazil. In Rna Biol, Dec 2015
In trypanosomatids, 2 eIF4E homologues (EIF4E3 and EIF4E4) have been shown to be part of eIF4F-like complexes with presumed roles in translation initiation.
Delineation of the 3p14.1p13 microdeletion associated with syndromic distal limb contractures.
Thauvin-Robinet et al., Dijon, France. In Am J Med Genet A, 2014
This region contained one gene, EIF4E3, the first three exons of the FOXP1 gene, and an intronic enhancer of FOXP1 named hs1149.
Polysomes of Trypanosoma brucei: Association with Initiation Factors and RNA-Binding Proteins.
Clayton et al., Heidelberg, Germany. In Plos One, 2014
Results suggested that cap-binding proteins EIF4E3 and EIF4E4 were associated with both free and membrane-bound polysomes.
Loss-of-function analysis reveals distinct requirements of the translation initiation factors eIF4E, eIF4E-3, eIF4G and eIF4G2 in Drosophila spermatogenesis.
Lasko et al., Montréal, Canada. In Plos One, 2014
Testes-specific translation initiation factors eIF4E-3 and eIF4G2 are essential specifically for male fertility.
Two related trypanosomatid eIF4G homologues have functional differences compatible with distinct roles during translation initiation.
de Melo Neto et al., Recife, Brazil. In Rna Biol, 2014
In higher eukaryotes, eIF4A, eIF4E and eIF4G homologues interact to enable mRNA recruitment to the ribosome.
Involvement of microRNAs in the regulation of muscle wasting during catabolic conditions.
Sandri et al., Coimbra, Portugal. In J Biol Chem, 2014
In silico and in vivo approaches identified transcription factor YY1 and the translational initiator factor eIF4E3 as downstream targets of these miRNAs.
MNKs act as a regulatory switch for eIF4E1 and eIF4E3 driven mRNA translation in DLBCL.
Gartenhaus et al., Baltimore, United States. In Nat Commun, 2013
Here, we interrogate the MNK-eIF4E axis in diffuse large B-cell lymphoma (DLBCL) and show a distinct distribution of MNK1 and MNK2 in germinal centre B-cell (GCB) and activated B-cell (ABC) DLBCL.
The eIF4E subunits of two distinct trypanosomatid eIF4F complexes are subjected to differential post-translational modifications associated to distinct growth phases in culture.
de Melo Neto et al., Recife, Brazil. In Mol Biochem Parasitol, 2013
In trypanosomatids, various eIF4E and eIF4G homologues were identified, with two eIF4F-like complexes confirmed (EIF4E4/EIF4G3/EIF4AI and EIF4E3/EIF4G4/EIF4AI).
Hypoxia-inducible factor-1α (HIF-1α) promotes cap-dependent translation of selective mRNAs through up-regulating initiation factor eIF4E1 in breast cancer cells under hypoxia conditions.
Wagner et al., Boston, United States. In J Biol Chem, 2013
The eIF4E translation initiation factors, eIF4E1, eIF4E2, and eIF4E3, are essential for translation initiation.
eIF4E3 acts as a tumor suppressor by utilizing an atypical mode of methyl-7-guanosine cap recognition.
Borden et al., Montréal, Canada. In Proc Natl Acad Sci U S A, 2013
We demonstrate that eIF4E3 relies on this cap-binding activity to act as a tumor suppressor, competing with the growth-promoting functions of eIF4E.
Eukaryotic initiation factor 4E-3 is essential for meiotic chromosome segregation, cytokinesis and male fertility in Drosophila.
Lasko et al., Montréal, Canada. In Development, 2012
Here, we report that Drosophila eIF4E-3 is required specifically during spermatogenesis.
Genetic alterations in oral squamous cell carcinoma progression detected by combining array-based comparative genomic hybridization and multiplex ligation-dependent probe amplification.
Cha et al., Pusan, South Korea. In Oral Surg Oral Med Oral Pathol Oral Radiol Endod, 2011
RESULTS: The highest amplification frequencies (100%, 7/7) were detected in FAM5B, TIPARP, PIK3CA, NLGN1, FGF10, HDAC9, GRM3, DDEF1, EDNRB, CHRDL1, and HTR2C, and the highest deletion frequencies in THRAP3, CTTNBP2NL, GATAD2B, REL, CKAP2L, RHOA, EIF4E3, PDLIM5, FBXO3, NEUROD4, and ABCA5 in the OSCC.
A 785kb deletion of 3p14.1p13, including the FOXP1 gene, associated with speech delay, contractures, hypertonia and blepharophimosis.
Rimoin et al., Los Angeles, United States. In Eur J Med Genet, 2009
region including the genes FOXP1, EIF4E3, PROK2, GPR27 resulting in speech delay, contractures, hypertonia and blepharophimosis.
Evolutionary origin and phylogenetic analysis of the novel oocyte-specific eukaryotic translation initiation factor 4E in Tetrapoda.
Marín de Evsikova et al., Bar Harbor, United States. In Dev Genes Evol, 2009
Unlike other known proteins of three subfamilies comprising eIF4E family (eIF4E1, eIF4E2, and eIF4E3), cDNA library evidence suggests that Eif41b locus has an oocyte-restricted expression across all classes of Tetrapoda.
A new paradigm for translational control: inhibition via 5'-3' mRNA tethering by Bicoid and the eIF4E cognate 4EHP.
Sonenberg et al., Montréal, Canada. In Cell, 2005
d4EHP, an eIF4E-related cap binding protein, interacts with Bcd to suppress cad translation, and this cap-dependent translational control defines a new paradigm for translational inhibition involving tethering of the mRNA 5' and 3' ends.
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