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Eukaryotic translation initiation factor 4H

eIF4H, WSCR1, WBSCR1, heIF4H, eukaryotic translation initiation factor 4H
This gene encodes one of the translation initiation factors, which functions to stimulate the initiation of protein synthesis at the level of mRNA utilization. This gene is deleted in Williams syndrome, a multisystem developmental disorder caused by the deletion of contiguous genes at 7q11.23. Alternative splicing of this gene generates 2 transcript variants. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: eIF4B, CAN, eIF4E, caspase-3, LIMK1
Papers on eIF4H
The pseudorabies virus vhs protein cleaves RNA containing an IRES sequence.
Hsu et al., T'ai-chung-shih, Taiwan. In Febs J, Feb 2016
Moreover, the addition of the translation initiation factors eIF4H and eIF4B significantly increased the RNase activity of recombinant PrV vhs against capped RNA.
Key contribution of eIF4H-mediated translational control in tumor promotion.
Touriol et al., Toulouse, France. In Oncotarget, Dec 2015
Here we show that eIF4H (eukaryotic translation initiation factor 4H), an activator of the RNA helicase eIF4A, is overexpressed in lung carcinomas and predictive of response to chemotherapy.
A ribonucleoprotein complex protects the interleukin-6 mRNA from degradation by distinct herpesviral endonucleases.
Glaunsinger et al., Berkeley, United States. In Plos Pathog, May 2015
After loading onto the IL-6 3' UTR, NCL differentially bound to the translation initiation factor eIF4H.
A Novel Recurrent Breakpoint Responsible for Rearrangements in the Williams-Beuren Region.
Tizzano et al., Barcelona, Spain. In Cytogenet Genome Res, 2014
We found 2 patients with a deletion and 1 patient with a duplication in this region sharing a common breakpoint located between the LIMK1 and EIF4H(WBSCR1) genes.
Identification of the responsible proteins for increased selenium bioavailability in the brain of transgenic rats overexpressing selenoprotein M.
Seong et al., Seoul, South Korea. In Int J Mol Med, 2014
The results revealed that: ⅰ) CMV/hSelM Tg rats showed a high level of enzyme activity for antioxidant protein in the brain cortex compared to non-Tg rats; ⅱ) the high activity of these enzymes induced a decrease in total antioxidant concentration and γ-secretase activity in CMV/hSelM Tg rats; ⅲ) five proteins were upregulated and three were downregulated by SelM overexpression; ⅳ) among the five upregulated proteins, two associated with creatine kinase B-type (B-CK) and E3 ubiquitin-protein ligase RING1 (RING finger protein 1) were further increased in the two groups following Sel treatment, whereas synaptotagmin-15 (SytXV), eukaryotic translation initiation factor 4H (eIF-4H) and lactate dehydrogenase B (LDH-B) were increased or decreased under the same conditions; ⅴ) the three downregulated proteins did not induce a significant change in expression following Sel treatment; and ⅵ) the protein expression level alterations of the two selected spots (B-CK and SytXV) identified by 2-DE were extremely similar to the results from western blot analysis.
Single-molecule kinetics of the eukaryotic initiation factor 4AI upon RNA unwinding.
Meller et al., Boston, United States. In Structure, 2014
Previous studies demonstrated that eIF4AI, in conjunction with eIF4H, bind to loop structures and repetitively unwind RNA hairpins.
Drosha promotes splicing of a pre-microRNA-like alternative exon.
Hastings et al., Lake Forest, United States. In Plos Genet, 2014
We find that Drosha can cleave the alternatively spliced exon 5 of the eIF4H gene into a pre-miRNA both in vitro and in cells.
mRNA decay during herpes simplex virus (HSV) infections: mutations that affect translation of an mRNA influence the sites at which it is cleaved by the HSV virion host shutoff (Vhs) protein.
Read et al., Kansas City, United States. In J Virol, 2013
Vhs binds the translation initiation factors eIF4H, eIF4AI, and eIF4AII, suggesting that its mRNA degradative function is somehow linked to translation.
Eukaryotic Initiation Factor 4H Is under Transcriptional Control of p65/NF-κB.
Quinto et al., Catanzaro, Italy. In Plos One, 2012
We show that the p65 subunit of NF-κB activates the transcription of eIF4H gene, which is the regulatory subunit of eIF4A, the most relevant RNA helicase in translation initiation.
The eukaryotic initiation factor eIF4H facilitates loop-binding, repetitive RNA unwinding by the eIF4A DEAD-box helicase.
Meller et al., Boston, United States. In Nucleic Acids Res, 2012
Single molecule fluorescence resonance energy transfer (sm-FRET) is applied here to directly observe and quantify the helicase activity of eIF4AI in the presence of the ancillary RNA-binding factor eIF4H. Results show that eIF4H can significantly enhance the helicase activity of eIF4AI by strongly binding both to loop structures within the RNA transcript as well as to eIF4AI.
Growth defects and impaired cognitive-behavioral abilities in mice with knockout for Eif4h, a gene located in the mouse homolog of the Williams-Beuren syndrome critical region.
Pannese et al., Milano, Italy. In Am J Pathol, 2012
Eukaryotic translation initiation factor 4h (Eif4h) encodes a protein involved in the process of protein synthesis, at the level of initiation phase.
mRNA helicases: the tacticians of translational control.
Sonenberg et al., Montréal, Canada. In Nat Rev Mol Cell Biol, 2011
Studies indicate that eIF4A (DDX2), together with its accessory proteins eIF4B and eIF4H, is thought to act as a helicase that unwinds secondary structures in the mRNA 5' UTR.
An alternative splicing isoform of eukaryotic initiation factor 4H promotes tumorigenesis in vivo and is a potential therapeutic target for human cancer.
Tomonaga et al., Chiba, Japan. In Int J Cancer, 2011
results suggest that eIF4H isoform 1 plays an important role in carcinogenesis through the activation of oncogenic signaling and could be a promising molecular target for cancer therapy
Uncoupling stress granule assembly and translation initiation inhibition.
Mazroui et al., Québec, Canada. In Mol Biol Cell, 2009
Data show that reduced levels of eIF4B, eIF4H, or polyA-binding protein, also trigger SG formation.
Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation.
Wagner et al., Boston, United States. In Cell, 2009
Study reports the topology of the eIF4A/4G/4H helicase complex, which is built from multiple experimentally observed domain-domain contacts.
Interactions between eIF4AI and its accessory factors eIF4B and eIF4H.
Moore et al., Waltham, United States. In Rna, 2008
The interaction of eIF4AI with two accessory factors, eIF4B and eIF4H, was studied.
Translation initiation factor 4A: a prototype member of dead-box protein family.
Tuteja et al., New Delhi, India. In Physiol Mol Biol Plants, 2008
The biochemical activities of eIF4A are reported to be upregulated by eIF4B, eIF4H and eIF4G.
eIF4A: the godfather of the DEAD box helicases.
Merrick et al., Cleveland, United States. In Prog Nucleic Acid Res Mol Biol, 2001
Also examined is the influence of ancillary protein factors (eIF4B, eIF4G, and eIF4H) on this activity.
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