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Eukaryotic translation initiation factor 2A, 65kDa

eukaryotic translation initiation factor 2, eukaryotic translation initiation factor 2alpha, eIF2a
EIF2A is a 65-kD protein that catalyzes the formation of puromycin-sensitive 80S preinitiation complexes (Zoll et al., 2002 [PubMed 12133843]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: eIF2alpha, PKR, V1a, CAN, ACID
Papers on eukaryotic translation initiation factor 2
Oxytocin opposes effects of bacterial endotoxin on ER-stress signaling in Caco2BB gut cells.
Welch et al., New York City, United States. In Biochim Biophys Acta, Feb 2016
OT inactivates eukaryotic translation initiation factor 2a (eIF2a) without significant activation of protein kinase RNA-like endoplasmic reticulum kinase (PERK).
Involvement of Endoplasmic Reticulum Stress in Uremic Cardiomyopathy: Protective Effects of Tauroursodeoxycholic Acid.
Gu et al., Shanghai, China. In Cell Physiol Biochem, Feb 2016
ERS markers (GRP78, GRP94, P-PERK, P-eIF2a) and ERS-induced apoptosis pathways (activation of CHOP and caspase-12) were increased significantly in 5/6 nephrectomy mice, and TUDCA treatment blunted these changes.
CCN1/CYR61 overexpression in hepatic stellate cells induces ER stress-related apoptosis.
Weiskirchen et al., Aachen, Germany. In Cell Signal, Jan 2016
The UPR arm PERK and eIF2a was phosphorylated, combined with significant CHOP upregulation.
Unfolded protein response is activated in aged retinas.
Gorbatyuk et al., Birmingham, United States. In Neurosci Lett, Dec 2015
Using western blotting, we determined that the hallmarks of the UPR PERK arm, phosphorylated (p) eIF2a, ATF4, and GADD34, were significantly altered in aged vs. young rat retinas.
Pur-alpha functionally interacts with FUS carrying ALS-associated mutations.
Cestra et al., Roma, Italy. In Cell Death Dis, 2014
We observe that both Pur-alpha and mutated FUS upregulate phosphorylation of the translation initiation factor eukaryotic translation initiation factor 2 alpha and consistently inhibit global protein synthesis.
Experimental Evidence Shows Salubrinal, an eIF2α Dephosphorylation Inhibitor, Reduces Xenotoxicant-Induced Cellular Damage.
Komoike et al., Tokyo, Japan. In Int J Mol Sci, 2014
The substance salubrinal has been shown to prevent dephosphorylation of the eukaryotic translation initiation factor 2 alpha (eIF2α).
EIF2A-dependent translational arrest protects leukemia cells from the energetic stress induced by NAMPT inhibition.
Provenzani et al., Trento, Italy. In Bmc Cancer, 2014
RESULTS: We show that FK866 induces a translational arrest in leukemia cells through inhibition of MTOR/4EBP1 signaling and of the initiation factors EIF4E and EIF2A.
Integrated stress response-altered pro-inflammatory signals in mucosal immune-related cells.
Moon et al., Yangsan, South Korea. In Immunopharmacol Immunotoxicol, 2013
Various cells are associated with the integrated stress response (ISR) that leads to translation arrest via phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2. Pathogenic insults or nutritional imbalance in the mucosal tissues including the intestinal, airway, and genitourinary epithelia can cause ISRs, which have been linked to different mucosal inflammatory responses and subsequent systemic diseases.
Translational control in Plasmodium and toxoplasma parasites.
Nussenzweig et al., New York City, United States. In Eukaryot Cell, 2013
This review focuses on the mechanisms that regulate translational control in Plasmodium and Toxoplasma, with a particular emphasis on the phosphorylation of the α subunit of eukaryotic translation initiation factor 2 (eIF2α).
dsRNA-dependent protein kinase PKR and its role in stress, signaling and HCV infection.
Meurs et al., Paris, France. In Viruses, 2012
As a member of the interferon (IFN)‑Stimulated Genes, PKR was initially recognized as an actor in the antiviral action of IFN, due to its ability to control translation, through phosphorylation, of the alpha subunit of eukaryotic initiation factor 2 (eIF2a).
Selective small molecule activator of the apoptotic arm of the UPR
Kaufman et al., Bethesda, United States. In Unknown Journal, 2012
The progenitor of this probe was identified through a high-throughput screen of the NIH Molecular Libraries Small Molecule Repository (MLSMR) of >350,000 compounds through complementary cell-based reporter assays using stably transfected CHO-K1 cells that specifically identify activators of the PERK/eIF2a/CHOP (apoptotic), but not the IRE1/XBP1 (adaptive) UPR subpathways.
Inhibition of nonsense-mediated RNA decay by the tumor microenvironment promotes tumorigenesis.
Gardner et al., New York City, United States. In Mol Cell Biol, 2011
Data show that the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) translation initiation factor by a variety of cellular stresses leads to the inhibition of NMD and that eIF2alpha phosphorylation and NMD inhibition occur in tumors.
ICP34.5 protein of herpes simplex virus facilitates the initiation of protein translation by bridging eukaryotic initiation factor 2alpha (eIF2alpha) and protein phosphatase 1.
Cao et al., Tianjin, China. In J Biol Chem, 2011
herpes simplex virus protein ICP34.5 bridges PP1 and eIF2alpha via their binding motifs and thereby facilitates the protein synthesis and viral replication.
Investigation of the eIF2alpha phosphorylation mechanism in response to proteasome inhibition in melanoma and breast cancer cells.
DoKudur et al., Kütahya, Turkey. In Mol Biol (mosk), 2010
Investigation of the eIF2alpha phosphorylation mechanism in response to proteasome inhibition in melanoma and breast cancer cells
Suppression of hypoxia-inducible factor 1α (HIF-1α) by tirapazamine is dependent on eIF2α phosphorylation rather than the mTORC1/4E-BP1 pathway.
Yang et al., Hangzhou, China. In Plos One, 2009
Data show that the inhibitory effect of TPZ on HIF-1alpha protein synthesis is dependent on the phosphorylation of translation initiation factor 2alpha (eIF2alpha).
Amino acid availability controls TRB3 transcription in liver through the GCN2/eIF2α/ATF4 pathway.
Bruhat et al., France. In Plos One, 2009
the GCN2/eIF2alpha/ATF4 pathway is essential for the induction of the TRB3 gene transcription
Systems biology approach predicts immunogenicity of the yellow fever vaccine in humans.
Pulendran et al., Atlanta, United States. In Nat Immunol, 2009
Computational analyses identified a gene signature, including complement protein C1qB and eukaryotic translation initiation factor 2 alpha kinase 4-an orchestrator of the integrated stress response-that correlated with and predicted YF-17D CD8(+) T cell responses with up to 90% accuracy in an independent, blinded trial.
A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress.
Yuan et al., Boston, United States. In Science, 2005
In a screen for small molecules that protect cells from endoplasmic reticulum (ER) stress, we identified salubrinal, a selective inhibitor of cellular complexes that dephosphorylate eukaryotic translation initiation factor 2 subunit alpha (eIF2alpha).
EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome.
Julier et al., France. In Nat Genet, 2000
The gene encoding the eukaryotic translation initiation factor 2-alpha kinase 3 (EIF2AK3) resides in this interval; thus we explored it as a candidate.
Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast.
Hinnebusch et al., Bethesda, United States. In Cell, 1992
We show that phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2) by the protein kinase GCN2 mediates translational control of the yeast transcriptional activator GCN4.
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