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the direct interaction of AKT2 (show AKT2 Proteins) and EF2 was found to be dynamically regulated in embryonic rat cardiomyocytes
These results suggest that binding of eEF2 to the ribosome alters its conformation, resulting in a weakened affinity of eIF5A (show EIF5 Proteins) and impairment of this interplay compromises cell growth due to translation elongation defects.
nuclear localization of active eEF-2 depends upon its interaction with p53 (show TP53 Proteins), as cells lacking p53 (show TP53 Proteins) contain less active eEF-2 in the nuclear compartment
High serum eukaryotic elongation factor 2 level is associated with non-small cell lung cancer.
Results indicated that the eEF2 gene is overexpressed in the majority of several types of cancers and plays an oncogenic role in cancer cell growth.
The expression levels of three putative HA-regulated proteins (TALDO, ANXA1 (show ANXA1 Proteins) and EF2) in control, H2O2-, HA- and HA/H2O2-treated OA chondrocytes were verified by Western blotting and the results indeed support the notion that HA acts in anti-oxidation
Data indicate that the accumulation of the cleaved C-terminal small fragment of eukaryotic elongation factor 2 (eEF2) in the nucleus, and C-terminal Src kinase (Csk (show CSK Proteins)) could enhance the proteolytic cleavage of eEF2.
Thiopental inhibits global protein synthesis by repression of eukaryotic elongation factor 2 and protects from hypoxic neuronal cell death.
A single amino acid substitution in eukaryotic elongation factor 2 co-segregates with the disease phenotype of spinocerebellar ataxia 26.
EEF2 phosphorylation by cyclin A (show CCNA2 Proteins)-cyclin-dependent kinase 2 (CDK2 (show CDK2 Proteins)) on a novel site, serine 595 (S595), directly regulates T56 phosphorylation by eEF2K (show EEF2K Proteins).
Myostatin (show MSTN Proteins) inhibits eEF2K (show EEF2K Proteins)-eEF2 by regulating AMPK (show PRKAA1 Proteins) to suppress protein synthesis.
IL-6 (show IL6 Proteins) induces the activation of the Stat3 (show STAT3 Proteins) signaling and promotes the downmodulation of the p90RSK (show RPS6KA1 Proteins)/eEF2 and mTOR (show FRAP1 Proteins)/p70S6K (show RPS6KB1 Proteins) axes, while it does not affect the activation of AKT (show AKT1 Proteins).
AMPKalpha2 (show PRKAA2 Proteins) controls cardiac p70S6K (show RPS6KB1 Proteins) under normoxia and regulates eEF-2 but not the mTOR (show FRAP1 Proteins)-p70S6K (show RPS6KB1 Proteins) pathway during ischemia.
The MKK3 (show MAP2K3 Proteins)/6-p38gamma (show MAPK12 Proteins)/delta pathway mediated an inhibitory phosphorylation of eukaryotic elongation factor 2 (eEF2) kinase, which in turn promoted eEF2 activation (dephosphorylation) and subsequent TNF-alpha (show TNF Proteins) elongation.
Diphthamide modification on eukaryotic elongation factor 2 is needed to assure fidelity of mRNA translation and mouse development
induced by basic fibroblast growth factor (show FGF2 Proteins) via mitogen-activated protein kinase (show MAPK1 Proteins)
eEF-2 is activated by both lithium and GSK-3, whereas, lithium treatment and inhibition of GSK-3 have opposing effects on eEF-2.
eEF-2 phosphorylation has a role in protein synthesis for memory consolidation
A mouse that was mutant for the gene, Dph4 (show DNAJC24 Proteins), was identified.
Eukaryotic elongation factor-2 (eEF2) may be a limiting factor in milk protein (show CSN2 Proteins) synthesis (Review)
This gene encodes a member of the GTP-binding translation elongation factor family. This protein is an essential factor for protein synthesis. It promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome. This protein is completely inactivated by EF-2 kinase phosporylation.
eukaryotic translation elongation factor 2
, elongation factor 2-like
, elongation factor 2
, polypeptidyl-tRNA translocase
, elongation factor-2