Obesity and insulin resistance are independent risk factors for metabolic syndrome, diabetes, and cardiovascular disease. Adipose tissue samples from nonobese (NO), insulin-sensitive obese (ISO), and insulin-resistant obese (IRO) subjects from ...
R. MacLaren +3 more
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Activation of PKR causes amyloid ß-peptide accumulation via de-repression of BACE1 expression.
BACE1 is a key enzyme involved in the production of amyloid ß-peptide (Aß) in Alzheimer's disease (AD) brains. Normally, its expression is constitutively inhibited due to the presence of the 5'untranslated region (5'UTR) in the BACE1 promoter.
Gerard Ill-Raga +14 more
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A major mechanism of regulation of mammalian protein synthesis initiation is accomplished by the phosphorylation of the alpha subunit of eukaryotic initiation factor (eIF) 2. This modification inhibits the activity of another initiation factor, guanine nucleotide exchange factor, preventing conversion of eIF-2.GDP to eIF-2.GTP and hence binding of ...
E A, Olmsted +3 more
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Casein Kinase II Mediates Multiple Phosphorylation of Saccharomyces cerevisiae eIF-2α (Encoded by SUI2), Which Is Required for Optimal eIF-2 Function in S. cerevisiae [PDF]
Previous studies have demonstrated that the alpha subunit of eukaryotic initiation factor 2 (eIF-2 alpha), encoded by the SUI2 gene in the yeast Saccharomyces cerevisiae, is phosphorylated at Ser-51 by the GCN2 kinase in response to general amino acid control.
L, Feng, H, Yoon, T F, Donahue
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Site-specific phosphorylation of the α subunit of eukaryotic initiation factor eIF-2 by the heme-regulated and double-stranded RNA-activated eIF-2α kinases from rabbit reticulocyte lysates [PDF]
The site specificity of phosphorylation of the α subunit of eukaryotic initiation factor 2 (eIF-2α) by the heme-regulated and double-stranded RNA-activated eIF-2α kinases were compared by phosphopeptide mapping. eIF-2α was maximally phosphorylated in vitro with [γ- 32 P]ATP and either crude ...
V, Ernst +3 more
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RNA-dependent protein kinase (PKR) may have a positive regulatory role in controlling tumor growth and progression in hepatocellular carcinoma (HCC). However, the downstream substrates and the molecular mechanism of PKR in the growth and progression of ...
Yusuke Okujima +16 more
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Presence of haemin-controlled eIF-2α kinases in both undifferentiated and differentiating mouse erythroleukaemia cells [PDF]
In rabbit reticulocytes, globin synthesis is regulated by a haemin-controlled translational inhibitor (HCI) which acts by phosphorylating the alpha-subunit of eukaryotic initiation factor 2 (eIF-2). With purified eIF-2 as substrate, haemin-controlled eIF-2 alpha kinases could be partially purified from cultured mouse erythroleukaemia cells (MEL cells),
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Mechanism of interferon action: autoregulation of RNA-dependent P1/eIF-2 alpha protein kinase (PKR) expression in transfected mammalian cells. [PDF]
The expression of a molecular cDNA clone (P1 KIN) of the human RNA-dependent P1/eIF-2 alpha protein kinase (PKR) was examined in transfected monkey cells and in cell-free protein-synthesizing systems. Expression of the wild-type (wt) P1 KIN cDNA, which encodes an active protein kinase, was compared with that of the phosphotransfer catalytic domain II ...
D C, Thomis, C E, Samuel
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To study further the regulation of the heme-regulated eIF-2 alpha kinase (HRI), we have produced functional wild type HRI using the baculovirus expression system. The amount of recombinant HRI protein expressed in insect cells is approximately 10 times higher than levels in reticulocytes. Baculovirus-expressed HRI (BV-HRI) is indistinguishable from HRI
P J, Chefalo +4 more
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Renal ischemia and reperfusion activates the eIF2 alpha kinase PERK
Inhibition of protein synthesis occurs in the post-ischemic reperfused kidney but the molecular mechanism of renal translation arrest is unknown. Several pathways have been identified whereby cell stress inhibits translation initiation via phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF 2 alpha, phospho-form eIF 2 alpha(P)].
Montie, Heather L. +4 more
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