Results 21 to 30 of about 15,232 (136)

Influence of obesity and insulin sensitivity on insulin signaling genes in human omental and subcutaneous adipose tissues⃞

open access: yesJournal of Lipid Research, 2008
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
doaj   +1 more source

Activation of PKR causes amyloid ß-peptide accumulation via de-repression of BACE1 expression.

open access: yesPLoS ONE, 2011
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
doaj   +1 more source

Purification and characterization of eukaryotic initiation factor (eIF)-2 alpha kinases from Ehrlich ascites tumor cells

open access: yesJournal of Biological Chemistry, 1993
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
openaire   +2 more sources

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]

open access: yesMolecular and Cellular Biology, 1994
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
openaire   +2 more sources

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]

open access: yesProceedings of the National Academy of Sciences, 1980
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
openaire   +2 more sources

PKR associates with 4.1R to promote anchorage-independent growth of hepatocellular carcinoma and lead to poor prognosis

open access: yesScientific Reports
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
doaj   +1 more source

Presence of haemin-controlled eIF-2α kinases in both undifferentiated and differentiating mouse erythroleukaemia cells [PDF]

open access: yesBiochemical Journal, 1989
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),
openaire   +2 more sources

Mechanism of interferon action: autoregulation of RNA-dependent P1/eIF-2 alpha protein kinase (PKR) expression in transfected mammalian cells. [PDF]

open access: yesProceedings of the National Academy of Sciences, 1992
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
openaire   +2 more sources

Inhibition of protein synthesis in insect cells by baculovirus-expressed heme-regulated eIF-2 alpha kinase.

open access: yesJournal of Biological Chemistry, 1994
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
openaire   +2 more sources

Renal ischemia and reperfusion activates the eIF2 alpha kinase PERK

open access: yesBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 2005
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
openaire   +2 more sources

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