The eIF-2 alpha protein kinases, regulators of translation in eukaryotes from yeasts to humans.
Charles E. Samuel
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Inhibition of protein synthesis in rabbit reticulocyte lysates occurs in response to a variety of conditions including heme deficiency, addition of oxidants, and heat stress. The inhibition of translation is due to the activation of a heme-regulated protein kinase (HRI) which specifically phosphorylates the alpha-subunit of the eukaryotic initiation ...
Robert L. Matts +3 more
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Casein kinase II mediates multiple phosphorylation of Saccharomyces cerevisiae eIF-2 alpha (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.
Lan Feng, Haejin Yoon, Thomas F. Donahue
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The kinetics of phosphorylation of eukaryotic initiation factor 2 (eIF-2) by two cyclic nucleotide-independent protein kinases from rabbit reticulocytes have been studied. The hemin-controlled repressor (HCR) and casein kinase II phosphorylate the alpha and beta subunits of eIF-2, respectively.
Mary Isabel Gonzatti, Jolinda A. Traugh
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Neonatal growth is characterized by a high protein synthesis rate that is largely due to an enhanced sensitivity to the postprandial rise in insulin and amino acids, especially leucine. The mechanism of leucine's action in vivo is not well understood. In
Suryawan Agus +3 more
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Previous studies indicated that bone marrow mesenchymal stem cells (BM-MSCs) from patients with systemic lupus erythematosus (SLE) exhibited the phenomenon of apoptosis.
Genkai Guo +6 more
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Phospholipid‐sensitive Ca2+‐dependent protein kinase phosphorylates the β subunit of eukaryotic initiation factor 2 (eIF‐2) [PDF]
The ability of homogeneous phospholipid‐sensitive Ca2+‐dependent protein kinase (PL‐Ca‐PK) from pig spleen to phosphorylate eukaryotic initiation factor 2 (eIF‐2) was examined. PL‐Ca‐PK phosphorylated the β‐subunit of eIF‐2, whereas myosin light chain kinase (MLCK) and cyclic AMP‐ and cyclic GMP‐dependent protein kinases (cA‐PK and cG‐PK) did not.
Schatzman, Randall C. +3 more
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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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Application of the Mass Spectrometry-High-Throughput Technique Over the Immunohistochemical Analysis for Human Brain Tumor Diagnosis and Prognosis: Insights Into Biomarkers' Identification for the Case Study of Grade IV Astrocytomas and Meningiomas. [PDF]
ABSTRACT Human brain tumors were commonly monitored in hospital/clinical laboratories by immunohistochemistry (IHC) technique, which provides major insights into their classification. However, this technique remains laborious and still shows pitfalls. Therefore, the current study was endeavored to reveal the assets of the application of high‐throughput
Louati K +16 more
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