Results 181 to 190 of about 291,615 (215)

Isolation of a translational inhibitor from wheat germ with protein kinase activity that phosphorylates initiation factor eIF-2

open access: closedBiochemical and Biophysical Research Communications, 1980
Abstract A translational inhibitor (WGI) has been partially purified from wheat germ extracts. WGI inhibits protein synthesis in rabbit reticulocyte lysates with inhibition kinetics that are similar to those observed in heme-deficiency or by the addition of purified heme-regulated translational inhibitor (HRI).
Rajinder Singh Ranu
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Phosphorylation of Wheat Germ Initiation Factor 2 (eIF-2) byN-Ethylmaleimide-Treated Wheat Germ Lysates and by Purified Casein Kinase II Does Not Affect the Guanine Nucleotide Exchange on eIF-2

open access: closedArchives of Biochemistry and Biophysics, 1995
Phosphorylation of the small subunit of eukaryotic initiation factor-2 (eIF-2 alpha) impairs protein synthesis in mammalian systems. It is not known, however, if a similar regulatory mechanism exists in plants. Previous reports indicate that one of the wheat germ eIF-2 subunits, the p40-41 doublet, is phosphorylated by heterologous eIF-2 alpha kinases.
Janaki Narahari   +2 more
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Activation of the double-stranded RNA-dependent eIF-2 alpha kinase by cellular RNA from 3T3-F442A cells.

European Journal of Biochemistry, 1991
The interferon induced double-stranded-RNA-dependent eIF-2 alpha kinase has an established role in mediating part of interferons anti-viral effects. Several studies have suggested that it may have additional functions in cells not infected with virus ...
J. Li, R. Petryshyn
semanticscholar   +1 more source

Regulation of the interferon-inducible eIF-2α protein kinase by small RNAs

Biochimie, 1994
This review describes the structure and function of the double-stranded RNA-dependent protein kinase (PKR) and its interaction with RNA activators and inhibitors. The abilities of small virally-encoded RNAs such as VAI RNA of adenovirus, the Epstein-Barr virus encoded (EBER) RNAs and the Tat-responsive region RNA of HIV-1 to bind to and regulate PKR ...
Tyson V. Sharp   +8 more
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Regulation of eukaryotic protein synthesis by protein kinases that phosphorylate initiation factor eIF-2: Further evidence for a common mechanism of inhibition of protein synthesis

open access: closedBiochemical and Biophysical Research Communications, 1982
Abstract The role of reversing factor (RF) in the regulation of protein synthesis by inhibitory protein kinases that phosphorylate the 38,000-dalton subunit of initiation factor eIF-2 has been examined. Results show that as with the heme-regulated protein kinase (HRI), RF restores protein synthesis in reticulocyte lysates inhibited by translational ...
Rajinder Singh Ranu
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elF-2 kinases: regulators of general and gene-specific translation initiation

Trends in Biochemical Sciences, 1994
Phosphorylation of eukaryotic initiation factor-2 (eIF-2) is an important mechanism regulating general translation initiation. Two mammalian eIF-2 kinases, the double-stranded-RNA-dependent kinase (PKR) and heme-regulated inhibitor kinase (HRI), have been characterized by sequencing, revealing shared sequence and structural features distinct from other
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Partial purification and characterization of a 90000-dalton peptide involved in activation of the eIF-2.alpha. protein kinase of the hemin-controlled translational repressor

Biochemistry, 1980
In the absence of heme, a negative translational control system is activated in reticulocytes or their lysates that causes the phosphorylation of the smallest subunit of peptide initiation factor 2 and the inhibition of peptide initiation. Two partially purified enzyme fractions are shown to give a concerted effect for phosphorylation of this subunit ...
Boyd Hardesty   +2 more
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Molecular Cloning and Sequencing of the Human Heme-regulated Eukaryotic Initiation Factor 2 Alpha (eIF-2 Alpha) Kinase from Bone Marrow Culture

DNA Sequence, 2002
The cDNA encoding human heme-regulated eukaryotic initiation factor-2 alpha (eIF-2 alpha) kinase was cloned from a human bone marrow culture. Its deduced amino acid sequence comprised of 629 amino acids with a calculated molecular weight of 71,031 Da.
Yi-Guang Chen   +4 more
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Regulation of protein synthesis by heme-regulated eIF-2α kinase

Trends in Biochemical Sciences, 1995
Protein synthesis is regulated by the phosphorylation of the alpha-subunit of eukaryotic initiation factor 2 (eIF-2 alpha) in a variety of cells. At present, there are two distinct mammalian eIF-2 alpha kinases that have been cloned, the double-stranded-RNA-dependent eIF-2 alpha kinase (PKR) and the heme-regulated eIF-2 alpha kinase (HRI).
Irving M. London, Jane-Jane Chen
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Rat Liver pp49, a Protein That Forms Complexes with Protein Kinase CK2, Is Composed of the β and the γ Subunits of Translation Initiation Factor eIF-2

Biochemical and Biophysical Research Communications, 1996
Comparison of the amino acid sequences of two peptides derived from proteolysis of rat liver pp49 identified it as composed of the beta-subunit and the gamma-subunit of eukaryotic initiation factor-2 (eIF-2). Partial purification of rat liver eIF-2 showed that its trimeric form (alpha beta gamma) co-eluted with protein kinase CK2.
Emilio Itarte   +3 more
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