Results 131 to 140 of about 15,176 (154)

Association of protein kinase CK2 with eukaryotic translation initiation factor eIF-2 and with grp94/endoplasmin

Molecular and Cellular Biochemistry, 1999
Protein kinase CK2 forms complexes with some protein substrates what may be relevant for the physiological control of this protein kinase. In previous studies in rat liver cytosol we had detected that the trimeric form of eukaryotic translation initiation factor 2 (eIF-2) co-eluted with protein kinase CK2.
M, Riera, N, Roher, F, Miró, C, Gil, R, Trujillo, J, Aguilera, M, Plana, E, Itarte   +7 more
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Frog virus 3-induced translational shut-off: activation of an eIF-2 kinase in virus-infected cells

Virus Research, 1989
Infection of susceptible fathead minnow or Friend erythroleukemia cells with either infectious or heat-inactivated frog virus 3 led to the rapid inhibition of cellular protein synthesis. As seen in other cells, translational shut-off was accompanied by the dissociation of polysomes, but not the degradation of irreversible inactivation of cellular mRNAs.
V G, Chinchar, J N, Dholakia
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Specific phosphorylation of the β subunit of eIF-2 factor from brain by three different protein kinases

Biochemical and Biophysical Research Communications, 1988
The eukaryotic initiation factor 2 (eIF-2) from calf brain has been purified to homogeneity and free of endogenous kinase activity. Phosphorylation of eIF-2 factor has been examined with four different protein kinases. Casein kinase II, calcium/phospholipid-dependent protein kinase and cyclic AMP-dependent protein kinase from brain, phosphorylate the ...
A, Alcazar, E, Mendez, J, L-Fando, M, Salinas   +3 more
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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

Archives 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.
N, Janaki, V M, Krishna, K V, Ramaiah
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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).
J J, Chen, I M, London
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Purification of a novel eIF-2α protein kinase from calf brain

Biochemical and Biophysical Research Communications, 1990
A new eukaryotic initiation factor 2 kinase has been purified for the first time from calf brain cytosol. The purification of a nonabundant novel protein kinase activity, designated as PKI, that phosphorylates the alpha subunit of eukaryotic initiation factor 2 is described.
A, Alcázar, E, Méndez, M E, Martín, M, Salinas   +3 more
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Denatured proteins inhibit translation in hemin-supplemented rabbit reticulocyte lysate by inducing the activation of the heme-regulated eIF-2.alpha. kinase

Biochemistry, 1993
The heme-regulated inhibitor (HRI) of protein synthesis becomes activated in rabbit reticulocyte lysates in response to a variety of conditions including heme-deficiency, addition of oxidants, and heat shock. Activated HRI inhibits translation by catalyzing the phosphorylation of the alpha-subunit of eukaryotic initiation factor eIF-2.
Robert L. Matts, Robin Hurst, Zuoyu Xu
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Interdomain interactions regulate the activation of the heme-regulated eIF2α kinase

Biochimica et Biophysica Acta (BBA) - General Subjects, 2005
The heme-regulated inhibitor of protein synthesis (HRI) regulates translation through the phosphorylation of the alpha-subunit of eukaryotic initiation factor-2 (eIF 2). While HRI is best known for its activation in response to heme-deficiency, we recently showed that the binding of NO and CO to the N-terminal heme-binding domain (NT-HBD) of HRI ...
Bo-Geon, Yun, Jessica A B, Matts, Robert L, Matts   +2 more
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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 ...
M J, Clemens, K G, Laing, I W, Jeffrey, A, Schofield, T V, Sharp, A, Elia, V, Matys, M C, James, V J, Tilleray   +8 more
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Isolation of a translational inhibitor from wheat germ with protein kinase activity that phosphorylates initiation factor eIF-2

Biochemical 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).
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