Results 121 to 130 of about 15,971 (150)

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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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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Purification of Eukaryotic Initiation Factors elF-2, eIF-2B and elF-2a Kinase from Bovine Liver

Preparative Biochemistry, 1993
Eukaryotic initiation factors 2 and 2B (eIF-2; eIF-2B) are components of the rate-limiting step in the initiation of eukaryotic protein synthesis and are involved in the regulation of this process. When the alpha-subunit of eIF-2 is phosphorylated by an eIF-2 alpha kinase, the phosphorylated eIF-2 alpha (eIF-2 alpha(P)) binds tightly to eIF-2B and ...
R C, Feldhoff, A M, Karinch, S R, Kimball, L S, Jefferson   +3 more
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Induction of an antiviral state by interferon in the absence of elevated levels of 2,5-oligo(A) synthetase and eIF-2 kinase

Virology, 1988
A series of clones has been derived from an interferon-resistant murine cell line, Ltk- aprt-, and their antiviral properties have been characterized. In the parental Ltk- aprt- line interferon is unable to establish antiviral properties or to increase the levels of 2,5-oligo(A) synthetase, the 2,5-oligo(A)-activated endonuclease F, 2',5 ...
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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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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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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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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.
R L, Matts, R, Hurst, Z, Xu
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The 90-kilodalton peptide of the heme-regulated eIF-2.alpha. kinase has sequence homology with the 90-kilodalton heat shock protein

Biochemistry, 1987
Highly purified preparations of the heme-controlled eIF-2 alpha (eukaryotic peptide initiation factor 2 alpha subunit) kinase of rabbit reticulocytes contain an abundant 90-kilodalton (kDa) peptide that is immunologically cross-reactive with spectrin and that modulates the activity of the enzyme [Kudlicki, W., Fullilove, S., Read, R., Kramer, G ...
D W, Rose, R E, Wettenhall, W, Kudlicki, G, Kramer, B, Hardesty   +4 more
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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 ...
M H, Wallis, G, Kramer, B, Hardesty
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