Results 111 to 120 of about 16,001 (150)

The PERK inhibitor GSK2606414 evokes developmental defects in zebrafish consistent with Wolcott-Rallison syndrome phenotypes. [PDF]

Pharmacol Rep
Almeida LM, Lima LP, Oliveira NAS, Silva RFO, Sousa B, Bessa J, Pinho BR, Oliveira JMA.   +7 more
europepmc   +1 more source

Structural Transformation of a BRAF Inhibitor into a Selective PKR Inhibitor. [PDF]

J Med Chem
Yin J, Srivastava S, Tang X, Galbraith C, Uchenunu O, Miller J, Liu Y, Crescenzi I, Kiyota T, Kurinov I, Costa-Mattioli M, Laufer R, Aman A, Rottapel R, Ramnauth J, Haakonsen DL, Uehling DE, Sicheri F.   +17 more
europepmc   +1 more source

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A ribosomal protein mediates eIF-2 phosphorylation by interferon-induced kinase

Nature, 1980
We have previously reported that treatment of mouse L cells with interferon (IFN) induces a reduction of initiation factor (eIF-2) activity (ternary complex formation of eIF-2 with Met-tRNAf and GTP)1, and that the reduction of eIF-2 activity involves the phosphorylation of eIF-2 by an IFN-induced protein kinase2.
Masataka Nakamura, Samuel Baron, K Ohtsuki   +2 more
exaly   +3 more sources

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 ...
Matilde Salinas, Enrique Méndez
exaly   +3 more sources

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).
Jane-Jane Chen, I M London, Irving M London   +2 more
exaly   +3 more sources

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.
M Elena Martin, Matilde Salinas, Enrique Méndez   +2 more
exaly   +3 more sources

Tissue distribution and immunoreactivity of heme-regulated eIF-2.alpha. kinase determined by monoclonal antibodies

Biochemistry, 1991
A highly purified preparation of heme-regulated inhibitor (HRI), an eIF-2 alpha kinase, from rabbit reticulocyte lysates has been used for generating monoclonal antibodies (mAB). Two hybridoma clones secreting HRI-specific antibodies (mAB A and mAB F) were obtained.
J K, Pal, J J, Chen, I M, London
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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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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
openaire   +2 more sources