Results 91 to 100 of about 15,232 (136)
Targeting the UPR with Small Molecules: Emerging Strategies for Immune Regulation. [PDF]
Duan J, Huang D, Fong YW.
europepmc +1 more source
Decoding the anti-inflammatory properties of sesquiterpene coumarins from the active fractions of Ferula assa-foetida through integrated experimental and in silico analyses. [PDF]
Alamri MA +8 more
europepmc +1 more source
eIF3m promotes fowl adenovirus serotype 4 replication via interacting with ORF1B protein. [PDF]
Wang Z +7 more
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A ribosomal protein mediates eIF-2 phosphorylation by interferon-induced kinase
Nature, 1980We 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.
K, Ohtsuki +4 more
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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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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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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 +7 more
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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 +7 more
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Purification of Eukaryotic Initiation Factors elF-2, eIF-2B and elF-2a Kinase from Bovine Liver
Preparative Biochemistry, 1993Eukaryotic 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 +3 more
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Frog virus 3-induced translational shut-off: activation of an eIF-2 kinase in virus-infected cells
Virus Research, 1989Infection 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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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 +3 more
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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 +3 more
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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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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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