Results 1 to 10 of about 291,615 (215)

Translational control by influenza virus: suppression of the kinase that phosphorylates the alpha subunit of initiation factor eIF-2 and selective translation of influenza viral mRNAs. [PDF]

open access: greenMolecular and Cellular Biology, 1986
Selective translation of influenza viral mRNAs occurs after influenza virus superinfection of cells infected with the VAI RNA-negative adenovirus mutant dl331 (M. G. Katze, Y.-T. Chen, and R. M. Krug, Cell 37:483-490, 1984).
Michael G. Katze   +3 more
semanticscholar   +9 more sources

Cloning of the cDNA of the heme-regulated eukaryotic initiation factor 2 alpha (eIF-2 alpha) kinase of rabbit reticulocytes: homology to yeast GCN2 protein kinase and human double-stranded-RNA-dependent eIF-2 alpha kinase. [PDF]

open access: greenProceedings of the National Academy of Sciences, 1991
We have cloned the cDNA of the heme-regulated eIF-2 alpha kinase (HRI) of rabbit reticulocytes. In vitro translation of mRNA transcribed from the HRI cDNA yields a 90-kDa polypeptide that exhibits eIF-2 alpha kinase activity and is recognized by a ...
J J Chen   +6 more
semanticscholar   +4 more sources

Histidyl-tRNA Synthetase-related Sequences in GCN2 Protein Kinase Regulate in Vitro Phosphorylation of eIF-2 [PDF]

open access: hybridJournal of Biological Chemistry, 1996
In yeast, starvation for amino acids stimulates GCN2 phosphorylation of the α subunit of eukaryotic initiation factor-2 (eIF-2). Phosphorylation of eIF-2α induces the translational expression of GCN4, a transcriptional activator of the general amino acid
Shuhao Zhu   +2 more
semanticscholar   +6 more sources

Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI. [PDF]

open access: greenMolecular and Cellular Biology, 1989
The double-stranded RNA (dsRNA)-dependent protein kinase DAI (also termed dsI and P1) possesses two kinase activities; one is an autophosphorylation activity, and the other phosphorylates initiation factor eIF-2. We purified the enzyme, in a latent form, to near homogeneity from interferon-treated human 293 cells.
Matthew J. Kostura, Michael B. Mathews
semanticscholar   +6 more sources

Mechanism of interferon action: autoregulation of RNA-dependent P1/eIF-2 alpha protein kinase (PKR) expression in transfected mammalian cells. [PDF]

open access: bronzeProceedings of the National Academy of Sciences, 1992
The expression of a molecular cDNA clone (P1 KIN) of the human RNA-dependent P1/eIF-2 alpha protein kinase (PKR) was examined in transfected monkey cells and in cell-free protein-synthesizing systems.
Daniel C. Thomis, Charles E. Samuel
semanticscholar   +6 more sources

Casein kinase II mediates multiple phosphorylation of Saccharomyces cerevisiae eIF-2 alpha (encoded by SUI2), which is required for optimal eIF-2 function in S. cerevisiae. [PDF]

open access: greenMolecular and Cellular Biology, 1994
Previous studies have demonstrated that the alpha subunit of eukaryotic initiation factor 2 (eIF-2 alpha), encoded by the SUI2 gene in the yeast Saccharomyces cerevisiae, is phosphorylated at Ser-51 by the GCN2 kinase in response to general amino acid control.
Lan Feng, Haejin Yoon, Thomas F. Donahue
semanticscholar   +5 more sources

Association of a M(r) 90,000 phosphoprotein with protein kinase PKR in cells exhibiting enhanced phosphorylation of translation initiation factor eIF-2 alpha and premature shutoff of protein synthesis after infection with gamma 134.5- mutants of herpes simplex virus 1.

open access: greenProceedings of the National Academy of Sciences of the United States of America, 1995
The protein encoded by the gamma 134.5 gene of herpes simplex virus precludes premature shutoff of protein synthesis in human cells triggered by stress associated with onset of viral DNA synthesis.
J Chou   +3 more
openalex   +2 more sources

Mechanism of interferon action: Phosphorylation of protein synthesis initiation factor eIF-2 in interferon-treated human cells by a ribosome-associated kinase processing site specificity similar to hemin-regulated rabbit reticulocyte kinase

open access: greenProceedings of the National Academy of Sciences of the United States of America, 1979
The phosphorylation of purified protein synthesis factors catalyzed by protein kinase preparations isolated from interferon-treated human amnion cells was examined.
Charles E. Samuel
openalex   +2 more sources

Regulation of protein synthesis in rabbit reticulocyte lysates: Additional initiation factor required for formation of ternary complex (eIF-2·GTP·Met-tRNA f ) and demonstration of inhibitory effect of heme-regulated protein kinase

open access: greenProceedings of the National Academy of Sciences of the United States of America, 1979
Heme deficiency in rabbit reticulocytes and their lysates leads to the activation of a heme-regulated translational inhibitor (HRI) which causes the cessation of polypeptide initiation.
Rajinder Singh Ranu, Irving M. London
openalex   +2 more sources

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