Results 21 to 30 of about 15,176 (154)

Regulation of protein synthesis in eukaryotes by the protein kinases that phosphorylate initiation factor eIF‐2 [PDF]

FEBS Letters, 1980
Rajinder Singh Ranu
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Dissociation of the mTOR Protein Interaction Network Following Neuronal Activation Is Altered by Shank3 Mutation. [PDF]

J Neurochem
Neurons encode activity through precise, stimulus‐dependent rearrangements of protein interaction networks, including the mTOR signaling cascade. Using multiplex co‐immunoprecipitation in primary cortical neurons, we show that IGF1, glutamate, and homeostatic up‐ or down‐scaling with Tetrodotoxin (TTX) or Bicuculline (BIC), respectively, each induce ...
Wehle DT, Brown EA, Stamenkovic V, Gniffen B, Harsh FM, Smith SEP.   +5 more
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Purification and characterization of eukaryotic initiation factor (eIF)-2 alpha kinases from Ehrlich ascites tumor cells

Journal of Biological Chemistry, 1993
A major mechanism of regulation of mammalian protein synthesis initiation is accomplished by the phosphorylation of the alpha subunit of eukaryotic initiation factor (eIF) 2. This modification inhibits the activity of another initiation factor, guanine nucleotide exchange factor, preventing conversion of eIF-2.GDP to eIF-2.GTP and hence binding of ...
Elizabeth A. Olmsted‐Davis, Lynn O'Brien, Edgar C. Henshaw, R Panniers   +3 more
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Inhibition of protein synthesis in insect cells by baculovirus-expressed heme-regulated eIF-2 alpha kinase.

Journal of Biological Chemistry, 1994
To study further the regulation of the heme-regulated eIF-2 alpha kinase (HRI), we have produced functional wild type HRI using the baculovirus expression system. The amount of recombinant HRI protein expressed in insect cells is approximately 10 times higher than levels in reticulocytes. Baculovirus-expressed HRI (BV-HRI) is indistinguishable from HRI
Peter J. Chefalo, Jane Yang, Kolluru V.A. Ramaiah, Lee Gehrke, Jinshi Chen   +4 more
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Presence of haemin-controlled eIF-2α kinases in both undifferentiated and differentiating mouse erythroleukaemia cells [PDF]

Biochemical Journal, 1989
In rabbit reticulocytes, globin synthesis is regulated by a haemin-controlled translational inhibitor (HCI) which acts by phosphorylating the alpha-subunit of eukaryotic initiation factor 2 (eIF-2). With purified eIF-2 as substrate, haemin-controlled eIF-2 alpha kinases could be partially purified from cultured mouse erythroleukaemia cells (MEL cells),
Thomas F. Sarre
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Effects of glucose 6-phosphate and hemin on activation of heme-regulated eIF-2 alpha kinase in gel-filtered reticulocyte lysates.

Journal of Biological Chemistry, 1984
In heme-deficient reticulocyte lysates, protein synthesis initiation is inhibited due to the activation of a heme-regulated protein kinase which blocks protein synthesis by the specific phosphorylation of the alpha-sub-unit of eukaryotic initiation factor 2 (eIF-2 alpha).
A.M. Michelson, Vivian Ernst, Daniel H. Levin, Irving M. London   +3 more
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Cloning and characterization of cDNA encoding rat hemin-sensitive initiation factor-2 alpha (eIF-2 alpha) kinase. Evidence for multitissue expression.

Journal of Biological Chemistry, 1994
Reticulocytes contain an eukaryotic initiation factor-2 alpha (eIF-2 alpha) kinase that is negatively regulated by hemin. This protein kinase, which has been termed heme-regulated inhibitor and heme-controlled repressor (HCR), has a strong inhibitory effect on the initiation of protein synthesis and plays an important role in translational control in ...
Xiangyi Gan, Kevin M. Flowers, Scot R. Kimball, Leonard S. Jefferson   +3 more
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Site-specific phosphorylation of the α subunit of eukaryotic initiation factor eIF-2 by the heme-regulated and double-stranded RNA-activated eIF-2α kinases from rabbit reticulocyte lysates [PDF]

Proceedings of the National Academy of Sciences, 1980
The site specificity of phosphorylation of the α subunit of eukaryotic initiation factor 2 (eIF-2α) by the heme-regulated and double-stranded RNA-activated eIF-2α kinases were compared by phosphopeptide mapping. eIF-2α was maximally phosphorylated in vitro with [γ- 32 P]ATP and either crude ...
Vivian Ernst, Daniel H. Levin, Alena Leroux, Irving M. London   +3 more
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Endoplasmic Reticulum Stress Amplifies Cytokine Responses in Astrocytes via a PERK/eIF2α/JAK1 Signaling Axis. [PDF]

Glia
Main Points ER stress amplifies TNF‐α, OSM, and IL‐1β responses in astrocytes. PERK and JAK1 signaling are required for the synergistic interaction between ER stress and inflammatory cytokines. Translational suppression attenuates the synthesis of the negative feedback regulators IκBα and SOCS3.
Lahiri A, Sims SG, Herstine JA, Meyer A, Marshall MJ, Jahan I, Adhicary S, Bradbury AM, Meares GP.   +8 more
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Mechanism of interferon action: autoregulation of RNA-dependent P1/eIF-2 alpha protein kinase (PKR) expression in transfected mammalian cells. [PDF]

Proceedings 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. Expression of the wild-type (wt) P1 KIN cDNA, which encodes an active protein kinase, was compared with that of the phosphotransfer catalytic domain II ...
Daniel C. Thomis, Charles E. Samuel
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