Results 11 to 20 of about 291,615 (215)
Erythroid expression of the heme-regulated eIF-2 alpha kinase. [PDF]
Molecular and Cellular Biology, 1994 The role of heme-regulated eIF-2 alpha kinase (HRI) in the regulation of protein synthesis in rabbit reticulocytes is well documented. Inhibitors of protein synthesis with properties similar to those of HRI have been described in some nonerythroid cell types, but it has not yet been determined whether these eIF-2 alpha kinase activities are mediated by
John S. Crosby +3 more
semanticscholar +5 more sources
Journal of Biological Chemistry, 1989 We have reported previously that a 67-kDa polypeptide (p67) present in reticulocyte lysates protects the alpha-subunit of reticulocyte eukaryotic peptide chain initiation factor 2 (eIF-2) from phosphorylation by an eIF-2 kinase, heme-regulated protein synthesis inhibitor (Datta, B., Chakrabarti, D., Roy, A.L., and Gupta, N. K. (1988) Proc. Natl.
B Datta +4 more
semanticscholar +4 more sources
Sensory Denervation Modulates eIF-2 Alpha Kinase Expression in the Rabbit Lacrimal Gland [PDF]
Current Eye Research, 2006 To investigate the hypothesis that sensory denervation of the rabbit lacrimal gland results in dysregulation of protein synthesis. We used differential display of mRNA to identify genes associated with protein synthesis and secretion that may be altered in this situation.New Zealand white rabbits underwent unilateral sensory denervation by the ablation
Doan Nguyen +3 more
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Generation of a mutant form of protein synthesis initiation factor eIF-2 lacking the site of phosphorylation by eIF-2 kinases. [PDF]
Molecular and Cellular Biology, 1988 The phosphorylation of the alpha-subunit of initiation factor eIF-2 leads to an inhibition of protein synthesis in mammalian cells. We have performed site-directed mutagenesis on a cDNA encoding the alpha-subunit of human eIF-2 and have replaced the candidate sites of phosphorylation, Ser-48 and Ser-51, with alanines.
Vinay K. Pathak +2 more
+6 more sources
The eIF-2 alpha protein kinases, regulators of translation in eukaryotes from yeasts to humans.
Journal of Biological Chemistry, 1993 Charles E. Samuel
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Mutations activating the yeast eIF-2 alpha kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases. [PDF]
Molecular and Cellular Biology, 1992 Manuel Ramírez +5 more
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Regulation of eukaryotic protein synthesis by protein kinases that phosphorylate initiation factor eIF-2 [PDF]
Molecular Biology Reports, 1994 Michael J. Clemens
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Journal of Biological Chemistry, 1992 Inhibition of protein synthesis in rabbit reticulocyte lysates occurs in response to a variety of conditions including heme deficiency, addition of oxidants, and heat stress. The inhibition of translation is due to the activation of a heme-regulated protein kinase (HRI) which specifically phosphorylates the alpha-subunit of the eukaryotic initiation ...
Robert L. Matts +3 more
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