Results 151 to 160 of about 173,490 (195)
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Isolation of Eukaryotic Initiation Factor 2 from Rat Brain
Journal of Neurochemistry, 1985Abstract: Eukaryotic initiation factor 2 (eIF‐2) was isolated from salt‐washed microsomes of 4‐day‐old rat brain which show a high rate of protein synthesis. A three‐step purification scheme was employed, including heparin‐Sepharose, phosphocellulose, and DEAE‐cellulose column chromatography.
C, Calés, M, Salinas, J L, Fando
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Eukaryotic type translation initiation factor 2: Structure–functional aspects
Biochemistry (Moscow), 2011Translation initiation factor 2 (IF2) is one of key components of the translation initiation system in living cells. In bacteria IF2 is a multidomain monomeric protein, while in eukaryotic and archaean cells e/aIF2 is heterotrimer (αβγ). Data, including our own, on eukaryotic type translation initiation factor 2 (e/aIF2) structure and functioning are ...
E A, Stolboushkina, M B, Garber
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Regulation of eukaryotic initiation factor-2 expression during sepsis
American Journal of Physiology-Endocrinology and Metabolism, 1994Protein synthesis is stimulated at the level of peptide chain initiation in livers from rats with a sterile or septic abscess. In contrast, peptide chain initiation is inhibited in fast-twitch skeletal muscles from septic rats. We investigated the possible mechanisms responsible for these differential changes in peptide chain initiation between liver ...
T C, Vary +3 more
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Phosphorylation inhibits guanine nucleotide exchange on eukaryotic initiation factor 2
Nature, 1982There is extensive evidence that protein synthesis in reticulocyte lysates is inhibited during haem deficiency because of phosphorylation of initiation factor eIF-2 by a protein kinase (the haem-controlled represser, HCR)1–5. Other protein kinases, which are activated by low concentrations of double-stranded RNA, have also been identified in ...
M J, Clemens +3 more
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1987
The available evidence indicates that although the basic steps of peptide chain initiation are similar in all eukaryotic cells, the specific regulatory mechanisms may be different in animal cells and in lower eukaryotic cells. The basic steps are: (1) formation of a ternary complex between eukaryotic peptide chain initiation factor 2 (eIF-2), Met ...
Naba K. Gupta +3 more
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The available evidence indicates that although the basic steps of peptide chain initiation are similar in all eukaryotic cells, the specific regulatory mechanisms may be different in animal cells and in lower eukaryotic cells. The basic steps are: (1) formation of a ternary complex between eukaryotic peptide chain initiation factor 2 (eIF-2), Met ...
Naba K. Gupta +3 more
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Characteristics of the eukaryotic initiation factor 2 associated 67-kDa polypeptide
Biochemistry, 1993A eukaryotic initiation factor 2 (eIF-2) associated 67-kDa polypeptide (p67) protects the eIF-2 alpha-subunit from eIF-2 kinase(s) catalyzed phosphorylation, and this promotes protein synthesis in the presence of active eIF-2 kinase(s), [Datta, B., et al. (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 3324-3328].
Ray, Manas K. +10 more
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Journal of Bone and Mineral Metabolism, 2013
In response to various stresses including viral infection, nutrient deprivation, and stress to the endoplasmic reticulum, eukaryotic translation initiation factor 2 alpha (eIF2α) is phosphorylated to cope with stress induced apoptosis. Although bone cells are sensitive to environmental stresses that alter the phosphorylation level of eIF2α, little is ...
Kazunori, Hamamura +2 more
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In response to various stresses including viral infection, nutrient deprivation, and stress to the endoplasmic reticulum, eukaryotic translation initiation factor 2 alpha (eIF2α) is phosphorylated to cope with stress induced apoptosis. Although bone cells are sensitive to environmental stresses that alter the phosphorylation level of eIF2α, little is ...
Kazunori, Hamamura +2 more
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Biochemical and Biophysical Research Communications, 1979
Abstract Eukaryotic initiation factor 2 (eIF-2), purified to at least 98% homogeneity as judged by polyacrylamide gel electrophoresis in sodium dodecyl sulfate, and containing no detectable amounts of eukaryotic initiation factor 4B (eIF-4B), is active both in the binding of Met-tRNA and in the binding of globin mRNA.
H, Rosen, R, Kaempfer
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Abstract Eukaryotic initiation factor 2 (eIF-2), purified to at least 98% homogeneity as judged by polyacrylamide gel electrophoresis in sodium dodecyl sulfate, and containing no detectable amounts of eukaryotic initiation factor 4B (eIF-4B), is active both in the binding of Met-tRNA and in the binding of globin mRNA.
H, Rosen, R, Kaempfer
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1982
Publisher Summary This chapter discusses a possible mechanism of protein synthesis inhibition by eukaryotic initiation factor-2 (eIF-2) kinases, heme-regulated protein synthesis inhibitor, and double-stranded RNA-activated inhibitor; it discusses the roles of four eIF-2 ancillary protein factors in the complex regulation of protein synthesis ...
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Publisher Summary This chapter discusses a possible mechanism of protein synthesis inhibition by eukaryotic initiation factor-2 (eIF-2) kinases, heme-regulated protein synthesis inhibitor, and double-stranded RNA-activated inhibitor; it discusses the roles of four eIF-2 ancillary protein factors in the complex regulation of protein synthesis ...
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