The guanine nucleotide-exchange factor, eIF-2B.
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[1] B. L. Jones,et al. Use of monoclonal antibodies to study the structure and function of eukaryotic protein synthesis initiation factor eIF-2B. , 1994, European journal of biochemistry.
[2] C. Proud,et al. Guanine nucleotide exchange factor for eukaryotic initiation factor-2. Cloning of cDNA for the delta-subunit of rabbit translation initiation factor-2B. , 1994, Biochimica et biophysica acta.
[3] T. Kinzy,et al. Translation initiation factor eIF-2. Cloning and expression of the human cDNA encoding the gamma-subunit. , 1994, The Journal of biological chemistry.
[4] Mark S. Boguski,et al. Proteins regulating Ras and its relatives , 1993, Nature.
[5] P. Cohen,et al. Inactivation of glycogen synthase kinase-3 beta by phosphorylation: new kinase connections in insulin and growth-factor signalling. , 1993, The Biochemical journal.
[6] A. Hinnebusch. Gene‐specific translational control of the yeast GCN4 gene by phosphorylation of eukaryotic initiation factor 2 , 1993, Molecular microbiology.
[7] C. Proud,et al. Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B. , 1993, The Biochemical journal.
[8] A. Hinnebusch,et al. Guanine nucleotide exchange factor for eukaryotic translation initiation factor 2 in Saccharomyces cerevisiae: interactions between the essential subunits GCD2, GCD6, and GCD7 and the regulatory subunit GCN3 , 1993, Molecular and cellular biology.
[9] C. R. Vázquez de Aldana,et al. Mutations in the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2 alpha) that overcome the inhibitory effect of eIF-2 alpha phosphorylation on translation initiation. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[10] A. Hinnebusch,et al. A protein complex of translational regulators of GCN4 mRNA is the guanine nucleotide-exchange factor for translation initiation factor 2 in yeast. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[11] M. Katze,et al. Mammalian eukaryotic initiation factor 2 alpha kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[12] C. Samuel,et al. The eIF-2 alpha protein kinases, regulators of translation in eukaryotes from yeasts to humans. , 1993, The Journal of biological chemistry.
[13] A. Hinnebusch,et al. Evidence that GCD6 and GCD7, translational regulators of GCN4, are subunits of the guanine nucleotide exchange factor for eIF-2 in Saccharomyces cerevisiae , 1993, Molecular and cellular biology.
[14] R. Rhoads. Regulation of eukaryotic protein synthesis by initiation factors. , 1993, The Journal of biological chemistry.
[15] J. Morales,et al. Elongation factor 1 contains two homologous guanine-nucleotide exchange proteins as shown from the molecular cloning of beta and delta subunits. , 1993, Nucleic acids research.
[16] T. Kinzy,et al. GCD11, a negative regulator of GCN4 expression, encodes the gamma subunit of eIF-2 in Saccharomyces cerevisiae , 1993, Molecular and cellular biology.
[17] J. Woodgett,et al. Glycogen synthase kinase-3: functions in oncogenesis and development. , 1992, Biochimica et biophysica acta.
[18] J. Tavaré,et al. Characterization of insulin-stimulated protein serine/threonine kinases in CHO cells expressing human insulin receptors with point and deletion mutations. , 1992, The Biochemical journal.
[19] M. Brostrom,et al. Phosphorylation of eukaryotic initiation factor (eIF) 2 alpha and inhibition of eIF-2B in GH3 pituitary cells by perturbants of early protein processing that induce GRP78. , 1992, The Journal of biological chemistry.
[20] W. Möller,et al. Identification of the sites in the eukaryotic elongation factor 1α involved in the binding of elongation factor 1β and aminoacyl-tRNA , 1992 .
[21] S. Oldfield,et al. Purification, phosphorylation and control of the guanine-nucleotide-exchange factor from rabbit reticulocyte lysates. , 1992, European journal of biochemistry.
[22] A. Chakrabarti,et al. Release and recycling of eukaryotic initiation factor 2 in the formation of an 80 S ribosomal polypeptide chain initiation complex. , 1992, The Journal of biological chemistry.
[23] W. Merrick. Mechanism and regulation of eukaryotic protein synthesis. , 1992, Microbiological reviews.
[24] C. Proud,et al. Regulation of protein synthesis in Swiss 3T3 fibroblasts. Rapid activation of the guanine-nucleotide-exchange factor by insulin and growth factors. , 1992, The Biochemical journal.
[25] M. Rabinovitz. The pleiotypic response to amino acid deprivation is the result of interactions between components of the glycolysis and protein synthesis pathways , 1992, FEBS letters.
[26] A. Hinnebusch,et al. Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast , 1992, Cell.
[27] R. Jagus,et al. Increase in eukaryotic initiation factor 2B activity following fertilization reflects changes in redox potential. , 1991, The Journal of biological chemistry.
[28] J. Labbé,et al. A major substrate of maturation promoting factor identified as elongation factor 1 beta gamma delta in Xenopus laevis. , 1991, The Journal of biological chemistry.
[29] J. Traugh,et al. Phosphorylation of elongation factor 1 (EF-1) and valyl-tRNA synthetase by protein kinase C and stimulation of EF-1 activity. , 1991, The Journal of biological chemistry.
[30] S. Kimball,et al. Inhibition of microsomal calcium sequestration causes an impairment of initiation of protein synthesis in perfused rat liver. , 1991, Biochemical and biophysical research communications.
[31] J. Traugh,et al. Phosphorylation of valyl-tRNA synthetase and elongation factor 1 in response to phorbol esters is associated with stimulation of both activities. , 1991, The Journal of biological chemistry.
[32] A. Hinnebusch,et al. Complex formation by positive and negative translational regulators of GCN4 , 1991, Molecular and cellular biology.
[33] G. Janssen,et al. Mapping the functional domains of the eukaryotic elongation factor 1 beta gamma. , 1991, European journal of biochemistry.
[34] D. Antonetti,et al. Mechanism of inhibition of peptide chain initiation by amino acid deprivation in perfused rat liver. Regulation involving inhibition of eukaryotic initiation factor 2 alpha phosphatase activity. , 1991, The Journal of biological chemistry.
[35] Frank McCormick,et al. The GTPase superfamily: conserved structure and molecular mechanism , 1991, Nature.
[36] Frank McCormick,et al. The GTPase superfamily: a conserved switch for diverse cell functions , 1990, Nature.
[37] Z. Xu,et al. Purification and characterization of sea urchin initiation factor 2. The requirement of guanine nucleotide exchange factor for the release of eukaryotic polypeptide chain initiation factor 2-bound GDP. , 1990, The Journal of biological chemistry.
[38] S. Kimball,et al. Mechanism of the inhibition of protein synthesis by vasopressin in rat liver. , 1990, The Journal of biological chemistry.
[39] H. Suzuki,et al. Chemical modification of pig liver initiation factor eIF-2 with N-ethylmaleimide. Amino acid sequences around the N-ethylmaleimide-reactive sulfhydryl groups and the effect of GDP on the modification. , 1990, Journal of biochemistry.
[40] F. Kelly,et al. Effect of starvation and diabetes on the activity of the eukaryotic initiation factor eIF-2 in rat skeletal muscle. , 1990, Biochimie.
[41] L. Pinna. Casein kinase 2: an 'eminence grise' in cellular regulation? , 1990, Biochimica et biophysica acta.
[42] C. Timmers,et al. Elongation factor 1β of artemia: Localization of functional sites and homology to elongation factor 1δ , 1990 .
[43] T. Kinzy,et al. Affinity labeling of eukaryotic initiation factor 2 and elongation factor 1 alpha beta gamma with GTP analogs. , 1990, Archives of biochemistry and biophysics.
[44] M. Gross,et al. Regulation of eukaryotic initiation factor-2B activity by polyamines and amino acid starvation in rabbit reticulocyte lysate. , 1989, The Journal of biological chemistry.
[45] K. Montine,et al. Serum growth factors cause rapid stimulation of protein synthesis and dephosphorylation of eIF-2 in serum deprived Ehrlich cells. , 1989, Biochimica et biophysica acta.
[46] A. Wahba,et al. Photoaffinity labeling of the rabbit reticulocyte guanine nucleotide exchange factor and eukaryotic initiation factor 2 with 8-azidopurine nucleotides. Identification of GTP- and ATP-binding domains. , 1989, The Journal of biological chemistry.
[47] B. Safer. Nomenclature of initiation, elongation and termination factors for translation in eukaryotes. Recommendations 1988. Nomenclature Committee of the International Union of Biochemistry (NC-IUB). , 1989, European journal of biochemistry.
[48] A. Hinnebusch,et al. Mutations in the structural genes for eukaryotic initiation factors 2 alpha and 2 beta of Saccharomyces cerevisiae disrupt translational control of GCN4 mRNA. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[49] A. Hinnebusch,et al. Amino acid sequence similarity between GCN3 and GCD2, positive and negative translational regulators of GCN4: evidence for antagonism by competition. , 1989, Genetics.
[50] A. Hinnebusch,et al. gcd12 mutations are gcn3-dependent alleles of GCD2, a negative regulator of GCN4 in the general amino acid control of Saccharomyces cerevisiae. , 1989, Genetics.
[51] J. M. Sierra,et al. Phosphorylation and guanine nucleotide exchange on polypeptide chain initiation factor-2 from Artemia embryos. , 1989, Biochimica et biophysica acta.
[52] A. Wahba,et al. Mechanism of the nucleotide exchange reaction in eukaryotic polypeptide chain initiation. Characterization of the guanine nucleotide exchange factor as a GTP-binding protein. , 1989, The Journal of biological chemistry.
[53] C. Proud,et al. Regulation of polypeptide‐chain initiation in rat skeletal muscle Starvation does not alter the activity or phosphorylation state of initiation factor eIF‐2 , 1988, FEBS letters.
[54] A. Hinnebusch,et al. Molecular analysis of GCN3, a translational activator of GCN4: evidence for posttranslational control of GCN3 regulatory function , 1988, Molecular and cellular biology.
[55] S. Kimball,et al. Effect of diabetes on guanine nucleotide exchange factor activity in skeletal muscle and heart. , 1988, Biochemical and biophysical research communications.
[56] K. Struhl,et al. Molecular characterization of GCD1, a yeast gene required for general control of amino acid biosynthesis and cell-cycle initiation. , 1988, Nucleic acids research.
[57] A. Wolfson,et al. Mammalian valyl‐tRNA synthetase forms a complex with the first elongation factor , 1988, FEBS letters.
[58] M. Gross,et al. Regulation of protein synthesis in rabbit reticulocyte lysate. Glucose 6-phosphate is required to maintain the activity of eukaryotic initiation factor (eIF)-2B by a mechanism that is independent of the phosphorylation of eIF-2 alpha. , 1988, The Journal of biological chemistry.
[59] G. Janssen,et al. Phosphorylation of elongation factor 1 beta by an endogenous kinase affects its catalytic nucleotide exchange activity. , 1988, The Journal of biological chemistry.
[60] A. Hinnebusch. Mechanisms of gene regulation in the general control of amino acid biosynthesis in Saccharomyces cerevisiae. , 1988, Microbiological reviews.
[61] R. Panniers,et al. The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2. , 1988, The Journal of biological chemistry.
[62] R. Panniers,et al. The effect of Mg2+ and guanine nucleotide exchange factor on the binding of guanine nucleotides to eukaryotic initiation factor 2. , 1988, The Journal of biological chemistry.
[63] G. Janssen,et al. Kinetic studies on the role of elongation factors 1 beta and 1 gamma in protein synthesis. , 1988, The Journal of biological chemistry.
[64] Manchester Kl. Kinetic constants in the functioning of eIF-2 and eIF-2B. , 1987 .
[65] A. Hinnebusch,et al. Interactions between positive and negative regulators of GCN4 controlling gene expression and entry into the yeast cell cycle. , 1987, Genetics.
[66] J. M. Sierra,et al. Protein synthesis in Drosophila melanogaster embryos. Two mechanisms for guanine nucleotide exchange on eukaryotic initiation factor 2. , 1987, European journal of biochemistry.
[67] K. Montine,et al. Physiological stresses inhibit guanine-nucleotide-exchange factor in Ehrlich cells. , 1987, European journal of biochemistry.
[68] S. Kimball,et al. Purification and characterization of eukaryotic initiation factor 2 and a guanine nucleotide exchange factor from rat liver. , 1987, The Journal of biological chemistry.
[69] J. Pollard,et al. Regulation of polypeptide chain initiation in Chinese hamster ovary cells with a temperature-sensitive leucyl-tRNA synthetase. Changes in phosphorylation of initiation factor eIF-2 and in the activity of the guanine nucleotide exchange factor GEF. , 1987, The Journal of biological chemistry.
[70] C. Proud. Guanine nucleotides, protein phosphorylation and the control of translation , 1986 .
[71] A. De Benedetti,et al. Activation of hemin-regulated initiation factor-2 kinase in heat-shocked HeLa cells. , 1986, The Journal of biological chemistry.
[72] E. Henshaw,et al. Nucleoside diphosphate regulation of overall rates of protein biosynthesis acting at the level of initiation. , 1985, The Journal of biological chemistry.
[73] Y. Hwang,et al. A study of the kinetic mechanism of elongation factor Ts. , 1985, The Journal of biological chemistry.
[74] V. Chau,et al. Kinetics and thermodynamics of the interaction of elongation factor Tu with elongation factor Ts, guanine nucleotides, and aminoacyl-tRNA. , 1985, The Journal of biological chemistry.
[75] J. Hershey,et al. Regulation of initiation factors during translational repression caused by serum depletion. Covalent modification. , 1985, The Journal of biological chemistry.
[76] J. Hershey,et al. Regulation of initiation factors during translational repression caused by serum depletion. Covalent modification. , 1985, The Journal of biological chemistry.
[77] I. London,et al. Distribution of reversing factor in reticulocyte lysates during active protein synthesis and on inhibition by heme deprivation or double-stranded RNA. , 1984, Proceedings of the National Academy of Sciences of the United States of America.
[78] R. Benne,et al. Regulation of protein synthesis in eukaryotes. Mode of action of eRF, an eIF-2-recycling factor from rabbit reticulocytes involved in GDP/GTP exchange. , 1984, European journal of biochemistry.
[79] B. Safer,et al. The association of eIF-2 with Met-tRNAi or eIF-2B alters the specificity of eIF-2 phosphatase. , 1984, The Journal of biological chemistry.
[80] C. Woodley,et al. Studies on the role of eukaryotic nucleotide exchange factor in polypeptide chain initiation. , 1984, The Journal of biological chemistry.
[81] J. Devereux,et al. A comprehensive set of sequence analysis programs for the VAX , 1984, Nucleic Acids Res..
[82] S. Seal,et al. Wheat germ eIF2 and CoeIF2. Resolution and functional characterization in in vitro protein synthesis. , 1983, The Journal of biological chemistry.
[83] R. Panniers,et al. A GDP/GTP exchange factor essential for eukaryotic initiation factor 2 cycling in Ehrlich ascites tumor cells and its regulation by eukaryotic initiation factor 2 phosphorylation. , 1983, The Journal of biological chemistry.
[84] B. Safer. 2B or not 2B: Regulation of the catalytic utilization of elF-2 , 1983, Cell.
[85] T. Hunt,et al. The use of affinity chromatography on 2'5' ADP-sepharose reveals a requirement for NADPH, thioredoxin and thioredoxin reductase for the maintenance of high protein synthesis activity in rabbit reticulocyte lysates. , 1983, European journal of biochemistry.
[86] R. D. De Abreu,et al. High-performance liquid chromatographic assay for identification and quantitation of nucleotides in lymphocytes and malignant lymphoblasts. , 1982, Journal of chromatography.
[87] G. M. Walton,et al. Nucleotide regulation of a eukaryotic protein synthesis initiation complex;. , 1975, Biochimica et biophysica acta.
[88] A. Greenbaum,et al. The distribution of hepatic metabolites and the control of the pathways of carbohydrate metabolism in animals of different dietary and hormonal status. , 1971, Archives of biochemistry and biophysics.
[89] V. M. Pain. Translational control during amino acid starvation. , 1994, Biochimie.
[90] R. Jagus,et al. Proteins that interact with PKR. , 1994, Biochimie.
[91] I. London,et al. Regulation of heme-regulated eIF-2α kinase and its expression in erythroid cells , 1994 .
[92] R. Panniers. Translational control during heat shock. , 1994, Biochimie.
[93] Tyson V. Sharp,et al. Regulation of the interferon-inducible eIF-2α protein kinase by small RNAs , 1994 .
[94] S. Kimball,et al. Mechanisms of translational control in liver and skeletal muscle. , 1994, Biochimie.
[95] C. Proud,et al. Protein phosphorylation in translational control. , 1992, Current topics in cellular regulation.
[96] J. Woodgett,et al. A common denominator linking glycogen metabolism, nuclear oncogenes and development. , 1991, Trends in biochemical sciences.
[97] G. Janssen,et al. Elongation factor 1βγ from Artemia , 1988 .
[98] A. Wahba,et al. Phosphorylation of the guanine nucleotide exchange factor from rabbit reticulocytes regulates its activity in polypeptide chain initiation. , 1988, Proceedings of the National Academy of Sciences of the United States of America.
[99] L. Stryer,et al. G proteins: a family of signal transducers. , 1986, Annual review of cell biology.
[100] J. Ravel,et al. Factors from wheat germ that enhance the activity of eukaryotic initiation factor eIF-2. Isolation and characterization of Co-eIF-2 alpha. , 1983, The Journal of biological chemistry.