The guanine nucleotide-exchange factor, eIF-2B.

[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.