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591 related items for PubMed ID: 8099443

  • 1. Mammalian eukaryotic initiation factor 2 alpha kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast.
    Dever TE, Chen JJ, Barber GN, Cigan AM, Feng L, Donahue TF, London IM, Katze MG, Hinnebusch AG.
    Proc Natl Acad Sci U S A; 1993 May 15; 90(10):4616-20. PubMed ID: 8099443
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  • 2. A protein complex of translational regulators of GCN4 mRNA is the guanine nucleotide-exchange factor for translation initiation factor 2 in yeast.
    Cigan AM, Bushman JL, Boal TR, Hinnebusch AG.
    Proc Natl Acad Sci U S A; 1993 Jun 01; 90(11):5350-4. PubMed ID: 8506384
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  • 3. Mutations in the GCD7 subunit of yeast guanine nucleotide exchange factor eIF-2B overcome the inhibitory effects of phosphorylated eIF-2 on translation initiation.
    Vazquez de Aldana CR, Hinnebusch AG.
    Mol Cell Biol; 1994 May 01; 14(5):3208-22. PubMed ID: 8164676
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  • 4. Evidence that GCD6 and GCD7, translational regulators of GCN4, are subunits of the guanine nucleotide exchange factor for eIF-2 in Saccharomyces cerevisiae.
    Bushman JL, Asuru AI, Matts RL, Hinnebusch AG.
    Mol Cell Biol; 1993 Mar 01; 13(3):1920-32. PubMed ID: 8441423
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  • 5. Gene-specific translational control of the yeast GCN4 gene by phosphorylation of eukaryotic initiation factor 2.
    Hinnebusch AG.
    Mol Microbiol; 1993 Oct 01; 10(2):215-23. PubMed ID: 7934812
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  • 6. GCN1, a translational activator of GCN4 in Saccharomyces cerevisiae, is required for phosphorylation of eukaryotic translation initiation factor 2 by protein kinase GCN2.
    Marton MJ, Crouch D, Hinnebusch AG.
    Mol Cell Biol; 1993 Jun 01; 13(6):3541-56. PubMed ID: 8497269
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  • 7. Mutations activating the yeast eIF-2 alpha kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases.
    Ramirez M, Wek RC, Vazquez de Aldana CR, Jackson BM, Freeman B, Hinnebusch AG.
    Mol Cell Biol; 1992 Dec 01; 12(12):5801-15. PubMed ID: 1448107
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  • 8. Translation of the yeast transcriptional activator GCN4 is stimulated by purine limitation: implications for activation of the protein kinase GCN2.
    Rolfes RJ, Hinnebusch AG.
    Mol Cell Biol; 1993 Aug 01; 13(8):5099-111. PubMed ID: 8336737
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  • 9. Multicopy tRNA genes functionally suppress mutations in yeast eIF-2 alpha kinase GCN2: evidence for separate pathways coupling GCN4 expression to unchanged tRNA.
    Vazquez de Aldana CR, Wek RC, Segundo PS, Truesdell AG, Hinnebusch AG.
    Mol Cell Biol; 1994 Dec 01; 14(12):7920-32. PubMed ID: 7969132
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  • 10. Modulation of tRNA(iMet), eIF-2, and eIF-2B expression shows that GCN4 translation is inversely coupled to the level of eIF-2.GTP.Met-tRNA(iMet) ternary complexes.
    Dever TE, Yang W, Aström S, Byström AS, Hinnebusch AG.
    Mol Cell Biol; 1995 Nov 01; 15(11):6351-63. PubMed ID: 7565788
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  • 11. The highly acidic C-terminal region of the yeast initiation factor subunit 2 alpha (eIF-2 alpha) contains casein kinase phosphorylation sites and is essential for maintaining normal regulation of GCN4.
    van den Heuvel J, Lang V, Richter G, Price N, Peacock L, Proud C, McCarthy JE.
    Biochim Biophys Acta; 1995 Apr 26; 1261(3):337-48. PubMed ID: 7742363
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  • 12. Mutations in the structural genes for eukaryotic initiation factors 2 alpha and 2 beta of Saccharomyces cerevisiae disrupt translational control of GCN4 mRNA.
    Williams NP, Hinnebusch AG, Donahue TF.
    Proc Natl Acad Sci U S A; 1989 Oct 26; 86(19):7515-9. PubMed ID: 2678106
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  • 15. Complex formation by positive and negative translational regulators of GCN4.
    Cigan AM, Foiani M, Hannig EM, Hinnebusch AG.
    Mol Cell Biol; 1991 Jun 26; 11(6):3217-28. PubMed ID: 2038327
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  • 18. Truncated protein phosphatase GLC7 restores translational activation of GCN4 expression in yeast mutants defective for the eIF-2 alpha kinase GCN2.
    Wek RC, Cannon JF, Dever TE, Hinnebusch AG.
    Mol Cell Biol; 1992 Dec 26; 12(12):5700-10. PubMed ID: 1333044
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  • 20. GCD10, a translational repressor of GCN4, is the RNA-binding subunit of eukaryotic translation initiation factor-3.
    Garcia-Barrio MT, Naranda T, Vazquez de Aldana CR, Cuesta R, Hinnebusch AG, Hershey JW, Tamame M.
    Genes Dev; 1995 Jul 15; 9(14):1781-96. PubMed ID: 7542616
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