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22. The tRNA-binding moiety in GCN2 contains a dimerization domain that interacts with the kinase domain and is required for tRNA binding and kinase activation. Qiu H, Dong J, Hu C, Francklyn CS, Hinnebusch AG. EMBO J; 2001 Mar 15; 20(6):1425-38. PubMed ID: 11250908 [Abstract] [Full Text] [Related]
26. Translational control by TOR and TAP42 through dephosphorylation of eIF2alpha kinase GCN2. Cherkasova VA, Hinnebusch AG. Genes Dev; 2003 Apr 01; 17(7):859-72. PubMed ID: 12654728 [Abstract] [Full Text] [Related]
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29. Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain. Dong J, Qiu H, Garcia-Barrio M, Anderson J, Hinnebusch AG. Mol Cell; 2000 Aug 02; 6(2):269-79. PubMed ID: 10983975 [Abstract] [Full Text] [Related]
30. IMPACT, a protein preferentially expressed in the mouse brain, binds GCN1 and inhibits GCN2 activation. Pereira CM, Sattlegger E, Jiang HY, Longo BM, Jaqueta CB, Hinnebusch AG, Wek RC, Mello LE, Castilho BA. J Biol Chem; 2005 Aug 05; 280(31):28316-23. PubMed ID: 15937339 [Abstract] [Full Text] [Related]
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32. Defects in tRNA processing and nuclear export induce GCN4 translation independently of phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2. Qiu H, Hu C, Anderson J, Björk GR, Sarkar S, Hopper AK, Hinnebusch AG. Mol Cell Biol; 2000 Apr 05; 20(7):2505-16. PubMed ID: 10713174 [Abstract] [Full Text] [Related]
33. Regulation of translation initiation by amino acids in eukaryotic cells. Kimball SR. Prog Mol Subcell Biol; 2001 Apr 05; 26():155-84. PubMed ID: 11575165 [Abstract] [Full Text] [Related]
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