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615 related items for PubMed ID: 15798194

  • 1. PKR and GCN2 kinases and guanine nucleotide exchange factor eukaryotic translation initiation factor 2B (eIF2B) recognize overlapping surfaces on eIF2alpha.
    Dey M, Trieselmann B, Locke EG, Lu J, Cao C, Dar AC, Krishnamoorthy T, Dong J, Sicheri F, Dever TE.
    Mol Cell Biol; 2005 Apr; 25(8):3063-75. PubMed ID: 15798194
    [Abstract] [Full Text] [Related]

  • 2. Phosphorylation of translation initiation factor eIF2α at Ser51 depends on site- and context-specific information.
    Uppala JK, Ghosh C, Sathe L, Dey M.
    FEBS Lett; 2018 Sep; 592(18):3116-3125. PubMed ID: 30070006
    [Abstract] [Full Text] [Related]

  • 3. The double-stranded RNA-activated protein kinase PKR is dispensable for regulation of translation initiation in response to either calcium mobilization from the endoplasmic reticulum or essential amino acid starvation.
    Kimball SR, Clemens MJ, Tilleray VJ, Wek RC, Horetsky RL, Jefferson LS.
    Biochem Biophys Res Commun; 2001 Jan 12; 280(1):293-300. PubMed ID: 11162513
    [Abstract] [Full Text] [Related]

  • 4. Functional complementation by wheat eIF2alpha in the yeast GCN2-mediated pathway.
    Chang LY, Yang WY, Roth D.
    Biochem Biophys Res Commun; 2000 Dec 20; 279(2):468-74. PubMed ID: 11118310
    [Abstract] [Full Text] [Related]

  • 5. The beta/Gcd7 subunit of eukaryotic translation initiation factor 2B (eIF2B), a guanine nucleotide exchange factor, is crucial for binding eIF2 in vivo.
    Dev K, Qiu H, Dong J, Zhang F, Barthlme D, Hinnebusch AG.
    Mol Cell Biol; 2010 Nov 20; 30(21):5218-33. PubMed ID: 20805354
    [Abstract] [Full Text] [Related]

  • 6. Regulation of translation initiation by amino acids in eukaryotic cells.
    Kimball SR.
    Prog Mol Subcell Biol; 2001 Nov 20; 26():155-84. PubMed ID: 11575165
    [Abstract] [Full Text] [Related]

  • 7. Nck-1 selectively modulates eIF2alphaSer51 phosphorylation by a subset of eIF2alpha-kinases.
    Cardin E, Latreille M, Khoury C, Greenwood MT, Larose L.
    FEBS J; 2007 Nov 20; 274(22):5865-75. PubMed ID: 17944934
    [Abstract] [Full Text] [Related]

  • 8. Residues required for phosphorylation of translation initiation factor eIF2α under diverse stress conditions are divergent between yeast and human.
    Majumder M, Mitchell D, Merkulov S, Wu J, Guan BJ, Snider MD, Krokowski D, Yee VC, Hatzoglou M.
    Int J Biochem Cell Biol; 2015 Feb 20; 59():135-41. PubMed ID: 25541374
    [Abstract] [Full Text] [Related]

  • 9. Requirement for kinase-induced conformational change in eukaryotic initiation factor 2alpha (eIF2alpha) restricts phosphorylation of Ser51.
    Dey M, Velyvis A, Li JJ, Chiu E, Chiovitti D, Kay LE, Sicheri F, Dever TE.
    Proc Natl Acad Sci U S A; 2011 Mar 15; 108(11):4316-21. PubMed ID: 21368187
    [Abstract] [Full Text] [Related]

  • 10. Mechanistic link between PKR dimerization, autophosphorylation, and eIF2alpha substrate recognition.
    Dey M, Cao C, Dar AC, Tamura T, Ozato K, Sicheri F, Dever TE.
    Cell; 2005 Sep 23; 122(6):901-13. PubMed ID: 16179259
    [Abstract] [Full Text] [Related]

  • 11. Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2alpha kinases PKR and GCN2.
    Romano PR, Garcia-Barrio MT, Zhang X, Wang Q, Taylor DR, Zhang F, Herring C, Mathews MB, Qin J, Hinnebusch AG.
    Mol Cell Biol; 1998 Apr 23; 18(4):2282-97. PubMed ID: 9528799
    [Abstract] [Full Text] [Related]

  • 12. Phosphorylation of serine 51 in initiation factor 2 alpha (eIF2 alpha) promotes complex formation between eIF2 alpha(P) and eIF2B and causes inhibition in the guanine nucleotide exchange activity of eIF2B.
    Sudhakar A, Ramachandran A, Ghosh S, Hasnain SE, Kaufman RJ, Ramaiah KV.
    Biochemistry; 2000 Oct 24; 39(42):12929-38. PubMed ID: 11041858
    [Abstract] [Full Text] [Related]

  • 13. Tight binding of the phosphorylated alpha subunit of initiation factor 2 (eIF2alpha) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation.
    Krishnamoorthy T, Pavitt GD, Zhang F, Dever TE, Hinnebusch AG.
    Mol Cell Biol; 2001 Aug 24; 21(15):5018-30. PubMed ID: 11438658
    [Abstract] [Full Text] [Related]

  • 14. Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2.
    Asano K, Krishnamoorthy T, Phan L, Pavitt GD, Hinnebusch AG.
    EMBO J; 1999 Mar 15; 18(6):1673-88. PubMed ID: 10075937
    [Abstract] [Full Text] [Related]

  • 15. Identification of domains and residues within the epsilon subunit of eukaryotic translation initiation factor 2B (eIF2Bepsilon) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation.
    Gomez E, Pavitt GD.
    Mol Cell Biol; 2000 Jun 15; 20(11):3965-76. PubMed ID: 10805739
    [Abstract] [Full Text] [Related]

  • 16. Expression and purification of the alpha-subunit of eukaryotic initiation factor eIF2: use as a kinase substrate.
    Kimball SR, Horetsky RL, Jagus R, Jefferson LS.
    Protein Expr Purif; 1998 Apr 15; 12(3):415-9. PubMed ID: 9535710
    [Abstract] [Full Text] [Related]

  • 17. eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange.
    Pavitt GD, Ramaiah KV, Kimball SR, Hinnebusch AG.
    Genes Dev; 1998 Feb 15; 12(4):514-26. PubMed ID: 9472020
    [Abstract] [Full Text] [Related]

  • 18. eIF2B as a Target for Viral Evasion of PKR-Mediated Translation Inhibition.
    Wuerth JD, Habjan M, Kainulainen M, Berisha B, Bertheloot D, Superti-Furga G, Pichlmair A, Weber F.
    mBio; 2020 Jul 14; 11(4):. PubMed ID: 32665273
    [Abstract] [Full Text] [Related]

  • 19. Study of translational control of eukaryotic gene expression using yeast.
    Hinnebusch AG, Asano K, Olsen DS, Phan L, Nielsen KH, Valásek L.
    Ann N Y Acad Sci; 2004 Dec 14; 1038():60-74. PubMed ID: 15838098
    [Abstract] [Full Text] [Related]

  • 20. Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2.
    Pavitt GD, Yang W, Hinnebusch AG.
    Mol Cell Biol; 1997 Mar 14; 17(3):1298-313. PubMed ID: 9032257
    [Abstract] [Full Text] [Related]

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