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235 related items for PubMed ID: 11389192

  • 1. Brain ischemia and reperfusion activates the eukaryotic initiation factor 2alpha kinase, PERK.
    Kumar R, Azam S, Sullivan JM, Owen C, Cavener DR, Zhang P, Ron D, Harding HP, Chen JJ, Han A, White BC, Krause GS, DeGracia DJ.
    J Neurochem; 2001 Jun; 77(5):1418-21. PubMed ID: 11389192
    [Abstract] [Full Text] [Related]

  • 2. PERK is responsible for the increased phosphorylation of eIF2alpha and the severe inhibition of protein synthesis after transient global brain ischemia.
    Owen CR, Kumar R, Zhang P, McGrath BC, Cavener DR, Krause GS.
    J Neurochem; 2005 Sep; 94(5):1235-42. PubMed ID: 16000157
    [Abstract] [Full Text] [Related]

  • 3. Eukaryotic initiation factor 2alpha kinase and phosphatase activity during postischemic brain reperfusion.
    DeGracia DJ, Adamczyk S, Folbe AJ, Konkoly LL, Pittman JE, Neumar RW, Sullivan JM, Scheuner D, Kaufman RJ, White BC, Krause GS.
    Exp Neurol; 1999 Feb; 155(2):221-7. PubMed ID: 10072297
    [Abstract] [Full Text] [Related]

  • 4. PERK and GCN2 contribute to eIF2alpha phosphorylation and cell cycle arrest after activation of the unfolded protein response pathway.
    Hamanaka RB, Bennett BS, Cullinan SB, Diehl JA.
    Mol Biol Cell; 2005 Dec; 16(12):5493-501. PubMed ID: 16176978
    [Abstract] [Full Text] [Related]

  • 5. eIF2alpha kinases GCN2 and PERK modulate transcription and translation of distinct sets of mRNAs in mouse liver.
    Dang Do AN, Kimball SR, Cavener DR, Jefferson LS.
    Physiol Genomics; 2009 Aug 07; 38(3):328-41. PubMed ID: 19509078
    [Abstract] [Full Text] [Related]

  • 6. 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]

  • 7. PKR-like endoplasmic reticulum kinase (PERK) activation following brain ischemia is independent of unfolded nascent proteins.
    Sanderson TH, Deogracias MP, Nangia KK, Wang J, Krause GS, Kumar R.
    Neuroscience; 2010 Sep 01; 169(3):1307-14. PubMed ID: 20538047
    [Abstract] [Full Text] [Related]

  • 8. Nanosecond pulsed electric fields induce the integrated stress response via reactive oxygen species-mediated heme-regulated inhibitor (HRI) activation.
    Hamada Y, Furumoto Y, Izutani A, Taniuchi S, Miyake M, Oyadomari M, Teranishi K, Shimomura N, Oyadomari S.
    PLoS One; 2020 Sep 01; 15(3):e0229948. PubMed ID: 32155190
    [Abstract] [Full Text] [Related]

  • 9. Functional characterization of Drosophila melanogaster PERK eukaryotic initiation factor 2alpha (eIF2alpha) kinase.
    Pomar N, Berlanga JJ, Campuzano S, Hernández G, Elías M, de Haro C.
    Eur J Biochem; 2003 Jan 01; 270(2):293-306. PubMed ID: 12605680
    [Abstract] [Full Text] [Related]

  • 10. PERK (Protein Kinase RNA-Like ER Kinase) Branch of the Unfolded Protein Response Confers Neuroprotection in Ischemic Stroke by Suppressing Protein Synthesis.
    Wang YC, Li X, Shen Y, Lyu J, Sheng H, Paschen W, Yang W.
    Stroke; 2020 May 01; 51(5):1570-1577. PubMed ID: 32212900
    [Abstract] [Full Text] [Related]

  • 11. Translation initiation control by heme-regulated eukaryotic initiation factor 2alpha kinase in erythroid cells under cytoplasmic stresses.
    Lu L, Han AP, Chen JJ.
    Mol Cell Biol; 2001 Dec 01; 21(23):7971-80. PubMed ID: 11689689
    [Abstract] [Full Text] [Related]

  • 12. p58IPK is an inhibitor of the eIF2α kinase GCN2 and its localization and expression underpin protein synthesis and ER processing capacity.
    Roobol A, Roobol J, Bastide A, Knight JR, Willis AE, Smales CM.
    Biochem J; 2015 Jan 15; 465(2):213-25. PubMed ID: 25329545
    [Abstract] [Full Text] [Related]

  • 13. Hepatic CYP3A suppression by high concentrations of proteasomal inhibitors: a consequence of endoplasmic reticulum (ER) stress induction, activation of RNA-dependent protein kinase-like ER-bound eukaryotic initiation factor 2alpha (eIF2alpha)-kinase (PERK) and general control nonderepressible-2 eIF2alpha kinase (GCN2), and global translational shutoff.
    Acharya P, Engel JC, Correia MA.
    Mol Pharmacol; 2009 Sep 15; 76(3):503-15. PubMed ID: 19520899
    [Abstract] [Full Text] [Related]

  • 14. Phosphorylation of eIF2alpha in response to 26S proteasome inhibition is mediated by the haem-regulated inhibitor (HRI) kinase.
    Yerlikaya A, Kimball SR, Stanley BA.
    Biochem J; 2008 Jun 15; 412(3):579-88. PubMed ID: 18290760
    [Abstract] [Full Text] [Related]

  • 15. Integrated stress response of vertebrates is regulated by four eIF2α kinases.
    Taniuchi S, Miyake M, Tsugawa K, Oyadomari M, Oyadomari S.
    Sci Rep; 2016 Sep 16; 6():32886. PubMed ID: 27633668
    [Abstract] [Full Text] [Related]

  • 16. Physiological Control of Nitric Oxide in Neuronal BACE1 Translation by Heme-Regulated eIF2α Kinase HRI Induces Synaptogenesis.
    Ill-Raga G, Tajes M, Busquets-García A, Ramos-Fernández E, Vargas LM, Bosch-Morató M, Guivernau B, Valls-Comamala V, Eraso-Pichot A, Guix FX, Fandos C, Rosen MD, Rabinowitz MH, Maldonado R, Alvarez AR, Ozaita A, Muñoz FJ.
    Antioxid Redox Signal; 2015 May 20; 22(15):1295-307. PubMed ID: 25706765
    [Abstract] [Full Text] [Related]

  • 17. Regulation of G(1) arrest and apoptosis in hypoxia by PERK and GCN2-mediated eIF2alpha phosphorylation.
    Liu Y, László C, Liu Y, Liu W, Chen X, Evans SC, Wu S.
    Neoplasia; 2010 Jan 20; 12(1):61-8. PubMed ID: 20072654
    [Abstract] [Full Text] [Related]

  • 18. Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha.
    Koumenis C, Naczki C, Koritzinsky M, Rastani S, Diehl A, Sonenberg N, Koromilas A, Wouters BG.
    Mol Cell Biol; 2002 Nov 20; 22(21):7405-16. PubMed ID: 12370288
    [Abstract] [Full Text] [Related]

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  • 20. Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinase.
    Berlanga JJ, Santoyo J, De Haro C.
    Eur J Biochem; 1999 Oct 20; 265(2):754-62. PubMed ID: 10504407
    [Abstract] [Full Text] [Related]

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