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Volumn 106, Issue , 2012, Pages 75-106

Targeting phosphorylation of eukaryotic initiation factor-2α to treat human disease

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EID: 84857207261     PISSN: 18771173     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-396456-4.00005-5     Document Type: Chapter
Times cited : (34)

References (150)
  • 1
    • 17144424622 scopus 로고    scopus 로고
    • Translational control in stress and apoptosis
    • DOI 10.1038/nrm1618
    • M. Holcik, and N. Sonenberg Translational control in stress and apoptosis Nat Rev Mol Cell Biol 6 2005 318 327 (Pubitemid 40516898)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.4 , pp. 318-327
    • Holcik, M.1    Sonenberg, N.2
  • 2
    • 0015527030 scopus 로고
    • Control of globin synthesis: Role of heme
    • T. Hunt, G. Vanderhoff, and I.M. London Control of globin synthesis: role of heme J Mol Biol 66 1971 471 481
    • (1971) J Mol Biol , vol.66 , pp. 471-481
    • Hunt, T.1    Vanderhoff, G.2    London, I.M.3
  • 3
    • 0025779365 scopus 로고
    • Cloning of the cDNA of the heme-regulated eukaryotic initiation factor 2α (eIF-2α) kinase of rabbit reticulocytes: Homology to yeast GCN2 protein kinase and human double-stranded-RNA-dependent eIF-2α kinase
    • J.J. Chen, M.S. Throop, L. Gehrke, I. Kuo, J.K. Pal, and M. Brodsky Cloning of the cDNA of the heme-regulated eukaryotic initiation factor 2 alpha (eIF-2 alpha) kinase of rabbit reticulocytes: homology to yeast GCN2 protein kinase and human double-stranded-RNA-dependent eIF-2 alpha kinase Proc Natl Acad Sci USA 88 1991 7729 7733 (Pubitemid 21915228)
    • (1991) Proceedings of the National Academy of Sciences of the United States of America , vol.88 , Issue.17 , pp. 7729-7733
    • Chen, J.-J.1    Throop, M.S.2    Gehrke, L.3    Kuo, I.4    Pal, J.K.5    Brodsky, M.6    London, I.M.7
  • 5
    • 0026556814 scopus 로고
    • Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast
    • T.E. Dever, L. Feng, R.C. Wek, A.M. Cigan, T.F. Donahue, and A.G. Hinnebusch Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast Cell 68 1992 585 596
    • (1992) Cell , vol.68 , pp. 585-596
    • Dever, T.E.1    Feng, L.2    Wek, R.C.3    Cigan, A.M.4    Donahue, T.F.5    Hinnebusch, A.G.6
  • 6
    • 0036771638 scopus 로고    scopus 로고
    • The GCN2 eIF2alpha kinase is required for adaptation to amino acid deprivation in mice
    • P. Zhang, B.C. McGrath, J. Reinert, D.S. Olsen, L. Lei, and S. Gill The GCN2 eIF2alpha kinase is required for adaptation to amino acid deprivation in mice Mol Cell Biol 22 2002 6681 6688
    • (2002) Mol Cell Biol , vol.22 , pp. 6681-6688
    • Zhang, P.1    McGrath, B.C.2    Reinert, J.3    Olsen, D.S.4    Lei, L.5    Gill, S.6
  • 7
    • 2542489215 scopus 로고    scopus 로고
    • Dimerization is required for activation of eIF2 kinase Gcn2 in response to diverse environmental stress conditions
    • DOI 10.1074/jbc.M402228200
    • J. Narasimhan, K.A. Staschke, and R.C. Wek Dimerization is required for activation of eIF2 kinase Gcn2 in response to diverse environmental stress conditions J Biol Chem 279 2004 22820 22832 (Pubitemid 38685582)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.22 , pp. 22820-22832
    • Narasimhan, J.1    Staschke, K.A.2    Wek, R.C.3
  • 10
    • 0031755020 scopus 로고    scopus 로고
    • Identification and characterization of pancreatic eukaryotic initiation factor 2 α-subunit kinase, PEK, involved in translational control
    • Y. Shi, K.M. Vattem, R. Sood, J. An, J. Liang, and L. Stramm Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control Mol Cell Biol 18 1998 7499 7509 (Pubitemid 28533068)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.12 , pp. 7499-7509
    • Shi, Y.1    Vattem, K.M.2    Sood, R.3    An, J.4    Liang, J.5    Stramm, L.6    Wek, R.C.7
  • 11
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • H.P. Harding, Y. Zhang, A. Bertolotti, H. Zeng, and D. Ron Perk is essential for translational regulation and cell survival during the unfolded protein response Mol Cell 5 2000 897 904
    • (2000) Mol Cell , vol.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 12
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • F.U. Hartl, A. Bracher, and M. Hayer-Hartl Molecular chaperones in protein folding and proteostasis Nature 475 2011 324 332
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 13
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: Protein folding, quality control, degradation, and related human diseases
    • DOI 10.1152/physrev.00050.2006
    • D.N. Hebert, and M. Molinari In and out of the ER: protein folding, quality control, degradation, and related human diseases Physiol Rev 87 2007 1377 1408 (Pubitemid 350041473)
    • (2007) Physiological Reviews , vol.87 , Issue.4 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 14
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • G.S. Hotamisligil Endoplasmic reticulum stress and the inflammatory basis of metabolic disease Cell 140 2010 900 917
    • (2010) Cell , vol.140 , pp. 900-917
    • Hotamisligil, G.S.1
  • 15
    • 34347355500 scopus 로고    scopus 로고
    • Diseases originating from altered protein quality control in the endoplasmic reticulum
    • DOI 10.2174/092986707780830952
    • M. Otsu, and R. Sitia Diseases originating from altered protein quality control in the endoplasmic reticulum Curr Med Chem 14 2007 1639 1652 (Pubitemid 47010153)
    • (2007) Current Medicinal Chemistry , vol.14 , Issue.15 , pp. 1639-1652
    • Otsu, M.1    Sitia, R.2
  • 16
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • R.R. Kopito Aggresomes, inclusion bodies and protein aggregation Trends Cell Biol 10 2000 524 530
    • (2000) Trends Cell Biol , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 17
    • 77649202326 scopus 로고    scopus 로고
    • Protein aggregation diseases: Pathogenicity and therapeutic perspectives
    • A. Aguzzi, and T. O'Connor Protein aggregation diseases: pathogenicity and therapeutic perspectives Nat Rev Drug Discov 9 2010 237 248
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 237-248
    • Aguzzi, A.1    O'Connor, T.2
  • 18
    • 43549105167 scopus 로고    scopus 로고
    • The unfolded protein response: A pathway that links insulin demand with β-cell failure and diabetes
    • DOI 10.1210/er.2007-0039
    • D. Scheuner, and R.J. Kaufman The unfolded protein response: a pathway that links insulin demand with beta-cell failure and diabetes Endocr Rev 29 2008 317 333 (Pubitemid 351679702)
    • (2008) Endocrine Reviews , vol.29 , Issue.3 , pp. 317-333
    • Scheuner, D.1    Kaufman, R.J.2
  • 19
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • DOI 10.1038/nature06384, PII NATURE06384
    • T.A. Rapoport Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes Nature 450 2007 663 669 (Pubitemid 350207698)
    • (2007) Nature , vol.450 , Issue.7170 , pp. 663-669
    • Rapoport, T.A.1
  • 20
    • 0041832111 scopus 로고    scopus 로고
    • Partitioning and translation of mRNAs encoding soluble proteins on membrane-bound ribosomes
    • DOI 10.1261/rna.5610403
    • R.S. Lerner, R.M. Seiser, T. Zheng, P.J. Lager, M.C. Reedy, and J.D. Keene Partitioning and translation of mRNAs encoding soluble proteins on membrane-bound ribosomes RNA 9 2003 1123 1137 (Pubitemid 37093621)
    • (2003) RNA , vol.9 , Issue.9 , pp. 1123-1137
    • Lerner, R.S.1    Seiser, R.M.2    Zheng, T.3    Lager, P.J.4    Reedy, M.C.5    Keene, J.D.6    Nicchitta, C.V.7
  • 21
    • 39449120506 scopus 로고    scopus 로고
    • Divergent regulation of protein synthesis in the cytosol and endoplasmic reticulum compartments of mammalian cells
    • DOI 10.1091/mbc.E07-07-0677
    • S.B. Stephens, and C.V. Nicchitta Divergent regulation of protein synthesis in the cytosol and endoplasmic reticulum compartments of mammalian cells Mol Biol Cell 19 2008 623 632 (Pubitemid 351272150)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.2 , pp. 623-632
    • Stephens, S.B.1    Nicchitta, C.V.2
  • 22
    • 51749116326 scopus 로고    scopus 로고
    • HMG-CoA reductase inhibitors activate the unfolded protein response and induce cytoprotective GRP78 expression
    • J.C. Chen, M.L. Wu, K.C. Huang, and W.W. Lin HMG-CoA reductase inhibitors activate the unfolded protein response and induce cytoprotective GRP78 expression Cardiovasc Res 80 2008 138 150
    • (2008) Cardiovasc Res , vol.80 , pp. 138-150
    • Chen, J.C.1    Wu, M.L.2    Huang, K.C.3    Lin, W.W.4
  • 23
    • 0141646834 scopus 로고
    • Appearance of crystalloid endoplasmic reticulum in compactin-resistant Chinese hamster cells with a 500-fold increase in 3-hydroxy-3-methylglutaryl- coenzyme A reductase
    • DOI 10.1073/pnas.79.4.1185
    • D.J. Chin, K.L. Luskey, R.G. Anderson, J.R. Faust, J.L. Goldstein, and M.S. Brown Appearance of crystalloid endoplasmic reticulum in compactin-resistant Chinese hamster cells with a 500-fold increase in 3-hydroxy-3-methylglutaryl-coenzyme A reductase Proc Natl Acad Sci USA 79 1982 1185 1189 (Pubitemid 12105572)
    • (1982) Proceedings of the National Academy of Sciences of the United States of America , vol.79 , Issue.I4 , pp. 1185-1189
    • Chin, D.J.1    Luskey, K.L.2    Anderson, R.G.W.3
  • 24
    • 33748980413 scopus 로고    scopus 로고
    • Immunohistochemical and electron-microscopic observation of β-cells in pancreatic islets of spontaneously diabetic Goto-Kakizaki rats
    • DOI 10.1007/s00795-006-0324-9
    • K. Momose, S. Nunomiya, M. Nakata, T. Yada, M. Kikuchi, and T. Yashiro Immunohistochemical and electron-microscopic observation of beta-cells in pancreatic islets of spontaneously diabetic Goto-Kakizaki rats Med Mol Morphol 39 2006 146 153 (Pubitemid 44440463)
    • (2006) Medical Molecular Morphology , vol.39 , Issue.3 , pp. 146-153
    • Momose, K.1    Nunomiya, S.2    Nakata, M.3    Yada, T.4    Kikuchi, M.5    Yashiro, T.6
  • 25
    • 4644247806 scopus 로고    scopus 로고
    • Misfolded proinsulin accumulates in expanded pre-Golgi intermediates and endoplasmic reticulum subdomains in pancreatic beta cells of Akita mice
    • C. Zuber, J.Y. Fan, B. Guhl, and J. Roth Misfolded proinsulin accumulates in expanded pre-Golgi intermediates and endoplasmic reticulum subdomains in pancreatic beta cells of Akita mice FASEB J 18 2004 917 919
    • (2004) FASEB J , vol.18 , pp. 917-919
    • Zuber, C.1    Fan, J.Y.2    Guhl, B.3    Roth, J.4
  • 26
    • 84857217832 scopus 로고    scopus 로고
    • ER stress and its functional link to mitochondria: Role in cell survival and death
    • J.D. Malhotra, and R.J. Kaufman ER stress and its functional link to mitochondria: role in cell survival and death Cold Spring Harb Perspect Biol 3 2011 a004424
    • (2011) Cold Spring Harb Perspect Biol , vol.3 , pp. 004424
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 27
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • A. Bertolotti, Y. Zhang, L.M. Hendershot, H.P. Harding, and D. Ron Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response Nat Cell Biol 2 2000 326 332
    • (2000) Nat Cell Biol , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 28
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • M.H. Glickman, and A. Ciechanover The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction Physiol Rev 82 2002 373 428 (Pubitemid 34654457)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 29
    • 0034637605 scopus 로고    scopus 로고
    • Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum
    • DOI 10.1074/jbc.M004454200
    • C.Y. Liu, M. Schroder, and R.J. Kaufman Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum J Biol Chem 275 2000 24881 24885 (Pubitemid 30626593)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.32 , pp. 24881-24885
    • Chuan Yin Liu1    Schroder, M.2    Kaufman, R.J.3
  • 31
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • DOI 10.1038/nrm2199, PII NRM2199
    • D. Ron, and P. Walter Signal integration in the endoplasmic reticulum unfolded protein response Nat Rev Mol Cell Biol 8 2007 519 529 (Pubitemid 46985379)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.7 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 32
    • 0023655446 scopus 로고
    • Protein synthesis in rabbit reticulocytes: Mg2+-inhibition of ternary complex (Met-tRNA(f).eIF-2.GTP) formation by reticulocyte eIF-2
    • A.L. Roy, D. Chakrabarti, and N.K. Gupta Protein synthesis in rabbit reticulocytes: Mg2+-inhibition of ternary complex (Met-tRNA(f).eIF-2.GTP) formation by reticulocyte eIF-2 Biochem Biophys Res Commun 146 1987 114 120
    • (1987) Biochem Biophys Res Commun , vol.146 , pp. 114-120
    • Roy, A.L.1    Chakrabarti, D.2    Gupta, N.K.3
  • 33
    • 0034960171 scopus 로고    scopus 로고
    • Tight binding of the phosphorylated α at subunit of initiation factor 2 (eIF2α) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation
    • DOI 10.1128/MCB.21.15.5018-5030.2001
    • T. Krishnamoorthy, G.D. Pavitt, F. Zhang, T.E. Dever, and A.G. Hinnebusch 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 Mol Cell Biol 21 2001 5018 5030 (Pubitemid 32656399)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.15 , pp. 5018-5030
    • Krishnamoorthy, T.1    Pavitt, G.D.2    Zhang, F.3    Dever, T.E.4    Hinnebusch, A.G.5
  • 35
    • 79953224498 scopus 로고    scopus 로고
    • Phosphorylation of eIF2 facilitates ribosomal bypass of an inhibitory upstream ORF to enhance CHOP translation
    • L.R. Palam, T.D. Baird, and R.C. Wek Phosphorylation of eIF2 facilitates ribosomal bypass of an inhibitory upstream ORF to enhance CHOP translation J Biol Chem 286 2011 10939 10949
    • (2011) J Biol Chem , vol.286 , pp. 10939-10949
    • Palam, L.R.1    Baird, T.D.2    Wek, R.C.3
  • 36
    • 65449141379 scopus 로고    scopus 로고
    • An upstream open reading frame regulates translation of GADD34 during cellular stresses that induce eIF2alpha phosphorylation
    • Y.Y. Lee, R.C. Cevallos, and E. Jan An upstream open reading frame regulates translation of GADD34 during cellular stresses that induce eIF2alpha phosphorylation J Biol Chem 284 2009 6661 6673
    • (2009) J Biol Chem , vol.284 , pp. 6661-6673
    • Lee, Y.Y.1    Cevallos, R.C.2    Jan, E.3
  • 39
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha
    • I. Novoa, H. Zeng, H.P. Harding, and D. Ron Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha J Cell Biol 153 2001 1011 1022
    • (2001) J Cell Biol , vol.153 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 40
    • 0041315834 scopus 로고    scopus 로고
    • Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress
    • DOI 10.1074/jbc.M301107200
    • Y. Ma, and L.M. Hendershot Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress J Biol Chem 278 2003 34864 34873 (Pubitemid 37102245)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.37 , pp. 34864-34873
    • Ma, Y.1    Hendershot, L.M.2
  • 41
    • 33751069967 scopus 로고    scopus 로고
    • Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins
    • D.T. Rutkowski, S.M. Arnold, C.N. Miller, J. Wu, J. Li, and K.M. Gunnison Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins PLoS Biol 4 11 2006 e374
    • (2006) PLoS Biol , vol.4 , Issue.11 , pp. 374
    • Rutkowski, D.T.1    Arnold, S.M.2    Miller, C.N.3    Wu, J.4    Li, J.5    Gunnison, K.M.6
  • 44
    • 79958695905 scopus 로고    scopus 로고
    • Association with endoplasmic reticulum promotes proteasomal degradation of GADD34 protein
    • W. Zhou, M.H. Brush, M.S. Choy, and S. Shenolikar Association with endoplasmic reticulum promotes proteasomal degradation of GADD34 protein J Biol Chem 286 2011 21687 21696
    • (2011) J Biol Chem , vol.286 , pp. 21687-21696
    • Zhou, W.1    Brush, M.H.2    Choy, M.S.3    Shenolikar, S.4
  • 45
    • 57349198343 scopus 로고    scopus 로고
    • Control of cellular GADD34 levels by the 26S proteasome
    • M.H. Brush, and S. Shenolikar Control of cellular GADD34 levels by the 26S proteasome Mol Cell Biol 28 2008 6989 7000
    • (2008) Mol Cell Biol , vol.28 , pp. 6989-7000
    • Brush, M.H.1    Shenolikar, S.2
  • 46
    • 0037416211 scopus 로고    scopus 로고
    • Stress-induced gene expression requires programmed recovery from translational repression
    • DOI 10.1093/emboj/cdg112
    • I. Novoa, Y. Zhang, H. Zeng, R. Jungreis, H.P. Harding, and D. Ron Stress-induced gene expression requires programmed recovery from translational repression EMBO J 22 2003 1180 1187 (Pubitemid 36313601)
    • (2003) EMBO Journal , vol.22 , Issue.5 , pp. 1180-1187
    • Novoa, I.1    Zhang, Y.2    Zeng, H.3    Jungreis, R.4    Harding, H.P.5    Ron, D.6
  • 47
  • 48
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • DOI 10.1016/S1097-2765(00)00133-7
    • J. Ye, R.B. Rawson, R. Komuro, X. Chen, U.P. Dave, and R. Prywes ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs Mol Cell 6 2000 1355 1364 (Pubitemid 32045928)
    • (2000) Molecular Cell , vol.6 , Issue.6 , pp. 1355-1364
    • Ye, J.1    Rawson, R.B.2    Komuro, R.3    Chen, X.4    Dave, U.P.5    Prywes, R.6    Brown, M.S.7    Goldstein, J.L.8
  • 49
    • 10044271037 scopus 로고    scopus 로고
    • SREBP transcription factors: Master regulators of lipid homeostasis
    • DOI 10.1016/j.biochi.2004.09.018, PII S0300908404001658, Recent Advances in Lipid Metabolism and Related Disorders
    • D. Eberlé, B. Hegarty, P. Bossard, P. Ferré, and F. Foufelle SREBP transcription factors: master regulators of lipid homeostasis Biochimie 86 2004 839 848 (Pubitemid 39602764)
    • (2004) Biochimie , vol.86 , Issue.11 , pp. 839-848
    • Eberle, D.1    Hegarty, B.2    Bossard, P.3    Ferre, P.4    Foufelle, F.5
  • 50
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of golgi localization signals
    • DOI 10.1016/S1534-5807(02)00203-4
    • J. Shen, X. Chen, L. Hendershot, and R. Prywes ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals Dev Cell 3 2002 99 111 (Pubitemid 34778399)
    • (2002) Developmental Cell , vol.3 , Issue.1 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 51
    • 34548172495 scopus 로고    scopus 로고
    • Transcriptional Induction of Mammalian ER Quality Control Proteins Is Mediated by Single or Combined Action of ATF6α and XBP1
    • DOI 10.1016/j.devcel.2007.07.018, PII S1534580707003000
    • K. Yamamoto, T. Sato, T. Matsui, M. Sato, T. Okada, and H. Yoshida Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1 Dev Cell 13 2007 365 376 (Pubitemid 47308680)
    • (2007) Developmental Cell , vol.13 , Issue.3 , pp. 365-376
    • Yamamoto, K.1    Sato, T.2    Matsui, T.3    Sato, M.4    Okada, T.5    Yoshida, H.6    Harada, A.7    Mori, K.8
  • 52
    • 2442647920 scopus 로고    scopus 로고
    • Opposing roles for ATF6α and ATF6β in endoplasmic reticulum stress response gene induction
    • DOI 10.1074/jbc.M400713200
    • D.J. Thuerauf, L. Morrison, and C.C. Glembotski Opposing roles for ATF6alpha and ATF6beta in endoplasmic reticulum stress response gene induction J Biol Chem 279 2004 21078 21084 (Pubitemid 38656510)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.20 , pp. 21078-21084
    • Thuerauf, D.J.1    Morrison, L.2    Glembotski, C.C.3
  • 54
    • 33745893809 scopus 로고    scopus 로고
    • Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response
    • DOI 10.1126/science.1129631
    • J. Hollien, and J.S. Weissman Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response Science 313 2006 104 107 (Pubitemid 44051264)
    • (2006) Science , vol.313 , Issue.5783 , pp. 104-107
    • Hollien, J.1    Weissman, J.S.2
  • 55
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulum-associated degradation
    • S.S. Vembar, and J.L. Brodsky One step at a time: endoplasmic reticulum-associated degradation Nat Rev Mol Cell Biol 9 2008 944 957
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 56
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 Regulates a Subset of Endoplasmic Reticulum Resident Chaperone Genes in the Unfolded Protein Response
    • DOI 10.1128/MCB.23.21.7448-7459.2003
    • A.H. Lee, N.N. Iwakoshi, and L.H. Glimcher XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response Mol Cell Biol 23 2003 7448 7459 (Pubitemid 37271447)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.21 , pp. 7448-7459
    • Lee, A.-H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 57
    • 0027949937 scopus 로고
    • The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins
    • T.G. Lee, N. Tang, S. Thompson, J. Miller, and M.G. Katze The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins Mol Cell Biol 14 1994 2331 2342
    • (1994) Mol Cell Biol , vol.14 , pp. 2331-2342
    • Lee, T.G.1    Tang, N.2    Thompson, S.3    Miller, J.4    Katze, M.G.5
  • 58
    • 0025180598 scopus 로고
    • Purification and partial characterization of a cellular inhibitor of the interferon-induced protein kinase of Mr 68,000 from influenza virus-infected cells
    • T.G. Lee, J. Tomita, A.G. Hovanessian, and M.G. Katze Purification and partial characterization of a cellular inhibitor of the interferon-induced protein kinase of Mr 68,000 from influenza virus-infected cells Proc Natl Acad Sci USA 87 1990 6208 6212
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6208-6212
    • Lee, T.G.1    Tomita, J.2    Hovanessian, A.G.3    Katze, M.G.4
  • 59
    • 0038182518 scopus 로고    scopus 로고
    • IPK , a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2α signaling
    • DOI 10.1074/jbc.M212074200
    • R. Van Huizen, J.L. Martindale, M. Gorospe, and N.J. Holbrook P58IPK, a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2alpha signaling J Biol Chem 278 2003 15558 15564 (Pubitemid 36799663)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.18 , pp. 15558-15564
    • Van Huizen, R.1    Martindale, J.L.2    Gorospe, M.3    Holbrook, N.J.4
  • 62
  • 65
    • 0037118259 scopus 로고    scopus 로고
    • Neuronal α-synucleinopathy with severe movement disorder in mice expressing A53T human α-synuclein
    • DOI 10.1016/S0896-6273(02)00682-7
    • B.I. Giasson, J.E. Duda, S.M. Quinn, B. Zhang, J.Q. Trojanowski, and V.M. Lee Neuronal alpha-synucleinopathy with severe movement disorder in mice expressing A53T human alpha-synuclein Neuron 34 2002 521 533 (Pubitemid 34628750)
    • (2002) Neuron , vol.34 , Issue.4 , pp. 521-533
    • Giasson, B.I.1    Duda, J.E.2    Quinn, S.M.3    Zhang, B.4    Trojanowski, J.Q.5    Lee, V.M.-Y.6
  • 70
    • 17944362905 scopus 로고    scopus 로고
    • Heme-regulated eIF2α kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency
    • DOI 10.1093/emboj/20.23.6909
    • A.P. Han, C. Yu, L. Lu, Y. Fujiwara, C. Browne, and G. Chin Heme-regulated eIF2alpha kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency EMBO J 20 2001 6909 6918 (Pubitemid 33134220)
    • (2001) EMBO Journal , vol.20 , Issue.23 , pp. 6909-6918
    • Han, A.-P.1    Yu, C.2    Lu, L.3    Fujiwara, Y.4    Browne, C.5    Chin, G.6    Fleming, M.7    Leboulch, P.8    Orkin, S.H.9    Chen, J.-J.10
  • 73
    • 33751430251 scopus 로고    scopus 로고
    • PERK EIF2AK3 control of pancreatic β cell differentiation and proliferation is required for postnatal glucose homeostasis
    • DOI 10.1016/j.cmet.2006.11.002, PII S1550413106003640
    • W. Zhang, D. Feng, Y. Li, K. Iida, B. McGrath, and D.R. Cavener PERK EIF2AK3 control of pancreatic beta cell differentiation and proliferation is required for postnatal glucose homeostasis Cell Metab 4 2006 491 497 (Pubitemid 44817351)
    • (2006) Cell Metabolism , vol.4 , Issue.6 , pp. 491-497
    • Zhang, W.1    Feng, D.2    Li, Y.3    Iida, K.4    McGrath, B.5    Cavener, D.R.6
  • 75
    • 60549114848 scopus 로고    scopus 로고
    • Ppp 1r15 gene knockout reveals an essential role for translation initiation factor 2 alpha (eIF2alpha) dephosphorylation in mammalian development
    • H.P. Harding, Y. Zhang, D. Scheuner, J.J. Chen, R.J. Kaufman, and D. Ron Ppp 1r15 gene knockout reveals an essential role for translation initiation factor 2 alpha (eIF2alpha) dephosphorylation in mammalian development Proc Natl Acad Sci USA 106 2009 1832 1837
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1832-1837
    • Harding, H.P.1    Zhang, Y.2    Scheuner, D.3    Chen, J.J.4    Kaufman, R.J.5    Ron, D.6
  • 76
    • 0032452122 scopus 로고    scopus 로고
    • Targeted disruption of ATF4 discloses its essential role in the formation of eye lens fibres
    • DOI 10.1046/j.1365-2443.1998.00230.x
    • T. Tanaka, T. Tsujimura, K. Takeda, A. Sugihara, A. Maekawa, and N. Terada Targeted disruption of ATF4 discloses its essential role in the formation of eye lens fibres Genes Cells 3 1998 801 810 (Pubitemid 29098936)
    • (1998) Genes to Cells , vol.3 , Issue.12 , pp. 801-810
    • Tanaka, T.1    Tsujimura, T.2    Takeda, K.3    Sugihara, A.4    Maekawa, A.5    Terada, N.6    Yoshida, N.7    Akira, S.8
  • 77
    • 0034213391 scopus 로고    scopus 로고
    • Microphthalmia due to p53-mediated apoptosis of anterior lens epithelial cells in mice lacking the CREB-2 transcription factor
    • DOI 10.1006/dbio.2000.9699
    • T. Hettmann, K. Barton, and J.M. Leiden Microphthalmia due to p53-mediated apoptosis of anterior lens epithelial cells in mice lacking the CREB-2 transcription factor Dev Biol 222 2000 110 123 (Pubitemid 30387733)
    • (2000) Developmental Biology , vol.222 , Issue.1 , pp. 110-123
    • Hettmann, T.1    Barton, K.2    Leiden, J.M.3
  • 78
    • 80051704067 scopus 로고    scopus 로고
    • The sarcoplasmic reticulum luminal thiol oxidase ERO1 regulates cardiomyocyte excitation-coupled calcium release and response to hemodynamic load
    • K.T. Chin, G. Kang, J. Qu, L.B. Gardner, W.A. Coetzee, and E. Zito The sarcoplasmic reticulum luminal thiol oxidase ERO1 regulates cardiomyocyte excitation-coupled calcium release and response to hemodynamic load FASEB J 25 2011 2583 2591
    • (2011) FASEB J , vol.25 , pp. 2583-2591
    • Chin, K.T.1    Kang, G.2    Qu, J.3    Gardner, L.B.4    Coetzee, W.A.5    Zito, E.6
  • 79
    • 77949716997 scopus 로고    scopus 로고
    • ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis
    • E. Zito, K.T. Chin, J. Blais, H.P. Harding, and D. Ron ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis J Cell Biol 188 2010 821 832
    • (2010) J Cell Biol , vol.188 , pp. 821-832
    • Zito, E.1    Chin, K.T.2    Blais, J.3    Harding, H.P.4    Ron, D.5
  • 80
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
    • DOI 10.1038/47513
    • T. Nakagawa, H. Zhu, N. Morishima, E. Li, J. Xu, and B.A. Yankner Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta Nature 403 2000 98 103 (Pubitemid 30038529)
    • (2000) Nature , vol.403 , Issue.6765 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 81
    • 33746500168 scopus 로고    scopus 로고
    • GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development
    • DOI 10.1128/MCB.00779-06
    • S. Luo, C. Mao, B. Lee, and A.S. Lee GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development Mol Cell Biol 26 2006 5688 5697 (Pubitemid 44134326)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.15 , pp. 5688-5697
    • Luo, S.1    Mao, C.2    Lee, B.3    Lee, A.S.4
  • 82
    • 14944371187 scopus 로고    scopus 로고
    • The unfolded protein response sensor IRE1α is required at 2 distinct steps in B cell lymphopoiesis
    • DOI 10.1172/JCI200521848
    • K. Zhang, H.N. Wong, B. Song, C.N. Miller, D. Scheuner, and R.J. Kaufman The unfolded protein response sensor IRE1alpha is required at 2 distinct steps in B cell lymphopoiesis J Clin Invest 115 2005 268 281 (Pubitemid 40385469)
    • (2005) Journal of Clinical Investigation , vol.115 , Issue.2 , pp. 268-281
    • Zhang, K.1    Wong, H.N.2    Song, B.3    Miller, C.N.4    Scheuner, D.5    Kaufman, R.J.6
  • 83
    • 70349756962 scopus 로고    scopus 로고
    • Function of IRE1 alpha in the placenta is essential for placental development and embryonic viability
    • T. Iwawaki, R. Akai, S. Yamanaka, and K. Kohno Function of IRE1 alpha in the placenta is essential for placental development and embryonic viability Proc Natl Acad Sci USA 106 2009 16657 16662
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 16657-16662
    • Iwawaki, T.1    Akai, R.2    Yamanaka, S.3    Kohno, K.4
  • 85
    • 45849137877 scopus 로고    scopus 로고
    • Regulation of hepatic lipogenesis by the transcription factor XBP1
    • DOI 10.1126/science.1158042
    • A.H. Lee, E.F. Scapa, D.E. Cohen, and L.H. Glimcher Regulation of hepatic lipogenesis by the transcription factor XBP1 Science 320 2008 1492 1496 (Pubitemid 351929428)
    • (2008) Science , vol.320 , Issue.5882 , pp. 1492-1496
    • Lee, A.-H.1    Scapa, E.F.2    Cohen, D.E.3    Glimcher, L.H.4
  • 86
    • 29244448729 scopus 로고    scopus 로고
    • XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands
    • DOI 10.1038/sj.emboj.7600903
    • A.H. Lee, G.C. Chu, N.N. Iwakoshi, and L.H. Glimcher XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands EMBO J 24 2005 4368 4380 (Pubitemid 41828911)
    • (2005) EMBO Journal , vol.24 , Issue.24 , pp. 4368-4380
    • Lee, A.-H.1    Chu, G.C.2    Iwakoshi, N.N.3    Glimcher, L.H.4
  • 87
    • 77956232915 scopus 로고    scopus 로고
    • Induction of liver steatosis and lipid droplet formation in ATF6alpha-knockout mice burdened with pharmacological endoplasmic reticulum stress
    • K. Yamamoto, K. Takahara, S. Oyadomari, T. Okada, T. Sato, and A. Harada Induction of liver steatosis and lipid droplet formation in ATF6alpha-knockout mice burdened with pharmacological endoplasmic reticulum stress Mol Biol Cell 21 2010 2975 2986
    • (2010) Mol Biol Cell , vol.21 , pp. 2975-2986
    • Yamamoto, K.1    Takahara, K.2    Oyadomari, S.3    Okada, T.4    Sato, T.5    Harada, A.6
  • 88
    • 34547933706 scopus 로고    scopus 로고
    • Effects of the isoform-specific characteristics of ATF6α and ATF6β on endoplasmic reticulum stress response gene expression and cell viability
    • DOI 10.1074/jbc.M701213200
    • D.J. Thuerauf, M. Marcinko, P.J. Belmont, and C.C. Glembotski Effects of the isoform-specific characteristics of ATF6 alpha and ATF6 beta on endoplasmic reticulum stress response gene expression and cell viability J Biol Chem 282 2007 22865 22878 (Pubitemid 47267311)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.31 , pp. 22865-22878
    • Thuerauf, D.J.1    Marcinko, M.2    Belmont, P.J.3    Glembotski, C.C.4
  • 91
    • 37549033821 scopus 로고    scopus 로고
    • Dysfunction of the ER chaperone BiP accelerates the renal tubular injury
    • K. Kimura, H. Jin, M. Ogawa, and T. Aoe Dysfunction of the ER chaperone BiP accelerates the renal tubular injury Biochem Biophys Res Commun 366 2008 1048 1053
    • (2008) Biochem Biophys Res Commun , vol.366 , pp. 1048-1053
    • Kimura, K.1    Jin, H.2    Ogawa, M.3    Aoe, T.4
  • 92
    • 77952786601 scopus 로고    scopus 로고
    • EIF2alpha phosphorylation tips the balance to apoptosis during osmotic stress
    • E. Bevilacqua, X. Wang, M. Majumder, F. Gaccioli, C.L. Yuan, and C. Wang eIF2alpha phosphorylation tips the balance to apoptosis during osmotic stress J Biol Chem 285 2010 17098 17111
    • (2010) J Biol Chem , vol.285 , pp. 17098-17111
    • Bevilacqua, E.1    Wang, X.2    Majumder, M.3    Gaccioli, F.4    Yuan, C.L.5    Wang, C.6
  • 93
    • 75749108288 scopus 로고    scopus 로고
    • Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis
    • T. Nakamura, M. Furuhashi, P. Li, H. Cao, G. Tuncman, and N. Sonenberg Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis Cell 140 2010 338 348
    • (2010) Cell , vol.140 , pp. 338-348
    • Nakamura, T.1    Furuhashi, M.2    Li, P.3    Cao, H.4    Tuncman, G.5    Sonenberg, N.6
  • 95
    • 17044376304 scopus 로고    scopus 로고
    • GCN2 whets the appetite for amino acids
    • T.E. Dever, and A.G. Hinnebusch GCN2 whets the appetite for amino acids Mol Cell 18 2005 141 142
    • (2005) Mol Cell , vol.18 , pp. 141-142
    • Dever, T.E.1    Hinnebusch, A.G.2
  • 96
    • 4344650113 scopus 로고    scopus 로고
    • Preservation of liver protein synthesis during dietary leucine deprivation occurs at the expense of skeletal muscle mass in mice deleted for eIF2 kinase GCN2
    • DOI 10.1074/jbc.M404559200
    • T.G. Anthony, B.J. McDaniel, R.L. Byerley, B.C. McGrath, D.R. Cavener, and M.A. McNurlan Preservation of liver protein synthesis during dietary leucine deprivation occurs at the expense of skeletal muscle mass in mice deleted for eIF2 kinase GCN2 J Biol Chem 279 2004 36553 36561 (Pubitemid 39128998)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.35 , pp. 36553-36561
    • Anthony, T.G.1    McDaniel, B.J.2    Byerley, R.L.3    McGrath, B.C.4    Cavener, D.B.5    McNurlan, M.A.6    Wek, R.C.7
  • 99
    • 77953565102 scopus 로고    scopus 로고
    • The GCN2-ATF4 pathway is critical for tumour cell survival and proliferation in response to nutrient deprivation
    • J. Ye, M. Kumanova, L.S. Hart, K. Sloane, H. Zhang, and D.N. De Panis The GCN2-ATF4 pathway is critical for tumour cell survival and proliferation in response to nutrient deprivation EMBO J 29 2010 2082 2096
    • (2010) EMBO J , vol.29 , pp. 2082-2096
    • Ye, J.1    Kumanova, M.2    Hart, L.S.3    Sloane, K.4    Zhang, H.5    De Panis, D.N.6
  • 100
    • 0037064118 scopus 로고    scopus 로고
    • Functional characterization of pkr gene products expressed in cells from mice with a targeted deletion of the N terminus or C terminus domain of PKR
    • DOI 10.1074/jbc.M203564200
    • D. Baltzis, S. Li, and A.E. Koromilas Functional characterization of pkr gene products expressed in cells from mice with a targeted deletion of the N terminus or C terminus domain of PKR J Biol Chem 277 2002 38364 38372 (Pubitemid 35154692)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.41 , pp. 38364-38372
    • Baltzis, D.1    Li, S.2    Koromilas, A.E.3
  • 101
    • 0034425698 scopus 로고    scopus 로고
    • EIF2AK3, encoding translation initiation factor 2-α kinase 3, is mutated in patients with Wolcott-Rallison syndrome
    • DOI 10.1038/78085
    • M. Delepine, M. Nicolino, T. Barrett, M. Golamaully, G.M. Lathrop, and C. Julier EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome Nat Genet 25 2000 406 409 (Pubitemid 32983431)
    • (2000) Nature Genetics , vol.25 , Issue.4 , pp. 406-409
    • Delepine, M.1    Nicolino, M.2    Barrett, T.3    Golamaully, M.4    Mark Lathrop, G.5    Julier, C.6
  • 103
    • 0034968330 scopus 로고    scopus 로고
    • Diabetes mellitus and exocrine pancreatic dysfunction in Perk-/- mice reveals a role for translational control in secretory cell survival
    • DOI 10.1016/S1097-2765(01)00264-7
    • H.P. Harding, H. Zeng, Y. Zhang, R. Jungries, P. Chung, and H. Plesken Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival Mol Cell 7 6 2001 1153 1163 (Pubitemid 32607350)
    • (2001) Molecular Cell , vol.7 , Issue.6 , pp. 1153-1163
    • Harding, H.P.1    Zeng, H.2    Zhang, Y.3    Jungries, R.4    Chung, P.5    Plesken, H.6    Sabatini, D.D.7    Ron, D.8
  • 105
    • 81755184374 scopus 로고    scopus 로고
    • The eIF2 kinase PERK and the integrated stress response facilitate activation of ATF6 during endoplasmic reticulum stress
    • Inpress - 10.1091/mbc.E11-06-0510
    • B.F. Teske, S.A. Wek, P. Bunpo, J.K. Cundiff, J.N. McClintick, and T.G. Anthony The eIF2 kinase PERK and the integrated stress response facilitate activation of ATF6 during endoplasmic reticulum stress Mol Biol Cell 2011 Inpress - 10.1091/mbc.E11-06-0510
    • (2011) Mol Biol Cell
    • Teske, B.F.1    Wek, S.A.2    Bunpo, P.3    Cundiff, J.K.4    McClintick, J.N.5    Anthony, T.G.6
  • 107
    • 0031761895 scopus 로고    scopus 로고
    • Diabetes insipidus, diabetes mellitus, optic atrophy and deafness (DIDMOAD) caused by mutations in a novel gene (wolframin) coding for a predicted transmembrane protein
    • T.M. Strom, K. Hortnagel, S. Hofmann, F. Gekeler, C. Scharfe, and W. Rabl Diabetes insipidus, diabetes mellitus, optic atrophy and deafness (DIDMOAD) caused by mutations in a novel gene (wolframin) coding for a predicted transmembrane protein Hum Mol Genet 7 1998 2021 2028 (Pubitemid 28546409)
    • (1998) Human Molecular Genetics , vol.7 , Issue.13 , pp. 2021-2028
    • Strom, T.M.1    Hortnagel, K.2    Hofmann, S.3    Gekeler, F.4    Scharfe, C.5    Rabl, W.6    Gerbitz, K.D.7    Meitinger, T.8
  • 108
    • 28244435870 scopus 로고    scopus 로고
    • WFS1 is a novel component of the unfolded protein response and maintains homeostasis of the endoplasmic reticulum in pacreatic β-cells
    • DOI 10.1074/jbc.M507426200
    • S.G. Fonseca, M. Fukuma, K.L. Lipson, L.X. Nguyen, J.R. Allen, and Y. Oka WFS1 is a novel component of the unfolded protein response and maintains homeostasis of the endoplasmic reticulum in pancreatic beta-cells J Biol Chem 280 2005 39609 39615 (Pubitemid 41713920)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39609-39615
    • Fonseca, S.G.1    Fukuma, M.2    Lipson, K.L.3    Nguyen, L.X.4    Allen, J.R.5    Oka, Y.6    Urano, F.7
  • 109
    • 0035032066 scopus 로고    scopus 로고
    • WFS1/wolframin mutations, wolfram syndrome, and associated diseases
    • DOI 10.1002/humu.1110
    • F. Khanim, J. Kirk, F. Latif, and T.G. Barrett WFS1/wolframin mutations, Wolfram syndrome, and associated diseases Hum Mutat 17 2001 357 367 (Pubitemid 32381669)
    • (2001) Human Mutation , vol.17 , Issue.5 , pp. 357-367
    • Khanim, F.1    Kirk, J.2    Latif, F.3    Barrett, T.G.4
  • 112
    • 27744523525 scopus 로고    scopus 로고
    • Mice conditionally lacking the Wolfram gene in pancreatic islet beta cells exhibit diabetes as a result of enhanced endoplasmic reticulum stress and apoptosis
    • DOI 10.1007/s00125-005-1947-4
    • A.C. Riggs, E. Bernal-Mizrachi, M. Ohsugi, J. Wasson, S. Fatrai, and C. Welling Mice conditionally lacking the Wolfram gene in pancreatic islet beta cells exhibit diabetes as a result of enhanced endoplasmic reticulum stress and apoptosis Diabetologia 48 2005 2313 2321 (Pubitemid 41618923)
    • (2005) Diabetologia , vol.48 , Issue.11 , pp. 2313-2321
    • Riggs, A.C.1    Bernal-Mizrachi, E.2    Ohsugi, M.3    Wasson, J.4    Fatrai, S.5    Welling, C.6    Murray, J.7    Schmidt, R.E.8    Herrera, P.L.9    Permutt, M.A.10
  • 114
    • 0037317592 scopus 로고    scopus 로고
    • Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1α to the endoplasmic reticulum and promotes dephosphorylation of the α subunit of eukaryotic translation initiation factor 2
    • DOI 10.1128/MCB.23.4.1292-1303.2003
    • M.H. Brush, D.C. Weiser, and S. Shenolikar Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 alpha to the endoplasmic reticulum and promotes dephosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 Mol Cell Biol 23 2003 1292 1303 (Pubitemid 36177038)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.4 , pp. 1292-1303
    • Brush, M.H.1    Weiser, D.C.2    Shenolikar, S.3
  • 115
    • 0345599024 scopus 로고    scopus 로고
    • Inhibition of a constitutive translation initiation factor 2α phosphatase, CReP, promotes survival of stressed cells
    • DOI 10.1083/jcb.200308075
    • C. Jousse, S. Oyadomari, I. Novoa, P. Lu, Y. Zhang, and H.P. Harding Inhibition of a constitutive translation initiation factor 2alpha phosphatase, CReP, promotes survival of stressed cells J Cell Biol 163 2003 767 775 (Pubitemid 37517884)
    • (2003) Journal of Cell Biology , vol.163 , Issue.4 , pp. 767-775
    • Jousse, C.1    Oyadomari, S.2    Novoa, I.3    Lu, P.4    Zhang, Y.5    Harding, H.P.6    Ron, D.7
  • 117
    • 0030971097 scopus 로고    scopus 로고
    • Mammalian GADD34, an apoptosis- and DNA damage-inducible gene
    • DOI 10.1074/jbc.272.21.13731
    • M.C. Hollander, Q. Zhan, I. Bae, and A.J. Fornace Mammalian GADD34, an apoptosis- and DNA damage-inducible gene J Biol Chem 272 1997 13731 13737 (Pubitemid 27224809)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.21 , pp. 13731-13737
    • Hollander, M.C.1    Zhan, Q.2    Bae, I.3    Fornace Jr., A.J.4
  • 119
    • 0026097775 scopus 로고
    • Sequence and expression of a cDNA encoding MyD118: A novel myeloid differentiation primary response gene induced by multiple cytokines
    • A. Abdollahi, K.A. Lord, B. Hoffman-Liebermann, and D.A. Liebermann Sequence and expression of a cDNA encoding MyD118: a novel myeloid differentiation primary response gene induced by multiple cytokines Oncogene 6 1991 165 167 (Pubitemid 21923998)
    • (1991) Oncogene , vol.6 , Issue.1 , pp. 165-167
    • Abdollahi, A.1    Lord, K.A.2    Hoffman-Liebermann, B.3    Liebermann, D.A.4
  • 120
    • 0041703031 scopus 로고    scopus 로고
    • The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: Elucidation by GADD34-deficient mice
    • E. Kojima, A. Takeuchi, M. Haneda, A. Yagi, T. Hasegawa, and K. Yamaki The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: elucidation by GADD34-deficient mice FASEB J 17 2003 1573 1575
    • (2003) FASEB J , vol.17 , pp. 1573-1575
    • Kojima, E.1    Takeuchi, A.2    Haneda, M.3    Yagi, A.4    Hasegawa, T.5    Yamaki, K.6
  • 121
    • 77954533365 scopus 로고    scopus 로고
    • GADD34 suppresses wound healing by upregulating expression of myosin IIA
    • C. Tanaka, S. Ito, N. Nishio, Y. Kodera, H. Sakurai, and H. Suzuki GADD34 suppresses wound healing by upregulating expression of myosin IIA Transgenic Res 19 2010 637 645
    • (2010) Transgenic Res , vol.19 , pp. 637-645
    • Tanaka, C.1    Ito, S.2    Nishio, N.3    Kodera, Y.4    Sakurai, H.5    Suzuki, H.6
  • 122
    • 81355150598 scopus 로고    scopus 로고
    • GADD34 mediates cytoprotective autophagy in mutant huntingtin expressing cells via the mTOR pathway
    • In press
    • A. Hyrskyluoto, S. Reijonen, J. Kivinen, D. Lindholm, and L. Korhonen GADD34 mediates cytoprotective autophagy in mutant huntingtin expressing cells via the mTOR pathway Exp Cell Res 2011 In press
    • (2011) Exp Cell Res
    • Hyrskyluoto, A.1    Reijonen, S.2    Kivinen, J.3    Lindholm, D.4    Korhonen, L.5
  • 123
    • 79955005054 scopus 로고    scopus 로고
    • Gadd34 induces autophagy through the suppression of the mTOR pathway during starvation
    • M.N. Uddin, S. Ito, N. Nishio, T. Suganya, and K. Isobe Gadd34 induces autophagy through the suppression of the mTOR pathway during starvation Biochem Biophys Res Commun 407 2011 692 698
    • (2011) Biochem Biophys Res Commun , vol.407 , pp. 692-698
    • Uddin, M.N.1    Ito, S.2    Nishio, N.3    Suganya, T.4    Isobe, K.5
  • 124
    • 44349163999 scopus 로고    scopus 로고
    • Dephosphorylation of Translation Initiation Factor 2α Enhances Glucose Tolerance and Attenuates Hepatosteatosis in Mice
    • DOI 10.1016/j.cmet.2008.04.011, PII S1550413108001435
    • S. Oyadomari, H.P. Harding, Y. Zhang, M. Oyadomari, and D. Ron Dephosphorylation of translation initiation factor 2alpha enhances glucose tolerance and attenuates hepatosteatosis in mice Cell Metab 7 2008 520 532 (Pubitemid 351729207)
    • (2008) Cell Metabolism , vol.7 , Issue.6 , pp. 520-532
    • Oyadomari, S.1    Harding, H.P.2    Zhang, Y.3    Oyadomari, M.4    Ron, D.5
  • 125
    • 80054712654 scopus 로고    scopus 로고
    • Influence of the hepatic eIF2{alpha} ER stress response pathway on insulin mediated ER stress, Hepatic and Peripheral Glucose Metabolism
    • A.L. Birkenfeld, H.Y. Lee, S. Majumdar, M.J. Juzcak, J. Camporez, and F.R. Jornayvaz Influence of the hepatic eIF2{alpha} ER stress response pathway on insulin mediated ER stress, Hepatic and Peripheral Glucose Metabolism J Biol Chem 286 2011 36163 36170
    • (2011) J Biol Chem , vol.286 , pp. 36163-36170
    • Birkenfeld, A.L.1    Lee, H.Y.2    Majumdar, S.3    Juzcak, M.J.4    Camporez, J.5    Jornayvaz, F.R.6
  • 126
    • 79955632933 scopus 로고    scopus 로고
    • Transmission of endoplasmic reticulum stress and pro-inflammation from tumor cells to myeloid cells
    • N.R. Mahadevan, J. Rodvold, H. Sepulveda, S. Rossi, A.F. Drew, and M. Zanetti Transmission of endoplasmic reticulum stress and pro-inflammation from tumor cells to myeloid cells Proc Natl Acad Sci USA 108 2011 6561 6566
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 6561-6566
    • Mahadevan, N.R.1    Rodvold, J.2    Sepulveda, H.3    Rossi, S.4    Drew, A.F.5    Zanetti, M.6
  • 127
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • H.P. Harding, I. Novoa, Y. Zhang, H. Zeng, R. Wek, and M. Schapira Regulated translation initiation controls stress-induced gene expression in mammalian cells Mol Cell 6 2000 1099 1108
    • (2000) Mol Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6
  • 130
    • 50349102156 scopus 로고    scopus 로고
    • ICP34.5-dependent and -independent activities of salubrinal in herpes simplex virus-1 infected cells
    • K.F. Bryant, E.R. Macari, N. Malik, M. Boyce, J. Yuan, and D.M. Coen ICP34.5-dependent and -independent activities of salubrinal in herpes simplex virus-1 infected cells Virology 379 2008 197 204
    • (2008) Virology , vol.379 , pp. 197-204
    • Bryant, K.F.1    MacAri, E.R.2    Malik, N.3    Boyce, M.4    Yuan, J.5    Coen, D.M.6
  • 131
    • 79960112123 scopus 로고    scopus 로고
    • ICP34.5 protein of herpes simplex virus facilitates the initiation of protein translation by bridging eukaryotic initiation factor 2α (eIF2α) and protein phosphatase 1
    • Y. Li, C. Zhang, X. Chen, J. Yu, Y. Wang, and Y. Yang ICP34.5 protein of herpes simplex virus facilitates the initiation of protein translation by bridging eukaryotic initiation factor 2α (eIF2α) and protein phosphatase 1 J Biol Chem 286 2011 24785 24792
    • (2011) J Biol Chem , vol.286 , pp. 24785-24792
    • Li, Y.1    Zhang, C.2    Chen, X.3    Yu, J.4    Wang, Y.5    Yang, Y.6
  • 133
    • 77956288847 scopus 로고    scopus 로고
    • Activation of PERK signaling attenuates Abeta-mediated ER stress
    • Y. Lee do, K.S. Lee, H.J. Lee, H. Kim do, Y.H. Noh, and K. Yu Activation of PERK signaling attenuates Abeta-mediated ER stress PLoS One 5 2010 e10489
    • (2010) PLoS One , vol.5 , pp. 10489
    • Lee Do, Y.1    Lee, K.S.2    Lee, H.J.3    Kim Do, H.4    Noh, Y.H.5    Yu, K.6
  • 134
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • DOI 10.1146/annurev.neuro.23.1.217
    • H.Y. Zoghbi, and H.T. Orr Glutamine repeats and neurodegeneration Annu Rev Neurosci 23 2000 217 247 (Pubitemid 30350043)
    • (2000) Annual Review of Neuroscience , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 135
    • 39649114320 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins
    • S. Reijonen, N. Putkonen, A. Norremolle, D. Lindholm, and L. Korhonen Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins Exp Cell Res 314 2008 950 960
    • (2008) Exp Cell Res , vol.314 , pp. 950-960
    • Reijonen, S.1    Putkonen, N.2    Norremolle, A.3    Lindholm, D.4    Korhonen, L.5
  • 138
    • 67349164383 scopus 로고    scopus 로고
    • A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice
    • S. Saxena, E. Cabuy, and P. Caroni A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice Nat Neurosci 12 2009 627 636
    • (2009) Nat Neurosci , vol.12 , pp. 627-636
    • Saxena, S.1    Cabuy, E.2    Caroni, P.3
  • 139
    • 35748966391 scopus 로고    scopus 로고
    • Dengue virus serotype infection specifies the activation of the unfolded protein response
    • I. Umareddy, O. Pluquet, Q.Y. Wang, S.G. Vasudevan, E. Chevet, and F. Gu Dengue virus serotype infection specifies the activation of the unfolded protein response Virol J 4 2007 91 96
    • (2007) Virol J , vol.4 , pp. 91-96
    • Umareddy, I.1    Pluquet, O.2    Wang, Q.Y.3    Vasudevan, S.G.4    Chevet, E.5    Gu, F.6
  • 140
    • 60549106248 scopus 로고    scopus 로고
    • Inhibition of eIF2alpha dephosphorylation maximizes bortezomib efficiency and eliminates quiescent multiple myeloma cells surviving proteasome inhibitor therapy
    • D.M. Schewe, and J.A. Aguirre-Ghiso Inhibition of eIF2alpha dephosphorylation maximizes bortezomib efficiency and eliminates quiescent multiple myeloma cells surviving proteasome inhibitor therapy Cancer Res 69 2009 1545 1552
    • (2009) Cancer Res , vol.69 , pp. 1545-1552
    • Schewe, D.M.1    Aguirre-Ghiso, J.A.2
  • 141
    • 58349097747 scopus 로고    scopus 로고
    • Synergistic apoptosis induction in leukemic cells by the phosphatase inhibitor salubrinal and proteasome inhibitors
    • H.C. Drexler Synergistic apoptosis induction in leukemic cells by the phosphatase inhibitor salubrinal and proteasome inhibitors PLoS One 4 2009 e4161
    • (2009) PLoS One , vol.4 , pp. 4161
    • Drexler, H.C.1
  • 142
    • 23244443372 scopus 로고    scopus 로고
    • Structure-activity relationship studies of salubrinal lead to its active biotinylated derivative
    • DOI 10.1016/j.bmcl.2005.05.120, PII S0960894X05007110
    • K. Long, M. Boyce, H. Lin, J. Yuan, and D. Ma Structure-activity relationship studies of salubrinal lead to its active biotinylated derivative Bioorg Med Chem Lett 15 2005 3849 3852 (Pubitemid 41095481)
    • (2005) Bioorganic and Medicinal Chemistry Letters , vol.15 , Issue.17 , pp. 3849-3852
    • Long, K.1    Boyce, M.2    Lin, H.3    Yuan, J.4    Ma, D.5
  • 143
    • 0020545855 scopus 로고
    • Guanabenz. A review of its pharmacodynamic properties and therapeutic efficacy in hypertension
    • B. Holmes, R.N. Brogden, R.C. Heel, T.M. Speight, and G.S. Avery Guanabenz. A review of its pharmacodynamic properties and therapeutic efficacy in hypertension Drugs 26 1983 212 229 (Pubitemid 13033177)
    • (1983) Drugs , vol.26 , Issue.3 , pp. 212-229
    • Holmes, B.1    Brogden, R.N.2    Heel, R.C.3
  • 144
    • 44349185449 scopus 로고    scopus 로고
    • Antihypertensive drug guanabenz is active in vivo against both yeast and mammalian prions
    • D. Tribouillard-Tanvier, V. Beringue, N. Desban, F. Gug, S. Bach, and C. Voisset Antihypertensive drug guanabenz is active in vivo against both yeast and mammalian prions PLoS One 3 2008 e1981
    • (2008) PLoS One , vol.3 , pp. 1981
    • Tribouillard-Tanvier, D.1    Beringue, V.2    Desban, N.3    Gug, F.4    Bach, S.5    Voisset, C.6
  • 145
    • 79953288480 scopus 로고    scopus 로고
    • Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis
    • P. Tsaytler, H.P. Harding, D. Ron, and A. Bertolotti Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis Science 332 2011 91 94
    • (2011) Science , vol.332 , pp. 91-94
    • Tsaytler, P.1    Harding, H.P.2    Ron, D.3    Bertolotti, A.4
  • 146
    • 33644876816 scopus 로고    scopus 로고
    • Bioactive small molecules reveal antagonism between the integrated stress response and sterol-regulated gene expression
    • H.P. Harding, Y. Zhang, S. Khersonsky, S. Marciniak, D. Scheuner, and R.J. Kaufman Bioactive small molecules reveal antagonism between the integrated stress response and sterol-regulated gene expression Cell Metab 2 2005 361 371
    • (2005) Cell Metab , vol.2 , pp. 361-371
    • Harding, H.P.1    Zhang, Y.2    Khersonsky, S.3    Marciniak, S.4    Scheuner, D.5    Kaufman, R.J.6
  • 147
    • 80054758767 scopus 로고    scopus 로고
    • Complementary cell-based high-throughput screens identify novel modulators of the unfolded protein response
    • A.M. Fribley, P.G. Cruz, J.R. Miller, M.U. Callaghan, P. Cai, and N. Narula Complementary cell-based high-throughput screens identify novel modulators of the unfolded protein response J Biomol Screen 16 2011 825 835
    • (2011) J Biomol Screen , vol.16 , pp. 825-835
    • Fribley, A.M.1    Cruz, P.G.2    Miller, J.R.3    Callaghan, M.U.4    Cai, P.5    Narula, N.6
  • 148
    • 0034808081 scopus 로고    scopus 로고
    • Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1
    • DOI 10.1128/MCB.21.20.6841-6850.2001
    • J.H. Connor, D.C. Weiser, S. Li, J.M. Hallenbeck, and S. Shenolikar Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1 Mol Cell Biol 21 2001 6841 6850 (Pubitemid 32911245)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.20 , pp. 6841-6850
    • Connor, J.H.1    Weiser, D.C.2    Li, S.3    Hallenbeck, J.M.4    Shenolikar, S.5
  • 149
    • 73249116246 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 agonists protect pancreatic beta-cells from lipotoxic endoplasmic reticulum stress through upregulation of BiP and JunB
    • D.A. Cunha, L. Ladriere, F. Ortis, M. Igoillo-Esteve, E.N. Gurzov, and R. Lupi Glucagon-like peptide-1 agonists protect pancreatic beta-cells from lipotoxic endoplasmic reticulum stress through upregulation of BiP and JunB Diabetes 58 2009 2851 2862
    • (2009) Diabetes , vol.58 , pp. 2851-2862
    • Cunha, D.A.1    Ladriere, L.2    Ortis, F.3    Igoillo-Esteve, M.4    Gurzov, E.N.5    Lupi, R.6
  • 150
    • 77449095179 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress plays critical role in brain damage after cerebral ischemia/reperfusion in rats
    • V.P. Nakka, A. Gusain, and R. Raghubir Endoplasmic reticulum stress plays critical role in brain damage after cerebral ischemia/reperfusion in rats Neurotox Res 17 2010 189 202
    • (2010) Neurotox Res , vol.17 , pp. 189-202
    • Nakka, V.P.1    Gusain, A.2    Raghubir, R.3


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