메뉴 건너뛰기




Volumn 85, Issue 23, 2011, Pages 12594-12604

Rotavirus infection induces the unfolded protein response of the cell and controls it through the nonstructural protein NSP3

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 6; LUCIFERASE; MESSENGER RNA; NONSTRUCTURAL PROTEIN 3; PROTEIN IRE1;

EID: 81255184274     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.05620-11     Document Type: Article
Times cited : (58)

References (69)
  • 1
    • 79952407316 scopus 로고    scopus 로고
    • West Nile virus differentially modulates the unfolded protein response to facilitate replication and immune evasion
    • Ambrose, R. L., and J. M. Mackenzie. 2011. West Nile virus differentially modulates the unfolded protein response to facilitate replication and immune evasion. J. Virol. 85:2723-2732.
    • (2011) J. Virol. , vol.85 , pp. 2723-2732
    • Ambrose, R.L.1    Mackenzie, J.M.2
  • 2
    • 77953306075 scopus 로고    scopus 로고
    • Rotavirus nonstructural protein 1 suppresses virus-induced cellular apoptosis to facilitate viral growth by activating the cell survival pathways during early stages of infection
    • Bagchi, P., et al. 2010. Rotavirus nonstructural protein 1 suppresses virus-induced cellular apoptosis to facilitate viral growth by activating the cell survival pathways during early stages of infection. J. Virol. 84:6834-6845.
    • (2010) J. Virol. , vol.84 , pp. 6834-6845
    • Bagchi, P.1
  • 3
    • 42449139748 scopus 로고    scopus 로고
    • Coronavirus infection modulates the unfolded protein response and mediates sustained translational repression
    • Bechill, J., Z. Chen, J. W. Brewer, and S. C. Baker. 2008. Coronavirus infection modulates the unfolded protein response and mediates sustained translational repression. J. Virol. 82:4492-4501.
    • (2008) J. Virol. , vol.82 , pp. 4492-4501
    • Bechill, J.1    Chen, Z.2    Brewer, J.W.3    Baker, S.C.4
  • 4
    • 13644256191 scopus 로고    scopus 로고
    • A selective inhibitor of eIF2Universal-GreekwithMathPi -1. H9251 dephosphorylation protects cells from ER stress
    • Boyce, M., et al. 2005. A selective inhibitor of eIF2Universal-GreekwithMathPi.-1.H9251 dephosphorylation protects cells from ER stress. Science 307:935-939.
    • (2005) Science , vol.307 , pp. 935-939
    • Boyce, M.1
  • 5
    • 79960711299 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum: recent lessons from yeast and mammalian cell systems
    • Brodsky, J. L., and W. R. Skach. 2011. Protein folding and quality control in the endoplasmic reticulum: recent lessons from yeast and mammalian cell systems. Curr. Opin. Cell Biol. 23:464-475.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 464-475
    • Brodsky, J.L.1    Skach, W.R.2
  • 6
    • 33748502744 scopus 로고    scopus 로고
    • Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein
    • Chan, C. P., et al. 2006. Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein. J. Virol. 80: 9279-9287.
    • (2006) J. Virol. , vol.80 , pp. 9279-9287
    • Chan, C.P.1
  • 7
    • 13744253138 scopus 로고    scopus 로고
    • Herpes simplex virus 1 infection activates the endoplasmic reticulum resident kinase PERK and mediates eIF-2αdephosphorylation by the γ34
    • Cheng, G., Z. Feng, and B. He. 2005. Herpes simplex virus 1 infection activates the endoplasmic reticulum resident kinase PERK and mediates eIF-2αdephosphorylation by the γ34.5 protein. J. Virol. 79:1379-1388.
    • (2005) 5 protein. J. Virol. , vol.79 , pp. 1379-1388
    • Cheng, G.1    Feng, Z.2    He, B.3
  • 8
    • 34548407520 scopus 로고    scopus 로고
    • D. M. Knipe and P. M. Howley (ed.), Fields virology 5th ed. Lippincott Williams & Wilkins, Philadelphia PA
    • Estes, M. K., and A. Z. Kapikia. 2007. Rotaviruses, p. 1917-1974. In D. M. Knipe and P. M. Howley (ed.), Fields virology, 5th ed., vol. 2. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) Rotaviruses , vol.2 , pp. 1917-1974
    • Estes, M.K.1    Kapikia, A.Z.2
  • 9
    • 0033118409 scopus 로고    scopus 로고
    • Complexes containing activating transcription factor (ATF)/cAMP-responsive-element-binding protein (CREB) interact with the CCAAT/enhancer-binding protein (C/EBP)-ATF composite site to regulate Gadd153 expression during the stress response
    • Fawcett, T. W., J. L. Martindale, K. Z. Guyton, T. Hai, and N. J. Holbrook. 1999. Complexes containing activating transcription factor (ATF)/cAMP-responsive-element-binding protein (CREB) interact with the CCAAT/enhancer-binding protein (C/EBP)-ATF composite site to regulate Gadd153 expression during the stress response. Biochem. J. 339:135-141.
    • (1999) Biochem. J. , vol.339 , pp. 135-141
    • Fawcett, T.W.1    Martindale, J.L.2    Guyton, K.Z.3    Hai, T.4    Holbrook, N.J.5
  • 10
    • 0033795726 scopus 로고    scopus 로고
    • Relative localization of viroplasmic and endoplasmic reticulum-resident rotavirus proteins in infected cells
    • Gonzalez, R. A., R. Espinosa, P. Romero, S. Lopez, and C. F. Arias. 2000. Relative localization of viroplasmic and endoplasmic reticulum-resident rotavirus proteins in infected cells. Arch. Virol. 145:1963-1973.
    • (2000) Arch. Virol. , vol.145 , pp. 1963-1973
    • Gonzalez, R.A.1    Espinosa, R.2    Romero, P.3    Lopez, S.4    Arias, C.F.5
  • 11
    • 0026680471 scopus 로고
    • Psoralen preparation of antigenically intact noninfectious rotavirus particles
    • Groene, W. S., and R. D. Shaw. 1992. Psoralen preparation of antigenically intact noninfectious rotavirus particles. J. Virol. Methods 38:93-102.
    • (1992) J. Virol. Methods , vol.38 , pp. 93-102
    • Groene, W.S.1    Shaw, R.D.2
  • 12
    • 0036298692 scopus 로고    scopus 로고
    • Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization
    • Groft, C. M., and S. K. Burley. 2002. Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization. Mol. Cell 9:1273-1283.
    • (2002) Mol. Cell , vol.9 , pp. 1273-1283
    • Groft, C.M.1    Burley, S.K.2
  • 13
    • 0033809258 scopus 로고    scopus 로고
    • Biochemical characterization of rotavirus receptors in MA104 cells
    • Guerrero, C. A., S. Zarate, G. Corkidi, S. Lopez, and C. F. Arias. 2000. Biochemical characterization of rotavirus receptors in MA104 cells. J. Virol. 74:9362-9371.
    • (2000) J. Virol. , vol.74 , pp. 9362-9371
    • Guerrero, C.A.1    Zarate, S.2    Corkidi, G.3    Lopez, S.4    Arias, C.F.5
  • 14
    • 77955044180 scopus 로고    scopus 로고
    • HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1α-XBP1 signaling through a physical interaction
    • Gupta, S., et al. 2010 HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1α-XBP1 signaling through a physical interaction. PLoS Biol. 8:e1000410.
    • (2010) PLoS Biol. , vol.8
    • Gupta, S.1
  • 15
    • 77956035360 scopus 로고    scopus 로고
    • Different rotavirus strains enter MA104 cells through different endocytic pathways: the role of clathrin-mediated endocytosis
    • Gutierrez, M., et al. 2010. Different rotavirus strains enter MA104 cells through different endocytic pathways: the role of clathrin-mediated endocytosis. J. Virol. 84:9161-9169.
    • (2010) J. Virol. , vol.84 , pp. 9161-9169
    • Gutierrez, M.1
  • 16
    • 77955283618 scopus 로고    scopus 로고
    • Death mechanisms in epithelial cells following rotavirus infection, exposure to inactivated rotavirus or genome transfection
    • Halasz, P., G. Holloway, and B. S. Coulson. 2010. Death mechanisms in epithelial cells following rotavirus infection, exposure to inactivated rotavirus or genome transfection. J. Gen. Virol. 91:2007-2018.
    • (2010) J. Gen. Virol. , vol.91 , pp. 2007-2018
    • Halasz, P.1    Holloway, G.2    Coulson, B.S.3
  • 17
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the mammalian unfolded protein response
    • Harding, H. P., M. Calfon, F. Urano, I. Novoa, and D. Ron. 2002. Transcriptional and translational control in the mammalian unfolded protein response. Annu. Rev. Cell Dev. Biol. 18:575-599.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 575-599
    • Harding, H.P.1    Calfon, M.2    Urano, F.3    Novoa, I.4    Ron, D.5
  • 18
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding, H. P., et al. 2000. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell 6:1099-1108.
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1
  • 19
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding, H. P., Y. Zhang, A. Bertolotti, H. Zeng, and D. Ron. 2000. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol. Cell 5:897-904.
    • (2000) Mol. Cell , vol.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 20
    • 0037353039 scopus 로고    scopus 로고
    • An integrated stress response regulates amino acid metabolism and resistance to oxidative stress
    • Harding, H. P., et al. 2003. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol. Cell 11:619-633.
    • (2003) Mol. Cell , vol.11 , pp. 619-633
    • Harding, H.P.1
  • 21
    • 35848969791 scopus 로고    scopus 로고
    • ER stress signaling and the BCL-2 family of proteins: from adaptation to irreversible cellular damage
    • Hetz, C. A. 2007. ER stress signaling and the BCL-2 family of proteins: from adaptation to irreversible cellular damage. Antioxid. Redox Signal. 9:2345-2355.
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 2345-2355
    • Hetz, C.A.1
  • 22
    • 77749320273 scopus 로고    scopus 로고
    • AATF mediates an antiapoptotic effect of the unfolded protein response through transcriptional regulation of AKT1
    • Ishigaki, S., et al. 2010. AATF mediates an antiapoptotic effect of the unfolded protein response through transcriptional regulation of AKT1. Cell Death Differ 17:774-786.
    • (2010) Cell Death Differ , vol.17 , pp. 774-786
    • Ishigaki, S.1
  • 23
    • 18844419215 scopus 로고    scopus 로고
    • Human cytomegalovirus infection activates and regulates the unfolded protein response
    • Isler, J. A., A. H. Skalet, and J. C. Alwine. 2005. Human cytomegalovirus infection activates and regulates the unfolded protein response. J. Virol. 79:6890-6899.
    • (2005) J. Virol. , vol.79 , pp. 6890-6899
    • Isler, J.A.1    Skalet, A.H.2    Alwine, J.C.3
  • 24
    • 77954144139 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is induced and modulated by enterovirus 71
    • Jheng, J. R., K. S. Lau, W. F. Tang, M. S. Wu, and J. T. Horng. 2010. Endoplasmic reticulum stress is induced and modulated by enterovirus 71. Cell. Microbiol. 12:796-813.
    • (2010) Cell. Microbiol. , vol.12 , pp. 796-813
    • Jheng, J.R.1    Lau, K.S.2    Tang, W.F.3    Wu, M.S.4    Horng, J.T.5
  • 25
    • 1542316306 scopus 로고    scopus 로고
    • Regulation of mRNA translation by protein folding in the endoplasmic reticulum
    • Kaufman, R. J. 2004. Regulation of mRNA translation by protein folding in the endoplasmic reticulum. Trends Biochem. Sci. 29:152-158.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 152-158
    • Kaufman, R.J.1
  • 26
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls
    • Kaufman, R. J. 1999. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13:1211-1233.
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 27
    • 19444370770 scopus 로고    scopus 로고
    • ROS mediates 4HPR-induced posttran-scriptional expression of the Gadd153 gene
    • Lai, W. L., and N. S. Wong. 2005. ROS mediates 4HPR-induced posttran-scriptional expression of the Gadd153 gene. Free Radic. Biol. Med. 38:1585-1593.
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1585-1593
    • Lai, W.L.1    Wong, N.S.2
  • 28
    • 0142059951 scopus 로고    scopus 로고
    • XBP 1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee, A. H., N. N. Iwakoshi, and L. H. Glimcher. 2003. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell. Biol. 23:7448-7459.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 29
    • 0027949937 scopus 로고
    • The 58000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins
    • Lee, T. G., N. Tang, S. Thompson, J. Miller, and M. G. Katze. 1994. 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. 14:2331-2342.
    • (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
  • 30
    • 65449141379 scopus 로고    scopus 로고
    • An upstream open reading frame regulates translation of GADD34 during cellular stresses that induce eIF2α phosphorylation
    • Lee, Y. Y., R. C. Cevallos, and E. Jan. 2009. An upstream open reading frame regulates translation of GADD34 during cellular stresses that induce eIF2α phosphorylation. J. Biol. Chem. 284:6661-6673.
    • (2009) J. Biol. Chem. , vol.284 , pp. 6661-6673
    • Lee, Y.Y.1    Cevallos, R.C.2    Jan, E.3
  • 32
    • 5444264022 scopus 로고    scopus 로고
    • Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response
    • Lu, P. D., H. P. Harding, and D. Ron. 2004. Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response. J. Cell Biol. 167:27-33.
    • (2004) J. Cell Biol. , vol.167 , pp. 27-33
    • Lu, P.D.1    Harding, H.P.2    Ron, D.3
  • 33
    • 0036556684 scopus 로고    scopus 로고
    • The mammalian endoplasmic reticulum as a sensor for cellular stress
    • Ma, Y., and L. M. Hendershot. 2002. The mammalian endoplasmic reticulum as a sensor for cellular stress. Cell Stress Chaperones 7:222-229.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 222-229
    • Ma, Y.1    Hendershot, L.M.2
  • 34
    • 36248949141 scopus 로고    scopus 로고
    • The endoplasmic reticulum and the unfolded protein response
    • Malhotra, J. D., and R. J. Kaufman. 2007. The endoplasmic reticulum and the unfolded protein response. Semin. Cell Dev. Biol. 18:716-731.
    • (2007) Semin. Cell Dev. Biol. , vol.18 , pp. 716-731
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 35
    • 43949107171 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperones are involved in the morphogenesis of rotavirus infectious particles
    • Maruri-Avidal, L., S. Lopez, and C. F. Arias. 2008. Endoplasmic reticulum chaperones are involved in the morphogenesis of rotavirus infectious particles. J. Virol. 82:5368-5380.
    • (2008) J. Virol. , vol.82 , pp. 5368-5380
    • Maruri-Avidal, L.1    Lopez, S.2    Arias, C.F.3
  • 36
    • 35148894008 scopus 로고    scopus 로고
    • West Nile virus infection activates the unfolded protein response, leading to CHOP induction and apoptosis
    • Medigeshi, G. R., et al. 2007. West Nile virus infection activates the unfolded protein response, leading to CHOP induction and apoptosis. J. Virol. 81: 10849-10860.
    • (2007) J. Virol. , vol.81 , pp. 10849-10860
    • Medigeshi, G.R.1
  • 37
    • 33748517008 scopus 로고    scopus 로고
    • Rotavirus nonstructural protein NSP3 is not required for viral protein synthesis
    • Montero, H., C. F. Arias, and S. Lopez. 2006. Rotavirus nonstructural protein NSP3 is not required for viral protein synthesis. J. Virol. 80:9031-9038
    • (2006) J. Virol. , vol.80 , pp. 9031-9038
    • Montero, H.1    Arias, C.F.2    Lopez, S.3
  • 38
    • 38349138566 scopus 로고    scopus 로고
    • Rotavirus infection induces the phosphorylation of eIF2α but prevents the formation of stress granules
    • Montero, H., M. Rojas, C. F. Arias, and S. Lopez. 2008. Rotavirus infection induces the phosphorylation of eIF2α but prevents the formation of stress granules. J. Virol. 82:1496-1504.
    • (2008) J. Virol. , vol.82 , pp. 1496-1504
    • Montero, H.1    Rojas, M.2    Arias, C.F.3    Lopez, S.4
  • 39
    • 75749108288 scopus 로고    scopus 로고
    • Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis
    • Nakamura, T., et al. 2010. Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis. Cell 140:338-348.
    • (2010) Cell , vol.140 , pp. 338-348
    • Nakamura, T.1
  • 40
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2α
    • Novoa, I., H. Zeng, H. P. Harding, and D. Ron. 2001. Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2α. J. Cell Biol. 153:1011-1022.
    • (2001) J. Cell Biol. , vol.153 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 41
    • 79953224498 scopus 로고    scopus 로고
    • Phosphorylation of eIF2 facilitates ribosomal bypass of an inhibitory upstream ORF to enhance CHOP translation
    • Palam, L. R., T. D. Baird, and R. C. Wek. 2011. Phosphorylation of eIF2 facilitates ribosomal bypass of an inhibitory upstream ORF to enhance CHOP translation. J. Biol. Chem. 286:10939-10949.
    • (2011) J. Biol. Chem. , vol.286 , pp. 10939-10949
    • Palam, L.R.1    Baird, T.D.2    Wek, R.C.3
  • 43
    • 0037333913 scopus 로고    scopus 로고
    • Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2α kinase PERK
    • Pavio, N., P. R. Romano, T. M. Graczyk, S. M. Feinstone, and D. R. Taylor. 2003. Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2α kinase PERK. J. Virol. 77:3578-3585.
    • (2003) J. Virol. , vol.77 , pp. 3578-3585
    • Pavio, N.1    Romano, P.R.2    Graczyk, T.M.3    Feinstone, S.M.4    Taylor, D.R.5
  • 44
    • 0032190508 scopus 로고    scopus 로고
    • Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F
    • Piron, M., P. Vende, J. Cohen, and D. Poncet. 1998. Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F. EMBO J. 17:5811-5821.
    • (1998) EMBO J , vol.17 , pp. 5811-5821
    • Piron, M.1    Vende, P.2    Cohen, J.3    Poncet, D.4
  • 45
    • 36148929735 scopus 로고    scopus 로고
    • In U. Desselberger and J. Gray (ed.), Viral gastroenteritis. Elsevier Science, Amsterdam, Netherlands
    • Poncet, D. 2003. Translation of rotavirus mRNAs in the infected cell, p. 185-205. In U. Desselberger and J. Gray (ed.), Viral gastroenteritis. Elsevier Science, Amsterdam, Netherlands.
    • (2003) Translation of rotavirus mRNAs in the infected cell , pp. 185-205
    • Poncet, D.1
  • 46
    • 33750532939 scopus 로고    scopus 로고
    • Initiation of protein synthesis by hepatitis C virus is refractory to reduced eIF2 GTP. Met-tRNA(i)(Met) ternary complex availability
    • Robert, F., et al. 2006. Initiation of protein synthesis by hepatitis C virus is refractory to reduced eIF2.GTP.Met-tRNA(i)(Met) ternary complex availability. Mol. Biol. Cell 17:4632-4644.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4632-4644
    • Robert, F.1
  • 47
    • 77957200555 scopus 로고    scopus 로고
    • Protein kinase R is responsible for the phosphorylation of eIF2α in rotavirus infection
    • Rojas, M., C. F. Arias, and S. Lopez. 2010. Protein kinase R is responsible for the phosphorylation of eIF2α in rotavirus infection. J. Virol. 84:10457-10466.
    • (2010) J. Virol. , vol.84 , pp. 10457-10466
    • Rojas, M.1    Arias, C.F.2    Lopez, S.3
  • 48
    • 0036856008 scopus 로고    scopus 로고
    • Translational control in the endoplasmic reticulum stress response
    • Ron, D. 2002. Translational control in the endoplasmic reticulum stress response. J. Clin. Invest. 110:1383-1388.
    • (2002) J. Clin. Invest. , vol.110 , pp. 1383-1388
    • Ron, D.1
  • 49
    • 33751069967 scopus 로고    scopus 로고
    • Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins
    • Rutkowski, D. T., et al. 2006. Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins. PLoS Biol. 4:e374.
    • (2006) PLoS Biol. , vol.4
    • Rutkowski, D.T.1
  • 50
    • 0347285295 scopus 로고    scopus 로고
    • A trip to the ER: coping with stress
    • Rutkowski, D. T., and R. J. Kaufman. 2004. A trip to the ER: coping with stress. Trends Cell Biol. 14:20-28.
    • (2004) Trends Cell Biol. , vol.14 , pp. 20-28
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 51
    • 1842426663 scopus 로고    scopus 로고
    • Discordance of UPR signaling by ATF6 and Ire1p-XBP1 with levels of target transcripts
    • Shang, J., and M. A. Lehrman. 2004. Discordance of UPR signaling by ATF6 and Ire1p-XBP1 with levels of target transcripts. Biochem. Biophys. Res. Commun. 317:390-396.
    • (2004) Biochem. Biophys. Res. Commun. , vol.317 , pp. 390-396
    • Shang, J.1    Lehrman, M.A.2
  • 52
    • 4444232905 scopus 로고    scopus 로고
    • The unfolded protein response: a stress signaling pathway of the endoplasmic reticulum
    • Shen, X., K. Zhang, and R. J. Kaufman. 2004. The unfolded protein response: a stress signaling pathway of the endoplasmic reticulum. J. Chem. Neuroanat. 28:79-92.
    • (2004) J. Chem. Neuroanat. , vol.28 , pp. 79-92
    • Shen, X.1    Zhang, K.2    Kaufman, R.J.3
  • 53
    • 32444441933 scopus 로고    scopus 로고
    • Reovirus induces and benefits from an integrated cellular stress response
    • Smith, J. A., et al. 2006. Reovirus induces and benefits from an integrated cellular stress response. J. Virol. 80:2019-2033.
    • (2006) J. Virol. , vol.80 , pp. 2019-2033
    • Smith, J.A.1
  • 54
    • 0036223410 scopus 로고    scopus 로고
    • Japanese encephalitis virus infection initiates endoplasmic reticulum stress and an unfolded protein response
    • Su, H. L., C. L. Liao, and Y. L. Lin. 2002. Japanese encephalitis virus infection initiates endoplasmic reticulum stress and an unfolded protein response. J. Virol. 76:4162-4171.
    • (2002) J. Virol. , vol.76 , pp. 4162-4171
    • Su, H.L.1    Liao, C.L.2    Lin, Y.L.3
  • 55
    • 2342435179 scopus 로고    scopus 로고
    • Hepatitis C virus suppresses the IRE1-XBP1 pathway of the unfolded protein response
    • Tardif, K. D., K. Mori, R. J. Kaufman, and A. Siddiqui. 2004. Hepatitis C virus suppresses the IRE1-XBP1 pathway of the unfolded protein response. J. Biol. Chem. 279:17158-17164.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17158-17164
    • Tardif, K.D.1    Mori, K.2    Kaufman, R.J.3    Siddiqui, A.4
  • 56
    • 0036314483 scopus 로고    scopus 로고
    • Hepatitis C virus subgenomic replicons induce endoplasmic reticulum stress activating an intracellular signaling pathway
    • Tardif, K. D., K. Mori, and A. Siddiqui. 2002. Hepatitis C virus subgenomic replicons induce endoplasmic reticulum stress activating an intracellular signaling pathway. J. Virol. 76:7453-7459.
    • (2002) J. Virol. , vol.76 , pp. 7453-7459
    • Tardif, K.D.1    Mori, K.2    Siddiqui, A.3
  • 57
    • 0032525990 scopus 로고    scopus 로고
    • A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells
    • Tirasophon, W., A. A. Welihinda, and R. J. Kaufman. 1998. A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. Genes Dev. 12:1812-1824.
    • (1998) Genes Dev. , vol.12 , pp. 1812-1824
    • Tirasophon, W.1    Welihinda, A.A.2    Kaufman, R.J.3
  • 58
    • 70350005336 scopus 로고    scopus 로고
    • Unconventional splicing of XBP1 mRNA occurs in the cytoplasm during the mammalian unfolded protein response
    • Uemura, A., M. Oku, K. Mori, and H. Yoshida. 2009. Unconventional splicing of XBP1 mRNA occurs in the cytoplasm during the mammalian unfolded protein response. J. Cell Sci. 122:2877-2886.
    • (2009) J. Cell Sci. , vol.122 , pp. 2877-2886
    • Uemura, A.1    Oku, M.2    Mori, K.3    Yoshida, H.4
  • 59
    • 3843117589 scopus 로고    scopus 로고
    • Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells
    • Vattem, K. M., and R. C. Wek. 2004. Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells. Proc. Natl. Acad. Sci. U. S. A. 101:11269-11274.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 11269-11274
    • Vattem, K.M.1    Wek, R.C.2
  • 60
    • 29944433224 scopus 로고    scopus 로고
    • Translational resistance of late alphavirus mRNA to eIF2α phosphorylation: a strategy to overcome the antiviral effect of protein kinase PKR
    • Ventoso, I., et al. 2006. Translational resistance of late alphavirus mRNA to eIF2α phosphorylation: a strategy to overcome the antiviral effect of protein kinase PKR. Genes Dev. 20:87-100.
    • (2006) Genes Dev. , vol.20 , pp. 87-100
    • Ventoso, I.1
  • 61
    • 0034282912 scopus 로고    scopus 로고
    • Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response
    • 62
    • Wang, Y., et al. 2000. Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response. J. Biol. Chem. 275:27013-27020. 62
    • (2000) J. Biol. Chem. , vol.275 , pp. 27013-27020
    • Wang, Y.1
  • 62
    • 32544446451 scopus 로고    scopus 로고
    • Coping with stress: eIF2 kinases and translational control
    • Wek, R. C., H. Y. Jiang, and T. G. Anthony. 2006. Coping with stress: eIF2 kinases and translational control. Biochem. Soc. Trans. 34:7-11.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 7-11
    • Wek, R.C.1    Jiang, H.Y.2    Anthony, T.G.3
  • 63
    • 33645156429 scopus 로고    scopus 로고
    • From acute ER stress to physiological roles of the unfolded protein response
    • Wu, J., and R. J. Kaufman. 2006. From acute ER stress to physiological roles of the unfolded protein response. Cell Death Differ. 13:374-384.
    • (2006) Cell Death Differ. , vol.13 , pp. 374-384
    • Wu, J.1    Kaufman, R.J.2
  • 64
    • 64049088651 scopus 로고    scopus 로고
    • Human cytomegalovirus protein pUL38 induces ATF4 expression, inhibits persistent JNK phosphorylation, and suppresses endoplasmic reticulum stress-induced cell death
    • Xuan, B., Z. Qian, E. Torigoi, and D. Yu. 2009. Human cytomegalovirus protein pUL38 induces ATF4 expression, inhibits persistent JNK phosphorylation, and suppresses endoplasmic reticulum stress-induced cell death. J. Virol. 83:3463-3474.
    • (2009) J. Virol. , vol.83 , pp. 3463-3474
    • Xuan, B.1    Qian, Z.2    Torigoi, E.3    Yu, D.4
  • 65
    • 0037058574 scopus 로고    scopus 로고
    • Control of PERK eIF2α kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK
    • Yan, W., et al. 2002. Control of PERK eIF2α kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK. Proc. Natl. Acad. Sci. U. S. A. 99:15920-15925.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 15920-15925
    • Yan, W.1
  • 66
    • 0032509216 scopus 로고    scopus 로고
    • Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins Involvement of basic leucine zipper transcription factors
    • Yoshida, H., K. Haze, H. Yanagi, T. Yura, and K. Mori. 1998. Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors. J. Biol. Chem. 273: 33741-33749.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33741-33749
    • Yoshida, H.1    Haze, K.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 67
    • 0033815971 scopus 로고    scopus 로고
    • ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response
    • Yoshida, H., et al. 2000. ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol. Cell. Biol. 20:6755-6767.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6755-6767
    • Yoshida, H.1
  • 68
    • 33751247922 scopus 로고    scopus 로고
    • Flavivirus infection activates the XBP1 pathway of the unfolded protein response to cope with endoplasmic reticulum stress
    • Yu, C. Y., Y. W. Hsu, C. L. Liao, and Y. L. Lin. 2006. Flavivirus infection activates the XBP1 pathway of the unfolded protein response to cope with endoplasmic reticulum stress. J. Virol. 80:11868-11880.
    • (2006) J. Virol. , vol.80 , pp. 11868-11880
    • Yu, C.Y.1    Hsu, Y.W.2    Liao, C.L.3    Lin, Y.L.4
  • 69
    • 77956642651 scopus 로고    scopus 로고
    • Coxsackievirus B3 infection activates the unfolded protein response and induces apoptosis through downregulation of p58IPK and activation of CHOP and SREBP1
    • Zhang, H. M., et al. 2010. Coxsackievirus B3 infection activates the unfolded protein response and induces apoptosis through downregulation of p58IPK and activation of CHOP and SREBP1. J. Virol. 84:8446-8459.
    • (2010) J. Virol. , vol.84 , pp. 8446-8459
    • Zhang, H.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.