메뉴 건너뛰기




Volumn 1, Issue 4, 2012, Pages 926-950

Unfolded protein responses with or without unfolded proteins?

Author keywords

BIP; Endoplasmic reticulum; Inositol; Ire1; Misfolded protein; Stress; Unfolded protein response

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 6; BETA GALACTOSIDASE; CHAPERONE; DITHIOTHREITOL; GLUCOSE REGULATED PROTEIN 94; HEAT SHOCK PROTEIN 90; HEAT SHOCK TRANSCRIPTION FACTOR 1; INOSITOL; MAJOR HISTOCOMPATIBILITY ANTIGEN; MESSENGER RNA; PROTEIN; PROTEIN DNAK; PROTEIN IRE1; SECRETORY PROTEIN; THAPSIGARGIN; TUNICAMYCIN; X BOX BINDING PROTEIN 1;

EID: 84969577902     PISSN: None     EISSN: 20734409     Source Type: Journal    
DOI: 10.3390/cells1040926     Document Type: Article
Times cited : (13)

References (117)
  • 1
    • 23744457478 scopus 로고    scopus 로고
    • Versatility of the endoplasmic reticulum protein folding factory
    • van Anken, E.; Braakman, I.; Craig, E. Versatility of the endoplasmic reticulum protein folding factory. Crit. Rev. Biochem. Mol. Biol. 2005, 40, 191-228.
    • (2005) Crit. Rev. Biochem. Mol. Biol. , vol.40 , pp. 191-228
    • van Anken, E.1    Braakman, I.2    Craig, E.3
  • 2
    • 0036810271 scopus 로고    scopus 로고
    • Protein folding during cotranslational translocation in the endoplasmic reticulum
    • Kowarik, M.; Kung, S.; Martoglio, B.; Helenius, A. Protein folding during cotranslational translocation in the endoplasmic reticulum. Mol. Cell. 2002, 10, 769-778.
    • (2002) Mol. Cell. , vol.10 , pp. 769-778
    • Kowarik, M.1    Kung, S.2    Martoglio, B.3    Helenius, A.4
  • 3
    • 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.; Skach, W.R. Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems. Curr. Opin. Cell. Biol. 2011, 23, 464-475.
    • (2011) Curr. Opin. Cell. Biol. , vol.23 , pp. 464-475
    • Brodsky, J.L.1    Skach, W.R.2
  • 4
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter, P.; Ron, D. The unfolded protein response: from stress pathway to homeostatic regulation. Science 2011, 334, 1081-1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 6
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron, D.; Walter, P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell. Biol. 2007, 8, 519-529.
    • (2007) Nat. Rev. Mol. Cell. Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 7
    • 33751159209 scopus 로고    scopus 로고
    • Intracellular signaling by the unfolded protein response
    • Bernales, S.; Papa, F.R.; Walter, P. Intracellular signaling by the unfolded protein response. Annu. Rev. Cell. Dev. Biol. 2006, 22, 487-508.
    • (2006) Annu. Rev. Cell. Dev. Biol. , vol.22 , pp. 487-508
    • Bernales, S.1    Papa, F.R.2    Walter, P.3
  • 8
    • 36248949141 scopus 로고    scopus 로고
    • The endoplasmic reticulum and the unfolded protein response
    • Malhotra, J.D.; Kaufman, R.J. The endoplasmic reticulum and the unfolded protein response. Semin. Cell. Dev. Biol. 2007, 18, 716-731.
    • (2007) Semin. Cell. Dev. Biol. , vol.18 , pp. 716-731
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 9
    • 33846548110 scopus 로고    scopus 로고
    • ER stress and diseases
    • Yoshida, H. ER stress and diseases. FEBS J. 2007, 274, 630-658.
    • (2007) FEBS J. , vol.274 , pp. 630-658
    • Yoshida, H.1
  • 11
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi, Y.; Segal, M.; Normington, K.; Gething, M.J.; Sambrook, J. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 1988, 332, 462-464.
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.J.4    Sambrook, J.5
  • 12
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding, H.P.; Novoa, I.; Zhang, Y.; Zeng, H.; Wek, R.; Schapira, M.; Ron, D. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell. 2000, 6, 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    Ron, D.7
  • 13
    • 73349106233 scopus 로고    scopus 로고
    • Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response
    • Schuck, S.; Prinz, W.A.; Thorn, K.S.; Voss, C.; Walter, P. Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response. J. Cell. Biol. 2009, 187, 525-536.
    • (2009) J. Cell. Biol. , vol.187 , pp. 525-536
    • Schuck, S.1    Prinz, W.A.2    Thorn, K.S.3    Voss, C.4    Walter, P.5
  • 14
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti, A.; Zhang, Y.; Hendershot, L.M.; Harding, H.P.; Ron, D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat. Cell. Biol. 2000, 2, 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
  • 15
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee, A.H.; Iwakoshi, N.N.; Glimcher, L.H. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell. Biol. 2003, 23, 7448-7459.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 16
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
    • Shen, J.; Chen, X.; Hendershot, L.; Prywes, R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell. 2002, 3, 99-111.
    • (2002) Dev. Cell. , vol.3 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 18
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • Tabas, I.; Ron, D. Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Nat. Cell. Biol. 2011, 13, 184-190.
    • (2011) Nat. Cell. Biol. , vol.13 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 19
    • 79955508656 scopus 로고    scopus 로고
    • Attenuation of yeast UPR is essential for survival and is mediated by IRE1 kinase
    • Chawla, A.; Chakrabarti, S.; Ghosh, G.; Niwa, M. Attenuation of yeast UPR is essential for survival and is mediated by IRE1 kinase. J. Cell. Biol. 2011, 193, 41-50.
    • (2011) J. Cell. Biol. , vol.193 , pp. 41-50
    • Chawla, A.1    Chakrabarti, S.2    Ghosh, G.3    Niwa, M.4
  • 20
    • 79955499906 scopus 로고    scopus 로고
    • Homeostatic adaptation to endoplasmic reticulum stress depends on Ire1 kinase activity
    • Rubio, C.; Pincus, D.; Korennykh, A.; Schuck, S.; El-Samad, H.; Walter, P. Homeostatic adaptation to endoplasmic reticulum stress depends on Ire1 kinase activity. J. Cell. Biol. 2011, 193, 171-184.
    • (2011) J. Cell. Biol. , vol.193 , pp. 171-184
    • Rubio, C.1    Pincus, D.2    Korennykh, A.3    Schuck, S.4    El-Samad, H.5    Walter, P.6
  • 22
    • 77953153048 scopus 로고    scopus 로고
    • Regulation of basal cellular physiology by the homeostatic unfolded protein response
    • Rutkowski, D.T.; Hegde, R.S. Regulation of basal cellular physiology by the homeostatic unfolded protein response. J. Cell. Biol. 2010, 189, 783-794.
    • (2010) J. Cell. Biol. , vol.189 , pp. 783-794
    • Rutkowski, D.T.1    Hegde, R.S.2
  • 23
    • 33745222805 scopus 로고    scopus 로고
    • Is (your cellular response to) stress killing you?
    • Sierra, F. Is (your cellular response to) stress killing you? J. Gerontol. 2006, 61, 557-561.
    • (2006) J. Gerontol. , vol.61 , pp. 557-561
    • Sierra, F.1
  • 24
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F.U.; Bracher, A.; Hayer-Hartl, M. Molecular chaperones in protein folding and proteostasis. Nature 2011, 475, 324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 26
    • 79959463520 scopus 로고    scopus 로고
    • Regulation of HSF1 function in the heat stress response: Implications in aging and disease
    • Anckar, J.; Sistonen, L. Regulation of HSF1 function in the heat stress response: Implications in aging and disease. Annu. Rev. Biochem. 2011, 80, 1089-1115.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 1089-1115
    • Anckar, J.1    Sistonen, L.2
  • 27
    • 0026710871 scopus 로고
    • IRE1 encodes a putative protein kinase containing a membranespanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae
    • Nikawa, J.; Yamashita, S. IRE1 encodes a putative protein kinase containing a membranespanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae. Mol. Microbiol. 1992, 6, 1441-1446.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1441-1446
    • Nikawa, J.1    Yamashita, S.2
  • 28
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox, J.S.; Shamu, C.E.; Walter, P. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 1993, 73, 1197-1206.
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 29
    • 0027305620 scopus 로고
    • A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus
    • Mori, K.; Ma, W.; Gething, M.J.; Sambrook J. A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell 1993, 74, 743-756.
    • (1993) Cell , vol.74 , pp. 743-756
    • Mori, K.1    Ma, W.2    Gething, M.J.3    Sambrook, J.4
  • 30
    • 0027314535 scopus 로고
    • Transactivation of the grp78 promoter by Ca2+ depletion. A comparative analysis with A23187 and the endoplasmic reticulum Ca(2+)-ATPase inhibitor thapsigargin
    • Li, W.W.; Alexandre, S.; Cao, X.; Lee, A.S. Transactivation of the grp78 promoter by Ca2+ depletion. A comparative analysis with A23187 and the endoplasmic reticulum Ca(2+)-ATPase inhibitor thapsigargin. J. Biol. Chem. 1993, 268, 12003-12009.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12003-12009
    • Li, W.W.1    Alexandre, S.2    Cao, X.3    Lee, A.S.4
  • 31
    • 0027427636 scopus 로고
    • A hybrid protein kinase-RNase in an interferon-induced pathway?
    • Bork, P.; Sander, C. A hybrid protein kinase-RNase in an interferon-induced pathway? FEBS Lett. 1993, 334, 149-152.
    • (1993) FEBS Lett. , vol.334 , pp. 149-152
    • Bork, P.1    Sander, C.2
  • 32
    • 0030297538 scopus 로고    scopus 로고
    • tRNA ligase is required for regulated mRNA splicing in the unfolded protein response
    • Sidrauski, C.; Cox, J.S.; Walter, P. tRNA ligase is required for regulated mRNA splicing in the unfolded protein response. Cell 1996, 87, 405-413.
    • (1996) Cell , vol.87 , pp. 405-413
    • Sidrauski, C.1    Cox, J.S.2    Walter, P.3
  • 33
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida, H.; Matsui, T.; Yamamoto, A.; Okada, T.; Mori, K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 2001, 107, 881-891.
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 34
    • 26844439863 scopus 로고    scopus 로고
    • An essential dimer-forming subregion of the endoplasmic reticulum stress sensor Ire1
    • Oikawa, D.; Kimata, Y.; Takeuchi, M.; Kohno, K. An essential dimer-forming subregion of the endoplasmic reticulum stress sensor Ire1. Biochem. J. 2005, 391, 135-142.
    • (2005) Biochem. J. , vol.391 , pp. 135-142
    • Oikawa, D.1    Kimata, Y.2    Takeuchi, M.3    Kohno, K.4
  • 35
    • 8444250981 scopus 로고    scopus 로고
    • A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1
    • Kimata, Y.; Oikawa, D.; Shimizu, Y.; Ishiwata-Kimata, Y.; Kohno, K. A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1. J. Cell. Biol. 2004, 167, 445-456.
    • (2004) J. Cell. Biol. , vol.167 , pp. 445-456
    • Kimata, Y.1    Oikawa, D.2    Shimizu, Y.3    Ishiwata-Kimata, Y.4    Kohno, K.5
  • 36
    • 80053369081 scopus 로고    scopus 로고
    • Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response
    • Gardner, B.M.; Walter, P. Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response. Science 2011, 333, 1891-1894.
    • (2011) Science , vol.333 , pp. 1891-1894
    • Gardner, B.M.1    Walter, P.2
  • 37
    • 35348967427 scopus 로고    scopus 로고
    • Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins
    • Kimata, Y.; Ishiwata-Kimata, Y.; Ito, T.; Hirata, A.; Suzuki, T.; Oikawa, D.; Takeuchi, M.; Kohno, K. Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins. J. Cell. Biol. 2007, 179, 75-86.
    • (2007) J. Cell. Biol. , vol.179 , pp. 75-86
    • Kimata, Y.1    Ishiwata-Kimata, Y.2    Ito, T.3    Hirata, A.4    Suzuki, T.5    Oikawa, D.6    Takeuchi, M.7    Kohno, K.8
  • 39
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • Cox, J.S.; Walter, P. A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 1996, 87, 391-404.
    • (1996) Cell , vol.87 , pp. 391-404
    • Cox, J.S.1    Walter, P.2
  • 40
    • 33745893809 scopus 로고    scopus 로고
    • Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response
    • Hollien, J.; Weissman, J.S. Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Science 2006, 313, 104-107.
    • (2006) Science , vol.313 , pp. 104-107
    • Hollien, J.1    Weissman, J.S.2
  • 42
    • 68049110633 scopus 로고    scopus 로고
    • IRE1alpha kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates
    • Han, D.; Lerner, A.G.; Vande, W.L.; Upton, J.P.; Xu, W.; Hagen, A.; Backes. B.J.; Oakes, S.A.; Papa, F.R. IRE1alpha kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates. Cell 2009, 138, 562-575.
    • (2009) Cell , vol.138 , pp. 562-575
    • Han, D.1    Lerner, A.G.2    Vande, W.L.3    Upton, J.P.4    Xu, W.5    Hagen, A.6    Backes, B.J.7    Oakes, S.A.8    Papa, F.R.9
  • 45
    • 58449084895 scopus 로고    scopus 로고
    • Divergent effects of PERK and IRE1 signaling on cell viability
    • Lin, J.H.; Li, H.; Zhang, Y.; Ron, D.; Walter, P. Divergent effects of PERK and IRE1 signaling on cell viability. PLoS One 2009, 4, e4170.
    • (2009) PLoS One , vol.4
    • Lin, J.H.1    Li, H.2    Zhang, Y.3    Ron, D.4    Walter, P.5
  • 46
    • 84864577751 scopus 로고    scopus 로고
    • The Yeast Rab GTPase Ypt1 Modulates Unfolded Protein Response Dynamics by Regulating the Stability of HAC1 RNA
    • Tsvetanova, N.G.; Riordan, D.P.; Brown, P.O. The Yeast Rab GTPase Ypt1 Modulates Unfolded Protein Response Dynamics by Regulating the Stability of HAC1 RNA. PLoS Gen. 2012, 8, e1002862.
    • (2012) PLoS Gen. , vol.8
    • Tsvetanova, N.G.1    Riordan, D.P.2    Brown, P.O.3
  • 47
    • 0031282636 scopus 로고    scopus 로고
    • Translational attenuation mediated by an mRNA intron
    • Chapman, R.E.; Walter, P. Translational attenuation mediated by an mRNA intron. Curr. Biol. 1997, 7, 850-859.
    • (1997) Curr. Biol. , vol.7 , pp. 850-859
    • Chapman, R.E.1    Walter, P.2
  • 48
    • 0030808558 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced mRNA splicing permits synthesis of transcription factor Hac1p/Ern4p that activates the unfolded protein response
    • Kawahara, T.; Yanagi, H.; Yura, T.; Mori, K. Endoplasmic reticulum stress-induced mRNA splicing permits synthesis of transcription factor Hac1p/Ern4p that activates the unfolded protein response. Mol. Biol. Cell. 1997, 8, 1845-1862.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 1845-1862
    • Kawahara, T.1    Yanagi, H.2    Yura, T.3    Mori, K.4
  • 49
    • 77955023666 scopus 로고    scopus 로고
    • BiP binding to the ER-stress sensor Ire1 tunes the homeostatic behavior of the unfolded protein response
    • Pincus, D.; Chevalier, M.W.; Aragon, T.; van Anken, E.; Vidal, S.E.; El-Samad, H.; Walter, P. BiP binding to the ER-stress sensor Ire1 tunes the homeostatic behavior of the unfolded protein response. PLoS Biol. 2010, 8, e1000415.
    • (2010) PLoS Biol. , vol.8
    • Pincus, D.1    Chevalier, M.W.2    Aragon, T.3    van Anken, E.4    Vidal, S.E.5    El-Samad, H.6    Walter, P.7
  • 50
    • 0035812716 scopus 로고    scopus 로고
    • Block of HAC1 mRNA translation by long-range base pairing is released by cytoplasmic splicing upon induction of the unfolded protein response
    • Ruegsegger, U.; Leber, J.H.; Walter, P. Block of HAC1 mRNA translation by long-range base pairing is released by cytoplasmic splicing upon induction of the unfolded protein response. Cell 2001, 107, 103-114.
    • (2001) Cell , vol.107 , pp. 103-114
    • Ruegsegger, U.1    Leber, J.H.2    Walter, P.3
  • 51
    • 57049117856 scopus 로고    scopus 로고
    • Cell death and endoplasmic reticulum stress: Disease relevance and therapeutic opportunities
    • Kim, I.; Xu, W.; Reed, J.C. Cell death and endoplasmic reticulum stress: Disease relevance and therapeutic opportunities. Nat. Rev. Drug Dis. 2008, 7, 1013-1030.
    • (2008) Nat. Rev. Drug Dis. , vol.7 , pp. 1013-1030
    • Kim, I.1    Xu, W.2    Reed, J.C.3
  • 52
    • 0029903049 scopus 로고    scopus 로고
    • Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
    • Shamu, C.E.; Walter, P. Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 1996, 15, 3028-3039.
    • (1996) EMBO J. , vol.15 , pp. 3028-3039
    • Shamu, C.E.1    Walter, P.2
  • 53
    • 77953501690 scopus 로고    scopus 로고
    • BiP availability distinguishes states of homeostasis and stress in the endoplasmic reticulum of living cells
    • Lai, C.W.; Aronson, D.E.; Snapp, E.L. BiP availability distinguishes states of homeostasis and stress in the endoplasmic reticulum of living cells. Mol. Biol. Cell. 2010, 21, 1909-19021.
    • (2010) Mol. Biol. Cell. , vol.21 , pp. 1909-19021
    • Lai, C.W.1    Aronson, D.E.2    Snapp, E.L.3
  • 54
    • 77958016968 scopus 로고    scopus 로고
    • Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering
    • Li, H.; Korennykh, A.V.; Behrman, S.L.; Walter, P. Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering. Proc. Natl. Acad. Sci. USA 2010, 107, 16113-16118.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 16113-16118
    • Li, H.1    Korennykh, A.V.2    Behrman, S.L.3    Walter, P.4
  • 56
    • 37649004940 scopus 로고    scopus 로고
    • Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing
    • Lee, K.P.; Dey, M.; Neculai, D.; Cao, C.; Dever, T.E.; Sicheri, F. Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing. Cell 2008, 132, 89-100.
    • (2008) Cell , vol.132 , pp. 89-100
    • Lee, K.P.1    Dey, M.2    Neculai, D.3    Cao, C.4    Dever, T.E.5    Sicheri, F.6
  • 57
    • 0037166303 scopus 로고    scopus 로고
    • The protein kinase/endoribonuclease IRE1alpha that signals the unfolded protein response has a luminal N-terminal ligand-independent dimerization domain
    • Liu, C.Y.; Wong, H.N.; Schauerte, J.A.; Kaufman, R.J. The protein kinase/endoribonuclease IRE1alpha that signals the unfolded protein response has a luminal N-terminal ligand-independent dimerization domain. J. Biol. Chem. 2002, 277, 18346-18356.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18346-18356
    • Liu, C.Y.1    Wong, H.N.2    Schauerte, J.A.3    Kaufman, R.J.4
  • 59
    • 80052825784 scopus 로고    scopus 로고
    • Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum stress sensor Ire1 in different ways
    • Promlek, T.; Ishiwata-Kimata, Y.; Shido, M.; Sakuramoto, M.; Kohno, K.; Kimata, Y. Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum stress sensor Ire1 in different ways. Mol. Biol. Cell. 2011, 22, 3520-3532.
    • (2011) Mol. Biol. Cell. , vol.22 , pp. 3520-3532
    • Promlek, T.1    Ishiwata-Kimata, Y.2    Shido, M.3    Sakuramoto, M.4    Kohno, K.5    Kimata, Y.6
  • 60
    • 33749233991 scopus 로고    scopus 로고
    • The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response
    • Zhou, J.; Liu, C.Y.; Back, S.H.; Clark, R.L.; Peisach, D.; Xu, Z.; Kaufman, R.J. The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. Proc. Natl. Acad. Sci. USA 2006, 103, 14343-14348.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 14343-14348
    • Zhou, J.1    Liu, C.Y.2    Back, S.H.3    Clark, R.L.4    Peisach, D.5    Xu, Z.6    Kaufman, R.J.7
  • 63
    • 77950887221 scopus 로고    scopus 로고
    • Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1
    • Wiseman, R.L.; Zhang, Y.; Lee, K.P.; Harding, H.P.; Haynes, C.M.; Price, J.; Sicheri, F.; Ron, D. Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1. Mol. Cell. 2010, 38, 291-304.
    • (2010) Mol. Cell. , vol.38 , pp. 291-304
    • Wiseman, R.L.1    Zhang, Y.2    Lee, K.P.3    Harding, H.P.4    Haynes, C.M.5    Price, J.6    Sicheri, F.7    Ron, D.8
  • 64
    • 84855496731 scopus 로고    scopus 로고
    • The unfolded protein response supports cellular robustness as a broad-spectrum compensatory pathway
    • Thibault, G.; Ismail, N.; Ng, D.T. The unfolded protein response supports cellular robustness as a broad-spectrum compensatory pathway. Proc. Natl. Acad. Sci. USA 2011, 108, 20597-20602.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 20597-20602
    • Thibault, G.1    Ismail, N.2    Ng, D.T.3
  • 65
    • 77955410103 scopus 로고    scopus 로고
    • Modeling the endoplasmic reticulum unfolded protein response
    • Onn, A.; Ron, D. Modeling the endoplasmic reticulum unfolded protein response. Nat. Struct. Mol. Biol. 2010, 17, 924-925.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 924-925
    • Onn, A.1    Ron, D.2
  • 66
    • 34249707984 scopus 로고    scopus 로고
    • Self-association and BiP dissociation are not sufficient for activation of the ER stress sensor Ire1
    • Oikawa, D.; Kimata, Y.; Kohno, K. Self-association and BiP dissociation are not sufficient for activation of the ER stress sensor Ire1. J. Cell. Sci. 2007, 120, 1681-1688.
    • (2007) J. Cell. Sci. , vol.120 , pp. 1681-1688
    • Oikawa, D.1    Kimata, Y.2    Kohno, K.3
  • 67
    • 0024395160 scopus 로고
    • Cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP
    • Normington, K.; Kohno, K.; Kozutsumi, Y.; Gething, M.J.; Sambrook, J.S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell 1989, 57, 1223-1236.
    • (1989) Cell , vol.57 , pp. 1223-1236
    • Normington, K.1    Kohno, K.2    Kozutsumi, Y.3    Gething, M.J.4    Sambrook, J.S.5
  • 68
    • 0038043221 scopus 로고    scopus 로고
    • Structure and intermolecular interactions of the luminal dimerization domain of human IRE1alpha
    • Liu, C.Y.; Xu, Z.; Kaufman, R.J. Structure and intermolecular interactions of the luminal dimerization domain of human IRE1alpha. J. Biol. Chem. 2003, 278, 17680-17687.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17680-17687
    • Liu, C.Y.1    Xu, Z.2    Kaufman, R.J.3
  • 69
    • 0033208953 scopus 로고    scopus 로고
    • Role and regulation of the ER chaperone BiP
    • Gething, M.J. Role and regulation of the ER chaperone BiP. Semin. Cell. Dev. Biol. 1999, 10, 465-472.
    • (1999) Semin. Cell. Dev. Biol. , vol.10 , pp. 465-472
    • Gething, M.J.1
  • 71
    • 7444240833 scopus 로고    scopus 로고
    • The ER function BiP is a master regulator of ER function
    • Hendershot, L.M. The ER function BiP is a master regulator of ER function. Mt. Sinai. J. Med. 2004, 71, 289-297.
    • (2004) Mt. Sinai. J. Med. , vol.71 , pp. 289-297
    • Hendershot, L.M.1
  • 73
    • 0027465942 scopus 로고
    • The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum
    • Kohno, K.; Normington, K.; Sambrook, J.; Gething, M.J.; Mori, K. The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum. Mol. Cell. Biol. 1993, 13, 877-890.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 877-890
    • Kohno, K.1    Normington, K.2    Sambrook, J.3    Gething, M.J.4    Mori, K.5
  • 75
    • 0034694896 scopus 로고    scopus 로고
    • Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast
    • Okamura, K.; Kimata, Y.; Higashio, H.; Tsuru, A.; Kohno, K. Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast. Biochem. Biophys. Res. Commun. 2000, 279, 445-450.
    • (2000) Biochem. Biophys. Res. Commun. , vol.279 , pp. 445-450
    • Okamura, K.1    Kimata, Y.2    Higashio, H.3    Tsuru, A.4    Kohno, K.5
  • 77
    • 0025291580 scopus 로고
    • Membrane biogenesis during B cell differentiation: Most endoplasmic reticulum proteins are expressed coordinately
    • Wiest, D.L.; Burkhardt, J.K.; Hester, S.; Hortsch, M.; Meyer, D.I.; Argon, Y. Membrane biogenesis during B cell differentiation: Most endoplasmic reticulum proteins are expressed coordinately. J. Cell. Biol. 1990, 110, 1501-1511.
    • (1990) J. Cell. Biol. , vol.110 , pp. 1501-1511
    • Wiest, D.L.1    Burkhardt, J.K.2    Hester, S.3    Hortsch, M.4    Meyer, D.I.5    Argon, Y.6
  • 78
    • 84857227073 scopus 로고    scopus 로고
    • ER stress regulation of the Kar2p/BiP chaperone alleviates proteotoxicity via dual degradation pathways
    • Hsu, C.L.; Prasad, R.; Blackman, C.; Ng, D.T. ER stress regulation of the Kar2p/BiP chaperone alleviates proteotoxicity via dual degradation pathways. Mol. Biol. Cell. 2012, 23, 630-641.
    • (2012) Mol. Biol. Cell. , vol.23 , pp. 630-641
    • Hsu, C.L.1    Prasad, R.2    Blackman, C.3    Ng, D.T.4
  • 79
    • 0038308388 scopus 로고    scopus 로고
    • Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins
    • Kimata, Y.; Kimata, Y.I.; Shimizu, Y.; Abe, H.; Farcasanu, I.C.; Takeuchi, M.; Rose, M.D.; Kohno, K. Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins. Mol. Biol. Cell. 2003, 14, 2559-2569.
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 2559-2569
    • Kimata, Y.1    Kimata, Y.I.2    Shimizu, Y.3    Abe, H.4    Farcasanu, I.C.5    Takeuchi, M.6    Rose, M.D.7    Kohno, K.8
  • 80
    • 0034637605 scopus 로고    scopus 로고
    • Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum
    • Liu, C.Y.; Schroder, M.; Kaufman, R.J. Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum. J. Biol. Chem. 2000, 275, 24881-24885.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24881-24885
    • Liu, C.Y.1    Schroder, M.2    Kaufman, R.J.3
  • 81
    • 0031054643 scopus 로고    scopus 로고
    • Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins
    • Morris, J.A.; Dorner, A.J.; Edwards, C.A.; Hendershot, L.M.; Kaufman, R.J. Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins. J. Biol. Chem. 1997, 272, 4327-4334.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4327-4334
    • Morris, J.A.1    Dorner, A.J.2    Edwards, C.A.3    Hendershot, L.M.4    Kaufman, R.J.5
  • 82
    • 3242892326 scopus 로고    scopus 로고
    • Protein transport into canine pancreatic microsomes: A quantitative approach
    • Guth, S.; Volzing, C.; Muller, A.; Jung, M.; Zimmermann, R. Protein transport into canine pancreatic microsomes: a quantitative approach. Eur. J. Biochem. 2004, 271, 3200-3207.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3200-3207
    • Guth, S.1    Volzing, C.2    Muller, A.3    Jung, M.4    Zimmermann, R.5
  • 85
    • 84858042337 scopus 로고    scopus 로고
    • ERdj4 protein is a soluble endoplasmic reticulum (ER) DnaJ family protein that interacts with ER-associated degradation machinery
    • Lai, C.W.; Otero, J.H.; Hendershot, L.M.; Snapp, E. ERdj4 protein is a soluble endoplasmic reticulum (ER) DnaJ family protein that interacts with ER-associated degradation machinery. J. Biol. Chem. 2012, 287, 7969-7978.
    • (2012) J. Biol. Chem. , vol.287 , pp. 7969-7978
    • Lai, C.W.1    Otero, J.H.2    Hendershot, L.M.3    Snapp, E.4
  • 86
    • 67651045789 scopus 로고    scopus 로고
    • Activation of mammalian IRE1alpha upon ER stress depends on dissociation of BiP rather than on direct interaction with unfolded proteins
    • Oikawa, D.; Kimata, Y.; Kohno, K.; Iwawaki, T. Activation of mammalian IRE1alpha upon ER stress depends on dissociation of BiP rather than on direct interaction with unfolded proteins. Exp. Cell. Res. 2009, 315, 2496-2504.
    • (2009) Exp. Cell. Res. , vol.315 , pp. 2496-2504
    • Oikawa, D.1    Kimata, Y.2    Kohno, K.3    Iwawaki, T.4
  • 87
    • 79551632223 scopus 로고    scopus 로고
    • Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions
    • Marcinowski, M.; Holler, M.; Feige, M.J.; Baerend, D.; Lamb, D.C.; Buchner, J. Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Nat. Struct. Mol. Biol. 2011, 18, 150-158.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 150-158
    • Marcinowski, M.1    Holler, M.2    Feige, M.J.3    Baerend, D.4    Lamb, D.C.5    Buchner, J.6
  • 88
    • 0034896499 scopus 로고    scopus 로고
    • Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release
    • Vanhove, M.; Usherwood, Y.K.; Hendershot, L.M. Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release. Immunity 2001, 15, 105-114.
    • (2001) Immunity , vol.15 , pp. 105-114
    • Vanhove, M.1    Usherwood, Y.K.2    Hendershot, L.M.3
  • 89
    • 84857868016 scopus 로고    scopus 로고
    • Kar2p Availability Defines Distinct Forms of Endoplasmic Reticulum Stress in Living Cells
    • doi: 10.1091/mbc.E11-12-0995
    • Lajoie, P.; Moir, R.D.; Willis, I.M.; Snapp, E.L. Kar2p Availability Defines Distinct Forms of Endoplasmic Reticulum Stress in Living Cells. Mol. Biol. Cell. 2012, doi: 10.1091/mbc.E11-12-0995.
    • (2012) Mol. Biol. Cell.
    • Lajoie, P.1    Moir, R.D.2    Willis, I.M.3    Snapp, E.L.4
  • 90
    • 33751333201 scopus 로고    scopus 로고
    • Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway
    • Kang, S.W.; Rane, N.S.; Kim, S.J.; Garrison, J.L.; Taunton, J.; Hegde, R.S. Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway. Cell 2006, 127, 999-1013.
    • (2006) Cell , vol.127 , pp. 999-1013
    • Kang, S.W.1    Rane, N.S.2    Kim, S.J.3    Garrison, J.L.4    Taunton, J.5    Hegde, R.S.6
  • 92
    • 14444280363 scopus 로고    scopus 로고
    • Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum
    • Kuznetsov, G.; Chen, L.B.; Nigam, S.K. Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum. J. Biol. Chem. 1997, 272, 3057-3063.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3057-3063
    • Kuznetsov, G.1    Chen, L.B.2    Nigam, S.K.3
  • 93
    • 84866455655 scopus 로고    scopus 로고
    • ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load
    • Chambers, J.E.; Petrova, K.; Tomba, G.; Vendruscolo, M.; Ron, D. ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load. J. Cell. Biol. 2012, 198, 371-385.
    • (2012) J. Cell. Biol. , vol.198 , pp. 371-385
    • Chambers, J.E.1    Petrova, K.2    Tomba, G.3    Vendruscolo, M.4    Ron, D.5
  • 94
    • 0026567520 scopus 로고
    • Interconversion of three differentially modified and assembled forms of BiP
    • Freiden, P.J.; Gaut, J.R.; Hendershot, L.M. Interconversion of three differentially modified and assembled forms of BiP. EMBO J. 1992, 11, 63-70.
    • (1992) EMBO J. , vol.11 , pp. 63-70
    • Freiden, P.J.1    Gaut, J.R.2    Hendershot, L.M.3
  • 95
    • 0024846211 scopus 로고
    • ADP-ribosylation of the 78-kDa glucose-regulated protein during nutritional stress
    • Leno, G.H.; Ledford, B.E. ADP-ribosylation of the 78-kDa glucose-regulated protein during nutritional stress. FEBS J. 1989, 186, 205-211.
    • (1989) FEBS J. , vol.186 , pp. 205-211
    • Leno, G.H.1    Ledford, B.E.2
  • 96
    • 0023684672 scopus 로고
    • Identity of the immunoglobulin heavy-chain-binding protein with the 78,000-dalton glucose-regulated protein and the role of posttranslational modifications in its binding function
    • Hendershot, L.M.; Ting, J.; Lee, A.S. Identity of the immunoglobulin heavy-chain-binding protein with the 78,000-dalton glucose-regulated protein and the role of posttranslational modifications in its binding function. Mol. Cell. Biol. 1988, 8, 4250-4256.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4250-4256
    • Hendershot, L.M.1    Ting, J.2    Lee, A.S.3
  • 97
    • 0032897211 scopus 로고    scopus 로고
    • The dynamic role of GRP78/BiP in the coordination of mRNA translation with protein processing
    • Laitusis, A.L.; Brostrom, M.A.; Brostrom, C.O. The dynamic role of GRP78/BiP in the coordination of mRNA translation with protein processing. J. Biol. Chem. 1999, 274, 486-493.
    • (1999) J. Biol. Chem. , vol.274 , pp. 486-493
    • Laitusis, A.L.1    Brostrom, M.A.2    Brostrom, C.O.3
  • 98
    • 0020807492 scopus 로고
    • ADP-ribosylation of the Mr 83,000 stress-inducible and glucoseregulated protein in avian and mammalian cells: Modulation by heat shock and glucose starvation
    • Carlsson, L.; Lazarides, E. ADP-ribosylation of the Mr 83,000 stress-inducible and glucoseregulated protein in avian and mammalian cells: modulation by heat shock and glucose starvation. Proc. Natl. Acad. Sci. USA 1983, 80, 4664-4668.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 4664-4668
    • Carlsson, L.1    Lazarides, E.2
  • 99
    • 0021254977 scopus 로고
    • Density of newly synthesized plasma membrane proteins in intracellular membranes. I. Stereological studies
    • Griffiths, G.; Warren, G.; Quinn, P.; Mathieu-Costello, O.; Hoppeler, H. Density of newly synthesized plasma membrane proteins in intracellular membranes. I. Stereological studies. J. Cell. Biol. 1984, 98, 2133-2141.
    • (1984) J. Cell. Biol. , vol.98 , pp. 2133-2141
    • Griffiths, G.1    Warren, G.2    Quinn, P.3    Mathieu-Costello, O.4    Hoppeler, H.5
  • 100
    • 33847324367 scopus 로고    scopus 로고
    • Lobe IB of the ATPase domain of Kar2p/BiP interacts with Ire1p to negatively regulate the unfolded protein response in Saccharomyces cerevisiae
    • Todd-Corlett, A.; Jones, E.; Seghers, C.; Gething, M.J. Lobe IB of the ATPase domain of Kar2p/BiP interacts with Ire1p to negatively regulate the unfolded protein response in Saccharomyces cerevisiae. J. Mol. Biol. 2007, 3, 67,770-787.
    • (2007) J. Mol. Biol. , vol.3
    • Todd-Corlett, A.1    Jones, E.2    Seghers, C.3    Gething, M.J.4
  • 101
    • 0030879870 scopus 로고    scopus 로고
    • The unfolded protein response coordinates the production of endoplasmic reticulum membrane
    • Cox, J.S.; Chapman, R.E.; Walter, P. The unfolded protein response coordinates the production of endoplasmic reticulum membrane. Mol. Biol. Cell. 1997, 8, 1805-1814.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 1805-1814
    • Cox, J.S.1    Chapman, R.E.2    Walter, P.3
  • 102
    • 0029860982 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae IRE2/HAC1 is involved in IRE1-mediated KAR2 expression
    • Nikawa, J.; Akiyoshi, M.; Hirata, S.; Fukuda, T. Saccharomyces cerevisiae IRE2/HAC1 is involved in IRE1-mediated KAR2 expression. Nucleic. Acids Res. 1996, 24, 4222-4226.
    • (1996) Nucleic. Acids Res. , vol.24 , pp. 4222-4226
    • Nikawa, J.1    Akiyoshi, M.2    Hirata, S.3    Fukuda, T.4
  • 103
    • 0034712734 scopus 로고    scopus 로고
    • mRNA splicing-mediated C-terminal replacement of transcription factor Hac1p is required for efficient activation of the unfolded protein response
    • Mori, K.; Ogawa, N.; Kawahara, T.; Yanagi, H.; Yura, T. mRNA splicing-mediated C-terminal replacement of transcription factor Hac1p is required for efficient activation of the unfolded protein response. Proc. Natl. Acad. Sci. USA 2000, 97, 4660-4665.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4660-4665
    • Mori, K.1    Ogawa, N.2    Kawahara, T.3    Yanagi, H.4    Yura, T.5
  • 104
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers, K.J.; Patil, C.K.; Wodicka, L.; Lockhart, D.J.; Weissman, J.S.; Walter, P. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 2000, 101, 249-258.
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 105
    • 14044266853 scopus 로고    scopus 로고
    • Gene recruitment of the activated INO1 locus to the nuclear membrane
    • Brickner, J.H.; Walter, P. Gene recruitment of the activated INO1 locus to the nuclear membrane. PLoS Biol. 2004, 2, e342.
    • (2004) PLoS Biol. , vol.2
    • Brickner, J.H.1    Walter, P.2
  • 107
    • 69749123786 scopus 로고    scopus 로고
    • Fine-tuning of the unfolded protein response: Assembling the IRE1alpha interactome
    • Hetz, C.; Glimcher, L.H. Fine-tuning of the unfolded protein response: Assembling the IRE1alpha interactome. Mol. Cell. 2009, 35, 551-561.
    • (2009) Mol. Cell. , vol.35 , pp. 551-561
    • Hetz, C.1    Glimcher, L.H.2
  • 108
    • 80054722420 scopus 로고    scopus 로고
    • The unfolded protein response: Integrating stress signals through the stress sensor IRE1alpha
    • Hetz, C.; Martinon, F.; Rodriguez, D.; Glimcher, L.H. The unfolded protein response: Integrating stress signals through the stress sensor IRE1alpha. Physiol Rev. 2011, 91, 1219-1243.
    • (2011) Physiol Rev. , vol.91 , pp. 1219-1243
    • Hetz, C.1    Martinon, F.2    Rodriguez, D.3    Glimcher, L.H.4
  • 110
    • 18744382408 scopus 로고    scopus 로고
    • Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha
    • Marcu, M.G.; Doyle, M.; Bertolotti, A.; Ron, D.; Hendershot, L.; Neckers, L. Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha. Mol. Cell. Biol. 2002, 22, 8506-8513.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8506-8513
    • Marcu, M.G.1    Doyle, M.2    Bertolotti, A.3    Ron, D.4    Hendershot, L.5    Neckers, L.6
  • 111
    • 33646844964 scopus 로고    scopus 로고
    • The affinity of a major Ca2+ binding site on GRP78 is differentially enhanced by ADP and ATP
    • Lamb, H.K.; Mee, C.; Xu, W.; Liu, L.; Blond, S.; Cooper, A.; Charles, I.G.; Hawkins, A.R. The affinity of a major Ca2+ binding site on GRP78 is differentially enhanced by ADP and ATP. J. Biol. Chem. 2006, 281, 8796-8805.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8796-8805
    • Lamb, H.K.1    Mee, C.2    Xu, W.3    Liu, L.4    Blond, S.5    Cooper, A.6    Charles, I.G.7    Hawkins, A.R.8
  • 112
    • 33750534382 scopus 로고    scopus 로고
    • Dcr2 targets Ire1 and downregulates the unfolded protein response in Saccharomyces cerevisiae
    • Guo, J.; Polymenis, M. Dcr2 targets Ire1 and downregulates the unfolded protein response in Saccharomyces cerevisiae. EMBO Rep. 2006, 7, 1124-1127.
    • (2006) EMBO Rep. , vol.7 , pp. 1124-1127
    • Guo, J.1    Polymenis, M.2
  • 113
    • 0031948846 scopus 로고    scopus 로고
    • Protein serine/threonine phosphatase Ptc2p negatively regulates the unfolded-protein response by dephosphorylating Ire1p kinase
    • Welihinda, A.A.; Tirasophon, W.; Green, S.R.; Kaufman, R.J. Protein serine/threonine phosphatase Ptc2p negatively regulates the unfolded-protein response by dephosphorylating Ire1p kinase. Mol. Cell. Biol. 1998, 18, 1967-1977.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1967-1977
    • Welihinda, A.A.1    Tirasophon, W.2    Green, S.R.3    Kaufman, R.J.4
  • 115
    • 41949129594 scopus 로고    scopus 로고
    • Heat shock response relieves ER stress
    • Liu, Y.; Chang, A. Heat shock response relieves ER stress. EMBO J. 2008, 27, 1049-1059.
    • (2008) EMBO J. , vol.27 , pp. 1049-1059
    • Liu, Y.1    Chang, A.2
  • 116
    • 33745590436 scopus 로고    scopus 로고
    • Intrinsic capacities of molecular sensors of the unfolded protein response to sense alternate forms of endoplasmic reticulum stress
    • DuRose, J.B.; Tam, A.B.; Niwa, M. Intrinsic capacities of molecular sensors of the unfolded protein response to sense alternate forms of endoplasmic reticulum stress. Mol. Biol. Cell. 2006, 17, 3095-3107.
    • (2006) Mol. Biol. Cell. , vol.17 , pp. 3095-3107
    • DuRose, J.B.1    Tam, A.B.2    Niwa, M.3
  • 117
    • 79956352017 scopus 로고    scopus 로고
    • Selective activation of the transcription factor ATF6 mediates endoplasmic reticulum proliferation triggered by a membrane protein
    • Maiuolo, J.; Bulotta, S.; Verderio, C.; Benfante, R.; Borgese, N. Selective activation of the transcription factor ATF6 mediates endoplasmic reticulum proliferation triggered by a membrane protein. Proc. Natl. Acad. Sci. USA. 2011, 108, 7832-7837.
    • (2011) Proc. Natl. Acad. Sci. USA. , vol.108 , pp. 7832-7837
    • Maiuolo, J.1    Bulotta, S.2    Verderio, C.3    Benfante, R.4    Borgese, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.