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Volumn 41, Issue 2, 2013, Pages 235-262

Xenobiotic perturbation of ER stress and the unfolded protein response

Author keywords

ATF6; ER stress; IRE1; PERK; unfolded protein response; xenobiotic

Indexed keywords

4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; 4 PHENYLBUTYRIC ACID; ACETYLCYSTEINE; ATAZANAVIR; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; BREFELDIN A; CELECOXIB; DANTROLENE; DITHIOTHREITOL; EEYERESTATIN I; FLAVONOID; FLUSPIRILENE; GSK 2606414; GUANABENZ; INDOMETACIN; LITHIUM; LOPINAVIR; NELFINAVIR; RESVERATROL; RITONAVIR; SALUBRINAL; SORAFENIB; STF 083010; THAPSIGARGIN; TUNICAMYCIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; VALPROIC ACID; VERSIPELOSTATIN; XENOBIOTIC AGENT;

EID: 84875734137     PISSN: 01926233     EISSN: 15331601     Source Type: Journal    
DOI: 10.1177/0192623312470764     Document Type: Article
Times cited : (25)

References (307)
  • 1
    • 69549135927 scopus 로고    scopus 로고
    • Hepatic CYP3A suppression by high concentrations of proteasomal inhibitors: A consequence of endoplasmic reticulum (ER) stress induction, activation of RNA-dependent protein kinase-like ER-bound eukaryotic initiation factor 2alpha (eIF2alpha)-kinase (PERK) and general control nonderepressible-2 eIF2alpha kinase (GCN2), and global translational shutoff
    • Acharya P., Engel J. C., Correia M. A.. Hepatic CYP3A suppression by high concentrations of proteasomal inhibitors: A consequence of endoplasmic reticulum (ER) stress induction, activation of RNA-dependent protein kinase-like ER-bound eukaryotic initiation factor 2alpha (eIF2alpha)-kinase (PERK) and general control nonderepressible-2 eIF2alpha kinase (GCN2), and global translational shutoff. Mol Pharmacol. 2009 ; 76: 503-15
    • (2009) Mol Pharmacol , vol.76 , pp. 503-515
    • Acharya, P.1    Engel, J.C.2    Correia, M.A.3
  • 3
    • 72149113307 scopus 로고    scopus 로고
    • Inhibition of hepatic carnitine palmitoyl-transferase i (CPT IA) by valproyl-CoA as a possible mechanism of valproate-induced steatosis
    • Aires C. C., Ijlst L., Stet F., Prip-Buus C., de Almeida I. T., Duran M., Wanders R. J., Silva M. F.. Inhibition of hepatic carnitine palmitoyl-transferase I (CPT IA) by valproyl-CoA as a possible mechanism of valproate-induced steatosis. Biochem Pharmacol. 2010 ; 79: 792-99
    • (2010) Biochem Pharmacol , vol.79 , pp. 792-799
    • Aires, C.C.1    Ijlst, L.2    Stet, F.3    Prip-Buus, C.4    De Almeida, I.T.5    Duran, M.6    Wanders, R.J.7    Silva, M.F.8
  • 5
    • 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. Ann Rev Biochem. 2011 ; 80: 1089-115
    • (2011) Ann Rev Biochem , vol.80 , pp. 1089-1115
    • Anckar, J.1    Sistonen, L.2
  • 7
    • 84861222698 scopus 로고    scopus 로고
    • The specialized unfolded protein response of B lymphocytes: ATF6alpha-independent development of antibody-secreting B cells
    • Aragon I. V., Barrington R. A., Jackowski S., Mori K., Brewer J. W.. The specialized unfolded protein response of B lymphocytes: ATF6alpha-independent development of antibody-secreting B cells. Mol Immunol. 2012 ; 51: 347-55
    • (2012) Mol Immunol , vol.51 , pp. 347-355
    • Aragon, I.V.1    Barrington, R.A.2    Jackowski, S.3    Mori, K.4    Brewer, J.W.5
  • 8
    • 27944432606 scopus 로고    scopus 로고
    • Modulating the endoplasmic reticulum stress response with trans-4,5-dihydroxy-1,2-dithiane prevents chemically induced renal injury in vivo
    • Asmellash S., Stevens J. L., Ichimura T.. Modulating the endoplasmic reticulum stress response with trans-4,5-dihydroxy-1,2-dithiane prevents chemically induced renal injury in vivo. Toxicol Sci. 2005 ; 88: 576-84
    • (2005) Toxicol Sci , vol.88 , pp. 576-584
    • Asmellash, S.1    Stevens, J.L.2    Ichimura, T.3
  • 9
    • 43649100018 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis
    • Atkin J. D., Farg M. A., Walker A. K., McLean C., Tomas D., Horne M. K.. Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis. Neurobiol Dis. 2008 ; 30: 400-407
    • (2008) Neurobiol Dis , vol.30 , pp. 400-407
    • Atkin, J.D.1    Farg, M.A.2    Walker, A.K.3    McLean, C.4    Tomas, D.5    Horne, M.K.6
  • 10
    • 68949209955 scopus 로고    scopus 로고
    • The unfolded protein response in health and disease
    • Austin R. C.. The unfolded protein response in health and disease. Antioxid Redox Signal. 2009 ; 11: 2279-87
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2279-2287
    • Austin, R.C.1
  • 14
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N. F., Sampat R. M., Kopito R. R.. Impairment of the ubiquitin-proteasome system by protein aggregation. Science. 2001 ; 292: 1552-55
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 15
    • 33845480131 scopus 로고    scopus 로고
    • Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response
    • Bernales S., McDonald K. L., Walter P.. Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. PLoS Biol. 2006 ; 4: e423
    • (2006) PLoS Biol , vol.4 , pp. 423
    • Bernales, S.1    McDonald, K.L.2    Walter, P.3
  • 17
    • 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: 326-32
    • (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
  • 18
    • 34047192683 scopus 로고    scopus 로고
    • Review. The endoplasmic reticulum: A target for new anticancer drugs
    • Boelens J., Lust S., Offner F., Bracke M. E., Vanhoecke B. W.. Review. The endoplasmic reticulum: A target for new anticancer drugs. In Vivo. 2007 ; 21: 215-26
    • (2007) Vivo , vol.21 , pp. 215-226
    • Boelens, J.1    Lust, S.2    Offner, F.3    Bracke, M.E.4    Vanhoecke, B.W.5
  • 20
    • 0036105204 scopus 로고    scopus 로고
    • Regulation of ER stress proteins by valproate: Therapeutic implications
    • Bown C. D., Wang J. F., Chen B., Young L. T.. Regulation of ER stress proteins by valproate: Therapeutic implications. Bipolar Disord. 2002 ; 4: 145-51
    • (2002) Bipolar Disord , vol.4 , pp. 145-151
    • Bown, C.D.1    Wang, J.F.2    Chen, B.3    Young, L.T.4
  • 21
    • 0033845743 scopus 로고    scopus 로고
    • Increased expression of endoplasmic reticulum stress proteins following chronic valproate treatment of rat C6 glioma cells
    • Bown C. D., Wang J. F., Young L. T.. Increased expression of endoplasmic reticulum stress proteins following chronic valproate treatment of rat C6 glioma cells. Neuropharmacology. 2000 ; 39: 2162-69
    • (2000) Neuropharmacology , vol.39 , pp. 2162-2169
    • Bown, C.D.1    Wang, J.F.2    Young, L.T.3
  • 23
    • 0033587675 scopus 로고    scopus 로고
    • Mammalian unfolded protein response inhibits cyclin D1 translation and cell-cycle progression
    • Brewer J. W., Hendershot L. M., Sherr C. J., Diehl J. A.. Mammalian unfolded protein response inhibits cyclin D1 translation and cell-cycle progression. Proc Natl Acad Sci USA. 1999 ; 96: 8505-10
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8505-8510
    • Brewer, J.W.1    Hendershot, L.M.2    Sherr, C.J.3    Diehl, J.A.4
  • 24
    • 33745747085 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and trophic factor withdrawal activate distinct signaling cascades that induce glycogen synthase kinase-3 beta and a caspase-9-dependent apoptosis in cerebellar granule neurons
    • Brewster J. L., Linseman D. A., Bouchard R. J., Loucks F. A., Precht T. A., Esch E. A., Heidenreich K. A.. Endoplasmic reticulum stress and trophic factor withdrawal activate distinct signaling cascades that induce glycogen synthase kinase-3 beta and a caspase-9-dependent apoptosis in cerebellar granule neurons. Mol Cell Neurosci. 2006 ; 32: 242-53
    • (2006) Mol Cell Neurosci , vol.32 , pp. 242-253
    • Brewster, J.L.1    Linseman, D.A.2    Bouchard, R.J.3    Loucks, F.A.4    Precht, T.A.5    Esch, E.A.6    Heidenreich, K.A.7
  • 25
    • 78649357985 scopus 로고    scopus 로고
    • Protein quality control in the cytosol and the endoplasmic reticulum: Brothers in arms
    • Buchberger A., Bukau B., Sommer T.. Protein quality control in the cytosol and the endoplasmic reticulum: Brothers in arms. Mol Cell. 2010 ; 40: 238-52
    • (2010) Mol Cell , vol.40 , pp. 238-252
    • Buchberger, A.1    Bukau, B.2    Sommer, T.3
  • 26
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon M., Zeng H., Urano F., Till J. H., Hubbard S. R., Harding H. P., Clark S. G., Ron D.. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature. 2002 ; 415: 92-96
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5    Harding, H.P.6    Clark, S.G.7    Ron, D.8
  • 27
    • 30144437016 scopus 로고    scopus 로고
    • Targeting endoplasmic reticulum protein transport: A novel strategy to kill malignant B cells and overcome fludarabine resistance in CLL
    • Carew J. S., Nawrocki S. T., Krupnik Y. V., Dunner K., McConkey D. J., Keating M. J., Huang P.. Targeting endoplasmic reticulum protein transport: A novel strategy to kill malignant B cells and overcome fludarabine resistance in CLL. Blood. 2006 ; 107: 222-31
    • (2006) Blood , vol.107 , pp. 222-231
    • Carew, J.S.1    Nawrocki, S.T.2    Krupnik, Y.V.3    Dunner, K.4    McConkey, D.J.5    Keating, M.J.6    Huang, P.7
  • 28
    • 79251508006 scopus 로고    scopus 로고
    • Assays for detecting the unfolded protein response
    • Cawley K., Deegan S., Samali A., Gupta S.. Assays for detecting the unfolded protein response. Methods Enzymol. 2011 ; 490: 31-51
    • (2011) Methods Enzymol , vol.490 , pp. 31-51
    • Cawley, K.1    Deegan, S.2    Samali, A.3    Gupta, S.4
  • 30
    • 80054026314 scopus 로고    scopus 로고
    • A review of the mammalian unfolded protein response
    • Chakrabarti A., Chen A. W., Varner J. D.. A review of the mammalian unfolded protein response. Biotechnol Bioeng. 2011 ; 108: 2777-93
    • (2011) Biotechnol Bioeng , vol.108 , pp. 2777-2793
    • Chakrabarti, A.1    Chen, A.W.2    Varner, J.D.3
  • 31
    • 0034307061 scopus 로고    scopus 로고
    • Chronic valproate treatment increases expression of endoplasmic reticulum stress proteins in the rat cerebral cortex and hippocampus
    • Chen B., Wang J. F., Young L. T.. Chronic valproate treatment increases expression of endoplasmic reticulum stress proteins in the rat cerebral cortex and hippocampus. Biol Psychiatry. 2000 ; 48: 658-64
    • (2000) Biol Psychiatry , vol.48 , pp. 658-664
    • Chen, B.1    Wang, J.F.2    Young, L.T.3
  • 32
    • 77954525706 scopus 로고    scopus 로고
    • SUMO modification regulates the transcriptional activity of XBP1
    • Chen H., Qi L.. SUMO modification regulates the transcriptional activity of XBP1. Biochem J. 2010 ; 429: 95-102
    • (2010) Biochem J , vol.429 , pp. 95-102
    • Chen, H.1    Qi, L.2
  • 33
    • 0028935374 scopus 로고
    • Regulation of protein synthesis by heme-regulated eIF-2 alpha kinase
    • Chen J. J., London I. M.. Regulation of protein synthesis by heme-regulated eIF-2 alpha kinase. Trends Biochem Sci. 1995 ; 20: 105-108
    • (1995) Trends Biochem Sci , vol.20 , pp. 105-108
    • Chen, J.J.1    London, I.M.2
  • 34
    • 0034786019 scopus 로고    scopus 로고
    • BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis
    • Cheng E. H., Wei M. C., Weiler S., Flavell R. A., Mak T. W., Lindsten T., Korsmeyer S. J.. BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol Cell. 2001 ; 8: 705-11
    • (2001) Mol Cell , vol.8 , pp. 705-711
    • Cheng, E.H.1    Wei, M.C.2    Weiler, S.3    Flavell, R.A.4    Mak, T.W.5    Lindsten, T.6    Korsmeyer, S.J.7
  • 35
    • 77953912212 scopus 로고    scopus 로고
    • Apigenin protects HT22 murine hippocampal neuronal cells against endoplasmic reticulum stress-induced apoptosis
    • Choi A. Y., Choi J. H., Lee J. Y., Yoon K. S., Choe W., Ha J., Yeo E. J., Kang I.. Apigenin protects HT22 murine hippocampal neuronal cells against endoplasmic reticulum stress-induced apoptosis. Neurochem Int. 2010 ; 57: 143-52
    • (2010) Neurochem Int , vol.57 , pp. 143-152
    • Choi, A.Y.1    Choi, J.H.2    Lee, J.Y.3    Yoon, K.S.4    Choe, W.5    Ha, J.6    Yeo, E.J.7    Kang, I.8
  • 36
    • 78650831339 scopus 로고    scopus 로고
    • Baicalein protects HT22 murine hippocampal neuronal cells against endoplasmic reticulum stress-induced apoptosis through inhibition of reactive oxygen species production and CHOP induction
    • Choi J. H., Choi A. Y., Yoon H., Choe W., Yoon K. S., Ha J., Yeo E. J., Kang I.. Baicalein protects HT22 murine hippocampal neuronal cells against endoplasmic reticulum stress-induced apoptosis through inhibition of reactive oxygen species production and CHOP induction. Exp Mol Med. 2010 ; 42: 811-22
    • (2010) Exp Mol Med , vol.42 , pp. 811-822
    • Choi, J.H.1    Choi, A.Y.2    Yoon, H.3    Choe, W.4    Yoon, K.S.5    Ha, J.6    Yeo, E.J.7    Kang, I.8
  • 38
    • 33947510911 scopus 로고    scopus 로고
    • Selective inhibition of eukaryotic translation initiation factor 2 alpha dephosphorylation potentiates fatty acid-induced endoplasmic reticulum stress and causes pancreatic beta-cell dysfunction and apoptosis
    • Cnop M., Ladriere L., Hekerman P., Ortis F., Cardozo A. K., Dogusan Z., Flamez D., Boyce M., Yuan J., Eizirik D. L.. Selective inhibition of eukaryotic translation initiation factor 2 alpha dephosphorylation potentiates fatty acid-induced endoplasmic reticulum stress and causes pancreatic beta-cell dysfunction and apoptosis. J Biol Chem. 2007 ; 282: 3989-97
    • (2007) J Biol Chem , vol.282 , pp. 3989-3997
    • Cnop, M.1    Ladriere, L.2    Hekerman, P.3    Ortis, F.4    Cardozo, A.K.5    Dogusan, Z.6    Flamez, D.7    Boyce, M.8    Yuan, J.9    Eizirik, D.L.10
  • 41
    • 74449085963 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in proteinuric kidney disease
    • Cybulsky A. V.. Endoplasmic reticulum stress in proteinuric kidney disease. Kidney Inter. 2010 ; 77: 187-93
    • (2010) Kidney Inter , vol.77 , pp. 187-193
    • Cybulsky, A.V.1
  • 42
    • 84863932273 scopus 로고    scopus 로고
    • Beta-adrenergic receptor stimulation induces endoplasmic reticulum stress in adult cardiac myocytes: Role in apoptosis
    • Dalal S., Foster C. R., Das B. C., Singh M., Singh K.. Beta-adrenergic receptor stimulation induces endoplasmic reticulum stress in adult cardiac myocytes: Role in apoptosis. Mol Cellular Biochem. 2012 ; 364: 59-70
    • (2012) Mol Cellular Biochem , vol.364 , pp. 59-70
    • Dalal, S.1    Foster, C.R.2    Das, B.C.3    Singh, M.4    Singh, K.5
  • 44
    • 8644282751 scopus 로고    scopus 로고
    • Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2
    • Deng J., Lu P. D., Zhang Y., Scheuner D., Kaufman R. J., Sonenberg N., Harding H. P., Ron D.. Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2. Mol Cell Biol. 2004 ; 24: 10161-68
    • (2004) Mol Cell Biol , vol.24 , pp. 10161-10168
    • Deng, J.1    Lu, P.D.2    Zhang, Y.3    Scheuner, D.4    Kaufman, R.J.5    Sonenberg, N.6    Harding, H.P.7    Ron, D.8
  • 45
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • Ding W. X., Ni H. M., Gao W., Yoshimori T., Stolz D. B., Ron D., Yin X. M.. Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am J Pathol. 2007 ; 171: 513-24
    • (2007) Am J Pathol , vol.171 , pp. 513-524
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Yoshimori, T.4    Stolz, D.B.5    Ron, D.6    Yin, X.M.7
  • 46
    • 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: 3095-107
    • (2006) Mol Biol Cell , vol.17 , pp. 3095-3107
    • Durose, J.B.1    Tam, A.B.2    Niwa, M.3
  • 47
    • 0141893341 scopus 로고    scopus 로고
    • Serine proteases mediate apoptosis-like cell death and phagocytosis under caspase-inhibiting conditions
    • Egger L., Schneider J., Rheme C., Tapernoux M., Hacki J., Borner C.. Serine proteases mediate apoptosis-like cell death and phagocytosis under caspase-inhibiting conditions. Cell Death Differ. 2003 ; 10: 1188-203
    • (2003) Cell Death Differ , vol.10 , pp. 1188-1203
    • Egger, L.1    Schneider, J.2    Rheme, C.3    Tapernoux, M.4    Hacki, J.5    Borner, C.6
  • 48
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard L., Molinari M., Helenius A.. Setting the standards: Quality control in the secretory pathway. Science. 1999 ; 286: 1882-888
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 50
    • 0037023688 scopus 로고    scopus 로고
    • Translation mediated by the internal ribosome entry site of the cat-1 mRNA is regulated by glucose availability in a PERK kinase-dependent manner
    • Fernandez J., Bode B., Koromilas A., Diehl J. A., Krukovets I., Snider M. D., Hatzoglou M.. Translation mediated by the internal ribosome entry site of the cat-1 mRNA is regulated by glucose availability in a PERK kinase-dependent manner. J Biol Chem. 2002 ; 277: 11780-787
    • (2002) J Biol Chem , vol.277 , pp. 11780-11787
    • Fernandez, J.1    Bode, B.2    Koromilas, A.3    Diehl, J.A.4    Krukovets, I.5    Snider, M.D.6    Hatzoglou, M.7
  • 53
    • 81255179936 scopus 로고    scopus 로고
    • The 26S proteasome complex: An attractive target for cancer therapy
    • Frankland-Searby S., Bhaumik S. R.. The 26S proteasome complex: An attractive target for cancer therapy. Biochim Biophys Acta. 2012 ; 1825: 64-76
    • (2012) Biochim Biophys Acta , vol.1825 , pp. 64-76
    • Frankland-Searby, S.1    Bhaumik, S.R.2
  • 54
    • 77957252262 scopus 로고    scopus 로고
    • The heat shock factor family and adaptation to proteotoxic stress
    • Fujimoto M., Nakai A.. The heat shock factor family and adaptation to proteotoxic stress. FEBS J. 2010 ; 277: 4112-25
    • (2010) FEBS J , vol.277 , pp. 4112-4125
    • Fujimoto, M.1    Nakai, A.2
  • 55
    • 1542651212 scopus 로고    scopus 로고
    • Upregulation and overexpression of human X-box binding protein 1 (hXBP-1) gene in primary breast cancers
    • Fujimoto T., Onda M., Nagai H., Nagahata T., Ogawa K., Emi M.. Upregulation and overexpression of human X-box binding protein 1 (hXBP-1) gene in primary breast cancers. Breast Canc. 2003 ; 10: 301-306
    • (2003) Breast Canc , vol.10 , pp. 301-306
    • Fujimoto, T.1    Onda, M.2    Nagai, H.3    Nagahata, T.4    Ogawa, K.5    Emi, M.6
  • 56
    • 34347225099 scopus 로고    scopus 로고
    • The dsRNA protein kinase PKR: Virus and cell control
    • Garcia M. A., Meurs E. F., Esteban M.. The dsRNA protein kinase PKR: Virus and cell control. Biochimie. 2007 ; 89: 799-811
    • (2007) Biochimie , vol.89 , pp. 799-811
    • Garcia, M.A.1    Meurs, E.F.2    Esteban, M.3
  • 58
    • 35548935675 scopus 로고    scopus 로고
    • The unfolded protein response of B-lymphocytes: PERK-independent development of antibody-secreting cells
    • Gass J. N., Jiang H. Y., Wek R. C., Brewer J. W.. The unfolded protein response of B-lymphocytes: PERK-independent development of antibody-secreting cells. Mol Immunol. 2008 ; 45: 1035-43
    • (2008) Mol Immunol , vol.45 , pp. 1035-1043
    • Gass, J.N.1    Jiang, H.Y.2    Wek, R.C.3    Brewer, J.W.4
  • 59
    • 84859743150 scopus 로고    scopus 로고
    • SIRT1 associates with eIF2-alpha and regulates the cellular stress response
    • Ghosh H. S., Reizis B., Robbins P. D.. SIRT1 associates with eIF2-alpha and regulates the cellular stress response. Scientific Reports. 2011 ; 1: 150
    • (2011) Scientific Reports , vol.1 , pp. 150
    • Ghosh, H.S.1    Reizis, B.2    Robbins, P.D.3
  • 60
    • 68149154728 scopus 로고    scopus 로고
    • BH3-only proteins and their roles in programmed cell death
    • GiamM.HuangD. C.BouilletP. (2008). BH3-only proteins and their roles in programmed cell death. Oncogene27Suppl 1, S128-36.
    • (2008) Oncogene , vol.27 , Issue.SUPPL. 1
    • Giam, M.1    Huang, D.C.2    Bouillet, P.3
  • 62
    • 33750902737 scopus 로고    scopus 로고
    • The endoplasmic reticulum: Folding, calcium homeostasis, signaling, and redox control
    • Gorlach A., Klappa P., Kietzmann T.. The endoplasmic reticulum: Folding, calcium homeostasis, signaling, and redox control. Antioxid Redox Signal. 2006 ; 8: 1391-418
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1391-1418
    • Gorlach, A.1    Klappa, P.2    Kietzmann, T.3
  • 63
    • 9644303176 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B potentiates IRE1 signaling during endoplasmic reticulum stress
    • Gu F., Nguyen D. T., Stuible M., Dube N., Tremblay M. L., Chevet E.. Protein-tyrosine phosphatase 1B potentiates IRE1 signaling during endoplasmic reticulum stress. J Biol Chem. 2004 ; 279: 49689-93
    • (2004) J Biol Chem , vol.279 , pp. 49689-49693
    • Gu, F.1    Nguyen, D.T.2    Stuible, M.3    Dube, N.4    Tremblay, M.L.5    Chevet, E.6
  • 64
    • 0035824621 scopus 로고    scopus 로고
    • Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex
    • Guo Y., Guettouche T., Fenna M., Boellmann F., Pratt W. B., Toft D. O., Smith D. F., Voellmy R.. Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex. J Biol Chem. 2001 ; 276: 45791-99
    • (2001) J Biol Chem , vol.276 , pp. 45791-45799
    • Guo, Y.1    Guettouche, T.2    Fenna, M.3    Boellmann, F.4    Pratt, W.B.5    Toft, D.O.6    Smith, D.F.7    Voellmy, R.8
  • 65
    • 77955044180 scopus 로고    scopus 로고
    • HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1alpha-XBP1 signaling through a physical interaction
    • Gupta S., Deepti A., Deegan S., Lisbona F., Hetz C., Samali A.. HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1alpha-XBP1 signaling through a physical interaction. PLoS biology. 2010 ; 8: e1000410
    • (2010) PLoS Biology , vol.8 , pp. 1000410
    • Gupta, S.1    Deepti, A.2    Deegan, S.3    Lisbona, F.4    Hetz, C.5    Samali, A.6
  • 66
    • 73649125333 scopus 로고    scopus 로고
    • Heat shock protein 72 protects insulin-secreting beta cells from lipopolysaccharide-induced endoplasmic reticulum stress
    • Hagiwara S., Iwasaka H., Shingu C., Matsumoto S., Hasegawa A., Asai N., Noguchi T.. Heat shock protein 72 protects insulin-secreting beta cells from lipopolysaccharide-induced endoplasmic reticulum stress. Intern J Hyperthermia. 2009 ; 25: 626-33
    • (2009) Intern J Hyperthermia , vol.25 , pp. 626-633
    • Hagiwara, S.1    Iwasaka, H.2    Shingu, C.3    Matsumoto, S.4    Hasegawa, A.5    Asai, N.6    Noguchi, T.7
  • 68
    • 68049110633 scopus 로고    scopus 로고
    • IRE1alpha kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates
    • Han D., Lerner A. G., Vande Walle 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: 562-75
    • (2009) Cell , vol.138 , pp. 562-575
    • Han, D.1    Lerner, A.G.2    Vande Walle, L.3    Upton, J.P.4    Xu, W.5    Hagen, A.6    Backes, B.J.7    Oakes, S.A.8    Papa, F.R.9
  • 69
    • 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: 1099-108
    • (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
  • 70
    • 0034968330 scopus 로고    scopus 로고
    • Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival
    • Harding H. P., Zeng H., Zhang Y., Jungries R., Chung P., Plesken H., Sabatini D. D., Ron D.. Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival. Mol Cell. 2001 ; 7: 1153-63
    • (2001) Mol Cell , vol.7 , 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
  • 71
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding H. P., Zhang Y., Bertolotti A., Zeng H., Ron D.. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell. 2000 ; 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
  • 72
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum- resident kinase
    • Harding H. P., Zhang Y., Ron D.. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature. 1999 ; 397: 271-74
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 75
    • 34848861368 scopus 로고    scopus 로고
    • ClpP mediates activation of a mitochondrial unfolded protein response in C. elegans
    • Haynes C. M., Petrova K., Benedetti C., Yang Y., Ron D.. ClpP mediates activation of a mitochondrial unfolded protein response in C. elegans. Dev Cell. 2007 ; 13: 467-80
    • (2007) Dev Cell , vol.13 , pp. 467-480
    • Haynes, C.M.1    Petrova, K.2    Benedetti, C.3    Yang, Y.4    Ron, D.5
  • 76
    • 78649728763 scopus 로고    scopus 로고
    • The mitochondrial UPR-protecting organelle protein homeostasis
    • Haynes C. M., Ron D.. The mitochondrial UPR-protecting organelle protein homeostasis. J Cell Sci. 2010 ; 123: 3849-55
    • (2010) J Cell Sci , vol.123 , pp. 3849-3855
    • Haynes, C.M.1    Ron, D.2
  • 77
    • 76849100919 scopus 로고    scopus 로고
    • The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C. elegans
    • Haynes C. M., Yang Y., Blais S. P., Neubert T. A., Ron D.. The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C. elegans. Mol Cell. 2010 ; 37: 529-40
    • (2010) Mol Cell , vol.37 , pp. 529-540
    • Haynes, C.M.1    Yang, Y.2    Blais, S.P.3    Neubert, T.A.4    Ron, D.5
  • 78
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze K., Yoshida H., Yanagi H., Yura T., Mori K.. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell. 1999 ; 10: 3787-99
    • (1999) Mol Biol Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 79
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: Controlling cell fate decisions under ER stress and beyond
    • Hetz C.. The unfolded protein response: Controlling cell fate decisions under ER stress and beyond. Nature reviews. Mol Cell Biol. 2012 ; 13: 89-102
    • (2012) Nature Reviews. Mol Cell Biol , vol.13 , pp. 89-102
    • Hetz, C.1
  • 81
    • 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: 551-61
    • (2009) Mol Cell , vol.35 , pp. 551-561
    • Hetz, C.1    Glimcher, L.H.2
  • 82
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • Hetz C., Russelakis-Carneiro M., Maundrell K., Castilla J., Soto C.. Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J. 2003 ; 22: 5435-45
    • (2003) EMBO J , vol.22 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 84
  • 85
    • 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
  • 87
    • 67349176043 scopus 로고    scopus 로고
    • XBP-1 regulates signal transduction, transcription factors and bone marrow colonization in B cells
    • Hu C. C., Dougan S. K., McGehee A. M., Love J. C., Ploegh H. L.. XBP-1 regulates signal transduction, transcription factors and bone marrow colonization in B cells. EMBO J. 2009 ; 28: 1624-36
    • (2009) EMBO J , vol.28 , pp. 1624-1636
    • Hu, C.C.1    Dougan, S.K.2    McGehee, A.M.3    Love, J.C.4    Ploegh, H.L.5
  • 89
    • 33645815074 scopus 로고    scopus 로고
    • Autocrine tumor necrosis factor alpha links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1alpha-mediated NF-kappaB activation and down-regulation of TRAF2 expression
    • Hu P., Han Z., Couvillon A. D., Kaufman R. J., Exton J. H.. Autocrine tumor necrosis factor alpha links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1alpha-mediated NF-kappaB activation and down-regulation of TRAF2 expression. Mol Cell Biol. 2006 ; 26: 3071-84
    • (2006) Mol Cell Biol , vol.26 , pp. 3071-3084
    • Hu, P.1    Han, Z.2    Couvillon, A.D.3    Kaufman, R.J.4    Exton, J.H.5
  • 91
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
    • Imai Y., Soda M., Takahashi R.. Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J Biol Chem. 2000 ; 275: 35661-64
    • (2000) J Biol Chem , vol.275 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 92
    • 63349088070 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in the kidney as a novel mediator of kidney injury
    • Inagi R.. Endoplasmic reticulum stress in the kidney as a novel mediator of kidney injury. Nephron Exp Nephrol. 2009 ; 112: e1-9
    • (2009) Nephron Exp Nephrol , vol.112 , pp. 1-9
    • Inagi, R.1
  • 93
    • 77949730282 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress as a progression factor for kidney injury
    • Inagi R.. Endoplasmic reticulum stress as a progression factor for kidney injury. Curr Opin Pharmacol. 2010 ; 10: 156-65
    • (2010) Curr Opin Pharmacol , vol.10 , pp. 156-165
    • Inagi, R.1
  • 95
    • 79960216863 scopus 로고    scopus 로고
    • Bax inhibitor-1: A highly conserved endoplasmic reticulum-resident cell death suppressor
    • Ishikawa T., Watanabe N., Nagano M., Kawai-Yamada M., Lam E.. Bax inhibitor-1: A highly conserved endoplasmic reticulum-resident cell death suppressor. Cell Death Differ. 2011 ; 18: 1271-78
    • (2011) Cell Death Differ , vol.18 , pp. 1271-1278
    • Ishikawa, T.1    Watanabe, N.2    Nagano, M.3    Kawai-Yamada, M.4    Lam, E.5
  • 96
    • 0038675136 scopus 로고    scopus 로고
    • The X-box binding protein-1 transcription factor is required for plasma cell differentiation and the unfolded protein response
    • Iwakoshi N. N., Lee A. H., Glimcher L. H.. The X-box binding protein-1 transcription factor is required for plasma cell differentiation and the unfolded protein response. Immunol Rev. 2003 ; 194: 29-38
    • (2003) Immunol Rev , vol.194 , pp. 29-38
    • Iwakoshi, N.N.1    Lee, A.H.2    Glimcher, L.H.3
  • 97
    • 77958590030 scopus 로고    scopus 로고
    • IRE1alpha disruption causes histological abnormality of exocrine tissues, increase of blood glucose level, and decrease of serum immunoglobulin level
    • Iwawaki T., Akai R., Kohno K.. IRE1alpha disruption causes histological abnormality of exocrine tissues, increase of blood glucose level, and decrease of serum immunoglobulin level. PLoS One. 2010 ; 5: e13052
    • (2010) PLoS One , vol.5 , pp. 13052
    • Iwawaki, T.1    Akai, R.2    Kohno, K.3
  • 99
    • 0029817451 scopus 로고    scopus 로고
    • Inhibition of tumor progression by suppression of stress protein GRP78/BiP induction in fibrosarcoma B/C10ME
    • Jamora C., Dennert G., Lee A. S.. Inhibition of tumor progression by suppression of stress protein GRP78/BiP induction in fibrosarcoma B/C10ME. Proc Natl Acad Sci USA. 1996 ; 93: 7690-94
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7690-7694
    • Jamora, C.1    Dennert, G.2    Lee, A.S.3
  • 100
    • 0345599024 scopus 로고    scopus 로고
    • Inhibition of a constitutive translation initiation factor 2alpha phosphatase, CReP, promotes survival of stressed cells
    • Jousse C., Oyadomari S., Novoa I., Lu P., Zhang Y., Harding H. P., Ron D.. Inhibition of a constitutive translation initiation factor 2alpha phosphatase, CReP, promotes survival of stressed cells. J Cell Biol. 2003 ; 163: 767-75
    • (2003) J Cell Biol , vol.163 , 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
  • 102
    • 59249087087 scopus 로고    scopus 로고
    • Valproate, a mood stabilizer, induces WFS1 expression and modulates its interaction with ER stress protein GRP94
    • Kakiuchi C., Ishigaki S., Oslowski C. M., Fonseca S. G., Kato T., Urano F.. Valproate, a mood stabilizer, induces WFS1 expression and modulates its interaction with ER stress protein GRP94. PLoS One. 2009 ; 4: e4134
    • (2009) PLoS One , vol.4 , pp. 4134
    • Kakiuchi, C.1    Ishigaki, S.2    Oslowski, C.M.3    Fonseca, S.G.4    Kato, T.5    Urano, F.6
  • 104
    • 66449137379 scopus 로고    scopus 로고
    • GRP78 expression inhibits insulin and ER stress-induced SREBP-1c activation and reduces hepatic steatosis in mice
    • Kammoun H. L., Chabanon H., Hainault I., Luquet S., Magnan C., Koike T., Ferre P., Foufelle F.. GRP78 expression inhibits insulin and ER stress-induced SREBP-1c activation and reduces hepatic steatosis in mice. J Clin Invest. 2009 ; 119: 1201-15
    • (2009) J Clin Invest , vol.119 , pp. 1201-1215
    • Kammoun, H.L.1    Chabanon, H.2    Hainault, I.3    Luquet, S.4    Magnan, C.5    Koike, T.6    Ferre, P.7    Foufelle, F.8
  • 105
    • 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
  • 106
    • 84864338917 scopus 로고    scopus 로고
    • Human immunodeficiency virus protease inhibitors modulate Ca(2+) homeostasis and potentiate alcoholic stress and injury in mice and primary mouse and human hepatocytes
    • Kao E., Shinohara M., Feng M., Lau M. Y., Ji C.. Human immunodeficiency virus protease inhibitors modulate Ca(2+) homeostasis and potentiate alcoholic stress and injury in mice and primary mouse and human hepatocytes. Hepatology. 2012 ;:
    • (2012) Hepatology
    • Kao, E.1    Shinohara, M.2    Feng, M.3    Lau, M.Y.4    Ji, C.5
  • 108
    • 70349768065 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the unfolded protein response
    • Kapoor A., Sanyal A. J.. Endoplasmic reticulum stress and the unfolded protein response. Clin Liver Dis. 2009 ; 13: 581-90
    • (2009) Clin Liver Dis , vol.13 , pp. 581-590
    • Kapoor, A.1    Sanyal, A.J.2
  • 110
    • 84855696465 scopus 로고    scopus 로고
    • MTORC1 serves ER stress-triggered apoptosis via selective activation of the IRE1-JNK pathway
    • Kato H., Nakajima S., Saito Y., Takahashi S., Katoh R., Kitamura M.. mTORC1 serves ER stress-triggered apoptosis via selective activation of the IRE1-JNK pathway. Cell Death Differ. 2012 ; 19: 310-20
    • (2012) Cell Death Differ , vol.19 , pp. 310-320
    • Kato, H.1    Nakajima, S.2    Saito, Y.3    Takahashi, S.4    Katoh, R.5    Kitamura, M.6
  • 111
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman R. J.. Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls. Genes Dev. 1999 ; 13: 1211-33
    • (1999) Genes Dev , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 113
    • 14044261099 scopus 로고    scopus 로고
    • Valproate protects cells from ER stress-induced lipid accumulation and apoptosis by inhibiting glycogen synthase kinase-3
    • Kim A. J., Shi Y., Austin R. C., Werstuck G. H.. Valproate protects cells from ER stress-induced lipid accumulation and apoptosis by inhibiting glycogen synthase kinase-3. J Cell Sci. 2005 ; 118: 89-99
    • (2005) J Cell Sci , vol.118 , pp. 89-99
    • Kim, A.J.1    Shi, Y.2    Austin, R.C.3    Werstuck, G.H.4
  • 114
    • 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. Nature reviews. Drug Discov. 2008 ; 7: 1013-30
    • (2008) Nature Reviews. Drug Discov , vol.7 , pp. 1013-1030
    • Kim, I.1    Xu, W.2    Reed, J.C.3
  • 115
    • 0027462166 scopus 로고
    • Hormonal regulation of thyroglobulin export from the endoplasmic reticulum of cultured thyrocytes
    • Kim P. S., Arvan P.. Hormonal regulation of thyroglobulin export from the endoplasmic reticulum of cultured thyrocytes. J Biol Chem. 1993 ; 268: 4873-79
    • (1993) J Biol Chem , vol.268 , pp. 4873-4879
    • Kim, P.S.1    Arvan, P.2
  • 116
    • 0035225871 scopus 로고    scopus 로고
    • Regulation of translation initiation by amino acids in eukaryotic cells
    • Kimball S. R.. Regulation of translation initiation by amino acids in eukaryotic cells. Prog Mol Subcell Biol. 2001 ; 26: 155-84
    • (2001) Prog Mol Subcell Biol , vol.26 , pp. 155-184
    • Kimball, S.R.1
  • 117
    • 52449128023 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and unfolded protein response in renal pathophysiology: Janus faces
    • Kitamura M.. Endoplasmic reticulum stress and unfolded protein response in renal pathophysiology: Janus faces. Am J Physiol Renal Physiol. 2008 ; 295: F323-34
    • (2008) Am J Physiol Renal Physiol , vol.295 , pp. 323-334
    • Kitamura, M.1
  • 121
  • 125
    • 69449095860 scopus 로고    scopus 로고
    • Caspases and kinases in a death grip
    • Kurokawa M., Kornbluth S.. Caspases and kinases in a death grip. Cell. 2009 ; 138: 838-54
    • (2009) Cell , vol.138 , pp. 838-854
    • Kurokawa, M.1    Kornbluth, S.2
  • 126
    • 77749246118 scopus 로고    scopus 로고
    • Enhanced signaling downstream of ribonucleic acid-activated protein kinase-like endoplasmic reticulum kinase potentiates lipotoxic endoplasmic reticulum stress in human islets
    • Ladriere L., Igoillo-Esteve M., Cunha D. A., Brion J. P., Bugliani M., Marchetti P., Eizirik D. L., Cnop M.. Enhanced signaling downstream of ribonucleic acid-activated protein kinase-like endoplasmic reticulum kinase potentiates lipotoxic endoplasmic reticulum stress in human islets. J Clin Endocrinol Metab. 2010 ; 95: 1442-49
    • (2010) J Clin Endocrinol Metab , vol.95 , pp. 1442-1449
    • Ladriere, L.1    Igoillo-Esteve, M.2    Cunha, D.A.3    Brion, J.P.4    Bugliani, M.5    Marchetti, P.6    Eizirik, D.L.7    Cnop, M.8
  • 127
    • 79952478406 scopus 로고    scopus 로고
    • Ryanodine receptors: Structure, expression, molecular details, and function in calcium release
    • Lanner J. T., Georgiou D. K., Joshi A. D., Hamilton S. L.. Ryanodine receptors: Structure, expression, molecular details, and function in calcium release. Cold Spring Harbor Perspec Biol. 2010 ; 2: a003996
    • (2010) Cold Spring Harbor Perspec Biol , vol.2 , pp. 003996
    • Lanner, J.T.1    Georgiou, D.K.2    Joshi, A.D.3    Hamilton, S.L.4
  • 128
    • 33748753172 scopus 로고    scopus 로고
    • Nck in a complex containing the catalytic subunit of protein phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling and cell survival to endoplasmic reticulum stress
    • Latreille M., Larose L.. Nck in a complex containing the catalytic subunit of protein phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling and cell survival to endoplasmic reticulum stress. J Biol Chem. 2006 ; 281: 26633-44
    • (2006) J Biol Chem , vol.281 , pp. 26633-26644
    • Latreille, M.1    Larose, L.2
  • 130
    • 29244448729 scopus 로고    scopus 로고
    • XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands
    • Lee A. H., Chu G. C., Iwakoshi N. N., Glimcher L. H.. XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands. EMBO J. 2005 ; 24: 4368-80
    • (2005) EMBO J , vol.24 , pp. 4368-4380
    • Lee, A.H.1    Chu, G.C.2    Iwakoshi, N.N.3    Glimcher, L.H.4
  • 131
    • 0043193876 scopus 로고    scopus 로고
    • Proteasome inhibitors disrupt the unfolded protein response in myeloma cells
    • Lee A. H., Iwakoshi N. N., Anderson K. C., Glimcher L. H.. Proteasome inhibitors disrupt the unfolded protein response in myeloma cells. Proc Natl Acad Sci USA. 2003 ; 100: 9946-51
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 9946-9951
    • Lee, A.H.1    Iwakoshi, N.N.2    Anderson, K.C.3    Glimcher, L.H.4
  • 132
    • 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: 7448-59
    • (2003) Mol Cell Biol , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 133
    • 45849137877 scopus 로고    scopus 로고
    • Regulation of hepatic lipogenesis by the transcription factor XBP1
    • Lee A. H., Scapa E. F., Cohen D. E., Glimcher L. H.. Regulation of hepatic lipogenesis by the transcription factor XBP1. Science. 2008 ; 320: 1492-96
    • (2008) Science , vol.320 , pp. 1492-1496
    • Lee, A.H.1    Scapa, E.F.2    Cohen, D.E.3    Glimcher, L.H.4
  • 135
    • 0037083755 scopus 로고    scopus 로고
    • IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response
    • Lee K., Tirasophon W., Shen X., Michalak M., Prywes R., Okada T., Yoshida H., Mori K., Kaufman R. J.. IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev. 2002 ; 16: 452-66
    • (2002) Genes Dev , vol.16 , pp. 452-466
    • Lee, K.1    Tirasophon, W.2    Shen, X.3    Michalak, M.4    Prywes, R.5    Okada, T.6    Yoshida, H.7    Mori, K.8    Kaufman, R.J.9
  • 136
    • 34247137486 scopus 로고    scopus 로고
    • Activation of the unfolded protein response and alternative splicing of ATF6alpha in HLA-B27 positive lymphocytes
    • Lemin A. J., Saleki K., van Lith M., Benham A. M.. Activation of the unfolded protein response and alternative splicing of ATF6alpha in HLA-B27 positive lymphocytes. FEBS Lett. 2007 ; 581: 1819-1824
    • (2007) FEBS Lett , vol.581 , pp. 1819-1824
    • Lemin, A.J.1    Saleki, K.2    Van Lith, M.3    Benham, A.M.4
  • 137
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine B., Kroemer G.. Autophagy in the pathogenesis of disease. Cell. 2008 ; 132: 27-42
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 138
    • 33846810143 scopus 로고    scopus 로고
    • Hepatitis B virus X protein (HBx) activates ATF6 and IRE1-XBP1 pathways of unfolded protein response
    • Li B., Gao B., Ye L., Han X., Wang W., Kong L., Fang X., Zeng Y., Zheng H., Li S., Wu Z.. Hepatitis B virus X protein (HBx) activates ATF6 and IRE1-XBP1 pathways of unfolded protein response. Virus Res. 2007 ; 124: 44-49
    • (2007) Virus Res , vol.124 , pp. 44-49
    • Li, B.1    Gao, B.2    Ye, L.3    Han, X.4    Wang, W.5    Kong, L.6    Fang, X.7    Zeng, Y.8    Zheng, H.9    Li, S.10    Wu, Z.11
  • 139
    • 20444390622 scopus 로고    scopus 로고
    • The protective effect of dantrolene on ischemic neuronal cell death is associated with reduced expression of endoplasmic reticulum stress markers
    • Li F., Hayashi T., Jin G., Deguchi K., Nagotani S., Nagano I., Shoji M., Chan P. H., Abe K.. The protective effect of dantrolene on ischemic neuronal cell death is associated with reduced expression of endoplasmic reticulum stress markers. Brain Res. 2005 ; 1048: 59-68
    • (2005) Brain Res , vol.1048 , pp. 59-68
    • Li, F.1    Hayashi, T.2    Jin, G.3    Deguchi, K.4    Nagotani, S.5    Nagano, I.6    Shoji, M.7    Chan, P.H.8    Abe, K.9
  • 140
    • 70349905357 scopus 로고    scopus 로고
    • Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis
    • Li G., Mongillo M., Chin K. T., Harding H., Ron D., Marks A. R., Tabas I.. Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J Cell Biol. 2009 ; 186: 783-92
    • (2009) J Cell Biol , vol.186 , pp. 783-792
    • Li, G.1    Mongillo, M.2    Chin, K.T.3    Harding, H.4    Ron, D.5    Marks, A.R.6    Tabas, I.7
  • 141
    • 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: 16113-18
    • (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
  • 142
    • 20444461628 scopus 로고    scopus 로고
    • Free cholesterol-loaded macrophages are an abundant source of tumor necrosis factor-alpha and interleukin-6: Model of NF-kappaB- and map kinase-dependent inflammation in advanced atherosclerosis
    • Li Y., Schwabe R. F., DeVries-Seimon T., Yao P. M., Gerbod-Giannone M. C., Tall A. R., Davis R. J., Flavell R., Brenner D. A., Tabas I.. Free cholesterol-loaded macrophages are an abundant source of tumor necrosis factor-alpha and interleukin-6: Model of NF-kappaB- and map kinase-dependent inflammation in advanced atherosclerosis. J Biol Chem. 2005b ; 280: 21763-72
    • (2005) J Biol Chem , vol.280 , pp. 21763-21772
    • Li, Y.1    Schwabe, R.F.2    Devries-Seimon, T.3    Yao, P.M.4    Gerbod-Giannone, M.C.5    Tall, A.R.6    Davis, R.J.7    Flavell, R.8    Brenner, D.A.9    Tabas, I.10
  • 144
    • 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 , pp. 4170
    • Lin, J.H.1    Li, H.2    Zhang, Y.3    Ron, D.4    Walter, P.5
  • 146
    • 72949115257 scopus 로고    scopus 로고
    • Implication of unfolded protein response in resveratrol-induced inhibition of K562 cell proliferation
    • Liu B. Q., Gao Y. Y., Niu X. F., Xie J. S., Meng X., Guan Y., Wang H. Q.. Implication of unfolded protein response in resveratrol-induced inhibition of K562 cell proliferation. Biochem Biophys Res Commun. 2010 ; 391: 778-82
    • (2010) Biochem Biophys Res Commun , vol.391 , pp. 778-782
    • Liu, B.Q.1    Gao, Y.Y.2    Niu, X.F.3    Xie, J.S.4    Meng, X.5    Guan, Y.6    Wang, H.Q.7
  • 147
    • 0030765016 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperones GRP78 and calreticulin prevent oxidative stress, Ca2+ disturbances, and cell death in renal epithelial cells
    • Liu H., Bowes R. C., van de Water B., Sillence C., Nagelkerke J. F., Stevens J. L.. Endoplasmic reticulum chaperones GRP78 and calreticulin prevent oxidative stress, Ca2+ disturbances, and cell death in renal epithelial cells. J Biol Chem. 1997 ; 272: 21751-59
    • (1997) J Biol Chem , vol.272 , pp. 21751-21759
    • Liu, H.1    Bowes, R.C.2    Van De Water, B.3    Sillence, C.4    Nagelkerke, J.F.5    Stevens, J.L.6
  • 148
    • 80055004410 scopus 로고    scopus 로고
    • Reactive oxygen species-mediated endoplasmic reticulum stress and mitochondrial dysfunction contribute to polydatin-induced apoptosis in human nasopharyngeal carcinoma CNE cells
    • Liu H., Zhao S., Zhang Y., Wu J., Peng H., Fan J., Liao J.. Reactive oxygen species-mediated endoplasmic reticulum stress and mitochondrial dysfunction contribute to polydatin-induced apoptosis in human nasopharyngeal carcinoma CNE cells. J Cell Biochem. 2011 ; 112: 3695-703
    • (2011) J Cell Biochem , vol.112 , pp. 3695-3703
    • Liu, H.1    Zhao, S.2    Zhang, Y.3    Wu, J.4    Peng, H.5    Fan, J.6    Liao, J.7
  • 150
    • 45549103421 scopus 로고    scopus 로고
    • AIP1 is critical in transducing IRE1-mediated endoplasmic reticulum stress response
    • Luo D., He Y., Zhang H., Yu L., Chen H., Xu Z., Tang S., Urano F., Min W.. AIP1 is critical in transducing IRE1-mediated endoplasmic reticulum stress response. J Biol Chem. 2008 ; 283: 11905-912
    • (2008) J Biol Chem , vol.283 , pp. 11905-11912
    • Luo, D.1    He, Y.2    Zhang, H.3    Yu, L.4    Chen, H.5    Xu, Z.6    Tang, S.7    Urano, F.8    Min, W.9
  • 151
    • 0036314984 scopus 로고    scopus 로고
    • Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response
    • Ma Y., Brewer J. W., Diehl J. A., Hendershot L. M.. Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J Mol Biol. 2002 ; 318: 1351-65
    • (2002) J Mol Biol , vol.318 , pp. 1351-1365
    • Ma, Y.1    Brewer, J.W.2    Diehl, J.A.3    Hendershot, L.M.4
  • 152
    • 0041315834 scopus 로고    scopus 로고
    • Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress
    • Ma Y., Hendershot L. M.. Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress. J Biol Chem. 2003 ; 278: 34864-73
    • (2003) J Biol Chem , vol.278 , pp. 34864-34873
    • Ma, Y.1    Hendershot, L.M.2
  • 153
    • 4444318357 scopus 로고    scopus 로고
    • ER chaperone functions during normal and stress conditions
    • Ma Y., Hendershot L. M.. ER chaperone functions during normal and stress conditions. J Chem Neuroanat. 2004 ; 28: 51-65
    • (2004) J Chem Neuroanat , vol.28 , pp. 51-65
    • Ma, Y.1    Hendershot, L.M.2
  • 154
    • 77951252041 scopus 로고    scopus 로고
    • Plasma cell differentiation initiates a limited ER stress response by specifically suppressing the PERK-dependent branch of the unfolded protein response
    • Ma Y., Shimizu Y., Mann M. J., Jin Y., Hendershot L. M.. Plasma cell differentiation initiates a limited ER stress response by specifically suppressing the PERK-dependent branch of the unfolded protein response. Cell Stress Chaperones. 2010 ; 15: 281-93
    • (2010) Cell Stress Chaperones , vol.15 , pp. 281-293
    • Ma, Y.1    Shimizu, Y.2    Mann, M.J.3    Jin, Y.4    Hendershot, L.M.5
  • 155
    • 79952708723 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in liver disease
    • Malhi H., Kaufman R. J.. Endoplasmic reticulum stress in liver disease. J Hepatol. 2011 ; 54: 795-809
    • (2011) J Hepatol , vol.54 , pp. 795-809
    • Malhi, H.1    Kaufman, R.J.2
  • 156
    • 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: 716-31
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 716-731
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 159
    • 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: 8506-13
    • (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
  • 160
    • 61549108620 scopus 로고    scopus 로고
    • Up regulation of the GRP-78 and GADD-153 and down regulation of Bcl-2 proteins in primary glomerular diseases: A possible involvement of the ER stress pathway in glomerulonephritis
    • Markan S., Kohli H. S., Joshi K., Minz R. W., Sud K., Ahuja M., Anand S., Khullar M.. Up regulation of the GRP-78 and GADD-153 and down regulation of Bcl-2 proteins in primary glomerular diseases: A possible involvement of the ER stress pathway in glomerulonephritis. Mol Cell Biochem. 2009 ; 324: 131-38
    • (2009) Mol Cell Biochem , vol.324 , pp. 131-138
    • Markan, S.1    Kohli, H.S.2    Joshi, K.3    Minz, R.W.4    Sud, K.5    Ahuja, M.6    Anand, S.7    Khullar, M.8
  • 161
    • 77951290227 scopus 로고    scopus 로고
    • TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages
    • Martinon F., Chen X., Lee A. H., Glimcher L. H.. TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages. Nat Immunol. 2010 ; 11: 411-18
    • (2010) Nat Immunol , vol.11 , pp. 411-418
    • Martinon, F.1    Chen, X.2    Lee, A.H.3    Glimcher, L.H.4
  • 162
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state
    • McCullough K. D., Martindale J. L., Klotz L. O., Aw T. Y., Holbrook N. J.. Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state. Mol Cell Biol. 2001 ; 21: 1249-59
    • (2001) Mol Cell Biol , vol.21 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.O.3    Aw, T.Y.4    Holbrook, N.J.5
  • 163
    • 84870313272 scopus 로고    scopus 로고
    • A diversity of SERCA Ca2+ pump inhibitors
    • Michelangeli F., East J. M.. A diversity of SERCA Ca2+ pump inhibitors. Biochem Soc Trans. 2011 ; 39: 789-97
    • (2011) Biochem Soc Trans , vol.39 , pp. 789-797
    • Michelangeli, F.1    East, J.M.2
  • 165
    • 0024989084 scopus 로고
    • Cis-acting sequences involved in the translational control of GCN4 expression
    • 1050
    • Miller P. F., Hinnebusch A. G. cis-acting sequences involved in the translational control of GCN4 expression. Biochim Biophys Acta. 1990 1050 ;: 151-54
    • (1990) Biochim Biophys Acta , pp. 151-154
    • Miller, P.F.1    Hinnebusch, A.G.2
  • 166
    • 0037072937 scopus 로고    scopus 로고
    • An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12
    • Morishima N., Nakanishi K., Takenouchi H., Shibata T., Yasuhiko Y.. An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12. J Biol Chem. 2002 ; 277: 34287-94
    • (2002) J Biol Chem , vol.277 , pp. 34287-34294
    • Morishima, N.1    Nakanishi, K.2    Takenouchi, H.3    Shibata, T.4    Yasuhiko, Y.5
  • 167
    • 0025300038 scopus 로고
    • In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation
    • Mosser D. D., Kotzbauer P. T., Sarge K. D., Morimoto R. I.. In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation. Proc Natl Acad Sci USA. 1990 ; 87: 3748-52
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3748-3752
    • Mosser, D.D.1    Kotzbauer, P.T.2    Sarge, K.D.3    Morimoto, R.I.4
  • 168
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis
    • Nakagawa T., Yuan J.. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J Cell Biol. 2000 ; 150: 887-94
    • (2000) J Cell Biol , vol.150 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 169
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T., Zhu H., Morishima N., Li E., Xu J., Yankner B. A., Yuan J.. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature. 2000 ; 403: 98-103
    • (2000) Nature , vol.403 , 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
  • 170
    • 77449095179 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress plays critical role in brain damage after cerebral ischemia/reperfusion in rats
    • Nakka V. P., Gusain A., Raghubir R.. Endoplasmic reticulum stress plays critical role in brain damage after cerebral ischemia/reperfusion in rats. Neurotox Res. 2010 ; 17: 189-202
    • (2010) Neurotox Res , vol.17 , pp. 189-202
    • Nakka, V.P.1    Gusain, A.2    Raghubir, R.3
  • 171
    • 32644469104 scopus 로고    scopus 로고
    • Drug-related hepatotoxicity
    • Navarro V. J., Senior J. R.. Drug-related hepatotoxicity. N Engl J Med. 2006 ; 354: 731-39
    • (2006) N Engl J Med , vol.354 , pp. 731-739
    • Navarro, V.J.1    Senior, J.R.2
  • 172
    • 29244470510 scopus 로고    scopus 로고
    • Bortezomib inhibits PKR-like endoplasmic reticulum (ER) kinase and induces apoptosis via ER stress in human pancreatic cancer cells
    • Nawrocki S. T., Carew J. S., Dunner K., Boise L. H., Chiao P. J., Huang P., Abbruzzese J. L., McConkey D. J.. Bortezomib inhibits PKR-like endoplasmic reticulum (ER) kinase and induces apoptosis via ER stress in human pancreatic cancer cells. Cancer Res. 2005 ; 65: 11510-19
    • (2005) Cancer Res , vol.65 , pp. 11510-11519
    • Nawrocki, S.T.1    Carew, J.S.2    Dunner, K.3    Boise, L.H.4    Chiao, P.J.5    Huang, P.6    Abbruzzese, J.L.7    McConkey, D.J.8
  • 174
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W.. Protein import into mitochondria. Ann Rev Biochem. 1997 ; 66: 863-917
    • (1997) Ann Rev Biochem , vol.66 , pp. 863-917
    • Neupert, W.1
  • 175
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W., Herrmann J. M.. Translocation of proteins into mitochondria. Ann Rev Biochem. 2007 ; 76: 723-49
    • (2007) Ann Rev Biochem , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 177
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh H., Matsuzawa A., Tobiume K., Saegusa K., Takeda K., Inoue K., Hori S., Kakizuka A., Ichijo H.. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev. 2002 ; 16: 1345-55
    • (2002) Genes Dev , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5    Inoue, K.6    Hori, S.7    Kakizuka, A.8    Ichijo, H.9
  • 178
    • 0033598996 scopus 로고    scopus 로고
    • A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response
    • Niwa M., Sidrauski C., Kaufman R. J., Walter P.. A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response. Cell. 1999 ; 99: 691-702
    • (1999) Cell , vol.99 , pp. 691-702
    • Niwa, M.1    Sidrauski, C.2    Kaufman, R.J.3    Walter, P.4
  • 179
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • Obeng E. A., Carlson L. M., Gutman D. M., Harrington W. J., Lee K. P., Boise L. H.. Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells. Blood. 2006 ; 107: 4907-16
    • (2006) Blood , vol.107 , pp. 4907-4916
    • Obeng, E.A.1    Carlson, L.M.2    Gutman, D.M.3    Harrington, W.J.4    Lee, K.P.5    Boise, L.H.6
  • 182
    • 79251525523 scopus 로고    scopus 로고
    • Measuring ER stress and the unfolded protein response using mammalian tissue culture system
    • Oslowski C. M., Urano F.. Measuring ER stress and the unfolded protein response using mammalian tissue culture system. Methods Enzymol. 2011 ; 490: 71-92
    • (2011) Methods Enzymol , vol.490 , pp. 71-92
    • Oslowski, C.M.1    Urano, F.2
  • 183
    • 84863158460 scopus 로고    scopus 로고
    • Cdc37/Hsp90 protein-mediated regulation of IRE1alpha protein activity in endoplasmic reticulum stress response and insulin synthesis in INS-1 cells
    • Ota A., Wang Y.. Cdc37/Hsp90 protein-mediated regulation of IRE1alpha protein activity in endoplasmic reticulum stress response and insulin synthesis in INS-1 cells. J Biol Chem. 2012 ; 287: 6266-74
    • (2012) J Biol Chem , vol.287 , pp. 6266-6274
    • Ota, A.1    Wang, Y.2
  • 184
    • 44349163999 scopus 로고    scopus 로고
    • Dephosphorylation of translation initiation factor 2alpha enhances glucose tolerance and attenuates hepatosteatosis in mice
    • Oyadomari S., Harding H. P., Zhang Y., Oyadomari M., Ron D.. Dephosphorylation of translation initiation factor 2alpha enhances glucose tolerance and attenuates hepatosteatosis in mice. Cell Metab. 2008 ; 7: 520-32
    • (2008) Cell Metab , vol.7 , pp. 520-532
    • Oyadomari, S.1    Harding, H.P.2    Zhang, Y.3    Oyadomari, M.4    Ron, D.5
  • 185
    • 1842843855 scopus 로고    scopus 로고
    • Roles of CHOP/GADD153 in endoplasmic reticulum stress
    • Oyadomari S., Mori M.. Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ. 2004 ; 11: 381-89
    • (2004) Cell Death Differ , vol.11 , pp. 381-389
    • Oyadomari, S.1    Mori, M.2
  • 187
    • 84855966721 scopus 로고    scopus 로고
    • Role of endoplasmic reticulum stress in metabolic disease and other disorders
    • Ozcan L., Tabas I.. Role of endoplasmic reticulum stress in metabolic disease and other disorders. Ann Rev Med. 2012 ; 63: 317-28
    • (2012) Ann Rev Med , vol.63 , pp. 317-328
    • Ozcan, L.1    Tabas, I.2
  • 193
    • 80053969555 scopus 로고    scopus 로고
    • Proteasome inhibitor MG132-induced apoptosis via ER stress-mediated apoptotic pathway and its potentiation by protein tyrosine kinase p56lck in human Jurkat T cells
    • Park H. S., Jun do Y., Han C. R., Woo H. J., Kim Y. H.. Proteasome inhibitor MG132-induced apoptosis via ER stress-mediated apoptotic pathway and its potentiation by protein tyrosine kinase p56lck in human Jurkat T cells. Biochem Pharmacol. 2011 ; 82: 1110-25
    • (2011) Biochem Pharmacol , vol.82 , pp. 1110-1125
    • Park, H.S.1    Jun Do, Y.2    Han, C.R.3    Woo, H.J.4    Kim, Y.H.5
  • 194
    • 77950523710 scopus 로고    scopus 로고
    • The regulatory subunits of PI3K, p85alpha and p85beta, interact with XBP-1 and increase its nuclear translocation
    • Park S. W., Zhou Y., Lee J., Lu A., Sun C., Chung J., Ueki K., Ozcan U.. The regulatory subunits of PI3K, p85alpha and p85beta, interact with XBP-1 and increase its nuclear translocation. Nat Med. 2010 ; 16: 429-37
    • (2010) Nat Med , vol.16 , pp. 429-437
    • Park, S.W.1    Zhou, Y.2    Lee, J.3    Lu, A.4    Sun, C.5    Chung, J.6    Ueki, K.7    Ozcan, U.8
  • 195
    • 84859817850 scopus 로고    scopus 로고
    • Sensing endoplasmic reticulum stress
    • Parmar V. M., Schroder M.. Sensing endoplasmic reticulum stress. Adv Exp Med Biol. 2012 ; 738: 153-68
    • (2012) Adv Exp Med Biol , vol.738 , pp. 153-168
    • Parmar, V.M.1    Schroder, M.2
  • 196
    • 59149090850 scopus 로고    scopus 로고
    • Role of JNK1-dependent Bcl-2 phosphorylation in ceramide-induced macroautophagy
    • Pattingre S., Bauvy C., Carpentier S., Levade T., Levine B., Codogno P.. Role of JNK1-dependent Bcl-2 phosphorylation in ceramide-induced macroautophagy. J Biol Chem. 2009 ; 284: 2719-28
    • (2009) J Biol Chem , vol.284 , pp. 2719-2728
    • Pattingre, S.1    Bauvy, C.2    Carpentier, S.3    Levade, T.4    Levine, B.5    Codogno, P.6
  • 197
    • 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 2alpha kinase PERK
    • Pavio N., Romano P. R., Graczyk T. M., Feinstone S. M., Taylor D. R.. Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2alpha kinase PERK. J Virol. 2003 ; 77: 3578-85
    • (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
  • 198
  • 199
    • 34247144663 scopus 로고    scopus 로고
    • Effect of endoplasmic reticulum stress preconditioning on cytotoxicity of clinically relevant nephrotoxins in renal cell lines
    • Peyrou M., Cribb A. E.. Effect of endoplasmic reticulum stress preconditioning on cytotoxicity of clinically relevant nephrotoxins in renal cell lines. Toxicol In Vitro. 2007 ; 21: 878-86
    • (2007) Toxicol in Vitro , vol.21 , pp. 878-886
    • Peyrou, M.1    Cribb, A.E.2
  • 202
    • 36348961452 scopus 로고    scopus 로고
    • HIV-1 protease inhibitors nelfinavir and atazanavir induce malignant glioma death by triggering endoplasmic reticulum stress
    • Pyrko P., Kardosh A., Wang W., Xiong W., Schonthal A. H., Chen T. C.. HIV-1 protease inhibitors nelfinavir and atazanavir induce malignant glioma death by triggering endoplasmic reticulum stress. Cancer Res. 2007 ; 67: 10920-28
    • (2007) Cancer Res , vol.67 , pp. 10920-10928
    • Pyrko, P.1    Kardosh, A.2    Wang, W.3    Xiong, W.4    Schonthal, A.H.5    Chen, T.C.6
  • 204
    • 58149109602 scopus 로고    scopus 로고
    • GRP78: A chaperone with diverse roles beyond the endoplasmic reticulum
    • Quinones Q. J., de Ridder G. G., Pizzo S. V.. GRP78: A chaperone with diverse roles beyond the endoplasmic reticulum. Histol Histopathol. 2008 ; 23: 1409-16
    • (2008) Histol Histopathol , vol.23 , pp. 1409-1416
    • Quinones, Q.J.1    De Ridder, G.G.2    Pizzo, S.V.3
  • 205
  • 206
    • 34547197343 scopus 로고    scopus 로고
    • The kinase inhibitor sorafenib induces cell death through a process involving induction of endoplasmic reticulum stress
    • Rahmani M., Davis E. M., Crabtree T. R., Habibi J. R., Nguyen T. K., Dent P., Grant S.. The kinase inhibitor sorafenib induces cell death through a process involving induction of endoplasmic reticulum stress. Mol Cell Biol. 2007 ; 27: 5499-513
    • (2007) Mol Cell Biol , vol.27 , pp. 5499-5513
    • Rahmani, M.1    Davis, E.M.2    Crabtree, T.R.3    Habibi, J.R.4    Nguyen, T.K.5    Dent, P.6    Grant, S.7
  • 208
    • 80052627393 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in Ca(2+)-dependent apoptosis and necrosis
    • Rasola A., Bernardi P.. Mitochondrial permeability transition in Ca(2+)-dependent apoptosis and necrosis. Cell Calcium. 2011 ; 50: 222-33
    • (2011) Cell Calcium , vol.50 , pp. 222-233
    • Rasola, A.1    Bernardi, P.2
  • 209
    • 39649114320 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins
    • Reijonen S., Putkonen N., Norremolle A., Lindholm D., Korhonen L.. Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins. Exp Cell Res. 2008 ; 314: 950-60
    • (2008) Exp Cell Res , vol.314 , pp. 950-960
    • Reijonen, S.1    Putkonen, N.2    Norremolle, A.3    Lindholm, D.4    Korhonen, L.5
  • 212
    • 33751508817 scopus 로고    scopus 로고
    • N-glycan processing in ER quality control
    • Ruddock L. W., Molinari M.. N-glycan processing in ER quality control. J Cell Sci. 2006 ; 119: 4373-80
    • (2006) J Cell Sci , vol.119 , pp. 4373-4380
    • Ruddock, L.W.1    Molinari, M.2
  • 213
  • 216
    • 0037114971 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease
    • Ryu E. J., Harding H. P., Angelastro J. M., Vitolo O. V., Ron D., Greene L. A.. Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease. J Neurosci. 2002 ; 22: 10690-98
    • (2002) J Neurosci , vol.22 , pp. 10690-10698
    • Ryu, E.J.1    Harding, H.P.2    Angelastro, J.M.3    Vitolo, O.V.4    Ron, D.5    Greene, L.A.6
  • 218
    • 74849136799 scopus 로고    scopus 로고
    • Role of ATF4 in regulation of autophagy and resistance to drugs and hypoxia
    • Rzymski T., Milani M., Singleton D. C., Harris A. L.. Role of ATF4 in regulation of autophagy and resistance to drugs and hypoxia. Cell Cycle. 2009 ; 8: 3838-47
    • (2009) Cell Cycle , vol.8 , pp. 3838-3847
    • Rzymski, T.1    Milani, M.2    Singleton, D.C.3    Harris, A.L.4
  • 220
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signaling by proteolysis
    • Salvesen G. S., Dixit V. M.. Caspases: Intracellular signaling by proteolysis. Cell. 1997 ; 91: 443-46
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 223
    • 6044255043 scopus 로고    scopus 로고
    • The physiological unfolded protein response in the thyroid epithelial cells
    • Sargsyan E., Baryshev M., Mkrtchian S.. The physiological unfolded protein response in the thyroid epithelial cells. Biochem Biophys Res Commun. 2004 ; 322: 570-76
    • (2004) Biochem Biophys Res Commun , vol.322 , pp. 570-576
    • Sargsyan, E.1    Baryshev, M.2    Mkrtchian, S.3
  • 224
    • 0037053397 scopus 로고    scopus 로고
    • Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complex
    • Sargsyan E., Baryshev M., Szekely L., Sharipo A., Mkrtchian S.. Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complex. J Biol Chem. 2002 ; 277: 17009-15
    • (2002) J Biol Chem , vol.277 , pp. 17009-17015
    • Sargsyan, E.1    Baryshev, M.2    Szekely, L.3    Sharipo, A.4    Mkrtchian, S.5
  • 226
    • 67349164383 scopus 로고    scopus 로고
    • A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice
    • Saxena S., Cabuy E., Caroni P.. A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice. Nat Neurosci. 2009 ; 12: 627-36
    • (2009) Nat Neurosci , vol.12 , pp. 627-636
    • Saxena, S.1    Cabuy, E.2    Caroni, P.3
  • 230
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder M., Kaufman R. J.. The mammalian unfolded protein response. Ann Rev Biochem. 2005 ; 74: 739-89
    • (2005) Ann Rev Biochem , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 231
    • 81755161377 scopus 로고    scopus 로고
    • Mechanisms of ER stress-induced apoptosis in atherosclerosis
    • Scull C. M., Tabas I.. Mechanisms of ER stress-induced apoptosis in atherosclerosis. Arterioscler Thromb Vasc Biol. 2011 ; 31: 2792-97
    • (2011) Arterioscler Thromb Vasc Biol , vol.31 , pp. 2792-2797
    • Scull, C.M.1    Tabas, I.2
  • 233
    • 32044462724 scopus 로고    scopus 로고
    • Mood stabilizing drug lithium increases expression of endoplasmic reticulum stress proteins in primary cultured rat cerebral cortical cells
    • Shao L., Sun X., Xu L., Young L. T., Wang J. F.. Mood stabilizing drug lithium increases expression of endoplasmic reticulum stress proteins in primary cultured rat cerebral cortical cells. Life Sci. 2006 ; 78: 1317-23
    • (2006) Life Sci , vol.78 , pp. 1317-1323
    • Shao, L.1    Sun, X.2    Xu, L.3    Young, L.T.4    Wang, J.F.5
  • 234
    • 34447333099 scopus 로고    scopus 로고
    • Induction of GRP78 by valproic acid is dependent upon histone deacetylase inhibition
    • Shi Y., Gerritsma D., Bowes A. J., Capretta A., Werstuck G. H.. Induction of GRP78 by valproic acid is dependent upon histone deacetylase inhibition. Bioorg Med Chem Lett. 2007 ; 17: 4491-94
    • (2007) Bioorg Med Chem Lett , vol.17 , pp. 4491-4494
    • Shi, Y.1    Gerritsma, D.2    Bowes, A.J.3    Capretta, A.4    Werstuck, G.H.5
  • 236
    • 33744504827 scopus 로고    scopus 로고
    • Ischemic preconditioning protects cardiomyocytes against ischemic injury by inducing GRP78
    • Shintani-Ishida K., Nakajima M., Uemura K., Yoshida K.. Ischemic preconditioning protects cardiomyocytes against ischemic injury by inducing GRP78. Biochem Biophys Res Commun. 2006 ; 345: 1600-05
    • (2006) Biochem Biophys Res Commun , vol.345 , pp. 1600-1605
    • Shintani-Ishida, K.1    Nakajima, M.2    Uemura, K.3    Yoshida, K.4
  • 239
    • 77953725586 scopus 로고    scopus 로고
    • Oxidative protein folding in the endoplasmic reticulum: Tight links to the mitochondria-associated membrane (MAM)
    • Simmen T., Lynes E. M., Gesson K., Thomas G.. Oxidative protein folding in the endoplasmic reticulum: Tight links to the mitochondria-associated membrane (MAM). Biochim Biophys Acta. 2010 ; 1798: 1465-73
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1465-1473
    • Simmen, T.1    Lynes, E.M.2    Gesson, K.3    Thomas, G.4
  • 240
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum
    • Smith M. H., Ploegh H. L., Weissman J. S.. Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum. Science. 2011 ; 334: 1086-90
    • (2011) Science , vol.334 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weissman, J.S.3
  • 241
    • 29644434199 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity
    • Smith W. W., Jiang H., Pei Z., Tanaka Y., Morita H., Sawa A., Dawson V. L., Dawson T. M., Ross C. A.. Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity. Human Mol Genet. 2005 ; 14: 3801-11
    • (2005) Human Mol Genet , vol.14 , pp. 3801-3811
    • Smith, W.W.1    Jiang, H.2    Pei, Z.3    Tanaka, Y.4    Morita, H.5    Sawa, A.6    Dawson, V.L.7    Dawson, T.M.8    Ross, C.A.9
  • 243
    • 55849096988 scopus 로고    scopus 로고
    • Chop deletion reduces oxidative stress, improves beta cell function, and promotes cell survival in multiple mouse models of diabetes
    • Song B., Scheuner D., Ron D., Pennathur S., Kaufman R. J.. Chop deletion reduces oxidative stress, improves beta cell function, and promotes cell survival in multiple mouse models of diabetes. J Clin Invest. 2008 ; 118: 3378-89
    • (2008) J Clin Invest , vol.118 , pp. 3378-3389
    • Song, B.1    Scheuner, D.2    Ron, D.3    Pennathur, S.4    Kaufman, R.J.5
  • 244
    • 0037160134 scopus 로고    scopus 로고
    • Central role of glycogen synthase kinase-3beta in endoplasmic reticulum stress-induced caspase-3 activation
    • Song L., De Sarno P., Jope R. S.. Central role of glycogen synthase kinase-3beta in endoplasmic reticulum stress-induced caspase-3 activation. J Biol Chem. 2002 ; 277: 44701-08
    • (2002) J Biol Chem , vol.277 , pp. 44701-44708
    • Song, L.1    De Sarno, P.2    Jope, R.S.3
  • 245
    • 30044441047 scopus 로고    scopus 로고
    • CREB4, a transmembrane bZip transcription factor and potential new substrate for regulation and cleavage by S1P
    • Stirling J., O'Hare P.. CREB4, a transmembrane bZip transcription factor and potential new substrate for regulation and cleavage by S1P. Mol Biol Cell. 2006 ; 17: 413-26
    • (2006) Mol Biol Cell , vol.17 , pp. 413-426
    • Stirling, J.1    O'Hare, P.2
  • 246
    • 1842854719 scopus 로고    scopus 로고
    • Ischemia-induced neuronal cell death is mediated by the endoplasmic reticulum stress pathway involving CHOP
    • Tajiri S., Oyadomari S., Yano S., Morioka M., Gotoh T., Hamada J. I., Ushio Y., Mori M.. Ischemia-induced neuronal cell death is mediated by the endoplasmic reticulum stress pathway involving CHOP. Cell Death Differ. 2004 ; 11: 403-15
    • (2004) Cell Death Differ , vol.11 , pp. 403-415
    • Tajiri, S.1    Oyadomari, S.2    Yano, S.3    Morioka, M.4    Gotoh, T.5    Hamada, J.I.6    Ushio, Y.7    Mori, M.8
  • 248
    • 33744918550 scopus 로고    scopus 로고
    • Ubiquitous calpains promote caspase-12 and JNK activation during endoplasmic reticulum stress-induced apoptosis
    • Tan Y., Dourdin N., Wu C., De Veyra T., Elce J. S., Greer P. A.. Ubiquitous calpains promote caspase-12 and JNK activation during endoplasmic reticulum stress-induced apoptosis. J Biol Chem. 2006 ; 281: 16016-24
    • (2006) J Biol Chem , vol.281 , pp. 16016-16024
    • Tan, Y.1    Dourdin, N.2    Wu, C.3    De Veyra, T.4    Elce, J.S.5    Greer, P.A.6
  • 249
    • 0034615941 scopus 로고    scopus 로고
    • Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death
    • Tanaka S., Uehara T., Nomura Y.. Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death. J Biol Chem. 2000 ; 275: 10388-93
    • (2000) J Biol Chem , vol.275 , pp. 10388-10393
    • Tanaka, S.1    Uehara, T.2    Nomura, Y.3
  • 250
    • 0035870881 scopus 로고    scopus 로고
    • Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis
    • Tanaka Y., Engelender S., Igarashi S., Rao R. K., Wanner T., Tanzi R. E., Sawa A. V. L. D., Dawson T. M., Ross C. A.. Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis. Human Mol Genet. 2001 ; 10: 919-26
    • (2001) Human Mol Genet , vol.10 , pp. 919-926
    • Tanaka, Y.1    Engelender, S.2    Igarashi, S.3    Rao, R.K.4    Wanner, T.5    Tanzi, R.E.6    Sawa, A.V.L.D.7    Dawson, T.M.8    Ross, C.A.9
  • 251
    • 2342435179 scopus 로고    scopus 로고
    • Hepatitis C virus suppresses the IRE1-XBP1 pathway of the unfolded protein response
    • Tardif K. D., Mori K., Kaufman R. J., Siddiqui A.. Hepatitis C virus suppresses the IRE1-XBP1 pathway of the unfolded protein response. J Biol Chem. 2004 ; 279: 17158-64
    • (2004) J Biol Chem , vol.279 , pp. 17158-17164
    • Tardif, K.D.1    Mori, K.2    Kaufman, R.J.3    Siddiqui, A.4
  • 252
    • 38549101188 scopus 로고    scopus 로고
    • Quality control of mitochondria: Protection against neurodegeneration and ageing
    • Tatsuta T., Langer T.. Quality control of mitochondria: Protection against neurodegeneration and ageing. EMBO J. 2008 ; 27: 306-14
    • (2008) EMBO J , vol.27 , pp. 306-314
    • Tatsuta, T.1    Langer, T.2
  • 253
    • 79251517391 scopus 로고    scopus 로고
    • Methods for analyzing eIF2 kinases and translational control in the unfolded protein response
    • Teske B. F., Baird T. D., Wek R. C.. Methods for analyzing eIF2 kinases and translational control in the unfolded protein response. Methods Enzymol. 2011 ; 490: 333-56
    • (2011) Methods Enzymol , vol.490 , pp. 333-356
    • Teske, B.F.1    Baird, T.D.2    Wek, R.C.3
  • 254
    • 33746788477 scopus 로고    scopus 로고
    • Activation of the unfolded protein response in infarcted mouse heart and hypoxic cultured cardiac myocytes
    • Thuerauf D. J., Marcinko M., Gude N., Rubio M., Sussman M. A., Glembotski C. C.. Activation of the unfolded protein response in infarcted mouse heart and hypoxic cultured cardiac myocytes. Circ Res. 2006 ; 99: 275-82
    • (2006) Circ Res , vol.99 , pp. 275-282
    • Thuerauf, D.J.1    Marcinko, M.2    Gude, N.3    Rubio, M.4    Sussman, M.A.5    Glembotski, C.C.6
  • 255
    • 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., Welihinda A. A., Kaufman R. J.. A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. Genes Dev. 1998 ; 12: 1812-24
    • (1998) Genes Dev , vol.12 , pp. 1812-1824
    • Tirasophon, W.1    Welihinda, A.A.2    Kaufman, R.J.3
  • 257
    • 79953288480 scopus 로고    scopus 로고
    • Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis
    • Tsaytler P., Harding H. P., Ron D., Bertolotti A.. Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis. Science. 2011 ; 332: 91-94
    • (2011) Science , vol.332 , pp. 91-94
    • Tsaytler, P.1    Harding, H.P.2    Ron, D.3    Bertolotti, A.4
  • 259
    • 33244495918 scopus 로고    scopus 로고
    • Celecoxib upregulates endoplasmic reticulum chaperones that inhibit celecoxib-induced apoptosis in human gastric cells
    • Tsutsumi S., Namba T., Tanaka K. I., Arai Y., Ishihara T., Aburaya M., Mima S., Hoshino T., Mizushima T.. Celecoxib upregulates endoplasmic reticulum chaperones that inhibit celecoxib-induced apoptosis in human gastric cells. Oncogene. 2006 ; 25: 1018-29
    • (2006) Oncogene , vol.25 , pp. 1018-1029
    • Tsutsumi, S.1    Namba, T.2    Tanaka, K.I.3    Arai, Y.4    Ishihara, T.5    Aburaya, M.6    Mima, S.7    Hoshino, T.8    Mizushima, T.9
  • 260
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: Mechanisms and consequences
    • Tu B. P., Weissman J. S.. Oxidative protein folding in eukaryotes: Mechanisms and consequences. J Cell Biol. 2004 ; 164: 341-46
    • (2004) J Cell Biol , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 261
    • 0032696587 scopus 로고    scopus 로고
    • CHOP enhancement of gene transcription by interactions with Jun/Fos AP-1 complex proteins
    • Ubeda M., Vallejo M., Habener J. F.. CHOP enhancement of gene transcription by interactions with Jun/Fos AP-1 complex proteins. Mol Cell Biol. 1999 ; 19: 7589-99
    • (1999) Mol Cell Biol , vol.19 , pp. 7589-7599
    • Ubeda, M.1    Vallejo, M.2    Habener, J.F.3
  • 262
  • 263
    • 0033693855 scopus 로고    scopus 로고
    • IRE1 and efferent signaling from the endoplasmic reticulum
    • Urano F., Bertolotti A., Ron D.. IRE1 and efferent signaling from the endoplasmic reticulum. J Cell Sci. 2000 ; 113 (Pt 21). 3697-702
    • (2000) J Cell Sci , vol.113 , Issue.PART 21 , pp. 3697-3702
    • Urano, F.1    Bertolotti, A.2    Ron, D.3
  • 264
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • Urano F., Wang X., Bertolotti A., Zhang Y., Chung P., Harding H. P., Ron D.. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science. 2000 ; 287: 664-66
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6    Ron, D.7
  • 265
    • 0037332128 scopus 로고    scopus 로고
    • Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion
    • van Anken E., Romijn E. P., Maggioni C., Mezghrani A., Sitia R., Braakman I., Heck A. J.. Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion. Immunity. 2003 ; 18: 243-53
    • (2003) Immunity , vol.18 , pp. 243-253
    • Van Anken, E.1    Romijn, E.P.2    Maggioni, C.3    Mezghrani, A.4    Sitia, R.5    Braakman, I.6    Heck, A.J.7
  • 266
    • 0038182518 scopus 로고    scopus 로고
    • P58IPK, a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2alpha signaling
    • van Huizen R., Martindale J. L., Gorospe M., Holbrook N. J.. P58IPK, a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2alpha signaling. J Biol Chem. 2003 ; 278: 15558-64
    • (2003) J Biol Chem , vol.278 , pp. 15558-15564
    • Van Huizen, R.1    Martindale, J.L.2    Gorospe, M.3    Holbrook, N.J.4
  • 268
    • 24344495336 scopus 로고    scopus 로고
    • Sodium 4-phenylbutyrate protects against liver ischemia reperfusion injury by inhibition of endoplasmic reticulum-stress mediated apoptosis
    • Vilatoba M., Eckstein C., Bilbao G., Smyth C. A., Jenkins S., Thompson J. A., Eckhoff D. E., Contreras J. L.. Sodium 4-phenylbutyrate protects against liver ischemia reperfusion injury by inhibition of endoplasmic reticulum-stress mediated apoptosis. Surgery. 2005 ; 138: 342-51
    • (2005) Surgery , vol.138 , pp. 342-351
    • Vilatoba, M.1    Eckstein, C.2    Bilbao, G.3    Smyth, C.A.4    Jenkins, S.5    Thompson, J.A.6    Eckhoff, D.E.7    Contreras, J.L.8
  • 269
    • 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: 1081-86
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 270
    • 79551474362 scopus 로고    scopus 로고
    • Regulation of unfolded protein response modulator XBP1s by acetylation and deacetylation
    • Wang F. M., Chen Y. J., Ouyang H. J.. Regulation of unfolded protein response modulator XBP1s by acetylation and deacetylation. Biochem J. 2011 ; 433: 245-52
    • (2011) Biochem J , vol.433 , pp. 245-252
    • Wang, F.M.1    Chen, Y.J.2    Ouyang, H.J.3
  • 271
    • 80052827034 scopus 로고    scopus 로고
    • Resveratrol triggers the pro-apoptotic endoplasmic reticulum stress response and represses pro-survival XBP1 signaling in human multiple myeloma cells
    • Wang F. M., Galson D. L., Roodman G. D., Ouyang H.. Resveratrol triggers the pro-apoptotic endoplasmic reticulum stress response and represses pro-survival XBP1 signaling in human multiple myeloma cells. Exp Hematol. 2011 ; 39: 999-1006
    • (2011) Exp Hematol , vol.39 , pp. 999-1006
    • Wang, F.M.1    Galson, D.L.2    Roodman, G.D.3    Ouyang, H.4
  • 273
    • 78649742954 scopus 로고    scopus 로고
    • The ERAD inhibitor Eeyarestatin i is a bifunctional compound with a membrane-binding domain and a p97/VCP inhibitory group
    • Wang Q., Shinkre B. A., Lee J. G., Weniger M. A., Liu Y., Chen W., Wiestner A., Trenkle W. C., Ye Y.. The ERAD inhibitor Eeyarestatin I is a bifunctional compound with a membrane-binding domain and a p97/VCP inhibitory group. PLoS One. 2010 ; 5: e15479
    • (2010) PLoS One , vol.5 , pp. 15479
    • Wang, Q.1    Shinkre, B.A.2    Lee, J.G.3    Weniger, M.A.4    Liu, Y.5    Chen, W.6    Wiestner, A.7    Trenkle, W.C.8    Ye, Y.9
  • 274
    • 0029938805 scopus 로고    scopus 로고
    • Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP Kinase
    • Wang X. Z., Ron D.. Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP Kinase. Science. 1996 ; 272: 1347-49
    • (1996) Science , vol.272 , pp. 1347-1349
    • Wang, X.Z.1    Ron, D.2
  • 275
    • 67749135249 scopus 로고    scopus 로고
    • The CREB coactivator CRTC2 links hepatic ER stress and fasting gluconeogenesis
    • Wang Y., Vera L., Fischer W. H., Montminy M.. The CREB coactivator CRTC2 links hepatic ER stress and fasting gluconeogenesis. Nature. 2009b ; 460: 534-37
    • (2009) Nature , vol.460 , pp. 534-537
    • Wang, Y.1    Vera, L.2    Fischer, W.H.3    Montminy, M.4
  • 276
    • 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: 1501-11
    • (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
  • 277
    • 73349141743 scopus 로고    scopus 로고
    • Adaptive suppression of the ATF4-CHOP branch of the unfolded protein response by toll-like receptor signalling
    • Woo C. W., Cui D., Arellano J., Dorweiler B., Harding H., Fitzgerald K. A., Ron D., Tabas I.. Adaptive suppression of the ATF4-CHOP branch of the unfolded protein response by toll-like receptor signalling. Nat Cell Biol. 2009 ; 11: 1473-80
    • (2009) Nat Cell Biol , vol.11 , pp. 1473-1480
    • Woo, C.W.1    Cui, D.2    Arellano, J.3    Dorweiler, B.4    Harding, H.5    Fitzgerald, K.A.6    Ron, D.7    Tabas, I.8
  • 278
    • 79959919089 scopus 로고    scopus 로고
    • Salubrinal, an eIF2alpha dephosphorylation inhibitor, enhances cisplatin-induced oxidative stress and nephrotoxicity in a mouse model
    • Wu C. T., Sheu M. L., Tsai K. S., Chiang C. K., Liu S. H.. Salubrinal, an eIF2alpha dephosphorylation inhibitor, enhances cisplatin-induced oxidative stress and nephrotoxicity in a mouse model. Free Rad Biol Med. 2011 ; 51: 671-80
    • (2011) Free Rad Biol Med , vol.51 , pp. 671-680
    • Wu, C.T.1    Sheu, M.L.2    Tsai, K.S.3    Chiang, C.K.4    Liu, S.H.5
  • 280
    • 26444442450 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: Cell life and death decisions
    • Xu C., Bailly-Maitre B., Reed J. C.. Endoplasmic reticulum stress: Cell life and death decisions. J Clin Invest. 2005 ; 115: 2656-64
    • (2005) J Clin Invest , vol.115 , pp. 2656-2664
    • Xu, C.1    Bailly-Maitre, B.2    Reed, J.C.3
  • 282
    • 0030756523 scopus 로고    scopus 로고
    • Activation of hepatitis B virus S promoter by the viral large surface protein via induction of stress in the endoplasmic reticulum
    • Xu Z., Jensen G., Yen T. S.. Activation of hepatitis B virus S promoter by the viral large surface protein via induction of stress in the endoplasmic reticulum. J Virol. 1997 ; 71: 7387-92
    • (1997) J Virol , vol.71 , pp. 7387-7392
    • Xu, Z.1    Jensen, G.2    Yen, T.S.3
  • 284
    • 8544283103 scopus 로고    scopus 로고
    • CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells
    • Yamaguchi H., Wang H. G.. CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells. J Biol Chem. 2004 ; 279: 45495-502
    • (2004) J Biol Chem , vol.279 , pp. 45495-45502
    • Yamaguchi, H.1    Wang, H.G.2
  • 285
    • 47749128073 scopus 로고    scopus 로고
    • Endoplasmic reticulum (ER) chaperone regulation and survival of cells compensating for deficiency in the ER stress response kinase, PERK
    • Yamaguchi Y., Larkin D., Lara-Lemus R., Ramos-Castaneda J., Liu M., Arvan P.. Endoplasmic reticulum (ER) chaperone regulation and survival of cells compensating for deficiency in the ER stress response kinase, PERK. J Biol Chem. 2008 ; 283: 17020-29
    • (2008) J Biol Chem , vol.283 , pp. 17020-17029
    • Yamaguchi, Y.1    Larkin, D.2    Lara-Lemus, R.3    Ramos-Castaneda, J.4    Liu, M.5    Arvan, P.6
  • 286
    • 0033499801 scopus 로고    scopus 로고
    • BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M
    • Yamamoto K., Ichijo H., Korsmeyer S. J.. BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M. Mol Cell Biol. 1999 ; 19: 8469-78
    • (1999) Mol Cell Biol , vol.19 , pp. 8469-8478
    • Yamamoto, K.1    Ichijo, H.2    Korsmeyer, S.J.3
  • 287
    • 34548172495 scopus 로고    scopus 로고
    • Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1
    • Yamamoto K., Sato T., Matsui T., Sato M., Okada T., Yoshida H., Harada A., Mori K.. Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1. Dev Cell. 2007 ; 13: 365-76
    • (2007) Dev Cell , vol.13 , 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
  • 288
    • 77956232915 scopus 로고    scopus 로고
    • Induction of liver steatosis and lipid droplet formation in ATF6alpha-knockout mice burdened with pharmacological endoplasmic reticulum stress
    • Yamamoto K., Takahara K., Oyadomari S., Okada T., Sato T., Harada A., Mori K.. Induction of liver steatosis and lipid droplet formation in ATF6alpha-knockout mice burdened with pharmacological endoplasmic reticulum stress. Mol Biol Cell. 2010 ; 21: 2975-86
    • (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    Mori, K.7
  • 289
    • 0037058574 scopus 로고    scopus 로고
    • Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK
    • Yan W., Frank C. L., Korth M. J., Sopher B. L., Novoa I., Ron D., Katze M. G.. Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK. Proc Natl Acad Sci USA. 2002 ; 99: 15920-25
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 15920-15925
    • Yan, W.1    Frank, C.L.2    Korth, M.J.3    Sopher, B.L.4    Novoa, I.5    Ron, D.6    Katze, M.G.7
  • 290
    • 64749103329 scopus 로고    scopus 로고
    • Cotranslational targeting of XBP1 protein to the membrane promotes cytoplasmic splicing of its own mRNA
    • Yanagitani K., Imagawa Y., Iwawaki T., Hosoda A., Saito M., Kimata Y., Kohno K.. Cotranslational targeting of XBP1 protein to the membrane promotes cytoplasmic splicing of its own mRNA. Mol Cell. 2009 ; 34: 191-200
    • (2009) Mol Cell , vol.34 , pp. 191-200
    • Yanagitani, K.1    Imagawa, Y.2    Iwawaki, T.3    Hosoda, A.4    Saito, M.5    Kimata, Y.6    Kohno, K.7
  • 292
    • 0035957929 scopus 로고    scopus 로고
    • Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress
    • Yoneda T., Imaizumi K., Oono K., Yui D., Gomi F., Katayama T., Tohyama M.. Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J Biol Chem. 2001 ; 276: 13935-40
    • (2001) J Biol Chem , vol.276 , pp. 13935-13940
    • Yoneda, T.1    Imaizumi, K.2    Oono, K.3    Yui, D.4    Gomi, F.5    Katayama, T.6    Tohyama, M.7
  • 293
    • 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: 881-91
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 294
    • 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., Okada T., Haze K., Yanagi H., Yura T., Negishi M., Mori K.. 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. 2000 ; 20: 6755-67
    • (2000) Mol Cell Biol , vol.20 , pp. 6755-6767
    • Yoshida, H.1    Okada, T.2    Haze, K.3    Yanagi, H.4    Yura, T.5    Negishi, M.6    Mori, K.7
  • 295
    • 32644432826 scopus 로고    scopus 로고
    • PXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response
    • Yoshida H., Oku M., Suzuki M., Mori K.. pXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response. J Cell Biol. 2006 ; 172: 565-75
    • (2006) J Cell Biol , vol.172 , pp. 565-575
    • Yoshida, H.1    Oku, M.2    Suzuki, M.3    Mori, K.4
  • 296
    • 63649157914 scopus 로고    scopus 로고
    • PXBP1(U), a negative regulator of the unfolded protein response activator pXBP1(S), targets ATF6 but not ATF4 in proteasome-mediated degradation
    • Yoshida H., Uemura A., Mori K.. pXBP1(U), a negative regulator of the unfolded protein response activator pXBP1(S), targets ATF6 but not ATF4 in proteasome-mediated degradation. Cell Struct Funct. 2009 ; 34: 1-10
    • (2009) Cell Struct Funct , vol.34 , pp. 1-10
    • Yoshida, H.1    Uemura, A.2    Mori, K.3
  • 297
    • 76549115938 scopus 로고    scopus 로고
    • MCP-1 causes cardiomyoblast death via autophagy resulting from ER stress caused by oxidative stress generated by inducing a novel zinc-finger protein, MCPIP
    • Younce C. W., Kolattukudy P. E.. MCP-1 causes cardiomyoblast death via autophagy resulting from ER stress caused by oxidative stress generated by inducing a novel zinc-finger protein, MCPIP. Biochem J. 2010 ; 426: 43-53
    • (2010) Biochem J , vol.426 , pp. 43-53
    • Younce, C.W.1    Kolattukudy, P.E.2
  • 298
    • 0035824403 scopus 로고    scopus 로고
    • Activation of JNK and transcriptional repressor ATF3/LRF1 through the IRE1/TRAF2 pathway is implicated in human vascular endothelial cell death by homocysteine
    • Zhang C., Kawauchi J., Adachi M. T., Hashimoto Y., Oshiro S., Aso T., Kitajima S.. Activation of JNK and transcriptional repressor ATF3/LRF1 through the IRE1/TRAF2 pathway is implicated in human vascular endothelial cell death by homocysteine. Biochem Biophys Res Commun. 2001 ; 289: 718-24
    • (2001) Biochem Biophys Res Commun , vol.289 , pp. 718-724
    • Zhang, C.1    Kawauchi, J.2    Adachi, M.T.3    Hashimoto, Y.4    Oshiro, S.5    Aso, T.6    Kitajima, S.7
  • 299
    • 77649196117 scopus 로고    scopus 로고
    • Integration of ER stress, oxidative stress and the inflammatory response in health and disease
    • Zhang K.. Integration of ER stress, oxidative stress and the inflammatory response in health and disease. Int J Clin Exp Med. 2010 ; 3: 33-40
    • (2010) Int J Clin Exp Med , vol.3 , pp. 33-40
    • Zhang, K.1
  • 300
    • 47949099916 scopus 로고    scopus 로고
    • From endoplasmic-reticulum stress to the inflammatory response
    • Zhang K., Kaufman R. J.. From endoplasmic-reticulum stress to the inflammatory response. Nature. 2008 ; 454: 455-62
    • (2008) Nature , vol.454 , pp. 455-462
    • Zhang, K.1    Kaufman, R.J.2
  • 301
    • 32044453080 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response
    • Zhang K., Shen X., Wu J., Sakaki K., Saunders T., Rutkowski D. T., Back S. H., Kaufman R. J.. Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response. Cell. 2006 ; 124: 587-99
    • (2006) Cell , vol.124 , pp. 587-599
    • Zhang, K.1    Shen, X.2    Wu, J.3    Sakaki, K.4    Saunders, T.5    Rutkowski, D.T.6    Back, S.H.7    Kaufman, R.J.8
  • 304
    • 11144288092 scopus 로고    scopus 로고
    • Preinduced molecular chaperones in the endoplasmic reticulum protect cardiomyocytes from lethal injury
    • Zhang P. L., Lun M., Teng J., Huang J., Blasick T. M., Yin L., Herrera G. A., Cheung J. Y.. Preinduced molecular chaperones in the endoplasmic reticulum protect cardiomyocytes from lethal injury. Ann Clin Lab Sci. 2004 ; 34: 449-57
    • (2004) Ann Clin Lab Sci , vol.34 , pp. 449-457
    • Zhang, P.L.1    Lun, M.2    Teng, J.3    Huang, J.4    Blasick, T.M.5    Yin, L.6    Herrera, G.A.7    Cheung, J.Y.8
  • 305
    • 79251525864 scopus 로고    scopus 로고
    • Measurement of ER stress response and inflammation in the mouse model of nonalcoholic fatty liver disease
    • Zheng Z., Zhang C., Zhang K.. Measurement of ER stress response and inflammation in the mouse model of nonalcoholic fatty liver disease. Methods Enzymol. 2011 ; 489: 329-48
    • (2011) Methods Enzymol , vol.489 , pp. 329-348
    • Zheng, Z.1    Zhang, C.2    Zhang, K.3


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